data_5FFO
# 
_entry.id   5FFO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5FFO         
WWPDB D_1000216498 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          5FFG 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5FFO 
_pdbx_database_status.recvd_initial_deposition_date   2015-12-18 
_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.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Dong, X.'       1 
'Zhao, B.'       2 
'Springer, T.A.' 3 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nature 
_citation.journal_id_ASTM           NATUAS 
_citation.journal_id_CSD            0006 
_citation.journal_id_ISSN           1476-4687 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            542 
_citation.language                  ? 
_citation.page_first                55 
_citation.page_last                 59 
_citation.title                     'Force interacts with macromolecular structure in activation of TGF-beta.' 
_citation.year                      2017 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/nature21035 
_citation.pdbx_database_id_PubMed   28117447 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Dong, X.'       1 
primary 'Zhao, B.'       2 
primary 'Iacob, R.E.'    3 
primary 'Zhu, J.'        4 
primary 'Koksal, A.C.'   5 
primary 'Lu, C.'         6 
primary 'Engen, J.R.'    7 
primary 'Springer, T.A.' 8 
# 
_cell.entry_id           5FFO 
_cell.length_a           81.440 
_cell.length_b           91.440 
_cell.length_c           131.030 
_cell.angle_alpha        89.98 
_cell.angle_beta         86.25 
_cell.angle_gamma        89.85 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         5FFO 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
# 
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 'Integrin alpha-V'                  65982.922 2  ? ? 'UNP residues 31-627'  ? 
2 polymer     man 'Integrin beta-6'                   28851.707 2  ? ? 'Unp residues 128-378' ? 
3 polymer     man 'Transforming growth factor beta-1' 41489.371 4  ? ? 'UNP residues 34-390'  ? 
4 non-polymer syn 'CALCIUM ION'                       40.078    8  ? ? ?                      ? 
5 non-polymer man N-ACETYL-D-GLUCOSAMINE              221.208   32 ? ? ?                      ? 
6 non-polymer man BETA-D-MANNOSE                      180.156   12 ? ? ?                      ? 
7 non-polymer man ALPHA-D-MANNOSE                     180.156   22 ? ? ?                      ? 
8 non-polymer syn 'MANGANESE (II) ION'                54.938    6  ? ? ?                      ? 
9 water       nat water                               18.015    5  ? ? ?                      ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Vitronectin receptor subunit alpha' 
3 TGF-beta-1                           
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;FNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDY
AKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFS
IDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFV
SGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQ
RASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSG
CPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCL
KADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFM
EYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDTGGLE
;
;FNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDY
AKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFS
IDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFV
SGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQ
RASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSG
CPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCL
KADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFM
EYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDTGGLE
;
A,E     ? 
2 'polypeptide(L)' no no 
;TEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKPVSPFVKTTPEEIANPCSSIPYFCLPT
FGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVC
PNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENYAKLIPGATVGLLQKDSGNILQLIISA
YEELRSEVELEHHHHHH
;
;TEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKPVSPFVKTTPEEIANPCSSIPYFCLPT
FGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVC
PNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENYAKLIPGATVGLLQKDSGNILQLIISA
YEELRSEVELEHHHHHH
;
B,F     ? 
3 'polypeptide(L)' no no 
;GPLSTSKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKE
VTRVLMVETHNEIYDKFKQSTHSIYMFFQTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSQNSWRYLSNRLL
APSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLER
AQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHN
PGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS
;
;GPLSTSKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKE
VTRVLMVETHNEIYDKFKQSTHSIYMFFQTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSQNSWRYLSNRLL
APSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLER
AQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHN
PGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS
;
C,D,G,H ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PHE n 
1 2   ASN n 
1 3   LEU n 
1 4   ASP n 
1 5   VAL n 
1 6   ASP n 
1 7   SER n 
1 8   PRO n 
1 9   ALA n 
1 10  GLU n 
1 11  TYR n 
1 12  SER n 
1 13  GLY n 
1 14  PRO n 
1 15  GLU n 
1 16  GLY n 
1 17  SER n 
1 18  TYR n 
1 19  PHE n 
1 20  GLY n 
1 21  PHE n 
1 22  ALA n 
1 23  VAL n 
1 24  ASP n 
1 25  PHE n 
1 26  PHE n 
1 27  VAL n 
1 28  PRO n 
1 29  SER n 
1 30  ALA n 
1 31  SER n 
1 32  SER n 
1 33  ARG n 
1 34  MET n 
1 35  PHE n 
1 36  LEU n 
1 37  LEU n 
1 38  VAL n 
1 39  GLY n 
1 40  ALA n 
1 41  PRO n 
1 42  LYS n 
1 43  ALA n 
1 44  ASN n 
1 45  THR n 
1 46  THR n 
1 47  GLN n 
1 48  PRO n 
1 49  GLY n 
1 50  ILE n 
1 51  VAL n 
1 52  GLU n 
1 53  GLY n 
1 54  GLY n 
1 55  GLN n 
1 56  VAL n 
1 57  LEU n 
1 58  LYS n 
1 59  CYS n 
1 60  ASP n 
1 61  TRP n 
1 62  SER n 
1 63  SER n 
1 64  THR n 
1 65  ARG n 
1 66  ARG n 
1 67  CYS n 
1 68  GLN n 
1 69  PRO n 
1 70  ILE n 
1 71  GLU n 
1 72  PHE n 
1 73  ASP n 
1 74  ALA n 
1 75  THR n 
1 76  GLY n 
1 77  ASN n 
1 78  ARG n 
1 79  ASP n 
1 80  TYR n 
1 81  ALA n 
1 82  LYS n 
1 83  ASP n 
1 84  ASP n 
1 85  PRO n 
1 86  LEU n 
1 87  GLU n 
1 88  PHE n 
1 89  LYS n 
1 90  SER n 
1 91  HIS n 
1 92  GLN n 
1 93  TRP n 
1 94  PHE n 
1 95  GLY n 
1 96  ALA n 
1 97  SER n 
1 98  VAL n 
1 99  ARG n 
1 100 SER n 
1 101 LYS n 
1 102 GLN n 
1 103 ASP n 
1 104 LYS n 
1 105 ILE n 
1 106 LEU n 
1 107 ALA n 
1 108 CYS n 
1 109 ALA n 
1 110 PRO n 
1 111 LEU n 
1 112 TYR n 
1 113 HIS n 
1 114 TRP n 
1 115 ARG n 
1 116 THR n 
1 117 GLU n 
1 118 MET n 
1 119 LYS n 
1 120 GLN n 
1 121 GLU n 
1 122 ARG n 
1 123 GLU n 
1 124 PRO n 
1 125 VAL n 
1 126 GLY n 
1 127 THR n 
1 128 CYS n 
1 129 PHE n 
1 130 LEU n 
1 131 GLN n 
1 132 ASP n 
1 133 GLY n 
1 134 THR n 
1 135 LYS n 
1 136 THR n 
1 137 VAL n 
1 138 GLU n 
1 139 TYR n 
1 140 ALA n 
1 141 PRO n 
1 142 CYS n 
1 143 ARG n 
1 144 SER n 
1 145 GLN n 
1 146 ASP n 
1 147 ILE n 
1 148 ASP n 
1 149 ALA n 
1 150 ASP n 
1 151 GLY n 
1 152 GLN n 
1 153 GLY n 
1 154 PHE n 
1 155 CYS n 
1 156 GLN n 
1 157 GLY n 
1 158 GLY n 
1 159 PHE n 
1 160 SER n 
1 161 ILE n 
1 162 ASP n 
1 163 PHE n 
1 164 THR n 
1 165 LYS n 
1 166 ALA n 
1 167 ASP n 
1 168 ARG n 
1 169 VAL n 
1 170 LEU n 
1 171 LEU n 
1 172 GLY n 
1 173 GLY n 
1 174 PRO n 
1 175 GLY n 
1 176 SER n 
1 177 PHE n 
1 178 TYR n 
1 179 TRP n 
1 180 GLN n 
1 181 GLY n 
1 182 GLN n 
1 183 LEU n 
1 184 ILE n 
1 185 SER n 
1 186 ASP n 
1 187 GLN n 
1 188 VAL n 
1 189 ALA n 
1 190 GLU n 
1 191 ILE n 
1 192 VAL n 
1 193 SER n 
1 194 LYS n 
1 195 TYR n 
1 196 ASP n 
1 197 PRO n 
1 198 ASN n 
1 199 VAL n 
1 200 TYR n 
1 201 SER n 
1 202 ILE n 
1 203 LYS n 
1 204 TYR n 
1 205 ASN n 
1 206 ASN n 
1 207 GLN n 
1 208 LEU n 
1 209 ALA n 
1 210 THR n 
1 211 ARG n 
1 212 THR n 
1 213 ALA n 
1 214 GLN n 
1 215 ALA n 
1 216 ILE n 
1 217 PHE n 
1 218 ASP n 
1 219 ASP n 
1 220 SER n 
1 221 TYR n 
1 222 LEU n 
1 223 GLY n 
1 224 TYR n 
1 225 SER n 
1 226 VAL n 
1 227 ALA n 
1 228 VAL n 
1 229 GLY n 
1 230 ASP n 
1 231 PHE n 
1 232 ASN n 
1 233 GLY n 
1 234 ASP n 
1 235 GLY n 
1 236 ILE n 
1 237 ASP n 
1 238 ASP n 
1 239 PHE n 
1 240 VAL n 
1 241 SER n 
1 242 GLY n 
1 243 VAL n 
1 244 PRO n 
1 245 ARG n 
1 246 ALA n 
1 247 ALA n 
1 248 ARG n 
1 249 THR n 
1 250 LEU n 
1 251 GLY n 
1 252 MET n 
1 253 VAL n 
1 254 TYR n 
1 255 ILE n 
1 256 TYR n 
1 257 ASP n 
1 258 GLY n 
1 259 LYS n 
1 260 ASN n 
1 261 MET n 
1 262 SER n 
1 263 SER n 
1 264 LEU n 
1 265 TYR n 
1 266 ASN n 
1 267 PHE n 
1 268 THR n 
1 269 GLY n 
1 270 GLU n 
1 271 GLN n 
1 272 MET n 
1 273 ALA n 
1 274 ALA n 
1 275 TYR n 
1 276 PHE n 
1 277 GLY n 
1 278 PHE n 
1 279 SER n 
1 280 VAL n 
1 281 ALA n 
1 282 ALA n 
1 283 THR n 
1 284 ASP n 
1 285 ILE n 
1 286 ASN n 
1 287 GLY n 
1 288 ASP n 
1 289 ASP n 
1 290 TYR n 
1 291 ALA n 
1 292 ASP n 
1 293 VAL n 
1 294 PHE n 
1 295 ILE n 
1 296 GLY n 
1 297 ALA n 
1 298 PRO n 
1 299 LEU n 
1 300 PHE n 
1 301 MET n 
1 302 ASP n 
1 303 ARG n 
1 304 GLY n 
1 305 SER n 
1 306 ASP n 
1 307 GLY n 
1 308 LYS n 
1 309 LEU n 
1 310 GLN n 
1 311 GLU n 
1 312 VAL n 
1 313 GLY n 
1 314 GLN n 
1 315 VAL n 
1 316 SER n 
1 317 VAL n 
1 318 SER n 
1 319 LEU n 
1 320 GLN n 
1 321 ARG n 
1 322 ALA n 
1 323 SER n 
1 324 GLY n 
1 325 ASP n 
1 326 PHE n 
1 327 GLN n 
1 328 THR n 
1 329 THR n 
1 330 LYS n 
1 331 LEU n 
1 332 ASN n 
1 333 GLY n 
1 334 PHE n 
1 335 GLU n 
1 336 VAL n 
1 337 PHE n 
1 338 ALA n 
1 339 ARG n 
1 340 PHE n 
1 341 GLY n 
1 342 SER n 
1 343 ALA n 
1 344 ILE n 
1 345 ALA n 
1 346 PRO n 
1 347 LEU n 
1 348 GLY n 
1 349 ASP n 
1 350 LEU n 
1 351 ASP n 
1 352 GLN n 
1 353 ASP n 
1 354 GLY n 
1 355 PHE n 
1 356 ASN n 
1 357 ASP n 
1 358 ILE n 
1 359 ALA n 
1 360 ILE n 
1 361 ALA n 
1 362 ALA n 
1 363 PRO n 
1 364 TYR n 
1 365 GLY n 
1 366 GLY n 
1 367 GLU n 
1 368 ASP n 
1 369 LYS n 
1 370 LYS n 
1 371 GLY n 
1 372 ILE n 
1 373 VAL n 
1 374 TYR n 
1 375 ILE n 
1 376 PHE n 
1 377 ASN n 
1 378 GLY n 
1 379 ARG n 
1 380 SER n 
1 381 THR n 
1 382 GLY n 
1 383 LEU n 
1 384 ASN n 
1 385 ALA n 
1 386 VAL n 
1 387 PRO n 
1 388 SER n 
1 389 GLN n 
1 390 ILE n 
1 391 LEU n 
1 392 GLU n 
1 393 GLY n 
1 394 GLN n 
1 395 TRP n 
1 396 ALA n 
1 397 ALA n 
1 398 ARG n 
1 399 SER n 
1 400 GLY n 
1 401 CYS n 
1 402 PRO n 
1 403 PRO n 
1 404 SER n 
1 405 PHE n 
1 406 GLY n 
1 407 TYR n 
1 408 SER n 
1 409 MET n 
1 410 LYS n 
1 411 GLY n 
1 412 ALA n 
1 413 THR n 
1 414 ASP n 
1 415 ILE n 
1 416 ASP n 
1 417 LYS n 
1 418 ASN n 
1 419 GLY n 
1 420 TYR n 
1 421 PRO n 
1 422 ASP n 
1 423 LEU n 
1 424 ILE n 
1 425 VAL n 
1 426 GLY n 
1 427 ALA n 
1 428 PHE n 
1 429 GLY n 
1 430 VAL n 
1 431 ASP n 
1 432 ARG n 
1 433 ALA n 
1 434 ILE n 
1 435 LEU n 
1 436 TYR n 
1 437 ARG n 
1 438 ALA n 
1 439 ARG n 
1 440 PRO n 
1 441 VAL n 
1 442 ILE n 
1 443 THR n 
1 444 VAL n 
1 445 ASN n 
1 446 ALA n 
1 447 GLY n 
1 448 LEU n 
1 449 GLU n 
1 450 VAL n 
1 451 TYR n 
1 452 PRO n 
1 453 SER n 
1 454 ILE n 
1 455 LEU n 
1 456 ASN n 
1 457 GLN n 
1 458 ASP n 
1 459 ASN n 
1 460 LYS n 
1 461 THR n 
1 462 CYS n 
1 463 SER n 
1 464 LEU n 
1 465 PRO n 
1 466 GLY n 
1 467 THR n 
1 468 ALA n 
1 469 LEU n 
1 470 LYS n 
1 471 VAL n 
1 472 SER n 
1 473 CYS n 
1 474 PHE n 
1 475 ASN n 
1 476 VAL n 
1 477 ARG n 
1 478 PHE n 
1 479 CYS n 
1 480 LEU n 
1 481 LYS n 
1 482 ALA n 
1 483 ASP n 
1 484 GLY n 
1 485 LYS n 
1 486 GLY n 
1 487 VAL n 
1 488 LEU n 
1 489 PRO n 
1 490 ARG n 
1 491 LYS n 
1 492 LEU n 
1 493 ASN n 
1 494 PHE n 
1 495 GLN n 
1 496 VAL n 
1 497 GLU n 
1 498 LEU n 
1 499 LEU n 
1 500 LEU n 
1 501 ASP n 
1 502 LYS n 
1 503 LEU n 
1 504 LYS n 
1 505 GLN n 
1 506 LYS n 
1 507 GLY n 
1 508 ALA n 
1 509 ILE n 
1 510 ARG n 
1 511 ARG n 
1 512 ALA n 
1 513 LEU n 
1 514 PHE n 
1 515 LEU n 
1 516 TYR n 
1 517 SER n 
1 518 ARG n 
1 519 SER n 
1 520 PRO n 
1 521 SER n 
1 522 HIS n 
1 523 SER n 
1 524 LYS n 
1 525 ASN n 
1 526 MET n 
1 527 THR n 
1 528 ILE n 
1 529 SER n 
1 530 ARG n 
1 531 GLY n 
1 532 GLY n 
1 533 LEU n 
1 534 MET n 
1 535 GLN n 
1 536 CYS n 
1 537 GLU n 
1 538 GLU n 
1 539 LEU n 
1 540 ILE n 
1 541 ALA n 
1 542 TYR n 
1 543 LEU n 
1 544 ARG n 
1 545 ASP n 
1 546 GLU n 
1 547 SER n 
1 548 GLU n 
1 549 PHE n 
1 550 ARG n 
1 551 ASP n 
1 552 LYS n 
1 553 LEU n 
1 554 THR n 
1 555 PRO n 
1 556 ILE n 
1 557 THR n 
1 558 ILE n 
1 559 PHE n 
1 560 MET n 
1 561 GLU n 
1 562 TYR n 
1 563 ARG n 
1 564 LEU n 
1 565 ASP n 
1 566 TYR n 
1 567 ARG n 
1 568 THR n 
1 569 ALA n 
1 570 ALA n 
1 571 ASP n 
1 572 THR n 
1 573 THR n 
1 574 GLY n 
1 575 LEU n 
1 576 GLN n 
1 577 PRO n 
1 578 ILE n 
1 579 LEU n 
1 580 ASN n 
1 581 GLN n 
1 582 PHE n 
1 583 THR n 
1 584 PRO n 
1 585 ALA n 
1 586 ASN n 
1 587 ILE n 
1 588 SER n 
1 589 ARG n 
1 590 GLN n 
1 591 ALA n 
1 592 HIS n 
1 593 ILE n 
1 594 LEU n 
1 595 LEU n 
1 596 ASP n 
1 597 THR n 
1 598 GLY n 
1 599 GLY n 
1 600 LEU n 
1 601 GLU n 
2 1   THR n 
2 2   GLU n 
2 3   ASP n 
2 4   TYR n 
2 5   PRO n 
2 6   VAL n 
2 7   ASP n 
2 8   LEU n 
2 9   TYR n 
2 10  TYR n 
2 11  LEU n 
2 12  MET n 
2 13  ASP n 
2 14  LEU n 
2 15  SER n 
2 16  ALA n 
2 17  SER n 
2 18  MET n 
2 19  ASP n 
2 20  ASP n 
2 21  ASP n 
2 22  LEU n 
2 23  ASN n 
2 24  THR n 
2 25  ILE n 
2 26  LYS n 
2 27  GLU n 
2 28  LEU n 
2 29  GLY n 
2 30  SER n 
2 31  ARG n 
2 32  LEU n 
2 33  SER n 
2 34  LYS n 
2 35  GLU n 
2 36  MET n 
2 37  SER n 
2 38  LYS n 
2 39  LEU n 
2 40  THR n 
2 41  SER n 
2 42  ASN n 
2 43  PHE n 
2 44  ARG n 
2 45  LEU n 
2 46  GLY n 
2 47  PHE n 
2 48  GLY n 
2 49  SER n 
2 50  PHE n 
2 51  VAL n 
2 52  GLU n 
2 53  LYS n 
2 54  PRO n 
2 55  VAL n 
2 56  SER n 
2 57  PRO n 
2 58  PHE n 
2 59  VAL n 
2 60  LYS n 
2 61  THR n 
2 62  THR n 
2 63  PRO n 
2 64  GLU n 
2 65  GLU n 
2 66  ILE n 
2 67  ALA n 
2 68  ASN n 
2 69  PRO n 
2 70  CYS n 
2 71  SER n 
2 72  SER n 
2 73  ILE n 
2 74  PRO n 
2 75  TYR n 
2 76  PHE n 
2 77  CYS n 
2 78  LEU n 
2 79  PRO n 
2 80  THR n 
2 81  PHE n 
2 82  GLY n 
2 83  PHE n 
2 84  LYS n 
2 85  HIS n 
2 86  ILE n 
2 87  LEU n 
2 88  PRO n 
2 89  LEU n 
2 90  THR n 
2 91  ASN n 
2 92  ASP n 
2 93  ALA n 
2 94  GLU n 
2 95  ARG n 
2 96  PHE n 
2 97  ASN n 
2 98  GLU n 
2 99  ILE n 
2 100 VAL n 
2 101 LYS n 
2 102 ASN n 
2 103 GLN n 
2 104 LYS n 
2 105 ILE n 
2 106 SER n 
2 107 ALA n 
2 108 ASN n 
2 109 ILE n 
2 110 ASP n 
2 111 THR n 
2 112 PRO n 
2 113 GLU n 
2 114 GLY n 
2 115 GLY n 
2 116 PHE n 
2 117 ASP n 
2 118 ALA n 
2 119 ILE n 
2 120 MET n 
2 121 GLN n 
2 122 ALA n 
2 123 ALA n 
2 124 VAL n 
2 125 CYS n 
2 126 LYS n 
2 127 GLU n 
2 128 LYS n 
2 129 ILE n 
2 130 GLY n 
2 131 TRP n 
2 132 ARG n 
2 133 ASN n 
2 134 ASP n 
2 135 SER n 
2 136 LEU n 
2 137 HIS n 
2 138 LEU n 
2 139 LEU n 
2 140 VAL n 
2 141 PHE n 
2 142 VAL n 
2 143 SER n 
2 144 ASP n 
2 145 ALA n 
2 146 ASP n 
2 147 SER n 
2 148 HIS n 
2 149 PHE n 
2 150 GLY n 
2 151 MET n 
2 152 ASP n 
2 153 SER n 
2 154 LYS n 
2 155 LEU n 
2 156 ALA n 
2 157 GLY n 
2 158 ILE n 
2 159 VAL n 
2 160 CYS n 
2 161 PRO n 
2 162 ASN n 
2 163 ASP n 
2 164 GLY n 
2 165 LEU n 
2 166 CYS n 
2 167 HIS n 
2 168 LEU n 
2 169 ASP n 
2 170 SER n 
2 171 LYS n 
2 172 ASN n 
2 173 GLU n 
2 174 TYR n 
2 175 SER n 
2 176 MET n 
2 177 SER n 
2 178 THR n 
2 179 VAL n 
2 180 LEU n 
2 181 GLU n 
2 182 TYR n 
2 183 PRO n 
2 184 THR n 
2 185 ILE n 
2 186 GLY n 
2 187 GLN n 
2 188 LEU n 
2 189 ILE n 
2 190 ASP n 
2 191 LYS n 
2 192 LEU n 
2 193 VAL n 
2 194 GLN n 
2 195 ASN n 
2 196 ASN n 
2 197 VAL n 
2 198 LEU n 
2 199 LEU n 
2 200 ILE n 
2 201 PHE n 
2 202 ALA n 
2 203 VAL n 
2 204 THR n 
2 205 GLN n 
2 206 GLU n 
2 207 GLN n 
2 208 VAL n 
2 209 HIS n 
2 210 LEU n 
2 211 TYR n 
2 212 GLU n 
2 213 ASN n 
2 214 TYR n 
2 215 ALA n 
2 216 LYS n 
2 217 LEU n 
2 218 ILE n 
2 219 PRO n 
2 220 GLY n 
2 221 ALA n 
2 222 THR n 
2 223 VAL n 
2 224 GLY n 
2 225 LEU n 
2 226 LEU n 
2 227 GLN n 
2 228 LYS n 
2 229 ASP n 
2 230 SER n 
2 231 GLY n 
2 232 ASN n 
2 233 ILE n 
2 234 LEU n 
2 235 GLN n 
2 236 LEU n 
2 237 ILE n 
2 238 ILE n 
2 239 SER n 
2 240 ALA n 
2 241 TYR n 
2 242 GLU n 
2 243 GLU n 
2 244 LEU n 
2 245 ARG n 
2 246 SER n 
2 247 GLU n 
2 248 VAL n 
2 249 GLU n 
2 250 LEU n 
2 251 GLU n 
2 252 HIS n 
2 253 HIS n 
2 254 HIS n 
2 255 HIS n 
2 256 HIS n 
2 257 HIS n 
3 1   GLY n 
3 2   PRO n 
3 3   LEU n 
3 4   SER n 
3 5   THR n 
3 6   SER n 
3 7   LYS n 
3 8   THR n 
3 9   ILE n 
3 10  ASP n 
3 11  MET n 
3 12  GLU n 
3 13  LEU n 
3 14  VAL n 
3 15  LYS n 
3 16  ARG n 
3 17  LYS n 
3 18  ARG n 
3 19  ILE n 
3 20  GLU n 
3 21  ALA n 
3 22  ILE n 
3 23  ARG n 
3 24  GLY n 
3 25  GLN n 
3 26  ILE n 
3 27  LEU n 
3 28  SER n 
3 29  LYS n 
3 30  LEU n 
3 31  ARG n 
3 32  LEU n 
3 33  ALA n 
3 34  SER n 
3 35  PRO n 
3 36  PRO n 
3 37  SER n 
3 38  GLN n 
3 39  GLY n 
3 40  GLU n 
3 41  VAL n 
3 42  PRO n 
3 43  PRO n 
3 44  GLY n 
3 45  PRO n 
3 46  LEU n 
3 47  PRO n 
3 48  GLU n 
3 49  ALA n 
3 50  VAL n 
3 51  LEU n 
3 52  ALA n 
3 53  LEU n 
3 54  TYR n 
3 55  ASN n 
3 56  SER n 
3 57  THR n 
3 58  ARG n 
3 59  ASP n 
3 60  ARG n 
3 61  VAL n 
3 62  ALA n 
3 63  GLY n 
3 64  GLU n 
3 65  SER n 
3 66  ALA n 
3 67  GLU n 
3 68  PRO n 
3 69  GLU n 
3 70  PRO n 
3 71  GLU n 
3 72  PRO n 
3 73  GLU n 
3 74  ALA n 
3 75  ASP n 
3 76  TYR n 
3 77  TYR n 
3 78  ALA n 
3 79  LYS n 
3 80  GLU n 
3 81  VAL n 
3 82  THR n 
3 83  ARG n 
3 84  VAL n 
3 85  LEU n 
3 86  MET n 
3 87  VAL n 
3 88  GLU n 
3 89  THR n 
3 90  HIS n 
3 91  ASN n 
3 92  GLU n 
3 93  ILE n 
3 94  TYR n 
3 95  ASP n 
3 96  LYS n 
3 97  PHE n 
3 98  LYS n 
3 99  GLN n 
3 100 SER n 
3 101 THR n 
3 102 HIS n 
3 103 SER n 
3 104 ILE n 
3 105 TYR n 
3 106 MET n 
3 107 PHE n 
3 108 PHE n 
3 109 GLN n 
3 110 THR n 
3 111 SER n 
3 112 GLU n 
3 113 LEU n 
3 114 ARG n 
3 115 GLU n 
3 116 ALA n 
3 117 VAL n 
3 118 PRO n 
3 119 GLU n 
3 120 PRO n 
3 121 VAL n 
3 122 LEU n 
3 123 LEU n 
3 124 SER n 
3 125 ARG n 
3 126 ALA n 
3 127 GLU n 
3 128 LEU n 
3 129 ARG n 
3 130 LEU n 
3 131 LEU n 
3 132 ARG n 
3 133 LEU n 
3 134 LYS n 
3 135 LEU n 
3 136 LYS n 
3 137 VAL n 
3 138 GLU n 
3 139 GLN n 
3 140 HIS n 
3 141 VAL n 
3 142 GLU n 
3 143 LEU n 
3 144 TYR n 
3 145 GLN n 
3 146 LYS n 
3 147 TYR n 
3 148 SER n 
3 149 GLN n 
3 150 ASN n 
3 151 SER n 
3 152 TRP n 
3 153 ARG n 
3 154 TYR n 
3 155 LEU n 
3 156 SER n 
3 157 ASN n 
3 158 ARG n 
3 159 LEU n 
3 160 LEU n 
3 161 ALA n 
3 162 PRO n 
3 163 SER n 
3 164 ASP n 
3 165 SER n 
3 166 PRO n 
3 167 GLU n 
3 168 TRP n 
3 169 LEU n 
3 170 SER n 
3 171 PHE n 
3 172 ASP n 
3 173 VAL n 
3 174 THR n 
3 175 GLY n 
3 176 VAL n 
3 177 VAL n 
3 178 ARG n 
3 179 GLN n 
3 180 TRP n 
3 181 LEU n 
3 182 SER n 
3 183 ARG n 
3 184 GLY n 
3 185 GLY n 
3 186 GLU n 
3 187 ILE n 
3 188 GLU n 
3 189 GLY n 
3 190 PHE n 
3 191 ARG n 
3 192 LEU n 
3 193 SER n 
3 194 ALA n 
3 195 HIS n 
3 196 CYS n 
3 197 SER n 
3 198 CYS n 
3 199 ASP n 
3 200 SER n 
3 201 ARG n 
3 202 ASP n 
3 203 ASN n 
3 204 THR n 
3 205 LEU n 
3 206 GLN n 
3 207 VAL n 
3 208 ASP n 
3 209 ILE n 
3 210 ASN n 
3 211 GLY n 
3 212 PHE n 
3 213 THR n 
3 214 THR n 
3 215 GLY n 
3 216 ARG n 
3 217 ARG n 
3 218 GLY n 
3 219 ASP n 
3 220 LEU n 
3 221 ALA n 
3 222 THR n 
3 223 ILE n 
3 224 HIS n 
3 225 GLY n 
3 226 MET n 
3 227 ASN n 
3 228 ARG n 
3 229 PRO n 
3 230 PHE n 
3 231 LEU n 
3 232 LEU n 
3 233 LEU n 
3 234 MET n 
3 235 ALA n 
3 236 THR n 
3 237 PRO n 
3 238 LEU n 
3 239 GLU n 
3 240 ARG n 
3 241 ALA n 
3 242 GLN n 
3 243 HIS n 
3 244 LEU n 
3 245 GLN n 
3 246 SER n 
3 247 SER n 
3 248 ARG n 
3 249 HIS n 
3 250 ARG n 
3 251 ARG n 
3 252 ALA n 
3 253 LEU n 
3 254 ASP n 
3 255 THR n 
3 256 ASN n 
3 257 TYR n 
3 258 CYS n 
3 259 PHE n 
3 260 SER n 
3 261 SER n 
3 262 THR n 
3 263 GLU n 
3 264 LYS n 
3 265 ASN n 
3 266 CYS n 
3 267 CYS n 
3 268 VAL n 
3 269 ARG n 
3 270 GLN n 
3 271 LEU n 
3 272 TYR n 
3 273 ILE n 
3 274 ASP n 
3 275 PHE n 
3 276 ARG n 
3 277 LYS n 
3 278 ASP n 
3 279 LEU n 
3 280 GLY n 
3 281 TRP n 
3 282 LYS n 
3 283 TRP n 
3 284 ILE n 
3 285 HIS n 
3 286 GLU n 
3 287 PRO n 
3 288 LYS n 
3 289 GLY n 
3 290 TYR n 
3 291 HIS n 
3 292 ALA n 
3 293 ASN n 
3 294 PHE n 
3 295 CYS n 
3 296 LEU n 
3 297 GLY n 
3 298 PRO n 
3 299 CYS n 
3 300 PRO n 
3 301 TYR n 
3 302 ILE n 
3 303 TRP n 
3 304 SER n 
3 305 LEU n 
3 306 ASP n 
3 307 THR n 
3 308 GLN n 
3 309 TYR n 
3 310 SER n 
3 311 LYS n 
3 312 VAL n 
3 313 LEU n 
3 314 ALA n 
3 315 LEU n 
3 316 TYR n 
3 317 ASN n 
3 318 GLN n 
3 319 HIS n 
3 320 ASN n 
3 321 PRO n 
3 322 GLY n 
3 323 ALA n 
3 324 SER n 
3 325 ALA n 
3 326 ALA n 
3 327 PRO n 
3 328 CYS n 
3 329 CYS n 
3 330 VAL n 
3 331 PRO n 
3 332 GLN n 
3 333 ALA n 
3 334 LEU n 
3 335 GLU n 
3 336 PRO n 
3 337 LEU n 
3 338 PRO n 
3 339 ILE n 
3 340 VAL n 
3 341 TYR n 
3 342 TYR n 
3 343 VAL n 
3 344 GLY n 
3 345 ARG n 
3 346 LYS n 
3 347 PRO n 
3 348 LYS n 
3 349 VAL n 
3 350 GLU n 
3 351 GLN n 
3 352 LEU n 
3 353 SER n 
3 354 ASN n 
3 355 MET n 
3 356 ILE n 
3 357 VAL n 
3 358 ARG n 
3 359 SER n 
3 360 CYS n 
3 361 LYS n 
3 362 CYS n 
3 363 SER n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 601 Human ? 'ITGAV, MSK8, VNRA' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 257 Human ? ITGB6               ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 363 Human ? 'TGFB1, TGFB'       ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP ITAV_HUMAN  P06756 ? 1 
;FNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDY
AKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFS
IDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFV
SGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQ
RASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSM
PPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLK
ADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFME
YRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCG
;
31  
2 UNP ITB6_HUMAN  P18564 ? 2 
;TEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKPVSPFVKTTPEEIANPCSSIPYFCLPT
FGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVI
PNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENYAKLIPGATVGLLQKDSGNILQLIISA
YEELRSEVELE
;
128 
3 UNP TGFB1_HUMAN P01137 ? 3 
;KTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLM
VETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSP
EWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQS
SRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAA
PCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS
;
34  
# 
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 5FFO A 1 ? 598 ? P06756 31  ? 627 ? 1   598 
2 2 5FFO B 1 ? 251 ? P18564 128 ? 378 ? 111 361 
3 3 5FFO C 7 ? 363 ? P01137 34  ? 390 ? 5   361 
4 3 5FFO D 7 ? 363 ? P01137 34  ? 390 ? 5   361 
5 1 5FFO E 1 ? 598 ? P06756 31  ? 627 ? 1   598 
6 2 5FFO F 1 ? 251 ? P18564 128 ? 378 ? 111 361 
7 3 5FFO G 7 ? 363 ? P01137 34  ? 390 ? 5   361 
8 3 5FFO H 7 ? 363 ? P01137 34  ? 390 ? 5   361 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 5FFO GLY A 400 ? UNP P06756 ?   ?   insertion        400 1  
1 5FFO CYS A 401 ? UNP P06756 MET 430 conflict         401 2  
1 5FFO THR A 597 ? UNP P06756 CYS 626 conflict         597 3  
1 5FFO GLY A 599 ? UNP P06756 ?   ?   'expression tag' 599 4  
1 5FFO LEU A 600 ? UNP P06756 ?   ?   'expression tag' 600 5  
1 5FFO GLU A 601 ? UNP P06756 ?   ?   'expression tag' 601 6  
2 5FFO CYS B 160 ? UNP P18564 ILE 287 conflict         270 7  
2 5FFO HIS B 252 ? UNP P18564 ?   ?   'expression tag' 362 8  
2 5FFO HIS B 253 ? UNP P18564 ?   ?   'expression tag' 363 9  
2 5FFO HIS B 254 ? UNP P18564 ?   ?   'expression tag' 364 10 
2 5FFO HIS B 255 ? UNP P18564 ?   ?   'expression tag' 365 11 
2 5FFO HIS B 256 ? UNP P18564 ?   ?   'expression tag' 366 12 
2 5FFO HIS B 257 ? UNP P18564 ?   ?   'expression tag' 367 13 
3 5FFO GLY C 1   ? UNP P01137 ?   ?   'expression tag' -1  14 
3 5FFO PRO C 2   ? UNP P01137 ?   ?   'expression tag' 0   15 
3 5FFO LEU C 3   ? UNP P01137 ?   ?   'expression tag' 1   16 
3 5FFO SER C 4   ? UNP P01137 ?   ?   'expression tag' 2   17 
3 5FFO THR C 5   ? UNP P01137 ?   ?   'expression tag' 3   18 
3 5FFO SER C 6   ? UNP P01137 ?   ?   'expression tag' 4   19 
3 5FFO GLN C 109 ? UNP P01137 ASN 136 conflict         107 20 
3 5FFO GLN C 149 ? UNP P01137 ASN 176 conflict         147 21 
4 5FFO GLY D 1   ? UNP P01137 ?   ?   'expression tag' -1  22 
4 5FFO PRO D 2   ? UNP P01137 ?   ?   'expression tag' 0   23 
4 5FFO LEU D 3   ? UNP P01137 ?   ?   'expression tag' 1   24 
4 5FFO SER D 4   ? UNP P01137 ?   ?   'expression tag' 2   25 
4 5FFO THR D 5   ? UNP P01137 ?   ?   'expression tag' 3   26 
4 5FFO SER D 6   ? UNP P01137 ?   ?   'expression tag' 4   27 
4 5FFO GLN D 109 ? UNP P01137 ASN 136 conflict         107 28 
4 5FFO GLN D 149 ? UNP P01137 ASN 176 conflict         147 29 
5 5FFO GLY E 400 ? UNP P06756 ?   ?   insertion        400 30 
5 5FFO CYS E 401 ? UNP P06756 MET 430 conflict         401 31 
5 5FFO THR E 597 ? UNP P06756 CYS 626 conflict         597 32 
5 5FFO GLY E 599 ? UNP P06756 ?   ?   'expression tag' 599 33 
5 5FFO LEU E 600 ? UNP P06756 ?   ?   'expression tag' 600 34 
5 5FFO GLU E 601 ? UNP P06756 ?   ?   'expression tag' 601 35 
6 5FFO CYS F 160 ? UNP P18564 ILE 287 conflict         270 36 
6 5FFO HIS F 252 ? UNP P18564 ?   ?   'expression tag' 362 37 
6 5FFO HIS F 253 ? UNP P18564 ?   ?   'expression tag' 363 38 
6 5FFO HIS F 254 ? UNP P18564 ?   ?   'expression tag' 364 39 
6 5FFO HIS F 255 ? UNP P18564 ?   ?   'expression tag' 365 40 
6 5FFO HIS F 256 ? UNP P18564 ?   ?   'expression tag' 366 41 
6 5FFO HIS F 257 ? UNP P18564 ?   ?   'expression tag' 367 42 
7 5FFO GLY G 1   ? UNP P01137 ?   ?   'expression tag' -1  43 
7 5FFO PRO G 2   ? UNP P01137 ?   ?   'expression tag' 0   44 
7 5FFO LEU G 3   ? UNP P01137 ?   ?   'expression tag' 1   45 
7 5FFO SER G 4   ? UNP P01137 ?   ?   'expression tag' 2   46 
7 5FFO THR G 5   ? UNP P01137 ?   ?   'expression tag' 3   47 
7 5FFO SER G 6   ? UNP P01137 ?   ?   'expression tag' 4   48 
7 5FFO GLN G 109 ? UNP P01137 ASN 136 conflict         107 49 
7 5FFO GLN G 149 ? UNP P01137 ASN 176 conflict         147 50 
8 5FFO GLY H 1   ? UNP P01137 ?   ?   'expression tag' -1  51 
8 5FFO PRO H 2   ? UNP P01137 ?   ?   'expression tag' 0   52 
8 5FFO LEU H 3   ? UNP P01137 ?   ?   'expression tag' 1   53 
8 5FFO SER H 4   ? UNP P01137 ?   ?   'expression tag' 2   54 
8 5FFO THR H 5   ? UNP P01137 ?   ?   'expression tag' 3   55 
8 5FFO SER H 6   ? UNP P01137 ?   ?   'expression tag' 4   56 
8 5FFO GLN H 109 ? UNP P01137 ASN 136 conflict         107 57 
8 5FFO GLN H 149 ? UNP P01137 ASN 176 conflict         147 58 
# 
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 
BMA D-saccharide        . BETA-D-MANNOSE         ? 'C6 H12 O6'      180.156 
CA  non-polymer         . 'CALCIUM ION'          ? 'Ca 2'           40.078  
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                  ? 'H2 O'           18.015  
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 
MAN D-saccharide        . ALPHA-D-MANNOSE        ? 'C6 H12 O6'      180.156 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
MN  non-polymer         . 'MANGANESE (II) ION'   ? 'Mn 2'           54.938  
NAG D-saccharide        . 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 
# 
_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                   5FFO 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.74 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         55.13 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;8% PEG8000
0.1M Immidazole
;
_exptl_crystal_grow.pdbx_pH_range   7.5-8.0 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MAR CCD 165 mm' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-07-27 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.03318 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.03318 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5FFO 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                3.49 
_reflns.d_resolution_low                 50 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       45279 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             94.6 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  1.8 
_reflns.pdbx_Rmerge_I_obs                0.168 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            4.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     0.988 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  3.5 
_reflns_shell.d_res_low                   3.64 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         0.4 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.percent_possible_all        97.1 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.pdbx_redundancy             1.8 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 5FFO 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     45279 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.91 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             45.720 
_refine.ls_d_res_high                            3.490 
_refine.ls_percent_reflns_obs                    94.40 
_refine.ls_R_factor_obs                          0.2257 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2236 
_refine.ls_R_factor_R_free                       0.2774 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 2.46 
_refine.ls_number_reflns_R_free                  1116 
_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                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       TWIN_LSQ_F 
_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                 27.95 
_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          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        22945 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         836 
_refine_hist.number_atoms_solvent             5 
_refine_hist.number_atoms_total               23786 
_refine_hist.d_res_high                       3.490 
_refine_hist.d_res_low                        45.720 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.007  ? ? 24469 'X-RAY DIFFRACTION' ? 
f_angle_d          0.798  ? ? 33145 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 11.435 ? ? 14775 'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.045  ? ? 3786  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.004  ? ? 4184  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' . 3.4948 3.6535  5647 0.2814 95.00 0.3078 . . 139 . . . . 
'X-RAY DIFFRACTION' . 3.6535 3.8456  5610 0.2832 94.00 0.2944 . . 129 . . . . 
'X-RAY DIFFRACTION' . 3.8456 4.0859  5609 0.2889 94.00 0.2905 . . 135 . . . . 
'X-RAY DIFFRACTION' . 4.0859 4.4002  5430 0.2809 92.00 0.3565 . . 147 . . . . 
'X-RAY DIFFRACTION' . 4.4002 4.8408  5551 0.2504 93.00 0.3077 . . 120 . . . . 
'X-RAY DIFFRACTION' . 4.8408 5.5364  5496 0.2258 93.00 0.2611 . . 138 . . . . 
'X-RAY DIFFRACTION' . 5.5364 6.9568  5485 0.2132 92.00 0.3155 . . 124 . . . . 
'X-RAY DIFFRACTION' . 6.9568 27.6276 5273 0.1668 89.00 0.2328 . . 126 . . . . 
# 
_struct.entry_id                     5FFO 
_struct.title                        'Integrin alpha V beta 6 in complex with pro-TGF-beta' 
_struct.pdbx_descriptor              'Integrin alpha-V, Integrin beta-6, Transforming growth factor beta-1' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5FFO 
_struct_keywords.text            'Integrin, TGF-beta, CELL ADHESION' 
_struct_keywords.pdbx_keywords   'CELL ADHESION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 2 ? 
C  N N 3 ? 
D  N N 3 ? 
E  N N 1 ? 
F  N N 2 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 4 ? 
J  N N 4 ? 
K  N N 4 ? 
L  N N 4 ? 
M  N N 5 ? 
N  N N 5 ? 
O  N N 6 ? 
P  N N 5 ? 
Q  N N 5 ? 
R  N N 6 ? 
S  N N 7 ? 
T  N N 7 ? 
U  N N 7 ? 
V  N N 5 ? 
W  N N 5 ? 
X  N N 6 ? 
Y  N N 7 ? 
Z  N N 7 ? 
AA N N 7 ? 
BA N N 7 ? 
CA N N 5 ? 
DA N N 5 ? 
EA N N 6 ? 
FA N N 7 ? 
GA N N 5 ? 
HA N N 5 ? 
IA N N 5 ? 
JA N N 8 ? 
KA N N 8 ? 
LA N N 8 ? 
MA N N 5 ? 
NA N N 5 ? 
OA N N 5 ? 
PA N N 6 ? 
QA N N 7 ? 
RA N N 5 ? 
SA N N 5 ? 
TA N N 6 ? 
UA N N 7 ? 
VA N N 4 ? 
WA N N 4 ? 
XA N N 4 ? 
YA N N 4 ? 
ZA N N 5 ? 
AB N N 5 ? 
BB N N 6 ? 
CB N N 5 ? 
DB N N 5 ? 
EB N N 6 ? 
FB N N 7 ? 
GB N N 7 ? 
HB N N 7 ? 
IB N N 5 ? 
JB N N 5 ? 
KB N N 6 ? 
LB N N 7 ? 
MB N N 7 ? 
NB N N 7 ? 
OB N N 7 ? 
PB N N 5 ? 
QB N N 5 ? 
RB N N 6 ? 
SB N N 7 ? 
TB N N 5 ? 
UB N N 5 ? 
VB N N 5 ? 
WB N N 8 ? 
XB N N 8 ? 
YB N N 8 ? 
ZB N N 5 ? 
AC N N 5 ? 
BC N N 5 ? 
CC N N 6 ? 
DC N N 7 ? 
EC N N 5 ? 
FC N N 5 ? 
GC N N 6 ? 
HC N N 7 ? 
IC N N 7 ? 
JC N N 7 ? 
KC N N 9 ? 
LC N N 9 ? 
# 
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 GLY A 175 ? GLN A 180 ? GLY A 175 GLN A 180 1 ? 6  
HELX_P HELX_P2  AA2 VAL A 188 ? LYS A 194 ? VAL A 188 LYS A 194 1 ? 7  
HELX_P HELX_P3  AA3 GLN A 214 ? ASP A 218 ? GLN A 214 ASP A 218 5 ? 5  
HELX_P HELX_P4  AA4 ARG A 245 ? LEU A 250 ? ARG A 245 LEU A 250 1 ? 6  
HELX_P HELX_P5  AA5 GLY A 366 ? LYS A 370 ? GLY A 366 LYS A 370 5 ? 5  
HELX_P HELX_P6  AA6 ASP A 545 ? PHE A 549 ? ASP A 545 PHE A 549 5 ? 5  
HELX_P HELX_P7  AA7 TYR A 566 ? ALA A 570 ? TYR A 566 ALA A 570 5 ? 5  
HELX_P HELX_P8  AA8 SER B 15  ? ASP B 19  ? SER B 125 ASP B 129 5 ? 5  
HELX_P HELX_P9  AA9 ASP B 21  ? THR B 40  ? ASP B 131 THR B 150 1 ? 20 
HELX_P HELX_P10 AB1 THR B 62  ? ASN B 68  ? THR B 172 ASN B 178 1 ? 7  
HELX_P HELX_P11 AB2 ALA B 93  ? ASN B 102 ? ALA B 203 ASN B 212 1 ? 10 
HELX_P HELX_P12 AB3 GLY B 114 ? CYS B 125 ? GLY B 224 CYS B 235 1 ? 12 
HELX_P HELX_P13 AB4 MET B 151 ? LEU B 155 ? MET B 261 LEU B 265 5 ? 5  
HELX_P HELX_P14 AB5 THR B 184 ? ASN B 195 ? THR B 294 ASN B 305 1 ? 12 
HELX_P HELX_P15 AB6 THR B 204 ? ILE B 218 ? THR B 314 ILE B 328 1 ? 15 
HELX_P HELX_P16 AB7 SER B 230 ? SER B 239 ? SER B 340 SER B 349 1 ? 10 
HELX_P HELX_P17 AB8 MET C 11  ? LEU C 30  ? MET C 9   LEU C 28  1 ? 20 
HELX_P HELX_P18 AB9 PRO C 47  ? ARG C 58  ? PRO C 45  ARG C 56  1 ? 12 
HELX_P HELX_P19 AC1 THR C 110 ? VAL C 117 ? THR C 108 VAL C 115 1 ? 8  
HELX_P HELX_P20 AC2 VAL C 173 ? ARG C 183 ? VAL C 171 ARG C 181 1 ? 11 
HELX_P HELX_P21 AC3 PRO C 237 ? GLN C 242 ? PRO C 235 GLN C 240 1 ? 6  
HELX_P HELX_P22 AC4 ASP C 254 ? PHE C 259 ? ASP C 252 PHE C 257 1 ? 6  
HELX_P HELX_P23 AC5 LEU D 13  ? LEU D 30  ? LEU D 11  LEU D 28  1 ? 18 
HELX_P HELX_P24 AC6 PRO D 47  ? ARG D 58  ? PRO D 45  ARG D 56  1 ? 12 
HELX_P HELX_P25 AC7 GLU D 112 ? VAL D 117 ? GLU D 110 VAL D 115 1 ? 6  
HELX_P HELX_P26 AC8 GLU D 119 ? VAL D 121 ? GLU D 117 VAL D 119 5 ? 3  
HELX_P HELX_P27 AC9 VAL D 173 ? ARG D 183 ? VAL D 171 ARG D 181 1 ? 11 
HELX_P HELX_P28 AD1 ASP D 219 ? MET D 226 ? ASP D 217 MET D 224 5 ? 8  
HELX_P HELX_P29 AD2 GLY E 175 ? GLN E 180 ? GLY E 175 GLN E 180 1 ? 6  
HELX_P HELX_P30 AD3 VAL E 188 ? LYS E 194 ? VAL E 188 LYS E 194 1 ? 7  
HELX_P HELX_P31 AD4 GLN E 214 ? ASP E 218 ? GLN E 214 ASP E 218 5 ? 5  
HELX_P HELX_P32 AD5 ARG E 245 ? LEU E 250 ? ARG E 245 LEU E 250 1 ? 6  
HELX_P HELX_P33 AD6 GLY E 366 ? LYS E 370 ? GLY E 366 LYS E 370 5 ? 5  
HELX_P HELX_P34 AD7 PHE E 428 ? VAL E 430 ? PHE E 428 VAL E 430 5 ? 3  
HELX_P HELX_P35 AD8 ASP E 545 ? PHE E 549 ? ASP E 545 PHE E 549 5 ? 5  
HELX_P HELX_P36 AD9 TYR E 566 ? ALA E 570 ? TYR E 566 ALA E 570 5 ? 5  
HELX_P HELX_P37 AE1 SER F 15  ? ASP F 19  ? SER F 125 ASP F 129 5 ? 5  
HELX_P HELX_P38 AE2 ASP F 21  ? THR F 40  ? ASP F 131 THR F 150 1 ? 20 
HELX_P HELX_P39 AE3 THR F 62  ? ASN F 68  ? THR F 172 ASN F 178 1 ? 7  
HELX_P HELX_P40 AE4 ALA F 93  ? ASN F 102 ? ALA F 203 ASN F 212 1 ? 10 
HELX_P HELX_P41 AE5 GLY F 114 ? CYS F 125 ? GLY F 224 CYS F 235 1 ? 12 
HELX_P HELX_P42 AE6 MET F 151 ? LEU F 155 ? MET F 261 LEU F 265 5 ? 5  
HELX_P HELX_P43 AE7 THR F 184 ? VAL F 193 ? THR F 294 VAL F 303 1 ? 10 
HELX_P HELX_P44 AE8 THR F 204 ? ILE F 218 ? THR F 314 ILE F 328 1 ? 15 
HELX_P HELX_P45 AE9 SER F 230 ? SER F 239 ? SER F 340 SER F 349 1 ? 10 
HELX_P HELX_P46 AF1 LEU G 13  ? LEU G 30  ? LEU G 11  LEU G 28  1 ? 18 
HELX_P HELX_P47 AF2 PRO G 47  ? ARG G 58  ? PRO G 45  ARG G 56  1 ? 12 
HELX_P HELX_P48 AF3 THR G 110 ? VAL G 117 ? THR G 108 VAL G 115 1 ? 8  
HELX_P HELX_P49 AF4 VAL G 173 ? ARG G 183 ? VAL G 171 ARG G 181 1 ? 11 
HELX_P HELX_P50 AF5 PRO G 237 ? GLN G 242 ? PRO G 235 GLN G 240 1 ? 6  
HELX_P HELX_P51 AF6 ASP G 254 ? PHE G 259 ? ASP G 252 PHE G 257 1 ? 6  
HELX_P HELX_P52 AF7 GLU H 12  ? LEU H 30  ? GLU H 10  LEU H 28  1 ? 19 
HELX_P HELX_P53 AF8 PRO H 47  ? ARG H 58  ? PRO H 45  ARG H 56  1 ? 12 
HELX_P HELX_P54 AF9 GLU H 112 ? VAL H 117 ? GLU H 110 VAL H 115 1 ? 6  
HELX_P HELX_P55 AG1 GLU H 119 ? VAL H 121 ? GLU H 117 VAL H 119 5 ? 3  
HELX_P HELX_P56 AG2 VAL H 173 ? ARG H 183 ? VAL H 171 ARG H 181 1 ? 11 
HELX_P HELX_P57 AG3 ASP H 219 ? MET H 226 ? ASP H 217 MET H 224 5 ? 8  
# 
_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 
disulf1  disulf ?    ? A  CYS 59  SG  ? ? ? 1_555 A  CYS 67  SG ? ? A CYS 59   A CYS 67   1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf2  disulf ?    ? A  CYS 108 SG  ? ? ? 1_555 A  CYS 128 SG ? ? A CYS 108  A CYS 128  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf3  disulf ?    ? A  CYS 142 SG  ? ? ? 1_555 A  CYS 155 SG ? ? A CYS 142  A CYS 155  1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf4  disulf ?    ? A  CYS 401 SG  ? ? ? 1_555 B  CYS 160 SG ? ? A CYS 401  B CYS 270  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf5  disulf ?    ? A  CYS 462 SG  ? ? ? 1_555 A  CYS 473 SG ? ? A CYS 462  A CYS 473  1_555 ? ? ? ? ? ? ? 2.024 ? 
disulf6  disulf ?    ? A  CYS 479 SG  ? ? ? 1_555 A  CYS 536 SG ? ? A CYS 479  A CYS 536  1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf7  disulf ?    ? B  CYS 70  SG  ? ? ? 1_555 B  CYS 77  SG ? ? B CYS 180  B CYS 187  1_555 ? ? ? ? ? ? ? 2.023 ? 
disulf8  disulf ?    ? B  CYS 125 SG  ? ? ? 1_555 B  CYS 166 SG ? ? B CYS 235  B CYS 276  1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf9  disulf ?    ? C  CYS 196 SG  ? ? ? 1_555 D  CYS 198 SG ? ? C CYS 194  D CYS 196  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf10 disulf ?    ? C  CYS 198 SG  ? ? ? 1_555 D  CYS 196 SG ? ? C CYS 196  D CYS 194  1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf11 disulf ?    ? C  CYS 258 SG  ? ? ? 1_555 C  CYS 267 SG ? ? C CYS 256  C CYS 265  1_555 ? ? ? ? ? ? ? 2.023 ? 
disulf12 disulf ?    ? C  CYS 266 SG  ? ? ? 1_555 C  CYS 329 SG ? ? C CYS 264  C CYS 327  1_555 ? ? ? ? ? ? ? 2.029 ? 
disulf13 disulf ?    ? C  CYS 295 SG  ? ? ? 1_555 C  CYS 360 SG ? ? C CYS 293  C CYS 358  1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf14 disulf ?    ? C  CYS 299 SG  ? ? ? 1_555 C  CYS 362 SG ? ? C CYS 297  C CYS 360  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf15 disulf ?    ? C  CYS 328 SG  ? ? ? 1_555 D  CYS 328 SG ? ? C CYS 326  D CYS 326  1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf16 disulf ?    ? D  CYS 258 SG  ? ? ? 1_555 D  CYS 267 SG ? ? D CYS 256  D CYS 265  1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf17 disulf ?    ? D  CYS 266 SG  ? ? ? 1_555 D  CYS 329 SG ? ? D CYS 264  D CYS 327  1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf18 disulf ?    ? D  CYS 295 SG  ? ? ? 1_555 D  CYS 360 SG ? ? D CYS 293  D CYS 358  1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf19 disulf ?    ? D  CYS 299 SG  ? ? ? 1_555 D  CYS 362 SG ? ? D CYS 297  D CYS 360  1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf20 disulf ?    ? E  CYS 59  SG  ? ? ? 1_555 E  CYS 67  SG ? ? E CYS 59   E CYS 67   1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf21 disulf ?    ? E  CYS 108 SG  ? ? ? 1_555 E  CYS 128 SG ? ? E CYS 108  E CYS 128  1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf22 disulf ?    ? E  CYS 142 SG  ? ? ? 1_555 E  CYS 155 SG ? ? E CYS 142  E CYS 155  1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf23 disulf ?    ? E  CYS 401 SG  ? ? ? 1_555 F  CYS 160 SG ? ? E CYS 401  F CYS 270  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf24 disulf ?    ? E  CYS 462 SG  ? ? ? 1_555 E  CYS 473 SG ? ? E CYS 462  E CYS 473  1_555 ? ? ? ? ? ? ? 2.024 ? 
disulf25 disulf ?    ? E  CYS 479 SG  ? ? ? 1_555 E  CYS 536 SG ? ? E CYS 479  E CYS 536  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf26 disulf ?    ? F  CYS 70  SG  ? ? ? 1_555 F  CYS 77  SG ? ? F CYS 180  F CYS 187  1_555 ? ? ? ? ? ? ? 2.026 ? 
disulf27 disulf ?    ? F  CYS 125 SG  ? ? ? 1_555 F  CYS 166 SG ? ? F CYS 235  F CYS 276  1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf28 disulf ?    ? G  CYS 196 SG  ? ? ? 1_555 H  CYS 198 SG ? ? G CYS 194  H CYS 196  1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf29 disulf ?    ? G  CYS 198 SG  ? ? ? 1_555 H  CYS 196 SG ? ? G CYS 196  H CYS 194  1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf30 disulf ?    ? G  CYS 258 SG  ? ? ? 1_555 G  CYS 267 SG ? ? G CYS 256  G CYS 265  1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf31 disulf ?    ? G  CYS 266 SG  ? ? ? 1_555 G  CYS 329 SG ? ? G CYS 264  G CYS 327  1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf32 disulf ?    ? G  CYS 295 SG  ? ? ? 1_555 G  CYS 360 SG ? ? G CYS 293  G CYS 358  1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf33 disulf ?    ? G  CYS 299 SG  ? ? ? 1_555 G  CYS 362 SG ? ? G CYS 297  G CYS 360  1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf34 disulf ?    ? G  CYS 328 SG  ? ? ? 1_555 H  CYS 328 SG ? ? G CYS 326  H CYS 326  1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf35 disulf ?    ? H  CYS 266 SG  ? ? ? 1_555 H  CYS 329 SG ? ? H CYS 264  H CYS 327  1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf36 disulf ?    ? H  CYS 295 SG  ? ? ? 1_555 H  CYS 360 SG ? ? H CYS 293  H CYS 358  1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf37 disulf ?    ? H  CYS 299 SG  ? ? ? 1_555 H  CYS 362 SG ? ? H CYS 297  H CYS 360  1_555 ? ? ? ? ? ? ? 2.043 ? 
covale1  covale one  ? A  ASN 44  ND2 ? ? ? 1_555 M  NAG .   C1 ? ? A ASN 44   A NAG 2005 1_555 ? ? ? ? ? ? ? 1.443 ? 
metalc1  metalc ?    ? A  ASP 230 OD1 ? ? ? 1_555 L  CA  .   CA ? ? A ASP 230  A CA  2004 1_555 ? ? ? ? ? ? ? 2.569 ? 
metalc2  metalc ?    ? A  ASN 232 OD1 ? ? ? 1_555 L  CA  .   CA ? ? A ASN 232  A CA  2004 1_555 ? ? ? ? ? ? ? 2.287 ? 
metalc3  metalc ?    ? A  ASP 234 OD1 ? ? ? 1_555 L  CA  .   CA ? ? A ASP 234  A CA  2004 1_555 ? ? ? ? ? ? ? 2.330 ? 
metalc4  metalc ?    ? A  ILE 236 O   ? ? ? 1_555 L  CA  .   CA ? ? A ILE 236  A CA  2004 1_555 ? ? ? ? ? ? ? 2.180 ? 
metalc5  metalc ?    ? A  ASP 238 OD1 ? ? ? 1_555 L  CA  .   CA ? ? A ASP 238  A CA  2004 1_555 ? ? ? ? ? ? ? 2.338 ? 
metalc6  metalc ?    ? A  ASP 238 OD2 ? ? ? 1_555 L  CA  .   CA ? ? A ASP 238  A CA  2004 1_555 ? ? ? ? ? ? ? 2.438 ? 
covale2  covale one  ? A  ASN 260 ND2 ? ? ? 1_555 P  NAG .   C1 ? ? A ASN 260  A NAG 2008 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale3  covale one  ? A  ASN 266 ND2 ? ? ? 1_555 V  NAG .   C1 ? ? A ASN 266  A NAG 2014 1_555 ? ? ? ? ? ? ? 1.433 ? 
metalc7  metalc ?    ? A  ASP 284 OD1 ? ? ? 1_555 I  CA  .   CA ? ? A ASP 284  A CA  2001 1_555 ? ? ? ? ? ? ? 2.340 ? 
metalc8  metalc ?    ? A  ASN 286 OD1 ? ? ? 1_555 I  CA  .   CA ? ? A ASN 286  A CA  2001 1_555 ? ? ? ? ? ? ? 2.380 ? 
metalc9  metalc ?    ? A  ASP 288 OD1 ? ? ? 1_555 I  CA  .   CA ? ? A ASP 288  A CA  2001 1_555 ? ? ? ? ? ? ? 2.401 ? 
metalc10 metalc ?    ? A  TYR 290 O   ? ? ? 1_555 I  CA  .   CA ? ? A TYR 290  A CA  2001 1_555 ? ? ? ? ? ? ? 2.244 ? 
metalc11 metalc ?    ? A  ASP 292 OD1 ? ? ? 1_555 I  CA  .   CA ? ? A ASP 292  A CA  2001 1_555 ? ? ? ? ? ? ? 2.326 ? 
metalc12 metalc ?    ? A  ASP 292 OD2 ? ? ? 1_555 I  CA  .   CA ? ? A ASP 292  A CA  2001 1_555 ? ? ? ? ? ? ? 2.369 ? 
metalc13 metalc ?    ? A  ASP 349 OD1 ? ? ? 1_555 J  CA  .   CA ? ? A ASP 349  A CA  2002 1_555 ? ? ? ? ? ? ? 2.589 ? 
metalc14 metalc ?    ? A  ASP 351 OD1 ? ? ? 1_555 J  CA  .   CA ? ? A ASP 351  A CA  2002 1_555 ? ? ? ? ? ? ? 2.477 ? 
metalc15 metalc ?    ? A  ASP 353 OD1 ? ? ? 1_555 J  CA  .   CA ? ? A ASP 353  A CA  2002 1_555 ? ? ? ? ? ? ? 2.322 ? 
metalc16 metalc ?    ? A  ASP 353 OD2 ? ? ? 1_555 J  CA  .   CA ? ? A ASP 353  A CA  2002 1_555 ? ? ? ? ? ? ? 2.456 ? 
metalc17 metalc ?    ? A  PHE 355 O   ? ? ? 1_555 J  CA  .   CA ? ? A PHE 355  A CA  2002 1_555 ? ? ? ? ? ? ? 2.498 ? 
metalc18 metalc ?    ? A  ASP 357 OD1 ? ? ? 1_555 J  CA  .   CA ? ? A ASP 357  A CA  2002 1_555 ? ? ? ? ? ? ? 2.397 ? 
metalc19 metalc ?    ? A  ASP 357 OD2 ? ? ? 1_555 J  CA  .   CA ? ? A ASP 357  A CA  2002 1_555 ? ? ? ? ? ? ? 2.431 ? 
metalc20 metalc ?    ? A  ASP 414 OD1 ? ? ? 1_555 K  CA  .   CA ? ? A ASP 414  A CA  2003 1_555 ? ? ? ? ? ? ? 2.631 ? 
metalc21 metalc ?    ? A  ASP 416 OD1 ? ? ? 1_555 K  CA  .   CA ? ? A ASP 416  A CA  2003 1_555 ? ? ? ? ? ? ? 2.558 ? 
metalc22 metalc ?    ? A  ASN 418 OD1 ? ? ? 1_555 K  CA  .   CA ? ? A ASN 418  A CA  2003 1_555 ? ? ? ? ? ? ? 2.202 ? 
metalc23 metalc ?    ? A  TYR 420 O   ? ? ? 1_555 K  CA  .   CA ? ? A TYR 420  A CA  2003 1_555 ? ? ? ? ? ? ? 2.375 ? 
metalc24 metalc ?    ? A  ASP 422 OD1 ? ? ? 1_555 K  CA  .   CA ? ? A ASP 422  A CA  2003 1_555 ? ? ? ? ? ? ? 2.395 ? 
metalc25 metalc ?    ? A  ASP 422 OD2 ? ? ? 1_555 K  CA  .   CA ? ? A ASP 422  A CA  2003 1_555 ? ? ? ? ? ? ? 2.364 ? 
covale4  covale one  ? A  ASN 459 ND2 ? ? ? 1_555 CA NAG .   C1 ? ? A ASN 459  A NAG 2021 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale5  covale one  ? A  ASN 525 ND2 ? ? ? 1_555 GA NAG .   C1 ? ? A ASN 525  A NAG 2025 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale6  covale one  ? A  ASN 586 ND2 ? ? ? 1_555 HA NAG .   C1 ? ? A ASN 586  A NAG 2026 1_555 ? ? ? ? ? ? ? 1.430 ? 
metalc26 metalc ?    ? B  SER 15  OG  ? ? ? 1_555 KA MN  .   MN ? ? B SER 125  B MN  2002 1_555 ? ? ? ? ? ? ? 2.166 ? 
metalc27 metalc ?    ? B  SER 17  O   ? ? ? 1_555 JA MN  .   MN ? ? B SER 127  B MN  2001 1_555 ? ? ? ? ? ? ? 2.252 ? 
metalc28 metalc ?    ? B  SER 17  OG  ? ? ? 1_555 KA MN  .   MN ? ? B SER 127  B MN  2002 1_555 ? ? ? ? ? ? ? 2.185 ? 
metalc29 metalc ?    ? B  ASP 20  OD1 ? ? ? 1_555 JA MN  .   MN ? ? B ASP 130  B MN  2001 1_555 ? ? ? ? ? ? ? 2.173 ? 
metalc30 metalc ?    ? B  ASP 20  OD2 ? ? ? 1_555 JA MN  .   MN ? ? B ASP 130  B MN  2001 1_555 ? ? ? ? ? ? ? 2.195 ? 
metalc31 metalc ?    ? B  ASP 21  OD1 ? ? ? 1_555 JA MN  .   MN ? ? B ASP 131  B MN  2001 1_555 ? ? ? ? ? ? ? 2.278 ? 
metalc32 metalc ?    ? B  ASP 21  OD2 ? ? ? 1_555 JA MN  .   MN ? ? B ASP 131  B MN  2001 1_555 ? ? ? ? ? ? ? 2.158 ? 
metalc33 metalc ?    ? B  GLU 52  OE2 ? ? ? 1_555 LA MN  .   MN ? ? B GLU 162  B MN  2003 1_555 ? ? ? ? ? ? ? 2.148 ? 
metalc34 metalc ?    ? B  ASN 108 OD1 ? ? ? 1_555 LA MN  .   MN ? ? B ASN 218  B MN  2003 1_555 ? ? ? ? ? ? ? 2.165 ? 
metalc35 metalc ?    ? B  ASP 110 O   ? ? ? 1_555 LA MN  .   MN ? ? B ASP 220  B MN  2003 1_555 ? ? ? ? ? ? ? 2.143 ? 
metalc36 metalc ?    ? B  ASP 110 OD1 ? ? ? 1_555 LA MN  .   MN ? ? B ASP 220  B MN  2003 1_555 ? ? ? ? ? ? ? 2.186 ? 
metalc37 metalc ?    ? B  PRO 112 O   ? ? ? 1_555 LA MN  .   MN ? ? B PRO 222  B MN  2003 1_555 ? ? ? ? ? ? ? 2.370 ? 
metalc38 metalc ?    ? B  GLU 113 OE1 ? ? ? 1_555 LA MN  .   MN ? ? B GLU 223  B MN  2003 1_555 ? ? ? ? ? ? ? 2.176 ? 
metalc39 metalc ?    ? B  GLU 113 OE2 ? ? ? 1_555 KA MN  .   MN ? ? B GLU 223  B MN  2002 1_555 ? ? ? ? ? ? ? 2.137 ? 
covale7  covale one  ? B  ASN 133 ND2 ? ? ? 1_555 MA NAG .   C1 ? ? B ASN 243  B NAG 2004 1_555 ? ? ? ? ? ? ? 1.443 ? 
metalc40 metalc ?    ? B  ASP 144 OD2 ? ? ? 1_555 JA MN  .   MN ? ? B ASP 254  B MN  2001 1_555 ? ? ? ? ? ? ? 2.214 ? 
covale8  covale one  ? C  ASN 55  ND2 ? ? ? 1_555 NA NAG .   C1 ? ? C ASN 53   C NAG 401  1_555 ? ? ? ? ? ? ? 1.433 ? 
covale9  covale one  ? D  ASN 55  ND2 ? ? ? 1_555 RA NAG .   C1 ? ? D ASN 53   D NAG 401  1_555 ? ? ? ? ? ? ? 1.430 ? 
metalc41 metalc ?    ? D  ASP 219 OD1 ? ? ? 1_555 KA MN  .   MN ? ? D ASP 217  B MN  2002 1_555 ? ? ? ? ? ? ? 2.107 ? 
covale10 covale one  ? E  ASN 44  ND2 ? ? ? 1_555 ZA NAG .   C1 ? ? E ASN 44   E NAG 2005 1_555 ? ? ? ? ? ? ? 1.442 ? 
metalc42 metalc ?    ? E  ASN 232 OD1 ? ? ? 1_555 YA CA  .   CA ? ? E ASN 232  E CA  2004 1_555 ? ? ? ? ? ? ? 2.309 ? 
metalc43 metalc ?    ? E  ASP 234 OD1 ? ? ? 1_555 YA CA  .   CA ? ? E ASP 234  E CA  2004 1_555 ? ? ? ? ? ? ? 2.362 ? 
metalc44 metalc ?    ? E  ILE 236 O   ? ? ? 1_555 YA CA  .   CA ? ? E ILE 236  E CA  2004 1_555 ? ? ? ? ? ? ? 2.387 ? 
metalc45 metalc ?    ? E  ASP 238 OD1 ? ? ? 1_555 YA CA  .   CA ? ? E ASP 238  E CA  2004 1_555 ? ? ? ? ? ? ? 2.329 ? 
metalc46 metalc ?    ? E  ASP 238 OD2 ? ? ? 1_555 YA CA  .   CA ? ? E ASP 238  E CA  2004 1_555 ? ? ? ? ? ? ? 2.446 ? 
covale11 covale one  ? E  ASN 260 ND2 ? ? ? 1_555 CB NAG .   C1 ? ? E ASN 260  E NAG 2008 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale12 covale one  ? E  ASN 266 ND2 ? ? ? 1_555 IB NAG .   C1 ? ? E ASN 266  E NAG 2014 1_555 ? ? ? ? ? ? ? 1.429 ? 
metalc47 metalc ?    ? E  ASP 284 OD1 ? ? ? 1_555 VA CA  .   CA ? ? E ASP 284  E CA  2001 1_555 ? ? ? ? ? ? ? 2.367 ? 
metalc48 metalc ?    ? E  ASN 286 OD1 ? ? ? 1_555 VA CA  .   CA ? ? E ASN 286  E CA  2001 1_555 ? ? ? ? ? ? ? 2.351 ? 
metalc49 metalc ?    ? E  ASP 288 OD1 ? ? ? 1_555 VA CA  .   CA ? ? E ASP 288  E CA  2001 1_555 ? ? ? ? ? ? ? 2.384 ? 
metalc50 metalc ?    ? E  ASP 288 OD2 ? ? ? 1_555 VA CA  .   CA ? ? E ASP 288  E CA  2001 1_555 ? ? ? ? ? ? ? 3.171 ? 
metalc51 metalc ?    ? E  TYR 290 O   ? ? ? 1_555 VA CA  .   CA ? ? E TYR 290  E CA  2001 1_555 ? ? ? ? ? ? ? 2.307 ? 
metalc52 metalc ?    ? E  ASP 292 OD1 ? ? ? 1_555 VA CA  .   CA ? ? E ASP 292  E CA  2001 1_555 ? ? ? ? ? ? ? 2.331 ? 
metalc53 metalc ?    ? E  ASP 292 OD2 ? ? ? 1_555 VA CA  .   CA ? ? E ASP 292  E CA  2001 1_555 ? ? ? ? ? ? ? 2.366 ? 
metalc54 metalc ?    ? E  ASP 349 OD1 ? ? ? 1_555 WA CA  .   CA ? ? E ASP 349  E CA  2002 1_555 ? ? ? ? ? ? ? 2.429 ? 
metalc55 metalc ?    ? E  ASP 351 OD1 ? ? ? 1_555 WA CA  .   CA ? ? E ASP 351  E CA  2002 1_555 ? ? ? ? ? ? ? 2.435 ? 
metalc56 metalc ?    ? E  ASP 353 OD1 ? ? ? 1_555 WA CA  .   CA ? ? E ASP 353  E CA  2002 1_555 ? ? ? ? ? ? ? 2.351 ? 
metalc57 metalc ?    ? E  ASP 353 OD2 ? ? ? 1_555 WA CA  .   CA ? ? E ASP 353  E CA  2002 1_555 ? ? ? ? ? ? ? 2.487 ? 
metalc58 metalc ?    ? E  PHE 355 O   ? ? ? 1_555 WA CA  .   CA ? ? E PHE 355  E CA  2002 1_555 ? ? ? ? ? ? ? 2.495 ? 
metalc59 metalc ?    ? E  ASP 357 OD1 ? ? ? 1_555 WA CA  .   CA ? ? E ASP 357  E CA  2002 1_555 ? ? ? ? ? ? ? 2.388 ? 
metalc60 metalc ?    ? E  ASP 357 OD2 ? ? ? 1_555 WA CA  .   CA ? ? E ASP 357  E CA  2002 1_555 ? ? ? ? ? ? ? 2.382 ? 
metalc61 metalc ?    ? E  ASP 414 OD1 ? ? ? 1_555 XA CA  .   CA ? ? E ASP 414  E CA  2003 1_555 ? ? ? ? ? ? ? 2.511 ? 
metalc62 metalc ?    ? E  ASP 416 OD1 ? ? ? 1_555 XA CA  .   CA ? ? E ASP 416  E CA  2003 1_555 ? ? ? ? ? ? ? 2.322 ? 
metalc63 metalc ?    ? E  ASN 418 OD1 ? ? ? 1_555 XA CA  .   CA ? ? E ASN 418  E CA  2003 1_555 ? ? ? ? ? ? ? 2.380 ? 
metalc64 metalc ?    ? E  TYR 420 O   ? ? ? 1_555 XA CA  .   CA ? ? E TYR 420  E CA  2003 1_555 ? ? ? ? ? ? ? 2.327 ? 
metalc65 metalc ?    ? E  ASP 422 OD1 ? ? ? 1_555 XA CA  .   CA ? ? E ASP 422  E CA  2003 1_555 ? ? ? ? ? ? ? 2.317 ? 
metalc66 metalc ?    ? E  ASP 422 OD2 ? ? ? 1_555 XA CA  .   CA ? ? E ASP 422  E CA  2003 1_555 ? ? ? ? ? ? ? 2.451 ? 
covale13 covale one  ? E  ASN 459 ND2 ? ? ? 1_555 PB NAG .   C1 ? ? E ASN 459  E NAG 2021 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale14 covale one  ? E  ASN 525 ND2 ? ? ? 1_555 TB NAG .   C1 ? ? E ASN 525  E NAG 2025 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale15 covale one  ? E  ASN 586 ND2 ? ? ? 1_555 UB NAG .   C1 ? ? E ASN 586  E NAG 2026 1_555 ? ? ? ? ? ? ? 1.428 ? 
metalc67 metalc ?    ? F  SER 15  OG  ? ? ? 1_555 XB MN  .   MN ? ? F SER 125  F MN  2002 1_555 ? ? ? ? ? ? ? 2.182 ? 
metalc68 metalc ?    ? F  SER 17  O   ? ? ? 1_555 WB MN  .   MN ? ? F SER 127  F MN  2001 1_555 ? ? ? ? ? ? ? 2.171 ? 
metalc69 metalc ?    ? F  SER 17  OG  ? ? ? 1_555 XB MN  .   MN ? ? F SER 127  F MN  2002 1_555 ? ? ? ? ? ? ? 2.162 ? 
metalc70 metalc ?    ? F  ASP 20  OD1 ? ? ? 1_555 WB MN  .   MN ? ? F ASP 130  F MN  2001 1_555 ? ? ? ? ? ? ? 2.153 ? 
metalc71 metalc ?    ? F  ASP 20  OD2 ? ? ? 1_555 WB MN  .   MN ? ? F ASP 130  F MN  2001 1_555 ? ? ? ? ? ? ? 2.180 ? 
metalc72 metalc ?    ? F  ASP 21  OD2 ? ? ? 1_555 WB MN  .   MN ? ? F ASP 131  F MN  2001 1_555 ? ? ? ? ? ? ? 2.189 ? 
metalc73 metalc ?    ? F  GLU 52  OE2 ? ? ? 1_555 YB MN  .   MN ? ? F GLU 162  F MN  2003 1_555 ? ? ? ? ? ? ? 2.167 ? 
metalc74 metalc ?    ? F  ASN 108 OD1 ? ? ? 1_555 YB MN  .   MN ? ? F ASN 218  F MN  2003 1_555 ? ? ? ? ? ? ? 2.177 ? 
metalc75 metalc ?    ? F  ASP 110 O   ? ? ? 1_555 YB MN  .   MN ? ? F ASP 220  F MN  2003 1_555 ? ? ? ? ? ? ? 2.169 ? 
metalc76 metalc ?    ? F  ASP 110 OD1 ? ? ? 1_555 YB MN  .   MN ? ? F ASP 220  F MN  2003 1_555 ? ? ? ? ? ? ? 2.151 ? 
metalc77 metalc ?    ? F  PRO 112 O   ? ? ? 1_555 YB MN  .   MN ? ? F PRO 222  F MN  2003 1_555 ? ? ? ? ? ? ? 2.318 ? 
metalc78 metalc ?    ? F  GLU 113 OE1 ? ? ? 1_555 YB MN  .   MN ? ? F GLU 223  F MN  2003 1_555 ? ? ? ? ? ? ? 2.184 ? 
metalc79 metalc ?    ? F  GLU 113 OE2 ? ? ? 1_555 XB MN  .   MN ? ? F GLU 223  F MN  2002 1_555 ? ? ? ? ? ? ? 2.139 ? 
covale16 covale one  ? F  ASN 133 ND2 ? ? ? 1_555 ZB NAG .   C1 ? ? F ASN 243  F NAG 2004 1_555 ? ? ? ? ? ? ? 1.442 ? 
metalc80 metalc ?    ? F  ASP 144 OD2 ? ? ? 1_555 WB MN  .   MN ? ? F ASP 254  F MN  2001 1_555 ? ? ? ? ? ? ? 2.165 ? 
covale17 covale one  ? G  ASN 55  ND2 ? ? ? 1_555 AC NAG .   C1 ? ? G ASN 53   G NAG 401  1_555 ? ? ? ? ? ? ? 1.440 ? 
covale18 covale one  ? H  ASN 55  ND2 ? ? ? 1_555 EC NAG .   C1 ? ? H ASN 53   H NAG 401  1_555 ? ? ? ? ? ? ? 1.434 ? 
metalc81 metalc ?    ? H  ASP 219 OD1 ? ? ? 1_555 XB MN  .   MN ? ? H ASP 217  F MN  2002 1_555 ? ? ? ? ? ? ? 2.171 ? 
covale19 covale both ? M  NAG .   O4  ? ? ? 1_555 N  NAG .   C1 ? ? A NAG 2005 A NAG 2006 1_555 ? ? ? ? ? ? ? 1.435 ? 
covale20 covale both ? N  NAG .   O4  ? ? ? 1_555 O  BMA .   C1 ? ? A NAG 2006 A BMA 2007 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale21 covale both ? P  NAG .   O4  ? ? ? 1_555 Q  NAG .   C1 ? ? A NAG 2008 A NAG 2009 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale22 covale both ? Q  NAG .   O4  ? ? ? 1_555 R  BMA .   C1 ? ? A NAG 2009 A BMA 2010 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale23 covale one  ? R  BMA .   O3  ? ? ? 1_555 U  MAN .   C1 ? ? A BMA 2010 A MAN 2013 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale24 covale one  ? R  BMA .   O6  ? ? ? 1_555 S  MAN .   C1 ? ? A BMA 2010 A MAN 2011 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale25 covale one  ? S  MAN .   O6  ? ? ? 1_555 T  MAN .   C1 ? ? A MAN 2011 A MAN 2012 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale26 covale both ? V  NAG .   O4  ? ? ? 1_555 W  NAG .   C1 ? ? A NAG 2014 A NAG 2015 1_555 ? ? ? ? ? ? ? 1.433 ? 
covale27 covale both ? W  NAG .   O4  ? ? ? 1_555 X  BMA .   C1 ? ? A NAG 2015 A BMA 2016 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale28 covale one  ? X  BMA .   O3  ? ? ? 1_555 Y  MAN .   C1 ? ? A BMA 2016 A MAN 2017 1_555 ? ? ? ? ? ? ? 1.433 ? 
covale29 covale one  ? X  BMA .   O6  ? ? ? 1_555 Z  MAN .   C1 ? ? A BMA 2016 A MAN 2018 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale30 covale one  ? Z  MAN .   O3  ? ? ? 1_555 BA MAN .   C1 ? ? A MAN 2018 A MAN 2020 1_555 ? ? ? ? ? ? ? 1.437 ? 
covale31 covale one  ? Z  MAN .   O6  ? ? ? 1_555 AA MAN .   C1 ? ? A MAN 2018 A MAN 2019 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale32 covale both ? CA NAG .   O4  ? ? ? 1_555 DA NAG .   C1 ? ? A NAG 2021 A NAG 2022 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale33 covale both ? DA NAG .   O4  ? ? ? 1_555 EA BMA .   C1 ? ? A NAG 2022 A BMA 2023 1_555 ? ? ? ? ? ? ? 1.433 ? 
covale34 covale one  ? EA BMA .   O6  ? ? ? 1_555 FA MAN .   C1 ? ? A BMA 2023 A MAN 2024 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale35 covale both ? HA NAG .   O4  ? ? ? 1_555 IA NAG .   C1 ? ? A NAG 2026 A NAG 2027 1_555 ? ? ? ? ? ? ? 1.437 ? 
metalc82 metalc ?    ? JA MN  .   MN  ? ? ? 1_555 KC HOH .   O  ? ? B MN  2001 B HOH 2103 1_555 ? ? ? ? ? ? ? 2.238 ? 
metalc83 metalc ?    ? KA MN  .   MN  ? ? ? 1_555 KC HOH .   O  ? ? B MN  2002 B HOH 2102 1_555 ? ? ? ? ? ? ? 2.167 ? 
metalc84 metalc ?    ? KA MN  .   MN  ? ? ? 1_555 KC HOH .   O  ? ? B MN  2002 B HOH 2101 1_555 ? ? ? ? ? ? ? 2.196 ? 
covale36 covale both ? NA NAG .   O4  ? ? ? 1_555 OA NAG .   C1 ? ? C NAG 401  C NAG 402  1_555 ? ? ? ? ? ? ? 1.438 ? 
covale37 covale both ? OA NAG .   O4  ? ? ? 1_555 PA BMA .   C1 ? ? C NAG 402  C BMA 403  1_555 ? ? ? ? ? ? ? 1.442 ? 
covale38 covale one  ? PA BMA .   O3  ? ? ? 1_555 QA MAN .   C1 ? ? C BMA 403  C MAN 404  1_555 ? ? ? ? ? ? ? 1.443 ? 
covale39 covale both ? RA NAG .   O4  ? ? ? 1_555 SA NAG .   C1 ? ? D NAG 401  D NAG 402  1_555 ? ? ? ? ? ? ? 1.440 ? 
covale40 covale both ? SA NAG .   O4  ? ? ? 1_555 TA BMA .   C1 ? ? D NAG 402  D BMA 403  1_555 ? ? ? ? ? ? ? 1.441 ? 
covale41 covale one  ? TA BMA .   O3  ? ? ? 1_555 UA MAN .   C1 ? ? D BMA 403  D MAN 404  1_555 ? ? ? ? ? ? ? 1.431 ? 
covale42 covale both ? ZA NAG .   O4  ? ? ? 1_555 AB NAG .   C1 ? ? E NAG 2005 E NAG 2006 1_555 ? ? ? ? ? ? ? 1.435 ? 
covale43 covale both ? AB NAG .   O4  ? ? ? 1_555 BB BMA .   C1 ? ? E NAG 2006 E BMA 2007 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale44 covale both ? CB NAG .   O4  ? ? ? 1_555 DB NAG .   C1 ? ? E NAG 2008 E NAG 2009 1_555 ? ? ? ? ? ? ? 1.435 ? 
covale45 covale both ? DB NAG .   O4  ? ? ? 1_555 EB BMA .   C1 ? ? E NAG 2009 E BMA 2010 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale46 covale one  ? EB BMA .   O3  ? ? ? 1_555 HB MAN .   C1 ? ? E BMA 2010 E MAN 2013 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale47 covale one  ? EB BMA .   O6  ? ? ? 1_555 FB MAN .   C1 ? ? E BMA 2010 E MAN 2011 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale48 covale one  ? FB MAN .   O6  ? ? ? 1_555 GB MAN .   C1 ? ? E MAN 2011 E MAN 2012 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale49 covale both ? IB NAG .   O4  ? ? ? 1_555 JB NAG .   C1 ? ? E NAG 2014 E NAG 2015 1_555 ? ? ? ? ? ? ? 1.430 ? 
covale50 covale both ? JB NAG .   O4  ? ? ? 1_555 KB BMA .   C1 ? ? E NAG 2015 E BMA 2016 1_555 ? ? ? ? ? ? ? 1.433 ? 
covale51 covale one  ? KB BMA .   O3  ? ? ? 1_555 LB MAN .   C1 ? ? E BMA 2016 E MAN 2017 1_555 ? ? ? ? ? ? ? 1.435 ? 
covale52 covale one  ? KB BMA .   O6  ? ? ? 1_555 MB MAN .   C1 ? ? E BMA 2016 E MAN 2018 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale53 covale one  ? MB MAN .   O3  ? ? ? 1_555 OB MAN .   C1 ? ? E MAN 2018 E MAN 2020 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale54 covale one  ? MB MAN .   O6  ? ? ? 1_555 NB MAN .   C1 ? ? E MAN 2018 E MAN 2019 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale55 covale both ? PB NAG .   O4  ? ? ? 1_555 QB NAG .   C1 ? ? E NAG 2021 E NAG 2022 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale56 covale both ? QB NAG .   O4  ? ? ? 1_555 RB BMA .   C1 ? ? E NAG 2022 E BMA 2023 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale57 covale one  ? RB BMA .   O6  ? ? ? 1_555 SB MAN .   C1 ? ? E BMA 2023 E MAN 2024 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale58 covale both ? UB NAG .   O4  ? ? ? 1_555 VB NAG .   C1 ? ? E NAG 2026 E NAG 2027 1_555 ? ? ? ? ? ? ? 1.439 ? 
metalc85 metalc ?    ? XB MN  .   MN  ? ? ? 1_555 LC HOH .   O  ? ? F MN  2002 F HOH 2101 1_555 ? ? ? ? ? ? ? 2.195 ? 
metalc86 metalc ?    ? XB MN  .   MN  ? ? ? 1_555 LC HOH .   O  ? ? F MN  2002 F HOH 2102 1_555 ? ? ? ? ? ? ? 2.196 ? 
covale59 covale both ? AC NAG .   O4  ? ? ? 1_555 BC NAG .   C1 ? ? G NAG 401  G NAG 402  1_555 ? ? ? ? ? ? ? 1.447 ? 
covale60 covale both ? BC NAG .   O4  ? ? ? 1_555 CC BMA .   C1 ? ? G NAG 402  G BMA 403  1_555 ? ? ? ? ? ? ? 1.440 ? 
covale61 covale one  ? CC BMA .   O3  ? ? ? 1_555 DC MAN .   C1 ? ? G BMA 403  G MAN 404  1_555 ? ? ? ? ? ? ? 1.458 ? 
covale62 covale both ? EC NAG .   O4  ? ? ? 1_555 FC NAG .   C1 ? ? H NAG 401  H NAG 402  1_555 ? ? ? ? ? ? ? 1.447 ? 
covale63 covale both ? FC NAG .   O4  ? ? ? 1_555 GC BMA .   C1 ? ? H NAG 402  H BMA 403  1_555 ? ? ? ? ? ? ? 1.433 ? 
covale64 covale one  ? GC BMA .   O3  ? ? ? 1_555 HC MAN .   C1 ? ? H BMA 403  H MAN 404  1_555 ? ? ? ? ? ? ? 1.438 ? 
covale65 covale one  ? GC BMA .   O6  ? ? ? 1_555 IC MAN .   C1 ? ? H BMA 403  H MAN 405  1_555 ? ? ? ? ? ? ? 1.449 ? 
covale66 covale one  ? HC MAN .   O2  ? ? ? 1_555 JC MAN .   C1 ? ? H MAN 404  H MAN 406  1_555 ? ? ? ? ? ? ? 1.441 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
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  TYR 451 A . ? TYR 451 A PRO 452 A ? PRO 452 A 1 0.41  
2  SER 56  B . ? SER 166 B PRO 57  B ? PRO 167 B 1 4.33  
3  ILE 73  B . ? ILE 183 B PRO 74  B ? PRO 184 B 1 -4.44 
4  VAL 41  C . ? VAL 39  C PRO 42  C ? PRO 40  C 1 -7.65 
5  GLU 286 C . ? GLU 284 C PRO 287 C ? PRO 285 C 1 -3.41 
6  GLU 286 D . ? GLU 284 D PRO 287 D ? PRO 285 D 1 -1.58 
7  TYR 451 E . ? TYR 451 E PRO 452 E ? PRO 452 E 1 -0.12 
8  SER 56  F . ? SER 166 F PRO 57  F ? PRO 167 F 1 4.95  
9  ILE 73  F . ? ILE 183 F PRO 74  F ? PRO 184 F 1 -4.48 
10 VAL 41  G . ? VAL 39  G PRO 42  G ? PRO 40  G 1 -4.23 
11 GLU 286 G . ? GLU 284 G PRO 287 G ? PRO 285 G 1 -3.31 
12 GLU 286 H . ? GLU 284 H PRO 287 H ? PRO 285 H 1 -1.74 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 2 ? 
AB1 ? 4 ? 
AB2 ? 2 ? 
AB3 ? 5 ? 
AB4 ? 4 ? 
AB5 ? 6 ? 
AB6 ? 7 ? 
AB7 ? 4 ? 
AB8 ? 2 ? 
AB9 ? 2 ? 
AC1 ? 7 ? 
AC2 ? 2 ? 
AC3 ? 4 ? 
AC4 ? 2 ? 
AC5 ? 2 ? 
AC6 ? 4 ? 
AC7 ? 4 ? 
AC8 ? 2 ? 
AC9 ? 2 ? 
AD1 ? 4 ? 
AD2 ? 4 ? 
AD3 ? 4 ? 
AD4 ? 4 ? 
AD5 ? 2 ? 
AD6 ? 4 ? 
AD7 ? 2 ? 
AD8 ? 5 ? 
AD9 ? 4 ? 
AE1 ? 6 ? 
AE2 ? 7 ? 
AE3 ? 4 ? 
AE4 ? 2 ? 
AE5 ? 2 ? 
AE6 ? 7 ? 
AE7 ? 2 ? 
AE8 ? 4 ? 
AE9 ? 2 ? 
AF1 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? parallel      
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? parallel      
AB5 5 6 ? parallel      
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB6 5 6 ? anti-parallel 
AB6 6 7 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC1 4 5 ? anti-parallel 
AC1 5 6 ? anti-parallel 
AC1 6 7 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC6 3 4 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC7 2 3 ? anti-parallel 
AC7 3 4 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC9 1 2 ? anti-parallel 
AD1 1 2 ? anti-parallel 
AD1 2 3 ? anti-parallel 
AD1 3 4 ? anti-parallel 
AD2 1 2 ? anti-parallel 
AD2 2 3 ? anti-parallel 
AD2 3 4 ? anti-parallel 
AD3 1 2 ? anti-parallel 
AD3 2 3 ? anti-parallel 
AD3 3 4 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD4 2 3 ? anti-parallel 
AD4 3 4 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD7 1 2 ? anti-parallel 
AD8 1 2 ? anti-parallel 
AD8 2 3 ? anti-parallel 
AD8 3 4 ? anti-parallel 
AD8 4 5 ? parallel      
AD9 1 2 ? anti-parallel 
AD9 2 3 ? anti-parallel 
AD9 3 4 ? anti-parallel 
AE1 1 2 ? anti-parallel 
AE1 2 3 ? parallel      
AE1 3 4 ? parallel      
AE1 4 5 ? parallel      
AE1 5 6 ? parallel      
AE2 1 2 ? anti-parallel 
AE2 2 3 ? anti-parallel 
AE2 3 4 ? anti-parallel 
AE2 4 5 ? anti-parallel 
AE2 5 6 ? anti-parallel 
AE2 6 7 ? anti-parallel 
AE3 1 2 ? anti-parallel 
AE3 2 3 ? anti-parallel 
AE3 3 4 ? anti-parallel 
AE4 1 2 ? anti-parallel 
AE5 1 2 ? anti-parallel 
AE6 1 2 ? anti-parallel 
AE6 2 3 ? anti-parallel 
AE6 3 4 ? anti-parallel 
AE6 4 5 ? anti-parallel 
AE6 5 6 ? anti-parallel 
AE6 6 7 ? anti-parallel 
AE7 1 2 ? anti-parallel 
AE8 1 2 ? anti-parallel 
AE8 2 3 ? anti-parallel 
AE8 3 4 ? anti-parallel 
AE9 1 2 ? anti-parallel 
AF1 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 9   ? SER A 12  ? ALA A 9   SER A 12  
AA1 2 ARG A 432 ? TYR A 436 ? ARG A 432 TYR A 436 
AA1 3 ASP A 422 ? ALA A 427 ? ASP A 422 ALA A 427 
AA1 4 PHE A 405 ? THR A 413 ? PHE A 405 THR A 413 
AA2 1 VAL A 23  ? PHE A 26  ? VAL A 23  PHE A 26  
AA2 2 PHE A 35  ? ALA A 40  ? PHE A 35  ALA A 40  
AA2 3 GLN A 55  ? ASP A 60  ? GLN A 55  ASP A 60  
AA2 4 CYS A 67  ? PRO A 69  ? CYS A 67  PRO A 69  
AA3 1 ASP A 79  ? ALA A 81  ? ASP A 79  ALA A 81  
AA3 2 ASP A 84  ? PRO A 85  ? ASP A 84  PRO A 85  
AA4 1 GLU A 87  ? PHE A 88  ? GLU A 87  PHE A 88  
AA4 2 HIS A 113 ? TRP A 114 ? HIS A 113 TRP A 114 
AA5 1 VAL A 98  ? LYS A 101 ? VAL A 98  LYS A 101 
AA5 2 LYS A 104 ? ALA A 109 ? LYS A 104 ALA A 109 
AA5 3 THR A 127 ? GLN A 131 ? THR A 127 GLN A 131 
AA5 4 THR A 136 ? TYR A 139 ? THR A 136 TYR A 139 
AA6 1 ILE A 161 ? PHE A 163 ? ILE A 161 PHE A 163 
AA6 2 ARG A 168 ? GLY A 173 ? ARG A 168 GLY A 173 
AA6 3 GLN A 182 ? GLN A 187 ? GLN A 182 GLN A 187 
AA6 4 LEU A 208 ? ALA A 209 ? LEU A 208 ALA A 209 
AA7 1 VAL A 226 ? GLY A 229 ? VAL A 226 GLY A 229 
AA7 2 ASP A 238 ? VAL A 243 ? ASP A 238 VAL A 243 
AA7 3 MET A 252 ? TYR A 256 ? MET A 252 TYR A 256 
AA7 4 SER A 263 ? THR A 268 ? SER A 263 THR A 268 
AA8 1 VAL A 280 ? THR A 283 ? VAL A 280 THR A 283 
AA8 2 ASP A 292 ? ALA A 297 ? ASP A 292 ALA A 297 
AA8 3 GLN A 314 ? GLN A 320 ? GLN A 314 GLN A 320 
AA8 4 PHE A 326 ? ASN A 332 ? PHE A 326 ASN A 332 
AA9 1 MET A 301 ? ARG A 303 ? MET A 301 ARG A 303 
AA9 2 LEU A 309 ? GLU A 311 ? LEU A 309 GLU A 311 
AB1 1 ILE A 344 ? GLY A 348 ? ILE A 344 GLY A 348 
AB1 2 ASP A 357 ? ALA A 362 ? ASP A 357 ALA A 362 
AB1 3 ILE A 372 ? PHE A 376 ? ILE A 372 PHE A 376 
AB1 4 GLN A 389 ? GLU A 392 ? GLN A 389 GLU A 392 
AB2 1 GLY A 378 ? ARG A 379 ? GLY A 378 ARG A 379 
AB2 2 GLY A 382 ? LEU A 383 ? GLY A 382 LEU A 383 
AB3 1 ALA A 512 ? PHE A 514 ? ALA A 512 PHE A 514 
AB3 2 GLN A 535 ? LEU A 543 ? GLN A 535 LEU A 543 
AB3 3 CYS A 473 ? GLY A 484 ? CYS A 473 GLY A 484 
AB3 4 VAL A 441 ? TYR A 451 ? VAL A 441 TYR A 451 
AB3 5 ILE A 578 ? LEU A 579 ? ILE A 578 LEU A 579 
AB4 1 SER A 521 ? SER A 529 ? SER A 521 SER A 529 
AB4 2 LYS A 491 ? LEU A 500 ? LYS A 491 LEU A 500 
AB4 3 ILE A 556 ? LEU A 564 ? ILE A 556 LEU A 564 
AB4 4 ILE A 587 ? ALA A 591 ? ILE A 587 ALA A 591 
AB5 1 PHE B 83  ? THR B 90  ? PHE B 193 THR B 200 
AB5 2 PHE B 43  ? PHE B 50  ? PHE B 153 PHE B 160 
AB5 3 VAL B 6   ? ASP B 13  ? VAL B 116 ASP B 123 
AB5 4 LEU B 136 ? VAL B 142 ? LEU B 246 VAL B 252 
AB5 5 VAL B 197 ? VAL B 203 ? VAL B 307 VAL B 313 
AB5 6 THR B 222 ? LEU B 225 ? THR B 332 LEU B 335 
AB6 1 SER C 170 ? ASP C 172 ? SER C 168 ASP C 170 
AB6 2 LEU C 123 ? ARG C 129 ? LEU C 121 ARG C 127 
AB6 3 PHE C 230 ? ALA C 235 ? PHE C 228 ALA C 233 
AB6 4 LYS C 79  ? LEU C 85  ? LYS C 77  LEU C 83  
AB6 5 LYS D 348 ? VAL D 357 ? LYS D 346 VAL D 355 
AB6 6 LEU D 334 ? TYR D 341 ? LEU D 332 TYR D 339 
AB6 7 ILE D 284 ? GLU D 286 ? ILE D 282 GLU D 284 
AB7 1 ILE C 104 ? GLN C 109 ? ILE C 102 GLN C 107 
AB7 2 ILE C 187 ? ALA C 194 ? ILE C 185 ALA C 192 
AB7 3 HIS C 140 ? TYR C 147 ? HIS C 138 TYR C 145 
AB7 4 SER C 151 ? LEU C 159 ? SER C 149 LEU C 157 
AB8 1 CYS C 267 ? ARG C 269 ? CYS C 265 ARG C 267 
AB8 2 PHE C 294 ? LEU C 296 ? PHE C 292 LEU C 294 
AB9 1 TYR C 272 ? ILE C 273 ? TYR C 270 ILE C 271 
AB9 2 TYR C 290 ? HIS C 291 ? TYR C 288 HIS C 289 
AC1 1 ILE C 284 ? GLU C 286 ? ILE C 282 GLU C 284 
AC1 2 LEU C 334 ? VAL C 343 ? LEU C 332 VAL C 341 
AC1 3 LYS C 346 ? VAL C 357 ? LYS C 344 VAL C 355 
AC1 4 LYS D 79  ? LEU D 85  ? LYS D 77  LEU D 83  
AC1 5 PHE D 230 ? ALA D 235 ? PHE D 228 ALA D 233 
AC1 6 LEU D 123 ? ARG D 129 ? LEU D 121 ARG D 127 
AC1 7 PHE D 171 ? ASP D 172 ? PHE D 169 ASP D 170 
AC2 1 CYS C 328 ? PRO C 331 ? CYS C 326 PRO C 329 
AC2 2 CYS C 360 ? SER C 363 ? CYS C 358 SER C 361 
AC3 1 SER D 103 ? PHE D 108 ? SER D 101 PHE D 106 
AC3 2 GLU D 188 ? ALA D 194 ? GLU D 186 ALA D 192 
AC3 3 HIS D 140 ? TYR D 147 ? HIS D 138 TYR D 145 
AC3 4 SER D 151 ? LEU D 159 ? SER D 149 LEU D 157 
AC4 1 CYS D 267 ? ARG D 269 ? CYS D 265 ARG D 267 
AC4 2 PHE D 294 ? LEU D 296 ? PHE D 292 LEU D 294 
AC5 1 CYS D 328 ? PRO D 331 ? CYS D 326 PRO D 329 
AC5 2 CYS D 360 ? SER D 363 ? CYS D 358 SER D 361 
AC6 1 ALA E 9   ? SER E 12  ? ALA E 9   SER E 12  
AC6 2 ARG E 432 ? TYR E 436 ? ARG E 432 TYR E 436 
AC6 3 ASP E 422 ? ALA E 427 ? ASP E 422 ALA E 427 
AC6 4 SER E 408 ? THR E 413 ? SER E 408 THR E 413 
AC7 1 VAL E 23  ? PHE E 26  ? VAL E 23  PHE E 26  
AC7 2 PHE E 35  ? ALA E 40  ? PHE E 35  ALA E 40  
AC7 3 GLN E 55  ? ASP E 60  ? GLN E 55  ASP E 60  
AC7 4 CYS E 67  ? ILE E 70  ? CYS E 67  ILE E 70  
AC8 1 ASP E 79  ? ALA E 81  ? ASP E 79  ALA E 81  
AC8 2 ASP E 84  ? PRO E 85  ? ASP E 84  PRO E 85  
AC9 1 GLU E 87  ? PHE E 88  ? GLU E 87  PHE E 88  
AC9 2 HIS E 113 ? TRP E 114 ? HIS E 113 TRP E 114 
AD1 1 VAL E 98  ? LYS E 101 ? VAL E 98  LYS E 101 
AD1 2 LYS E 104 ? ALA E 109 ? LYS E 104 ALA E 109 
AD1 3 THR E 127 ? GLN E 131 ? THR E 127 GLN E 131 
AD1 4 THR E 136 ? TYR E 139 ? THR E 136 TYR E 139 
AD2 1 ILE E 161 ? PHE E 163 ? ILE E 161 PHE E 163 
AD2 2 ARG E 168 ? GLY E 173 ? ARG E 168 GLY E 173 
AD2 3 GLN E 182 ? GLN E 187 ? GLN E 182 GLN E 187 
AD2 4 LEU E 208 ? ALA E 209 ? LEU E 208 ALA E 209 
AD3 1 VAL E 226 ? GLY E 229 ? VAL E 226 GLY E 229 
AD3 2 ASP E 238 ? VAL E 243 ? ASP E 238 VAL E 243 
AD3 3 MET E 252 ? TYR E 256 ? MET E 252 TYR E 256 
AD3 4 SER E 263 ? THR E 268 ? SER E 263 THR E 268 
AD4 1 VAL E 280 ? THR E 283 ? VAL E 280 THR E 283 
AD4 2 ASP E 292 ? ALA E 297 ? ASP E 292 ALA E 297 
AD4 3 GLN E 314 ? GLN E 320 ? GLN E 314 GLN E 320 
AD4 4 PHE E 326 ? ASN E 332 ? PHE E 326 ASN E 332 
AD5 1 MET E 301 ? ARG E 303 ? MET E 301 ARG E 303 
AD5 2 LEU E 309 ? GLU E 311 ? LEU E 309 GLU E 311 
AD6 1 ILE E 344 ? GLY E 348 ? ILE E 344 GLY E 348 
AD6 2 ASP E 357 ? ALA E 362 ? ASP E 357 ALA E 362 
AD6 3 ILE E 372 ? PHE E 376 ? ILE E 372 PHE E 376 
AD6 4 GLN E 389 ? GLU E 392 ? GLN E 389 GLU E 392 
AD7 1 GLY E 378 ? ARG E 379 ? GLY E 378 ARG E 379 
AD7 2 GLY E 382 ? LEU E 383 ? GLY E 382 LEU E 383 
AD8 1 ALA E 512 ? PHE E 514 ? ALA E 512 PHE E 514 
AD8 2 GLN E 535 ? LEU E 543 ? GLN E 535 LEU E 543 
AD8 3 CYS E 473 ? GLY E 484 ? CYS E 473 GLY E 484 
AD8 4 VAL E 441 ? TYR E 451 ? VAL E 441 TYR E 451 
AD8 5 ILE E 578 ? LEU E 579 ? ILE E 578 LEU E 579 
AD9 1 SER E 521 ? SER E 529 ? SER E 521 SER E 529 
AD9 2 LYS E 491 ? LEU E 500 ? LYS E 491 LEU E 500 
AD9 3 ILE E 556 ? LEU E 564 ? ILE E 556 LEU E 564 
AD9 4 ILE E 587 ? ALA E 591 ? ILE E 587 ALA E 591 
AE1 1 PHE F 83  ? THR F 90  ? PHE F 193 THR F 200 
AE1 2 PHE F 43  ? PHE F 50  ? PHE F 153 PHE F 160 
AE1 3 VAL F 6   ? ASP F 13  ? VAL F 116 ASP F 123 
AE1 4 LEU F 136 ? VAL F 142 ? LEU F 246 VAL F 252 
AE1 5 VAL F 197 ? VAL F 203 ? VAL F 307 VAL F 313 
AE1 6 THR F 222 ? LEU F 225 ? THR F 332 LEU F 335 
AE2 1 SER G 170 ? ASP G 172 ? SER G 168 ASP G 170 
AE2 2 LEU G 123 ? ARG G 129 ? LEU G 121 ARG G 127 
AE2 3 PHE G 230 ? ALA G 235 ? PHE G 228 ALA G 233 
AE2 4 LYS G 79  ? LEU G 85  ? LYS G 77  LEU G 83  
AE2 5 LYS H 348 ? VAL H 357 ? LYS H 346 VAL H 355 
AE2 6 LEU H 334 ? TYR H 341 ? LEU H 332 TYR H 339 
AE2 7 ILE H 284 ? GLU H 286 ? ILE H 282 GLU H 284 
AE3 1 ILE G 104 ? GLN G 109 ? ILE G 102 GLN G 107 
AE3 2 ILE G 187 ? ALA G 194 ? ILE G 185 ALA G 192 
AE3 3 HIS G 140 ? TYR G 147 ? HIS G 138 TYR G 145 
AE3 4 SER G 151 ? LEU G 159 ? SER G 149 LEU G 157 
AE4 1 CYS G 267 ? ARG G 269 ? CYS G 265 ARG G 267 
AE4 2 PHE G 294 ? LEU G 296 ? PHE G 292 LEU G 294 
AE5 1 TYR G 272 ? ILE G 273 ? TYR G 270 ILE G 271 
AE5 2 TYR G 290 ? HIS G 291 ? TYR G 288 HIS G 289 
AE6 1 ILE G 284 ? GLU G 286 ? ILE G 282 GLU G 284 
AE6 2 LEU G 334 ? VAL G 343 ? LEU G 332 VAL G 341 
AE6 3 LYS G 346 ? VAL G 357 ? LYS G 344 VAL G 355 
AE6 4 LYS H 79  ? LEU H 85  ? LYS H 77  LEU H 83  
AE6 5 PHE H 230 ? ALA H 235 ? PHE H 228 ALA H 233 
AE6 6 LEU H 123 ? ARG H 129 ? LEU H 121 ARG H 127 
AE6 7 SER H 170 ? ASP H 172 ? SER H 168 ASP H 170 
AE7 1 CYS G 328 ? PRO G 331 ? CYS G 326 PRO G 329 
AE7 2 CYS G 360 ? SER G 363 ? CYS G 358 SER G 361 
AE8 1 SER H 103 ? PHE H 108 ? SER H 101 PHE H 106 
AE8 2 GLU H 188 ? ALA H 194 ? GLU H 186 ALA H 192 
AE8 3 HIS H 140 ? TYR H 147 ? HIS H 138 TYR H 145 
AE8 4 SER H 151 ? LEU H 159 ? SER H 149 LEU H 157 
AE9 1 CYS H 267 ? ARG H 269 ? CYS H 265 ARG H 267 
AE9 2 PHE H 294 ? LEU H 296 ? PHE H 292 LEU H 294 
AF1 1 CYS H 328 ? PRO H 331 ? CYS H 326 PRO H 329 
AF1 2 CYS H 360 ? SER H 363 ? CYS H 358 SER H 361 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TYR A 11  ? N TYR A 11  O ALA A 433 ? O ALA A 433 
AA1 2 3 O ARG A 432 ? O ARG A 432 N ALA A 427 ? N ALA A 427 
AA1 3 4 O GLY A 426 ? O GLY A 426 N SER A 408 ? N SER A 408 
AA2 1 2 N ASP A 24  ? N ASP A 24  O LEU A 37  ? O LEU A 37  
AA2 2 3 N LEU A 36  ? N LEU A 36  O CYS A 59  ? O CYS A 59  
AA2 3 4 N LYS A 58  ? N LYS A 58  O GLN A 68  ? O GLN A 68  
AA3 1 2 N TYR A 80  ? N TYR A 80  O ASP A 84  ? O ASP A 84  
AA4 1 2 N PHE A 88  ? N PHE A 88  O HIS A 113 ? O HIS A 113 
AA5 1 2 N ARG A 99  ? N ARG A 99  O LEU A 106 ? O LEU A 106 
AA5 2 3 N ALA A 109 ? N ALA A 109 O THR A 127 ? O THR A 127 
AA5 3 4 N CYS A 128 ? N CYS A 128 O TYR A 139 ? O TYR A 139 
AA6 1 2 N ASP A 162 ? N ASP A 162 O LEU A 170 ? O LEU A 170 
AA6 2 3 N LEU A 171 ? N LEU A 171 O ILE A 184 ? O ILE A 184 
AA6 3 4 N SER A 185 ? N SER A 185 O LEU A 208 ? O LEU A 208 
AA7 1 2 N ALA A 227 ? N ALA A 227 O VAL A 240 ? O VAL A 240 
AA7 2 3 N VAL A 243 ? N VAL A 243 O MET A 252 ? O MET A 252 
AA7 3 4 N ILE A 255 ? N ILE A 255 O LEU A 264 ? O LEU A 264 
AA8 1 2 N ALA A 281 ? N ALA A 281 O PHE A 294 ? O PHE A 294 
AA8 2 3 N ALA A 297 ? N ALA A 297 O GLN A 314 ? O GLN A 314 
AA8 3 4 N VAL A 315 ? N VAL A 315 O LEU A 331 ? O LEU A 331 
AA9 1 2 N ASP A 302 ? N ASP A 302 O GLN A 310 ? O GLN A 310 
AB1 1 2 N GLY A 348 ? N GLY A 348 O ASP A 357 ? O ASP A 357 
AB1 2 3 N ALA A 362 ? N ALA A 362 O ILE A 372 ? O ILE A 372 
AB1 3 4 N VAL A 373 ? N VAL A 373 O LEU A 391 ? O LEU A 391 
AB2 1 2 N ARG A 379 ? N ARG A 379 O GLY A 382 ? O GLY A 382 
AB3 1 2 N LEU A 513 ? N LEU A 513 O TYR A 542 ? O TYR A 542 
AB3 2 3 O LEU A 539 ? O LEU A 539 N VAL A 476 ? N VAL A 476 
AB3 3 4 O ASP A 483 ? O ASP A 483 N THR A 443 ? N THR A 443 
AB3 4 5 N ILE A 442 ? N ILE A 442 O ILE A 578 ? O ILE A 578 
AB4 1 2 O MET A 526 ? O MET A 526 N PHE A 494 ? N PHE A 494 
AB4 2 3 N GLU A 497 ? N GLU A 497 O GLU A 561 ? O GLU A 561 
AB4 3 4 N MET A 560 ? N MET A 560 O ILE A 587 ? O ILE A 587 
AB5 1 2 O LYS B 84  ? O LYS B 194 N SER B 49  ? N SER B 159 
AB5 2 3 O GLY B 48  ? O GLY B 158 N MET B 12  ? N MET B 122 
AB5 3 4 N TYR B 9   ? N TYR B 119 O LEU B 138 ? O LEU B 248 
AB5 4 5 N PHE B 141 ? N PHE B 251 O ALA B 202 ? O ALA B 312 
AB5 5 6 N PHE B 201 ? N PHE B 311 O THR B 222 ? O THR B 332 
AB6 1 2 O PHE C 171 ? O PHE C 169 N LEU C 128 ? N LEU C 126 
AB6 2 3 N ARG C 125 ? N ARG C 123 O MET C 234 ? O MET C 232 
AB6 3 4 O LEU C 233 ? O LEU C 231 N THR C 82  ? N THR C 80  
AB6 4 5 N VAL C 81  ? N VAL C 79  O VAL D 349 ? O VAL D 347 
AB6 5 6 O GLU D 350 ? O GLU D 348 N ILE D 339 ? N ILE D 337 
AB6 6 7 O VAL D 340 ? O VAL D 338 N GLU D 286 ? N GLU D 284 
AB7 1 2 N ILE C 104 ? N ILE C 102 O LEU C 192 ? O LEU C 190 
AB7 2 3 O ARG C 191 ? O ARG C 189 N TYR C 144 ? N TYR C 142 
AB7 3 4 N TYR C 147 ? N TYR C 145 O SER C 151 ? O SER C 149 
AB8 1 2 N ARG C 269 ? N ARG C 267 O PHE C 294 ? O PHE C 292 
AB9 1 2 N ILE C 273 ? N ILE C 271 O TYR C 290 ? O TYR C 288 
AC1 1 2 N GLU C 286 ? N GLU C 284 O VAL C 340 ? O VAL C 338 
AC1 2 3 N ILE C 339 ? N ILE C 337 O GLU C 350 ? O GLU C 348 
AC1 3 4 N VAL C 349 ? N VAL C 347 O VAL D 81  ? O VAL D 79  
AC1 4 5 N THR D 82  ? N THR D 80  O LEU D 233 ? O LEU D 231 
AC1 5 6 O PHE D 230 ? O PHE D 228 N ARG D 129 ? N ARG D 127 
AC1 6 7 N LEU D 128 ? N LEU D 126 O PHE D 171 ? O PHE D 169 
AC2 1 2 N VAL C 330 ? N VAL C 328 O LYS C 361 ? O LYS C 359 
AC3 1 2 N MET D 106 ? N MET D 104 O PHE D 190 ? O PHE D 188 
AC3 2 3 O ARG D 191 ? O ARG D 189 N TYR D 144 ? N TYR D 142 
AC3 3 4 N TYR D 147 ? N TYR D 145 O SER D 151 ? O SER D 149 
AC4 1 2 N ARG D 269 ? N ARG D 267 O PHE D 294 ? O PHE D 292 
AC5 1 2 N VAL D 330 ? N VAL D 328 O LYS D 361 ? O LYS D 359 
AC6 1 2 N TYR E 11  ? N TYR E 11  O ALA E 433 ? O ALA E 433 
AC6 2 3 O ARG E 432 ? O ARG E 432 N ALA E 427 ? N ALA E 427 
AC6 3 4 O GLY E 426 ? O GLY E 426 N SER E 408 ? N SER E 408 
AC7 1 2 N ASP E 24  ? N ASP E 24  O LEU E 37  ? O LEU E 37  
AC7 2 3 N LEU E 36  ? N LEU E 36  O CYS E 59  ? O CYS E 59  
AC7 3 4 N LYS E 58  ? N LYS E 58  O GLN E 68  ? O GLN E 68  
AC8 1 2 N TYR E 80  ? N TYR E 80  O ASP E 84  ? O ASP E 84  
AC9 1 2 N PHE E 88  ? N PHE E 88  O HIS E 113 ? O HIS E 113 
AD1 1 2 N ARG E 99  ? N ARG E 99  O LEU E 106 ? O LEU E 106 
AD1 2 3 N ALA E 109 ? N ALA E 109 O THR E 127 ? O THR E 127 
AD1 3 4 N CYS E 128 ? N CYS E 128 O TYR E 139 ? O TYR E 139 
AD2 1 2 N ASP E 162 ? N ASP E 162 O LEU E 170 ? O LEU E 170 
AD2 2 3 N LEU E 171 ? N LEU E 171 O ILE E 184 ? O ILE E 184 
AD2 3 4 N SER E 185 ? N SER E 185 O LEU E 208 ? O LEU E 208 
AD3 1 2 N GLY E 229 ? N GLY E 229 O ASP E 238 ? O ASP E 238 
AD3 2 3 N VAL E 243 ? N VAL E 243 O MET E 252 ? O MET E 252 
AD3 3 4 N ILE E 255 ? N ILE E 255 O LEU E 264 ? O LEU E 264 
AD4 1 2 N ALA E 281 ? N ALA E 281 O PHE E 294 ? O PHE E 294 
AD4 2 3 N ALA E 297 ? N ALA E 297 O GLN E 314 ? O GLN E 314 
AD4 3 4 N VAL E 315 ? N VAL E 315 O LEU E 331 ? O LEU E 331 
AD5 1 2 N ASP E 302 ? N ASP E 302 O GLN E 310 ? O GLN E 310 
AD6 1 2 N GLY E 348 ? N GLY E 348 O ASP E 357 ? O ASP E 357 
AD6 2 3 N ALA E 362 ? N ALA E 362 O ILE E 372 ? O ILE E 372 
AD6 3 4 N VAL E 373 ? N VAL E 373 O LEU E 391 ? O LEU E 391 
AD7 1 2 N ARG E 379 ? N ARG E 379 O GLY E 382 ? O GLY E 382 
AD8 1 2 N LEU E 513 ? N LEU E 513 O TYR E 542 ? O TYR E 542 
AD8 2 3 O LEU E 539 ? O LEU E 539 N VAL E 476 ? N VAL E 476 
AD8 3 4 O ASP E 483 ? O ASP E 483 N THR E 443 ? N THR E 443 
AD8 4 5 N ILE E 442 ? N ILE E 442 O ILE E 578 ? O ILE E 578 
AD9 1 2 O MET E 526 ? O MET E 526 N PHE E 494 ? N PHE E 494 
AD9 2 3 N GLU E 497 ? N GLU E 497 O GLU E 561 ? O GLU E 561 
AD9 3 4 N ILE E 556 ? N ILE E 556 O ALA E 591 ? O ALA E 591 
AE1 1 2 O LYS F 84  ? O LYS F 194 N SER F 49  ? N SER F 159 
AE1 2 3 O GLY F 48  ? O GLY F 158 N MET F 12  ? N MET F 122 
AE1 3 4 N LEU F 11  ? N LEU F 121 O VAL F 140 ? O VAL F 250 
AE1 4 5 N PHE F 141 ? N PHE F 251 O ILE F 200 ? O ILE F 310 
AE1 5 6 N PHE F 201 ? N PHE F 311 O THR F 222 ? O THR F 332 
AE2 1 2 O PHE G 171 ? O PHE G 169 N LEU G 128 ? N LEU G 126 
AE2 2 3 N ARG G 125 ? N ARG G 123 O MET G 234 ? O MET G 232 
AE2 3 4 O LEU G 233 ? O LEU G 231 N THR G 82  ? N THR G 80  
AE2 4 5 N VAL G 81  ? N VAL G 79  O VAL H 349 ? O VAL H 347 
AE2 5 6 O GLU H 350 ? O GLU H 348 N ILE H 339 ? N ILE H 337 
AE2 6 7 O VAL H 340 ? O VAL H 338 N GLU H 286 ? N GLU H 284 
AE3 1 2 N ILE G 104 ? N ILE G 102 O LEU G 192 ? O LEU G 190 
AE3 2 3 O ARG G 191 ? O ARG G 189 N TYR G 144 ? N TYR G 142 
AE3 3 4 N TYR G 147 ? N TYR G 145 O SER G 151 ? O SER G 149 
AE4 1 2 N ARG G 269 ? N ARG G 267 O PHE G 294 ? O PHE G 292 
AE5 1 2 N ILE G 273 ? N ILE G 271 O TYR G 290 ? O TYR G 288 
AE6 1 2 N GLU G 286 ? N GLU G 284 O VAL G 340 ? O VAL G 338 
AE6 2 3 N ILE G 339 ? N ILE G 337 O GLU G 350 ? O GLU G 348 
AE6 3 4 N VAL G 349 ? N VAL G 347 O VAL H 81  ? O VAL H 79  
AE6 4 5 N THR H 82  ? N THR H 80  O LEU H 233 ? O LEU H 231 
AE6 5 6 O PHE H 230 ? O PHE H 228 N ARG H 129 ? N ARG H 127 
AE6 6 7 N LEU H 128 ? N LEU H 126 O PHE H 171 ? O PHE H 169 
AE7 1 2 N VAL G 330 ? N VAL G 328 O LYS G 361 ? O LYS G 359 
AE8 1 2 N ILE H 104 ? N ILE H 102 O LEU H 192 ? O LEU H 190 
AE8 2 3 O ARG H 191 ? O ARG H 189 N TYR H 144 ? N TYR H 142 
AE8 3 4 N TYR H 147 ? N TYR H 145 O SER H 151 ? O SER H 149 
AE9 1 2 N ARG H 269 ? N ARG H 267 O PHE H 294 ? O PHE H 292 
AF1 1 2 N VAL H 330 ? N VAL H 328 O LYS H 361 ? O LYS H 359 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A CA  2001 ? 5  'binding site for residue CA A 2001'                                                         
AC2 Software A CA  2002 ? 5  'binding site for residue CA A 2002'                                                         
AC3 Software A CA  2003 ? 5  'binding site for residue CA A 2003'                                                         
AC4 Software A CA  2004 ? 5  'binding site for residue CA A 2004'                                                         
AC5 Software B MN  2001 ? 5  'binding site for residue MN B 2001'                                                         
AC6 Software B MN  2002 ? 6  'binding site for residue MN B 2002'                                                         
AC7 Software B MN  2003 ? 5  'binding site for residue MN B 2003'                                                         
AC8 Software E CA  2001 ? 5  'binding site for residue CA E 2001'                                                         
AC9 Software E CA  2002 ? 5  'binding site for residue CA E 2002'                                                         
AD1 Software E CA  2003 ? 5  'binding site for residue CA E 2003'                                                         
AD2 Software E CA  2004 ? 6  'binding site for residue CA E 2004'                                                         
AD3 Software F MN  2001 ? 4  'binding site for residue MN F 2001'                                                         
AD4 Software F MN  2002 ? 6  'binding site for residue MN F 2002'                                                         
AD5 Software F MN  2003 ? 5  'binding site for residue MN F 2003'                                                         
AD6 Software A ASN 44   ? 3  'binding site for Poly-Saccharide residues NAG A 2005 through BMA A 2007 bound to ASN A 44'  
AD7 Software A ASN 260  ? 11 'binding site for Poly-Saccharide residues NAG A 2008 through MAN A 2013 bound to ASN A 260' 
AD8 Software A ASN 266  ? 8  'binding site for Poly-Saccharide residues NAG A 2014 through MAN A 2020 bound to ASN A 266' 
AD9 Software A ASN 459  ? 6  'binding site for Poly-Saccharide residues NAG A 2021 through MAN A 2024 bound to ASN A 459' 
AE1 Software A NAG 2025 ? 2  'binding site for Mono-Saccharide NAG A 2025 bound to ASN A 525'                             
AE2 Software A ASN 586  ? 4  'binding site for Poly-Saccharide residues NAG A 2026 through NAG A 2027 bound to ASN A 586' 
AE3 Software B NAG 2004 ? 1  'binding site for Mono-Saccharide NAG B 2004 bound to ASN B 243'                             
AE4 Software C ASN 53   ? 3  'binding site for Poly-Saccharide residues NAG C 401 through MAN C 404 bound to ASN C 53'    
AE5 Software D ASN 53   ? 4  'binding site for Poly-Saccharide residues NAG D 401 through MAN D 404 bound to ASN D 53'    
AE6 Software E ASN 44   ? 4  'binding site for Poly-Saccharide residues NAG E 2005 through BMA E 2007 bound to ASN E 44'  
AE7 Software E ASN 260  ? 11 'binding site for Poly-Saccharide residues NAG E 2008 through MAN E 2013 bound to ASN E 260' 
AE8 Software E ASN 266  ? 9  'binding site for Poly-Saccharide residues NAG E 2014 through MAN E 2020 bound to ASN E 266' 
AE9 Software E ASN 459  ? 6  'binding site for Poly-Saccharide residues NAG E 2021 through MAN E 2024 bound to ASN E 459' 
AF1 Software E NAG 2025 ? 1  'binding site for Mono-Saccharide NAG E 2025 bound to ASN E 525'                             
AF2 Software E ASN 586  ? 4  'binding site for Poly-Saccharide residues NAG E 2026 through NAG E 2027 bound to ASN E 586' 
AF3 Software F NAG 2004 ? 1  'binding site for Mono-Saccharide NAG F 2004 bound to ASN F 243'                             
AF4 Software G ASN 53   ? 2  'binding site for Poly-Saccharide residues NAG G 401 through MAN G 404 bound to ASN G 53'    
AF5 Software H ASN 53   ? 3  'binding site for Poly-Saccharide residues NAG H 401 through MAN H 406 bound to ASN H 53'    
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 5  ASP A  284 ? ASP A 284  . ? 1_555 ? 
2   AC1 5  ASN A  286 ? ASN A 286  . ? 1_555 ? 
3   AC1 5  ASP A  288 ? ASP A 288  . ? 1_555 ? 
4   AC1 5  TYR A  290 ? TYR A 290  . ? 1_555 ? 
5   AC1 5  ASP A  292 ? ASP A 292  . ? 1_555 ? 
6   AC2 5  ASP A  349 ? ASP A 349  . ? 1_555 ? 
7   AC2 5  ASP A  351 ? ASP A 351  . ? 1_555 ? 
8   AC2 5  ASP A  353 ? ASP A 353  . ? 1_555 ? 
9   AC2 5  PHE A  355 ? PHE A 355  . ? 1_555 ? 
10  AC2 5  ASP A  357 ? ASP A 357  . ? 1_555 ? 
11  AC3 5  ASP A  414 ? ASP A 414  . ? 1_555 ? 
12  AC3 5  ASP A  416 ? ASP A 416  . ? 1_555 ? 
13  AC3 5  ASN A  418 ? ASN A 418  . ? 1_555 ? 
14  AC3 5  TYR A  420 ? TYR A 420  . ? 1_555 ? 
15  AC3 5  ASP A  422 ? ASP A 422  . ? 1_555 ? 
16  AC4 5  ASP A  230 ? ASP A 230  . ? 1_555 ? 
17  AC4 5  ASN A  232 ? ASN A 232  . ? 1_555 ? 
18  AC4 5  ASP A  234 ? ASP A 234  . ? 1_555 ? 
19  AC4 5  ILE A  236 ? ILE A 236  . ? 1_555 ? 
20  AC4 5  ASP A  238 ? ASP A 238  . ? 1_555 ? 
21  AC5 5  SER B  17  ? SER B 127  . ? 1_555 ? 
22  AC5 5  ASP B  20  ? ASP B 130  . ? 1_555 ? 
23  AC5 5  ASP B  21  ? ASP B 131  . ? 1_555 ? 
24  AC5 5  ASP B  144 ? ASP B 254  . ? 1_555 ? 
25  AC5 5  HOH KC .   ? HOH B 2103 . ? 1_555 ? 
26  AC6 6  SER B  15  ? SER B 125  . ? 1_555 ? 
27  AC6 6  SER B  17  ? SER B 127  . ? 1_555 ? 
28  AC6 6  GLU B  113 ? GLU B 223  . ? 1_555 ? 
29  AC6 6  HOH KC .   ? HOH B 2101 . ? 1_555 ? 
30  AC6 6  HOH KC .   ? HOH B 2102 . ? 1_555 ? 
31  AC6 6  ASP D  219 ? ASP D 217  . ? 1_555 ? 
32  AC7 5  GLU B  52  ? GLU B 162  . ? 1_555 ? 
33  AC7 5  ASN B  108 ? ASN B 218  . ? 1_555 ? 
34  AC7 5  ASP B  110 ? ASP B 220  . ? 1_555 ? 
35  AC7 5  PRO B  112 ? PRO B 222  . ? 1_555 ? 
36  AC7 5  GLU B  113 ? GLU B 223  . ? 1_555 ? 
37  AC8 5  ASP E  284 ? ASP E 284  . ? 1_555 ? 
38  AC8 5  ASN E  286 ? ASN E 286  . ? 1_555 ? 
39  AC8 5  ASP E  288 ? ASP E 288  . ? 1_555 ? 
40  AC8 5  TYR E  290 ? TYR E 290  . ? 1_555 ? 
41  AC8 5  ASP E  292 ? ASP E 292  . ? 1_555 ? 
42  AC9 5  ASP E  349 ? ASP E 349  . ? 1_555 ? 
43  AC9 5  ASP E  351 ? ASP E 351  . ? 1_555 ? 
44  AC9 5  ASP E  353 ? ASP E 353  . ? 1_555 ? 
45  AC9 5  PHE E  355 ? PHE E 355  . ? 1_555 ? 
46  AC9 5  ASP E  357 ? ASP E 357  . ? 1_555 ? 
47  AD1 5  ASP E  414 ? ASP E 414  . ? 1_555 ? 
48  AD1 5  ASP E  416 ? ASP E 416  . ? 1_555 ? 
49  AD1 5  ASN E  418 ? ASN E 418  . ? 1_555 ? 
50  AD1 5  TYR E  420 ? TYR E 420  . ? 1_555 ? 
51  AD1 5  ASP E  422 ? ASP E 422  . ? 1_555 ? 
52  AD2 6  ASP E  230 ? ASP E 230  . ? 1_555 ? 
53  AD2 6  ASN E  232 ? ASN E 232  . ? 1_555 ? 
54  AD2 6  ASP E  234 ? ASP E 234  . ? 1_555 ? 
55  AD2 6  ILE E  236 ? ILE E 236  . ? 1_555 ? 
56  AD2 6  ASP E  238 ? ASP E 238  . ? 1_555 ? 
57  AD2 6  ASP E  257 ? ASP E 257  . ? 1_555 ? 
58  AD3 4  SER F  17  ? SER F 127  . ? 1_555 ? 
59  AD3 4  ASP F  20  ? ASP F 130  . ? 1_555 ? 
60  AD3 4  ASP F  21  ? ASP F 131  . ? 1_555 ? 
61  AD3 4  ASP F  144 ? ASP F 254  . ? 1_555 ? 
62  AD4 6  SER F  15  ? SER F 125  . ? 1_555 ? 
63  AD4 6  SER F  17  ? SER F 127  . ? 1_555 ? 
64  AD4 6  GLU F  113 ? GLU F 223  . ? 1_555 ? 
65  AD4 6  HOH LC .   ? HOH F 2101 . ? 1_555 ? 
66  AD4 6  HOH LC .   ? HOH F 2102 . ? 1_555 ? 
67  AD4 6  ASP H  219 ? ASP H 217  . ? 1_555 ? 
68  AD5 5  GLU F  52  ? GLU F 162  . ? 1_555 ? 
69  AD5 5  ASN F  108 ? ASN F 218  . ? 1_555 ? 
70  AD5 5  ASP F  110 ? ASP F 220  . ? 1_555 ? 
71  AD5 5  PRO F  112 ? PRO F 222  . ? 1_555 ? 
72  AD5 5  GLU F  113 ? GLU F 223  . ? 1_555 ? 
73  AD6 3  GLU A  15  ? GLU A 15   . ? 1_555 ? 
74  AD6 3  ASN A  44  ? ASN A 44   . ? 1_555 ? 
75  AD6 3  GLU A  52  ? GLU A 52   . ? 1_555 ? 
76  AD7 11 PHE A  231 ? PHE A 231  . ? 1_555 ? 
77  AD7 11 ASN A  232 ? ASN A 232  . ? 1_555 ? 
78  AD7 11 ASP A  257 ? ASP A 257  . ? 1_555 ? 
79  AD7 11 ASN A  260 ? ASN A 260  . ? 1_555 ? 
80  AD7 11 TYR A  265 ? TYR A 265  . ? 1_555 ? 
81  AD7 11 ALA A  322 ? ALA A 322  . ? 1_555 ? 
82  AD7 11 ARG E  550 ? ARG E 550  . ? 1_556 ? 
83  AD7 11 LYS H  136 ? LYS H 134  . ? 1_555 ? 
84  AD7 11 VAL H  137 ? VAL H 135  . ? 1_555 ? 
85  AD7 11 PRO H  162 ? PRO H 160  . ? 1_555 ? 
86  AD7 11 ASP H  164 ? ASP H 162  . ? 1_555 ? 
87  AD8 8  THR A  212 ? THR A 212  . ? 1_555 ? 
88  AD8 8  ALA A  213 ? ALA A 213  . ? 1_555 ? 
89  AD8 8  GLN A  214 ? GLN A 214  . ? 1_555 ? 
90  AD8 8  TYR A  254 ? TYR A 254  . ? 1_555 ? 
91  AD8 8  SER A  263 ? SER A 263  . ? 1_555 ? 
92  AD8 8  LEU A  264 ? LEU A 264  . ? 1_555 ? 
93  AD8 8  ASN A  266 ? ASN A 266  . ? 1_555 ? 
94  AD8 8  LYS E  82  ? LYS E 82   . ? 1_555 ? 
95  AD9 6  PRO A  452 ? PRO A 452  . ? 1_555 ? 
96  AD9 6  ASN A  459 ? ASN A 459  . ? 1_555 ? 
97  AD9 6  THR A  461 ? THR A 461  . ? 1_555 ? 
98  AD9 6  CYS A  473 ? CYS A 473  . ? 1_555 ? 
99  AD9 6  ASN A  475 ? ASN A 475  . ? 1_555 ? 
100 AD9 6  GLU A  538 ? GLU A 538  . ? 1_555 ? 
101 AE1 2  GLN A  495 ? GLN A 495  . ? 1_555 ? 
102 AE1 2  ASN A  525 ? ASN A 525  . ? 1_555 ? 
103 AE2 4  LYS A  502 ? LYS A 502  . ? 1_555 ? 
104 AE2 4  PHE A  559 ? PHE A 559  . ? 1_555 ? 
105 AE2 4  ALA A  585 ? ALA A 585  . ? 1_555 ? 
106 AE2 4  ASN A  586 ? ASN A 586  . ? 1_555 ? 
107 AE3 1  ASN B  133 ? ASN B 243  . ? 1_555 ? 
108 AE4 3  GLU C  48  ? GLU C 46   . ? 1_555 ? 
109 AE4 3  ASN C  55  ? ASN C 53   . ? 1_555 ? 
110 AE4 3  ARG C  58  ? ARG C 56   . ? 1_555 ? 
111 AE5 4  ALA B  67  ? ALA B 177  . ? 1_555 ? 
112 AE5 4  PHE B  76  ? PHE B 186  . ? 1_555 ? 
113 AE5 4  ASN D  55  ? ASN D 53   . ? 1_555 ? 
114 AE5 4  ARG D  58  ? ARG D 56   . ? 1_555 ? 
115 AE6 4  GLU E  15  ? GLU E 15   . ? 1_555 ? 
116 AE6 4  GLY E  16  ? GLY E 16   . ? 1_555 ? 
117 AE6 4  ASN E  44  ? ASN E 44   . ? 1_555 ? 
118 AE6 4  GLU E  52  ? GLU E 52   . ? 1_555 ? 
119 AE7 11 ARG A  550 ? ARG A 550  . ? 1_544 ? 
120 AE7 11 LYS D  136 ? LYS D 134  . ? 1_545 ? 
121 AE7 11 VAL D  137 ? VAL D 135  . ? 1_545 ? 
122 AE7 11 ASP D  164 ? ASP D 162  . ? 1_545 ? 
123 AE7 11 PHE E  231 ? PHE E 231  . ? 1_555 ? 
124 AE7 11 ASN E  232 ? ASN E 232  . ? 1_555 ? 
125 AE7 11 ASP E  257 ? ASP E 257  . ? 1_555 ? 
126 AE7 11 LYS E  259 ? LYS E 259  . ? 1_555 ? 
127 AE7 11 ASN E  260 ? ASN E 260  . ? 1_555 ? 
128 AE7 11 TYR E  265 ? TYR E 265  . ? 1_555 ? 
129 AE7 11 ALA E  322 ? ALA E 322  . ? 1_555 ? 
130 AE8 9  LYS A  82  ? LYS A 82   . ? 1_545 ? 
131 AE8 9  THR E  212 ? THR E 212  . ? 1_555 ? 
132 AE8 9  ALA E  213 ? ALA E 213  . ? 1_555 ? 
133 AE8 9  GLN E  214 ? GLN E 214  . ? 1_555 ? 
134 AE8 9  TYR E  254 ? TYR E 254  . ? 1_555 ? 
135 AE8 9  TYR E  256 ? TYR E 256  . ? 1_555 ? 
136 AE8 9  SER E  263 ? SER E 263  . ? 1_555 ? 
137 AE8 9  LEU E  264 ? LEU E 264  . ? 1_555 ? 
138 AE8 9  ASN E  266 ? ASN E 266  . ? 1_555 ? 
139 AE9 6  ILE E  454 ? ILE E 454  . ? 1_555 ? 
140 AE9 6  ASN E  459 ? ASN E 459  . ? 1_555 ? 
141 AE9 6  THR E  461 ? THR E 461  . ? 1_555 ? 
142 AE9 6  CYS E  473 ? CYS E 473  . ? 1_555 ? 
143 AE9 6  ASN E  475 ? ASN E 475  . ? 1_555 ? 
144 AE9 6  GLU E  538 ? GLU E 538  . ? 1_555 ? 
145 AF1 1  ASN E  525 ? ASN E 525  . ? 1_555 ? 
146 AF2 4  LYS E  502 ? LYS E 502  . ? 1_555 ? 
147 AF2 4  PHE E  559 ? PHE E 559  . ? 1_555 ? 
148 AF2 4  ALA E  585 ? ALA E 585  . ? 1_555 ? 
149 AF2 4  ASN E  586 ? ASN E 586  . ? 1_555 ? 
150 AF3 1  ASN F  133 ? ASN F 243  . ? 1_555 ? 
151 AF4 2  ASN G  55  ? ASN G 53   . ? 1_555 ? 
152 AF4 2  ARG G  58  ? ARG G 56   . ? 1_555 ? 
153 AF5 3  PHE F  76  ? PHE F 186  . ? 1_555 ? 
154 AF5 3  ASN H  55  ? ASN H 53   . ? 1_555 ? 
155 AF5 3  ARG H  58  ? ARG H 56   . ? 1_555 ? 
# 
_atom_sites.entry_id                    5FFO 
_atom_sites.fract_transf_matrix[1][1]   0.012279 
_atom_sites.fract_transf_matrix[1][2]   -0.000033 
_atom_sites.fract_transf_matrix[1][3]   -0.000805 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010936 
_atom_sites.fract_transf_matrix[2][3]   -0.000002 
_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]   0.007648 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CA 
MN 
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   . PHE A  1 1   ? 10.681  -12.973 52.010   1.00 193.07 ? 1    PHE A N   1 
ATOM   2     C  CA  . PHE A  1 1   ? 10.743  -12.103 53.178   1.00 196.40 ? 1    PHE A CA  1 
ATOM   3     C  C   . PHE A  1 1   ? 12.059  -11.341 53.217   1.00 200.86 ? 1    PHE A C   1 
ATOM   4     O  O   . PHE A  1 1   ? 12.170  -10.309 53.880   1.00 203.55 ? 1    PHE A O   1 
ATOM   5     C  CB  . PHE A  1 1   ? 10.561  -12.914 54.465   1.00 198.62 ? 1    PHE A CB  1 
ATOM   6     C  CG  . PHE A  1 1   ? 11.634  -13.944 54.694   1.00 213.80 ? 1    PHE A CG  1 
ATOM   7     C  CD1 . PHE A  1 1   ? 11.543  -15.195 54.107   1.00 211.37 ? 1    PHE A CD1 1 
ATOM   8     C  CD2 . PHE A  1 1   ? 12.723  -13.672 55.512   1.00 234.17 ? 1    PHE A CD2 1 
ATOM   9     C  CE1 . PHE A  1 1   ? 12.523  -16.150 54.316   1.00 226.39 ? 1    PHE A CE1 1 
ATOM   10    C  CE2 . PHE A  1 1   ? 13.708  -14.626 55.728   1.00 210.93 ? 1    PHE A CE2 1 
ATOM   11    C  CZ  . PHE A  1 1   ? 13.606  -15.866 55.130   1.00 208.87 ? 1    PHE A CZ  1 
ATOM   12    N  N   . ASN A  1 2   ? 13.051  -11.857 52.493   1.00 213.47 ? 2    ASN A N   1 
ATOM   13    C  CA  . ASN A  1 2   ? 14.417  -11.353 52.541   1.00 219.49 ? 2    ASN A CA  1 
ATOM   14    C  C   . ASN A  1 2   ? 14.743  -10.366 51.425   1.00 216.01 ? 2    ASN A C   1 
ATOM   15    O  O   . ASN A  1 2   ? 15.921  -10.063 51.211   1.00 229.72 ? 2    ASN A O   1 
ATOM   16    C  CB  . ASN A  1 2   ? 15.399  -12.525 52.504   1.00 209.52 ? 2    ASN A CB  1 
ATOM   17    C  CG  . ASN A  1 2   ? 15.156  -13.451 51.327   1.00 205.75 ? 2    ASN A CG  1 
ATOM   18    O  OD1 . ASN A  1 2   ? 14.013  -13.695 50.939   1.00 202.74 ? 2    ASN A OD1 1 
ATOM   19    N  ND2 . ASN A  1 2   ? 16.233  -13.979 50.758   1.00 209.61 ? 2    ASN A ND2 1 
ATOM   20    N  N   . LEU A  1 3   ? 13.742  -9.855  50.711   1.00 215.89 ? 3    LEU A N   1 
ATOM   21    C  CA  . LEU A  1 3   ? 14.005  -8.836  49.701   1.00 215.49 ? 3    LEU A CA  1 
ATOM   22    C  C   . LEU A  1 3   ? 14.290  -7.497  50.367   1.00 214.18 ? 3    LEU A C   1 
ATOM   23    O  O   . LEU A  1 3   ? 13.561  -7.067  51.267   1.00 209.47 ? 3    LEU A O   1 
ATOM   24    C  CB  . LEU A  1 3   ? 12.829  -8.707  48.733   1.00 209.95 ? 3    LEU A CB  1 
ATOM   25    C  CG  . LEU A  1 3   ? 12.728  -9.788  47.658   1.00 198.24 ? 3    LEU A CG  1 
ATOM   26    C  CD1 . LEU A  1 3   ? 11.462  -9.614  46.843   1.00 191.72 ? 3    LEU A CD1 1 
ATOM   27    C  CD2 . LEU A  1 3   ? 13.953  -9.759  46.762   1.00 204.86 ? 3    LEU A CD2 1 
ATOM   28    N  N   . ASP A  1 4   ? 15.360  -6.842  49.927   1.00 213.10 ? 4    ASP A N   1 
ATOM   29    C  CA  . ASP A  1 4   ? 15.782  -5.572  50.507   1.00 220.22 ? 4    ASP A CA  1 
ATOM   30    C  C   . ASP A  1 4   ? 14.908  -4.453  49.948   1.00 209.44 ? 4    ASP A C   1 
ATOM   31    O  O   . ASP A  1 4   ? 15.027  -4.090  48.771   1.00 207.88 ? 4    ASP A O   1 
ATOM   32    C  CB  . ASP A  1 4   ? 17.256  -5.324  50.207   1.00 217.00 ? 4    ASP A CB  1 
ATOM   33    C  CG  . ASP A  1 4   ? 17.755  -4.018  50.781   1.00 221.80 ? 4    ASP A CG  1 
ATOM   34    O  OD1 . ASP A  1 4   ? 17.872  -3.916  52.019   1.00 225.20 ? 4    ASP A OD1 1 
ATOM   35    O  OD2 . ASP A  1 4   ? 18.028  -3.096  49.989   1.00 222.40 ? 4    ASP A OD2 1 
ATOM   36    N  N   . VAL A  1 5   ? 14.040  -3.896  50.800   1.00 209.31 ? 5    VAL A N   1 
ATOM   37    C  CA  . VAL A  1 5   ? 13.201  -2.764  50.430   1.00 207.63 ? 5    VAL A CA  1 
ATOM   38    C  C   . VAL A  1 5   ? 13.765  -1.464  50.967   1.00 212.84 ? 5    VAL A C   1 
ATOM   39    O  O   . VAL A  1 5   ? 13.212  -0.388  50.699   1.00 212.55 ? 5    VAL A O   1 
ATOM   40    C  CB  . VAL A  1 5   ? 11.745  -2.954  50.909   1.00 204.11 ? 5    VAL A CB  1 
ATOM   41    C  CG1 . VAL A  1 5   ? 10.768  -2.232  49.981   1.00 200.49 ? 5    VAL A CG1 1 
ATOM   42    C  CG2 . VAL A  1 5   ? 11.392  -4.427  50.999   1.00 208.31 ? 5    VAL A CG2 1 
ATOM   43    N  N   . ASP A  1 6   ? 14.853  -1.537  51.738   1.00 238.68 ? 6    ASP A N   1 
ATOM   44    C  CA  . ASP A  1 6   ? 15.469  -0.335  52.287   1.00 244.32 ? 6    ASP A CA  1 
ATOM   45    C  C   . ASP A  1 6   ? 16.241  0.431   51.218   1.00 230.92 ? 6    ASP A C   1 
ATOM   46    O  O   . ASP A  1 6   ? 16.125  1.658   51.128   1.00 229.46 ? 6    ASP A O   1 
ATOM   47    C  CB  . ASP A  1 6   ? 16.396  -0.698  53.453   1.00 266.63 ? 6    ASP A CB  1 
ATOM   48    C  CG  . ASP A  1 6   ? 15.656  -1.324  54.626   1.00 265.59 ? 6    ASP A CG  1 
ATOM   49    O  OD1 . ASP A  1 6   ? 14.410  -1.206  54.683   1.00 259.60 ? 6    ASP A OD1 1 
ATOM   50    O  OD2 . ASP A  1 6   ? 16.325  -1.927  55.495   1.00 260.20 ? 6    ASP A OD2 1 
ATOM   51    N  N   . SER A  1 7   ? 17.025  -0.266  50.392   1.00 238.00 ? 7    SER A N   1 
ATOM   52    C  CA  . SER A  1 7   ? 17.865  0.377   49.377   1.00 251.97 ? 7    SER A CA  1 
ATOM   53    C  C   . SER A  1 7   ? 17.773  -0.373  48.051   1.00 236.07 ? 7    SER A C   1 
ATOM   54    O  O   . SER A  1 7   ? 18.697  -1.092  47.653   1.00 227.49 ? 7    SER A O   1 
ATOM   55    C  CB  . SER A  1 7   ? 19.317  0.479   49.856   1.00 264.07 ? 7    SER A CB  1 
ATOM   56    O  OG  . SER A  1 7   ? 19.833  -0.782  50.249   1.00 266.56 ? 7    SER A OG  1 
ATOM   57    N  N   . PRO A  1 8   ? 16.653  -0.238  47.345   1.00 219.15 ? 8    PRO A N   1 
ATOM   58    C  CA  . PRO A  1 8   ? 16.532  -0.835  46.013   1.00 231.12 ? 8    PRO A CA  1 
ATOM   59    C  C   . PRO A  1 8   ? 17.066  0.072   44.914   1.00 253.55 ? 8    PRO A C   1 
ATOM   60    O  O   . PRO A  1 8   ? 17.078  1.299   45.026   1.00 269.28 ? 8    PRO A O   1 
ATOM   61    C  CB  . PRO A  1 8   ? 15.016  -1.030  45.873   1.00 207.13 ? 8    PRO A CB  1 
ATOM   62    C  CG  . PRO A  1 8   ? 14.448  0.112   46.639   1.00 208.78 ? 8    PRO A CG  1 
ATOM   63    C  CD  . PRO A  1 8   ? 15.385  0.370   47.791   1.00 214.57 ? 8    PRO A CD  1 
ATOM   64    N  N   . ALA A  1 9   ? 17.508  -0.562  43.825   1.00 248.54 ? 9    ALA A N   1 
ATOM   65    C  CA  . ALA A  1 9   ? 18.035  0.149   42.662   1.00 233.18 ? 9    ALA A CA  1 
ATOM   66    C  C   . ALA A  1 9   ? 16.894  0.634   41.768   1.00 224.66 ? 9    ALA A C   1 
ATOM   67    O  O   . ALA A  1 9   ? 16.043  -0.159  41.348   1.00 205.14 ? 9    ALA A O   1 
ATOM   68    C  CB  . ALA A  1 9   ? 18.982  -0.757  41.879   1.00 215.57 ? 9    ALA A CB  1 
ATOM   69    N  N   . GLU A  1 10  ? 16.872  1.936   41.474   1.00 228.29 ? 10   GLU A N   1 
ATOM   70    C  CA  . GLU A  1 10  ? 15.827  2.549   40.654   1.00 225.28 ? 10   GLU A CA  1 
ATOM   71    C  C   . GLU A  1 10  ? 16.391  2.877   39.273   1.00 220.88 ? 10   GLU A C   1 
ATOM   72    O  O   . GLU A  1 10  ? 17.233  3.771   39.135   1.00 248.99 ? 10   GLU A O   1 
ATOM   73    C  CB  . GLU A  1 10  ? 15.266  3.799   41.331   1.00 234.08 ? 10   GLU A CB  1 
ATOM   74    C  CG  . GLU A  1 10  ? 14.228  4.548   40.500   1.00 239.54 ? 10   GLU A CG  1 
ATOM   75    C  CD  . GLU A  1 10  ? 13.566  5.685   41.261   1.00 237.40 ? 10   GLU A CD  1 
ATOM   76    O  OE1 . GLU A  1 10  ? 13.708  5.741   42.499   1.00 247.46 ? 10   GLU A OE1 1 
ATOM   77    O  OE2 . GLU A  1 10  ? 12.894  6.520   40.621   1.00 224.85 ? 10   GLU A OE2 1 
ATOM   78    N  N   . TYR A  1 11  ? 15.931  2.148   38.258   1.00 208.72 ? 11   TYR A N   1 
ATOM   79    C  CA  . TYR A  1 11  ? 16.294  2.403   36.869   1.00 209.17 ? 11   TYR A CA  1 
ATOM   80    C  C   . TYR A  1 11  ? 15.133  3.070   36.145   1.00 205.95 ? 11   TYR A C   1 
ATOM   81    O  O   . TYR A  1 11  ? 13.968  2.750   36.395   1.00 209.09 ? 11   TYR A O   1 
ATOM   82    C  CB  . TYR A  1 11  ? 16.686  1.112   36.148   1.00 207.52 ? 11   TYR A CB  1 
ATOM   83    C  CG  . TYR A  1 11  ? 17.920  0.457   36.718   1.00 225.59 ? 11   TYR A CG  1 
ATOM   84    C  CD1 . TYR A  1 11  ? 17.841  -0.384  37.821   1.00 234.20 ? 11   TYR A CD1 1 
ATOM   85    C  CD2 . TYR A  1 11  ? 19.167  0.697   36.163   1.00 228.49 ? 11   TYR A CD2 1 
ATOM   86    C  CE1 . TYR A  1 11  ? 18.970  -0.976  38.345   1.00 231.25 ? 11   TYR A CE1 1 
ATOM   87    C  CE2 . TYR A  1 11  ? 20.299  0.112   36.681   1.00 226.38 ? 11   TYR A CE2 1 
ATOM   88    C  CZ  . TYR A  1 11  ? 20.194  -0.722  37.770   1.00 226.99 ? 11   TYR A CZ  1 
ATOM   89    O  OH  . TYR A  1 11  ? 21.327  -1.302  38.278   1.00 228.54 ? 11   TYR A OH  1 
ATOM   90    N  N   . SER A  1 12  ? 15.455  3.995   35.241   1.00 209.04 ? 12   SER A N   1 
ATOM   91    C  CA  . SER A  1 12  ? 14.431  4.752   34.538   1.00 204.37 ? 12   SER A CA  1 
ATOM   92    C  C   . SER A  1 12  ? 14.749  4.859   33.052   1.00 213.24 ? 12   SER A C   1 
ATOM   93    O  O   . SER A  1 12  ? 15.912  4.844   32.639   1.00 208.40 ? 12   SER A O   1 
ATOM   94    C  CB  . SER A  1 12  ? 14.287  6.158   35.130   1.00 213.08 ? 12   SER A CB  1 
ATOM   95    O  OG  . SER A  1 12  ? 15.503  6.880   35.024   1.00 213.33 ? 12   SER A OG  1 
ATOM   96    N  N   . GLY A  1 13  ? 13.689  4.979   32.253   1.00 203.74 ? 13   GLY A N   1 
ATOM   97    C  CA  . GLY A  1 13  ? 13.799  5.172   30.827   1.00 210.41 ? 13   GLY A CA  1 
ATOM   98    C  C   . GLY A  1 13  ? 12.998  6.382   30.389   1.00 207.38 ? 13   GLY A C   1 
ATOM   99    O  O   . GLY A  1 13  ? 12.450  7.114   31.220   1.00 200.60 ? 13   GLY A O   1 
ATOM   100   N  N   . PRO A  1 14  ? 12.899  6.609   29.078   1.00 213.21 ? 14   PRO A N   1 
ATOM   101   C  CA  . PRO A  1 14  ? 12.142  7.768   28.582   1.00 212.90 ? 14   PRO A CA  1 
ATOM   102   C  C   . PRO A  1 14  ? 10.706  7.767   29.084   1.00 203.46 ? 14   PRO A C   1 
ATOM   103   O  O   . PRO A  1 14  ? 10.058  6.722   29.164   1.00 200.97 ? 14   PRO A O   1 
ATOM   104   C  CB  . PRO A  1 14  ? 12.198  7.602   27.060   1.00 210.58 ? 14   PRO A CB  1 
ATOM   105   C  CG  . PRO A  1 14  ? 13.433  6.782   26.815   1.00 215.52 ? 14   PRO A CG  1 
ATOM   106   C  CD  . PRO A  1 14  ? 13.526  5.846   27.985   1.00 214.81 ? 14   PRO A CD  1 
ATOM   107   N  N   . GLU A  1 15  ? 10.212  8.955   29.429   1.00 198.66 ? 15   GLU A N   1 
ATOM   108   C  CA  . GLU A  1 15  ? 8.849   9.074   29.925   1.00 195.66 ? 15   GLU A CA  1 
ATOM   109   C  C   . GLU A  1 15  ? 7.857   8.815   28.798   1.00 192.22 ? 15   GLU A C   1 
ATOM   110   O  O   . GLU A  1 15  ? 8.128   9.085   27.625   1.00 193.44 ? 15   GLU A O   1 
ATOM   111   C  CB  . GLU A  1 15  ? 8.600   10.454  30.533   1.00 201.02 ? 15   GLU A CB  1 
ATOM   112   C  CG  . GLU A  1 15  ? 8.185   11.514  29.531   1.00 213.71 ? 15   GLU A CG  1 
ATOM   113   C  CD  . GLU A  1 15  ? 7.667   12.766  30.201   1.00 230.43 ? 15   GLU A CD  1 
ATOM   114   O  OE1 . GLU A  1 15  ? 7.850   12.900  31.431   1.00 236.12 ? 15   GLU A OE1 1 
ATOM   115   O  OE2 . GLU A  1 15  ? 7.058   13.603  29.499   1.00 235.65 ? 15   GLU A OE2 1 
ATOM   116   N  N   . GLY A  1 16  ? 6.707   8.253   29.160   1.00 193.95 ? 16   GLY A N   1 
ATOM   117   C  CA  . GLY A  1 16  ? 5.685   7.942   28.184   1.00 193.42 ? 16   GLY A CA  1 
ATOM   118   C  C   . GLY A  1 16  ? 6.009   6.778   27.279   1.00 194.46 ? 16   GLY A C   1 
ATOM   119   O  O   . GLY A  1 16  ? 5.205   6.459   26.395   1.00 184.29 ? 16   GLY A O   1 
ATOM   120   N  N   . SER A  1 17  ? 7.152   6.129   27.472   1.00 187.44 ? 17   SER A N   1 
ATOM   121   C  CA  . SER A  1 17  ? 7.603   5.066   26.591   1.00 181.89 ? 17   SER A CA  1 
ATOM   122   C  C   . SER A  1 17  ? 7.195   3.686   27.074   1.00 177.80 ? 17   SER A C   1 
ATOM   123   O  O   . SER A  1 17  ? 7.530   2.697   26.415   1.00 190.70 ? 17   SER A O   1 
ATOM   124   C  CB  . SER A  1 17  ? 9.128   5.120   26.436   1.00 185.86 ? 17   SER A CB  1 
ATOM   125   O  OG  . SER A  1 17  ? 9.785   4.891   27.671   1.00 187.02 ? 17   SER A OG  1 
ATOM   126   N  N   . TYR A  1 18  ? 6.474   3.598   28.192   1.00 175.94 ? 18   TYR A N   1 
ATOM   127   C  CA  . TYR A  1 18  ? 6.135   2.317   28.808   1.00 172.54 ? 18   TYR A CA  1 
ATOM   128   C  C   . TYR A  1 18  ? 7.398   1.532   29.149   1.00 174.01 ? 18   TYR A C   1 
ATOM   129   O  O   . TYR A  1 18  ? 7.434   0.303   29.049   1.00 171.84 ? 18   TYR A O   1 
ATOM   130   C  CB  . TYR A  1 18  ? 5.208   1.492   27.915   1.00 168.80 ? 18   TYR A CB  1 
ATOM   131   C  CG  . TYR A  1 18  ? 3.801   2.030   27.830   1.00 166.95 ? 18   TYR A CG  1 
ATOM   132   C  CD1 . TYR A  1 18  ? 3.461   3.232   28.434   1.00 168.87 ? 18   TYR A CD1 1 
ATOM   133   C  CD2 . TYR A  1 18  ? 2.814   1.335   27.151   1.00 163.69 ? 18   TYR A CD2 1 
ATOM   134   C  CE1 . TYR A  1 18  ? 2.186   3.730   28.361   1.00 167.66 ? 18   TYR A CE1 1 
ATOM   135   C  CE2 . TYR A  1 18  ? 1.535   1.826   27.072   1.00 165.16 ? 18   TYR A CE2 1 
ATOM   136   C  CZ  . TYR A  1 18  ? 1.222   3.023   27.680   1.00 176.40 ? 18   TYR A CZ  1 
ATOM   137   O  OH  . TYR A  1 18  ? -0.065  3.510   27.600   1.00 184.04 ? 18   TYR A OH  1 
ATOM   138   N  N   . PHE A  1 19  ? 8.444   2.263   29.540   1.00 179.10 ? 19   PHE A N   1 
ATOM   139   C  CA  . PHE A  1 19  ? 9.689   1.667   30.009   1.00 180.31 ? 19   PHE A CA  1 
ATOM   140   C  C   . PHE A  1 19  ? 9.433   0.741   31.189   1.00 178.20 ? 19   PHE A C   1 
ATOM   141   O  O   . PHE A  1 19  ? 9.041   1.190   32.269   1.00 178.39 ? 19   PHE A O   1 
ATOM   142   C  CB  . PHE A  1 19  ? 10.665  2.775   30.398   1.00 185.27 ? 19   PHE A CB  1 
ATOM   143   C  CG  . PHE A  1 19  ? 11.965  2.272   30.933   1.00 188.19 ? 19   PHE A CG  1 
ATOM   144   C  CD1 . PHE A  1 19  ? 12.993  1.920   30.077   1.00 190.47 ? 19   PHE A CD1 1 
ATOM   145   C  CD2 . PHE A  1 19  ? 12.158  2.151   32.296   1.00 189.01 ? 19   PHE A CD2 1 
ATOM   146   C  CE1 . PHE A  1 19  ? 14.185  1.457   30.573   1.00 193.56 ? 19   PHE A CE1 1 
ATOM   147   C  CE2 . PHE A  1 19  ? 13.345  1.687   32.797   1.00 192.01 ? 19   PHE A CE2 1 
ATOM   148   C  CZ  . PHE A  1 19  ? 14.362  1.340   31.937   1.00 195.63 ? 19   PHE A CZ  1 
ATOM   149   N  N   . GLY A  1 20  ? 9.715   -0.543  31.003   1.00 176.70 ? 20   GLY A N   1 
ATOM   150   C  CA  . GLY A  1 20  ? 9.426   -1.551  32.000   1.00 174.62 ? 20   GLY A CA  1 
ATOM   151   C  C   . GLY A  1 20  ? 8.267   -2.452  31.645   1.00 170.08 ? 20   GLY A C   1 
ATOM   152   O  O   . GLY A  1 20  ? 7.841   -3.255  32.485   1.00 168.15 ? 20   GLY A O   1 
ATOM   153   N  N   . PHE A  1 21  ? 7.741   -2.334  30.427   1.00 168.59 ? 21   PHE A N   1 
ATOM   154   C  CA  . PHE A  1 21  ? 6.660   -3.202  29.988   1.00 164.63 ? 21   PHE A CA  1 
ATOM   155   C  C   . PHE A  1 21  ? 7.107   -4.654  29.924   1.00 163.91 ? 21   PHE A C   1 
ATOM   156   O  O   . PHE A  1 21  ? 6.295   -5.564  30.126   1.00 160.93 ? 21   PHE A O   1 
ATOM   157   C  CB  . PHE A  1 21  ? 6.161   -2.729  28.629   1.00 163.98 ? 21   PHE A CB  1 
ATOM   158   C  CG  . PHE A  1 21  ? 4.919   -3.409  28.177   1.00 160.22 ? 21   PHE A CG  1 
ATOM   159   C  CD1 . PHE A  1 21  ? 3.685   -2.903  28.527   1.00 158.27 ? 21   PHE A CD1 1 
ATOM   160   C  CD2 . PHE A  1 21  ? 4.980   -4.555  27.410   1.00 164.74 ? 21   PHE A CD2 1 
ATOM   161   C  CE1 . PHE A  1 21  ? 2.541   -3.521  28.114   1.00 155.16 ? 21   PHE A CE1 1 
ATOM   162   C  CE2 . PHE A  1 21  ? 3.832   -5.181  26.996   1.00 155.86 ? 21   PHE A CE2 1 
ATOM   163   C  CZ  . PHE A  1 21  ? 2.613   -4.663  27.348   1.00 153.91 ? 21   PHE A CZ  1 
ATOM   164   N  N   . ALA A  1 22  ? 8.384   -4.889  29.632   1.00 191.04 ? 22   ALA A N   1 
ATOM   165   C  CA  . ALA A  1 22  ? 8.985   -6.217  29.667   1.00 189.71 ? 22   ALA A CA  1 
ATOM   166   C  C   . ALA A  1 22  ? 10.369  -6.110  30.285   1.00 171.36 ? 22   ALA A C   1 
ATOM   167   O  O   . ALA A  1 22  ? 11.143  -5.216  29.928   1.00 174.52 ? 22   ALA A O   1 
ATOM   168   C  CB  . ALA A  1 22  ? 9.076   -6.833  28.264   1.00 185.21 ? 22   ALA A CB  1 
ATOM   169   N  N   . VAL A  1 23  ? 10.674  -7.015  31.214   1.00 171.61 ? 23   VAL A N   1 
ATOM   170   C  CA  . VAL A  1 23  ? 11.956  -7.026  31.907   1.00 184.41 ? 23   VAL A CA  1 
ATOM   171   C  C   . VAL A  1 23  ? 12.540  -8.434  31.866   1.00 193.02 ? 23   VAL A C   1 
ATOM   172   O  O   . VAL A  1 23  ? 11.810  -9.427  31.767   1.00 206.85 ? 23   VAL A O   1 
ATOM   173   C  CB  . VAL A  1 23  ? 11.816  -6.525  33.362   1.00 176.10 ? 23   VAL A CB  1 
ATOM   174   C  CG1 . VAL A  1 23  ? 11.297  -5.094  33.383   1.00 175.92 ? 23   VAL A CG1 1 
ATOM   175   C  CG2 . VAL A  1 23  ? 10.892  -7.433  34.147   1.00 172.83 ? 23   VAL A CG2 1 
ATOM   176   N  N   . ASP A  1 24  ? 13.866  -8.517  31.943   1.00 180.98 ? 24   ASP A N   1 
ATOM   177   C  CA  . ASP A  1 24  ? 14.573  -9.796  31.965   1.00 182.85 ? 24   ASP A CA  1 
ATOM   178   C  C   . ASP A  1 24  ? 16.009  -9.526  32.416   1.00 201.75 ? 24   ASP A C   1 
ATOM   179   O  O   . ASP A  1 24  ? 16.414  -8.373  32.601   1.00 213.60 ? 24   ASP A O   1 
ATOM   180   C  CB  . ASP A  1 24  ? 14.523  -10.473 30.592   1.00 182.34 ? 24   ASP A CB  1 
ATOM   181   C  CG  . ASP A  1 24  ? 14.703  -11.974 30.672   1.00 182.71 ? 24   ASP A CG  1 
ATOM   182   O  OD1 . ASP A  1 24  ? 13.694  -12.684 30.859   1.00 179.06 ? 24   ASP A OD1 1 
ATOM   183   O  OD2 . ASP A  1 24  ? 15.851  -12.446 30.546   1.00 224.03 ? 24   ASP A OD2 1 
ATOM   184   N  N   . PHE A  1 25  ? 16.784  -10.598 32.572   1.00 200.47 ? 25   PHE A N   1 
ATOM   185   C  CA  . PHE A  1 25  ? 18.193  -10.510 32.930   1.00 196.51 ? 25   PHE A CA  1 
ATOM   186   C  C   . PHE A  1 25  ? 19.081  -10.723 31.707   1.00 199.95 ? 25   PHE A C   1 
ATOM   187   O  O   . PHE A  1 25  ? 18.621  -11.069 30.618   1.00 197.99 ? 25   PHE A O   1 
ATOM   188   C  CB  . PHE A  1 25  ? 18.560  -11.540 34.004   1.00 198.06 ? 25   PHE A CB  1 
ATOM   189   C  CG  . PHE A  1 25  ? 17.917  -11.298 35.334   1.00 196.00 ? 25   PHE A CG  1 
ATOM   190   C  CD1 . PHE A  1 25  ? 16.675  -11.827 35.625   1.00 191.18 ? 25   PHE A CD1 1 
ATOM   191   C  CD2 . PHE A  1 25  ? 18.563  -10.546 36.300   1.00 199.26 ? 25   PHE A CD2 1 
ATOM   192   C  CE1 . PHE A  1 25  ? 16.087  -11.608 36.855   1.00 197.22 ? 25   PHE A CE1 1 
ATOM   193   C  CE2 . PHE A  1 25  ? 17.983  -10.323 37.530   1.00 197.78 ? 25   PHE A CE2 1 
ATOM   194   C  CZ  . PHE A  1 25  ? 16.743  -10.854 37.810   1.00 192.99 ? 25   PHE A CZ  1 
ATOM   195   N  N   . PHE A  1 26  ? 20.381  -10.509 31.906   1.00 205.51 ? 26   PHE A N   1 
ATOM   196   C  CA  . PHE A  1 26  ? 21.376  -10.729 30.865   1.00 209.85 ? 26   PHE A CA  1 
ATOM   197   C  C   . PHE A  1 26  ? 22.635  -11.289 31.506   1.00 215.51 ? 26   PHE A C   1 
ATOM   198   O  O   . PHE A  1 26  ? 23.249  -10.628 32.348   1.00 224.41 ? 26   PHE A O   1 
ATOM   199   C  CB  . PHE A  1 26  ? 21.682  -9.437  30.110   1.00 211.53 ? 26   PHE A CB  1 
ATOM   200   C  CG  . PHE A  1 26  ? 22.533  -9.633  28.893   1.00 215.59 ? 26   PHE A CG  1 
ATOM   201   C  CD1 . PHE A  1 26  ? 22.480  -10.817 28.174   1.00 215.43 ? 26   PHE A CD1 1 
ATOM   202   C  CD2 . PHE A  1 26  ? 23.400  -8.640  28.476   1.00 234.18 ? 26   PHE A CD2 1 
ATOM   203   C  CE1 . PHE A  1 26  ? 23.271  -10.997 27.050   1.00 219.61 ? 26   PHE A CE1 1 
ATOM   204   C  CE2 . PHE A  1 26  ? 24.195  -8.813  27.358   1.00 233.92 ? 26   PHE A CE2 1 
ATOM   205   C  CZ  . PHE A  1 26  ? 24.130  -9.993  26.644   1.00 227.97 ? 26   PHE A CZ  1 
ATOM   206   N  N   . VAL A  1 27  ? 23.009  -12.507 31.123   1.00 231.79 ? 27   VAL A N   1 
ATOM   207   C  CA  . VAL A  1 27  ? 24.228  -13.139 31.624   1.00 244.52 ? 27   VAL A CA  1 
ATOM   208   C  C   . VAL A  1 27  ? 25.052  -13.629 30.435   1.00 245.83 ? 27   VAL A C   1 
ATOM   209   O  O   . VAL A  1 27  ? 24.848  -14.752 29.950   1.00 250.50 ? 27   VAL A O   1 
ATOM   210   C  CB  . VAL A  1 27  ? 23.897  -14.259 32.625   1.00 243.54 ? 27   VAL A CB  1 
ATOM   211   C  CG1 . VAL A  1 27  ? 22.739  -15.129 32.125   1.00 216.75 ? 27   VAL A CG1 1 
ATOM   212   C  CG2 . VAL A  1 27  ? 25.136  -15.099 32.952   1.00 265.30 ? 27   VAL A CG2 1 
ATOM   213   N  N   . PRO A  1 28  ? 25.980  -12.813 29.915   1.00 235.48 ? 28   PRO A N   1 
ATOM   214   C  CA  . PRO A  1 28  ? 26.753  -13.227 28.736   1.00 239.97 ? 28   PRO A CA  1 
ATOM   215   C  C   . PRO A  1 28  ? 27.890  -14.194 29.034   1.00 250.62 ? 28   PRO A C   1 
ATOM   216   O  O   . PRO A  1 28  ? 27.932  -14.845 30.084   1.00 246.50 ? 28   PRO A O   1 
ATOM   217   C  CB  . PRO A  1 28  ? 27.287  -11.896 28.194   1.00 260.48 ? 28   PRO A CB  1 
ATOM   218   C  CG  . PRO A  1 28  ? 27.413  -11.044 29.397   1.00 263.31 ? 28   PRO A CG  1 
ATOM   219   C  CD  . PRO A  1 28  ? 26.260  -11.419 30.293   1.00 236.61 ? 28   PRO A CD  1 
ATOM   220   N  N   . SER A  1 29  ? 28.811  -14.281 28.074   1.00 258.67 ? 29   SER A N   1 
ATOM   221   C  CA  . SER A  1 29  ? 29.862  -15.293 28.072   1.00 261.58 ? 29   SER A CA  1 
ATOM   222   C  C   . SER A  1 29  ? 30.757  -15.213 29.304   1.00 289.26 ? 29   SER A C   1 
ATOM   223   O  O   . SER A  1 29  ? 31.058  -14.127 29.807   1.00 292.65 ? 29   SER A O   1 
ATOM   224   C  CB  . SER A  1 29  ? 30.699  -15.145 26.803   1.00 267.04 ? 29   SER A CB  1 
ATOM   225   O  OG  . SER A  1 29  ? 29.863  -15.175 25.658   1.00 263.08 ? 29   SER A OG  1 
ATOM   226   N  N   . ALA A  1 30  ? 31.176  -16.379 29.781   1.00 306.68 ? 30   ALA A N   1 
ATOM   227   C  CA  . ALA A  1 30  ? 32.128  -16.566 30.883   1.00 313.62 ? 30   ALA A CA  1 
ATOM   228   C  C   . ALA A  1 30  ? 31.646  -15.835 32.142   1.00 323.17 ? 30   ALA A C   1 
ATOM   229   O  O   . ALA A  1 30  ? 30.448  -15.590 32.320   1.00 320.99 ? 30   ALA A O   1 
ATOM   230   C  CB  . ALA A  1 30  ? 33.514  -16.165 30.408   1.00 292.91 ? 30   ALA A CB  1 
ATOM   231   N  N   . SER A  1 31  ? 32.582  -15.485 33.030   1.00 320.79 ? 31   SER A N   1 
ATOM   232   C  CA  . SER A  1 31  ? 32.269  -14.792 34.282   1.00 308.45 ? 31   SER A CA  1 
ATOM   233   C  C   . SER A  1 31  ? 32.424  -13.286 34.074   1.00 307.64 ? 31   SER A C   1 
ATOM   234   O  O   . SER A  1 31  ? 33.401  -12.661 34.493   1.00 306.70 ? 31   SER A O   1 
ATOM   235   C  CB  . SER A  1 31  ? 33.156  -15.302 35.411   1.00 298.52 ? 31   SER A CB  1 
ATOM   236   O  OG  . SER A  1 31  ? 34.532  -15.194 35.081   1.00 296.26 ? 31   SER A OG  1 
ATOM   237   N  N   . SER A  1 32  ? 31.431  -12.700 33.406   1.00 295.17 ? 32   SER A N   1 
ATOM   238   C  CA  . SER A  1 32  ? 31.433  -11.278 33.103   1.00 285.88 ? 32   SER A CA  1 
ATOM   239   C  C   . SER A  1 32  ? 30.481  -10.533 34.041   1.00 255.94 ? 32   SER A C   1 
ATOM   240   O  O   . SER A  1 32  ? 30.014  -11.080 35.048   1.00 253.57 ? 32   SER A O   1 
ATOM   241   C  CB  . SER A  1 32  ? 31.065  -11.071 31.627   1.00 275.32 ? 32   SER A CB  1 
ATOM   242   O  OG  . SER A  1 32  ? 31.951  -11.771 30.773   1.00 283.89 ? 32   SER A OG  1 
ATOM   243   N  N   . ARG A  1 33  ? 30.173  -9.287  33.703   1.00 254.29 ? 33   ARG A N   1 
ATOM   244   C  CA  . ARG A  1 33  ? 29.204  -8.507  34.445   1.00 249.35 ? 33   ARG A CA  1 
ATOM   245   C  C   . ARG A  1 33  ? 27.796  -8.919  34.034   1.00 246.30 ? 33   ARG A C   1 
ATOM   246   O  O   . ARG A  1 33  ? 27.594  -9.650  33.061   1.00 261.11 ? 33   ARG A O   1 
ATOM   247   C  CB  . ARG A  1 33  ? 29.441  -7.013  34.217   1.00 251.17 ? 33   ARG A CB  1 
ATOM   248   C  CG  . ARG A  1 33  ? 30.724  -6.493  34.865   1.00 260.46 ? 33   ARG A CG  1 
ATOM   249   C  CD  . ARG A  1 33  ? 31.104  -5.091  34.397   1.00 261.50 ? 33   ARG A CD  1 
ATOM   250   N  NE  . ARG A  1 33  ? 31.299  -5.011  32.951   1.00 262.29 ? 33   ARG A NE  1 
ATOM   251   C  CZ  . ARG A  1 33  ? 30.470  -4.396  32.115   1.00 266.60 ? 33   ARG A CZ  1 
ATOM   252   N  NH1 . ARG A  1 33  ? 29.384  -3.792  32.578   1.00 270.57 ? 33   ARG A NH1 1 
ATOM   253   N  NH2 . ARG A  1 33  ? 30.736  -4.373  30.815   1.00 262.97 ? 33   ARG A NH2 1 
ATOM   254   N  N   . MET A  1 34  ? 26.814  -8.455  34.802   1.00 248.06 ? 34   MET A N   1 
ATOM   255   C  CA  . MET A  1 34  ? 25.415  -8.779  34.579   1.00 231.22 ? 34   MET A CA  1 
ATOM   256   C  C   . MET A  1 34  ? 24.637  -7.500  34.290   1.00 232.97 ? 34   MET A C   1 
ATOM   257   O  O   . MET A  1 34  ? 25.025  -6.409  34.715   1.00 241.00 ? 34   MET A O   1 
ATOM   258   C  CB  . MET A  1 34  ? 24.823  -9.496  35.798   1.00 240.57 ? 34   MET A CB  1 
ATOM   259   C  CG  . MET A  1 34  ? 25.471  -10.836 36.126   1.00 240.93 ? 34   MET A CG  1 
ATOM   260   S  SD  . MET A  1 34  ? 24.443  -12.253 35.692   1.00 266.01 ? 34   MET A SD  1 
ATOM   261   C  CE  . MET A  1 34  ? 25.425  -13.593 36.362   1.00 258.99 ? 34   MET A CE  1 
ATOM   262   N  N   . PHE A  1 35  ? 23.522  -7.637  33.570   1.00 220.91 ? 35   PHE A N   1 
ATOM   263   C  CA  . PHE A  1 35  ? 22.767  -6.477  33.116   1.00 218.01 ? 35   PHE A CA  1 
ATOM   264   C  C   . PHE A  1 35  ? 21.274  -6.718  33.276   1.00 211.25 ? 35   PHE A C   1 
ATOM   265   O  O   . PHE A  1 35  ? 20.816  -7.854  33.410   1.00 208.62 ? 35   PHE A O   1 
ATOM   266   C  CB  . PHE A  1 35  ? 23.064  -6.143  31.650   1.00 221.35 ? 35   PHE A CB  1 
ATOM   267   C  CG  . PHE A  1 35  ? 24.509  -5.824  31.377   1.00 232.09 ? 35   PHE A CG  1 
ATOM   268   C  CD1 . PHE A  1 35  ? 24.994  -4.536  31.544   1.00 230.70 ? 35   PHE A CD1 1 
ATOM   269   C  CD2 . PHE A  1 35  ? 25.380  -6.811  30.942   1.00 229.90 ? 35   PHE A CD2 1 
ATOM   270   C  CE1 . PHE A  1 35  ? 26.320  -4.240  31.286   1.00 236.34 ? 35   PHE A CE1 1 
ATOM   271   C  CE2 . PHE A  1 35  ? 26.702  -6.520  30.683   1.00 236.67 ? 35   PHE A CE2 1 
ATOM   272   C  CZ  . PHE A  1 35  ? 27.172  -5.234  30.855   1.00 239.85 ? 35   PHE A CZ  1 
ATOM   273   N  N   . LEU A  1 36  ? 20.520  -5.620  33.247   1.00 208.83 ? 36   LEU A N   1 
ATOM   274   C  CA  . LEU A  1 36  ? 19.063  -5.646  33.214   1.00 202.77 ? 36   LEU A CA  1 
ATOM   275   C  C   . LEU A  1 36  ? 18.578  -5.310  31.807   1.00 200.78 ? 36   LEU A C   1 
ATOM   276   O  O   . LEU A  1 36  ? 19.012  -4.317  31.214   1.00 203.35 ? 36   LEU A O   1 
ATOM   277   C  CB  . LEU A  1 36  ? 18.469  -4.657  34.223   1.00 201.70 ? 36   LEU A CB  1 
ATOM   278   C  CG  . LEU A  1 36  ? 18.704  -4.843  35.728   1.00 203.22 ? 36   LEU A CG  1 
ATOM   279   C  CD1 . LEU A  1 36  ? 20.039  -4.259  36.157   1.00 233.40 ? 36   LEU A CD1 1 
ATOM   280   C  CD2 . LEU A  1 36  ? 17.581  -4.191  36.512   1.00 200.07 ? 36   LEU A CD2 1 
ATOM   281   N  N   . LEU A  1 37  ? 17.674  -6.132  31.283   1.00 196.54 ? 37   LEU A N   1 
ATOM   282   C  CA  . LEU A  1 37  ? 17.027  -5.884  30.000   1.00 201.37 ? 37   LEU A CA  1 
ATOM   283   C  C   . LEU A  1 37  ? 15.623  -5.343  30.252   1.00 189.35 ? 37   LEU A C   1 
ATOM   284   O  O   . LEU A  1 37  ? 14.804  -6.013  30.888   1.00 185.87 ? 37   LEU A O   1 
ATOM   285   C  CB  . LEU A  1 37  ? 16.967  -7.164  29.168   1.00 193.02 ? 37   LEU A CB  1 
ATOM   286   C  CG  . LEU A  1 37  ? 18.311  -7.729  28.718   1.00 198.06 ? 37   LEU A CG  1 
ATOM   287   C  CD1 . LEU A  1 37  ? 18.091  -8.974  27.887   1.00 196.84 ? 37   LEU A CD1 1 
ATOM   288   C  CD2 . LEU A  1 37  ? 19.069  -6.685  27.923   1.00 201.94 ? 37   LEU A CD2 1 
ATOM   289   N  N   . VAL A  1 38  ? 15.350  -4.133  29.768   1.00 189.53 ? 38   VAL A N   1 
ATOM   290   C  CA  . VAL A  1 38  ? 14.065  -3.477  29.982   1.00 185.80 ? 38   VAL A CA  1 
ATOM   291   C  C   . VAL A  1 38  ? 13.458  -3.109  28.635   1.00 185.28 ? 38   VAL A C   1 
ATOM   292   O  O   . VAL A  1 38  ? 14.142  -2.550  27.770   1.00 187.29 ? 38   VAL A O   1 
ATOM   293   C  CB  . VAL A  1 38  ? 14.205  -2.230  30.869   1.00 187.92 ? 38   VAL A CB  1 
ATOM   294   C  CG1 . VAL A  1 38  ? 12.834  -1.666  31.173   1.00 201.66 ? 38   VAL A CG1 1 
ATOM   295   C  CG2 . VAL A  1 38  ? 14.952  -2.567  32.150   1.00 190.33 ? 38   VAL A CG2 1 
ATOM   296   N  N   . GLY A  1 39  ? 12.171  -3.410  28.469   1.00 195.66 ? 39   GLY A N   1 
ATOM   297   C  CA  . GLY A  1 39  ? 11.446  -3.046  27.261   1.00 178.05 ? 39   GLY A CA  1 
ATOM   298   C  C   . GLY A  1 39  ? 10.728  -1.711  27.401   1.00 177.62 ? 39   GLY A C   1 
ATOM   299   O  O   . GLY A  1 39  ? 10.162  -1.399  28.448   1.00 176.33 ? 39   GLY A O   1 
ATOM   300   N  N   . ALA A  1 40  ? 10.798  -0.908  26.340   1.00 179.20 ? 40   ALA A N   1 
ATOM   301   C  CA  . ALA A  1 40  ? 10.050  0.345   26.227   1.00 179.03 ? 40   ALA A CA  1 
ATOM   302   C  C   . ALA A  1 40  ? 9.381   0.361   24.858   1.00 177.60 ? 40   ALA A C   1 
ATOM   303   O  O   . ALA A  1 40  ? 9.920   0.930   23.896   1.00 180.46 ? 40   ALA A O   1 
ATOM   304   C  CB  . ALA A  1 40  ? 10.953  1.562   26.428   1.00 183.68 ? 40   ALA A CB  1 
ATOM   305   N  N   . PRO A  1 41  ? 8.200   -0.258  24.733   1.00 173.47 ? 41   PRO A N   1 
ATOM   306   C  CA  . PRO A  1 41  ? 7.611   -0.465  23.398   1.00 172.23 ? 41   PRO A CA  1 
ATOM   307   C  C   . PRO A  1 41  ? 7.088   0.798   22.728   1.00 173.33 ? 41   PRO A C   1 
ATOM   308   O  O   . PRO A  1 41  ? 6.893   0.789   21.507   1.00 173.61 ? 41   PRO A O   1 
ATOM   309   C  CB  . PRO A  1 41  ? 6.482   -1.466  23.668   1.00 167.77 ? 41   PRO A CB  1 
ATOM   310   C  CG  . PRO A  1 41  ? 6.126   -1.239  25.087   1.00 166.65 ? 41   PRO A CG  1 
ATOM   311   C  CD  . PRO A  1 41  ? 7.390   -0.879  25.796   1.00 170.07 ? 41   PRO A CD  1 
ATOM   312   N  N   . LYS A  1 42  ? 6.829   1.874   23.469   1.00 174.23 ? 42   LYS A N   1 
ATOM   313   C  CA  . LYS A  1 42  ? 6.360   3.118   22.876   1.00 175.82 ? 42   LYS A CA  1 
ATOM   314   C  C   . LYS A  1 42  ? 7.467   4.156   22.748   1.00 180.68 ? 42   LYS A C   1 
ATOM   315   O  O   . LYS A  1 42  ? 7.175   5.343   22.565   1.00 182.67 ? 42   LYS A O   1 
ATOM   316   C  CB  . LYS A  1 42  ? 5.190   3.683   23.683   1.00 174.00 ? 42   LYS A CB  1 
ATOM   317   C  CG  . LYS A  1 42  ? 3.855   3.042   23.345   1.00 170.01 ? 42   LYS A CG  1 
ATOM   318   C  CD  . LYS A  1 42  ? 2.688   3.844   23.886   1.00 169.27 ? 42   LYS A CD  1 
ATOM   319   C  CE  . LYS A  1 42  ? 1.380   3.362   23.280   1.00 178.08 ? 42   LYS A CE  1 
ATOM   320   N  NZ  . LYS A  1 42  ? 0.201   4.141   23.753   1.00 191.44 ? 42   LYS A NZ  1 
ATOM   321   N  N   . ALA A  1 43  ? 8.728   3.735   22.839   1.00 207.63 ? 43   ALA A N   1 
ATOM   322   C  CA  . ALA A  1 43  ? 9.854   4.663   22.853   1.00 202.63 ? 43   ALA A CA  1 
ATOM   323   C  C   . ALA A  1 43  ? 10.225  5.128   21.447   1.00 202.61 ? 43   ALA A C   1 
ATOM   324   O  O   . ALA A  1 43  ? 10.419  4.312   20.540   1.00 190.26 ? 43   ALA A O   1 
ATOM   325   C  CB  . ALA A  1 43  ? 11.061  4.008   23.521   1.00 189.65 ? 43   ALA A CB  1 
ATOM   326   N  N   . ASN A  1 44  ? 10.371  6.441   21.286   1.00 194.24 ? 44   ASN A N   1 
ATOM   327   C  CA  . ASN A  1 44  ? 10.883  6.995   20.043   1.00 197.88 ? 44   ASN A CA  1 
ATOM   328   C  C   . ASN A  1 44  ? 12.335  6.586   19.846   1.00 201.40 ? 44   ASN A C   1 
ATOM   329   O  O   . ASN A  1 44  ? 13.132  6.594   20.788   1.00 203.17 ? 44   ASN A O   1 
ATOM   330   C  CB  . ASN A  1 44  ? 10.762  8.520   20.048   1.00 201.27 ? 44   ASN A CB  1 
ATOM   331   C  CG  . ASN A  1 44  ? 9.387   9.002   19.626   1.00 204.54 ? 44   ASN A CG  1 
ATOM   332   O  OD1 . ASN A  1 44  ? 8.839   8.533   18.630   1.00 198.58 ? 44   ASN A OD1 1 
ATOM   333   N  ND2 . ASN A  1 44  ? 8.819   9.943   20.382   1.00 274.51 ? 44   ASN A ND2 1 
ATOM   334   N  N   . THR A  1 45  ? 12.671  6.196   18.622   1.00 218.55 ? 45   THR A N   1 
ATOM   335   C  CA  . THR A  1 45  ? 14.032  5.818   18.266   1.00 216.18 ? 45   THR A CA  1 
ATOM   336   C  C   . THR A  1 45  ? 14.559  6.758   17.186   1.00 212.36 ? 45   THR A C   1 
ATOM   337   O  O   . THR A  1 45  ? 13.873  7.678   16.736   1.00 225.08 ? 45   THR A O   1 
ATOM   338   C  CB  . THR A  1 45  ? 14.094  4.362   17.795   1.00 213.01 ? 45   THR A CB  1 
ATOM   339   O  OG1 . THR A  1 45  ? 13.398  4.228   16.550   1.00 213.65 ? 45   THR A OG1 1 
ATOM   340   C  CG2 . THR A  1 45  ? 13.455  3.442   18.823   1.00 211.11 ? 45   THR A CG2 1 
ATOM   341   N  N   . THR A  1 46  ? 15.795  6.509   16.764   1.00 219.39 ? 46   THR A N   1 
ATOM   342   C  CA  . THR A  1 46  ? 16.437  7.314   15.734   1.00 238.51 ? 46   THR A CA  1 
ATOM   343   C  C   . THR A  1 46  ? 16.167  6.786   14.334   1.00 236.32 ? 46   THR A C   1 
ATOM   344   O  O   . THR A  1 46  ? 16.709  7.326   13.366   1.00 248.53 ? 46   THR A O   1 
ATOM   345   C  CB  . THR A  1 46  ? 17.949  7.379   15.975   1.00 235.89 ? 46   THR A CB  1 
ATOM   346   O  OG1 . THR A  1 46  ? 18.493  6.055   15.947   1.00 226.08 ? 46   THR A OG1 1 
ATOM   347   C  CG2 . THR A  1 46  ? 18.249  8.010   17.324   1.00 227.67 ? 46   THR A CG2 1 
ATOM   348   N  N   . GLN A  1 47  ? 15.351  5.746   14.215   1.00 223.47 ? 47   GLN A N   1 
ATOM   349   C  CA  . GLN A  1 47  ? 15.057  5.147   12.922   1.00 225.37 ? 47   GLN A CA  1 
ATOM   350   C  C   . GLN A  1 47  ? 14.411  6.161   11.980   1.00 231.38 ? 47   GLN A C   1 
ATOM   351   O  O   . GLN A  1 47  ? 13.468  6.859   12.378   1.00 234.05 ? 47   GLN A O   1 
ATOM   352   C  CB  . GLN A  1 47  ? 14.147  3.939   13.110   1.00 221.82 ? 47   GLN A CB  1 
ATOM   353   C  CG  . GLN A  1 47  ? 14.828  2.763   13.786   1.00 223.01 ? 47   GLN A CG  1 
ATOM   354   C  CD  . GLN A  1 47  ? 13.840  1.762   14.344   1.00 215.81 ? 47   GLN A CD  1 
ATOM   355   O  OE1 . GLN A  1 47  ? 12.647  2.044   14.448   1.00 216.61 ? 47   GLN A OE1 1 
ATOM   356   N  NE2 . GLN A  1 47  ? 14.330  0.581   14.699   1.00 212.14 ? 47   GLN A NE2 1 
ATOM   357   N  N   . PRO A  1 48  ? 14.892  6.277   10.741   1.00 221.17 ? 48   PRO A N   1 
ATOM   358   C  CA  . PRO A  1 48  ? 14.379  7.301   9.816    1.00 224.28 ? 48   PRO A CA  1 
ATOM   359   C  C   . PRO A  1 48  ? 12.903  7.103   9.513    1.00 232.68 ? 48   PRO A C   1 
ATOM   360   O  O   . PRO A  1 48  ? 12.486  6.058   9.010    1.00 226.62 ? 48   PRO A O   1 
ATOM   361   C  CB  . PRO A  1 48  ? 15.241  7.108   8.563    1.00 228.31 ? 48   PRO A CB  1 
ATOM   362   C  CG  . PRO A  1 48  ? 16.458  6.378   9.030    1.00 236.95 ? 48   PRO A CG  1 
ATOM   363   C  CD  . PRO A  1 48  ? 15.979  5.488   10.138   1.00 224.64 ? 48   PRO A CD  1 
ATOM   364   N  N   . GLY A  1 49  ? 12.106  8.119   9.837    1.00 238.72 ? 49   GLY A N   1 
ATOM   365   C  CA  . GLY A  1 49  ? 10.695  8.105   9.526    1.00 225.26 ? 49   GLY A CA  1 
ATOM   366   C  C   . GLY A  1 49  ? 9.860   7.217   10.412   1.00 208.32 ? 49   GLY A C   1 
ATOM   367   O  O   . GLY A  1 49  ? 8.642   7.133   10.206   1.00 209.31 ? 49   GLY A O   1 
ATOM   368   N  N   . ILE A  1 50  ? 10.468  6.549   11.384   1.00 208.75 ? 50   ILE A N   1 
ATOM   369   C  CA  . ILE A  1 50  ? 9.774   5.612   12.256   1.00 210.97 ? 50   ILE A CA  1 
ATOM   370   C  C   . ILE A  1 50  ? 9.417   6.335   13.549   1.00 218.24 ? 50   ILE A C   1 
ATOM   371   O  O   . ILE A  1 50  ? 10.302  6.739   14.312   1.00 222.18 ? 50   ILE A O   1 
ATOM   372   C  CB  . ILE A  1 50  ? 10.624  4.365   12.518   1.00 210.29 ? 50   ILE A CB  1 
ATOM   373   C  CG1 . ILE A  1 50  ? 10.979  3.695   11.189   1.00 202.66 ? 50   ILE A CG1 1 
ATOM   374   C  CG2 . ILE A  1 50  ? 9.884   3.408   13.439   1.00 214.05 ? 50   ILE A CG2 1 
ATOM   375   C  CD1 . ILE A  1 50  ? 11.618  2.343   11.339   1.00 202.09 ? 50   ILE A CD1 1 
ATOM   376   N  N   . VAL A  1 51  ? 8.119   6.512   13.791   1.00 204.25 ? 51   VAL A N   1 
ATOM   377   C  CA  . VAL A  1 51  ? 7.628   7.153   15.008   1.00 203.22 ? 51   VAL A CA  1 
ATOM   378   C  C   . VAL A  1 51  ? 7.285   6.078   16.035   1.00 193.14 ? 51   VAL A C   1 
ATOM   379   O  O   . VAL A  1 51  ? 6.478   5.181   15.766   1.00 186.51 ? 51   VAL A O   1 
ATOM   380   C  CB  . VAL A  1 51  ? 6.419   8.058   14.718   1.00 217.25 ? 51   VAL A CB  1 
ATOM   381   C  CG1 . VAL A  1 51  ? 5.466   7.403   13.731   1.00 220.27 ? 51   VAL A CG1 1 
ATOM   382   C  CG2 . VAL A  1 51  ? 5.692   8.414   16.014   1.00 214.96 ? 51   VAL A CG2 1 
ATOM   383   N  N   . GLU A  1 52  ? 7.908   6.168   17.210   1.00 190.54 ? 52   GLU A N   1 
ATOM   384   C  CA  . GLU A  1 52  ? 7.670   5.246   18.322   1.00 186.77 ? 52   GLU A CA  1 
ATOM   385   C  C   . GLU A  1 52  ? 7.877   3.795   17.900   1.00 186.77 ? 52   GLU A C   1 
ATOM   386   O  O   . GLU A  1 52  ? 7.012   2.936   18.090   1.00 180.67 ? 52   GLU A O   1 
ATOM   387   C  CB  . GLU A  1 52  ? 6.280   5.443   18.919   1.00 183.30 ? 52   GLU A CB  1 
ATOM   388   C  CG  . GLU A  1 52  ? 6.118   6.746   19.661   1.00 185.35 ? 52   GLU A CG  1 
ATOM   389   C  CD  . GLU A  1 52  ? 4.808   6.814   20.410   1.00 219.70 ? 52   GLU A CD  1 
ATOM   390   O  OE1 . GLU A  1 52  ? 4.654   7.722   21.253   1.00 222.33 ? 52   GLU A OE1 1 
ATOM   391   O  OE2 . GLU A  1 52  ? 3.935   5.956   20.161   1.00 232.89 ? 52   GLU A OE2 1 
ATOM   392   N  N   . GLY A  1 53  ? 9.041   3.529   17.301   1.00 193.48 ? 53   GLY A N   1 
ATOM   393   C  CA  . GLY A  1 53  ? 9.388   2.164   16.946   1.00 187.92 ? 53   GLY A CA  1 
ATOM   394   C  C   . GLY A  1 53  ? 9.588   1.272   18.155   1.00 189.57 ? 53   GLY A C   1 
ATOM   395   O  O   . GLY A  1 53  ? 9.346   0.063   18.084   1.00 182.01 ? 53   GLY A O   1 
ATOM   396   N  N   . GLY A  1 54  ? 10.019  1.846   19.272   1.00 200.56 ? 54   GLY A N   1 
ATOM   397   C  CA  . GLY A  1 54  ? 10.293  1.087   20.473   1.00 184.02 ? 54   GLY A CA  1 
ATOM   398   C  C   . GLY A  1 54  ? 11.722  0.577   20.516   1.00 187.46 ? 54   GLY A C   1 
ATOM   399   O  O   . GLY A  1 54  ? 12.390  0.414   19.497   1.00 190.25 ? 54   GLY A O   1 
ATOM   400   N  N   . GLN A  1 55  ? 12.197  0.323   21.733   1.00 187.59 ? 55   GLN A N   1 
ATOM   401   C  CA  . GLN A  1 55  ? 13.551  -0.181  21.898   1.00 191.12 ? 55   GLN A CA  1 
ATOM   402   C  C   . GLN A  1 55  ? 13.674  -0.997  23.175   1.00 189.52 ? 55   GLN A C   1 
ATOM   403   O  O   . GLN A  1 55  ? 12.820  -0.946  24.064   1.00 186.27 ? 55   GLN A O   1 
ATOM   404   C  CB  . GLN A  1 55  ? 14.584  0.953   21.916   1.00 204.54 ? 55   GLN A CB  1 
ATOM   405   C  CG  . GLN A  1 55  ? 14.339  2.034   22.961   1.00 196.86 ? 55   GLN A CG  1 
ATOM   406   C  CD  . GLN A  1 55  ? 15.308  3.200   22.824   1.00 211.93 ? 55   GLN A CD  1 
ATOM   407   O  OE1 . GLN A  1 55  ? 16.125  3.236   21.904   1.00 205.62 ? 55   GLN A OE1 1 
ATOM   408   N  NE2 . GLN A  1 55  ? 15.226  4.154   23.745   1.00 213.23 ? 55   GLN A NE2 1 
ATOM   409   N  N   . VAL A  1 56  ? 14.766  -1.754  23.248   1.00 212.67 ? 56   VAL A N   1 
ATOM   410   C  CA  . VAL A  1 56  ? 15.150  -2.506  24.436   1.00 207.77 ? 56   VAL A CA  1 
ATOM   411   C  C   . VAL A  1 56  ? 16.487  -1.959  24.925   1.00 206.50 ? 56   VAL A C   1 
ATOM   412   O  O   . VAL A  1 56  ? 17.456  -1.897  24.159   1.00 201.43 ? 56   VAL A O   1 
ATOM   413   C  CB  . VAL A  1 56  ? 15.234  -4.015  24.141   1.00 206.20 ? 56   VAL A CB  1 
ATOM   414   C  CG1 . VAL A  1 56  ? 15.727  -4.773  25.360   1.00 214.89 ? 56   VAL A CG1 1 
ATOM   415   C  CG2 . VAL A  1 56  ? 13.881  -4.537  23.684   1.00 185.88 ? 56   VAL A CG2 1 
ATOM   416   N  N   . LEU A  1 57  ? 16.537  -1.560  26.194   1.00 197.45 ? 57   LEU A N   1 
ATOM   417   C  CA  . LEU A  1 57  ? 17.706  -0.902  26.759   1.00 202.55 ? 57   LEU A CA  1 
ATOM   418   C  C   . LEU A  1 57  ? 18.500  -1.858  27.637   1.00 204.19 ? 57   LEU A C   1 
ATOM   419   O  O   . LEU A  1 57  ? 17.931  -2.678  28.365   1.00 200.86 ? 57   LEU A O   1 
ATOM   420   C  CB  . LEU A  1 57  ? 17.316  0.330   27.578   1.00 202.67 ? 57   LEU A CB  1 
ATOM   421   C  CG  . LEU A  1 57  ? 16.802  1.546   26.811   1.00 202.86 ? 57   LEU A CG  1 
ATOM   422   C  CD1 . LEU A  1 57  ? 15.293  1.448   26.607   1.00 210.44 ? 57   LEU A CD1 1 
ATOM   423   C  CD2 . LEU A  1 57  ? 17.169  2.823   27.545   1.00 206.34 ? 57   LEU A CD2 1 
ATOM   424   N  N   . LYS A  1 58  ? 19.821  -1.733  27.559   1.00 241.97 ? 58   LYS A N   1 
ATOM   425   C  CA  . LYS A  1 58  ? 20.761  -2.471  28.394   1.00 234.04 ? 58   LYS A CA  1 
ATOM   426   C  C   . LYS A  1 58  ? 21.219  -1.537  29.508   1.00 217.75 ? 58   LYS A C   1 
ATOM   427   O  O   . LYS A  1 58  ? 21.918  -0.552  29.251   1.00 225.68 ? 58   LYS A O   1 
ATOM   428   C  CB  . LYS A  1 58  ? 21.939  -2.969  27.557   1.00 217.36 ? 58   LYS A CB  1 
ATOM   429   C  CG  . LYS A  1 58  ? 22.938  -3.838  28.300   1.00 220.82 ? 58   LYS A CG  1 
ATOM   430   C  CD  . LYS A  1 58  ? 24.225  -3.986  27.490   1.00 229.18 ? 58   LYS A CD  1 
ATOM   431   C  CE  . LYS A  1 58  ? 24.904  -2.635  27.272   1.00 231.45 ? 58   LYS A CE  1 
ATOM   432   N  NZ  . LYS A  1 58  ? 26.202  -2.757  26.556   1.00 237.95 ? 58   LYS A NZ  1 
ATOM   433   N  N   . CYS A  1 59  ? 20.812  -1.833  30.739   1.00 218.03 ? 59   CYS A N   1 
ATOM   434   C  CA  . CYS A  1 59  ? 21.163  -1.019  31.893   1.00 221.10 ? 59   CYS A CA  1 
ATOM   435   C  C   . CYS A  1 59  ? 22.238  -1.713  32.721   1.00 224.93 ? 59   CYS A C   1 
ATOM   436   O  O   . CYS A  1 59  ? 22.225  -2.939  32.876   1.00 223.22 ? 59   CYS A O   1 
ATOM   437   C  CB  . CYS A  1 59  ? 19.925  -0.725  32.758   1.00 225.59 ? 59   CYS A CB  1 
ATOM   438   S  SG  . CYS A  1 59  ? 18.577  0.192   31.932   1.00 234.05 ? 59   CYS A SG  1 
ATOM   439   N  N   . ASP A  1 60  ? 23.170  -0.922  33.240   1.00 225.51 ? 60   ASP A N   1 
ATOM   440   C  CA  . ASP A  1 60  ? 24.305  -1.419  34.005   1.00 235.83 ? 60   ASP A CA  1 
ATOM   441   C  C   . ASP A  1 60  ? 24.009  -1.249  35.489   1.00 231.48 ? 60   ASP A C   1 
ATOM   442   O  O   . ASP A  1 60  ? 23.380  -0.267  35.895   1.00 228.72 ? 60   ASP A O   1 
ATOM   443   C  CB  . ASP A  1 60  ? 25.597  -0.678  33.615   1.00 244.01 ? 60   ASP A CB  1 
ATOM   444   C  CG  . ASP A  1 60  ? 26.803  -1.083  34.462   1.00 242.90 ? 60   ASP A CG  1 
ATOM   445   O  OD1 . ASP A  1 60  ? 27.014  -2.297  34.672   1.00 242.57 ? 60   ASP A OD1 1 
ATOM   446   O  OD2 . ASP A  1 60  ? 27.547  -0.182  34.910   1.00 248.03 ? 60   ASP A OD2 1 
ATOM   447   N  N   . TRP A  1 61  ? 24.368  -2.256  36.279   1.00 255.64 ? 61   TRP A N   1 
ATOM   448   C  CA  . TRP A  1 61  ? 24.270  -2.167  37.732   1.00 248.59 ? 61   TRP A CA  1 
ATOM   449   C  C   . TRP A  1 61  ? 25.554  -1.589  38.349   1.00 262.06 ? 61   TRP A C   1 
ATOM   450   O  O   . TRP A  1 61  ? 26.636  -1.648  37.756   1.00 248.18 ? 61   TRP A O   1 
ATOM   451   C  CB  . TRP A  1 61  ? 23.946  -3.539  38.325   1.00 233.63 ? 61   TRP A CB  1 
ATOM   452   C  CG  . TRP A  1 61  ? 24.216  -3.664  39.789   1.00 236.07 ? 61   TRP A CG  1 
ATOM   453   C  CD1 . TRP A  1 61  ? 25.090  -4.524  40.387   1.00 242.93 ? 61   TRP A CD1 1 
ATOM   454   C  CD2 . TRP A  1 61  ? 23.613  -2.905  40.846   1.00 247.49 ? 61   TRP A CD2 1 
ATOM   455   N  NE1 . TRP A  1 61  ? 25.066  -4.353  41.750   1.00 257.17 ? 61   TRP A NE1 1 
ATOM   456   C  CE2 . TRP A  1 61  ? 24.168  -3.365  42.058   1.00 262.33 ? 61   TRP A CE2 1 
ATOM   457   C  CE3 . TRP A  1 61  ? 22.658  -1.883  40.889   1.00 243.07 ? 61   TRP A CE3 1 
ATOM   458   C  CZ2 . TRP A  1 61  ? 23.798  -2.838  43.297   1.00 267.36 ? 61   TRP A CZ2 1 
ATOM   459   C  CZ3 . TRP A  1 61  ? 22.295  -1.361  42.121   1.00 249.45 ? 61   TRP A CZ3 1 
ATOM   460   C  CH2 . TRP A  1 61  ? 22.862  -1.841  43.306   1.00 256.86 ? 61   TRP A CH2 1 
ATOM   461   N  N   . ARG A  1 65  ? 25.755  3.151   36.854   1.00 251.95 ? 65   ARG A N   1 
ATOM   462   C  CA  . ARG A  1 65  ? 24.476  2.457   36.728   1.00 262.51 ? 65   ARG A CA  1 
ATOM   463   C  C   . ARG A  1 65  ? 23.576  3.089   35.662   1.00 257.37 ? 65   ARG A C   1 
ATOM   464   O  O   . ARG A  1 65  ? 22.368  3.241   35.864   1.00 236.20 ? 65   ARG A O   1 
ATOM   465   C  CB  . ARG A  1 65  ? 23.762  2.417   38.085   1.00 251.43 ? 65   ARG A CB  1 
ATOM   466   C  CG  . ARG A  1 65  ? 24.671  1.996   39.233   1.00 246.97 ? 65   ARG A CG  1 
ATOM   467   C  CD  . ARG A  1 65  ? 23.930  1.954   40.556   1.00 246.55 ? 65   ARG A CD  1 
ATOM   468   N  NE  . ARG A  1 65  ? 23.753  3.286   41.121   1.00 254.70 ? 65   ARG A NE  1 
ATOM   469   C  CZ  . ARG A  1 65  ? 23.113  3.534   42.259   1.00 257.77 ? 65   ARG A CZ  1 
ATOM   470   N  NH1 . ARG A  1 65  ? 22.588  2.535   42.957   1.00 253.21 ? 65   ARG A NH1 1 
ATOM   471   N  NH2 . ARG A  1 65  ? 23.000  4.778   42.702   1.00 257.08 ? 65   ARG A NH2 1 
ATOM   472   N  N   . ARG A  1 66  ? 24.175  3.429   34.522   1.00 253.43 ? 66   ARG A N   1 
ATOM   473   C  CA  . ARG A  1 66  ? 23.482  4.078   33.418   1.00 242.60 ? 66   ARG A CA  1 
ATOM   474   C  C   . ARG A  1 66  ? 22.929  3.045   32.437   1.00 240.28 ? 66   ARG A C   1 
ATOM   475   O  O   . ARG A  1 66  ? 23.437  1.925   32.335   1.00 232.41 ? 66   ARG A O   1 
ATOM   476   C  CB  . ARG A  1 66  ? 24.425  5.037   32.684   1.00 242.86 ? 66   ARG A CB  1 
ATOM   477   C  CG  . ARG A  1 66  ? 25.056  6.099   33.573   1.00 248.41 ? 66   ARG A CG  1 
ATOM   478   C  CD  . ARG A  1 66  ? 26.200  6.803   32.856   1.00 269.86 ? 66   ARG A CD  1 
ATOM   479   N  NE  . ARG A  1 66  ? 27.222  5.869   32.382   1.00 273.06 ? 66   ARG A NE  1 
ATOM   480   C  CZ  . ARG A  1 66  ? 28.311  5.530   33.067   1.00 262.59 ? 66   ARG A CZ  1 
ATOM   481   N  NH1 . ARG A  1 66  ? 28.531  6.043   34.270   1.00 269.86 ? 66   ARG A NH1 1 
ATOM   482   N  NH2 . ARG A  1 66  ? 29.182  4.675   32.549   1.00 265.12 ? 66   ARG A NH2 1 
ATOM   483   N  N   . CYS A  1 67  ? 21.878  3.437   31.712   1.00 240.45 ? 67   CYS A N   1 
ATOM   484   C  CA  . CYS A  1 67  ? 21.252  2.602   30.692   1.00 222.10 ? 67   CYS A CA  1 
ATOM   485   C  C   . CYS A  1 67  ? 21.736  2.984   29.293   1.00 224.70 ? 67   CYS A C   1 
ATOM   486   O  O   . CYS A  1 67  ? 21.950  4.164   28.995   1.00 227.83 ? 67   CYS A O   1 
ATOM   487   C  CB  . CYS A  1 67  ? 19.725  2.705   30.758   1.00 231.30 ? 67   CYS A CB  1 
ATOM   488   S  SG  . CYS A  1 67  ? 18.952  2.155   32.314   1.00 248.84 ? 67   CYS A SG  1 
ATOM   489   N  N   . GLN A  1 68  ? 21.887  1.975   28.430   1.00 224.35 ? 68   GLN A N   1 
ATOM   490   C  CA  . GLN A  1 68  ? 22.370  2.143   27.062   1.00 242.89 ? 68   GLN A CA  1 
ATOM   491   C  C   . GLN A  1 68  ? 21.422  1.439   26.095   1.00 222.00 ? 68   GLN A C   1 
ATOM   492   O  O   . GLN A  1 68  ? 21.089  0.259   26.308   1.00 218.74 ? 68   GLN A O   1 
ATOM   493   C  CB  . GLN A  1 68  ? 23.800  1.579   26.925   1.00 253.63 ? 68   GLN A CB  1 
ATOM   494   C  CG  . GLN A  1 68  ? 24.938  2.583   27.135   1.00 239.32 ? 68   GLN A CG  1 
ATOM   495   C  CD  . GLN A  1 68  ? 24.912  3.724   26.136   1.00 241.46 ? 68   GLN A CD  1 
ATOM   496   O  OE1 . GLN A  1 68  ? 24.445  3.568   25.007   1.00 239.45 ? 68   GLN A OE1 1 
ATOM   497   N  NE2 . GLN A  1 68  ? 25.401  4.885   26.553   1.00 253.69 ? 68   GLN A NE2 1 
ATOM   498   N  N   . PRO A  1 69  ? 20.956  2.113   25.040   1.00 225.24 ? 69   PRO A N   1 
ATOM   499   C  CA  . PRO A  1 69  ? 20.084  1.448   24.059   1.00 242.36 ? 69   PRO A CA  1 
ATOM   500   C  C   . PRO A  1 69  ? 20.798  0.330   23.306   1.00 222.82 ? 69   PRO A C   1 
ATOM   501   O  O   . PRO A  1 69  ? 21.976  0.438   22.966   1.00 228.30 ? 69   PRO A O   1 
ATOM   502   C  CB  . PRO A  1 69  ? 19.677  2.587   23.115   1.00 237.86 ? 69   PRO A CB  1 
ATOM   503   C  CG  . PRO A  1 69  ? 19.892  3.842   23.900   1.00 233.49 ? 69   PRO A CG  1 
ATOM   504   C  CD  . PRO A  1 69  ? 21.084  3.557   24.771   1.00 228.39 ? 69   PRO A CD  1 
ATOM   505   N  N   . ILE A  1 70  ? 20.077  -0.766  23.074   1.00 239.67 ? 70   ILE A N   1 
ATOM   506   C  CA  . ILE A  1 70  ? 20.569  -1.871  22.251   1.00 218.84 ? 70   ILE A CA  1 
ATOM   507   C  C   . ILE A  1 70  ? 20.101  -1.668  20.814   1.00 220.69 ? 70   ILE A C   1 
ATOM   508   O  O   . ILE A  1 70  ? 18.895  -1.594  20.553   1.00 218.32 ? 70   ILE A O   1 
ATOM   509   C  CB  . ILE A  1 70  ? 20.094  -3.229  22.789   1.00 217.80 ? 70   ILE A CB  1 
ATOM   510   C  CG1 . ILE A  1 70  ? 20.515  -3.409  24.244   1.00 212.89 ? 70   ILE A CG1 1 
ATOM   511   C  CG2 . ILE A  1 70  ? 20.673  -4.353  21.949   1.00 217.66 ? 70   ILE A CG2 1 
ATOM   512   C  CD1 . ILE A  1 70  ? 20.056  -4.713  24.852   1.00 221.13 ? 70   ILE A CD1 1 
ATOM   513   N  N   . GLU A  1 71  ? 21.053  -1.561  19.884   1.00 229.45 ? 71   GLU A N   1 
ATOM   514   C  CA  . GLU A  1 71  ? 20.763  -1.361  18.461   1.00 235.84 ? 71   GLU A CA  1 
ATOM   515   C  C   . GLU A  1 71  ? 20.344  -2.680  17.820   1.00 236.60 ? 71   GLU A C   1 
ATOM   516   O  O   . GLU A  1 71  ? 21.177  -3.472  17.371   1.00 243.76 ? 71   GLU A O   1 
ATOM   517   C  CB  . GLU A  1 71  ? 21.967  -0.782  17.733   1.00 259.05 ? 71   GLU A CB  1 
ATOM   518   C  CG  . GLU A  1 71  ? 21.675  -0.417  16.283   1.00 260.21 ? 71   GLU A CG  1 
ATOM   519   C  CD  . GLU A  1 71  ? 22.891  0.117   15.556   1.00 267.40 ? 71   GLU A CD  1 
ATOM   520   O  OE1 . GLU A  1 71  ? 23.983  0.139   16.164   1.00 249.13 ? 71   GLU A OE1 1 
ATOM   521   O  OE2 . GLU A  1 71  ? 22.756  0.501   14.374   1.00 269.99 ? 71   GLU A OE2 1 
ATOM   522   N  N   . PHE A  1 72  ? 19.032  -2.921  17.765   1.00 236.31 ? 72   PHE A N   1 
ATOM   523   C  CA  . PHE A  1 72  ? 18.502  -4.077  17.051   1.00 234.05 ? 72   PHE A CA  1 
ATOM   524   C  C   . PHE A  1 72  ? 18.301  -3.784  15.569   1.00 217.83 ? 72   PHE A C   1 
ATOM   525   O  O   . PHE A  1 72  ? 18.570  -4.644  14.722   1.00 219.66 ? 72   PHE A O   1 
ATOM   526   C  CB  . PHE A  1 72  ? 17.178  -4.526  17.677   1.00 209.77 ? 72   PHE A CB  1 
ATOM   527   C  CG  . PHE A  1 72  ? 17.343  -5.252  18.981   1.00 213.28 ? 72   PHE A CG  1 
ATOM   528   C  CD1 . PHE A  1 72  ? 17.591  -6.616  19.002   1.00 211.62 ? 72   PHE A CD1 1 
ATOM   529   C  CD2 . PHE A  1 72  ? 17.255  -4.573  20.184   1.00 210.51 ? 72   PHE A CD2 1 
ATOM   530   C  CE1 . PHE A  1 72  ? 17.747  -7.288  20.199   1.00 207.39 ? 72   PHE A CE1 1 
ATOM   531   C  CE2 . PHE A  1 72  ? 17.406  -5.241  21.386   1.00 206.00 ? 72   PHE A CE2 1 
ATOM   532   C  CZ  . PHE A  1 72  ? 17.656  -6.600  21.393   1.00 206.13 ? 72   PHE A CZ  1 
ATOM   533   N  N   . ASP A  1 73  ? 17.840  -2.578  15.245   1.00 218.79 ? 73   ASP A N   1 
ATOM   534   C  CA  . ASP A  1 73  ? 17.572  -2.200  13.860   1.00 224.46 ? 73   ASP A CA  1 
ATOM   535   C  C   . ASP A  1 73  ? 17.628  -0.685  13.751   1.00 231.30 ? 73   ASP A C   1 
ATOM   536   O  O   . ASP A  1 73  ? 16.908  0.012   14.474   1.00 233.76 ? 73   ASP A O   1 
ATOM   537   C  CB  . ASP A  1 73  ? 16.208  -2.731  13.411   1.00 225.40 ? 73   ASP A CB  1 
ATOM   538   C  CG  . ASP A  1 73  ? 15.805  -2.221  12.039   1.00 232.08 ? 73   ASP A CG  1 
ATOM   539   O  OD1 . ASP A  1 73  ? 16.676  -2.171  11.144   1.00 235.86 ? 73   ASP A OD1 1 
ATOM   540   O  OD2 . ASP A  1 73  ? 14.618  -1.871  11.854   1.00 239.61 ? 73   ASP A OD2 1 
ATOM   541   N  N   . ALA A  1 74  ? 18.482  -0.175  12.862   1.00 237.42 ? 74   ALA A N   1 
ATOM   542   C  CA  . ALA A  1 74  ? 18.616  1.260   12.637   1.00 245.48 ? 74   ALA A CA  1 
ATOM   543   C  C   . ALA A  1 74  ? 17.900  1.739   11.382   1.00 245.21 ? 74   ALA A C   1 
ATOM   544   O  O   . ALA A  1 74  ? 17.804  2.952   11.165   1.00 247.92 ? 74   ALA A O   1 
ATOM   545   C  CB  . ALA A  1 74  ? 20.099  1.649   12.553   1.00 253.13 ? 74   ALA A CB  1 
ATOM   546   N  N   . THR A  1 75  ? 17.419  0.825   10.547   1.00 239.44 ? 75   THR A N   1 
ATOM   547   C  CA  . THR A  1 75  ? 16.815  1.176   9.272    1.00 235.54 ? 75   THR A CA  1 
ATOM   548   C  C   . THR A  1 75  ? 15.351  1.578   9.441    1.00 227.41 ? 75   THR A C   1 
ATOM   549   O  O   . THR A  1 75  ? 14.702  1.286   10.448   1.00 228.67 ? 75   THR A O   1 
ATOM   550   C  CB  . THR A  1 75  ? 16.925  0.012   8.286    1.00 241.00 ? 75   THR A CB  1 
ATOM   551   O  OG1 . THR A  1 75  ? 16.040  -1.047  8.683    1.00 232.76 ? 75   THR A OG1 1 
ATOM   552   C  CG2 . THR A  1 75  ? 18.353  -0.515  8.249    1.00 260.45 ? 75   THR A CG2 1 
ATOM   553   N  N   . GLY A  1 76  ? 14.838  2.263   8.427    1.00 218.56 ? 76   GLY A N   1 
ATOM   554   C  CA  . GLY A  1 76  ? 13.442  2.643   8.356    1.00 220.78 ? 76   GLY A CA  1 
ATOM   555   C  C   . GLY A  1 76  ? 12.588  1.574   7.709    1.00 222.90 ? 76   GLY A C   1 
ATOM   556   O  O   . GLY A  1 76  ? 12.869  0.376   7.804    1.00 227.32 ? 76   GLY A O   1 
ATOM   557   N  N   . ASN A  1 77  ? 11.518  2.014   7.049    1.00 211.66 ? 77   ASN A N   1 
ATOM   558   C  CA  . ASN A  1 77  ? 10.604  1.107   6.361    1.00 214.81 ? 77   ASN A CA  1 
ATOM   559   C  C   . ASN A  1 77  ? 11.160  0.727   4.992    1.00 223.29 ? 77   ASN A C   1 
ATOM   560   O  O   . ASN A  1 77  ? 11.362  1.595   4.135    1.00 235.56 ? 77   ASN A O   1 
ATOM   561   C  CB  . ASN A  1 77  ? 9.228   1.751   6.211    1.00 221.32 ? 77   ASN A CB  1 
ATOM   562   C  CG  . ASN A  1 77  ? 8.546   1.992   7.543    1.00 218.79 ? 77   ASN A CG  1 
ATOM   563   O  OD1 . ASN A  1 77  ? 9.186   1.972   8.595    1.00 224.32 ? 77   ASN A OD1 1 
ATOM   564   N  ND2 . ASN A  1 77  ? 7.238   2.215   7.505    1.00 210.51 ? 77   ASN A ND2 1 
ATOM   565   N  N   . ARG A  1 78  ? 11.396  -0.566  4.780    1.00 223.62 ? 78   ARG A N   1 
ATOM   566   C  CA  . ARG A  1 78  ? 11.790  -1.039  3.460    1.00 240.12 ? 78   ARG A CA  1 
ATOM   567   C  C   . ARG A  1 78  ? 10.662  -0.827  2.456    1.00 245.45 ? 78   ARG A C   1 
ATOM   568   O  O   . ARG A  1 78  ? 9.477   -0.883  2.795    1.00 238.87 ? 78   ARG A O   1 
ATOM   569   C  CB  . ARG A  1 78  ? 12.181  -2.518  3.510    1.00 243.35 ? 78   ARG A CB  1 
ATOM   570   C  CG  . ARG A  1 78  ? 13.574  -2.779  4.075    1.00 245.34 ? 78   ARG A CG  1 
ATOM   571   C  CD  . ARG A  1 78  ? 13.827  -4.265  4.299    1.00 243.20 ? 78   ARG A CD  1 
ATOM   572   N  NE  . ARG A  1 78  ? 12.915  -4.843  5.282    1.00 242.55 ? 78   ARG A NE  1 
ATOM   573   C  CZ  . ARG A  1 78  ? 13.006  -6.083  5.753    1.00 234.05 ? 78   ARG A CZ  1 
ATOM   574   N  NH1 . ARG A  1 78  ? 13.971  -6.891  5.330    1.00 231.47 ? 78   ARG A NH1 1 
ATOM   575   N  NH2 . ARG A  1 78  ? 12.130  -6.519  6.648    1.00 234.76 ? 78   ARG A NH2 1 
ATOM   576   N  N   . ASP A  1 79  ? 11.046  -0.569  1.208    1.00 239.78 ? 79   ASP A N   1 
ATOM   577   C  CA  . ASP A  1 79  ? 10.103  -0.400  0.109    1.00 245.36 ? 79   ASP A CA  1 
ATOM   578   C  C   . ASP A  1 79  ? 9.964   -1.709  -0.660   1.00 246.98 ? 79   ASP A C   1 
ATOM   579   O  O   . ASP A  1 79  ? 10.968  -2.342  -1.004   1.00 249.19 ? 79   ASP A O   1 
ATOM   580   C  CB  . ASP A  1 79  ? 10.554  0.713   -0.843   1.00 254.74 ? 79   ASP A CB  1 
ATOM   581   C  CG  . ASP A  1 79  ? 10.135  2.099   -0.378   1.00 255.91 ? 79   ASP A CG  1 
ATOM   582   O  OD1 . ASP A  1 79  ? 8.971   2.268   0.044    1.00 258.71 ? 79   ASP A OD1 1 
ATOM   583   O  OD2 . ASP A  1 79  ? 10.965  3.029   -0.458   1.00 253.67 ? 79   ASP A OD2 1 
ATOM   584   N  N   . TYR A  1 80  ? 8.717   -2.117  -0.912   1.00 240.96 ? 80   TYR A N   1 
ATOM   585   C  CA  . TYR A  1 80  ? 8.478   -3.181  -1.880   1.00 245.60 ? 80   TYR A CA  1 
ATOM   586   C  C   . TYR A  1 80  ? 8.717   -2.679  -3.299   1.00 262.37 ? 80   TYR A C   1 
ATOM   587   O  O   . TYR A  1 80  ? 9.340   -3.369  -4.115   1.00 270.77 ? 80   TYR A O   1 
ATOM   588   C  CB  . TYR A  1 80  ? 7.056   -3.724  -1.728   1.00 244.19 ? 80   TYR A CB  1 
ATOM   589   C  CG  . TYR A  1 80  ? 6.637   -4.678  -2.827   1.00 252.05 ? 80   TYR A CG  1 
ATOM   590   C  CD1 . TYR A  1 80  ? 6.899   -6.039  -2.730   1.00 255.76 ? 80   TYR A CD1 1 
ATOM   591   C  CD2 . TYR A  1 80  ? 5.979   -4.216  -3.961   1.00 259.66 ? 80   TYR A CD2 1 
ATOM   592   C  CE1 . TYR A  1 80  ? 6.517   -6.912  -3.732   1.00 260.50 ? 80   TYR A CE1 1 
ATOM   593   C  CE2 . TYR A  1 80  ? 5.598   -5.079  -4.968   1.00 264.99 ? 80   TYR A CE2 1 
ATOM   594   C  CZ  . TYR A  1 80  ? 5.867   -6.426  -4.848   1.00 265.95 ? 80   TYR A CZ  1 
ATOM   595   O  OH  . TYR A  1 80  ? 5.485   -7.288  -5.850   1.00 271.12 ? 80   TYR A OH  1 
ATOM   596   N  N   . ALA A  1 81  ? 8.233   -1.478  -3.604   1.00 260.39 ? 81   ALA A N   1 
ATOM   597   C  CA  . ALA A  1 81  ? 8.484   -0.823  -4.878   1.00 264.49 ? 81   ALA A CA  1 
ATOM   598   C  C   . ALA A  1 81  ? 8.476   0.683   -4.646   1.00 261.91 ? 81   ALA A C   1 
ATOM   599   O  O   . ALA A  1 81  ? 8.283   1.158   -3.522   1.00 266.97 ? 81   ALA A O   1 
ATOM   600   C  CB  . ALA A  1 81  ? 7.453   -1.244  -5.929   1.00 258.74 ? 81   ALA A CB  1 
ATOM   601   N  N   . LYS A  1 82  ? 8.703   1.438   -5.720   1.00 243.16 ? 82   LYS A N   1 
ATOM   602   C  CA  . LYS A  1 82  ? 8.686   2.894   -5.629   1.00 239.50 ? 82   LYS A CA  1 
ATOM   603   C  C   . LYS A  1 82  ? 7.314   3.381   -5.171   1.00 242.64 ? 82   LYS A C   1 
ATOM   604   O  O   . LYS A  1 82  ? 6.286   3.005   -5.744   1.00 244.65 ? 82   LYS A O   1 
ATOM   605   C  CB  . LYS A  1 82  ? 9.050   3.506   -6.981   1.00 246.37 ? 82   LYS A CB  1 
ATOM   606   C  CG  . LYS A  1 82  ? 9.092   5.024   -6.990   1.00 248.89 ? 82   LYS A CG  1 
ATOM   607   C  CD  . LYS A  1 82  ? 9.331   5.561   -8.391   1.00 255.75 ? 82   LYS A CD  1 
ATOM   608   C  CE  . LYS A  1 82  ? 9.288   7.080   -8.415   1.00 258.42 ? 82   LYS A CE  1 
ATOM   609   N  NZ  . LYS A  1 82  ? 9.413   7.619   -9.798   1.00 265.15 ? 82   LYS A NZ  1 
ATOM   610   N  N   . ASP A  1 83  ? 7.303   4.202   -4.116   1.00 248.23 ? 83   ASP A N   1 
ATOM   611   C  CA  . ASP A  1 83  ? 6.086   4.727   -3.488   1.00 246.16 ? 83   ASP A CA  1 
ATOM   612   C  C   . ASP A  1 83  ? 5.187   3.621   -2.938   1.00 248.16 ? 83   ASP A C   1 
ATOM   613   O  O   . ASP A  1 83  ? 3.973   3.812   -2.798   1.00 241.24 ? 83   ASP A O   1 
ATOM   614   C  CB  . ASP A  1 83  ? 5.288   5.620   -4.449   1.00 244.05 ? 83   ASP A CB  1 
ATOM   615   C  CG  . ASP A  1 83  ? 6.094   6.799   -4.963   1.00 242.76 ? 83   ASP A CG  1 
ATOM   616   O  OD1 . ASP A  1 83  ? 6.249   7.790   -4.218   1.00 239.43 ? 83   ASP A OD1 1 
ATOM   617   O  OD2 . ASP A  1 83  ? 6.559   6.743   -6.120   1.00 255.94 ? 83   ASP A OD2 1 
ATOM   618   N  N   . ASP A  1 84  ? 5.764   2.466   -2.615   1.00 260.08 ? 84   ASP A N   1 
ATOM   619   C  CA  . ASP A  1 84  ? 5.014   1.312   -2.118   1.00 250.34 ? 84   ASP A CA  1 
ATOM   620   C  C   . ASP A  1 84  ? 5.762   0.705   -0.942   1.00 244.00 ? 84   ASP A C   1 
ATOM   621   O  O   . ASP A  1 84  ? 6.531   -0.251  -1.098   1.00 245.11 ? 84   ASP A O   1 
ATOM   622   C  CB  . ASP A  1 84  ? 4.800   0.280   -3.228   1.00 252.11 ? 84   ASP A CB  1 
ATOM   623   C  CG  . ASP A  1 84  ? 3.663   -0.672  -2.927   1.00 240.47 ? 84   ASP A CG  1 
ATOM   624   O  OD1 . ASP A  1 84  ? 2.736   -0.290  -2.183   1.00 227.47 ? 84   ASP A OD1 1 
ATOM   625   O  OD2 . ASP A  1 84  ? 3.696   -1.805  -3.447   1.00 243.20 ? 84   ASP A OD2 1 
ATOM   626   N  N   . PRO A  1 85  ? 5.573   1.253   0.260    1.00 234.96 ? 85   PRO A N   1 
ATOM   627   C  CA  . PRO A  1 85  ? 6.317   0.758   1.427    1.00 225.28 ? 85   PRO A CA  1 
ATOM   628   C  C   . PRO A  1 85  ? 5.974   -0.692  1.746    1.00 229.14 ? 85   PRO A C   1 
ATOM   629   O  O   . PRO A  1 85  ? 4.811   -1.097  1.706    1.00 227.69 ? 85   PRO A O   1 
ATOM   630   C  CB  . PRO A  1 85  ? 5.877   1.704   2.553    1.00 213.27 ? 85   PRO A CB  1 
ATOM   631   C  CG  . PRO A  1 85  ? 5.338   2.918   1.849    1.00 218.83 ? 85   PRO A CG  1 
ATOM   632   C  CD  . PRO A  1 85  ? 4.710   2.396   0.597    1.00 227.38 ? 85   PRO A CD  1 
ATOM   633   N  N   . LEU A  1 86  ? 7.008   -1.480  2.065    1.00 233.30 ? 86   LEU A N   1 
ATOM   634   C  CA  . LEU A  1 86  ? 6.810   -2.899  2.350    1.00 222.33 ? 86   LEU A CA  1 
ATOM   635   C  C   . LEU A  1 86  ? 6.359   -3.158  3.780    1.00 221.59 ? 86   LEU A C   1 
ATOM   636   O  O   . LEU A  1 86  ? 5.592   -4.097  4.023    1.00 220.23 ? 86   LEU A O   1 
ATOM   637   C  CB  . LEU A  1 86  ? 8.097   -3.680  2.080    1.00 218.03 ? 86   LEU A CB  1 
ATOM   638   C  CG  . LEU A  1 86  ? 8.053   -5.160  2.467    1.00 212.41 ? 86   LEU A CG  1 
ATOM   639   C  CD1 . LEU A  1 86  ? 7.290   -5.967  1.430    1.00 222.90 ? 86   LEU A CD1 1 
ATOM   640   C  CD2 . LEU A  1 86  ? 9.450   -5.712  2.668    1.00 211.54 ? 86   LEU A CD2 1 
ATOM   641   N  N   . GLU A  1 87  ? 6.823   -2.361  4.738    1.00 228.61 ? 87   GLU A N   1 
ATOM   642   C  CA  . GLU A  1 87  ? 6.541   -2.623  6.141    1.00 206.77 ? 87   GLU A CA  1 
ATOM   643   C  C   . GLU A  1 87  ? 6.245   -1.317  6.862    1.00 204.81 ? 87   GLU A C   1 
ATOM   644   O  O   . GLU A  1 87  ? 6.507   -0.224  6.355    1.00 220.95 ? 87   GLU A O   1 
ATOM   645   C  CB  . GLU A  1 87  ? 7.708   -3.349  6.810    1.00 202.55 ? 87   GLU A CB  1 
ATOM   646   C  CG  . GLU A  1 87  ? 9.037   -2.643  6.623    1.00 216.28 ? 87   GLU A CG  1 
ATOM   647   C  CD  . GLU A  1 87  ? 10.222  -3.521  6.969    1.00 222.56 ? 87   GLU A CD  1 
ATOM   648   O  OE1 . GLU A  1 87  ? 10.007  -4.683  7.376    1.00 221.14 ? 87   GLU A OE1 1 
ATOM   649   O  OE2 . GLU A  1 87  ? 11.370  -3.049  6.829    1.00 227.49 ? 87   GLU A OE2 1 
ATOM   650   N  N   . PHE A  1 88  ? 5.714   -1.446  8.078    1.00 200.31 ? 88   PHE A N   1 
ATOM   651   C  CA  . PHE A  1 88  ? 5.345   -0.294  8.903    1.00 198.38 ? 88   PHE A CA  1 
ATOM   652   C  C   . PHE A  1 88  ? 5.849   -0.561  10.316   1.00 183.71 ? 88   PHE A C   1 
ATOM   653   O  O   . PHE A  1 88  ? 5.192   -1.258  11.097   1.00 179.57 ? 88   PHE A O   1 
ATOM   654   C  CB  . PHE A  1 88  ? 3.840   -0.057  8.894    1.00 203.18 ? 88   PHE A CB  1 
ATOM   655   C  CG  . PHE A  1 88  ? 3.246   0.017   7.521    1.00 196.30 ? 88   PHE A CG  1 
ATOM   656   C  CD1 . PHE A  1 88  ? 2.820   -1.130  6.868    1.00 192.35 ? 88   PHE A CD1 1 
ATOM   657   C  CD2 . PHE A  1 88  ? 3.104   1.237   6.885    1.00 198.50 ? 88   PHE A CD2 1 
ATOM   658   C  CE1 . PHE A  1 88  ? 2.272   -1.060  5.601    1.00 200.13 ? 88   PHE A CE1 1 
ATOM   659   C  CE2 . PHE A  1 88  ? 2.555   1.316   5.620    1.00 205.93 ? 88   PHE A CE2 1 
ATOM   660   C  CZ  . PHE A  1 88  ? 2.138   0.166   4.977    1.00 206.93 ? 88   PHE A CZ  1 
ATOM   661   N  N   . LYS A  1 89  ? 6.999   0.015   10.645   1.00 186.60 ? 89   LYS A N   1 
ATOM   662   C  CA  . LYS A  1 89  ? 7.614   -0.191  11.946   1.00 189.31 ? 89   LYS A CA  1 
ATOM   663   C  C   . LYS A  1 89  ? 7.176   0.852   12.955   1.00 184.78 ? 89   LYS A C   1 
ATOM   664   O  O   . LYS A  1 89  ? 7.525   0.742   14.133   1.00 200.35 ? 89   LYS A O   1 
ATOM   665   C  CB  . LYS A  1 89  ? 9.144   -0.180  11.822   1.00 211.20 ? 89   LYS A CB  1 
ATOM   666   C  CG  . LYS A  1 89  ? 9.727   -1.394  11.106   1.00 215.60 ? 89   LYS A CG  1 
ATOM   667   C  CD  . LYS A  1 89  ? 11.219  -1.234  10.867   1.00 207.23 ? 89   LYS A CD  1 
ATOM   668   C  CE  . LYS A  1 89  ? 11.776  -2.403  10.082   1.00 200.40 ? 89   LYS A CE  1 
ATOM   669   N  NZ  . LYS A  1 89  ? 13.216  -2.204  9.772    1.00 209.94 ? 89   LYS A NZ  1 
ATOM   670   N  N   . SER A  1 90  ? 6.453   1.872   12.515   1.00 185.31 ? 90   SER A N   1 
ATOM   671   C  CA  . SER A  1 90  ? 5.906   2.851   13.437   1.00 183.71 ? 90   SER A CA  1 
ATOM   672   C  C   . SER A  1 90  ? 4.854   2.205   14.328   1.00 178.82 ? 90   SER A C   1 
ATOM   673   O  O   . SER A  1 90  ? 4.004   1.442   13.858   1.00 176.31 ? 90   SER A O   1 
ATOM   674   C  CB  . SER A  1 90  ? 5.298   4.022   12.668   1.00 191.50 ? 90   SER A CB  1 
ATOM   675   O  OG  . SER A  1 90  ? 6.306   4.765   12.008   1.00 198.21 ? 90   SER A OG  1 
ATOM   676   N  N   . HIS A  1 91  ? 4.929   2.504   15.628   1.00 178.66 ? 91   HIS A N   1 
ATOM   677   C  CA  . HIS A  1 91  ? 3.991   1.975   16.623   1.00 175.90 ? 91   HIS A CA  1 
ATOM   678   C  C   . HIS A  1 91  ? 3.967   0.449   16.627   1.00 171.79 ? 91   HIS A C   1 
ATOM   679   O  O   . HIS A  1 91  ? 2.923   -0.168  16.857   1.00 181.61 ? 91   HIS A O   1 
ATOM   680   C  CB  . HIS A  1 91  ? 2.577   2.524   16.408   1.00 194.94 ? 91   HIS A CB  1 
ATOM   681   C  CG  . HIS A  1 91  ? 2.512   4.016   16.283   1.00 208.62 ? 91   HIS A CG  1 
ATOM   682   N  ND1 . HIS A  1 91  ? 2.769   4.867   17.337   1.00 210.60 ? 91   HIS A ND1 1 
ATOM   683   C  CD2 . HIS A  1 91  ? 2.219   4.809   15.225   1.00 208.12 ? 91   HIS A CD2 1 
ATOM   684   C  CE1 . HIS A  1 91  ? 2.633   6.118   16.936   1.00 200.75 ? 91   HIS A CE1 1 
ATOM   685   N  NE2 . HIS A  1 91  ? 2.301   6.111   15.657   1.00 201.63 ? 91   HIS A NE2 1 
ATOM   686   N  N   . GLN A  1 92  ? 5.118   -0.174  16.378   1.00 172.81 ? 92   GLN A N   1 
ATOM   687   C  CA  . GLN A  1 92  ? 5.202   -1.626  16.309   1.00 171.04 ? 92   GLN A CA  1 
ATOM   688   C  C   . GLN A  1 92  ? 5.364   -2.274  17.672   1.00 168.93 ? 92   GLN A C   1 
ATOM   689   O  O   . GLN A  1 92  ? 5.321   -3.507  17.758   1.00 167.28 ? 92   GLN A O   1 
ATOM   690   C  CB  . GLN A  1 92  ? 6.364   -2.053  15.413   1.00 174.51 ? 92   GLN A CB  1 
ATOM   691   C  CG  . GLN A  1 92  ? 7.738   -1.824  16.019   1.00 177.53 ? 92   GLN A CG  1 
ATOM   692   C  CD  . GLN A  1 92  ? 8.854   -2.149  15.047   1.00 196.89 ? 92   GLN A CD  1 
ATOM   693   O  OE1 . GLN A  1 92  ? 8.641   -2.839  14.050   1.00 203.42 ? 92   GLN A OE1 1 
ATOM   694   N  NE2 . GLN A  1 92  ? 10.049  -1.647  15.328   1.00 202.48 ? 92   GLN A NE2 1 
ATOM   695   N  N   . TRP A  1 93  ? 5.583   -1.484  18.721   1.00 169.36 ? 93   TRP A N   1 
ATOM   696   C  CA  . TRP A  1 93  ? 5.684   -2.001  20.083   1.00 167.60 ? 93   TRP A CA  1 
ATOM   697   C  C   . TRP A  1 93  ? 6.846   -2.983  20.227   1.00 169.09 ? 93   TRP A C   1 
ATOM   698   O  O   . TRP A  1 93  ? 6.719   -4.033  20.863   1.00 167.03 ? 93   TRP A O   1 
ATOM   699   C  CB  . TRP A  1 93  ? 4.361   -2.635  20.518   1.00 163.36 ? 93   TRP A CB  1 
ATOM   700   C  CG  . TRP A  1 93  ? 3.363   -1.626  21.018   1.00 162.21 ? 93   TRP A CG  1 
ATOM   701   C  CD1 . TRP A  1 93  ? 2.773   -0.622  20.304   1.00 163.09 ? 93   TRP A CD1 1 
ATOM   702   C  CD2 . TRP A  1 93  ? 2.851   -1.524  22.350   1.00 160.42 ? 93   TRP A CD2 1 
ATOM   703   N  NE1 . TRP A  1 93  ? 1.928   0.096   21.112   1.00 162.04 ? 93   TRP A NE1 1 
ATOM   704   C  CE2 . TRP A  1 93  ? 1.960   -0.439  22.374   1.00 160.40 ? 93   TRP A CE2 1 
ATOM   705   C  CE3 . TRP A  1 93  ? 3.063   -2.249  23.528   1.00 159.14 ? 93   TRP A CE3 1 
ATOM   706   C  CZ2 . TRP A  1 93  ? 1.280   -0.063  23.528   1.00 167.75 ? 93   TRP A CZ2 1 
ATOM   707   C  CZ3 . TRP A  1 93  ? 2.392   -1.872  24.671   1.00 157.88 ? 93   TRP A CZ3 1 
ATOM   708   C  CH2 . TRP A  1 93  ? 1.510   -0.791  24.664   1.00 160.91 ? 93   TRP A CH2 1 
ATOM   709   N  N   . PHE A  1 94  ? 7.986   -2.641  19.620   1.00 206.50 ? 94   PHE A N   1 
ATOM   710   C  CA  . PHE A  1 94  ? 9.197   -3.437  19.773   1.00 175.36 ? 94   PHE A CA  1 
ATOM   711   C  C   . PHE A  1 94  ? 9.735   -3.312  21.193   1.00 175.76 ? 94   PHE A C   1 
ATOM   712   O  O   . PHE A  1 94  ? 10.034  -2.209  21.665   1.00 177.55 ? 94   PHE A O   1 
ATOM   713   C  CB  . PHE A  1 94  ? 10.264  -3.000  18.770   1.00 180.00 ? 94   PHE A CB  1 
ATOM   714   C  CG  . PHE A  1 94  ? 11.577  -3.710  18.942   1.00 183.13 ? 94   PHE A CG  1 
ATOM   715   C  CD1 . PHE A  1 94  ? 11.716  -5.036  18.564   1.00 182.82 ? 94   PHE A CD1 1 
ATOM   716   C  CD2 . PHE A  1 94  ? 12.667  -3.059  19.496   1.00 186.74 ? 94   PHE A CD2 1 
ATOM   717   C  CE1 . PHE A  1 94  ? 12.914  -5.697  18.728   1.00 186.11 ? 94   PHE A CE1 1 
ATOM   718   C  CE2 . PHE A  1 94  ? 13.869  -3.718  19.663   1.00 189.98 ? 94   PHE A CE2 1 
ATOM   719   C  CZ  . PHE A  1 94  ? 13.990  -5.039  19.278   1.00 189.68 ? 94   PHE A CZ  1 
ATOM   720   N  N   . GLY A  1 95  ? 9.922   -4.452  21.846   1.00 174.59 ? 95   GLY A N   1 
ATOM   721   C  CA  . GLY A  1 95  ? 10.255  -4.497  23.251   1.00 174.65 ? 95   GLY A CA  1 
ATOM   722   C  C   . GLY A  1 95  ? 9.087   -4.785  24.164   1.00 195.87 ? 95   GLY A C   1 
ATOM   723   O  O   . GLY A  1 95  ? 9.223   -4.626  25.383   1.00 200.68 ? 95   GLY A O   1 
ATOM   724   N  N   . ALA A  1 96  ? 7.949   -5.221  23.615   1.00 167.06 ? 96   ALA A N   1 
ATOM   725   C  CA  . ALA A  1 96  ? 6.801   -5.565  24.443   1.00 163.28 ? 96   ALA A CA  1 
ATOM   726   C  C   . ALA A  1 96  ? 7.034   -6.851  25.220   1.00 162.40 ? 96   ALA A C   1 
ATOM   727   O  O   . ALA A  1 96  ? 6.440   -7.045  26.286   1.00 175.35 ? 96   ALA A O   1 
ATOM   728   C  CB  . ALA A  1 96  ? 5.550   -5.692  23.575   1.00 188.44 ? 96   ALA A CB  1 
ATOM   729   N  N   . SER A  1 97  ? 7.876   -7.741  24.704   1.00 164.25 ? 97   SER A N   1 
ATOM   730   C  CA  . SER A  1 97  ? 8.278   -8.944  25.420   1.00 167.46 ? 97   SER A CA  1 
ATOM   731   C  C   . SER A  1 97  ? 9.761   -9.178  25.176   1.00 172.52 ? 97   SER A C   1 
ATOM   732   O  O   . SER A  1 97  ? 10.198  -9.253  24.024   1.00 174.74 ? 97   SER A O   1 
ATOM   733   C  CB  . SER A  1 97  ? 7.456   -10.158 24.974   1.00 174.80 ? 97   SER A CB  1 
ATOM   734   O  OG  . SER A  1 97  ? 7.752   -10.506 23.635   1.00 191.75 ? 97   SER A OG  1 
ATOM   735   N  N   . VAL A  1 98  ? 10.532  -9.292  26.256   1.00 170.39 ? 98   VAL A N   1 
ATOM   736   C  CA  . VAL A  1 98  ? 11.972  -9.509  26.181   1.00 174.92 ? 98   VAL A CA  1 
ATOM   737   C  C   . VAL A  1 98  ? 12.311  -10.785 26.937   1.00 184.62 ? 98   VAL A C   1 
ATOM   738   O  O   . VAL A  1 98  ? 11.902  -10.956 28.090   1.00 206.33 ? 98   VAL A O   1 
ATOM   739   C  CB  . VAL A  1 98  ? 12.760  -8.320  26.756   1.00 177.83 ? 98   VAL A CB  1 
ATOM   740   C  CG1 . VAL A  1 98  ? 14.255  -8.499  26.504   1.00 182.99 ? 98   VAL A CG1 1 
ATOM   741   C  CG2 . VAL A  1 98  ? 12.248  -7.004  26.174   1.00 187.02 ? 98   VAL A CG2 1 
ATOM   742   N  N   . ARG A  1 99  ? 13.060  -11.674 26.288   1.00 178.03 ? 99   ARG A N   1 
ATOM   743   C  CA  . ARG A  1 99  ? 13.471  -12.938 26.883   1.00 179.19 ? 99   ARG A CA  1 
ATOM   744   C  C   . ARG A  1 99  ? 14.924  -13.181 26.520   1.00 184.65 ? 99   ARG A C   1 
ATOM   745   O  O   . ARG A  1 99  ? 15.313  -12.997 25.363   1.00 186.74 ? 99   ARG A O   1 
ATOM   746   C  CB  . ARG A  1 99  ? 12.598  -14.103 26.400   1.00 188.83 ? 99   ARG A CB  1 
ATOM   747   C  CG  . ARG A  1 99  ? 11.227  -14.193 27.062   1.00 195.78 ? 99   ARG A CG  1 
ATOM   748   C  CD  . ARG A  1 99  ? 11.316  -14.231 28.584   1.00 205.19 ? 99   ARG A CD  1 
ATOM   749   N  NE  . ARG A  1 99  ? 10.995  -12.936 29.185   1.00 225.31 ? 99   ARG A NE  1 
ATOM   750   C  CZ  . ARG A  1 99  ? 9.775   -12.569 29.577   1.00 200.80 ? 99   ARG A CZ  1 
ATOM   751   N  NH1 . ARG A  1 99  ? 8.746   -13.394 29.430   1.00 188.13 ? 99   ARG A NH1 1 
ATOM   752   N  NH2 . ARG A  1 99  ? 9.579   -11.370 30.113   1.00 188.83 ? 99   ARG A NH2 1 
ATOM   753   N  N   . SER A  1 100 ? 15.719  -13.598 27.502   1.00 190.19 ? 100  SER A N   1 
ATOM   754   C  CA  . SER A  1 100 ? 17.158  -13.749 27.336   1.00 196.89 ? 100  SER A CA  1 
ATOM   755   C  C   . SER A  1 100 ? 17.620  -15.119 27.806   1.00 196.88 ? 100  SER A C   1 
ATOM   756   O  O   . SER A  1 100 ? 17.175  -15.617 28.845   1.00 208.23 ? 100  SER A O   1 
ATOM   757   C  CB  . SER A  1 100 ? 17.914  -12.670 28.107   1.00 195.59 ? 100  SER A CB  1 
ATOM   758   O  OG  . SER A  1 100 ? 19.291  -12.681 27.791   1.00 201.46 ? 100  SER A OG  1 
ATOM   759   N  N   . LYS A  1 101 ? 18.538  -15.712 27.046   1.00 200.05 ? 101  LYS A N   1 
ATOM   760   C  CA  . LYS A  1 101 ? 19.129  -17.002 27.389   1.00 203.18 ? 101  LYS A CA  1 
ATOM   761   C  C   . LYS A  1 101 ? 20.628  -16.907 27.146   1.00 220.02 ? 101  LYS A C   1 
ATOM   762   O  O   . LYS A  1 101 ? 21.073  -16.894 25.995   1.00 233.40 ? 101  LYS A O   1 
ATOM   763   C  CB  . LYS A  1 101 ? 18.509  -18.129 26.567   1.00 201.83 ? 101  LYS A CB  1 
ATOM   764   C  CG  . LYS A  1 101 ? 19.095  -19.498 26.848   1.00 212.41 ? 101  LYS A CG  1 
ATOM   765   C  CD  . LYS A  1 101 ? 18.505  -20.552 25.929   1.00 204.64 ? 101  LYS A CD  1 
ATOM   766   C  CE  . LYS A  1 101 ? 19.047  -21.933 26.260   1.00 219.66 ? 101  LYS A CE  1 
ATOM   767   N  NZ  . LYS A  1 101 ? 20.525  -22.015 26.089   1.00 237.00 ? 101  LYS A NZ  1 
ATOM   768   N  N   . GLN A  1 102 ? 21.401  -16.844 28.229   1.00 212.39 ? 102  GLN A N   1 
ATOM   769   C  CA  . GLN A  1 102 ? 22.861  -16.728 28.185   1.00 219.20 ? 102  GLN A CA  1 
ATOM   770   C  C   . GLN A  1 102 ? 23.222  -15.440 27.458   1.00 220.48 ? 102  GLN A C   1 
ATOM   771   O  O   . GLN A  1 102 ? 22.792  -14.359 27.896   1.00 217.67 ? 102  GLN A O   1 
ATOM   772   C  CB  . GLN A  1 102 ? 23.448  -17.982 27.541   1.00 223.39 ? 102  GLN A CB  1 
ATOM   773   C  CG  . GLN A  1 102 ? 23.064  -19.301 28.139   1.00 222.46 ? 102  GLN A CG  1 
ATOM   774   C  CD  . GLN A  1 102 ? 23.370  -20.427 27.177   1.00 225.79 ? 102  GLN A CD  1 
ATOM   775   O  OE1 . GLN A  1 102 ? 23.962  -20.206 26.120   1.00 229.23 ? 102  GLN A OE1 1 
ATOM   776   N  NE2 . GLN A  1 102 ? 22.989  -21.640 27.541   1.00 227.78 ? 102  GLN A NE2 1 
ATOM   777   N  N   . ASP A  1 103 ? 23.964  -15.502 26.355   1.00 241.92 ? 103  ASP A N   1 
ATOM   778   C  CA  . ASP A  1 103 ? 24.365  -14.347 25.572   1.00 246.52 ? 103  ASP A CA  1 
ATOM   779   C  C   . ASP A  1 103 ? 23.384  -14.050 24.449   1.00 222.58 ? 103  ASP A C   1 
ATOM   780   O  O   . ASP A  1 103 ? 23.707  -13.282 23.538   1.00 224.63 ? 103  ASP A O   1 
ATOM   781   C  CB  . ASP A  1 103 ? 25.784  -14.561 25.021   1.00 236.45 ? 103  ASP A CB  1 
ATOM   782   C  CG  . ASP A  1 103 ? 25.872  -15.718 24.038   1.00 236.46 ? 103  ASP A CG  1 
ATOM   783   O  OD1 . ASP A  1 103 ? 25.101  -16.689 24.189   1.00 247.47 ? 103  ASP A OD1 1 
ATOM   784   O  OD2 . ASP A  1 103 ? 26.732  -15.672 23.130   1.00 241.84 ? 103  ASP A OD2 1 
ATOM   785   N  N   . LYS A  1 104 ? 22.188  -14.623 24.511   1.00 217.08 ? 104  LYS A N   1 
ATOM   786   C  CA  . LYS A  1 104 ? 21.154  -14.420 23.509   1.00 221.59 ? 104  LYS A CA  1 
ATOM   787   C  C   . LYS A  1 104 ? 20.093  -13.490 24.081   1.00 226.89 ? 104  LYS A C   1 
ATOM   788   O  O   . LYS A  1 104 ? 19.623  -13.693 25.206   1.00 233.64 ? 104  LYS A O   1 
ATOM   789   C  CB  . LYS A  1 104 ? 20.528  -15.757 23.111   1.00 218.00 ? 104  LYS A CB  1 
ATOM   790   C  CG  . LYS A  1 104 ? 21.542  -16.816 22.685   1.00 217.16 ? 104  LYS A CG  1 
ATOM   791   C  CD  . LYS A  1 104 ? 20.869  -18.167 22.483   1.00 215.45 ? 104  LYS A CD  1 
ATOM   792   C  CE  . LYS A  1 104 ? 21.863  -19.235 22.068   1.00 221.67 ? 104  LYS A CE  1 
ATOM   793   N  NZ  . LYS A  1 104 ? 22.472  -18.921 20.751   1.00 236.68 ? 104  LYS A NZ  1 
ATOM   794   N  N   . ILE A  1 105 ? 19.702  -12.489 23.300   1.00 213.30 ? 105  ILE A N   1 
ATOM   795   C  CA  . ILE A  1 105 ? 18.646  -11.561 23.679   1.00 201.11 ? 105  ILE A CA  1 
ATOM   796   C  C   . ILE A  1 105 ? 17.613  -11.569 22.567   1.00 197.79 ? 105  ILE A C   1 
ATOM   797   O  O   . ILE A  1 105 ? 17.943  -11.289 21.408   1.00 200.26 ? 105  ILE A O   1 
ATOM   798   C  CB  . ILE A  1 105 ? 19.175  -10.138 23.919   1.00 203.19 ? 105  ILE A CB  1 
ATOM   799   C  CG1 . ILE A  1 105 ? 20.228  -10.138 25.029   1.00 213.85 ? 105  ILE A CG1 1 
ATOM   800   C  CG2 . ILE A  1 105 ? 18.030  -9.200  24.260   1.00 198.36 ? 105  ILE A CG2 1 
ATOM   801   C  CD1 . ILE A  1 105 ? 20.788  -8.770  25.340   1.00 209.79 ? 105  ILE A CD1 1 
ATOM   802   N  N   . LEU A  1 106 ? 16.375  -11.908 22.913   1.00 194.71 ? 106  LEU A N   1 
ATOM   803   C  CA  . LEU A  1 106 ? 15.277  -11.970 21.959   1.00 189.19 ? 106  LEU A CA  1 
ATOM   804   C  C   . LEU A  1 106 ? 14.244  -10.905 22.312   1.00 185.03 ? 106  LEU A C   1 
ATOM   805   O  O   . LEU A  1 106 ? 13.705  -10.900 23.425   1.00 182.16 ? 106  LEU A O   1 
ATOM   806   C  CB  . LEU A  1 106 ? 14.656  -13.367 21.947   1.00 187.09 ? 106  LEU A CB  1 
ATOM   807   C  CG  . LEU A  1 106 ? 13.460  -13.605 21.029   1.00 183.70 ? 106  LEU A CG  1 
ATOM   808   C  CD1 . LEU A  1 106 ? 13.882  -13.477 19.576   1.00 186.88 ? 106  LEU A CD1 1 
ATOM   809   C  CD2 . LEU A  1 106 ? 12.853  -14.974 21.294   1.00 181.72 ? 106  LEU A CD2 1 
ATOM   810   N  N   . ALA A  1 107 ? 13.998  -9.989  21.376   1.00 190.24 ? 107  ALA A N   1 
ATOM   811   C  CA  . ALA A  1 107 ? 12.972  -8.967  21.523   1.00 181.66 ? 107  ALA A CA  1 
ATOM   812   C  C   . ALA A  1 107 ? 12.051  -8.996  20.311   1.00 179.74 ? 107  ALA A C   1 
ATOM   813   O  O   . ALA A  1 107 ? 12.475  -9.329  19.201   1.00 182.31 ? 107  ALA A O   1 
ATOM   814   C  CB  . ALA A  1 107 ? 13.590  -7.574  21.688   1.00 184.24 ? 107  ALA A CB  1 
ATOM   815   N  N   . CYS A  1 108 ? 10.789  -8.623  20.526   1.00 175.55 ? 108  CYS A N   1 
ATOM   816   C  CA  . CYS A  1 108 ? 9.764   -8.753  19.498   1.00 184.74 ? 108  CYS A CA  1 
ATOM   817   C  C   . CYS A  1 108 ? 8.903   -7.499  19.417   1.00 171.55 ? 108  CYS A C   1 
ATOM   818   O  O   . CYS A  1 108 ? 8.805   -6.714  20.363   1.00 177.85 ? 108  CYS A O   1 
ATOM   819   C  CB  . CYS A  1 108 ? 8.864   -9.964  19.747   1.00 189.09 ? 108  CYS A CB  1 
ATOM   820   S  SG  . CYS A  1 108 ? 9.715   -11.541 19.649   1.00 224.81 ? 108  CYS A SG  1 
ATOM   821   N  N   . ALA A  1 109 ? 8.251   -7.343  18.263   1.00 171.09 ? 109  ALA A N   1 
ATOM   822   C  CA  . ALA A  1 109 ? 7.368   -6.214  17.979   1.00 169.72 ? 109  ALA A CA  1 
ATOM   823   C  C   . ALA A  1 109 ? 5.993   -6.764  17.627   1.00 166.17 ? 109  ALA A C   1 
ATOM   824   O  O   . ALA A  1 109 ? 5.705   -7.045  16.453   1.00 166.78 ? 109  ALA A O   1 
ATOM   825   C  CB  . ALA A  1 109 ? 7.922   -5.346  16.853   1.00 175.26 ? 109  ALA A CB  1 
ATOM   826   N  N   . PRO A  1 110 ? 5.124   -6.961  18.619   1.00 162.71 ? 110  PRO A N   1 
ATOM   827   C  CA  . PRO A  1 110 ? 3.809   -7.567  18.346   1.00 175.91 ? 110  PRO A CA  1 
ATOM   828   C  C   . PRO A  1 110 ? 2.905   -6.725  17.459   1.00 186.18 ? 110  PRO A C   1 
ATOM   829   O  O   . PRO A  1 110 ? 2.055   -7.287  16.758   1.00 173.97 ? 110  PRO A O   1 
ATOM   830   C  CB  . PRO A  1 110 ? 3.214   -7.750  19.752   1.00 166.94 ? 110  PRO A CB  1 
ATOM   831   C  CG  . PRO A  1 110 ? 4.414   -7.805  20.658   1.00 177.21 ? 110  PRO A CG  1 
ATOM   832   C  CD  . PRO A  1 110 ? 5.404   -6.852  20.058   1.00 165.53 ? 110  PRO A CD  1 
ATOM   833   N  N   . LEU A  1 111 ? 3.050   -5.399  17.464   1.00 186.94 ? 111  LEU A N   1 
ATOM   834   C  CA  . LEU A  1 111 ? 2.218   -4.530  16.642   1.00 162.48 ? 111  LEU A CA  1 
ATOM   835   C  C   . LEU A  1 111 ? 2.907   -4.124  15.345   1.00 176.03 ? 111  LEU A C   1 
ATOM   836   O  O   . LEU A  1 111 ? 2.524   -3.122  14.728   1.00 182.22 ? 111  LEU A O   1 
ATOM   837   C  CB  . LEU A  1 111 ? 1.790   -3.296  17.432   1.00 160.29 ? 111  LEU A CB  1 
ATOM   838   C  CG  . LEU A  1 111 ? 0.557   -3.568  18.285   1.00 156.75 ? 111  LEU A CG  1 
ATOM   839   C  CD1 . LEU A  1 111 ? 0.201   -2.354  19.109   1.00 169.06 ? 111  LEU A CD1 1 
ATOM   840   C  CD2 . LEU A  1 111 ? -0.610  -3.978  17.402   1.00 158.93 ? 111  LEU A CD2 1 
ATOM   841   N  N   . TYR A  1 112 ? 3.930   -4.869  14.938   1.00 188.58 ? 112  TYR A N   1 
ATOM   842   C  CA  . TYR A  1 112 ? 4.522   -4.698  13.621   1.00 172.96 ? 112  TYR A CA  1 
ATOM   843   C  C   . TYR A  1 112 ? 3.537   -5.138  12.547   1.00 169.07 ? 112  TYR A C   1 
ATOM   844   O  O   . TYR A  1 112 ? 3.037   -6.266  12.569   1.00 167.05 ? 112  TYR A O   1 
ATOM   845   C  CB  . TYR A  1 112 ? 5.819   -5.506  13.535   1.00 172.55 ? 112  TYR A CB  1 
ATOM   846   C  CG  . TYR A  1 112 ? 6.347   -5.761  12.141   1.00 176.12 ? 112  TYR A CG  1 
ATOM   847   C  CD1 . TYR A  1 112 ? 7.176   -4.844  11.508   1.00 193.27 ? 112  TYR A CD1 1 
ATOM   848   C  CD2 . TYR A  1 112 ? 6.045   -6.941  11.472   1.00 175.84 ? 112  TYR A CD2 1 
ATOM   849   C  CE1 . TYR A  1 112 ? 7.671   -5.086  10.239   1.00 201.01 ? 112  TYR A CE1 1 
ATOM   850   C  CE2 . TYR A  1 112 ? 6.532   -7.190  10.207   1.00 183.28 ? 112  TYR A CE2 1 
ATOM   851   C  CZ  . TYR A  1 112 ? 7.345   -6.262  9.595    1.00 191.47 ? 112  TYR A CZ  1 
ATOM   852   O  OH  . TYR A  1 112 ? 7.832   -6.515  8.334    1.00 196.96 ? 112  TYR A OH  1 
ATOM   853   N  N   . HIS A  1 113 ? 3.267   -4.249  11.601   1.00 170.93 ? 113  HIS A N   1 
ATOM   854   C  CA  . HIS A  1 113 ? 2.401   -4.548  10.474   1.00 170.90 ? 113  HIS A CA  1 
ATOM   855   C  C   . HIS A  1 113 ? 3.265   -4.754  9.242    1.00 185.31 ? 113  HIS A C   1 
ATOM   856   O  O   . HIS A  1 113 ? 4.337   -4.158  9.112    1.00 214.52 ? 113  HIS A O   1 
ATOM   857   C  CB  . HIS A  1 113 ? 1.385   -3.429  10.226   1.00 176.28 ? 113  HIS A CB  1 
ATOM   858   C  CG  . HIS A  1 113 ? 0.435   -3.207  11.365   1.00 186.14 ? 113  HIS A CG  1 
ATOM   859   N  ND1 . HIS A  1 113 ? 0.835   -2.670  12.570   1.00 181.50 ? 113  HIS A ND1 1 
ATOM   860   C  CD2 . HIS A  1 113 ? -0.894  -3.445  11.481   1.00 168.01 ? 113  HIS A CD2 1 
ATOM   861   C  CE1 . HIS A  1 113 ? -0.206  -2.592  13.381   1.00 164.14 ? 113  HIS A CE1 1 
ATOM   862   N  NE2 . HIS A  1 113 ? -1.267  -3.057  12.745   1.00 161.72 ? 113  HIS A NE2 1 
ATOM   863   N  N   . TRP A  1 114 ? 2.789   -5.593  8.327    1.00 181.81 ? 114  TRP A N   1 
ATOM   864   C  CA  . TRP A  1 114 ? 3.552   -5.878  7.121    1.00 204.03 ? 114  TRP A CA  1 
ATOM   865   C  C   . TRP A  1 114 ? 2.616   -5.974  5.927    1.00 189.65 ? 114  TRP A C   1 
ATOM   866   O  O   . TRP A  1 114 ? 1.539   -6.576  6.007    1.00 185.38 ? 114  TRP A O   1 
ATOM   867   C  CB  . TRP A  1 114 ? 4.375   -7.167  7.282    1.00 228.13 ? 114  TRP A CB  1 
ATOM   868   C  CG  . TRP A  1 114 ? 4.619   -7.947  6.007    1.00 236.32 ? 114  TRP A CG  1 
ATOM   869   C  CD1 . TRP A  1 114 ? 5.650   -7.778  5.125    1.00 240.48 ? 114  TRP A CD1 1 
ATOM   870   C  CD2 . TRP A  1 114 ? 3.841   -9.044  5.503    1.00 230.52 ? 114  TRP A CD2 1 
ATOM   871   N  NE1 . TRP A  1 114 ? 5.550   -8.684  4.096    1.00 239.34 ? 114  TRP A NE1 1 
ATOM   872   C  CE2 . TRP A  1 114 ? 4.450   -9.474  4.306    1.00 242.13 ? 114  TRP A CE2 1 
ATOM   873   C  CE3 . TRP A  1 114 ? 2.684   -9.697  5.942    1.00 211.29 ? 114  TRP A CE3 1 
ATOM   874   C  CZ2 . TRP A  1 114 ? 3.941   -10.524 3.544    1.00 244.25 ? 114  TRP A CZ2 1 
ATOM   875   C  CZ3 . TRP A  1 114 ? 2.182   -10.740 5.185    1.00 209.11 ? 114  TRP A CZ3 1 
ATOM   876   C  CH2 . TRP A  1 114 ? 2.809   -11.142 4.000    1.00 230.46 ? 114  TRP A CH2 1 
ATOM   877   N  N   . ARG A  1 115 ? 3.032   -5.350  4.827    1.00 184.25 ? 115  ARG A N   1 
ATOM   878   C  CA  . ARG A  1 115 ? 2.215   -5.281  3.626    1.00 189.71 ? 115  ARG A CA  1 
ATOM   879   C  C   . ARG A  1 115 ? 2.393   -6.559  2.825    1.00 199.96 ? 115  ARG A C   1 
ATOM   880   O  O   . ARG A  1 115 ? 3.501   -7.100  2.738    1.00 219.91 ? 115  ARG A O   1 
ATOM   881   C  CB  . ARG A  1 115 ? 2.613   -4.070  2.781    1.00 198.79 ? 115  ARG A CB  1 
ATOM   882   C  CG  . ARG A  1 115 ? 2.018   -4.062  1.387    1.00 211.37 ? 115  ARG A CG  1 
ATOM   883   C  CD  . ARG A  1 115 ? 2.828   -3.151  0.476    1.00 224.40 ? 115  ARG A CD  1 
ATOM   884   N  NE  . ARG A  1 115 ? 2.325   -3.131  -0.893   1.00 238.67 ? 115  ARG A NE  1 
ATOM   885   C  CZ  . ARG A  1 115 ? 2.618   -4.051  -1.806   1.00 257.78 ? 115  ARG A CZ  1 
ATOM   886   N  NH1 . ARG A  1 115 ? 3.411   -5.065  -1.494   1.00 269.22 ? 115  ARG A NH1 1 
ATOM   887   N  NH2 . ARG A  1 115 ? 2.119   -3.963  -3.031   1.00 264.02 ? 115  ARG A NH2 1 
ATOM   888   N  N   . THR A  1 116 ? 1.296   -7.054  2.260    1.00 194.64 ? 116  THR A N   1 
ATOM   889   C  CA  . THR A  1 116 ? 1.345   -8.352  1.612    1.00 202.91 ? 116  THR A CA  1 
ATOM   890   C  C   . THR A  1 116 ? 2.237   -8.258  0.380    1.00 223.62 ? 116  THR A C   1 
ATOM   891   O  O   . THR A  1 116 ? 2.421   -7.184  -0.195   1.00 239.86 ? 116  THR A O   1 
ATOM   892   C  CB  . THR A  1 116 ? -0.072  -8.795  1.212    1.00 202.52 ? 116  THR A CB  1 
ATOM   893   O  OG1 . THR A  1 116 ? -0.914  -8.781  2.374    1.00 199.88 ? 116  THR A OG1 1 
ATOM   894   C  CG2 . THR A  1 116 ? -0.084  -10.199 0.639    1.00 210.97 ? 116  THR A CG2 1 
ATOM   895   N  N   . GLU A  1 117 ? 2.775   -9.395  -0.042   1.00 204.83 ? 117  GLU A N   1 
ATOM   896   C  CA  . GLU A  1 117 ? 3.654   -9.437  -1.199   1.00 201.76 ? 117  GLU A CA  1 
ATOM   897   C  C   . GLU A  1 117 ? 2.873   -9.754  -2.460   1.00 210.15 ? 117  GLU A C   1 
ATOM   898   O  O   . GLU A  1 117 ? 3.447   -9.843  -3.551   1.00 223.31 ? 117  GLU A O   1 
ATOM   899   C  CB  . GLU A  1 117 ? 4.766   -10.466 -0.967   1.00 203.85 ? 117  GLU A CB  1 
ATOM   900   C  CG  . GLU A  1 117 ? 6.008   -10.235 -1.797   1.00 215.55 ? 117  GLU A CG  1 
ATOM   901   C  CD  . GLU A  1 117 ? 7.123   -11.187 -1.437   1.00 213.80 ? 117  GLU A CD  1 
ATOM   902   O  OE1 . GLU A  1 117 ? 6.889   -12.089 -0.604   1.00 208.94 ? 117  GLU A OE1 1 
ATOM   903   O  OE2 . GLU A  1 117 ? 8.243   -11.006 -1.957   1.00 230.77 ? 117  GLU A OE2 1 
ATOM   904   N  N   . MET A  1 118 ? 1.568   -9.931  -2.313   1.00 232.47 ? 118  MET A N   1 
ATOM   905   C  CA  . MET A  1 118 ? 0.617   -10.153 -3.386   1.00 233.79 ? 118  MET A CA  1 
ATOM   906   C  C   . MET A  1 118 ? -0.179  -8.895  -3.700   1.00 231.98 ? 118  MET A C   1 
ATOM   907   O  O   . MET A  1 118 ? -0.474  -8.629  -4.870   1.00 240.54 ? 118  MET A O   1 
ATOM   908   C  CB  . MET A  1 118 ? -0.326  -11.299 -3.004   1.00 241.39 ? 118  MET A CB  1 
ATOM   909   C  CG  . MET A  1 118 ? 0.361   -12.667 -2.974   1.00 248.52 ? 118  MET A CG  1 
ATOM   910   S  SD  . MET A  1 118 ? -0.525  -13.881 -1.967   1.00 256.73 ? 118  MET A SD  1 
ATOM   911   C  CE  . MET A  1 118 ? 0.636   -15.246 -1.941   1.00 244.47 ? 118  MET A CE  1 
ATOM   912   N  N   . LYS A  1 119 ? -0.526  -8.111  -2.678   1.00 232.26 ? 119  LYS A N   1 
ATOM   913   C  CA  . LYS A  1 119 ? -1.262  -6.864  -2.848   1.00 226.72 ? 119  LYS A CA  1 
ATOM   914   C  C   . LYS A  1 119 ? -0.891  -5.911  -1.716   1.00 216.93 ? 119  LYS A C   1 
ATOM   915   O  O   . LYS A  1 119 ? -0.089  -6.237  -0.836   1.00 213.69 ? 119  LYS A O   1 
ATOM   916   C  CB  . LYS A  1 119 ? -2.769  -7.118  -2.896   1.00 227.71 ? 119  LYS A CB  1 
ATOM   917   C  CG  . LYS A  1 119 ? -3.218  -8.310  -2.073   1.00 229.18 ? 119  LYS A CG  1 
ATOM   918   C  CD  . LYS A  1 119 ? -4.657  -8.688  -2.377   1.00 235.63 ? 119  LYS A CD  1 
ATOM   919   C  CE  . LYS A  1 119 ? -4.995  -10.043 -1.772   1.00 235.08 ? 119  LYS A CE  1 
ATOM   920   N  NZ  . LYS A  1 119 ? -4.165  -11.134 -2.359   1.00 240.82 ? 119  LYS A NZ  1 
ATOM   921   N  N   . GLN A  1 120 ? -1.492  -4.720  -1.738   1.00 208.15 ? 120  GLN A N   1 
ATOM   922   C  CA  . GLN A  1 120 ? -1.164  -3.650  -0.790   1.00 200.03 ? 120  GLN A CA  1 
ATOM   923   C  C   . GLN A  1 120 ? -2.054  -3.759  0.445    1.00 196.56 ? 120  GLN A C   1 
ATOM   924   O  O   . GLN A  1 120 ? -3.121  -3.152  0.524    1.00 186.39 ? 120  GLN A O   1 
ATOM   925   C  CB  . GLN A  1 120 ? -1.315  -2.288  -1.451   1.00 203.36 ? 120  GLN A CB  1 
ATOM   926   C  CG  . GLN A  1 120 ? -0.250  -1.962  -2.485   1.00 217.70 ? 120  GLN A CG  1 
ATOM   927   C  CD  . GLN A  1 120 ? -0.552  -0.688  -3.243   1.00 221.41 ? 120  GLN A CD  1 
ATOM   928   O  OE1 . GLN A  1 120 ? -1.366  0.122   -2.806   1.00 218.89 ? 120  GLN A OE1 1 
ATOM   929   N  NE2 . GLN A  1 120 ? 0.115   -0.496  -4.377   1.00 233.66 ? 120  GLN A NE2 1 
ATOM   930   N  N   . GLU A  1 121 ? -1.609  -4.539  1.430    1.00 210.27 ? 121  GLU A N   1 
ATOM   931   C  CA  . GLU A  1 121 ? -2.284  -4.636  2.719    1.00 208.33 ? 121  GLU A CA  1 
ATOM   932   C  C   . GLU A  1 121 ? -1.411  -4.046  3.824    1.00 197.11 ? 121  GLU A C   1 
ATOM   933   O  O   . GLU A  1 121 ? -0.331  -3.501  3.581    1.00 192.30 ? 121  GLU A O   1 
ATOM   934   C  CB  . GLU A  1 121 ? -2.656  -6.085  3.038    1.00 205.98 ? 121  GLU A CB  1 
ATOM   935   C  CG  . GLU A  1 121 ? -3.632  -6.718  2.061    1.00 198.12 ? 121  GLU A CG  1 
ATOM   936   C  CD  . GLU A  1 121 ? -5.014  -6.100  2.159    1.00 187.91 ? 121  GLU A CD  1 
ATOM   937   O  OE1 . GLU A  1 121 ? -5.799  -6.231  1.196    1.00 190.61 ? 121  GLU A OE1 1 
ATOM   938   O  OE2 . GLU A  1 121 ? -5.315  -5.477  3.199    1.00 176.94 ? 121  GLU A OE2 1 
ATOM   939   N  N   . ARG A  1 122 ? -1.908  -4.153  5.066    1.00 200.83 ? 122  ARG A N   1 
ATOM   940   C  CA  . ARG A  1 122 ? -1.195  -3.697  6.262    1.00 194.06 ? 122  ARG A CA  1 
ATOM   941   C  C   . ARG A  1 122 ? -1.575  -4.671  7.379    1.00 194.62 ? 122  ARG A C   1 
ATOM   942   O  O   . ARG A  1 122 ? -2.444  -4.408  8.216    1.00 185.34 ? 122  ARG A O   1 
ATOM   943   C  CB  . ARG A  1 122 ? -1.538  -2.251  6.625    1.00 192.38 ? 122  ARG A CB  1 
ATOM   944   C  CG  . ARG A  1 122 ? -0.658  -1.644  7.715    1.00 192.65 ? 122  ARG A CG  1 
ATOM   945   C  CD  . ARG A  1 122 ? -0.824  -0.126  7.788    1.00 194.31 ? 122  ARG A CD  1 
ATOM   946   N  NE  . ARG A  1 122 ? 0.200   0.507   8.616    1.00 202.12 ? 122  ARG A NE  1 
ATOM   947   C  CZ  . ARG A  1 122 ? 0.081   0.730   9.921    1.00 199.25 ? 122  ARG A CZ  1 
ATOM   948   N  NH1 . ARG A  1 122 ? -1.028  0.376   10.559   1.00 176.46 ? 122  ARG A NH1 1 
ATOM   949   N  NH2 . ARG A  1 122 ? 1.072   1.307   10.589   1.00 204.07 ? 122  ARG A NH2 1 
ATOM   950   N  N   . GLU A  1 123 ? -0.906  -5.819  7.386    1.00 185.01 ? 123  GLU A N   1 
ATOM   951   C  CA  . GLU A  1 123 ? -1.310  -6.916  8.242    1.00 173.99 ? 123  GLU A CA  1 
ATOM   952   C  C   . GLU A  1 123 ? -0.316  -7.112  9.371    1.00 175.47 ? 123  GLU A C   1 
ATOM   953   O  O   . GLU A  1 123 ? 0.886   -7.271  9.117    1.00 185.73 ? 123  GLU A O   1 
ATOM   954   C  CB  . GLU A  1 123 ? -1.437  -8.204  7.428    1.00 181.18 ? 123  GLU A CB  1 
ATOM   955   C  CG  . GLU A  1 123 ? -2.464  -8.103  6.318    1.00 201.71 ? 123  GLU A CG  1 
ATOM   956   C  CD  . GLU A  1 123 ? -2.664  -9.410  5.578    1.00 201.15 ? 123  GLU A CD  1 
ATOM   957   O  OE1 . GLU A  1 123 ? -3.615  -9.489  4.770    1.00 207.42 ? 123  GLU A OE1 1 
ATOM   958   O  OE2 . GLU A  1 123 ? -1.881  -10.357 5.813    1.00 187.02 ? 123  GLU A OE2 1 
ATOM   959   N  N   . PRO A  1 124 ? -0.772  -7.102  10.609   1.00 172.86 ? 124  PRO A N   1 
ATOM   960   C  CA  . PRO A  1 124 ? 0.128   -7.218  11.780   1.00 169.78 ? 124  PRO A CA  1 
ATOM   961   C  C   . PRO A  1 124 ? 0.652   -8.630  12.040   1.00 167.99 ? 124  PRO A C   1 
ATOM   962   O  O   . PRO A  1 124 ? 0.197   -9.358  12.917   1.00 172.97 ? 124  PRO A O   1 
ATOM   963   C  CB  . PRO A  1 124 ? -0.755  -6.719  12.926   1.00 158.71 ? 124  PRO A CB  1 
ATOM   964   C  CG  . PRO A  1 124 ? -2.144  -7.032  12.496   1.00 156.96 ? 124  PRO A CG  1 
ATOM   965   C  CD  . PRO A  1 124 ? -2.172  -6.870  11.003   1.00 161.49 ? 124  PRO A CD  1 
ATOM   966   N  N   . VAL A  1 125 ? 1.656   -9.035  11.254   1.00 165.01 ? 125  VAL A N   1 
ATOM   967   C  CA  . VAL A  1 125 ? 2.222   -10.376 11.394   1.00 165.57 ? 125  VAL A CA  1 
ATOM   968   C  C   . VAL A  1 125 ? 3.247   -10.464 12.516   1.00 166.23 ? 125  VAL A C   1 
ATOM   969   O  O   . VAL A  1 125 ? 3.626   -11.575 12.910   1.00 172.89 ? 125  VAL A O   1 
ATOM   970   C  CB  . VAL A  1 125 ? 2.879   -10.860 10.090   1.00 172.99 ? 125  VAL A CB  1 
ATOM   971   C  CG1 . VAL A  1 125 ? 1.830   -11.052 9.010    1.00 177.07 ? 125  VAL A CG1 1 
ATOM   972   C  CG2 . VAL A  1 125 ? 3.975   -9.901  9.643    1.00 177.36 ? 125  VAL A CG2 1 
ATOM   973   N  N   . GLY A  1 126 ? 3.746   -9.336  13.008   1.00 166.31 ? 126  GLY A N   1 
ATOM   974   C  CA  . GLY A  1 126 ? 4.747   -9.355  14.053   1.00 166.93 ? 126  GLY A CA  1 
ATOM   975   C  C   . GLY A  1 126 ? 6.115   -9.805  13.584   1.00 180.62 ? 126  GLY A C   1 
ATOM   976   O  O   . GLY A  1 126 ? 6.236   -10.653 12.693   1.00 194.36 ? 126  GLY A O   1 
ATOM   977   N  N   . THR A  1 127 ? 7.156   -9.263  14.210   1.00 173.44 ? 127  THR A N   1 
ATOM   978   C  CA  . THR A  1 127 ? 8.525   -9.617  13.878   1.00 177.39 ? 127  THR A CA  1 
ATOM   979   C  C   . THR A  1 127 ? 9.374   -9.545  15.136   1.00 177.88 ? 127  THR A C   1 
ATOM   980   O  O   . THR A  1 127 ? 9.044   -8.832  16.087   1.00 175.63 ? 127  THR A O   1 
ATOM   981   C  CB  . THR A  1 127 ? 9.105   -8.695  12.800   1.00 191.04 ? 127  THR A CB  1 
ATOM   982   O  OG1 . THR A  1 127 ? 10.379  -9.196  12.377   1.00 206.62 ? 127  THR A OG1 1 
ATOM   983   C  CG2 . THR A  1 127 ? 9.271   -7.279  13.336   1.00 181.35 ? 127  THR A CG2 1 
ATOM   984   N  N   . CYS A  1 128 ? 10.456  -10.316 15.142   1.00 185.50 ? 128  CYS A N   1 
ATOM   985   C  CA  . CYS A  1 128 ? 11.397  -10.324 16.249   1.00 182.47 ? 128  CYS A CA  1 
ATOM   986   C  C   . CYS A  1 128 ? 12.813  -10.110 15.734   1.00 188.12 ? 128  CYS A C   1 
ATOM   987   O  O   . CYS A  1 128 ? 13.134  -10.440 14.588   1.00 191.10 ? 128  CYS A O   1 
ATOM   988   C  CB  . CYS A  1 128 ? 11.309  -11.632 17.033   1.00 181.66 ? 128  CYS A CB  1 
ATOM   989   S  SG  . CYS A  1 128 ? 9.641   -11.978 17.666   1.00 213.58 ? 128  CYS A SG  1 
ATOM   990   N  N   . PHE A  1 129 ? 13.648  -9.519  16.583   1.00 189.86 ? 129  PHE A N   1 
ATOM   991   C  CA  . PHE A  1 129 ? 15.077  -9.402  16.336   1.00 197.50 ? 129  PHE A CA  1 
ATOM   992   C  C   . PHE A  1 129 ? 15.847  -10.179 17.398   1.00 196.81 ? 129  PHE A C   1 
ATOM   993   O  O   . PHE A  1 129 ? 15.591  -10.025 18.598   1.00 194.21 ? 129  PHE A O   1 
ATOM   994   C  CB  . PHE A  1 129 ? 15.500  -7.933  16.308   1.00 207.52 ? 129  PHE A CB  1 
ATOM   995   C  CG  . PHE A  1 129 ? 15.011  -7.191  15.092   1.00 210.60 ? 129  PHE A CG  1 
ATOM   996   C  CD1 . PHE A  1 129 ? 15.744  -7.198  13.917   1.00 220.88 ? 129  PHE A CD1 1 
ATOM   997   C  CD2 . PHE A  1 129 ? 13.804  -6.508  15.120   1.00 193.67 ? 129  PHE A CD2 1 
ATOM   998   C  CE1 . PHE A  1 129 ? 15.294  -6.520  12.801   1.00 214.68 ? 129  PHE A CE1 1 
ATOM   999   C  CE2 . PHE A  1 129 ? 13.346  -5.828  14.006   1.00 194.25 ? 129  PHE A CE2 1 
ATOM   1000  C  CZ  . PHE A  1 129 ? 14.092  -5.834  12.845   1.00 198.93 ? 129  PHE A CZ  1 
ATOM   1001  N  N   . LEU A  1 130 ? 16.773  -11.024 16.951   1.00 207.93 ? 130  LEU A N   1 
ATOM   1002  C  CA  . LEU A  1 130 ? 17.601  -11.853 17.820   1.00 203.35 ? 130  LEU A CA  1 
ATOM   1003  C  C   . LEU A  1 130 ? 19.057  -11.416 17.730   1.00 209.56 ? 130  LEU A C   1 
ATOM   1004  O  O   . LEU A  1 130 ? 19.593  -11.255 16.628   1.00 213.52 ? 130  LEU A O   1 
ATOM   1005  C  CB  . LEU A  1 130 ? 17.478  -13.328 17.442   1.00 203.80 ? 130  LEU A CB  1 
ATOM   1006  C  CG  . LEU A  1 130 ? 18.388  -14.293 18.202   1.00 206.94 ? 130  LEU A CG  1 
ATOM   1007  C  CD1 . LEU A  1 130 ? 18.125  -14.232 19.698   1.00 203.76 ? 130  LEU A CD1 1 
ATOM   1008  C  CD2 . LEU A  1 130 ? 18.211  -15.706 17.672   1.00 207.80 ? 130  LEU A CD2 1 
ATOM   1009  N  N   . GLN A  1 131 ? 19.697  -11.233 18.887   1.00 216.35 ? 131  GLN A N   1 
ATOM   1010  C  CA  . GLN A  1 131 ? 21.097  -10.823 18.962   1.00 254.22 ? 131  GLN A CA  1 
ATOM   1011  C  C   . GLN A  1 131 ? 21.893  -11.885 19.714   1.00 249.32 ? 131  GLN A C   1 
ATOM   1012  O  O   . GLN A  1 131 ? 21.770  -12.015 20.937   1.00 243.16 ? 131  GLN A O   1 
ATOM   1013  C  CB  . GLN A  1 131 ? 21.248  -9.459  19.631   1.00 248.19 ? 131  GLN A CB  1 
ATOM   1014  C  CG  . GLN A  1 131 ? 22.679  -8.942  19.621   1.00 239.80 ? 131  GLN A CG  1 
ATOM   1015  C  CD  . GLN A  1 131 ? 22.772  -7.469  19.952   1.00 235.61 ? 131  GLN A CD  1 
ATOM   1016  O  OE1 . GLN A  1 131 ? 21.757  -6.781  20.052   1.00 230.27 ? 131  GLN A OE1 1 
ATOM   1017  N  NE2 . GLN A  1 131 ? 23.994  -6.978  20.137   1.00 235.08 ? 131  GLN A NE2 1 
ATOM   1018  N  N   . ASP A  1 132 ? 22.703  -12.647 18.983   1.00 230.64 ? 132  ASP A N   1 
ATOM   1019  C  CA  . ASP A  1 132 ? 23.584  -13.630 19.601   1.00 234.50 ? 132  ASP A CA  1 
ATOM   1020  C  C   . ASP A  1 132 ? 25.021  -13.125 19.594   1.00 255.31 ? 132  ASP A C   1 
ATOM   1021  O  O   . ASP A  1 132 ? 25.909  -13.757 19.011   1.00 259.11 ? 132  ASP A O   1 
ATOM   1022  C  CB  . ASP A  1 132 ? 23.486  -14.977 18.880   1.00 254.66 ? 132  ASP A CB  1 
ATOM   1023  C  CG  . ASP A  1 132 ? 24.174  -16.096 19.641   1.00 283.60 ? 132  ASP A CG  1 
ATOM   1024  O  OD1 . ASP A  1 132 ? 24.145  -16.068 20.890   1.00 294.57 ? 132  ASP A OD1 1 
ATOM   1025  O  OD2 . ASP A  1 132 ? 24.749  -16.998 18.993   1.00 297.43 ? 132  ASP A OD2 1 
ATOM   1026  N  N   . GLY A  1 133 ? 25.258  -11.980 20.227   1.00 246.75 ? 133  GLY A N   1 
ATOM   1027  C  CA  . GLY A  1 133 ? 26.584  -11.401 20.264   1.00 250.25 ? 133  GLY A CA  1 
ATOM   1028  C  C   . GLY A  1 133 ? 26.698  -10.239 19.304   1.00 252.34 ? 133  GLY A C   1 
ATOM   1029  O  O   . GLY A  1 133 ? 26.293  -9.114  19.616   1.00 258.06 ? 133  GLY A O   1 
ATOM   1030  N  N   . THR A  1 134 ? 27.245  -10.506 18.122   1.00 248.40 ? 134  THR A N   1 
ATOM   1031  C  CA  . THR A  1 134 ? 27.412  -9.494  17.090   1.00 250.71 ? 134  THR A CA  1 
ATOM   1032  C  C   . THR A  1 134 ? 26.295  -9.541  16.058   1.00 246.46 ? 134  THR A C   1 
ATOM   1033  O  O   . THR A  1 134 ? 25.698  -8.510  15.736   1.00 243.87 ? 134  THR A O   1 
ATOM   1034  C  CB  . THR A  1 134 ? 28.763  -9.672  16.389   1.00 259.23 ? 134  THR A CB  1 
ATOM   1035  O  OG1 . THR A  1 134 ? 28.722  -10.850 15.574   1.00 260.98 ? 134  THR A OG1 1 
ATOM   1036  C  CG2 . THR A  1 134 ? 29.875  -9.814  17.411   1.00 266.92 ? 134  THR A CG2 1 
ATOM   1037  N  N   . LYS A  1 135 ? 25.993  -10.729 15.545   1.00 245.96 ? 135  LYS A N   1 
ATOM   1038  C  CA  . LYS A  1 135 ? 24.991  -10.868 14.498   1.00 242.70 ? 135  LYS A CA  1 
ATOM   1039  C  C   . LYS A  1 135 ? 23.604  -10.540 15.031   1.00 234.71 ? 135  LYS A C   1 
ATOM   1040  O  O   . LYS A  1 135 ? 23.212  -11.000 16.107   1.00 231.05 ? 135  LYS A O   1 
ATOM   1041  C  CB  . LYS A  1 135 ? 25.016  -12.284 13.928   1.00 244.41 ? 135  LYS A CB  1 
ATOM   1042  C  CG  . LYS A  1 135 ? 26.365  -12.726 13.377   1.00 252.78 ? 135  LYS A CG  1 
ATOM   1043  C  CD  . LYS A  1 135 ? 26.740  -11.935 12.126   1.00 256.97 ? 135  LYS A CD  1 
ATOM   1044  C  CE  . LYS A  1 135 ? 28.139  -12.289 11.632   1.00 265.88 ? 135  LYS A CE  1 
ATOM   1045  N  NZ  . LYS A  1 135 ? 28.440  -11.695 10.298   1.00 270.27 ? 135  LYS A NZ  1 
ATOM   1046  N  N   . THR A  1 136 ? 22.875  -9.713  14.286   1.00 232.39 ? 136  THR A N   1 
ATOM   1047  C  CA  . THR A  1 136 ? 21.483  -9.394  14.574   1.00 225.29 ? 136  THR A CA  1 
ATOM   1048  C  C   . THR A  1 136 ? 20.639  -9.884  13.406   1.00 223.59 ? 136  THR A C   1 
ATOM   1049  O  O   . THR A  1 136 ? 20.858  -9.466  12.265   1.00 235.62 ? 136  THR A O   1 
ATOM   1050  C  CB  . THR A  1 136 ? 21.296  -7.893  14.786   1.00 224.20 ? 136  THR A CB  1 
ATOM   1051  O  OG1 . THR A  1 136 ? 22.068  -7.467  15.915   1.00 225.97 ? 136  THR A OG1 1 
ATOM   1052  C  CG2 . THR A  1 136 ? 19.835  -7.573  15.019   1.00 217.35 ? 136  THR A CG2 1 
ATOM   1053  N  N   . VAL A  1 137 ? 19.668  -10.755 13.689   1.00 218.82 ? 137  VAL A N   1 
ATOM   1054  C  CA  . VAL A  1 137 ? 18.829  -11.339 12.651   1.00 217.26 ? 137  VAL A CA  1 
ATOM   1055  C  C   . VAL A  1 137 ? 17.377  -10.976 12.921   1.00 210.50 ? 137  VAL A C   1 
ATOM   1056  O  O   . VAL A  1 137 ? 16.995  -10.624 14.038   1.00 206.81 ? 137  VAL A O   1 
ATOM   1057  C  CB  . VAL A  1 137 ? 18.984  -12.873 12.551   1.00 218.65 ? 137  VAL A CB  1 
ATOM   1058  C  CG1 . VAL A  1 137 ? 20.439  -13.254 12.353   1.00 242.53 ? 137  VAL A CG1 1 
ATOM   1059  C  CG2 . VAL A  1 137 ? 18.410  -13.556 13.787   1.00 214.05 ? 137  VAL A CG2 1 
ATOM   1060  N  N   . GLU A  1 138 ? 16.568  -11.054 11.869   1.00 209.37 ? 138  GLU A N   1 
ATOM   1061  C  CA  . GLU A  1 138 ? 15.128  -10.863 11.959   1.00 203.40 ? 138  GLU A CA  1 
ATOM   1062  C  C   . GLU A  1 138 ? 14.424  -12.214 11.996   1.00 200.90 ? 138  GLU A C   1 
ATOM   1063  O  O   . GLU A  1 138 ? 14.894  -13.197 11.415   1.00 204.23 ? 138  GLU A O   1 
ATOM   1064  C  CB  . GLU A  1 138 ? 14.605  -10.040 10.783   1.00 203.77 ? 138  GLU A CB  1 
ATOM   1065  C  CG  . GLU A  1 138 ? 13.192  -9.519  10.972   1.00 198.18 ? 138  GLU A CG  1 
ATOM   1066  C  CD  . GLU A  1 138 ? 12.701  -8.734  9.777    1.00 201.52 ? 138  GLU A CD  1 
ATOM   1067  O  OE1 . GLU A  1 138 ? 13.326  -8.844  8.701    1.00 212.83 ? 138  GLU A OE1 1 
ATOM   1068  O  OE2 . GLU A  1 138 ? 11.681  -8.025  9.905    1.00 199.19 ? 138  GLU A OE2 1 
ATOM   1069  N  N   . TYR A  1 139 ? 13.283  -12.254 12.683   1.00 202.92 ? 139  TYR A N   1 
ATOM   1070  C  CA  . TYR A  1 139 ? 12.504  -13.487 12.828   1.00 207.09 ? 139  TYR A CA  1 
ATOM   1071  C  C   . TYR A  1 139 ? 11.020  -13.143 12.765   1.00 194.59 ? 139  TYR A C   1 
ATOM   1072  O  O   . TYR A  1 139 ? 10.466  -12.577 13.712   1.00 183.78 ? 139  TYR A O   1 
ATOM   1073  C  CB  . TYR A  1 139 ? 12.845  -14.209 14.124   1.00 213.66 ? 139  TYR A CB  1 
ATOM   1074  C  CG  . TYR A  1 139 ? 12.042  -15.473 14.338   1.00 208.00 ? 139  TYR A CG  1 
ATOM   1075  C  CD1 . TYR A  1 139 ? 12.086  -16.512 13.417   1.00 208.79 ? 139  TYR A CD1 1 
ATOM   1076  C  CD2 . TYR A  1 139 ? 11.252  -15.633 15.467   1.00 184.49 ? 139  TYR A CD2 1 
ATOM   1077  C  CE1 . TYR A  1 139 ? 11.356  -17.671 13.611   1.00 195.11 ? 139  TYR A CE1 1 
ATOM   1078  C  CE2 . TYR A  1 139 ? 10.523  -16.789 15.670   1.00 182.43 ? 139  TYR A CE2 1 
ATOM   1079  C  CZ  . TYR A  1 139 ? 10.578  -17.804 14.741   1.00 185.02 ? 139  TYR A CZ  1 
ATOM   1080  O  OH  . TYR A  1 139 ? 9.851   -18.954 14.945   1.00 183.27 ? 139  TYR A OH  1 
ATOM   1081  N  N   . ALA A  1 140 ? 10.384  -13.474 11.643   1.00 201.98 ? 140  ALA A N   1 
ATOM   1082  C  CA  . ALA A  1 140 ? 8.954   -13.241 11.439   1.00 207.80 ? 140  ALA A CA  1 
ATOM   1083  C  C   . ALA A  1 140 ? 8.328   -14.511 10.879   1.00 219.35 ? 140  ALA A C   1 
ATOM   1084  O  O   . ALA A  1 140 ? 8.102   -14.626 9.666    1.00 231.90 ? 140  ALA A O   1 
ATOM   1085  C  CB  . ALA A  1 140 ? 8.715   -12.048 10.515   1.00 205.58 ? 140  ALA A CB  1 
ATOM   1086  N  N   . PRO A  1 141 ? 8.027   -15.490 11.741   1.00 211.18 ? 141  PRO A N   1 
ATOM   1087  C  CA  . PRO A  1 141 ? 7.472   -16.762 11.253   1.00 202.53 ? 141  PRO A CA  1 
ATOM   1088  C  C   . PRO A  1 141 ? 6.044   -16.649 10.766   1.00 194.41 ? 141  PRO A C   1 
ATOM   1089  O  O   . PRO A  1 141 ? 5.554   -17.581 10.113   1.00 198.50 ? 141  PRO A O   1 
ATOM   1090  C  CB  . PRO A  1 141 ? 7.566   -17.678 12.481   1.00 197.81 ? 141  PRO A CB  1 
ATOM   1091  C  CG  . PRO A  1 141 ? 7.461   -16.741 13.631   1.00 201.35 ? 141  PRO A CG  1 
ATOM   1092  C  CD  . PRO A  1 141 ? 8.173   -15.478 13.206   1.00 208.14 ? 141  PRO A CD  1 
ATOM   1093  N  N   . CYS A  1 142 ? 5.358   -15.552 11.084   1.00 174.73 ? 142  CYS A N   1 
ATOM   1094  C  CA  . CYS A  1 142 ? 4.004   -15.303 10.621   1.00 174.13 ? 142  CYS A CA  1 
ATOM   1095  C  C   . CYS A  1 142 ? 3.967   -14.426 9.376    1.00 180.56 ? 142  CYS A C   1 
ATOM   1096  O  O   . CYS A  1 142 ? 2.907   -14.289 8.754    1.00 185.99 ? 142  CYS A O   1 
ATOM   1097  C  CB  . CYS A  1 142 ? 3.187   -14.674 11.754   1.00 190.17 ? 142  CYS A CB  1 
ATOM   1098  S  SG  . CYS A  1 142 ? 2.711   -15.917 12.998   1.00 192.31 ? 142  CYS A SG  1 
ATOM   1099  N  N   . ARG A  1 143 ? 5.093   -13.817 9.014    1.00 187.79 ? 143  ARG A N   1 
ATOM   1100  C  CA  . ARG A  1 143 ? 5.235   -13.090 7.757    1.00 195.32 ? 143  ARG A CA  1 
ATOM   1101  C  C   . ARG A  1 143 ? 5.435   -14.113 6.641    1.00 211.51 ? 143  ARG A C   1 
ATOM   1102  O  O   . ARG A  1 143 ? 6.554   -14.390 6.203    1.00 218.35 ? 143  ARG A O   1 
ATOM   1103  C  CB  . ARG A  1 143 ? 6.408   -12.125 7.841    1.00 196.38 ? 143  ARG A CB  1 
ATOM   1104  C  CG  . ARG A  1 143 ? 6.499   -11.115 6.721    1.00 203.29 ? 143  ARG A CG  1 
ATOM   1105  C  CD  . ARG A  1 143 ? 7.668   -10.176 6.967    1.00 203.80 ? 143  ARG A CD  1 
ATOM   1106  N  NE  . ARG A  1 143 ? 8.945   -10.885 6.905    1.00 214.89 ? 143  ARG A NE  1 
ATOM   1107  C  CZ  . ARG A  1 143 ? 10.082  -10.430 7.422    1.00 231.95 ? 143  ARG A CZ  1 
ATOM   1108  N  NH1 . ARG A  1 143 ? 10.107  -9.260  8.045    1.00 222.59 ? 143  ARG A NH1 1 
ATOM   1109  N  NH2 . ARG A  1 143 ? 11.197  -11.145 7.316    1.00 242.85 ? 143  ARG A NH2 1 
ATOM   1110  N  N   . SER A  1 144 ? 4.327   -14.705 6.191    1.00 215.41 ? 144  SER A N   1 
ATOM   1111  C  CA  . SER A  1 144 ? 4.363   -15.788 5.210    1.00 226.71 ? 144  SER A CA  1 
ATOM   1112  C  C   . SER A  1 144 ? 3.496   -15.443 3.996    1.00 237.50 ? 144  SER A C   1 
ATOM   1113  O  O   . SER A  1 144 ? 3.009   -14.319 3.847    1.00 248.12 ? 144  SER A O   1 
ATOM   1114  C  CB  . SER A  1 144 ? 3.906   -17.103 5.851    1.00 214.62 ? 144  SER A CB  1 
ATOM   1115  O  OG  . SER A  1 144 ? 4.097   -18.211 4.985    1.00 216.14 ? 144  SER A OG  1 
ATOM   1116  N  N   . GLN A  1 145 ? 3.277   -16.447 3.140    1.00 233.55 ? 145  GLN A N   1 
ATOM   1117  C  CA  . GLN A  1 145 ? 2.353   -16.334 2.018    1.00 229.63 ? 145  GLN A CA  1 
ATOM   1118  C  C   . GLN A  1 145 ? 0.936   -16.689 2.434    1.00 216.44 ? 145  GLN A C   1 
ATOM   1119  O  O   . GLN A  1 145 ? -0.000  -16.495 1.650    1.00 214.08 ? 145  GLN A O   1 
ATOM   1120  C  CB  . GLN A  1 145 ? 2.785   -17.251 0.857    1.00 240.98 ? 145  GLN A CB  1 
ATOM   1121  C  CG  . GLN A  1 145 ? 4.241   -17.120 0.383    1.00 247.14 ? 145  GLN A CG  1 
ATOM   1122  C  CD  . GLN A  1 145 ? 4.650   -15.698 0.048    1.00 240.31 ? 145  GLN A CD  1 
ATOM   1123  O  OE1 . GLN A  1 145 ? 5.694   -15.222 0.495    1.00 239.18 ? 145  GLN A OE1 1 
ATOM   1124  N  NE2 . GLN A  1 145 ? 3.847   -15.024 -0.766   1.00 244.16 ? 145  GLN A NE2 1 
ATOM   1125  N  N   . ASP A  1 146 ? 0.773   -17.209 3.650    1.00 212.97 ? 146  ASP A N   1 
ATOM   1126  C  CA  . ASP A  1 146 ? -0.528  -17.468 4.261    1.00 202.54 ? 146  ASP A CA  1 
ATOM   1127  C  C   . ASP A  1 146 ? -1.050  -16.141 4.797    1.00 192.94 ? 146  ASP A C   1 
ATOM   1128  O  O   . ASP A  1 146 ? -0.896  -15.797 5.972    1.00 192.27 ? 146  ASP A O   1 
ATOM   1129  C  CB  . ASP A  1 146 ? -0.406  -18.516 5.358    1.00 194.35 ? 146  ASP A CB  1 
ATOM   1130  C  CG  . ASP A  1 146 ? -1.749  -18.945 5.906    1.00 189.35 ? 146  ASP A CG  1 
ATOM   1131  O  OD1 . ASP A  1 146 ? -2.767  -18.810 5.195    1.00 193.27 ? 146  ASP A OD1 1 
ATOM   1132  O  OD2 . ASP A  1 146 ? -1.785  -19.407 7.064    1.00 191.55 ? 146  ASP A OD2 1 
ATOM   1133  N  N   . ILE A  1 147 ? -1.657  -15.371 3.896    1.00 196.84 ? 147  ILE A N   1 
ATOM   1134  C  CA  . ILE A  1 147 ? -2.028  -13.989 4.181    1.00 200.88 ? 147  ILE A CA  1 
ATOM   1135  C  C   . ILE A  1 147 ? -3.459  -13.896 4.694    1.00 184.84 ? 147  ILE A C   1 
ATOM   1136  O  O   . ILE A  1 147 ? -4.153  -14.910 4.834    1.00 181.94 ? 147  ILE A O   1 
ATOM   1137  C  CB  . ILE A  1 147 ? -1.852  -13.102 2.935    1.00 215.34 ? 147  ILE A CB  1 
ATOM   1138  C  CG1 . ILE A  1 147 ? -2.881  -13.475 1.863    1.00 214.59 ? 147  ILE A CG1 1 
ATOM   1139  C  CG2 . ILE A  1 147 ? -0.437  -13.230 2.399    1.00 219.15 ? 147  ILE A CG2 1 
ATOM   1140  C  CD1 . ILE A  1 147 ? -2.744  -12.683 0.582    1.00 217.61 ? 147  ILE A CD1 1 
ATOM   1141  N  N   . ASP A  1 148 ? -3.890  -12.665 4.982    1.00 195.28 ? 148  ASP A N   1 
ATOM   1142  C  CA  . ASP A  1 148 ? -5.238  -12.338 5.432    1.00 201.06 ? 148  ASP A CA  1 
ATOM   1143  C  C   . ASP A  1 148 ? -5.550  -12.904 6.812    1.00 190.18 ? 148  ASP A C   1 
ATOM   1144  O  O   . ASP A  1 148 ? -4.766  -13.678 7.372    1.00 179.03 ? 148  ASP A O   1 
ATOM   1145  C  CB  . ASP A  1 148 ? -6.278  -12.828 4.420    1.00 212.35 ? 148  ASP A CB  1 
ATOM   1146  C  CG  . ASP A  1 148 ? -7.500  -11.937 4.367    1.00 198.25 ? 148  ASP A CG  1 
ATOM   1147  O  OD1 . ASP A  1 148 ? -7.815  -11.302 5.395    1.00 185.13 ? 148  ASP A OD1 1 
ATOM   1148  O  OD2 . ASP A  1 148 ? -8.142  -11.871 3.299    1.00 199.06 ? 148  ASP A OD2 1 
ATOM   1149  N  N   . ALA A  1 149 ? -6.694  -12.498 7.373    1.00 191.56 ? 149  ALA A N   1 
ATOM   1150  C  CA  . ALA A  1 149 ? -7.075  -12.952 8.705    1.00 179.45 ? 149  ALA A CA  1 
ATOM   1151  C  C   . ALA A  1 149 ? -7.197  -14.469 8.749    1.00 184.89 ? 149  ALA A C   1 
ATOM   1152  O  O   . ALA A  1 149 ? -6.902  -15.092 9.775    1.00 181.31 ? 149  ALA A O   1 
ATOM   1153  C  CB  . ALA A  1 149 ? -8.387  -12.291 9.129    1.00 163.35 ? 149  ALA A CB  1 
ATOM   1154  N  N   . ASP A  1 150 ? -7.648  -15.076 7.646    1.00 194.73 ? 150  ASP A N   1 
ATOM   1155  C  CA  . ASP A  1 150 ? -7.762  -16.529 7.573    1.00 189.42 ? 150  ASP A CA  1 
ATOM   1156  C  C   . ASP A  1 150 ? -6.422  -17.220 7.786    1.00 190.18 ? 150  ASP A C   1 
ATOM   1157  O  O   . ASP A  1 150 ? -6.382  -18.376 8.221    1.00 188.80 ? 150  ASP A O   1 
ATOM   1158  C  CB  . ASP A  1 150 ? -8.353  -16.936 6.227    1.00 193.44 ? 150  ASP A CB  1 
ATOM   1159  C  CG  . ASP A  1 150 ? -9.566  -16.116 5.862    1.00 207.71 ? 150  ASP A CG  1 
ATOM   1160  O  OD1 . ASP A  1 150 ? -10.674 -16.457 6.325    1.00 220.81 ? 150  ASP A OD1 1 
ATOM   1161  O  OD2 . ASP A  1 150 ? -9.408  -15.127 5.116    1.00 196.68 ? 150  ASP A OD2 1 
ATOM   1162  N  N   . GLY A  1 151 ? -5.322  -16.548 7.455    1.00 195.88 ? 151  GLY A N   1 
ATOM   1163  C  CA  . GLY A  1 151 ? -4.010  -17.123 7.655    1.00 194.96 ? 151  GLY A CA  1 
ATOM   1164  C  C   . GLY A  1 151 ? -3.277  -16.517 8.834    1.00 196.27 ? 151  GLY A C   1 
ATOM   1165  O  O   . GLY A  1 151 ? -3.835  -16.393 9.930    1.00 192.16 ? 151  GLY A O   1 
ATOM   1166  N  N   . GLN A  1 152 ? -2.031  -16.105 8.608    1.00 172.48 ? 152  GLN A N   1 
ATOM   1167  C  CA  . GLN A  1 152 ? -1.179  -15.555 9.652    1.00 162.89 ? 152  GLN A CA  1 
ATOM   1168  C  C   . GLN A  1 152 ? -1.020  -14.047 9.507    1.00 163.00 ? 152  GLN A C   1 
ATOM   1169  O  O   . GLN A  1 152 ? -0.095  -13.464 10.079   1.00 163.41 ? 152  GLN A O   1 
ATOM   1170  C  CB  . GLN A  1 152 ? 0.184   -16.247 9.630    1.00 165.94 ? 152  GLN A CB  1 
ATOM   1171  C  CG  . GLN A  1 152 ? 0.131   -17.743 9.913    1.00 166.57 ? 152  GLN A CG  1 
ATOM   1172  C  CD  . GLN A  1 152 ? 1.473   -18.430 9.705    1.00 170.67 ? 152  GLN A CD  1 
ATOM   1173  O  OE1 . GLN A  1 152 ? 2.431   -17.819 9.233    1.00 190.73 ? 152  GLN A OE1 1 
ATOM   1174  N  NE2 . GLN A  1 152 ? 1.543   -19.709 10.050   1.00 170.87 ? 152  GLN A NE2 1 
ATOM   1175  N  N   . GLY A  1 153 ? -1.905  -13.411 8.734    1.00 194.78 ? 153  GLY A N   1 
ATOM   1176  C  CA  . GLY A  1 153 ? -1.806  -11.980 8.510    1.00 195.95 ? 153  GLY A CA  1 
ATOM   1177  C  C   . GLY A  1 153 ? -1.955  -11.164 9.775    1.00 192.11 ? 153  GLY A C   1 
ATOM   1178  O  O   . GLY A  1 153 ? -1.319  -10.117 9.924    1.00 202.94 ? 153  GLY A O   1 
ATOM   1179  N  N   . PHE A  1 154 ? -2.791  -11.625 10.703   1.00 168.02 ? 154  PHE A N   1 
ATOM   1180  C  CA  . PHE A  1 154 ? -3.039  -10.915 11.949   1.00 157.49 ? 154  PHE A CA  1 
ATOM   1181  C  C   . PHE A  1 154 ? -2.518  -11.710 13.141   1.00 164.75 ? 154  PHE A C   1 
ATOM   1182  O  O   . PHE A  1 154 ? -3.024  -11.587 14.259   1.00 150.65 ? 154  PHE A O   1 
ATOM   1183  C  CB  . PHE A  1 154 ? -4.522  -10.589 12.083   1.00 154.00 ? 154  PHE A CB  1 
ATOM   1184  C  CG  . PHE A  1 154 ? -4.987  -9.528  11.118   1.00 168.17 ? 154  PHE A CG  1 
ATOM   1185  C  CD1 . PHE A  1 154 ? -5.115  -9.813  9.768    1.00 177.11 ? 154  PHE A CD1 1 
ATOM   1186  C  CD2 . PHE A  1 154 ? -5.256  -8.239  11.552   1.00 168.14 ? 154  PHE A CD2 1 
ATOM   1187  C  CE1 . PHE A  1 154 ? -5.527  -8.846  8.876    1.00 165.71 ? 154  PHE A CE1 1 
ATOM   1188  C  CE2 . PHE A  1 154 ? -5.665  -7.263  10.657   1.00 155.88 ? 154  PHE A CE2 1 
ATOM   1189  C  CZ  . PHE A  1 154 ? -5.800  -7.571  9.320    1.00 161.95 ? 154  PHE A CZ  1 
ATOM   1190  N  N   . CYS A  1 155 ? -1.484  -12.519 12.878   1.00 192.15 ? 155  CYS A N   1 
ATOM   1191  C  CA  . CYS A  1 155 ? -0.867  -13.395 13.873   1.00 167.79 ? 155  CYS A CA  1 
ATOM   1192  C  C   . CYS A  1 155 ? -0.272  -12.625 15.048   1.00 159.93 ? 155  CYS A C   1 
ATOM   1193  O  O   . CYS A  1 155 ? -0.366  -13.074 16.197   1.00 153.27 ? 155  CYS A O   1 
ATOM   1194  C  CB  . CYS A  1 155 ? 0.207   -14.241 13.187   1.00 160.65 ? 155  CYS A CB  1 
ATOM   1195  S  SG  . CYS A  1 155 ? 1.429   -14.988 14.275   1.00 158.95 ? 155  CYS A SG  1 
ATOM   1196  N  N   . GLN A  1 156 ? 0.378   -11.489 14.782   1.00 159.63 ? 156  GLN A N   1 
ATOM   1197  C  CA  . GLN A  1 156 ? 1.105   -10.737 15.812   1.00 166.22 ? 156  GLN A CA  1 
ATOM   1198  C  C   . GLN A  1 156 ? 2.126   -11.637 16.512   1.00 173.72 ? 156  GLN A C   1 
ATOM   1199  O  O   . GLN A  1 156 ? 2.169   -11.736 17.742   1.00 172.32 ? 156  GLN A O   1 
ATOM   1200  C  CB  . GLN A  1 156 ? 0.149   -10.090 16.819   1.00 154.37 ? 156  GLN A CB  1 
ATOM   1201  C  CG  . GLN A  1 156 ? -0.855  -9.134  16.188   1.00 168.72 ? 156  GLN A CG  1 
ATOM   1202  C  CD  . GLN A  1 156 ? -1.679  -8.372  17.212   1.00 175.15 ? 156  GLN A CD  1 
ATOM   1203  O  OE1 . GLN A  1 156 ? -2.874  -8.632  17.382   1.00 168.28 ? 156  GLN A OE1 1 
ATOM   1204  N  NE2 . GLN A  1 156 ? -1.047  -7.422  17.897   1.00 168.47 ? 156  GLN A NE2 1 
ATOM   1205  N  N   . GLY A  1 157 ? 2.943   -12.305 15.700   1.00 160.58 ? 157  GLY A N   1 
ATOM   1206  C  CA  . GLY A  1 157 ? 3.957   -13.192 16.244   1.00 161.18 ? 157  GLY A CA  1 
ATOM   1207  C  C   . GLY A  1 157 ? 4.931   -12.438 17.131   1.00 186.88 ? 157  GLY A C   1 
ATOM   1208  O  O   . GLY A  1 157 ? 5.332   -11.309 16.833   1.00 195.80 ? 157  GLY A O   1 
ATOM   1209  N  N   . GLY A  1 158 ? 5.310   -13.072 18.236   1.00 197.54 ? 158  GLY A N   1 
ATOM   1210  C  CA  . GLY A  1 158 ? 6.176   -12.453 19.214   1.00 188.22 ? 158  GLY A CA  1 
ATOM   1211  C  C   . GLY A  1 158 ? 5.444   -11.756 20.333   1.00 176.86 ? 158  GLY A C   1 
ATOM   1212  O  O   . GLY A  1 158 ? 6.076   -11.031 21.114   1.00 170.42 ? 158  GLY A O   1 
ATOM   1213  N  N   . PHE A  1 159 ? 4.128   -11.944 20.427   1.00 156.37 ? 159  PHE A N   1 
ATOM   1214  C  CA  . PHE A  1 159 ? 3.370   -11.347 21.518   1.00 153.69 ? 159  PHE A CA  1 
ATOM   1215  C  C   . PHE A  1 159 ? 3.869   -11.854 22.865   1.00 153.63 ? 159  PHE A C   1 
ATOM   1216  O  O   . PHE A  1 159 ? 3.984   -11.083 23.825   1.00 153.41 ? 159  PHE A O   1 
ATOM   1217  C  CB  . PHE A  1 159 ? 1.879   -11.643 21.319   1.00 158.22 ? 159  PHE A CB  1 
ATOM   1218  C  CG  . PHE A  1 159 ? 0.976   -10.872 22.233   1.00 152.61 ? 159  PHE A CG  1 
ATOM   1219  C  CD1 . PHE A  1 159 ? 0.743   -9.526  22.013   1.00 151.82 ? 159  PHE A CD1 1 
ATOM   1220  C  CD2 . PHE A  1 159 ? 0.348   -11.490 23.296   1.00 146.11 ? 159  PHE A CD2 1 
ATOM   1221  C  CE1 . PHE A  1 159 ? -0.086  -8.805  22.847   1.00 146.90 ? 159  PHE A CE1 1 
ATOM   1222  C  CE2 . PHE A  1 159 ? -0.484  -10.774 24.132   1.00 144.39 ? 159  PHE A CE2 1 
ATOM   1223  C  CZ  . PHE A  1 159 ? -0.701  -9.429  23.907   1.00 144.83 ? 159  PHE A CZ  1 
ATOM   1224  N  N   . SER A  1 160 ? 4.225   -13.135 22.937   1.00 154.28 ? 160  SER A N   1 
ATOM   1225  C  CA  . SER A  1 160 ? 4.873   -13.716 24.102   1.00 155.03 ? 160  SER A CA  1 
ATOM   1226  C  C   . SER A  1 160 ? 5.947   -14.678 23.625   1.00 158.21 ? 160  SER A C   1 
ATOM   1227  O  O   . SER A  1 160 ? 5.755   -15.370 22.621   1.00 158.69 ? 160  SER A O   1 
ATOM   1228  C  CB  . SER A  1 160 ? 3.882   -14.469 24.979   1.00 152.17 ? 160  SER A CB  1 
ATOM   1229  O  OG  . SER A  1 160 ? 3.343   -15.558 24.253   1.00 158.67 ? 160  SER A OG  1 
ATOM   1230  N  N   . ILE A  1 161 ? 7.064   -14.740 24.356   1.00 160.71 ? 161  ILE A N   1 
ATOM   1231  C  CA  . ILE A  1 161 ? 8.207   -15.565 23.986   1.00 164.47 ? 161  ILE A CA  1 
ATOM   1232  C  C   . ILE A  1 161 ? 8.802   -16.205 25.235   1.00 165.62 ? 161  ILE A C   1 
ATOM   1233  O  O   . ILE A  1 161 ? 8.511   -15.810 26.366   1.00 163.97 ? 161  ILE A O   1 
ATOM   1234  C  CB  . ILE A  1 161 ? 9.278   -14.748 23.237   1.00 168.00 ? 161  ILE A CB  1 
ATOM   1235  C  CG1 . ILE A  1 161 ? 9.512   -13.418 23.955   1.00 167.90 ? 161  ILE A CG1 1 
ATOM   1236  C  CG2 . ILE A  1 161 ? 8.862   -14.527 21.791   1.00 167.96 ? 161  ILE A CG2 1 
ATOM   1237  C  CD1 . ILE A  1 161 ? 10.591  -12.567 23.330   1.00 171.68 ? 161  ILE A CD1 1 
ATOM   1238  N  N   . ASP A  1 162 ? 9.642   -17.214 25.009   1.00 176.10 ? 162  ASP A N   1 
ATOM   1239  C  CA  . ASP A  1 162 ? 10.376  -17.916 26.060   1.00 179.23 ? 162  ASP A CA  1 
ATOM   1240  C  C   . ASP A  1 162 ? 11.427  -18.799 25.399   1.00 175.49 ? 162  ASP A C   1 
ATOM   1241  O  O   . ASP A  1 162 ? 11.347  -19.097 24.203   1.00 176.37 ? 162  ASP A O   1 
ATOM   1242  C  CB  . ASP A  1 162 ? 9.449   -18.751 26.955   1.00 184.05 ? 162  ASP A CB  1 
ATOM   1243  C  CG  . ASP A  1 162 ? 9.964   -18.878 28.386   1.00 178.35 ? 162  ASP A CG  1 
ATOM   1244  O  OD1 . ASP A  1 162 ? 11.171  -18.643 28.608   1.00 180.99 ? 162  ASP A OD1 1 
ATOM   1245  O  OD2 . ASP A  1 162 ? 9.162   -19.224 29.284   1.00 166.66 ? 162  ASP A OD2 1 
ATOM   1246  N  N   . PHE A  1 163 ? 12.420  -19.203 26.189   1.00 178.74 ? 163  PHE A N   1 
ATOM   1247  C  CA  . PHE A  1 163 ? 13.462  -20.119 25.747   1.00 183.64 ? 163  PHE A CA  1 
ATOM   1248  C  C   . PHE A  1 163 ? 13.350  -21.469 26.448   1.00 184.21 ? 163  PHE A C   1 
ATOM   1249  O  O   . PHE A  1 163 ? 12.981  -21.545 27.625   1.00 182.26 ? 163  PHE A O   1 
ATOM   1250  C  CB  . PHE A  1 163 ? 14.850  -19.524 25.999   1.00 188.11 ? 163  PHE A CB  1 
ATOM   1251  C  CG  . PHE A  1 163 ? 15.255  -18.474 25.004   1.00 189.45 ? 163  PHE A CG  1 
ATOM   1252  C  CD1 . PHE A  1 163 ? 15.721  -18.832 23.751   1.00 192.64 ? 163  PHE A CD1 1 
ATOM   1253  C  CD2 . PHE A  1 163 ? 15.174  -17.129 25.323   1.00 187.90 ? 163  PHE A CD2 1 
ATOM   1254  C  CE1 . PHE A  1 163 ? 16.103  -17.871 22.839   1.00 194.20 ? 163  PHE A CE1 1 
ATOM   1255  C  CE2 . PHE A  1 163 ? 15.552  -16.162 24.413   1.00 189.44 ? 163  PHE A CE2 1 
ATOM   1256  C  CZ  . PHE A  1 163 ? 16.017  -16.533 23.170   1.00 193.52 ? 163  PHE A CZ  1 
ATOM   1257  N  N   . THR A  1 164 ? 13.684  -22.532 25.718   1.00 199.96 ? 164  THR A N   1 
ATOM   1258  C  CA  . THR A  1 164 ? 13.829  -23.865 26.280   1.00 189.25 ? 164  THR A CA  1 
ATOM   1259  C  C   . THR A  1 164 ? 15.280  -24.108 26.681   1.00 199.75 ? 164  THR A C   1 
ATOM   1260  O  O   . THR A  1 164 ? 16.174  -23.303 26.412   1.00 197.58 ? 164  THR A O   1 
ATOM   1261  C  CB  . THR A  1 164 ? 13.398  -24.940 25.281   1.00 190.03 ? 164  THR A CB  1 
ATOM   1262  O  OG1 . THR A  1 164 ? 14.342  -24.996 24.201   1.00 210.83 ? 164  THR A OG1 1 
ATOM   1263  C  CG2 . THR A  1 164 ? 12.022  -24.643 24.728   1.00 184.97 ? 164  THR A CG2 1 
ATOM   1264  N  N   . LYS A  1 165 ? 15.514  -25.254 27.314   1.00 197.31 ? 165  LYS A N   1 
ATOM   1265  C  CA  . LYS A  1 165 ? 16.867  -25.601 27.713   1.00 203.21 ? 165  LYS A CA  1 
ATOM   1266  C  C   . LYS A  1 165 ? 17.662  -26.211 26.567   1.00 220.50 ? 165  LYS A C   1 
ATOM   1267  O  O   . LYS A  1 165 ? 18.880  -26.377 26.693   1.00 255.04 ? 165  LYS A O   1 
ATOM   1268  C  CB  . LYS A  1 165 ? 16.832  -26.563 28.911   1.00 204.09 ? 165  LYS A CB  1 
ATOM   1269  C  CG  . LYS A  1 165 ? 18.195  -26.828 29.559   1.00 225.02 ? 165  LYS A CG  1 
ATOM   1270  C  CD  . LYS A  1 165 ? 18.075  -27.460 30.938   1.00 233.99 ? 165  LYS A CD  1 
ATOM   1271  C  CE  . LYS A  1 165 ? 19.448  -27.856 31.472   1.00 216.99 ? 165  LYS A CE  1 
ATOM   1272  N  NZ  . LYS A  1 165 ? 19.386  -28.564 32.781   1.00 217.83 ? 165  LYS A NZ  1 
ATOM   1273  N  N   . ALA A  1 166 ? 17.018  -26.493 25.434   1.00 208.05 ? 166  ALA A N   1 
ATOM   1274  C  CA  . ALA A  1 166 ? 17.681  -27.105 24.288   1.00 249.06 ? 166  ALA A CA  1 
ATOM   1275  C  C   . ALA A  1 166 ? 17.789  -26.147 23.106   1.00 237.72 ? 166  ALA A C   1 
ATOM   1276  O  O   . ALA A  1 166 ? 17.782  -26.576 21.949   1.00 244.78 ? 166  ALA A O   1 
ATOM   1277  C  CB  . ALA A  1 166 ? 16.953  -28.380 23.866   1.00 240.42 ? 166  ALA A CB  1 
ATOM   1278  N  N   . ASP A  1 167 ? 17.889  -24.848 23.390   1.00 216.79 ? 167  ASP A N   1 
ATOM   1279  C  CA  . ASP A  1 167 ? 18.105  -23.825 22.370   1.00 213.84 ? 167  ASP A CA  1 
ATOM   1280  C  C   . ASP A  1 167 ? 16.998  -23.853 21.318   1.00 207.59 ? 167  ASP A C   1 
ATOM   1281  O  O   . ASP A  1 167 ? 17.249  -23.779 20.114   1.00 210.15 ? 167  ASP A O   1 
ATOM   1282  C  CB  . ASP A  1 167 ? 19.485  -23.958 21.714   1.00 230.51 ? 167  ASP A CB  1 
ATOM   1283  C  CG  . ASP A  1 167 ? 20.625  -23.799 22.699   1.00 222.09 ? 167  ASP A CG  1 
ATOM   1284  O  OD1 . ASP A  1 167 ? 20.424  -24.069 23.899   1.00 249.14 ? 167  ASP A OD1 1 
ATOM   1285  O  OD2 . ASP A  1 167 ? 21.721  -23.377 22.273   1.00 227.14 ? 167  ASP A OD2 1 
ATOM   1286  N  N   . ARG A  1 168 ? 15.760  -23.965 21.784   1.00 207.75 ? 168  ARG A N   1 
ATOM   1287  C  CA  . ARG A  1 168 ? 14.591  -23.768 20.943   1.00 217.19 ? 168  ARG A CA  1 
ATOM   1288  C  C   . ARG A  1 168 ? 13.838  -22.537 21.421   1.00 198.44 ? 168  ARG A C   1 
ATOM   1289  O  O   . ARG A  1 168 ? 13.706  -22.308 22.627   1.00 196.26 ? 168  ARG A O   1 
ATOM   1290  C  CB  . ARG A  1 168 ? 13.665  -24.991 20.956   1.00 202.15 ? 168  ARG A CB  1 
ATOM   1291  C  CG  . ARG A  1 168 ? 14.271  -26.234 20.323   1.00 235.20 ? 168  ARG A CG  1 
ATOM   1292  C  CD  . ARG A  1 168 ? 13.220  -27.296 20.026   1.00 231.89 ? 168  ARG A CD  1 
ATOM   1293  N  NE  . ARG A  1 168 ? 12.356  -26.925 18.907   1.00 203.62 ? 168  ARG A NE  1 
ATOM   1294  C  CZ  . ARG A  1 168 ? 12.320  -27.573 17.747   1.00 207.20 ? 168  ARG A CZ  1 
ATOM   1295  N  NH1 . ARG A  1 168 ? 13.105  -28.623 17.549   1.00 212.22 ? 168  ARG A NH1 1 
ATOM   1296  N  NH2 . ARG A  1 168 ? 11.502  -27.173 16.782   1.00 204.44 ? 168  ARG A NH2 1 
ATOM   1297  N  N   . VAL A  1 169 ? 13.356  -21.746 20.481   1.00 190.31 ? 169  VAL A N   1 
ATOM   1298  C  CA  . VAL A  1 169 ? 12.546  -20.575 20.793   1.00 185.52 ? 169  VAL A CA  1 
ATOM   1299  C  C   . VAL A  1 169 ? 11.075  -20.965 20.771   1.00 180.79 ? 169  VAL A C   1 
ATOM   1300  O  O   . VAL A  1 169 ? 10.622  -21.700 19.885   1.00 181.25 ? 169  VAL A O   1 
ATOM   1301  C  CB  . VAL A  1 169 ? 12.845  -19.437 19.802   1.00 186.64 ? 169  VAL A CB  1 
ATOM   1302  C  CG1 . VAL A  1 169 ? 11.817  -18.330 19.926   1.00 181.79 ? 169  VAL A CG1 1 
ATOM   1303  C  CG2 . VAL A  1 169 ? 14.247  -18.906 20.029   1.00 192.55 ? 169  VAL A CG2 1 
ATOM   1304  N  N   . LEU A  1 170 ? 10.320  -20.469 21.748   1.00 176.57 ? 170  LEU A N   1 
ATOM   1305  C  CA  . LEU A  1 170 ? 8.877   -20.661 21.803   1.00 172.05 ? 170  LEU A CA  1 
ATOM   1306  C  C   . LEU A  1 170 ? 8.189   -19.318 21.590   1.00 168.87 ? 170  LEU A C   1 
ATOM   1307  O  O   . LEU A  1 170 ? 8.347   -18.397 22.401   1.00 167.78 ? 170  LEU A O   1 
ATOM   1308  C  CB  . LEU A  1 170 ? 8.465   -21.280 23.135   1.00 170.08 ? 170  LEU A CB  1 
ATOM   1309  C  CG  . LEU A  1 170 ? 6.965   -21.367 23.370   1.00 165.48 ? 170  LEU A CG  1 
ATOM   1310  C  CD1 . LEU A  1 170 ? 6.310   -22.186 22.274   1.00 165.59 ? 170  LEU A CD1 1 
ATOM   1311  C  CD2 . LEU A  1 170 ? 6.709   -21.984 24.722   1.00 174.23 ? 170  LEU A CD2 1 
ATOM   1312  N  N   . LEU A  1 171 ? 7.415   -19.217 20.515   1.00 167.68 ? 171  LEU A N   1 
ATOM   1313  C  CA  . LEU A  1 171 ? 6.745   -17.984 20.134   1.00 165.24 ? 171  LEU A CA  1 
ATOM   1314  C  C   . LEU A  1 171 ? 5.233   -18.183 20.130   1.00 161.25 ? 171  LEU A C   1 
ATOM   1315  O  O   . LEU A  1 171 ? 4.730   -19.208 19.658   1.00 163.28 ? 171  LEU A O   1 
ATOM   1316  C  CB  . LEU A  1 171 ? 7.230   -17.509 18.756   1.00 168.03 ? 171  LEU A CB  1 
ATOM   1317  C  CG  . LEU A  1 171 ? 6.605   -16.269 18.115   1.00 166.38 ? 171  LEU A CG  1 
ATOM   1318  C  CD1 . LEU A  1 171 ? 7.650   -15.477 17.367   1.00 170.03 ? 171  LEU A CD1 1 
ATOM   1319  C  CD2 . LEU A  1 171 ? 5.490   -16.667 17.163   1.00 164.89 ? 171  LEU A CD2 1 
ATOM   1320  N  N   . GLY A  1 172 ? 4.517   -17.194 20.657   1.00 158.20 ? 172  GLY A N   1 
ATOM   1321  C  CA  . GLY A  1 172 ? 3.065   -17.201 20.690   1.00 154.65 ? 172  GLY A CA  1 
ATOM   1322  C  C   . GLY A  1 172 ? 2.507   -16.185 19.706   1.00 154.00 ? 172  GLY A C   1 
ATOM   1323  O  O   . GLY A  1 172 ? 3.002   -15.059 19.617   1.00 154.85 ? 172  GLY A O   1 
ATOM   1324  N  N   . GLY A  1 173 ? 1.490   -16.614 18.952   1.00 152.85 ? 173  GLY A N   1 
ATOM   1325  C  CA  . GLY A  1 173 ? 0.812   -15.768 17.993   1.00 152.32 ? 173  GLY A CA  1 
ATOM   1326  C  C   . GLY A  1 173 ? -0.699  -15.847 18.120   1.00 149.25 ? 173  GLY A C   1 
ATOM   1327  O  O   . GLY A  1 173 ? -1.348  -16.725 17.543   1.00 160.57 ? 173  GLY A O   1 
ATOM   1328  N  N   . PRO A  1 174 ? -1.286  -14.917 18.882   1.00 147.03 ? 174  PRO A N   1 
ATOM   1329  C  CA  . PRO A  1 174 ? -2.714  -15.033 19.233   1.00 144.30 ? 174  PRO A CA  1 
ATOM   1330  C  C   . PRO A  1 174 ? -3.682  -14.814 18.077   1.00 144.18 ? 174  PRO A C   1 
ATOM   1331  O  O   . PRO A  1 174 ? -4.857  -15.185 18.201   1.00 142.48 ? 174  PRO A O   1 
ATOM   1332  C  CB  . PRO A  1 174 ? -2.895  -13.955 20.312   1.00 142.79 ? 174  PRO A CB  1 
ATOM   1333  C  CG  . PRO A  1 174 ? -1.497  -13.622 20.776   1.00 144.56 ? 174  PRO A CG  1 
ATOM   1334  C  CD  . PRO A  1 174 ? -0.636  -13.797 19.578   1.00 147.28 ? 174  PRO A CD  1 
ATOM   1335  N  N   . GLY A  1 175 ? -3.245  -14.219 16.972   1.00 146.19 ? 175  GLY A N   1 
ATOM   1336  C  CA  . GLY A  1 175 ? -4.148  -13.849 15.895   1.00 146.37 ? 175  GLY A CA  1 
ATOM   1337  C  C   . GLY A  1 175 ? -4.207  -14.794 14.707   1.00 166.61 ? 175  GLY A C   1 
ATOM   1338  O  O   . GLY A  1 175 ? -4.980  -14.564 13.772   1.00 167.96 ? 175  GLY A O   1 
ATOM   1339  N  N   . SER A  1 176 ? -3.346  -15.811 14.692   1.00 178.62 ? 176  SER A N   1 
ATOM   1340  C  CA  . SER A  1 176 ? -3.286  -16.745 13.571   1.00 169.99 ? 176  SER A CA  1 
ATOM   1341  C  C   . SER A  1 176 ? -4.620  -17.460 13.348   1.00 176.13 ? 176  SER A C   1 
ATOM   1342  O  O   . SER A  1 176 ? -5.339  -17.784 14.298   1.00 171.80 ? 176  SER A O   1 
ATOM   1343  C  CB  . SER A  1 176 ? -2.175  -17.770 13.806   1.00 154.08 ? 176  SER A CB  1 
ATOM   1344  O  OG  . SER A  1 176 ? -0.893  -17.184 13.663   1.00 156.31 ? 176  SER A OG  1 
ATOM   1345  N  N   . PHE A  1 177 ? -4.936  -17.716 12.075   1.00 174.20 ? 177  PHE A N   1 
ATOM   1346  C  CA  . PHE A  1 177 ? -6.095  -18.517 11.666   1.00 170.76 ? 177  PHE A CA  1 
ATOM   1347  C  C   . PHE A  1 177 ? -7.396  -17.940 12.227   1.00 164.24 ? 177  PHE A C   1 
ATOM   1348  O  O   . PHE A  1 177 ? -8.150  -18.614 12.930   1.00 162.00 ? 177  PHE A O   1 
ATOM   1349  C  CB  . PHE A  1 177 ? -5.941  -19.985 12.089   1.00 178.37 ? 177  PHE A CB  1 
ATOM   1350  C  CG  . PHE A  1 177 ? -4.600  -20.586 11.767   1.00 191.34 ? 177  PHE A CG  1 
ATOM   1351  C  CD1 . PHE A  1 177 ? -3.994  -20.358 10.545   1.00 205.72 ? 177  PHE A CD1 1 
ATOM   1352  C  CD2 . PHE A  1 177 ? -3.956  -21.402 12.687   1.00 194.55 ? 177  PHE A CD2 1 
ATOM   1353  C  CE1 . PHE A  1 177 ? -2.762  -20.918 10.248   1.00 210.76 ? 177  PHE A CE1 1 
ATOM   1354  C  CE2 . PHE A  1 177 ? -2.726  -21.966 12.396   1.00 201.89 ? 177  PHE A CE2 1 
ATOM   1355  C  CZ  . PHE A  1 177 ? -2.128  -21.723 11.174   1.00 201.75 ? 177  PHE A CZ  1 
ATOM   1356  N  N   . TYR A  1 178 ? -7.658  -16.680 11.879   1.00 160.06 ? 178  TYR A N   1 
ATOM   1357  C  CA  . TYR A  1 178 ? -8.818  -15.949 12.388   1.00 161.77 ? 178  TYR A CA  1 
ATOM   1358  C  C   . TYR A  1 178 ? -8.860  -15.993 13.917   1.00 153.50 ? 178  TYR A C   1 
ATOM   1359  O  O   . TYR A  1 178 ? -9.877  -16.320 14.531   1.00 145.57 ? 178  TYR A O   1 
ATOM   1360  C  CB  . TYR A  1 178 ? -10.118 -16.475 11.775   1.00 162.45 ? 178  TYR A CB  1 
ATOM   1361  C  CG  . TYR A  1 178 ? -10.819 -15.469 10.886   1.00 166.19 ? 178  TYR A CG  1 
ATOM   1362  C  CD1 . TYR A  1 178 ? -11.450 -14.359 11.429   1.00 178.31 ? 178  TYR A CD1 1 
ATOM   1363  C  CD2 . TYR A  1 178 ? -10.853 -15.630 9.507    1.00 167.97 ? 178  TYR A CD2 1 
ATOM   1364  C  CE1 . TYR A  1 178 ? -12.087 -13.435 10.624   1.00 195.69 ? 178  TYR A CE1 1 
ATOM   1365  C  CE2 . TYR A  1 178 ? -11.491 -14.710 8.694    1.00 175.47 ? 178  TYR A CE2 1 
ATOM   1366  C  CZ  . TYR A  1 178 ? -12.106 -13.615 9.256    1.00 190.29 ? 178  TYR A CZ  1 
ATOM   1367  O  OH  . TYR A  1 178 ? -12.742 -12.701 8.444    1.00 195.33 ? 178  TYR A OH  1 
ATOM   1368  N  N   . TRP A  1 179 ? -7.708  -15.696 14.525   1.00 145.05 ? 179  TRP A N   1 
ATOM   1369  C  CA  . TRP A  1 179 ? -7.539  -15.588 15.981   1.00 142.46 ? 179  TRP A CA  1 
ATOM   1370  C  C   . TRP A  1 179 ? -7.796  -16.907 16.700   1.00 141.55 ? 179  TRP A C   1 
ATOM   1371  O  O   . TRP A  1 179 ? -8.119  -16.922 17.891   1.00 139.68 ? 179  TRP A O   1 
ATOM   1372  C  CB  . TRP A  1 179 ? -8.410  -14.485 16.584   1.00 140.71 ? 179  TRP A CB  1 
ATOM   1373  C  CG  . TRP A  1 179 ? -7.985  -13.107 16.199   1.00 141.67 ? 179  TRP A CG  1 
ATOM   1374  C  CD1 . TRP A  1 179 ? -7.073  -12.319 16.837   1.00 141.80 ? 179  TRP A CD1 1 
ATOM   1375  C  CD2 . TRP A  1 179 ? -8.471  -12.346 15.093   1.00 148.46 ? 179  TRP A CD2 1 
ATOM   1376  N  NE1 . TRP A  1 179 ? -6.953  -11.116 16.188   1.00 143.13 ? 179  TRP A NE1 1 
ATOM   1377  C  CE2 . TRP A  1 179 ? -7.805  -11.107 15.115   1.00 147.67 ? 179  TRP A CE2 1 
ATOM   1378  C  CE3 . TRP A  1 179 ? -9.406  -12.593 14.083   1.00 160.32 ? 179  TRP A CE3 1 
ATOM   1379  C  CZ2 . TRP A  1 179 ? -8.043  -10.120 14.165   1.00 151.02 ? 179  TRP A CZ2 1 
ATOM   1380  C  CZ3 . TRP A  1 179 ? -9.639  -11.615 13.144   1.00 145.33 ? 179  TRP A CZ3 1 
ATOM   1381  C  CH2 . TRP A  1 179 ? -8.962  -10.393 13.190   1.00 146.17 ? 179  TRP A CH2 1 
ATOM   1382  N  N   . GLN A  1 180 ? -7.629  -18.030 16.001   1.00 153.83 ? 180  GLN A N   1 
ATOM   1383  C  CA  . GLN A  1 180 ? -7.498  -19.296 16.709   1.00 153.94 ? 180  GLN A CA  1 
ATOM   1384  C  C   . GLN A  1 180 ? -6.224  -19.331 17.540   1.00 155.41 ? 180  GLN A C   1 
ATOM   1385  O  O   . GLN A  1 180 ? -6.179  -20.002 18.578   1.00 172.49 ? 180  GLN A O   1 
ATOM   1386  C  CB  . GLN A  1 180 ? -7.512  -20.470 15.728   1.00 165.68 ? 180  GLN A CB  1 
ATOM   1387  C  CG  . GLN A  1 180 ? -8.854  -20.739 15.080   1.00 164.63 ? 180  GLN A CG  1 
ATOM   1388  C  CD  . GLN A  1 180 ? -8.847  -21.980 14.203   1.00 180.00 ? 180  GLN A CD  1 
ATOM   1389  O  OE1 . GLN A  1 180 ? -7.969  -22.837 14.322   1.00 200.03 ? 180  GLN A OE1 1 
ATOM   1390  N  NE2 . GLN A  1 180 ? -9.831  -22.080 13.314   1.00 174.96 ? 180  GLN A NE2 1 
ATOM   1391  N  N   . GLY A  1 181 ? -5.195  -18.611 17.107   1.00 146.38 ? 181  GLY A N   1 
ATOM   1392  C  CA  . GLY A  1 181 ? -3.894  -18.628 17.737   1.00 153.22 ? 181  GLY A CA  1 
ATOM   1393  C  C   . GLY A  1 181 ? -2.999  -19.738 17.209   1.00 166.15 ? 181  GLY A C   1 
ATOM   1394  O  O   . GLY A  1 181 ? -3.446  -20.709 16.598   1.00 165.41 ? 181  GLY A O   1 
ATOM   1395  N  N   . GLN A  1 182 ? -1.703  -19.587 17.472   1.00 158.92 ? 182  GLN A N   1 
ATOM   1396  C  CA  . GLN A  1 182 ? -0.723  -20.546 16.989   1.00 153.71 ? 182  GLN A CA  1 
ATOM   1397  C  C   . GLN A  1 182 ? 0.533   -20.439 17.837   1.00 154.92 ? 182  GLN A C   1 
ATOM   1398  O  O   . GLN A  1 182 ? 0.907   -19.352 18.282   1.00 154.16 ? 182  GLN A O   1 
ATOM   1399  C  CB  . GLN A  1 182 ? -0.382  -20.310 15.513   1.00 161.00 ? 182  GLN A CB  1 
ATOM   1400  C  CG  . GLN A  1 182 ? 0.464   -21.405 14.879   1.00 171.43 ? 182  GLN A CG  1 
ATOM   1401  C  CD  . GLN A  1 182 ? 0.777   -21.131 13.420   1.00 174.68 ? 182  GLN A CD  1 
ATOM   1402  O  OE1 . GLN A  1 182 ? 0.719   -19.990 12.965   1.00 179.21 ? 182  GLN A OE1 1 
ATOM   1403  N  NE2 . GLN A  1 182 ? 1.081   -22.185 12.672   1.00 180.53 ? 182  GLN A NE2 1 
ATOM   1404  N  N   . LEU A  1 183 ? 1.174   -21.582 18.055   1.00 157.13 ? 183  LEU A N   1 
ATOM   1405  C  CA  . LEU A  1 183 ? 2.485   -21.658 18.681   1.00 159.50 ? 183  LEU A CA  1 
ATOM   1406  C  C   . LEU A  1 183 ? 3.501   -22.109 17.640   1.00 163.82 ? 183  LEU A C   1 
ATOM   1407  O  O   . LEU A  1 183 ? 3.275   -23.103 16.943   1.00 165.58 ? 183  LEU A O   1 
ATOM   1408  C  CB  . LEU A  1 183 ? 2.462   -22.619 19.872   1.00 181.46 ? 183  LEU A CB  1 
ATOM   1409  C  CG  . LEU A  1 183 ? 1.473   -22.298 20.999   1.00 154.86 ? 183  LEU A CG  1 
ATOM   1410  C  CD1 . LEU A  1 183 ? 1.640   -23.276 22.147   1.00 168.95 ? 183  LEU A CD1 1 
ATOM   1411  C  CD2 . LEU A  1 183 ? 1.666   -20.877 21.493   1.00 153.29 ? 183  LEU A CD2 1 
ATOM   1412  N  N   . ILE A  1 184 ? 4.610   -21.380 17.533   1.00 173.65 ? 184  ILE A N   1 
ATOM   1413  C  CA  . ILE A  1 184 ? 5.682   -21.703 16.598   1.00 179.96 ? 184  ILE A CA  1 
ATOM   1414  C  C   . ILE A  1 184 ? 6.976   -21.890 17.382   1.00 173.46 ? 184  ILE A C   1 
ATOM   1415  O  O   . ILE A  1 184 ? 7.313   -21.071 18.245   1.00 172.20 ? 184  ILE A O   1 
ATOM   1416  C  CB  . ILE A  1 184 ? 5.835   -20.616 15.517   1.00 189.10 ? 184  ILE A CB  1 
ATOM   1417  C  CG1 . ILE A  1 184 ? 4.546   -20.499 14.693   1.00 181.18 ? 184  ILE A CG1 1 
ATOM   1418  C  CG2 . ILE A  1 184 ? 7.024   -20.921 14.613   1.00 200.29 ? 184  ILE A CG2 1 
ATOM   1419  C  CD1 . ILE A  1 184 ? 4.640   -19.548 13.511   1.00 176.49 ? 184  ILE A CD1 1 
ATOM   1420  N  N   . SER A  1 185 ? 7.694   -22.971 17.084   1.00 183.89 ? 185  SER A N   1 
ATOM   1421  C  CA  . SER A  1 185 ? 8.966   -23.275 17.725   1.00 187.32 ? 185  SER A CA  1 
ATOM   1422  C  C   . SER A  1 185 ? 10.003  -23.571 16.653   1.00 209.00 ? 185  SER A C   1 
ATOM   1423  O  O   . SER A  1 185 ? 9.785   -24.438 15.801   1.00 214.61 ? 185  SER A O   1 
ATOM   1424  C  CB  . SER A  1 185 ? 8.826   -24.458 18.684   1.00 192.93 ? 185  SER A CB  1 
ATOM   1425  O  OG  . SER A  1 185 ? 10.023  -24.671 19.411   1.00 209.43 ? 185  SER A OG  1 
ATOM   1426  N  N   . ASP A  1 186 ? 11.123  -22.846 16.686   1.00 214.15 ? 186  ASP A N   1 
ATOM   1427  C  CA  . ASP A  1 186 ? 12.222  -23.074 15.757   1.00 216.93 ? 186  ASP A CA  1 
ATOM   1428  C  C   . ASP A  1 186 ? 13.542  -23.214 16.508   1.00 212.56 ? 186  ASP A C   1 
ATOM   1429  O  O   . ASP A  1 186 ? 13.770  -22.563 17.532   1.00 215.96 ? 186  ASP A O   1 
ATOM   1430  C  CB  . ASP A  1 186 ? 12.323  -21.945 14.727   1.00 205.72 ? 186  ASP A CB  1 
ATOM   1431  C  CG  . ASP A  1 186 ? 11.270  -22.056 13.649   1.00 208.67 ? 186  ASP A CG  1 
ATOM   1432  O  OD1 . ASP A  1 186 ? 11.373  -22.985 12.824   1.00 223.79 ? 186  ASP A OD1 1 
ATOM   1433  O  OD2 . ASP A  1 186 ? 10.334  -21.230 13.633   1.00 197.51 ? 186  ASP A OD2 1 
ATOM   1434  N  N   . GLN A  1 187 ? 14.416  -24.065 15.973   1.00 211.45 ? 187  GLN A N   1 
ATOM   1435  C  CA  . GLN A  1 187 ? 15.759  -24.231 16.517   1.00 216.22 ? 187  GLN A CA  1 
ATOM   1436  C  C   . GLN A  1 187 ? 16.621  -23.004 16.228   1.00 218.32 ? 187  GLN A C   1 
ATOM   1437  O  O   . GLN A  1 187 ? 16.644  -22.505 15.098   1.00 220.36 ? 187  GLN A O   1 
ATOM   1438  C  CB  . GLN A  1 187 ? 16.396  -25.485 15.932   1.00 224.80 ? 187  GLN A CB  1 
ATOM   1439  C  CG  . GLN A  1 187 ? 15.683  -26.759 16.335   1.00 225.39 ? 187  GLN A CG  1 
ATOM   1440  C  CD  . GLN A  1 187 ? 16.196  -27.968 15.589   1.00 246.51 ? 187  GLN A CD  1 
ATOM   1441  O  OE1 . GLN A  1 187 ? 16.968  -27.841 14.638   1.00 261.57 ? 187  GLN A OE1 1 
ATOM   1442  N  NE2 . GLN A  1 187 ? 15.777  -29.153 16.021   1.00 233.09 ? 187  GLN A NE2 1 
ATOM   1443  N  N   . VAL A  1 188 ? 17.317  -22.507 17.260   1.00 212.16 ? 188  VAL A N   1 
ATOM   1444  C  CA  . VAL A  1 188 ? 18.121  -21.290 17.118   1.00 217.42 ? 188  VAL A CA  1 
ATOM   1445  C  C   . VAL A  1 188 ? 19.206  -21.462 16.063   1.00 227.72 ? 188  VAL A C   1 
ATOM   1446  O  O   . VAL A  1 188 ? 19.651  -20.481 15.456   1.00 233.16 ? 188  VAL A O   1 
ATOM   1447  C  CB  . VAL A  1 188 ? 18.717  -20.868 18.479   1.00 217.85 ? 188  VAL A CB  1 
ATOM   1448  C  CG1 . VAL A  1 188 ? 17.603  -20.679 19.512   1.00 207.36 ? 188  VAL A CG1 1 
ATOM   1449  C  CG2 . VAL A  1 188 ? 19.769  -21.862 18.954   1.00 219.42 ? 188  VAL A CG2 1 
ATOM   1450  N  N   . ALA A  1 189 ? 19.655  -22.698 15.829   1.00 231.48 ? 189  ALA A N   1 
ATOM   1451  C  CA  . ALA A  1 189 ? 20.647  -22.920 14.786   1.00 238.52 ? 189  ALA A CA  1 
ATOM   1452  C  C   . ALA A  1 189 ? 20.052  -22.667 13.411   1.00 238.10 ? 189  ALA A C   1 
ATOM   1453  O  O   . ALA A  1 189 ? 20.764  -22.233 12.499   1.00 244.59 ? 189  ALA A O   1 
ATOM   1454  C  CB  . ALA A  1 189 ? 21.210  -24.339 14.873   1.00 243.60 ? 189  ALA A CB  1 
ATOM   1455  N  N   . GLU A  1 190 ? 18.758  -22.943 13.248   1.00 235.00 ? 190  GLU A N   1 
ATOM   1456  C  CA  . GLU A  1 190 ? 18.069  -22.703 11.986   1.00 239.88 ? 190  GLU A CA  1 
ATOM   1457  C  C   . GLU A  1 190 ? 17.634  -21.247 11.803   1.00 232.82 ? 190  GLU A C   1 
ATOM   1458  O  O   . GLU A  1 190 ? 17.563  -20.772 10.665   1.00 244.56 ? 190  GLU A O   1 
ATOM   1459  C  CB  . GLU A  1 190 ? 16.865  -23.640 11.888   1.00 239.18 ? 190  GLU A CB  1 
ATOM   1460  C  CG  . GLU A  1 190 ? 16.273  -23.789 10.501   1.00 244.07 ? 190  GLU A CG  1 
ATOM   1461  C  CD  . GLU A  1 190 ? 15.075  -24.720 10.501   1.00 239.53 ? 190  GLU A CD  1 
ATOM   1462  O  OE1 . GLU A  1 190 ? 14.669  -25.187 9.415    1.00 245.85 ? 190  GLU A OE1 1 
ATOM   1463  O  OE2 . GLU A  1 190 ? 14.550  -25.001 11.598   1.00 224.29 ? 190  GLU A OE2 1 
ATOM   1464  N  N   . ILE A  1 191 ? 17.342  -20.528 12.891   1.00 226.28 ? 191  ILE A N   1 
ATOM   1465  C  CA  . ILE A  1 191 ? 16.864  -19.149 12.781   1.00 222.71 ? 191  ILE A CA  1 
ATOM   1466  C  C   . ILE A  1 191 ? 17.939  -18.257 12.170   1.00 233.37 ? 191  ILE A C   1 
ATOM   1467  O  O   . ILE A  1 191 ? 17.669  -17.458 11.265   1.00 239.55 ? 191  ILE A O   1 
ATOM   1468  C  CB  . ILE A  1 191 ? 16.420  -18.630 14.161   1.00 217.49 ? 191  ILE A CB  1 
ATOM   1469  C  CG1 . ILE A  1 191 ? 15.240  -19.451 14.688   1.00 217.48 ? 191  ILE A CG1 1 
ATOM   1470  C  CG2 . ILE A  1 191 ? 16.086  -17.146 14.092   1.00 214.79 ? 191  ILE A CG2 1 
ATOM   1471  C  CD1 . ILE A  1 191 ? 14.776  -19.037 16.067   1.00 218.33 ? 191  ILE A CD1 1 
ATOM   1472  N  N   . VAL A  1 192 ? 19.171  -18.369 12.670   1.00 241.22 ? 192  VAL A N   1 
ATOM   1473  C  CA  . VAL A  1 192 ? 20.253  -17.519 12.186   1.00 246.86 ? 192  VAL A CA  1 
ATOM   1474  C  C   . VAL A  1 192 ? 20.782  -18.017 10.843   1.00 245.48 ? 192  VAL A C   1 
ATOM   1475  O  O   . VAL A  1 192 ? 21.121  -17.219 9.961    1.00 247.93 ? 192  VAL A O   1 
ATOM   1476  C  CB  . VAL A  1 192 ? 21.365  -17.432 13.252   1.00 246.96 ? 192  VAL A CB  1 
ATOM   1477  C  CG1 . VAL A  1 192 ? 21.787  -18.821 13.724   1.00 242.77 ? 192  VAL A CG1 1 
ATOM   1478  C  CG2 . VAL A  1 192 ? 22.560  -16.648 12.725   1.00 257.03 ? 192  VAL A CG2 1 
ATOM   1479  N  N   . SER A  1 193 ? 20.841  -19.337 10.654   1.00 236.99 ? 193  SER A N   1 
ATOM   1480  C  CA  . SER A  1 193 ? 21.428  -19.878 9.433    1.00 243.53 ? 193  SER A CA  1 
ATOM   1481  C  C   . SER A  1 193 ? 20.543  -19.601 8.225    1.00 241.98 ? 193  SER A C   1 
ATOM   1482  O  O   . SER A  1 193 ? 21.044  -19.272 7.144    1.00 246.83 ? 193  SER A O   1 
ATOM   1483  C  CB  . SER A  1 193 ? 21.667  -21.379 9.590    1.00 246.59 ? 193  SER A CB  1 
ATOM   1484  O  OG  . SER A  1 193 ? 20.448  -22.103 9.558    1.00 241.94 ? 193  SER A OG  1 
ATOM   1485  N  N   . LYS A  1 194 ? 19.230  -19.706 8.392    1.00 235.54 ? 194  LYS A N   1 
ATOM   1486  C  CA  . LYS A  1 194 ? 18.299  -19.511 7.293    1.00 233.96 ? 194  LYS A CA  1 
ATOM   1487  C  C   . LYS A  1 194 ? 17.867  -18.063 7.147    1.00 230.61 ? 194  LYS A C   1 
ATOM   1488  O  O   . LYS A  1 194 ? 17.009  -17.767 6.310    1.00 228.82 ? 194  LYS A O   1 
ATOM   1489  C  CB  . LYS A  1 194 ? 17.067  -20.396 7.495    1.00 229.21 ? 194  LYS A CB  1 
ATOM   1490  C  CG  . LYS A  1 194 ? 17.338  -21.883 7.391    1.00 232.96 ? 194  LYS A CG  1 
ATOM   1491  C  CD  . LYS A  1 194 ? 17.983  -22.242 6.073    1.00 240.12 ? 194  LYS A CD  1 
ATOM   1492  C  CE  . LYS A  1 194 ? 18.222  -23.737 5.990    1.00 245.55 ? 194  LYS A CE  1 
ATOM   1493  N  NZ  . LYS A  1 194 ? 19.010  -24.234 7.151    1.00 245.44 ? 194  LYS A NZ  1 
ATOM   1494  N  N   . TYR A  1 195 ? 18.429  -17.160 7.943    1.00 230.00 ? 195  TYR A N   1 
ATOM   1495  C  CA  . TYR A  1 195 ? 18.079  -15.750 7.849    1.00 227.35 ? 195  TYR A CA  1 
ATOM   1496  C  C   . TYR A  1 195 ? 18.624  -15.155 6.557    1.00 251.94 ? 195  TYR A C   1 
ATOM   1497  O  O   . TYR A  1 195 ? 19.781  -15.386 6.194    1.00 252.79 ? 195  TYR A O   1 
ATOM   1498  C  CB  . TYR A  1 195 ? 18.625  -14.988 9.053    1.00 226.12 ? 195  TYR A CB  1 
ATOM   1499  C  CG  . TYR A  1 195 ? 18.487  -13.489 8.930    1.00 224.82 ? 195  TYR A CG  1 
ATOM   1500  C  CD1 . TYR A  1 195 ? 17.239  -12.881 8.932    1.00 219.15 ? 195  TYR A CD1 1 
ATOM   1501  C  CD2 . TYR A  1 195 ? 19.609  -12.682 8.793    1.00 243.89 ? 195  TYR A CD2 1 
ATOM   1502  C  CE1 . TYR A  1 195 ? 17.114  -11.504 8.810    1.00 218.39 ? 195  TYR A CE1 1 
ATOM   1503  C  CE2 . TYR A  1 195 ? 19.494  -11.307 8.673    1.00 243.29 ? 195  TYR A CE2 1 
ATOM   1504  C  CZ  . TYR A  1 195 ? 18.244  -10.725 8.683    1.00 228.67 ? 195  TYR A CZ  1 
ATOM   1505  O  OH  . TYR A  1 195 ? 18.127  -9.358  8.564    1.00 222.86 ? 195  TYR A OH  1 
ATOM   1506  N  N   . ASP A  1 196 ? 17.786  -14.379 5.866    1.00 262.13 ? 196  ASP A N   1 
ATOM   1507  C  CA  . ASP A  1 196 ? 18.164  -13.701 4.630    1.00 263.95 ? 196  ASP A CA  1 
ATOM   1508  C  C   . ASP A  1 196 ? 17.450  -12.359 4.526    1.00 259.01 ? 196  ASP A C   1 
ATOM   1509  O  O   . ASP A  1 196 ? 16.220  -12.322 4.391    1.00 251.73 ? 196  ASP A O   1 
ATOM   1510  C  CB  . ASP A  1 196 ? 17.838  -14.563 3.407    1.00 255.12 ? 196  ASP A CB  1 
ATOM   1511  C  CG  . ASP A  1 196 ? 18.933  -15.560 3.080    1.00 261.50 ? 196  ASP A CG  1 
ATOM   1512  O  OD1 . ASP A  1 196 ? 20.106  -15.296 3.418    1.00 258.55 ? 196  ASP A OD1 1 
ATOM   1513  O  OD2 . ASP A  1 196 ? 18.619  -16.610 2.480    1.00 266.48 ? 196  ASP A OD2 1 
ATOM   1514  N  N   . PRO A  1 197 ? 18.182  -11.239 4.568    1.00 256.16 ? 197  PRO A N   1 
ATOM   1515  C  CA  . PRO A  1 197 ? 17.521  -9.922  4.549    1.00 256.42 ? 197  PRO A CA  1 
ATOM   1516  C  C   . PRO A  1 197 ? 16.759  -9.631  3.266    1.00 264.04 ? 197  PRO A C   1 
ATOM   1517  O  O   . PRO A  1 197 ? 16.000  -8.653  3.228    1.00 257.45 ? 197  PRO A O   1 
ATOM   1518  C  CB  . PRO A  1 197 ? 18.688  -8.941  4.740    1.00 255.53 ? 197  PRO A CB  1 
ATOM   1519  C  CG  . PRO A  1 197 ? 19.883  -9.682  4.240    1.00 255.67 ? 197  PRO A CG  1 
ATOM   1520  C  CD  . PRO A  1 197 ? 19.649  -11.118 4.627    1.00 254.68 ? 197  PRO A CD  1 
ATOM   1521  N  N   . ASN A  1 198 ? 16.929  -10.441 2.223    1.00 274.55 ? 198  ASN A N   1 
ATOM   1522  C  CA  . ASN A  1 198 ? 16.217  -10.270 0.965    1.00 276.62 ? 198  ASN A CA  1 
ATOM   1523  C  C   . ASN A  1 198 ? 15.047  -11.232 0.824    1.00 279.84 ? 198  ASN A C   1 
ATOM   1524  O  O   . ASN A  1 198 ? 14.350  -11.197 -0.196   1.00 282.76 ? 198  ASN A O   1 
ATOM   1525  C  CB  . ASN A  1 198 ? 17.181  -10.449 -0.214   1.00 279.83 ? 198  ASN A CB  1 
ATOM   1526  C  CG  . ASN A  1 198 ? 17.913  -11.779 -0.172   1.00 282.73 ? 198  ASN A CG  1 
ATOM   1527  O  OD1 . ASN A  1 198 ? 18.223  -12.294 0.902    1.00 276.53 ? 198  ASN A OD1 1 
ATOM   1528  N  ND2 . ASN A  1 198 ? 18.202  -12.334 -1.344   1.00 292.10 ? 198  ASN A ND2 1 
ATOM   1529  N  N   . VAL A  1 199 ? 14.815  -12.083 1.820    1.00 276.13 ? 199  VAL A N   1 
ATOM   1530  C  CA  . VAL A  1 199 ? 13.704  -13.027 1.829    1.00 265.51 ? 199  VAL A CA  1 
ATOM   1531  C  C   . VAL A  1 199 ? 12.752  -12.613 2.942    1.00 246.39 ? 199  VAL A C   1 
ATOM   1532  O  O   . VAL A  1 199 ? 13.142  -12.541 4.115    1.00 234.20 ? 199  VAL A O   1 
ATOM   1533  C  CB  . VAL A  1 199 ? 14.187  -14.473 2.018    1.00 266.63 ? 199  VAL A CB  1 
ATOM   1534  C  CG1 . VAL A  1 199 ? 13.006  -15.434 1.980    1.00 266.55 ? 199  VAL A CG1 1 
ATOM   1535  C  CG2 . VAL A  1 199 ? 15.204  -14.833 0.946    1.00 271.18 ? 199  VAL A CG2 1 
ATOM   1536  N  N   . TYR A  1 200 ? 11.505  -12.333 2.573    1.00 241.55 ? 200  TYR A N   1 
ATOM   1537  C  CA  . TYR A  1 200 ? 10.530  -11.840 3.531    1.00 247.26 ? 200  TYR A CA  1 
ATOM   1538  C  C   . TYR A  1 200 ? 9.689   -12.950 4.139    1.00 239.12 ? 200  TYR A C   1 
ATOM   1539  O  O   . TYR A  1 200 ? 9.074   -12.741 5.190    1.00 240.88 ? 200  TYR A O   1 
ATOM   1540  C  CB  . TYR A  1 200 ? 9.602   -10.814 2.867    1.00 257.37 ? 200  TYR A CB  1 
ATOM   1541  C  CG  . TYR A  1 200 ? 10.318  -9.764  2.044    1.00 264.33 ? 200  TYR A CG  1 
ATOM   1542  C  CD1 . TYR A  1 200 ? 11.487  -9.167  2.502    1.00 260.88 ? 200  TYR A CD1 1 
ATOM   1543  C  CD2 . TYR A  1 200 ? 9.820   -9.366  0.810    1.00 270.66 ? 200  TYR A CD2 1 
ATOM   1544  C  CE1 . TYR A  1 200 ? 12.140  -8.208  1.751    1.00 265.64 ? 200  TYR A CE1 1 
ATOM   1545  C  CE2 . TYR A  1 200 ? 10.465  -8.407  0.052    1.00 278.40 ? 200  TYR A CE2 1 
ATOM   1546  C  CZ  . TYR A  1 200 ? 11.623  -7.832  0.527    1.00 278.49 ? 200  TYR A CZ  1 
ATOM   1547  O  OH  . TYR A  1 200 ? 12.266  -6.877  -0.227   1.00 289.08 ? 200  TYR A OH  1 
ATOM   1548  N  N   . SER A  1 201 ? 9.660   -14.126 3.516    1.00 237.23 ? 201  SER A N   1 
ATOM   1549  C  CA  . SER A  1 201 ? 8.907   -15.272 4.020    1.00 236.81 ? 201  SER A CA  1 
ATOM   1550  C  C   . SER A  1 201 ? 9.840   -16.476 4.005    1.00 241.09 ? 201  SER A C   1 
ATOM   1551  O  O   . SER A  1 201 ? 9.934   -17.186 3.001    1.00 238.79 ? 201  SER A O   1 
ATOM   1552  C  CB  . SER A  1 201 ? 7.665   -15.510 3.179    1.00 242.96 ? 201  SER A CB  1 
ATOM   1553  O  OG  . SER A  1 201 ? 6.776   -14.411 3.271    1.00 251.45 ? 201  SER A OG  1 
ATOM   1554  N  N   . ILE A  1 202 ? 10.531  -16.701 5.115    1.00 248.10 ? 202  ILE A N   1 
ATOM   1555  C  CA  . ILE A  1 202 ? 11.480  -17.801 5.221    1.00 250.83 ? 202  ILE A CA  1 
ATOM   1556  C  C   . ILE A  1 202 ? 10.757  -19.010 5.795    1.00 241.01 ? 202  ILE A C   1 
ATOM   1557  O  O   . ILE A  1 202 ? 10.117  -18.924 6.851    1.00 232.81 ? 202  ILE A O   1 
ATOM   1558  C  CB  . ILE A  1 202 ? 12.684  -17.412 6.094    1.00 246.65 ? 202  ILE A CB  1 
ATOM   1559  C  CG1 . ILE A  1 202 ? 13.355  -16.144 5.558    1.00 247.12 ? 202  ILE A CG1 1 
ATOM   1560  C  CG2 . ILE A  1 202 ? 13.686  -18.552 6.153    1.00 245.67 ? 202  ILE A CG2 1 
ATOM   1561  C  CD1 . ILE A  1 202 ? 14.534  -15.680 6.391    1.00 248.69 ? 202  ILE A CD1 1 
ATOM   1562  N  N   . LYS A  1 203 ? 10.850  -20.135 5.096    1.00 241.36 ? 203  LYS A N   1 
ATOM   1563  C  CA  . LYS A  1 203 ? 10.260  -21.389 5.539    1.00 237.78 ? 203  LYS A CA  1 
ATOM   1564  C  C   . LYS A  1 203 ? 11.321  -22.210 6.258    1.00 229.82 ? 203  LYS A C   1 
ATOM   1565  O  O   . LYS A  1 203 ? 12.403  -22.450 5.710    1.00 225.19 ? 203  LYS A O   1 
ATOM   1566  C  CB  . LYS A  1 203 ? 9.686   -22.170 4.355    1.00 248.04 ? 203  LYS A CB  1 
ATOM   1567  C  CG  . LYS A  1 203 ? 8.731   -23.276 4.761    1.00 242.51 ? 203  LYS A CG  1 
ATOM   1568  C  CD  . LYS A  1 203 ? 7.699   -22.749 5.743    1.00 221.82 ? 203  LYS A CD  1 
ATOM   1569  C  CE  . LYS A  1 203 ? 6.808   -23.861 6.259    1.00 219.25 ? 203  LYS A CE  1 
ATOM   1570  N  NZ  . LYS A  1 203 ? 5.848   -23.364 7.282    1.00 211.36 ? 203  LYS A NZ  1 
ATOM   1571  N  N   . TYR A  1 204 ? 11.008  -22.638 7.477    1.00 234.07 ? 204  TYR A N   1 
ATOM   1572  C  CA  . TYR A  1 204 ? 11.911  -23.431 8.303    1.00 239.84 ? 204  TYR A CA  1 
ATOM   1573  C  C   . TYR A  1 204 ? 11.434  -24.879 8.354    1.00 252.39 ? 204  TYR A C   1 
ATOM   1574  O  O   . TYR A  1 204 ? 10.245  -25.136 8.573    1.00 258.86 ? 204  TYR A O   1 
ATOM   1575  C  CB  . TYR A  1 204 ? 12.010  -22.838 9.710    1.00 232.86 ? 204  TYR A CB  1 
ATOM   1576  C  CG  . TYR A  1 204 ? 12.342  -21.356 9.732    1.00 217.14 ? 204  TYR A CG  1 
ATOM   1577  C  CD1 . TYR A  1 204 ? 13.657  -20.928 9.623    1.00 215.31 ? 204  TYR A CD1 1 
ATOM   1578  C  CD2 . TYR A  1 204 ? 11.346  -20.389 9.854    1.00 208.13 ? 204  TYR A CD2 1 
ATOM   1579  C  CE1 . TYR A  1 204 ? 13.979  -19.587 9.642    1.00 214.75 ? 204  TYR A CE1 1 
ATOM   1580  C  CE2 . TYR A  1 204 ? 11.661  -19.036 9.873    1.00 207.31 ? 204  TYR A CE2 1 
ATOM   1581  C  CZ  . TYR A  1 204 ? 12.983  -18.644 9.766    1.00 209.89 ? 204  TYR A CZ  1 
ATOM   1582  O  OH  . TYR A  1 204 ? 13.323  -17.311 9.781    1.00 209.62 ? 204  TYR A OH  1 
ATOM   1583  N  N   . ASN A  1 205 ? 12.363  -25.820 8.136    1.00 258.87 ? 205  ASN A N   1 
ATOM   1584  C  CA  . ASN A  1 205 ? 11.991  -27.231 8.037    1.00 251.55 ? 205  ASN A CA  1 
ATOM   1585  C  C   . ASN A  1 205 ? 11.666  -27.832 9.402    1.00 236.59 ? 205  ASN A C   1 
ATOM   1586  O  O   . ASN A  1 205 ? 10.718  -28.615 9.529    1.00 231.82 ? 205  ASN A O   1 
ATOM   1587  C  CB  . ASN A  1 205 ? 13.105  -28.026 7.355    1.00 258.93 ? 205  ASN A CB  1 
ATOM   1588  C  CG  . ASN A  1 205 ? 13.425  -27.505 5.969    1.00 255.63 ? 205  ASN A CG  1 
ATOM   1589  O  OD1 . ASN A  1 205 ? 14.504  -26.965 5.735    1.00 247.15 ? 205  ASN A OD1 1 
ATOM   1590  N  ND2 . ASN A  1 205 ? 12.482  -27.658 5.041    1.00 258.56 ? 205  ASN A ND2 1 
ATOM   1591  N  N   . ASN A  1 206 ? 12.431  -27.483 10.436   1.00 215.51 ? 206  ASN A N   1 
ATOM   1592  C  CA  . ASN A  1 206 ? 12.209  -28.010 11.774   1.00 212.63 ? 206  ASN A CA  1 
ATOM   1593  C  C   . ASN A  1 206 ? 11.206  -27.184 12.564   1.00 210.83 ? 206  ASN A C   1 
ATOM   1594  O  O   . ASN A  1 206 ? 11.238  -27.199 13.800   1.00 212.91 ? 206  ASN A O   1 
ATOM   1595  C  CB  . ASN A  1 206 ? 13.534  -28.098 12.527   1.00 216.28 ? 206  ASN A CB  1 
ATOM   1596  C  CG  . ASN A  1 206 ? 14.536  -28.981 11.821   1.00 224.02 ? 206  ASN A CG  1 
ATOM   1597  O  OD1 . ASN A  1 206 ? 14.172  -29.996 11.228   1.00 228.52 ? 206  ASN A OD1 1 
ATOM   1598  N  ND2 . ASN A  1 206 ? 15.804  -28.588 11.857   1.00 228.34 ? 206  ASN A ND2 1 
ATOM   1599  N  N   . GLN A  1 207 ? 10.323  -26.469 11.870   1.00 225.83 ? 207  GLN A N   1 
ATOM   1600  C  CA  . GLN A  1 207 ? 9.310   -25.645 12.516   1.00 210.17 ? 207  GLN A CA  1 
ATOM   1601  C  C   . GLN A  1 207 ? 8.209   -26.526 13.091   1.00 198.24 ? 207  GLN A C   1 
ATOM   1602  O  O   . GLN A  1 207 ? 7.699   -27.424 12.416   1.00 209.06 ? 207  GLN A O   1 
ATOM   1603  C  CB  . GLN A  1 207 ? 8.728   -24.651 11.505   1.00 202.23 ? 207  GLN A CB  1 
ATOM   1604  C  CG  . GLN A  1 207 ? 7.777   -23.594 12.063   1.00 196.48 ? 207  GLN A CG  1 
ATOM   1605  C  CD  . GLN A  1 207 ? 7.356   -22.580 11.005   1.00 201.51 ? 207  GLN A CD  1 
ATOM   1606  O  OE1 . GLN A  1 207 ? 8.030   -22.414 9.988    1.00 206.55 ? 207  GLN A OE1 1 
ATOM   1607  N  NE2 . GLN A  1 207 ? 6.240   -21.900 11.241   1.00 196.57 ? 207  GLN A NE2 1 
ATOM   1608  N  N   . LEU A  1 208 ? 7.844   -26.264 14.340   1.00 188.29 ? 208  LEU A N   1 
ATOM   1609  C  CA  . LEU A  1 208 ? 6.721   -26.916 14.992   1.00 188.76 ? 208  LEU A CA  1 
ATOM   1610  C  C   . LEU A  1 208 ? 5.610   -25.888 15.158   1.00 194.76 ? 208  LEU A C   1 
ATOM   1611  O  O   . LEU A  1 208 ? 5.836   -24.821 15.739   1.00 208.31 ? 208  LEU A O   1 
ATOM   1612  C  CB  . LEU A  1 208 ? 7.151   -27.486 16.346   1.00 195.02 ? 208  LEU A CB  1 
ATOM   1613  C  CG  . LEU A  1 208 ? 8.200   -28.600 16.290   1.00 190.43 ? 208  LEU A CG  1 
ATOM   1614  C  CD1 . LEU A  1 208 ? 8.533   -29.085 17.688   1.00 190.14 ? 208  LEU A CD1 1 
ATOM   1615  C  CD2 . LEU A  1 208 ? 7.729   -29.751 15.417   1.00 193.06 ? 208  LEU A CD2 1 
ATOM   1616  N  N   . ALA A  1 209 ? 4.413   -26.207 14.664   1.00 191.92 ? 209  ALA A N   1 
ATOM   1617  C  CA  . ALA A  1 209 ? 3.332   -25.229 14.688   1.00 187.17 ? 209  ALA A CA  1 
ATOM   1618  C  C   . ALA A  1 209 ? 1.980   -25.905 14.866   1.00 176.41 ? 209  ALA A C   1 
ATOM   1619  O  O   . ALA A  1 209 ? 1.745   -26.997 14.338   1.00 181.43 ? 209  ALA A O   1 
ATOM   1620  C  CB  . ALA A  1 209 ? 3.332   -24.393 13.404   1.00 184.95 ? 209  ALA A CB  1 
ATOM   1621  N  N   . THR A  1 210 ? 1.099   -25.247 15.625   1.00 168.80 ? 210  THR A N   1 
ATOM   1622  C  CA  . THR A  1 210 ? -0.287  -25.685 15.784   1.00 168.41 ? 210  THR A CA  1 
ATOM   1623  C  C   . THR A  1 210 ? -1.075  -25.298 14.539   1.00 187.56 ? 210  THR A C   1 
ATOM   1624  O  O   . THR A  1 210 ? -1.343  -24.116 14.302   1.00 193.22 ? 210  THR A O   1 
ATOM   1625  C  CB  . THR A  1 210 ? -0.913  -25.076 17.035   1.00 167.47 ? 210  THR A CB  1 
ATOM   1626  O  OG1 . THR A  1 210 ? -0.720  -23.658 17.026   1.00 161.62 ? 210  THR A OG1 1 
ATOM   1627  C  CG2 . THR A  1 210 ? -0.274  -25.656 18.286   1.00 179.23 ? 210  THR A CG2 1 
ATOM   1628  N  N   . ARG A  1 211 ? -1.432  -26.294 13.737   1.00 194.10 ? 211  ARG A N   1 
ATOM   1629  C  CA  . ARG A  1 211 ? -2.128  -26.068 12.483   1.00 198.80 ? 211  ARG A CA  1 
ATOM   1630  C  C   . ARG A  1 211 ? -3.593  -25.677 12.733   1.00 207.20 ? 211  ARG A C   1 
ATOM   1631  O  O   . ARG A  1 211 ? -4.134  -25.824 13.832   1.00 208.54 ? 211  ARG A O   1 
ATOM   1632  C  CB  . ARG A  1 211 ? -1.990  -27.312 11.604   1.00 207.36 ? 211  ARG A CB  1 
ATOM   1633  C  CG  . ARG A  1 211 ? -0.522  -27.556 11.218   1.00 226.31 ? 211  ARG A CG  1 
ATOM   1634  C  CD  . ARG A  1 211 ? -0.283  -28.842 10.435   1.00 232.80 ? 211  ARG A CD  1 
ATOM   1635  N  NE  . ARG A  1 211 ? 1.117   -28.964 10.028   1.00 212.74 ? 211  ARG A NE  1 
ATOM   1636  C  CZ  . ARG A  1 211 ? 2.075   -29.522 10.763   1.00 198.52 ? 211  ARG A CZ  1 
ATOM   1637  N  NH1 . ARG A  1 211 ? 1.806   -30.024 11.960   1.00 193.05 ? 211  ARG A NH1 1 
ATOM   1638  N  NH2 . ARG A  1 211 ? 3.312   -29.573 10.296   1.00 201.54 ? 211  ARG A NH2 1 
ATOM   1639  N  N   . THR A  1 212 ? -4.235  -25.166 11.683   1.00 208.69 ? 212  THR A N   1 
ATOM   1640  C  CA  . THR A  1 212 ? -5.600  -24.654 11.778   1.00 205.93 ? 212  THR A CA  1 
ATOM   1641  C  C   . THR A  1 212 ? -6.619  -25.758 12.067   1.00 204.56 ? 212  THR A C   1 
ATOM   1642  O  O   . THR A  1 212 ? -6.488  -26.892 11.596   1.00 217.32 ? 212  THR A O   1 
ATOM   1643  C  CB  . THR A  1 212 ? -5.967  -23.920 10.485   1.00 212.91 ? 212  THR A CB  1 
ATOM   1644  O  OG1 . THR A  1 212 ? -7.358  -23.573 10.491   1.00 210.66 ? 212  THR A OG1 1 
ATOM   1645  C  CG2 . THR A  1 212 ? -5.665  -24.783 9.265    1.00 222.88 ? 212  THR A CG2 1 
ATOM   1646  N  N   . ALA A  1 213 ? -7.627  -25.424 12.873   1.00 195.93 ? 213  ALA A N   1 
ATOM   1647  C  CA  . ALA A  1 213 ? -8.695  -26.337 13.270   1.00 203.62 ? 213  ALA A CA  1 
ATOM   1648  C  C   . ALA A  1 213 ? -10.055 -25.821 12.781   1.00 202.42 ? 213  ALA A C   1 
ATOM   1649  O  O   . ALA A  1 213 ? -10.143 -24.923 11.937   1.00 207.62 ? 213  ALA A O   1 
ATOM   1650  C  CB  . ALA A  1 213 ? -8.678  -26.540 14.786   1.00 203.42 ? 213  ALA A CB  1 
ATOM   1651  N  N   . GLN A  1 214 ? -11.124 -26.423 13.306   1.00 189.69 ? 214  GLN A N   1 
ATOM   1652  C  CA  . GLN A  1 214 ? -12.480 -26.068 12.911   1.00 190.47 ? 214  GLN A CA  1 
ATOM   1653  C  C   . GLN A  1 214 ? -12.830 -24.641 13.318   1.00 190.02 ? 214  GLN A C   1 
ATOM   1654  O  O   . GLN A  1 214 ? -12.211 -24.038 14.198   1.00 195.58 ? 214  GLN A O   1 
ATOM   1655  C  CB  . GLN A  1 214 ? -13.502 -27.030 13.511   1.00 187.22 ? 214  GLN A CB  1 
ATOM   1656  C  CG  . GLN A  1 214 ? -13.357 -28.464 13.055   1.00 193.29 ? 214  GLN A CG  1 
ATOM   1657  C  CD  . GLN A  1 214 ? -12.372 -29.237 13.887   1.00 191.52 ? 214  GLN A CD  1 
ATOM   1658  O  OE1 . GLN A  1 214 ? -11.450 -28.668 14.469   1.00 190.85 ? 214  GLN A OE1 1 
ATOM   1659  N  NE2 . GLN A  1 214 ? -12.564 -30.547 13.958   1.00 199.95 ? 214  GLN A NE2 1 
ATOM   1660  N  N   . ALA A  1 215 ? -13.855 -24.105 12.648   1.00 189.24 ? 215  ALA A N   1 
ATOM   1661  C  CA  . ALA A  1 215 ? -14.269 -22.717 12.835   1.00 186.12 ? 215  ALA A CA  1 
ATOM   1662  C  C   . ALA A  1 215 ? -14.783 -22.423 14.241   1.00 185.04 ? 215  ALA A C   1 
ATOM   1663  O  O   . ALA A  1 215 ? -14.820 -21.252 14.634   1.00 183.53 ? 215  ALA A O   1 
ATOM   1664  C  CB  . ALA A  1 215 ? -15.340 -22.357 11.803   1.00 184.40 ? 215  ALA A CB  1 
ATOM   1665  N  N   . ILE A  1 216 ? -15.195 -23.440 15.003   1.00 186.75 ? 216  ILE A N   1 
ATOM   1666  C  CA  . ILE A  1 216 ? -15.697 -23.188 16.352   1.00 174.69 ? 216  ILE A CA  1 
ATOM   1667  C  C   . ILE A  1 216 ? -14.601 -22.663 17.265   1.00 170.36 ? 216  ILE A C   1 
ATOM   1668  O  O   . ILE A  1 216 ? -14.896 -22.006 18.273   1.00 159.63 ? 216  ILE A O   1 
ATOM   1669  C  CB  . ILE A  1 216 ? -16.330 -24.459 16.955   1.00 172.38 ? 216  ILE A CB  1 
ATOM   1670  C  CG1 . ILE A  1 216 ? -17.089 -24.129 18.247   1.00 174.03 ? 216  ILE A CG1 1 
ATOM   1671  C  CG2 . ILE A  1 216 ? -15.268 -25.513 17.205   1.00 178.84 ? 216  ILE A CG2 1 
ATOM   1672  C  CD1 . ILE A  1 216 ? -17.648 -25.343 18.964   1.00 180.82 ? 216  ILE A CD1 1 
ATOM   1673  N  N   . PHE A  1 217 ? -13.340 -22.927 16.938   1.00 185.94 ? 217  PHE A N   1 
ATOM   1674  C  CA  . PHE A  1 217 ? -12.213 -22.518 17.763   1.00 186.37 ? 217  PHE A CA  1 
ATOM   1675  C  C   . PHE A  1 217 ? -11.674 -21.136 17.413   1.00 181.44 ? 217  PHE A C   1 
ATOM   1676  O  O   . PHE A  1 217 ? -10.696 -20.703 18.030   1.00 176.82 ? 217  PHE A O   1 
ATOM   1677  C  CB  . PHE A  1 217 ? -11.090 -23.552 17.658   1.00 172.52 ? 217  PHE A CB  1 
ATOM   1678  C  CG  . PHE A  1 217 ? -11.473 -24.910 18.169   1.00 174.01 ? 217  PHE A CG  1 
ATOM   1679  C  CD1 . PHE A  1 217 ? -11.540 -25.159 19.530   1.00 195.31 ? 217  PHE A CD1 1 
ATOM   1680  C  CD2 . PHE A  1 217 ? -11.772 -25.935 17.288   1.00 178.45 ? 217  PHE A CD2 1 
ATOM   1681  C  CE1 . PHE A  1 217 ? -11.894 -26.410 20.004   1.00 204.02 ? 217  PHE A CE1 1 
ATOM   1682  C  CE2 . PHE A  1 217 ? -12.128 -27.187 17.753   1.00 188.53 ? 217  PHE A CE2 1 
ATOM   1683  C  CZ  . PHE A  1 217 ? -12.189 -27.425 19.113   1.00 202.41 ? 217  PHE A CZ  1 
ATOM   1684  N  N   . ASP A  1 218 ? -12.274 -20.436 16.449   1.00 194.41 ? 218  ASP A N   1 
ATOM   1685  C  CA  . ASP A  1 218 ? -11.875 -19.061 16.184   1.00 185.17 ? 218  ASP A CA  1 
ATOM   1686  C  C   . ASP A  1 218 ? -12.083 -18.202 17.427   1.00 173.07 ? 218  ASP A C   1 
ATOM   1687  O  O   . ASP A  1 218 ? -12.883 -18.521 18.313   1.00 183.08 ? 218  ASP A O   1 
ATOM   1688  C  CB  . ASP A  1 218 ? -12.668 -18.460 15.017   1.00 177.17 ? 218  ASP A CB  1 
ATOM   1689  C  CG  . ASP A  1 218 ? -12.392 -19.145 13.687   1.00 174.05 ? 218  ASP A CG  1 
ATOM   1690  O  OD1 . ASP A  1 218 ? -11.506 -20.022 13.628   1.00 181.93 ? 218  ASP A OD1 1 
ATOM   1691  O  OD2 . ASP A  1 218 ? -13.062 -18.788 12.691   1.00 165.69 ? 218  ASP A OD2 1 
ATOM   1692  N  N   . ASP A  1 219 ? -11.324 -17.107 17.493   1.00 142.09 ? 219  ASP A N   1 
ATOM   1693  C  CA  . ASP A  1 219 ? -11.425 -16.136 18.582   1.00 138.23 ? 219  ASP A CA  1 
ATOM   1694  C  C   . ASP A  1 219 ? -11.115 -16.799 19.927   1.00 135.26 ? 219  ASP A C   1 
ATOM   1695  O  O   . ASP A  1 219 ? -11.864 -16.689 20.898   1.00 133.99 ? 219  ASP A O   1 
ATOM   1696  C  CB  . ASP A  1 219 ? -12.804 -15.467 18.575   1.00 156.46 ? 219  ASP A CB  1 
ATOM   1697  C  CG  . ASP A  1 219 ? -12.907 -14.318 19.551   1.00 188.18 ? 219  ASP A CG  1 
ATOM   1698  O  OD1 . ASP A  1 219 ? -11.959 -13.506 19.617   1.00 151.29 ? 219  ASP A OD1 1 
ATOM   1699  O  OD2 . ASP A  1 219 ? -13.944 -14.223 20.243   1.00 220.18 ? 219  ASP A OD2 1 
ATOM   1700  N  N   . SER A  1 220 ? -9.983  -17.494 19.974   1.00 136.04 ? 220  SER A N   1 
ATOM   1701  C  CA  . SER A  1 220 ? -9.541  -18.198 21.172   1.00 158.89 ? 220  SER A CA  1 
ATOM   1702  C  C   . SER A  1 220 ? -8.286  -17.610 21.791   1.00 165.56 ? 220  SER A C   1 
ATOM   1703  O  O   . SER A  1 220 ? -8.067  -17.787 22.993   1.00 159.33 ? 220  SER A O   1 
ATOM   1704  C  CB  . SER A  1 220 ? -9.293  -19.683 20.866   1.00 168.95 ? 220  SER A CB  1 
ATOM   1705  O  OG  . SER A  1 220 ? -10.511 -20.377 20.650   1.00 176.46 ? 220  SER A OG  1 
ATOM   1706  N  N   . TYR A  1 221 ? -7.445  -16.951 20.995   1.00 150.66 ? 221  TYR A N   1 
ATOM   1707  C  CA  . TYR A  1 221 ? -6.242  -16.289 21.497   1.00 137.57 ? 221  TYR A CA  1 
ATOM   1708  C  C   . TYR A  1 221 ? -5.248  -17.296 22.087   1.00 138.50 ? 221  TYR A C   1 
ATOM   1709  O  O   . TYR A  1 221 ? -4.699  -17.085 23.171   1.00 138.28 ? 221  TYR A O   1 
ATOM   1710  C  CB  . TYR A  1 221 ? -6.593  -15.199 22.522   1.00 136.24 ? 221  TYR A CB  1 
ATOM   1711  C  CG  . TYR A  1 221 ? -7.329  -13.977 21.980   1.00 135.98 ? 221  TYR A CG  1 
ATOM   1712  C  CD1 . TYR A  1 221 ? -7.715  -13.892 20.646   1.00 136.77 ? 221  TYR A CD1 1 
ATOM   1713  C  CD2 . TYR A  1 221 ? -7.630  -12.902 22.812   1.00 135.34 ? 221  TYR A CD2 1 
ATOM   1714  C  CE1 . TYR A  1 221 ? -8.384  -12.769 20.159   1.00 168.50 ? 221  TYR A CE1 1 
ATOM   1715  C  CE2 . TYR A  1 221 ? -8.297  -11.778 22.333   1.00 135.52 ? 221  TYR A CE2 1 
ATOM   1716  C  CZ  . TYR A  1 221 ? -8.672  -11.718 21.007   1.00 136.27 ? 221  TYR A CZ  1 
ATOM   1717  O  OH  . TYR A  1 221 ? -9.330  -10.609 20.528   1.00 136.78 ? 221  TYR A OH  1 
ATOM   1718  N  N   . LEU A  1 222 ? -5.056  -18.428 21.400   1.00 139.83 ? 222  LEU A N   1 
ATOM   1719  C  CA  . LEU A  1 222 ? -3.972  -19.344 21.750   1.00 163.42 ? 222  LEU A CA  1 
ATOM   1720  C  C   . LEU A  1 222 ? -2.619  -18.684 21.504   1.00 161.38 ? 222  LEU A C   1 
ATOM   1721  O  O   . LEU A  1 222 ? -2.351  -18.176 20.412   1.00 155.18 ? 222  LEU A O   1 
ATOM   1722  C  CB  . LEU A  1 222 ? -4.074  -20.643 20.946   1.00 166.25 ? 222  LEU A CB  1 
ATOM   1723  C  CG  . LEU A  1 222 ? -2.818  -21.531 20.965   1.00 145.80 ? 222  LEU A CG  1 
ATOM   1724  C  CD1 . LEU A  1 222 ? -2.519  -22.055 22.369   1.00 145.40 ? 222  LEU A CD1 1 
ATOM   1725  C  CD2 . LEU A  1 222 ? -2.917  -22.680 19.965   1.00 147.93 ? 222  LEU A CD2 1 
ATOM   1726  N  N   . GLY A  1 223 ? -1.749  -18.733 22.507   1.00 160.56 ? 223  GLY A N   1 
ATOM   1727  C  CA  . GLY A  1 223 ? -0.467  -18.063 22.448   1.00 145.97 ? 223  GLY A CA  1 
ATOM   1728  C  C   . GLY A  1 223 ? -0.425  -16.737 23.169   1.00 144.89 ? 223  GLY A C   1 
ATOM   1729  O  O   . GLY A  1 223 ? 0.567   -16.010 23.038   1.00 146.65 ? 223  GLY A O   1 
ATOM   1730  N  N   . TYR A  1 224 ? -1.479  -16.400 23.917   1.00 166.21 ? 224  TYR A N   1 
ATOM   1731  C  CA  . TYR A  1 224 ? -1.532  -15.131 24.635   1.00 170.57 ? 224  TYR A CA  1 
ATOM   1732  C  C   . TYR A  1 224 ? -0.412  -15.034 25.661   1.00 143.01 ? 224  TYR A C   1 
ATOM   1733  O  O   . TYR A  1 224 ? 0.168   -13.962 25.858   1.00 143.95 ? 224  TYR A O   1 
ATOM   1734  C  CB  . TYR A  1 224 ? -2.902  -14.975 25.302   1.00 139.13 ? 224  TYR A CB  1 
ATOM   1735  C  CG  . TYR A  1 224 ? -3.233  -13.572 25.770   1.00 138.53 ? 224  TYR A CG  1 
ATOM   1736  C  CD1 . TYR A  1 224 ? -3.831  -12.659 24.908   1.00 138.30 ? 224  TYR A CD1 1 
ATOM   1737  C  CD2 . TYR A  1 224 ? -2.972  -13.165 27.072   1.00 138.55 ? 224  TYR A CD2 1 
ATOM   1738  C  CE1 . TYR A  1 224 ? -4.144  -11.376 25.320   1.00 138.17 ? 224  TYR A CE1 1 
ATOM   1739  C  CE2 . TYR A  1 224 ? -3.283  -11.881 27.492   1.00 138.43 ? 224  TYR A CE2 1 
ATOM   1740  C  CZ  . TYR A  1 224 ? -3.871  -10.992 26.611   1.00 138.27 ? 224  TYR A CZ  1 
ATOM   1741  O  OH  . TYR A  1 224 ? -4.191  -9.715  27.014   1.00 138.56 ? 224  TYR A OH  1 
ATOM   1742  N  N   . SER A  1 225 ? -0.091  -16.147 26.315   1.00 143.47 ? 225  SER A N   1 
ATOM   1743  C  CA  . SER A  1 225 ? 1.031   -16.231 27.235   1.00 145.29 ? 225  SER A CA  1 
ATOM   1744  C  C   . SER A  1 225 ? 1.668   -17.599 27.070   1.00 147.09 ? 225  SER A C   1 
ATOM   1745  O  O   . SER A  1 225 ? 1.024   -18.549 26.620   1.00 146.41 ? 225  SER A O   1 
ATOM   1746  C  CB  . SER A  1 225 ? 0.609   -16.020 28.693   1.00 144.05 ? 225  SER A CB  1 
ATOM   1747  O  OG  . SER A  1 225 ? -0.276  -17.043 29.114   1.00 142.90 ? 225  SER A OG  1 
ATOM   1748  N  N   . VAL A  1 226 ? 2.949   -17.692 27.427   1.00 149.78 ? 226  VAL A N   1 
ATOM   1749  C  CA  . VAL A  1 226 ? 3.696   -18.929 27.261   1.00 152.25 ? 226  VAL A CA  1 
ATOM   1750  C  C   . VAL A  1 226 ? 4.613   -19.157 28.456   1.00 154.20 ? 226  VAL A C   1 
ATOM   1751  O  O   . VAL A  1 226 ? 4.945   -18.239 29.208   1.00 156.02 ? 226  VAL A O   1 
ATOM   1752  C  CB  . VAL A  1 226 ? 4.508   -18.930 25.946   1.00 154.87 ? 226  VAL A CB  1 
ATOM   1753  C  CG1 . VAL A  1 226 ? 3.576   -18.996 24.739   1.00 153.38 ? 226  VAL A CG1 1 
ATOM   1754  C  CG2 . VAL A  1 226 ? 5.384   -17.695 25.871   1.00 167.89 ? 226  VAL A CG2 1 
ATOM   1755  N  N   . ALA A  1 227 ? 5.006   -20.418 28.625   1.00 156.07 ? 227  ALA A N   1 
ATOM   1756  C  CA  . ALA A  1 227 ? 5.959   -20.842 29.639   1.00 158.66 ? 227  ALA A CA  1 
ATOM   1757  C  C   . ALA A  1 227 ? 6.479   -22.205 29.216   1.00 161.50 ? 227  ALA A C   1 
ATOM   1758  O  O   . ALA A  1 227 ? 5.854   -22.899 28.412   1.00 160.82 ? 227  ALA A O   1 
ATOM   1759  C  CB  . ALA A  1 227 ? 5.330   -20.898 31.033   1.00 156.85 ? 227  ALA A CB  1 
ATOM   1760  N  N   . VAL A  1 228 ? 7.626   -22.591 29.760   1.00 165.05 ? 228  VAL A N   1 
ATOM   1761  C  CA  . VAL A  1 228 ? 8.251   -23.838 29.346   1.00 168.54 ? 228  VAL A CA  1 
ATOM   1762  C  C   . VAL A  1 228 ? 8.564   -24.698 30.562   1.00 170.33 ? 228  VAL A C   1 
ATOM   1763  O  O   . VAL A  1 228 ? 8.779   -24.195 31.670   1.00 170.15 ? 228  VAL A O   1 
ATOM   1764  C  CB  . VAL A  1 228 ? 9.518   -23.574 28.506   1.00 172.48 ? 228  VAL A CB  1 
ATOM   1765  C  CG1 . VAL A  1 228 ? 9.161   -22.810 27.238   1.00 170.98 ? 228  VAL A CG1 1 
ATOM   1766  C  CG2 . VAL A  1 228 ? 10.541  -22.800 29.316   1.00 186.29 ? 228  VAL A CG2 1 
ATOM   1767  N  N   . GLY A  1 229 ? 8.595   -26.012 30.336   1.00 173.92 ? 229  GLY A N   1 
ATOM   1768  C  CA  . GLY A  1 229 ? 8.871   -27.000 31.364   1.00 176.15 ? 229  GLY A CA  1 
ATOM   1769  C  C   . GLY A  1 229 ? 8.586   -28.413 30.887   1.00 177.84 ? 229  GLY A C   1 
ATOM   1770  O  O   . GLY A  1 229 ? 7.777   -28.612 29.975   1.00 175.96 ? 229  GLY A O   1 
ATOM   1771  N  N   . ASP A  1 230 ? 9.246   -29.405 31.488   1.00 199.61 ? 230  ASP A N   1 
ATOM   1772  C  CA  . ASP A  1 230 ? 9.059   -30.803 31.117   1.00 204.24 ? 230  ASP A CA  1 
ATOM   1773  C  C   . ASP A  1 230 ? 7.874   -31.370 31.890   1.00 212.32 ? 230  ASP A C   1 
ATOM   1774  O  O   . ASP A  1 230 ? 7.748   -31.141 33.097   1.00 219.70 ? 230  ASP A O   1 
ATOM   1775  C  CB  . ASP A  1 230 ? 10.318  -31.626 31.405   1.00 194.03 ? 230  ASP A CB  1 
ATOM   1776  C  CG  . ASP A  1 230 ? 10.281  -33.012 30.758   1.00 197.39 ? 230  ASP A CG  1 
ATOM   1777  O  OD1 . ASP A  1 230 ? 9.472   -33.222 29.821   1.00 201.24 ? 230  ASP A OD1 1 
ATOM   1778  O  OD2 . ASP A  1 230 ? 11.050  -33.896 31.200   1.00 202.18 ? 230  ASP A OD2 1 
ATOM   1779  N  N   . PHE A  1 231 ? 7.002   -32.101 31.195   1.00 205.52 ? 231  PHE A N   1 
ATOM   1780  C  CA  . PHE A  1 231 ? 5.785   -32.596 31.830   1.00 184.93 ? 231  PHE A CA  1 
ATOM   1781  C  C   . PHE A  1 231 ? 5.514   -34.060 31.521   1.00 189.42 ? 231  PHE A C   1 
ATOM   1782  O  O   . PHE A  1 231 ? 4.992   -34.790 32.369   1.00 199.05 ? 231  PHE A O   1 
ATOM   1783  C  CB  . PHE A  1 231 ? 4.593   -31.743 31.411   1.00 179.77 ? 231  PHE A CB  1 
ATOM   1784  C  CG  . PHE A  1 231 ? 4.618   -30.362 31.986   1.00 176.86 ? 231  PHE A CG  1 
ATOM   1785  C  CD1 . PHE A  1 231 ? 4.204   -30.133 33.286   1.00 175.25 ? 231  PHE A CD1 1 
ATOM   1786  C  CD2 . PHE A  1 231 ? 5.084   -29.295 31.239   1.00 176.80 ? 231  PHE A CD2 1 
ATOM   1787  C  CE1 . PHE A  1 231 ? 4.235   -28.863 33.822   1.00 173.01 ? 231  PHE A CE1 1 
ATOM   1788  C  CE2 . PHE A  1 231 ? 5.122   -28.020 31.774   1.00 182.26 ? 231  PHE A CE2 1 
ATOM   1789  C  CZ  . PHE A  1 231 ? 4.695   -27.804 33.066   1.00 173.67 ? 231  PHE A CZ  1 
ATOM   1790  N  N   . ASN A  1 232 ? 5.873   -34.505 30.323   1.00 186.77 ? 232  ASN A N   1 
ATOM   1791  C  CA  . ASN A  1 232 ? 5.722   -35.900 29.945   1.00 193.58 ? 232  ASN A CA  1 
ATOM   1792  C  C   . ASN A  1 232 ? 6.908   -36.759 30.368   1.00 190.96 ? 232  ASN A C   1 
ATOM   1793  O  O   . ASN A  1 232 ? 7.015   -37.908 29.926   1.00 194.89 ? 232  ASN A O   1 
ATOM   1794  C  CB  . ASN A  1 232 ? 5.520   -36.001 28.440   1.00 185.63 ? 232  ASN A CB  1 
ATOM   1795  C  CG  . ASN A  1 232 ? 6.572   -35.245 27.674   1.00 187.21 ? 232  ASN A CG  1 
ATOM   1796  O  OD1 . ASN A  1 232 ? 7.261   -34.394 28.229   1.00 186.70 ? 232  ASN A OD1 1 
ATOM   1797  N  ND2 . ASN A  1 232 ? 6.707   -35.550 26.393   1.00 189.45 ? 232  ASN A ND2 1 
ATOM   1798  N  N   . GLY A  1 233 ? 7.789   -36.230 31.215   1.00 191.91 ? 233  GLY A N   1 
ATOM   1799  C  CA  . GLY A  1 233 ? 8.872   -37.001 31.787   1.00 197.48 ? 233  GLY A CA  1 
ATOM   1800  C  C   . GLY A  1 233 ? 9.822   -37.576 30.759   1.00 215.94 ? 233  GLY A C   1 
ATOM   1801  O  O   . GLY A  1 233 ? 10.126  -38.773 30.801   1.00 237.24 ? 233  GLY A O   1 
ATOM   1802  N  N   . ASP A  1 234 ? 10.296  -36.750 29.829   1.00 202.50 ? 234  ASP A N   1 
ATOM   1803  C  CA  . ASP A  1 234 ? 11.231  -37.217 28.810   1.00 207.89 ? 234  ASP A CA  1 
ATOM   1804  C  C   . ASP A  1 234 ? 12.532  -36.431 28.774   1.00 210.97 ? 234  ASP A C   1 
ATOM   1805  O  O   . ASP A  1 234 ? 13.592  -37.016 28.528   1.00 234.03 ? 234  ASP A O   1 
ATOM   1806  C  CB  . ASP A  1 234 ? 10.569  -37.185 27.422   1.00 206.38 ? 234  ASP A CB  1 
ATOM   1807  C  CG  . ASP A  1 234 ? 10.444  -35.785 26.864   1.00 202.23 ? 234  ASP A CG  1 
ATOM   1808  O  OD1 . ASP A  1 234 ? 10.269  -34.845 27.662   1.00 198.33 ? 234  ASP A OD1 1 
ATOM   1809  O  OD2 . ASP A  1 234 ? 10.517  -35.622 25.628   1.00 203.13 ? 234  ASP A OD2 1 
ATOM   1810  N  N   . GLY A  1 235 ? 12.490  -35.124 29.013   1.00 206.37 ? 235  GLY A N   1 
ATOM   1811  C  CA  . GLY A  1 235 ? 13.706  -34.338 29.054   1.00 208.90 ? 235  GLY A CA  1 
ATOM   1812  C  C   . GLY A  1 235 ? 13.655  -33.163 28.106   1.00 206.18 ? 235  GLY A C   1 
ATOM   1813  O  O   . GLY A  1 235 ? 14.506  -32.270 28.156   1.00 207.26 ? 235  GLY A O   1 
ATOM   1814  N  N   . ILE A  1 236 ? 12.663  -33.163 27.224   1.00 202.97 ? 236  ILE A N   1 
ATOM   1815  C  CA  . ILE A  1 236 ? 12.476  -32.086 26.260   1.00 200.32 ? 236  ILE A CA  1 
ATOM   1816  C  C   . ILE A  1 236 ? 11.486  -31.085 26.837   1.00 193.78 ? 236  ILE A C   1 
ATOM   1817  O  O   . ILE A  1 236 ? 10.366  -31.453 27.208   1.00 190.38 ? 236  ILE A O   1 
ATOM   1818  C  CB  . ILE A  1 236 ? 11.989  -32.626 24.909   1.00 201.08 ? 236  ILE A CB  1 
ATOM   1819  C  CG1 . ILE A  1 236 ? 12.977  -33.656 24.360   1.00 208.15 ? 236  ILE A CG1 1 
ATOM   1820  C  CG2 . ILE A  1 236 ? 11.792  -31.484 23.927   1.00 198.53 ? 236  ILE A CG2 1 
ATOM   1821  C  CD1 . ILE A  1 236 ? 14.369  -33.105 24.145   1.00 212.45 ? 236  ILE A CD1 1 
ATOM   1822  N  N   . ASP A  1 237 ? 11.901  -29.822 26.920   1.00 192.41 ? 237  ASP A N   1 
ATOM   1823  C  CA  . ASP A  1 237 ? 11.017  -28.774 27.412   1.00 186.71 ? 237  ASP A CA  1 
ATOM   1824  C  C   . ASP A  1 237 ? 9.757   -28.703 26.557   1.00 182.82 ? 237  ASP A C   1 
ATOM   1825  O  O   . ASP A  1 237 ? 9.833   -28.600 25.329   1.00 183.84 ? 237  ASP A O   1 
ATOM   1826  C  CB  . ASP A  1 237 ? 11.745  -27.429 27.405   1.00 186.70 ? 237  ASP A CB  1 
ATOM   1827  C  CG  . ASP A  1 237 ? 12.596  -27.224 28.638   1.00 188.72 ? 237  ASP A CG  1 
ATOM   1828  O  OD1 . ASP A  1 237 ? 12.826  -28.212 29.364   1.00 191.08 ? 237  ASP A OD1 1 
ATOM   1829  O  OD2 . ASP A  1 237 ? 13.042  -26.081 28.873   1.00 188.25 ? 237  ASP A OD2 1 
ATOM   1830  N  N   . ASP A  1 238 ? 8.597   -28.766 27.213   1.00 182.01 ? 238  ASP A N   1 
ATOM   1831  C  CA  . ASP A  1 238 ? 7.301   -28.755 26.548   1.00 175.44 ? 238  ASP A CA  1 
ATOM   1832  C  C   . ASP A  1 238 ? 6.667   -27.364 26.612   1.00 170.93 ? 238  ASP A C   1 
ATOM   1833  O  O   . ASP A  1 238 ? 7.027   -26.530 27.447   1.00 170.05 ? 238  ASP A O   1 
ATOM   1834  C  CB  . ASP A  1 238 ? 6.365   -29.792 27.180   1.00 174.29 ? 238  ASP A CB  1 
ATOM   1835  C  CG  . ASP A  1 238 ? 6.944   -31.200 27.150   1.00 179.05 ? 238  ASP A CG  1 
ATOM   1836  O  OD1 . ASP A  1 238 ? 7.470   -31.607 26.092   1.00 182.39 ? 238  ASP A OD1 1 
ATOM   1837  O  OD2 . ASP A  1 238 ? 6.858   -31.909 28.178   1.00 184.84 ? 238  ASP A OD2 1 
ATOM   1838  N  N   . PHE A  1 239 ? 5.682   -27.136 25.736   1.00 174.93 ? 239  PHE A N   1 
ATOM   1839  C  CA  . PHE A  1 239 ? 5.109   -25.811 25.504   1.00 171.35 ? 239  PHE A CA  1 
ATOM   1840  C  C   . PHE A  1 239 ? 3.783   -25.655 26.249   1.00 181.99 ? 239  PHE A C   1 
ATOM   1841  O  O   . PHE A  1 239 ? 2.823   -26.390 25.985   1.00 166.04 ? 239  PHE A O   1 
ATOM   1842  C  CB  . PHE A  1 239 ? 4.908   -25.564 24.005   1.00 184.69 ? 239  PHE A CB  1 
ATOM   1843  C  CG  . PHE A  1 239 ? 6.152   -25.782 23.172   1.00 198.80 ? 239  PHE A CG  1 
ATOM   1844  C  CD1 . PHE A  1 239 ? 7.404   -25.415 23.648   1.00 208.70 ? 239  PHE A CD1 1 
ATOM   1845  C  CD2 . PHE A  1 239 ? 6.065   -26.358 21.911   1.00 200.65 ? 239  PHE A CD2 1 
ATOM   1846  C  CE1 . PHE A  1 239 ? 8.545   -25.622 22.879   1.00 221.72 ? 239  PHE A CE1 1 
ATOM   1847  C  CE2 . PHE A  1 239 ? 7.202   -26.565 21.140   1.00 202.02 ? 239  PHE A CE2 1 
ATOM   1848  C  CZ  . PHE A  1 239 ? 8.442   -26.199 21.626   1.00 210.28 ? 239  PHE A CZ  1 
ATOM   1849  N  N   . VAL A  1 240 ? 3.735   -24.693 27.173   1.00 165.04 ? 240  VAL A N   1 
ATOM   1850  C  CA  . VAL A  1 240 ? 2.528   -24.345 27.917   1.00 154.36 ? 240  VAL A CA  1 
ATOM   1851  C  C   . VAL A  1 240 ? 2.057   -22.964 27.485   1.00 151.84 ? 240  VAL A C   1 
ATOM   1852  O  O   . VAL A  1 240 ? 2.856   -22.023 27.410   1.00 152.72 ? 240  VAL A O   1 
ATOM   1853  C  CB  . VAL A  1 240 ? 2.786   -24.375 29.434   1.00 154.47 ? 240  VAL A CB  1 
ATOM   1854  C  CG1 . VAL A  1 240 ? 1.494   -24.127 30.191   1.00 189.70 ? 240  VAL A CG1 1 
ATOM   1855  C  CG2 . VAL A  1 240 ? 3.411   -25.696 29.836   1.00 160.26 ? 240  VAL A CG2 1 
ATOM   1856  N  N   . SER A  1 241 ? 0.752   -22.828 27.244   1.00 163.48 ? 241  SER A N   1 
ATOM   1857  C  CA  . SER A  1 241 ? 0.214   -21.563 26.765   1.00 146.88 ? 241  SER A CA  1 
ATOM   1858  C  C   . SER A  1 241 ? -1.218  -21.368 27.239   1.00 143.79 ? 241  SER A C   1 
ATOM   1859  O  O   . SER A  1 241 ? -2.019  -22.309 27.234   1.00 143.23 ? 241  SER A O   1 
ATOM   1860  C  CB  . SER A  1 241 ? 0.263   -21.481 25.238   1.00 147.75 ? 241  SER A CB  1 
ATOM   1861  O  OG  . SER A  1 241 ? -0.122  -20.193 24.798   1.00 146.20 ? 241  SER A OG  1 
ATOM   1862  N  N   . GLY A  1 242 ? -1.526  -20.137 27.649   1.00 142.17 ? 242  GLY A N   1 
ATOM   1863  C  CA  . GLY A  1 242 ? -2.888  -19.784 28.023   1.00 139.62 ? 242  GLY A CA  1 
ATOM   1864  C  C   . GLY A  1 242 ? -3.756  -19.486 26.806   1.00 138.57 ? 242  GLY A C   1 
ATOM   1865  O  O   . GLY A  1 242 ? -3.330  -18.851 25.840   1.00 139.28 ? 242  GLY A O   1 
ATOM   1866  N  N   . VAL A  1 243 ? -4.993  -19.962 26.866   1.00 137.14 ? 243  VAL A N   1 
ATOM   1867  C  CA  . VAL A  1 243 ? -5.973  -19.730 25.809   1.00 155.17 ? 243  VAL A CA  1 
ATOM   1868  C  C   . VAL A  1 243 ? -7.179  -19.066 26.463   1.00 159.46 ? 243  VAL A C   1 
ATOM   1869  O  O   . VAL A  1 243 ? -8.201  -19.728 26.707   1.00 148.38 ? 243  VAL A O   1 
ATOM   1870  C  CB  . VAL A  1 243 ? -6.346  -21.034 25.091   1.00 143.36 ? 243  VAL A CB  1 
ATOM   1871  C  CG1 . VAL A  1 243 ? -6.953  -20.738 23.727   1.00 137.06 ? 243  VAL A CG1 1 
ATOM   1872  C  CG2 . VAL A  1 243 ? -5.120  -21.915 24.953   1.00 139.37 ? 243  VAL A CG2 1 
ATOM   1873  N  N   . PRO A  1 244 ? -7.089  -17.768 26.776   1.00 145.47 ? 244  PRO A N   1 
ATOM   1874  C  CA  . PRO A  1 244 ? -8.026  -17.166 27.739   1.00 132.64 ? 244  PRO A CA  1 
ATOM   1875  C  C   . PRO A  1 244 ? -9.455  -17.056 27.242   1.00 131.69 ? 244  PRO A C   1 
ATOM   1876  O  O   . PRO A  1 244 ? -10.367 -16.972 28.072   1.00 137.35 ? 244  PRO A O   1 
ATOM   1877  C  CB  . PRO A  1 244 ? -7.420  -15.778 27.993   1.00 132.99 ? 244  PRO A CB  1 
ATOM   1878  C  CG  . PRO A  1 244 ? -6.631  -15.486 26.766   1.00 134.01 ? 244  PRO A CG  1 
ATOM   1879  C  CD  . PRO A  1 244 ? -6.087  -16.802 26.295   1.00 134.84 ? 244  PRO A CD  1 
ATOM   1880  N  N   . ARG A  1 245 ? -9.694  -17.051 25.934   1.00 131.95 ? 245  ARG A N   1 
ATOM   1881  C  CA  . ARG A  1 245 ? -11.053 -16.938 25.428   1.00 131.41 ? 245  ARG A CA  1 
ATOM   1882  C  C   . ARG A  1 245 ? -11.638 -18.282 25.015   1.00 131.61 ? 245  ARG A C   1 
ATOM   1883  O  O   . ARG A  1 245 ? -12.794 -18.335 24.585   1.00 163.26 ? 245  ARG A O   1 
ATOM   1884  C  CB  . ARG A  1 245 ? -11.110 -15.952 24.253   1.00 131.87 ? 245  ARG A CB  1 
ATOM   1885  C  CG  . ARG A  1 245 ? -10.977 -14.487 24.671   1.00 131.84 ? 245  ARG A CG  1 
ATOM   1886  C  CD  . ARG A  1 245 ? -11.346 -13.522 23.540   1.00 132.48 ? 245  ARG A CD  1 
ATOM   1887  N  NE  . ARG A  1 245 ? -12.752 -13.623 23.142   1.00 142.37 ? 245  ARG A NE  1 
ATOM   1888  C  CZ  . ARG A  1 245 ? -13.742 -12.898 23.664   1.00 132.15 ? 245  ARG A CZ  1 
ATOM   1889  N  NH1 . ARG A  1 245 ? -13.481 -12.000 24.598   1.00 132.17 ? 245  ARG A NH1 1 
ATOM   1890  N  NH2 . ARG A  1 245 ? -14.991 -13.061 23.243   1.00 132.35 ? 245  ARG A NH2 1 
ATOM   1891  N  N   . ALA A  1 246 ? -10.874 -19.365 25.138   1.00 132.29 ? 246  ALA A N   1 
ATOM   1892  C  CA  . ALA A  1 246 ? -11.371 -20.693 24.824   1.00 132.89 ? 246  ALA A CA  1 
ATOM   1893  C  C   . ALA A  1 246 ? -12.491 -21.099 25.785   1.00 132.19 ? 246  ALA A C   1 
ATOM   1894  O  O   . ALA A  1 246 ? -12.744 -20.458 26.809   1.00 131.36 ? 246  ALA A O   1 
ATOM   1895  C  CB  . ALA A  1 246 ? -10.236 -21.714 24.877   1.00 134.19 ? 246  ALA A CB  1 
ATOM   1896  N  N   . ALA A  1 247 ? -13.174 -22.186 25.422   1.00 149.07 ? 247  ALA A N   1 
ATOM   1897  C  CA  . ALA A  1 247 ? -14.266 -22.753 26.219   1.00 152.62 ? 247  ALA A CA  1 
ATOM   1898  C  C   . ALA A  1 247 ? -15.355 -21.724 26.507   1.00 133.83 ? 247  ALA A C   1 
ATOM   1899  O  O   . ALA A  1 247 ? -15.869 -21.634 27.624   1.00 131.49 ? 247  ALA A O   1 
ATOM   1900  C  CB  . ALA A  1 247 ? -13.738 -23.351 27.525   1.00 160.75 ? 247  ALA A CB  1 
ATOM   1901  N  N   . ARG A  1 248 ? -15.721 -20.952 25.485   1.00 131.81 ? 248  ARG A N   1 
ATOM   1902  C  CA  . ARG A  1 248 ? -16.802 -19.978 25.596   1.00 131.48 ? 248  ARG A CA  1 
ATOM   1903  C  C   . ARG A  1 248 ? -16.530 -18.984 26.726   1.00 137.80 ? 248  ARG A C   1 
ATOM   1904  O  O   . ARG A  1 248 ? -17.358 -18.781 27.615   1.00 165.93 ? 248  ARG A O   1 
ATOM   1905  C  CB  . ARG A  1 248 ? -18.144 -20.686 25.791   1.00 132.77 ? 248  ARG A CB  1 
ATOM   1906  C  CG  . ARG A  1 248 ? -19.331 -19.934 25.239   1.00 165.05 ? 248  ARG A CG  1 
ATOM   1907  C  CD  . ARG A  1 248 ? -19.147 -19.652 23.756   1.00 178.13 ? 248  ARG A CD  1 
ATOM   1908  N  NE  . ARG A  1 248 ? -20.319 -19.008 23.167   1.00 169.06 ? 248  ARG A NE  1 
ATOM   1909  C  CZ  . ARG A  1 248 ? -21.266 -19.647 22.488   1.00 158.43 ? 248  ARG A CZ  1 
ATOM   1910  N  NH1 . ARG A  1 248 ? -21.179 -20.957 22.303   1.00 168.03 ? 248  ARG A NH1 1 
ATOM   1911  N  NH2 . ARG A  1 248 ? -22.297 -18.976 21.990   1.00 136.37 ? 248  ARG A NH2 1 
ATOM   1912  N  N   . THR A  1 249 ? -15.339 -18.375 26.689   1.00 138.93 ? 249  THR A N   1 
ATOM   1913  C  CA  . THR A  1 249 ? -14.837 -17.373 27.636   1.00 133.73 ? 249  THR A CA  1 
ATOM   1914  C  C   . THR A  1 249 ? -14.570 -17.934 29.025   1.00 129.98 ? 249  THR A C   1 
ATOM   1915  O  O   . THR A  1 249 ? -14.344 -17.157 29.962   1.00 129.97 ? 249  THR A O   1 
ATOM   1916  C  CB  . THR A  1 249 ? -15.775 -16.165 27.762   1.00 152.39 ? 249  THR A CB  1 
ATOM   1917  O  OG1 . THR A  1 249 ? -16.991 -16.558 28.414   1.00 157.50 ? 249  THR A OG1 1 
ATOM   1918  C  CG2 . THR A  1 249 ? -16.093 -15.578 26.390   1.00 130.59 ? 249  THR A CG2 1 
ATOM   1919  N  N   . LEU A  1 250 ? -14.574 -19.257 29.187   1.00 130.23 ? 250  LEU A N   1 
ATOM   1920  C  CA  . LEU A  1 250 ? -14.161 -19.865 30.447   1.00 130.47 ? 250  LEU A CA  1 
ATOM   1921  C  C   . LEU A  1 250 ? -12.661 -19.762 30.659   1.00 130.68 ? 250  LEU A C   1 
ATOM   1922  O  O   . LEU A  1 250 ? -12.195 -19.731 31.803   1.00 130.98 ? 250  LEU A O   1 
ATOM   1923  C  CB  . LEU A  1 250 ? -14.581 -21.331 30.475   1.00 131.07 ? 250  LEU A CB  1 
ATOM   1924  C  CG  . LEU A  1 250 ? -15.183 -21.850 31.776   1.00 150.22 ? 250  LEU A CG  1 
ATOM   1925  C  CD1 . LEU A  1 250 ? -16.161 -20.842 32.359   1.00 131.34 ? 250  LEU A CD1 1 
ATOM   1926  C  CD2 . LEU A  1 250 ? -15.869 -23.186 31.541   1.00 164.03 ? 250  LEU A CD2 1 
ATOM   1927  N  N   . GLY A  1 251 ? -11.900 -19.726 29.574   1.00 130.85 ? 251  GLY A N   1 
ATOM   1928  C  CA  . GLY A  1 251 ? -10.453 -19.692 29.606   1.00 171.80 ? 251  GLY A CA  1 
ATOM   1929  C  C   . GLY A  1 251 ? -9.879  -21.086 29.736   1.00 148.11 ? 251  GLY A C   1 
ATOM   1930  O  O   . GLY A  1 251 ? -10.351 -21.885 30.550   1.00 164.61 ? 251  GLY A O   1 
ATOM   1931  N  N   . MET A  1 252 ? -8.831  -21.380 28.973   1.00 133.50 ? 252  MET A N   1 
ATOM   1932  C  CA  . MET A  1 252 ? -8.202  -22.685 29.022   1.00 134.99 ? 252  MET A CA  1 
ATOM   1933  C  C   . MET A  1 252 ? -6.700  -22.506 28.933   1.00 136.35 ? 252  MET A C   1 
ATOM   1934  O  O   . MET A  1 252 ? -6.195  -21.423 28.637   1.00 136.13 ? 252  MET A O   1 
ATOM   1935  C  CB  . MET A  1 252 ? -8.688  -23.607 27.896   1.00 135.66 ? 252  MET A CB  1 
ATOM   1936  C  CG  . MET A  1 252 ? -10.140 -24.025 28.002   1.00 134.91 ? 252  MET A CG  1 
ATOM   1937  S  SD  . MET A  1 252 ? -10.633 -25.231 26.753   1.00 136.31 ? 252  MET A SD  1 
ATOM   1938  C  CE  . MET A  1 252 ? -9.775  -26.692 27.346   1.00 149.78 ? 252  MET A CE  1 
ATOM   1939  N  N   . VAL A  1 253 ? -5.986  -23.588 29.212   1.00 138.10 ? 253  VAL A N   1 
ATOM   1940  C  CA  . VAL A  1 253 ? -4.544  -23.643 29.028   1.00 145.06 ? 253  VAL A CA  1 
ATOM   1941  C  C   . VAL A  1 253 ? -4.225  -24.945 28.305   1.00 165.41 ? 253  VAL A C   1 
ATOM   1942  O  O   . VAL A  1 253 ? -4.584  -26.027 28.782   1.00 195.18 ? 253  VAL A O   1 
ATOM   1943  C  CB  . VAL A  1 253 ? -3.791  -23.545 30.366   1.00 168.11 ? 253  VAL A CB  1 
ATOM   1944  C  CG1 . VAL A  1 253 ? -2.322  -23.948 30.200   1.00 143.57 ? 253  VAL A CG1 1 
ATOM   1945  C  CG2 . VAL A  1 253 ? -3.919  -22.135 30.939   1.00 141.02 ? 253  VAL A CG2 1 
ATOM   1946  N  N   . TYR A  1 254 ? -3.585  -24.841 27.146   1.00 155.32 ? 254  TYR A N   1 
ATOM   1947  C  CA  . TYR A  1 254 ? -3.207  -26.006 26.363   1.00 151.22 ? 254  TYR A CA  1 
ATOM   1948  C  C   . TYR A  1 254 ? -1.753  -26.351 26.638   1.00 149.14 ? 254  TYR A C   1 
ATOM   1949  O  O   . TYR A  1 254 ? -0.909  -25.461 26.767   1.00 179.35 ? 254  TYR A O   1 
ATOM   1950  C  CB  . TYR A  1 254 ? -3.398  -25.754 24.869   1.00 150.26 ? 254  TYR A CB  1 
ATOM   1951  C  CG  . TYR A  1 254 ? -4.823  -25.491 24.452   1.00 144.35 ? 254  TYR A CG  1 
ATOM   1952  C  CD1 . TYR A  1 254 ? -5.891  -25.821 25.279   1.00 142.76 ? 254  TYR A CD1 1 
ATOM   1953  C  CD2 . TYR A  1 254 ? -5.098  -24.898 23.230   1.00 157.02 ? 254  TYR A CD2 1 
ATOM   1954  C  CE1 . TYR A  1 254 ? -7.197  -25.569 24.892   1.00 187.66 ? 254  TYR A CE1 1 
ATOM   1955  C  CE2 . TYR A  1 254 ? -6.397  -24.638 22.836   1.00 174.72 ? 254  TYR A CE2 1 
ATOM   1956  C  CZ  . TYR A  1 254 ? -7.444  -24.976 23.667   1.00 185.08 ? 254  TYR A CZ  1 
ATOM   1957  O  OH  . TYR A  1 254 ? -8.736  -24.713 23.262   1.00 170.53 ? 254  TYR A OH  1 
ATOM   1958  N  N   . ILE A  1 255 ? -1.461  -27.641 26.733   1.00 158.24 ? 255  ILE A N   1 
ATOM   1959  C  CA  . ILE A  1 255 ? -0.090  -28.118 26.832   1.00 161.70 ? 255  ILE A CA  1 
ATOM   1960  C  C   . ILE A  1 255 ? 0.211   -28.956 25.602   1.00 164.64 ? 255  ILE A C   1 
ATOM   1961  O  O   . ILE A  1 255 ? -0.534  -29.889 25.283   1.00 165.09 ? 255  ILE A O   1 
ATOM   1962  C  CB  . ILE A  1 255 ? 0.148   -28.914 28.125   1.00 162.92 ? 255  ILE A CB  1 
ATOM   1963  C  CG1 . ILE A  1 255 ? 0.008   -27.994 29.340   1.00 164.66 ? 255  ILE A CG1 1 
ATOM   1964  C  CG2 . ILE A  1 255 ? 1.516   -29.561 28.096   1.00 167.14 ? 255  ILE A CG2 1 
ATOM   1965  C  CD1 . ILE A  1 255 ? 0.494   -28.604 30.637   1.00 162.27 ? 255  ILE A CD1 1 
ATOM   1966  N  N   . TYR A  1 256 ? 1.283   -28.605 24.899   1.00 171.31 ? 256  TYR A N   1 
ATOM   1967  C  CA  . TYR A  1 256 ? 1.714   -29.334 23.718   1.00 174.74 ? 256  TYR A CA  1 
ATOM   1968  C  C   . TYR A  1 256 ? 3.101   -29.930 23.929   1.00 179.15 ? 256  TYR A C   1 
ATOM   1969  O  O   . TYR A  1 256 ? 3.942   -29.357 24.626   1.00 190.11 ? 256  TYR A O   1 
ATOM   1970  C  CB  . TYR A  1 256 ? 1.714   -28.435 22.481   1.00 183.72 ? 256  TYR A CB  1 
ATOM   1971  C  CG  . TYR A  1 256 ? 0.340   -27.952 22.075   1.00 185.96 ? 256  TYR A CG  1 
ATOM   1972  C  CD1 . TYR A  1 256 ? -0.450  -28.696 21.206   1.00 185.81 ? 256  TYR A CD1 1 
ATOM   1973  C  CD2 . TYR A  1 256 ? -0.163  -26.746 22.545   1.00 177.26 ? 256  TYR A CD2 1 
ATOM   1974  C  CE1 . TYR A  1 256 ? -1.705  -28.258 20.826   1.00 184.25 ? 256  TYR A CE1 1 
ATOM   1975  C  CE2 . TYR A  1 256 ? -1.415  -26.297 22.167   1.00 164.27 ? 256  TYR A CE2 1 
ATOM   1976  C  CZ  . TYR A  1 256 ? -2.183  -27.057 21.311   1.00 178.31 ? 256  TYR A CZ  1 
ATOM   1977  O  OH  . TYR A  1 256 ? -3.430  -26.610 20.939   1.00 166.12 ? 256  TYR A OH  1 
ATOM   1978  N  N   . ASP A  1 257 ? 3.327   -31.096 23.325   1.00 186.80 ? 257  ASP A N   1 
ATOM   1979  C  CA  . ASP A  1 257 ? 4.646   -31.718 23.344   1.00 213.56 ? 257  ASP A CA  1 
ATOM   1980  C  C   . ASP A  1 257 ? 5.658   -30.875 22.574   1.00 210.34 ? 257  ASP A C   1 
ATOM   1981  O  O   . ASP A  1 257 ? 5.367   -30.360 21.490   1.00 209.72 ? 257  ASP A O   1 
ATOM   1982  C  CB  . ASP A  1 257 ? 4.574   -33.124 22.749   1.00 217.64 ? 257  ASP A CB  1 
ATOM   1983  C  CG  . ASP A  1 257 ? 5.904   -33.847 22.796   1.00 218.96 ? 257  ASP A CG  1 
ATOM   1984  O  OD1 . ASP A  1 257 ? 6.667   -33.642 23.766   1.00 226.93 ? 257  ASP A OD1 1 
ATOM   1985  O  OD2 . ASP A  1 257 ? 6.188   -34.616 21.855   1.00 219.70 ? 257  ASP A OD2 1 
ATOM   1986  N  N   . GLY A  1 258 ? 6.855   -30.738 23.142   1.00 204.92 ? 258  GLY A N   1 
ATOM   1987  C  CA  . GLY A  1 258 ? 7.890   -29.910 22.550   1.00 198.89 ? 258  GLY A CA  1 
ATOM   1988  C  C   . GLY A  1 258 ? 8.732   -30.594 21.493   1.00 204.45 ? 258  GLY A C   1 
ATOM   1989  O  O   . GLY A  1 258 ? 9.826   -30.122 21.166   1.00 207.51 ? 258  GLY A O   1 
ATOM   1990  N  N   . LYS A  1 259 ? 8.238   -31.698 20.945   1.00 198.43 ? 259  LYS A N   1 
ATOM   1991  C  CA  . LYS A  1 259 ? 8.952   -32.436 19.910   1.00 204.13 ? 259  LYS A CA  1 
ATOM   1992  C  C   . LYS A  1 259 ? 8.175   -32.539 18.608   1.00 218.17 ? 259  LYS A C   1 
ATOM   1993  O  O   . LYS A  1 259 ? 8.765   -32.384 17.535   1.00 226.73 ? 259  LYS A O   1 
ATOM   1994  C  CB  . LYS A  1 259 ? 9.308   -33.850 20.407   1.00 210.74 ? 259  LYS A CB  1 
ATOM   1995  C  CG  . LYS A  1 259 ? 10.284  -34.604 19.506   1.00 215.32 ? 259  LYS A CG  1 
ATOM   1996  C  CD  . LYS A  1 259 ? 10.509  -36.035 19.977   1.00 219.63 ? 259  LYS A CD  1 
ATOM   1997  C  CE  . LYS A  1 259 ? 9.268   -36.884 19.777   1.00 225.24 ? 259  LYS A CE  1 
ATOM   1998  N  NZ  . LYS A  1 259 ? 9.500   -38.305 20.153   1.00 235.00 ? 259  LYS A NZ  1 
ATOM   1999  N  N   . ASN A  1 260 ? 6.862   -32.788 18.663   1.00 191.97 ? 260  ASN A N   1 
ATOM   2000  C  CA  . ASN A  1 260 ? 6.071   -32.924 17.446   1.00 192.90 ? 260  ASN A CA  1 
ATOM   2001  C  C   . ASN A  1 260 ? 4.767   -32.141 17.492   1.00 185.96 ? 260  ASN A C   1 
ATOM   2002  O  O   . ASN A  1 260 ? 3.902   -32.353 16.633   1.00 185.55 ? 260  ASN A O   1 
ATOM   2003  C  CB  . ASN A  1 260 ? 5.773   -34.399 17.143   1.00 221.56 ? 260  ASN A CB  1 
ATOM   2004  C  CG  . ASN A  1 260 ? 5.117   -35.129 18.305   1.00 226.27 ? 260  ASN A CG  1 
ATOM   2005  O  OD1 . ASN A  1 260 ? 4.475   -34.521 19.163   1.00 188.62 ? 260  ASN A OD1 1 
ATOM   2006  N  ND2 . ASN A  1 260 ? 5.280   -36.450 18.331   1.00 316.68 ? 260  ASN A ND2 1 
ATOM   2007  N  N   . MET A  1 261 ? 4.597   -31.256 18.473   1.00 181.72 ? 261  MET A N   1 
ATOM   2008  C  CA  . MET A  1 261 ? 3.433   -30.378 18.569   1.00 176.37 ? 261  MET A CA  1 
ATOM   2009  C  C   . MET A  1 261 ? 2.141   -31.202 18.653   1.00 174.76 ? 261  MET A C   1 
ATOM   2010  O  O   . MET A  1 261 ? 1.331   -31.257 17.722   1.00 183.32 ? 261  MET A O   1 
ATOM   2011  C  CB  . MET A  1 261 ? 3.399   -29.397 17.390   1.00 178.12 ? 261  MET A CB  1 
ATOM   2012  C  CG  . MET A  1 261 ? 2.605   -28.143 17.673   1.00 170.98 ? 261  MET A CG  1 
ATOM   2013  S  SD  . MET A  1 261 ? 3.264   -27.276 19.114   1.00 168.86 ? 261  MET A SD  1 
ATOM   2014  C  CE  . MET A  1 261 ? 4.505   -26.224 18.376   1.00 171.36 ? 261  MET A CE  1 
ATOM   2015  N  N   . SER A  1 262 ? 1.981   -31.857 19.805   1.00 180.34 ? 262  SER A N   1 
ATOM   2016  C  CA  . SER A  1 262 ? 0.788   -32.631 20.122   1.00 186.34 ? 262  SER A CA  1 
ATOM   2017  C  C   . SER A  1 262 ? 0.274   -32.233 21.498   1.00 174.92 ? 262  SER A C   1 
ATOM   2018  O  O   . SER A  1 262 ? 1.057   -32.006 22.423   1.00 175.10 ? 262  SER A O   1 
ATOM   2019  C  CB  . SER A  1 262 ? 1.075   -34.138 20.094   1.00 209.01 ? 262  SER A CB  1 
ATOM   2020  O  OG  . SER A  1 262 ? -0.091  -34.888 20.387   1.00 221.93 ? 262  SER A OG  1 
ATOM   2021  N  N   . SER A  1 263 ? -1.050  -32.212 21.645   1.00 178.87 ? 263  SER A N   1 
ATOM   2022  C  CA  . SER A  1 263 ? -1.657  -31.800 22.904   1.00 174.10 ? 263  SER A CA  1 
ATOM   2023  C  C   . SER A  1 263 ? -1.435  -32.857 23.979   1.00 190.09 ? 263  SER A C   1 
ATOM   2024  O  O   . SER A  1 263 ? -1.649  -34.051 23.748   1.00 213.39 ? 263  SER A O   1 
ATOM   2025  C  CB  . SER A  1 263 ? -3.151  -31.548 22.719   1.00 174.19 ? 263  SER A CB  1 
ATOM   2026  O  OG  . SER A  1 263 ? -3.721  -31.005 23.898   1.00 178.50 ? 263  SER A OG  1 
ATOM   2027  N  N   . LEU A  1 264 ? -0.989  -32.418 25.156   1.00 181.82 ? 264  LEU A N   1 
ATOM   2028  C  CA  . LEU A  1 264 ? -0.700  -33.321 26.263   1.00 177.69 ? 264  LEU A CA  1 
ATOM   2029  C  C   . LEU A  1 264 ? -1.738  -33.226 27.374   1.00 174.61 ? 264  LEU A C   1 
ATOM   2030  O  O   . LEU A  1 264 ? -2.349  -34.235 27.737   1.00 175.61 ? 264  LEU A O   1 
ATOM   2031  C  CB  . LEU A  1 264 ? 0.701   -33.040 26.827   1.00 190.81 ? 264  LEU A CB  1 
ATOM   2032  C  CG  . LEU A  1 264 ? 1.915   -33.337 25.946   1.00 192.57 ? 264  LEU A CG  1 
ATOM   2033  C  CD1 . LEU A  1 264 ? 3.196   -33.058 26.714   1.00 185.89 ? 264  LEU A CD1 1 
ATOM   2034  C  CD2 . LEU A  1 264 ? 1.889   -34.772 25.451   1.00 195.11 ? 264  LEU A CD2 1 
ATOM   2035  N  N   . TYR A  1 265 ? -1.968  -32.032 27.913   1.00 174.19 ? 265  TYR A N   1 
ATOM   2036  C  CA  . TYR A  1 265 ? -2.857  -31.850 29.052   1.00 180.25 ? 265  TYR A CA  1 
ATOM   2037  C  C   . TYR A  1 265 ? -3.642  -30.557 28.868   1.00 161.55 ? 265  TYR A C   1 
ATOM   2038  O  O   . TYR A  1 265 ? -3.242  -29.664 28.115   1.00 160.85 ? 265  TYR A O   1 
ATOM   2039  C  CB  . TYR A  1 265 ? -2.080  -31.827 30.380   1.00 198.19 ? 265  TYR A CB  1 
ATOM   2040  C  CG  . TYR A  1 265 ? -1.372  -33.130 30.745   1.00 224.15 ? 265  TYR A CG  1 
ATOM   2041  C  CD1 . TYR A  1 265 ? -2.057  -34.171 31.367   1.00 218.37 ? 265  TYR A CD1 1 
ATOM   2042  C  CD2 . TYR A  1 265 ? -0.018  -33.311 30.478   1.00 210.46 ? 265  TYR A CD2 1 
ATOM   2043  C  CE1 . TYR A  1 265 ? -1.412  -35.358 31.706   1.00 202.35 ? 265  TYR A CE1 1 
ATOM   2044  C  CE2 . TYR A  1 265 ? 0.631   -34.492 30.814   1.00 191.06 ? 265  TYR A CE2 1 
ATOM   2045  C  CZ  . TYR A  1 265 ? -0.071  -35.509 31.426   1.00 178.66 ? 265  TYR A CZ  1 
ATOM   2046  O  OH  . TYR A  1 265 ? 0.567   -36.677 31.760   1.00 183.09 ? 265  TYR A OH  1 
ATOM   2047  N  N   . ASN A  1 266 ? -4.794  -30.481 29.538   1.00 165.01 ? 266  ASN A N   1 
ATOM   2048  C  CA  . ASN A  1 266 ? -5.636  -29.291 29.512   1.00 184.16 ? 266  ASN A CA  1 
ATOM   2049  C  C   . ASN A  1 266 ? -6.012  -28.808 30.907   1.00 182.45 ? 266  ASN A C   1 
ATOM   2050  O  O   . ASN A  1 266 ? -6.249  -29.607 31.820   1.00 195.61 ? 266  ASN A O   1 
ATOM   2051  C  CB  . ASN A  1 266 ? -6.919  -29.533 28.722   1.00 202.51 ? 266  ASN A CB  1 
ATOM   2052  C  CG  . ASN A  1 266 ? -6.724  -29.378 27.235   1.00 208.40 ? 266  ASN A CG  1 
ATOM   2053  O  OD1 . ASN A  1 266 ? -5.798  -28.698 26.783   1.00 182.27 ? 266  ASN A OD1 1 
ATOM   2054  N  ND2 . ASN A  1 266 ? -7.597  -30.001 26.459   1.00 264.21 ? 266  ASN A ND2 1 
ATOM   2055  N  N   . PHE A  1 267 ? -6.077  -27.488 31.051   1.00 148.17 ? 267  PHE A N   1 
ATOM   2056  C  CA  . PHE A  1 267 ? -6.674  -26.832 32.202   1.00 146.56 ? 267  PHE A CA  1 
ATOM   2057  C  C   . PHE A  1 267 ? -7.798  -25.933 31.714   1.00 173.15 ? 267  PHE A C   1 
ATOM   2058  O  O   . PHE A  1 267 ? -7.740  -25.384 30.610   1.00 165.52 ? 267  PHE A O   1 
ATOM   2059  C  CB  . PHE A  1 267 ? -5.661  -26.002 32.981   1.00 146.81 ? 267  PHE A CB  1 
ATOM   2060  C  CG  . PHE A  1 267 ? -4.491  -26.787 33.476   1.00 184.79 ? 267  PHE A CG  1 
ATOM   2061  C  CD1 . PHE A  1 267 ? -4.529  -27.422 34.707   1.00 194.40 ? 267  PHE A CD1 1 
ATOM   2062  C  CD2 . PHE A  1 267 ? -3.343  -26.891 32.706   1.00 191.66 ? 267  PHE A CD2 1 
ATOM   2063  C  CE1 . PHE A  1 267 ? -3.435  -28.148 35.160   1.00 194.62 ? 267  PHE A CE1 1 
ATOM   2064  C  CE2 . PHE A  1 267 ? -2.251  -27.611 33.148   1.00 154.08 ? 267  PHE A CE2 1 
ATOM   2065  C  CZ  . PHE A  1 267 ? -2.294  -28.241 34.376   1.00 177.83 ? 267  PHE A CZ  1 
ATOM   2066  N  N   . THR A  1 268 ? -8.826  -25.789 32.543   1.00 174.32 ? 268  THR A N   1 
ATOM   2067  C  CA  . THR A  1 268 ? -9.989  -24.984 32.205   1.00 141.24 ? 268  THR A CA  1 
ATOM   2068  C  C   . THR A  1 268 ? -10.331 -24.055 33.361   1.00 140.39 ? 268  THR A C   1 
ATOM   2069  O  O   . THR A  1 268 ? -10.338 -24.478 34.523   1.00 141.17 ? 268  THR A O   1 
ATOM   2070  C  CB  . THR A  1 268 ? -11.178 -25.881 31.855   1.00 161.05 ? 268  THR A CB  1 
ATOM   2071  O  OG1 . THR A  1 268 ? -10.762 -26.859 30.894   1.00 143.77 ? 268  THR A OG1 1 
ATOM   2072  C  CG2 . THR A  1 268 ? -12.329 -25.062 31.286   1.00 167.16 ? 268  THR A CG2 1 
ATOM   2073  N  N   . GLY A  1 269 ? -10.587 -22.786 33.037   1.00 134.44 ? 269  GLY A N   1 
ATOM   2074  C  CA  . GLY A  1 269 ? -11.099 -21.858 34.024   1.00 141.73 ? 269  GLY A CA  1 
ATOM   2075  C  C   . GLY A  1 269 ? -12.466 -22.271 34.526   1.00 133.01 ? 269  GLY A C   1 
ATOM   2076  O  O   . GLY A  1 269 ? -13.155 -23.094 33.927   1.00 133.11 ? 269  GLY A O   1 
ATOM   2077  N  N   . GLU A  1 270 ? -12.856 -21.695 35.659   1.00 133.21 ? 270  GLU A N   1 
ATOM   2078  C  CA  . GLU A  1 270 ? -14.100 -22.077 36.311   1.00 155.75 ? 270  GLU A CA  1 
ATOM   2079  C  C   . GLU A  1 270 ? -15.108 -20.938 36.409   1.00 162.38 ? 270  GLU A C   1 
ATOM   2080  O  O   . GLU A  1 270 ? -16.184 -21.123 37.000   1.00 133.98 ? 270  GLU A O   1 
ATOM   2081  C  CB  . GLU A  1 270 ? -13.801 -22.648 37.706   1.00 152.12 ? 270  GLU A CB  1 
ATOM   2082  C  CG  . GLU A  1 270 ? -12.905 -23.886 37.690   1.00 135.94 ? 270  GLU A CG  1 
ATOM   2083  C  CD  . GLU A  1 270 ? -13.643 -25.156 37.269   1.00 142.52 ? 270  GLU A CD  1 
ATOM   2084  O  OE1 . GLU A  1 270 ? -14.836 -25.077 36.903   1.00 142.97 ? 270  GLU A OE1 1 
ATOM   2085  O  OE2 . GLU A  1 270 ? -13.025 -26.240 37.295   1.00 146.79 ? 270  GLU A OE2 1 
ATOM   2086  N  N   . GLN A  1 271 ? -14.800 -19.778 35.832   1.00 170.55 ? 271  GLN A N   1 
ATOM   2087  C  CA  . GLN A  1 271 ? -15.684 -18.623 35.828   1.00 148.68 ? 271  GLN A CA  1 
ATOM   2088  C  C   . GLN A  1 271 ? -15.621 -17.922 34.479   1.00 149.14 ? 271  GLN A C   1 
ATOM   2089  O  O   . GLN A  1 271 ? -14.532 -17.725 33.930   1.00 173.44 ? 271  GLN A O   1 
ATOM   2090  C  CB  . GLN A  1 271 ? -15.290 -17.641 36.918   1.00 133.28 ? 271  GLN A CB  1 
ATOM   2091  C  CG  . GLN A  1 271 ? -16.217 -16.484 37.044   1.00 133.84 ? 271  GLN A CG  1 
ATOM   2092  C  CD  . GLN A  1 271 ? -15.783 -15.561 38.137   1.00 135.02 ? 271  GLN A CD  1 
ATOM   2093  O  OE1 . GLN A  1 271 ? -15.122 -14.555 37.892   1.00 135.03 ? 271  GLN A OE1 1 
ATOM   2094  N  NE2 . GLN A  1 271 ? -16.113 -15.918 39.368   1.00 136.32 ? 271  GLN A NE2 1 
ATOM   2095  N  N   . MET A  1 272 ? -16.787 -17.515 33.970   1.00 140.57 ? 272  MET A N   1 
ATOM   2096  C  CA  . MET A  1 272 ? -16.857 -16.839 32.676   1.00 131.18 ? 272  MET A CA  1 
ATOM   2097  C  C   . MET A  1 272 ? -16.074 -15.532 32.712   1.00 131.21 ? 272  MET A C   1 
ATOM   2098  O  O   . MET A  1 272 ? -16.170 -14.766 33.675   1.00 131.98 ? 272  MET A O   1 
ATOM   2099  C  CB  . MET A  1 272 ? -18.321 -16.571 32.303   1.00 131.76 ? 272  MET A CB  1 
ATOM   2100  C  CG  . MET A  1 272 ? -19.194 -17.819 32.266   1.00 152.44 ? 272  MET A CG  1 
ATOM   2101  S  SD  . MET A  1 272 ? -18.873 -18.810 30.795   1.00 198.23 ? 272  MET A SD  1 
ATOM   2102  C  CE  . MET A  1 272 ? -20.033 -20.164 30.993   1.00 187.45 ? 272  MET A CE  1 
ATOM   2103  N  N   . ALA A  1 273 ? -15.263 -15.303 31.676   1.00 130.69 ? 273  ALA A N   1 
ATOM   2104  C  CA  . ALA A  1 273 ? -14.562 -14.033 31.477   1.00 130.96 ? 273  ALA A CA  1 
ATOM   2105  C  C   . ALA A  1 273 ? -13.686 -13.652 32.669   1.00 142.78 ? 273  ALA A C   1 
ATOM   2106  O  O   . ALA A  1 273 ? -13.543 -12.469 32.998   1.00 134.26 ? 273  ALA A O   1 
ATOM   2107  C  CB  . ALA A  1 273 ? -15.547 -12.909 31.160   1.00 131.63 ? 273  ALA A CB  1 
ATOM   2108  N  N   . ALA A  1 274 ? -13.116 -14.653 33.338   1.00 158.67 ? 274  ALA A N   1 
ATOM   2109  C  CA  . ALA A  1 274 ? -12.129 -14.450 34.387   1.00 132.59 ? 274  ALA A CA  1 
ATOM   2110  C  C   . ALA A  1 274 ? -10.725 -14.303 33.831   1.00 132.29 ? 274  ALA A C   1 
ATOM   2111  O  O   . ALA A  1 274 ? -9.786  -14.056 34.599   1.00 137.45 ? 274  ALA A O   1 
ATOM   2112  C  CB  . ALA A  1 274 ? -12.166 -15.616 35.382   1.00 132.43 ? 274  ALA A CB  1 
ATOM   2113  N  N   . TYR A  1 275 ? -10.566 -14.462 32.521   1.00 131.70 ? 275  TYR A N   1 
ATOM   2114  C  CA  . TYR A  1 275 ? -9.267  -14.409 31.866   1.00 132.12 ? 275  TYR A CA  1 
ATOM   2115  C  C   . TYR A  1 275 ? -8.328  -15.460 32.450   1.00 132.68 ? 275  TYR A C   1 
ATOM   2116  O  O   . TYR A  1 275 ? -7.155  -15.192 32.719   1.00 133.71 ? 275  TYR A O   1 
ATOM   2117  C  CB  . TYR A  1 275 ? -8.654  -13.008 31.926   1.00 133.01 ? 275  TYR A CB  1 
ATOM   2118  C  CG  . TYR A  1 275 ? -8.333  -12.471 30.548   1.00 133.12 ? 275  TYR A CG  1 
ATOM   2119  C  CD1 . TYR A  1 275 ? -9.326  -11.924 29.739   1.00 132.70 ? 275  TYR A CD1 1 
ATOM   2120  C  CD2 . TYR A  1 275 ? -7.045  -12.535 30.042   1.00 133.98 ? 275  TYR A CD2 1 
ATOM   2121  C  CE1 . TYR A  1 275 ? -9.037  -11.443 28.467   1.00 133.07 ? 275  TYR A CE1 1 
ATOM   2122  C  CE2 . TYR A  1 275 ? -6.747  -12.058 28.776   1.00 134.40 ? 275  TYR A CE2 1 
ATOM   2123  C  CZ  . TYR A  1 275 ? -7.743  -11.515 27.994   1.00 133.90 ? 275  TYR A CZ  1 
ATOM   2124  O  OH  . TYR A  1 275 ? -7.432  -11.047 26.740   1.00 134.58 ? 275  TYR A OH  1 
ATOM   2125  N  N   . PHE A  1 276 ? -8.872  -16.652 32.705   1.00 156.10 ? 276  PHE A N   1 
ATOM   2126  C  CA  . PHE A  1 276 ? -8.069  -17.824 33.029   1.00 143.28 ? 276  PHE A CA  1 
ATOM   2127  C  C   . PHE A  1 276 ? -7.065  -18.069 31.913   1.00 133.66 ? 276  PHE A C   1 
ATOM   2128  O  O   . PHE A  1 276 ? -7.442  -18.494 30.817   1.00 133.26 ? 276  PHE A O   1 
ATOM   2129  C  CB  . PHE A  1 276 ? -8.964  -19.049 33.230   1.00 132.75 ? 276  PHE A CB  1 
ATOM   2130  C  CG  . PHE A  1 276 ? -8.220  -20.290 33.641   1.00 141.81 ? 276  PHE A CG  1 
ATOM   2131  C  CD1 . PHE A  1 276 ? -7.957  -20.541 34.977   1.00 168.96 ? 276  PHE A CD1 1 
ATOM   2132  C  CD2 . PHE A  1 276 ? -7.793  -21.210 32.695   1.00 143.37 ? 276  PHE A CD2 1 
ATOM   2133  C  CE1 . PHE A  1 276 ? -7.276  -21.682 35.363   1.00 180.05 ? 276  PHE A CE1 1 
ATOM   2134  C  CE2 . PHE A  1 276 ? -7.107  -22.352 33.076   1.00 153.67 ? 276  PHE A CE2 1 
ATOM   2135  C  CZ  . PHE A  1 276 ? -6.853  -22.588 34.412   1.00 164.50 ? 276  PHE A CZ  1 
ATOM   2136  N  N   . GLY A  1 277 ? -5.784  -17.835 32.185   1.00 134.95 ? 277  GLY A N   1 
ATOM   2137  C  CA  . GLY A  1 277 ? -4.753  -17.993 31.181   1.00 136.01 ? 277  GLY A CA  1 
ATOM   2138  C  C   . GLY A  1 277 ? -4.072  -16.716 30.745   1.00 136.57 ? 277  GLY A C   1 
ATOM   2139  O  O   . GLY A  1 277 ? -3.294  -16.758 29.788   1.00 137.60 ? 277  GLY A O   1 
ATOM   2140  N  N   . PHE A  1 278 ? -4.367  -15.577 31.378   1.00 136.22 ? 278  PHE A N   1 
ATOM   2141  C  CA  . PHE A  1 278 ? -3.693  -14.327 31.032   1.00 137.14 ? 278  PHE A CA  1 
ATOM   2142  C  C   . PHE A  1 278 ? -2.186  -14.431 31.194   1.00 139.24 ? 278  PHE A C   1 
ATOM   2143  O  O   . PHE A  1 278 ? -1.429  -13.914 30.365   1.00 140.39 ? 278  PHE A O   1 
ATOM   2144  C  CB  . PHE A  1 278 ? -4.212  -13.185 31.896   1.00 136.96 ? 278  PHE A CB  1 
ATOM   2145  C  CG  . PHE A  1 278 ? -3.518  -11.874 31.649   1.00 138.28 ? 278  PHE A CG  1 
ATOM   2146  C  CD1 . PHE A  1 278 ? -3.861  -11.095 30.564   1.00 138.04 ? 278  PHE A CD1 1 
ATOM   2147  C  CD2 . PHE A  1 278 ? -2.556  -11.402 32.522   1.00 140.06 ? 278  PHE A CD2 1 
ATOM   2148  C  CE1 . PHE A  1 278 ? -3.243  -9.884  30.333   1.00 139.54 ? 278  PHE A CE1 1 
ATOM   2149  C  CE2 . PHE A  1 278 ? -1.939  -10.189 32.300   1.00 141.58 ? 278  PHE A CE2 1 
ATOM   2150  C  CZ  . PHE A  1 278 ? -2.283  -9.430  31.203   1.00 141.32 ? 278  PHE A CZ  1 
ATOM   2151  N  N   . SER A  1 279 ? -1.731  -15.046 32.284   1.00 153.83 ? 279  SER A N   1 
ATOM   2152  C  CA  . SER A  1 279 ? -0.316  -15.266 32.535   1.00 142.47 ? 279  SER A CA  1 
ATOM   2153  C  C   . SER A  1 279 ? -0.116  -16.694 33.011   1.00 143.06 ? 279  SER A C   1 
ATOM   2154  O  O   . SER A  1 279 ? -0.946  -17.233 33.751   1.00 141.96 ? 279  SER A O   1 
ATOM   2155  C  CB  . SER A  1 279 ? 0.229   -14.294 33.577   1.00 143.83 ? 279  SER A CB  1 
ATOM   2156  O  OG  . SER A  1 279 ? -0.404  -14.505 34.824   1.00 143.27 ? 279  SER A OG  1 
ATOM   2157  N  N   . VAL A  1 280 ? 0.992   -17.300 32.581   1.00 145.15 ? 280  VAL A N   1 
ATOM   2158  C  CA  . VAL A  1 280 ? 1.365   -18.648 32.982   1.00 146.45 ? 280  VAL A CA  1 
ATOM   2159  C  C   . VAL A  1 280 ? 2.852   -18.676 33.311   1.00 149.68 ? 280  VAL A C   1 
ATOM   2160  O  O   . VAL A  1 280 ? 3.629   -17.830 32.865   1.00 150.96 ? 280  VAL A O   1 
ATOM   2161  C  CB  . VAL A  1 280 ? 1.040   -19.695 31.895   1.00 146.16 ? 280  VAL A CB  1 
ATOM   2162  C  CG1 . VAL A  1 280 ? -0.462  -19.902 31.793   1.00 143.41 ? 280  VAL A CG1 1 
ATOM   2163  C  CG2 . VAL A  1 280 ? 1.622   -19.267 30.559   1.00 147.07 ? 280  VAL A CG2 1 
ATOM   2164  N  N   . ALA A  1 281 ? 3.236   -19.664 34.114   1.00 151.28 ? 281  ALA A N   1 
ATOM   2165  C  CA  . ALA A  1 281 ? 4.625   -19.859 34.497   1.00 154.79 ? 281  ALA A CA  1 
ATOM   2166  C  C   . ALA A  1 281 ? 4.829   -21.326 34.830   1.00 156.46 ? 281  ALA A C   1 
ATOM   2167  O  O   . ALA A  1 281 ? 3.889   -22.022 35.215   1.00 154.89 ? 281  ALA A O   1 
ATOM   2168  C  CB  . ALA A  1 281 ? 5.016   -18.981 35.689   1.00 155.73 ? 281  ALA A CB  1 
ATOM   2169  N  N   . ALA A  1 282 ? 6.058   -21.801 34.655   1.00 159.98 ? 282  ALA A N   1 
ATOM   2170  C  CA  . ALA A  1 282 ? 6.383   -23.197 34.928   1.00 162.32 ? 282  ALA A CA  1 
ATOM   2171  C  C   . ALA A  1 282 ? 7.688   -23.283 35.710   1.00 166.34 ? 282  ALA A C   1 
ATOM   2172  O  O   . ALA A  1 282 ? 8.754   -22.929 35.194   1.00 168.94 ? 282  ALA A O   1 
ATOM   2173  C  CB  . ALA A  1 282 ? 6.460   -24.000 33.632   1.00 163.16 ? 282  ALA A CB  1 
ATOM   2174  N  N   . THR A  1 283 ? 7.598   -23.757 36.954   1.00 173.91 ? 283  THR A N   1 
ATOM   2175  C  CA  . THR A  1 283 ? 8.765   -23.997 37.795   1.00 188.97 ? 283  THR A CA  1 
ATOM   2176  C  C   . THR A  1 283 ? 8.398   -25.026 38.859   1.00 190.73 ? 283  THR A C   1 
ATOM   2177  O  O   . THR A  1 283 ? 7.270   -25.034 39.359   1.00 196.22 ? 283  THR A O   1 
ATOM   2178  C  CB  . THR A  1 283 ? 9.266   -22.702 38.451   1.00 180.22 ? 283  THR A CB  1 
ATOM   2179  O  OG1 . THR A  1 283 ? 10.314  -23.002 39.380   1.00 204.37 ? 283  THR A OG1 1 
ATOM   2180  C  CG2 . THR A  1 283 ? 8.138   -22.009 39.195   1.00 168.35 ? 283  THR A CG2 1 
ATOM   2181  N  N   . ASP A  1 284 ? 9.353   -25.895 39.191   1.00 200.04 ? 284  ASP A N   1 
ATOM   2182  C  CA  . ASP A  1 284 ? 9.171   -26.902 40.239   1.00 186.99 ? 284  ASP A CA  1 
ATOM   2183  C  C   . ASP A  1 284 ? 9.153   -26.229 41.608   1.00 187.12 ? 284  ASP A C   1 
ATOM   2184  O  O   . ASP A  1 284 ? 10.165  -25.675 42.045   1.00 221.50 ? 284  ASP A O   1 
ATOM   2185  C  CB  . ASP A  1 284 ? 10.283  -27.943 40.162   1.00 207.95 ? 284  ASP A CB  1 
ATOM   2186  C  CG  . ASP A  1 284 ? 10.173  -28.986 41.253   1.00 212.63 ? 284  ASP A CG  1 
ATOM   2187  O  OD1 . ASP A  1 284 ? 9.031   -29.317 41.636   1.00 205.53 ? 284  ASP A OD1 1 
ATOM   2188  O  OD2 . ASP A  1 284 ? 11.225  -29.472 41.727   1.00 199.19 ? 284  ASP A OD2 1 
ATOM   2189  N  N   . ILE A  1 285 ? 8.009   -26.278 42.292   1.00 175.50 ? 285  ILE A N   1 
ATOM   2190  C  CA  . ILE A  1 285 ? 7.838   -25.547 43.543   1.00 175.41 ? 285  ILE A CA  1 
ATOM   2191  C  C   . ILE A  1 285 ? 7.967   -26.434 44.780   1.00 178.43 ? 285  ILE A C   1 
ATOM   2192  O  O   . ILE A  1 285 ? 8.168   -25.907 45.885   1.00 179.81 ? 285  ILE A O   1 
ATOM   2193  C  CB  . ILE A  1 285 ? 6.482   -24.812 43.561   1.00 170.78 ? 285  ILE A CB  1 
ATOM   2194  C  CG1 . ILE A  1 285 ? 6.557   -23.553 44.428   1.00 170.76 ? 285  ILE A CG1 1 
ATOM   2195  C  CG2 . ILE A  1 285 ? 5.371   -25.740 44.036   1.00 169.53 ? 285  ILE A CG2 1 
ATOM   2196  C  CD1 . ILE A  1 285 ? 7.350   -22.433 43.786   1.00 171.09 ? 285  ILE A CD1 1 
ATOM   2197  N  N   . ASN A  1 286 ? 7.850   -27.753 44.633   1.00 179.77 ? 286  ASN A N   1 
ATOM   2198  C  CA  . ASN A  1 286 ? 7.844   -28.668 45.768   1.00 182.63 ? 286  ASN A CA  1 
ATOM   2199  C  C   . ASN A  1 286 ? 9.014   -29.646 45.734   1.00 187.73 ? 286  ASN A C   1 
ATOM   2200  O  O   . ASN A  1 286 ? 8.951   -30.699 46.375   1.00 190.28 ? 286  ASN A O   1 
ATOM   2201  C  CB  . ASN A  1 286 ? 6.522   -29.431 45.816   1.00 180.18 ? 286  ASN A CB  1 
ATOM   2202  C  CG  . ASN A  1 286 ? 6.212   -30.132 44.508   1.00 178.87 ? 286  ASN A CG  1 
ATOM   2203  O  OD1 . ASN A  1 286 ? 6.649   -29.700 43.440   1.00 178.11 ? 286  ASN A OD1 1 
ATOM   2204  N  ND2 . ASN A  1 286 ? 5.462   -31.224 44.585   1.00 179.25 ? 286  ASN A ND2 1 
ATOM   2205  N  N   . GLY A  1 287 ? 10.080  -29.312 45.010   1.00 189.60 ? 287  GLY A N   1 
ATOM   2206  C  CA  . GLY A  1 287 ? 11.299  -30.099 45.001   1.00 195.04 ? 287  GLY A CA  1 
ATOM   2207  C  C   . GLY A  1 287 ? 11.136  -31.547 44.581   1.00 196.82 ? 287  GLY A C   1 
ATOM   2208  O  O   . GLY A  1 287 ? 11.628  -32.449 45.265   1.00 221.52 ? 287  GLY A O   1 
ATOM   2209  N  N   . ASP A  1 288 ? 10.461  -31.795 43.460   1.00 199.69 ? 288  ASP A N   1 
ATOM   2210  C  CA  . ASP A  1 288 ? 10.320  -33.149 42.936   1.00 201.64 ? 288  ASP A CA  1 
ATOM   2211  C  C   . ASP A  1 288 ? 10.841  -33.281 41.509   1.00 202.50 ? 288  ASP A C   1 
ATOM   2212  O  O   . ASP A  1 288 ? 10.679  -34.344 40.896   1.00 204.03 ? 288  ASP A O   1 
ATOM   2213  C  CB  . ASP A  1 288 ? 8.857   -33.616 43.024   1.00 206.05 ? 288  ASP A CB  1 
ATOM   2214  C  CG  . ASP A  1 288 ? 7.860   -32.595 42.473   1.00 208.19 ? 288  ASP A CG  1 
ATOM   2215  O  OD1 . ASP A  1 288 ? 8.161   -31.382 42.476   1.00 217.77 ? 288  ASP A OD1 1 
ATOM   2216  O  OD2 . ASP A  1 288 ? 6.759   -33.007 42.046   1.00 189.38 ? 288  ASP A OD2 1 
ATOM   2217  N  N   . ASP A  1 289 ? 11.480  -32.239 40.976   1.00 198.65 ? 289  ASP A N   1 
ATOM   2218  C  CA  . ASP A  1 289 ? 12.029  -32.178 39.624   1.00 199.58 ? 289  ASP A CA  1 
ATOM   2219  C  C   . ASP A  1 289 ? 10.952  -32.238 38.549   1.00 204.39 ? 289  ASP A C   1 
ATOM   2220  O  O   . ASP A  1 289 ? 11.274  -32.422 37.364   1.00 196.41 ? 289  ASP A O   1 
ATOM   2221  C  CB  . ASP A  1 289 ? 13.073  -33.273 39.382   1.00 205.81 ? 289  ASP A CB  1 
ATOM   2222  C  CG  . ASP A  1 289 ? 14.236  -33.183 40.344   1.00 210.58 ? 289  ASP A CG  1 
ATOM   2223  O  OD1 . ASP A  1 289 ? 14.132  -33.736 41.459   1.00 219.92 ? 289  ASP A OD1 1 
ATOM   2224  O  OD2 . ASP A  1 289 ? 15.251  -32.548 39.988   1.00 212.88 ? 289  ASP A OD2 1 
ATOM   2225  N  N   . TYR A  1 290 ? 9.681   -32.098 38.925   1.00 210.68 ? 290  TYR A N   1 
ATOM   2226  C  CA  . TYR A  1 290 ? 8.572   -31.957 37.984   1.00 197.84 ? 290  TYR A CA  1 
ATOM   2227  C  C   . TYR A  1 290 ? 8.117   -30.501 37.967   1.00 182.09 ? 290  TYR A C   1 
ATOM   2228  O  O   . TYR A  1 290 ? 7.639   -29.980 38.982   1.00 180.18 ? 290  TYR A O   1 
ATOM   2229  C  CB  . TYR A  1 290 ? 7.419   -32.884 38.354   1.00 188.36 ? 290  TYR A CB  1 
ATOM   2230  C  CG  . TYR A  1 290 ? 7.684   -34.332 38.031   1.00 189.25 ? 290  TYR A CG  1 
ATOM   2231  C  CD1 . TYR A  1 290 ? 8.306   -34.702 36.845   1.00 191.71 ? 290  TYR A CD1 1 
ATOM   2232  C  CD2 . TYR A  1 290 ? 7.319   -35.329 38.919   1.00 191.02 ? 290  TYR A CD2 1 
ATOM   2233  C  CE1 . TYR A  1 290 ? 8.546   -36.025 36.555   1.00 195.87 ? 290  TYR A CE1 1 
ATOM   2234  C  CE2 . TYR A  1 290 ? 7.558   -36.648 38.641   1.00 195.10 ? 290  TYR A CE2 1 
ATOM   2235  C  CZ  . TYR A  1 290 ? 8.169   -36.995 37.461   1.00 197.56 ? 290  TYR A CZ  1 
ATOM   2236  O  OH  . TYR A  1 290 ? 8.405   -38.322 37.192   1.00 206.57 ? 290  TYR A OH  1 
ATOM   2237  N  N   . ALA A  1 291 ? 8.288   -29.844 36.822   1.00 181.78 ? 291  ALA A N   1 
ATOM   2238  C  CA  . ALA A  1 291 ? 7.825   -28.472 36.670   1.00 177.81 ? 291  ALA A CA  1 
ATOM   2239  C  C   . ALA A  1 291 ? 6.328   -28.389 36.937   1.00 173.42 ? 291  ALA A C   1 
ATOM   2240  O  O   . ALA A  1 291 ? 5.563   -29.279 36.554   1.00 173.19 ? 291  ALA A O   1 
ATOM   2241  C  CB  . ALA A  1 291 ? 8.145   -27.955 35.267   1.00 177.47 ? 291  ALA A CB  1 
ATOM   2242  N  N   . ASP A  1 292 ? 5.914   -27.313 37.605   1.00 199.52 ? 292  ASP A N   1 
ATOM   2243  C  CA  . ASP A  1 292 ? 4.534   -27.117 38.026   1.00 185.17 ? 292  ASP A CA  1 
ATOM   2244  C  C   . ASP A  1 292 ? 3.929   -25.911 37.315   1.00 163.85 ? 292  ASP A C   1 
ATOM   2245  O  O   . ASP A  1 292 ? 4.626   -24.940 37.004   1.00 184.00 ? 292  ASP A O   1 
ATOM   2246  C  CB  . ASP A  1 292 ? 4.457   -26.933 39.546   1.00 186.75 ? 292  ASP A CB  1 
ATOM   2247  C  CG  . ASP A  1 292 ? 5.142   -28.067 40.302   1.00 216.84 ? 292  ASP A CG  1 
ATOM   2248  O  OD1 . ASP A  1 292 ? 4.963   -29.239 39.905   1.00 224.37 ? 292  ASP A OD1 1 
ATOM   2249  O  OD2 . ASP A  1 292 ? 5.865   -27.791 41.285   1.00 220.66 ? 292  ASP A OD2 1 
ATOM   2250  N  N   . VAL A  1 293 ? 2.619   -25.972 37.078   1.00 159.39 ? 293  VAL A N   1 
ATOM   2251  C  CA  . VAL A  1 293 ? 1.913   -24.997 36.250   1.00 156.19 ? 293  VAL A CA  1 
ATOM   2252  C  C   . VAL A  1 293 ? 1.210   -23.974 37.132   1.00 167.56 ? 293  VAL A C   1 
ATOM   2253  O  O   . VAL A  1 293 ? 0.423   -24.336 38.016   1.00 163.68 ? 293  VAL A O   1 
ATOM   2254  C  CB  . VAL A  1 293 ? 0.906   -25.694 35.322   1.00 169.38 ? 293  VAL A CB  1 
ATOM   2255  C  CG1 . VAL A  1 293 ? 0.183   -24.672 34.458   1.00 172.63 ? 293  VAL A CG1 1 
ATOM   2256  C  CG2 . VAL A  1 293 ? 1.615   -26.725 34.460   1.00 157.19 ? 293  VAL A CG2 1 
ATOM   2257  N  N   . PHE A  1 294 ? 1.467   -22.696 36.865   1.00 162.43 ? 294  PHE A N   1 
ATOM   2258  C  CA  . PHE A  1 294 ? 0.829   -21.582 37.555   1.00 157.23 ? 294  PHE A CA  1 
ATOM   2259  C  C   . PHE A  1 294 ? 0.026   -20.789 36.536   1.00 146.44 ? 294  PHE A C   1 
ATOM   2260  O  O   . PHE A  1 294 ? 0.596   -20.252 35.581   1.00 163.39 ? 294  PHE A O   1 
ATOM   2261  C  CB  . PHE A  1 294 ? 1.869   -20.688 38.229   1.00 151.10 ? 294  PHE A CB  1 
ATOM   2262  C  CG  . PHE A  1 294 ? 2.659   -21.382 39.297   1.00 154.07 ? 294  PHE A CG  1 
ATOM   2263  C  CD1 . PHE A  1 294 ? 3.791   -22.111 38.970   1.00 167.09 ? 294  PHE A CD1 1 
ATOM   2264  C  CD2 . PHE A  1 294 ? 2.276   -21.304 40.625   1.00 154.40 ? 294  PHE A CD2 1 
ATOM   2265  C  CE1 . PHE A  1 294 ? 4.527   -22.753 39.944   1.00 166.44 ? 294  PHE A CE1 1 
ATOM   2266  C  CE2 . PHE A  1 294 ? 3.008   -21.943 41.608   1.00 172.48 ? 294  PHE A CE2 1 
ATOM   2267  C  CZ  . PHE A  1 294 ? 4.136   -22.670 41.266   1.00 185.93 ? 294  PHE A CZ  1 
ATOM   2268  N  N   . ILE A  1 295 ? -1.290  -20.723 36.728   1.00 144.20 ? 295  ILE A N   1 
ATOM   2269  C  CA  . ILE A  1 295 ? -2.199  -20.068 35.786   1.00 165.32 ? 295  ILE A CA  1 
ATOM   2270  C  C   . ILE A  1 295 ? -2.877  -18.891 36.476   1.00 162.05 ? 295  ILE A C   1 
ATOM   2271  O  O   . ILE A  1 295 ? -3.572  -19.071 37.484   1.00 177.92 ? 295  ILE A O   1 
ATOM   2272  C  CB  . ILE A  1 295 ? -3.246  -21.049 35.242   1.00 178.35 ? 295  ILE A CB  1 
ATOM   2273  C  CG1 . ILE A  1 295 ? -2.549  -22.267 34.634   1.00 190.23 ? 295  ILE A CG1 1 
ATOM   2274  C  CG2 . ILE A  1 295 ? -4.144  -20.356 34.223   1.00 138.47 ? 295  ILE A CG2 1 
ATOM   2275  C  CD1 . ILE A  1 295 ? -3.489  -23.390 34.270   1.00 197.67 ? 295  ILE A CD1 1 
ATOM   2276  N  N   . GLY A  1 296 ? -2.700  -17.695 35.917   1.00 140.35 ? 296  GLY A N   1 
ATOM   2277  C  CA  . GLY A  1 296 ? -3.322  -16.500 36.464   1.00 139.72 ? 296  GLY A CA  1 
ATOM   2278  C  C   . GLY A  1 296 ? -4.653  -16.203 35.792   1.00 137.63 ? 296  GLY A C   1 
ATOM   2279  O  O   . GLY A  1 296 ? -4.797  -16.346 34.582   1.00 136.77 ? 296  GLY A O   1 
ATOM   2280  N  N   . ALA A  1 297 ? -5.636  -15.805 36.607   1.00 154.05 ? 297  ALA A N   1 
ATOM   2281  C  CA  . ALA A  1 297 ? -6.957  -15.376 36.136   1.00 135.66 ? 297  ALA A CA  1 
ATOM   2282  C  C   . ALA A  1 297 ? -7.280  -14.047 36.804   1.00 136.28 ? 297  ALA A C   1 
ATOM   2283  O  O   . ALA A  1 297 ? -8.097  -13.988 37.733   1.00 136.53 ? 297  ALA A O   1 
ATOM   2284  C  CB  . ALA A  1 297 ? -8.027  -16.423 36.440   1.00 134.89 ? 297  ALA A CB  1 
ATOM   2285  N  N   . PRO A  1 298 ? -6.691  -12.950 36.315   1.00 136.85 ? 298  PRO A N   1 
ATOM   2286  C  CA  . PRO A  1 298 ? -6.738  -11.676 37.051   1.00 138.16 ? 298  PRO A CA  1 
ATOM   2287  C  C   . PRO A  1 298 ? -8.123  -11.094 37.168   1.00 137.73 ? 298  PRO A C   1 
ATOM   2288  O  O   . PRO A  1 298 ? -8.349  -10.207 38.005   1.00 139.15 ? 298  PRO A O   1 
ATOM   2289  C  CB  . PRO A  1 298 ? -5.828  -10.757 36.219   1.00 138.88 ? 298  PRO A CB  1 
ATOM   2290  C  CG  . PRO A  1 298 ? -5.043  -11.675 35.331   1.00 139.07 ? 298  PRO A CG  1 
ATOM   2291  C  CD  . PRO A  1 298 ? -5.964  -12.822 35.048   1.00 136.66 ? 298  PRO A CD  1 
ATOM   2292  N  N   . LEU A  1 299 ? -9.068  -11.597 36.389   1.00 148.63 ? 299  LEU A N   1 
ATOM   2293  C  CA  . LEU A  1 299 ? -10.420 -11.076 36.375   1.00 136.01 ? 299  LEU A CA  1 
ATOM   2294  C  C   . LEU A  1 299 ? -11.350 -11.988 37.144   1.00 135.76 ? 299  LEU A C   1 
ATOM   2295  O  O   . LEU A  1 299 ? -12.570 -11.792 37.115   1.00 173.49 ? 299  LEU A O   1 
ATOM   2296  C  CB  . LEU A  1 299 ? -10.910 -10.904 34.937   1.00 134.90 ? 299  LEU A CB  1 
ATOM   2297  C  CG  . LEU A  1 299 ? -9.987  -10.108 34.016   1.00 137.13 ? 299  LEU A CG  1 
ATOM   2298  C  CD1 . LEU A  1 299 ? -10.629 -9.918  32.650   1.00 134.47 ? 299  LEU A CD1 1 
ATOM   2299  C  CD2 . LEU A  1 299 ? -9.614  -8.770  34.638   1.00 137.09 ? 299  LEU A CD2 1 
ATOM   2300  N  N   . PHE A  1 300 ? -10.797 -12.989 37.820   1.00 135.87 ? 300  PHE A N   1 
ATOM   2301  C  CA  . PHE A  1 300 ? -11.609 -13.880 38.624   1.00 136.00 ? 300  PHE A CA  1 
ATOM   2302  C  C   . PHE A  1 300 ? -12.333 -13.094 39.698   1.00 137.57 ? 300  PHE A C   1 
ATOM   2303  O  O   . PHE A  1 300 ? -11.725 -12.309 40.430   1.00 139.07 ? 300  PHE A O   1 
ATOM   2304  C  CB  . PHE A  1 300 ? -10.749 -14.949 39.276   1.00 136.42 ? 300  PHE A CB  1 
ATOM   2305  C  CG  . PHE A  1 300 ? -11.540 -15.970 40.029   1.00 136.73 ? 300  PHE A CG  1 
ATOM   2306  C  CD1 . PHE A  1 300 ? -11.985 -17.115 39.399   1.00 135.69 ? 300  PHE A CD1 1 
ATOM   2307  C  CD2 . PHE A  1 300 ? -11.869 -15.771 41.361   1.00 138.37 ? 300  PHE A CD2 1 
ATOM   2308  C  CE1 . PHE A  1 300 ? -12.717 -18.059 40.088   1.00 136.26 ? 300  PHE A CE1 1 
ATOM   2309  C  CE2 . PHE A  1 300 ? -12.607 -16.706 42.054   1.00 138.94 ? 300  PHE A CE2 1 
ATOM   2310  C  CZ  . PHE A  1 300 ? -13.032 -17.853 41.417   1.00 137.87 ? 300  PHE A CZ  1 
ATOM   2311  N  N   . MET A  1 301 ? -13.628 -13.335 39.812   1.00 137.57 ? 301  MET A N   1 
ATOM   2312  C  CA  . MET A  1 301 ? -14.462 -12.719 40.825   1.00 139.43 ? 301  MET A CA  1 
ATOM   2313  C  C   . MET A  1 301 ? -14.809 -13.770 41.864   1.00 140.21 ? 301  MET A C   1 
ATOM   2314  O  O   . MET A  1 301 ? -15.231 -14.875 41.513   1.00 139.18 ? 301  MET A O   1 
ATOM   2315  C  CB  . MET A  1 301 ? -15.736 -12.152 40.208   1.00 139.48 ? 301  MET A CB  1 
ATOM   2316  C  CG  . MET A  1 301 ? -15.519 -11.293 38.995   1.00 138.66 ? 301  MET A CG  1 
ATOM   2317  S  SD  . MET A  1 301 ? -17.121 -10.742 38.416   1.00 139.30 ? 301  MET A SD  1 
ATOM   2318  C  CE  . MET A  1 301 ? -17.612 -9.676  39.765   1.00 142.44 ? 301  MET A CE  1 
ATOM   2319  N  N   . ASP A  1 302 ? -14.570 -13.465 43.130   1.00 142.25 ? 302  ASP A N   1 
ATOM   2320  C  CA  . ASP A  1 302 ? -15.036 -14.346 44.185   1.00 152.95 ? 302  ASP A CA  1 
ATOM   2321  C  C   . ASP A  1 302 ? -16.176 -13.675 44.941   1.00 167.10 ? 302  ASP A C   1 
ATOM   2322  O  O   . ASP A  1 302 ? -16.461 -12.486 44.773   1.00 172.70 ? 302  ASP A O   1 
ATOM   2323  C  CB  . ASP A  1 302 ? -13.899 -14.746 45.131   1.00 159.59 ? 302  ASP A CB  1 
ATOM   2324  C  CG  . ASP A  1 302 ? -13.576 -13.672 46.143   1.00 160.24 ? 302  ASP A CG  1 
ATOM   2325  O  OD1 . ASP A  1 302 ? -13.640 -12.481 45.785   1.00 172.57 ? 302  ASP A OD1 1 
ATOM   2326  O  OD2 . ASP A  1 302 ? -13.257 -14.018 47.299   1.00 151.05 ? 302  ASP A OD2 1 
ATOM   2327  N  N   . ARG A  1 303 ? -16.812 -14.455 45.805   1.00 177.75 ? 303  ARG A N   1 
ATOM   2328  C  CA  . ARG A  1 303 ? -17.919 -13.974 46.612   1.00 175.55 ? 303  ARG A CA  1 
ATOM   2329  C  C   . ARG A  1 303 ? -17.384 -13.444 47.934   1.00 184.54 ? 303  ARG A C   1 
ATOM   2330  O  O   . ARG A  1 303 ? -16.480 -14.031 48.530   1.00 189.49 ? 303  ARG A O   1 
ATOM   2331  C  CB  . ARG A  1 303 ? -18.925 -15.096 46.853   1.00 185.03 ? 303  ARG A CB  1 
ATOM   2332  C  CG  . ARG A  1 303 ? -20.179 -14.635 47.549   1.00 185.07 ? 303  ARG A CG  1 
ATOM   2333  C  CD  . ARG A  1 303 ? -20.959 -13.664 46.692   1.00 180.32 ? 303  ARG A CD  1 
ATOM   2334  N  NE  . ARG A  1 303 ? -21.715 -14.344 45.648   1.00 189.91 ? 303  ARG A NE  1 
ATOM   2335  C  CZ  . ARG A  1 303 ? -22.595 -13.743 44.853   1.00 214.46 ? 303  ARG A CZ  1 
ATOM   2336  N  NH1 . ARG A  1 303 ? -22.838 -12.447 44.993   1.00 222.76 ? 303  ARG A NH1 1 
ATOM   2337  N  NH2 . ARG A  1 303 ? -23.241 -14.436 43.926   1.00 217.28 ? 303  ARG A NH2 1 
ATOM   2338  N  N   . GLY A  1 304 ? -17.919 -12.306 48.372   1.00 188.74 ? 304  GLY A N   1 
ATOM   2339  C  CA  . GLY A  1 304 ? -17.524 -11.731 49.639   1.00 206.61 ? 304  GLY A CA  1 
ATOM   2340  C  C   . GLY A  1 304 ? -18.312 -12.288 50.814   1.00 210.28 ? 304  GLY A C   1 
ATOM   2341  O  O   . GLY A  1 304 ? -19.227 -13.098 50.671   1.00 200.04 ? 304  GLY A O   1 
ATOM   2342  N  N   . SER A  1 305 ? -17.936 -11.823 52.012   1.00 233.49 ? 305  SER A N   1 
ATOM   2343  C  CA  . SER A  1 305 ? -18.619 -12.264 53.224   1.00 242.81 ? 305  SER A CA  1 
ATOM   2344  C  C   . SER A  1 305 ? -20.039 -11.721 53.281   1.00 263.40 ? 305  SER A C   1 
ATOM   2345  O  O   . SER A  1 305 ? -20.924 -12.349 53.873   1.00 272.67 ? 305  SER A O   1 
ATOM   2346  C  CB  . SER A  1 305 ? -17.836 -11.829 54.466   1.00 241.76 ? 305  SER A CB  1 
ATOM   2347  O  OG  . SER A  1 305 ? -16.508 -12.329 54.459   1.00 242.58 ? 305  SER A OG  1 
ATOM   2348  N  N   . ASP A  1 306 ? -20.272 -10.573 52.654   1.00 273.88 ? 306  ASP A N   1 
ATOM   2349  C  CA  . ASP A  1 306 ? -21.563 -9.904  52.622   1.00 256.45 ? 306  ASP A CA  1 
ATOM   2350  C  C   . ASP A  1 306 ? -22.462 -10.413 51.508   1.00 236.93 ? 306  ASP A C   1 
ATOM   2351  O  O   . ASP A  1 306 ? -23.562 -9.880  51.329   1.00 213.65 ? 306  ASP A O   1 
ATOM   2352  C  CB  . ASP A  1 306 ? -21.361 -8.394  52.465   1.00 250.84 ? 306  ASP A CB  1 
ATOM   2353  C  CG  . ASP A  1 306 ? -20.204 -8.053  51.536   1.00 254.61 ? 306  ASP A CG  1 
ATOM   2354  O  OD1 . ASP A  1 306 ? -19.961 -8.812  50.572   1.00 245.85 ? 306  ASP A OD1 1 
ATOM   2355  O  OD2 . ASP A  1 306 ? -19.531 -7.028  51.773   1.00 261.42 ? 306  ASP A OD2 1 
ATOM   2356  N  N   . GLY A  1 307 ? -22.017 -11.411 50.749   1.00 236.94 ? 307  GLY A N   1 
ATOM   2357  C  CA  . GLY A  1 307 ? -22.787 -11.935 49.648   1.00 222.81 ? 307  GLY A CA  1 
ATOM   2358  C  C   . GLY A  1 307 ? -22.594 -11.203 48.340   1.00 226.09 ? 307  GLY A C   1 
ATOM   2359  O  O   . GLY A  1 307 ? -23.184 -11.608 47.329   1.00 230.35 ? 307  GLY A O   1 
ATOM   2360  N  N   . LYS A  1 308 ? -21.816 -10.126 48.327   1.00 238.79 ? 308  LYS A N   1 
ATOM   2361  C  CA  . LYS A  1 308 ? -21.558 -9.370  47.112   1.00 225.89 ? 308  LYS A CA  1 
ATOM   2362  C  C   . LYS A  1 308 ? -20.315 -9.895  46.395   1.00 205.20 ? 308  LYS A C   1 
ATOM   2363  O  O   . LYS A  1 308 ? -19.311 -10.248 47.025   1.00 177.49 ? 308  LYS A O   1 
ATOM   2364  C  CB  . LYS A  1 308 ? -21.405 -7.880  47.440   1.00 221.87 ? 308  LYS A CB  1 
ATOM   2365  C  CG  . LYS A  1 308 ? -21.508 -6.937  46.245   1.00 213.75 ? 308  LYS A CG  1 
ATOM   2366  C  CD  . LYS A  1 308 ? -21.208 -5.493  46.641   1.00 186.42 ? 308  LYS A CD  1 
ATOM   2367  C  CE  . LYS A  1 308 ? -22.211 -4.969  47.664   1.00 215.99 ? 308  LYS A CE  1 
ATOM   2368  N  NZ  . LYS A  1 308 ? -23.616 -4.980  47.160   1.00 220.20 ? 308  LYS A NZ  1 
ATOM   2369  N  N   . LEU A  1 309 ? -20.401 -9.955  45.067   1.00 195.64 ? 309  LEU A N   1 
ATOM   2370  C  CA  . LEU A  1 309 ? -19.263 -10.347 44.248   1.00 183.15 ? 309  LEU A CA  1 
ATOM   2371  C  C   . LEU A  1 309 ? -18.160 -9.306  44.357   1.00 178.11 ? 309  LEU A C   1 
ATOM   2372  O  O   . LEU A  1 309 ? -18.415 -8.112  44.535   1.00 189.27 ? 309  LEU A O   1 
ATOM   2373  C  CB  . LEU A  1 309 ? -19.689 -10.498 42.790   1.00 187.90 ? 309  LEU A CB  1 
ATOM   2374  C  CG  . LEU A  1 309 ? -20.637 -11.654 42.496   1.00 198.44 ? 309  LEU A CG  1 
ATOM   2375  C  CD1 . LEU A  1 309 ? -21.153 -11.548 41.076   1.00 197.11 ? 309  LEU A CD1 1 
ATOM   2376  C  CD2 . LEU A  1 309 ? -19.909 -12.970 42.714   1.00 158.53 ? 309  LEU A CD2 1 
ATOM   2377  N  N   . GLN A  1 310 ? -16.919 -9.764  44.254   1.00 151.61 ? 310  GLN A N   1 
ATOM   2378  C  CA  . GLN A  1 310 ? -15.790 -8.846  44.208   1.00 152.06 ? 310  GLN A CA  1 
ATOM   2379  C  C   . GLN A  1 310 ? -14.711 -9.414  43.299   1.00 158.70 ? 310  GLN A C   1 
ATOM   2380  O  O   . GLN A  1 310 ? -14.339 -10.585 43.424   1.00 148.05 ? 310  GLN A O   1 
ATOM   2381  C  CB  . GLN A  1 310 ? -15.243 -8.580  45.616   1.00 159.35 ? 310  GLN A CB  1 
ATOM   2382  C  CG  . GLN A  1 310 ? -15.055 -9.834  46.457   1.00 164.39 ? 310  GLN A CG  1 
ATOM   2383  C  CD  . GLN A  1 310 ? -14.327 -9.561  47.756   1.00 168.41 ? 310  GLN A CD  1 
ATOM   2384  O  OE1 . GLN A  1 310 ? -14.338 -8.440  48.252   1.00 192.74 ? 310  GLN A OE1 1 
ATOM   2385  N  NE2 . GLN A  1 310 ? -13.702 -10.591 48.322   1.00 157.20 ? 310  GLN A NE2 1 
ATOM   2386  N  N   . GLU A  1 311 ? -14.240 -8.588  42.366   1.00 145.87 ? 311  GLU A N   1 
ATOM   2387  C  CA  . GLU A  1 311 ? -13.156 -8.962  41.458   1.00 143.79 ? 311  GLU A CA  1 
ATOM   2388  C  C   . GLU A  1 311 ? -11.829 -8.899  42.200   1.00 144.89 ? 311  GLU A C   1 
ATOM   2389  O  O   . GLU A  1 311 ? -11.348 -7.814  42.533   1.00 146.81 ? 311  GLU A O   1 
ATOM   2390  C  CB  . GLU A  1 311 ? -13.113 -8.035  40.250   1.00 143.27 ? 311  GLU A CB  1 
ATOM   2391  C  CG  . GLU A  1 311 ? -11.979 -8.353  39.287   1.00 144.78 ? 311  GLU A CG  1 
ATOM   2392  C  CD  . GLU A  1 311 ? -11.829 -7.304  38.204   1.00 142.38 ? 311  GLU A CD  1 
ATOM   2393  O  OE1 . GLU A  1 311 ? -12.730 -6.451  38.076   1.00 179.57 ? 311  GLU A OE1 1 
ATOM   2394  O  OE2 . GLU A  1 311 ? -10.804 -7.322  37.491   1.00 140.94 ? 311  GLU A OE2 1 
ATOM   2395  N  N   . VAL A  1 312 ? -11.217 -10.056 42.434   1.00 143.97 ? 312  VAL A N   1 
ATOM   2396  C  CA  . VAL A  1 312 ? -9.937  -10.098 43.134   1.00 151.37 ? 312  VAL A CA  1 
ATOM   2397  C  C   . VAL A  1 312 ? -8.856  -10.827 42.358   1.00 143.75 ? 312  VAL A C   1 
ATOM   2398  O  O   . VAL A  1 312 ? -7.662  -10.683 42.686   1.00 144.99 ? 312  VAL A O   1 
ATOM   2399  C  CB  . VAL A  1 312 ? -10.108 -10.727 44.533   1.00 156.18 ? 312  VAL A CB  1 
ATOM   2400  C  CG1 . VAL A  1 312 ? -10.999 -9.860  45.399   1.00 149.19 ? 312  VAL A CG1 1 
ATOM   2401  C  CG2 . VAL A  1 312 ? -10.689 -12.122 44.410   1.00 152.49 ? 312  VAL A CG2 1 
ATOM   2402  N  N   . GLY A  1 313 ? -9.198  -11.608 41.339   1.00 141.49 ? 313  GLY A N   1 
ATOM   2403  C  CA  . GLY A  1 313 ? -8.214  -12.364 40.599   1.00 154.51 ? 313  GLY A CA  1 
ATOM   2404  C  C   . GLY A  1 313 ? -7.875  -13.662 41.301   1.00 143.39 ? 313  GLY A C   1 
ATOM   2405  O  O   . GLY A  1 313 ? -7.951  -13.746 42.531   1.00 142.36 ? 313  GLY A O   1 
ATOM   2406  N  N   . GLN A  1 314 ? -7.485  -14.681 40.539   1.00 139.63 ? 314  GLN A N   1 
ATOM   2407  C  CA  . GLN A  1 314 ? -7.172  -15.984 41.106   1.00 140.17 ? 314  GLN A CA  1 
ATOM   2408  C  C   . GLN A  1 314 ? -6.028  -16.626 40.339   1.00 160.17 ? 314  GLN A C   1 
ATOM   2409  O  O   . GLN A  1 314 ? -5.957  -16.535 39.110   1.00 172.34 ? 314  GLN A O   1 
ATOM   2410  C  CB  . GLN A  1 314 ? -8.380  -16.932 41.082   1.00 139.14 ? 314  GLN A CB  1 
ATOM   2411  C  CG  . GLN A  1 314 ? -8.148  -18.248 41.827   1.00 140.17 ? 314  GLN A CG  1 
ATOM   2412  C  CD  . GLN A  1 314 ? -9.308  -19.222 41.712   1.00 139.39 ? 314  GLN A CD  1 
ATOM   2413  O  OE1 . GLN A  1 314 ? -9.517  -19.835 40.663   1.00 138.14 ? 314  GLN A OE1 1 
ATOM   2414  N  NE2 . GLN A  1 314 ? -10.058 -19.385 42.798   1.00 183.29 ? 314  GLN A NE2 1 
ATOM   2415  N  N   . VAL A  1 315 ? -5.142  -17.282 41.077   1.00 141.86 ? 315  VAL A N   1 
ATOM   2416  C  CA  . VAL A  1 315 ? -4.092  -18.107 40.504   1.00 142.45 ? 315  VAL A CA  1 
ATOM   2417  C  C   . VAL A  1 315 ? -4.303  -19.534 40.983   1.00 143.02 ? 315  VAL A C   1 
ATOM   2418  O  O   . VAL A  1 315 ? -4.465  -19.775 42.185   1.00 144.32 ? 315  VAL A O   1 
ATOM   2419  C  CB  . VAL A  1 315 ? -2.698  -17.587 40.890   1.00 177.09 ? 315  VAL A CB  1 
ATOM   2420  C  CG1 . VAL A  1 315 ? -1.622  -18.538 40.395   1.00 168.85 ? 315  VAL A CG1 1 
ATOM   2421  C  CG2 . VAL A  1 315 ? -2.496  -16.191 40.326   1.00 169.21 ? 315  VAL A CG2 1 
ATOM   2422  N  N   . SER A  1 316 ? -4.324  -20.471 40.045   1.00 143.62 ? 316  SER A N   1 
ATOM   2423  C  CA  . SER A  1 316 ? -4.419  -21.887 40.362   1.00 144.55 ? 316  SER A CA  1 
ATOM   2424  C  C   . SER A  1 316 ? -3.028  -22.510 40.365   1.00 158.26 ? 316  SER A C   1 
ATOM   2425  O  O   . SER A  1 316 ? -2.224  -22.265 39.459   1.00 147.01 ? 316  SER A O   1 
ATOM   2426  C  CB  . SER A  1 316 ? -5.338  -22.601 39.372   1.00 142.95 ? 316  SER A CB  1 
ATOM   2427  O  OG  . SER A  1 316 ? -4.819  -22.535 38.059   1.00 182.83 ? 316  SER A OG  1 
ATOM   2428  N  N   . VAL A  1 317 ? -2.749  -23.309 41.390   1.00 150.05 ? 317  VAL A N   1 
ATOM   2429  C  CA  . VAL A  1 317 ? -1.467  -23.977 41.562   1.00 150.39 ? 317  VAL A CA  1 
ATOM   2430  C  C   . VAL A  1 317 ? -1.675  -25.465 41.316   1.00 151.26 ? 317  VAL A C   1 
ATOM   2431  O  O   . VAL A  1 317 ? -2.374  -26.135 42.085   1.00 151.68 ? 317  VAL A O   1 
ATOM   2432  C  CB  . VAL A  1 317 ? -0.894  -23.722 42.964   1.00 158.67 ? 317  VAL A CB  1 
ATOM   2433  C  CG1 . VAL A  1 317 ? 0.496   -24.312 43.089   1.00 163.75 ? 317  VAL A CG1 1 
ATOM   2434  C  CG2 . VAL A  1 317 ? -0.890  -22.231 43.261   1.00 151.99 ? 317  VAL A CG2 1 
ATOM   2435  N  N   . SER A  1 318 ? -1.050  -25.986 40.260   1.00 169.69 ? 318  SER A N   1 
ATOM   2436  C  CA  . SER A  1 318 ? -1.202  -27.381 39.847   1.00 186.31 ? 318  SER A CA  1 
ATOM   2437  C  C   . SER A  1 318 ? 0.133   -28.106 39.994   1.00 187.50 ? 318  SER A C   1 
ATOM   2438  O  O   . SER A  1 318 ? 1.080   -27.838 39.245   1.00 167.61 ? 318  SER A O   1 
ATOM   2439  C  CB  . SER A  1 318 ? -1.717  -27.466 38.413   1.00 161.15 ? 318  SER A CB  1 
ATOM   2440  O  OG  . SER A  1 318 ? -2.949  -26.783 38.290   1.00 158.12 ? 318  SER A OG  1 
ATOM   2441  N  N   . LEU A  1 319 ? 0.205   -29.024 40.957   1.00 181.57 ? 319  LEU A N   1 
ATOM   2442  C  CA  . LEU A  1 319 ? 1.420   -29.786 41.227   1.00 190.40 ? 319  LEU A CA  1 
ATOM   2443  C  C   . LEU A  1 319 ? 1.481   -31.020 40.326   1.00 196.06 ? 319  LEU A C   1 
ATOM   2444  O  O   . LEU A  1 319 ? 0.592   -31.879 40.378   1.00 178.87 ? 319  LEU A O   1 
ATOM   2445  C  CB  . LEU A  1 319 ? 1.485   -30.186 42.702   1.00 192.57 ? 319  LEU A CB  1 
ATOM   2446  C  CG  . LEU A  1 319 ? 2.134   -29.208 43.694   1.00 187.45 ? 319  LEU A CG  1 
ATOM   2447  C  CD1 . LEU A  1 319 ? 1.514   -27.817 43.634   1.00 183.80 ? 319  LEU A CD1 1 
ATOM   2448  C  CD2 . LEU A  1 319 ? 2.062   -29.756 45.108   1.00 194.40 ? 319  LEU A CD2 1 
ATOM   2449  N  N   . GLN A  1 320 ? 2.526   -31.099 39.499   1.00 197.47 ? 320  GLN A N   1 
ATOM   2450  C  CA  . GLN A  1 320 ? 2.726   -32.236 38.604   1.00 171.58 ? 320  GLN A CA  1 
ATOM   2451  C  C   . GLN A  1 320 ? 3.152   -33.482 39.375   1.00 175.75 ? 320  GLN A C   1 
ATOM   2452  O  O   . GLN A  1 320 ? 3.958   -33.411 40.309   1.00 178.24 ? 320  GLN A O   1 
ATOM   2453  C  CB  . GLN A  1 320 ? 3.781   -31.898 37.551   1.00 172.95 ? 320  GLN A CB  1 
ATOM   2454  C  CG  . GLN A  1 320 ? 4.038   -33.005 36.542   1.00 175.61 ? 320  GLN A CG  1 
ATOM   2455  C  CD  . GLN A  1 320 ? 5.203   -32.699 35.625   1.00 178.70 ? 320  GLN A CD  1 
ATOM   2456  O  OE1 . GLN A  1 320 ? 5.643   -33.554 34.855   1.00 191.59 ? 320  GLN A OE1 1 
ATOM   2457  N  NE2 . GLN A  1 320 ? 5.714   -31.478 35.707   1.00 176.61 ? 320  GLN A NE2 1 
ATOM   2458  N  N   . ARG A  1 321 ? 2.605   -34.631 38.977   1.00 197.83 ? 321  ARG A N   1 
ATOM   2459  C  CA  . ARG A  1 321 ? 2.979   -35.922 39.534   1.00 211.67 ? 321  ARG A CA  1 
ATOM   2460  C  C   . ARG A  1 321 ? 3.434   -36.883 38.440   1.00 192.75 ? 321  ARG A C   1 
ATOM   2461  O  O   . ARG A  1 321 ? 3.023   -36.777 37.279   1.00 190.95 ? 321  ARG A O   1 
ATOM   2462  C  CB  . ARG A  1 321 ? 1.820   -36.538 40.333   1.00 218.51 ? 321  ARG A CB  1 
ATOM   2463  C  CG  . ARG A  1 321 ? 1.235   -35.597 41.379   1.00 212.52 ? 321  ARG A CG  1 
ATOM   2464  C  CD  . ARG A  1 321 ? 2.207   -35.458 42.543   1.00 214.48 ? 321  ARG A CD  1 
ATOM   2465  N  NE  . ARG A  1 321 ? 1.700   -34.626 43.632   1.00 210.42 ? 321  ARG A NE  1 
ATOM   2466  C  CZ  . ARG A  1 321 ? 2.361   -34.399 44.766   1.00 198.20 ? 321  ARG A CZ  1 
ATOM   2467  N  NH1 . ARG A  1 321 ? 3.557   -34.939 44.965   1.00 194.57 ? 321  ARG A NH1 1 
ATOM   2468  N  NH2 . ARG A  1 321 ? 1.832   -33.625 45.703   1.00 187.76 ? 321  ARG A NH2 1 
ATOM   2469  N  N   . ALA A  1 322 ? 4.289   -37.833 38.836   1.00 192.74 ? 322  ALA A N   1 
ATOM   2470  C  CA  . ALA A  1 322 ? 4.806   -38.821 37.896   1.00 211.35 ? 322  ALA A CA  1 
ATOM   2471  C  C   . ALA A  1 322 ? 3.691   -39.697 37.346   1.00 212.22 ? 322  ALA A C   1 
ATOM   2472  O  O   . ALA A  1 322 ? 3.799   -40.209 36.227   1.00 212.11 ? 322  ALA A O   1 
ATOM   2473  C  CB  . ALA A  1 322 ? 5.875   -39.685 38.569   1.00 200.86 ? 322  ALA A CB  1 
ATOM   2474  N  N   . SER A  1 323 ? 2.607   -39.865 38.104   1.00 193.54 ? 323  SER A N   1 
ATOM   2475  C  CA  . SER A  1 323 ? 1.496   -40.680 37.638   1.00 193.14 ? 323  SER A CA  1 
ATOM   2476  C  C   . SER A  1 323 ? 0.696   -39.991 36.555   1.00 188.82 ? 323  SER A C   1 
ATOM   2477  O  O   . SER A  1 323 ? -0.284  -40.568 36.073   1.00 196.76 ? 323  SER A O   1 
ATOM   2478  C  CB  . SER A  1 323 ? 0.579   -41.044 38.806   1.00 192.56 ? 323  SER A CB  1 
ATOM   2479  O  OG  . SER A  1 323 ? 1.284   -41.777 39.787   1.00 197.02 ? 323  SER A OG  1 
ATOM   2480  N  N   . GLY A  1 324 ? 1.082   -38.778 36.171   1.00 198.11 ? 324  GLY A N   1 
ATOM   2481  C  CA  . GLY A  1 324 ? 0.439   -38.051 35.108   1.00 218.92 ? 324  GLY A CA  1 
ATOM   2482  C  C   . GLY A  1 324 ? -0.599  -37.050 35.568   1.00 229.23 ? 324  GLY A C   1 
ATOM   2483  O  O   . GLY A  1 324 ? -0.912  -36.114 34.820   1.00 216.16 ? 324  GLY A O   1 
ATOM   2484  N  N   . ASP A  1 325 ? -1.140  -37.219 36.774   1.00 235.69 ? 325  ASP A N   1 
ATOM   2485  C  CA  . ASP A  1 325 ? -2.193  -36.347 37.275   1.00 220.48 ? 325  ASP A CA  1 
ATOM   2486  C  C   . ASP A  1 325 ? -1.628  -34.986 37.687   1.00 219.78 ? 325  ASP A C   1 
ATOM   2487  O  O   . ASP A  1 325 ? -0.434  -34.703 37.556   1.00 230.61 ? 325  ASP A O   1 
ATOM   2488  C  CB  . ASP A  1 325 ? -2.911  -37.004 38.452   1.00 216.02 ? 325  ASP A CB  1 
ATOM   2489  C  CG  . ASP A  1 325 ? -3.303  -38.440 38.168   1.00 215.90 ? 325  ASP A CG  1 
ATOM   2490  O  OD1 . ASP A  1 325 ? -4.371  -38.649 37.549   1.00 222.53 ? 325  ASP A OD1 1 
ATOM   2491  O  OD2 . ASP A  1 325 ? -2.552  -39.358 38.567   1.00 194.98 ? 325  ASP A OD2 1 
ATOM   2492  N  N   . PHE A  1 326 ? -2.515  -34.135 38.202   1.00 201.65 ? 326  PHE A N   1 
ATOM   2493  C  CA  . PHE A  1 326 ? -2.155  -32.821 38.722   1.00 193.05 ? 326  PHE A CA  1 
ATOM   2494  C  C   . PHE A  1 326 ? -2.922  -32.571 40.011   1.00 198.90 ? 326  PHE A C   1 
ATOM   2495  O  O   . PHE A  1 326 ? -4.129  -32.826 40.074   1.00 210.05 ? 326  PHE A O   1 
ATOM   2496  C  CB  . PHE A  1 326 ? -2.455  -31.710 37.705   1.00 176.44 ? 326  PHE A CB  1 
ATOM   2497  C  CG  . PHE A  1 326 ? -1.473  -31.639 36.561   1.00 178.11 ? 326  PHE A CG  1 
ATOM   2498  C  CD1 . PHE A  1 326 ? -1.638  -32.422 35.428   1.00 180.23 ? 326  PHE A CD1 1 
ATOM   2499  C  CD2 . PHE A  1 326 ? -0.389  -30.774 36.618   1.00 170.42 ? 326  PHE A CD2 1 
ATOM   2500  C  CE1 . PHE A  1 326 ? -0.736  -32.347 34.379   1.00 178.26 ? 326  PHE A CE1 1 
ATOM   2501  C  CE2 . PHE A  1 326 ? 0.514   -30.696 35.573   1.00 171.76 ? 326  PHE A CE2 1 
ATOM   2502  C  CZ  . PHE A  1 326 ? 0.341   -31.483 34.453   1.00 172.67 ? 326  PHE A CZ  1 
ATOM   2503  N  N   . GLN A  1 327 ? -2.232  -32.067 41.030   1.00 190.41 ? 327  GLN A N   1 
ATOM   2504  C  CA  . GLN A  1 327 ? -2.869  -31.633 42.273   1.00 176.75 ? 327  GLN A CA  1 
ATOM   2505  C  C   . GLN A  1 327 ? -3.073  -30.125 42.202   1.00 171.95 ? 327  GLN A C   1 
ATOM   2506  O  O   . GLN A  1 327 ? -2.126  -29.352 42.360   1.00 171.44 ? 327  GLN A O   1 
ATOM   2507  C  CB  . GLN A  1 327 ? -2.030  -32.028 43.480   1.00 181.45 ? 327  GLN A CB  1 
ATOM   2508  C  CG  . GLN A  1 327 ? -1.672  -33.502 43.529   1.00 194.16 ? 327  GLN A CG  1 
ATOM   2509  C  CD  . GLN A  1 327 ? -1.129  -33.912 44.882   1.00 210.46 ? 327  GLN A CD  1 
ATOM   2510  O  OE1 . GLN A  1 327 ? -0.492  -33.116 45.571   1.00 217.07 ? 327  GLN A OE1 1 
ATOM   2511  N  NE2 . GLN A  1 327 ? -1.381  -35.157 45.274   1.00 213.56 ? 327  GLN A NE2 1 
ATOM   2512  N  N   . THR A  1 328 ? -4.315  -29.705 41.982   1.00 170.68 ? 328  THR A N   1 
ATOM   2513  C  CA  . THR A  1 328 ? -4.639  -28.307 41.738   1.00 178.69 ? 328  THR A CA  1 
ATOM   2514  C  C   . THR A  1 328 ? -5.299  -27.683 42.961   1.00 176.06 ? 328  THR A C   1 
ATOM   2515  O  O   . THR A  1 328 ? -6.249  -28.242 43.520   1.00 169.88 ? 328  THR A O   1 
ATOM   2516  C  CB  . THR A  1 328 ? -5.549  -28.163 40.516   1.00 180.95 ? 328  THR A CB  1 
ATOM   2517  O  OG1 . THR A  1 328 ? -4.906  -28.745 39.373   1.00 155.07 ? 328  THR A OG1 1 
ATOM   2518  C  CG2 . THR A  1 328 ? -5.868  -26.693 40.246   1.00 175.51 ? 328  THR A CG2 1 
ATOM   2519  N  N   . THR A  1 329 ? -4.790  -26.524 43.367   1.00 159.05 ? 329  THR A N   1 
ATOM   2520  C  CA  . THR A  1 329 ? -5.406  -25.665 44.365   1.00 149.85 ? 329  THR A CA  1 
ATOM   2521  C  C   . THR A  1 329 ? -5.621  -24.291 43.745   1.00 147.53 ? 329  THR A C   1 
ATOM   2522  O  O   . THR A  1 329 ? -5.241  -24.037 42.601   1.00 149.40 ? 329  THR A O   1 
ATOM   2523  C  CB  . THR A  1 329 ? -4.548  -25.569 45.637   1.00 154.84 ? 329  THR A CB  1 
ATOM   2524  O  OG1 . THR A  1 329 ? -3.216  -25.155 45.302   1.00 153.52 ? 329  THR A OG1 1 
ATOM   2525  C  CG2 . THR A  1 329 ? -4.495  -26.915 46.348   1.00 169.79 ? 329  THR A CG2 1 
ATOM   2526  N  N   . LYS A  1 330 ? -6.272  -23.407 44.485   1.00 147.21 ? 330  LYS A N   1 
ATOM   2527  C  CA  . LYS A  1 330 ? -6.573  -22.086 43.962   1.00 145.38 ? 330  LYS A CA  1 
ATOM   2528  C  C   . LYS A  1 330 ? -6.221  -21.023 44.989   1.00 146.76 ? 330  LYS A C   1 
ATOM   2529  O  O   . LYS A  1 330 ? -6.529  -21.166 46.176   1.00 148.43 ? 330  LYS A O   1 
ATOM   2530  C  CB  . LYS A  1 330 ? -8.039  -21.987 43.559   1.00 143.53 ? 330  LYS A CB  1 
ATOM   2531  C  CG  . LYS A  1 330 ? -8.322  -22.637 42.218   1.00 153.67 ? 330  LYS A CG  1 
ATOM   2532  C  CD  . LYS A  1 330 ? -9.806  -22.749 41.941   1.00 163.27 ? 330  LYS A CD  1 
ATOM   2533  C  CE  . LYS A  1 330 ? -10.055 -23.275 40.536   1.00 171.72 ? 330  LYS A CE  1 
ATOM   2534  N  NZ  . LYS A  1 330 ? -9.279  -24.523 40.270   1.00 177.13 ? 330  LYS A NZ  1 
ATOM   2535  N  N   . LEU A  1 331 ? -5.581  -19.955 44.519   1.00 146.35 ? 331  LEU A N   1 
ATOM   2536  C  CA  . LEU A  1 331 ? -5.117  -18.860 45.366   1.00 147.95 ? 331  LEU A CA  1 
ATOM   2537  C  C   . LEU A  1 331 ? -5.817  -17.581 44.927   1.00 146.51 ? 331  LEU A C   1 
ATOM   2538  O  O   . LEU A  1 331 ? -5.590  -17.095 43.814   1.00 148.38 ? 331  LEU A O   1 
ATOM   2539  C  CB  . LEU A  1 331 ? -3.597  -18.711 45.282   1.00 149.54 ? 331  LEU A CB  1 
ATOM   2540  C  CG  . LEU A  1 331 ? -2.942  -17.750 46.278   1.00 151.95 ? 331  LEU A CG  1 
ATOM   2541  C  CD1 . LEU A  1 331 ? -3.223  -18.195 47.703   1.00 162.38 ? 331  LEU A CD1 1 
ATOM   2542  C  CD2 . LEU A  1 331 ? -1.443  -17.642 46.038   1.00 153.65 ? 331  LEU A CD2 1 
ATOM   2543  N  N   . ASN A  1 332 ? -6.651  -17.032 45.803   1.00 147.28 ? 332  ASN A N   1 
ATOM   2544  C  CA  . ASN A  1 332 ? -7.409  -15.825 45.511   1.00 146.50 ? 332  ASN A CA  1 
ATOM   2545  C  C   . ASN A  1 332 ? -6.617  -14.581 45.894   1.00 148.23 ? 332  ASN A C   1 
ATOM   2546  O  O   . ASN A  1 332 ? -5.811  -14.598 46.828   1.00 150.56 ? 332  ASN A O   1 
ATOM   2547  C  CB  . ASN A  1 332 ? -8.745  -15.838 46.256   1.00 146.99 ? 332  ASN A CB  1 
ATOM   2548  C  CG  . ASN A  1 332 ? -9.744  -16.797 45.643   1.00 159.93 ? 332  ASN A CG  1 
ATOM   2549  O  OD1 . ASN A  1 332 ? -9.386  -17.629 44.809   1.00 165.28 ? 332  ASN A OD1 1 
ATOM   2550  N  ND2 . ASN A  1 332 ? -11.005 -16.688 46.053   1.00 154.00 ? 332  ASN A ND2 1 
ATOM   2551  N  N   . GLY A  1 333 ? -6.847  -13.500 45.153   1.00 147.34 ? 333  GLY A N   1 
ATOM   2552  C  CA  . GLY A  1 333 ? -6.209  -12.233 45.449   1.00 149.18 ? 333  GLY A CA  1 
ATOM   2553  C  C   . GLY A  1 333 ? -6.736  -11.588 46.719   1.00 151.63 ? 333  GLY A C   1 
ATOM   2554  O  O   . GLY A  1 333 ? -7.705  -12.032 47.335   1.00 151.84 ? 333  GLY A O   1 
ATOM   2555  N  N   . PHE A  1 334 ? -6.070  -10.502 47.121   1.00 153.89 ? 334  PHE A N   1 
ATOM   2556  C  CA  . PHE A  1 334 ? -6.375  -9.819  48.373   1.00 168.81 ? 334  PHE A CA  1 
ATOM   2557  C  C   . PHE A  1 334 ? -7.091  -8.494  48.194   1.00 183.18 ? 334  PHE A C   1 
ATOM   2558  O  O   . PHE A  1 334 ? -7.851  -8.096  49.079   1.00 197.11 ? 334  PHE A O   1 
ATOM   2559  C  CB  . PHE A  1 334 ? -5.094  -9.561  49.181   1.00 175.06 ? 334  PHE A CB  1 
ATOM   2560  C  CG  . PHE A  1 334 ? -4.235  -10.776 49.372   1.00 176.63 ? 334  PHE A CG  1 
ATOM   2561  C  CD1 . PHE A  1 334 ? -4.416  -11.605 50.468   1.00 166.23 ? 334  PHE A CD1 1 
ATOM   2562  C  CD2 . PHE A  1 334 ? -3.242  -11.088 48.460   1.00 176.65 ? 334  PHE A CD2 1 
ATOM   2563  C  CE1 . PHE A  1 334 ? -3.622  -12.726 50.648   1.00 163.82 ? 334  PHE A CE1 1 
ATOM   2564  C  CE2 . PHE A  1 334 ? -2.446  -12.208 48.633   1.00 173.53 ? 334  PHE A CE2 1 
ATOM   2565  C  CZ  . PHE A  1 334 ? -2.637  -13.027 49.729   1.00 168.41 ? 334  PHE A CZ  1 
ATOM   2566  N  N   . GLU A  1 335 ? -6.868  -7.795  47.087   1.00 179.69 ? 335  GLU A N   1 
ATOM   2567  C  CA  . GLU A  1 335 ? -7.441  -6.476  46.875   1.00 174.11 ? 335  GLU A CA  1 
ATOM   2568  C  C   . GLU A  1 335 ? -8.401  -6.486  45.691   1.00 168.69 ? 335  GLU A C   1 
ATOM   2569  O  O   . GLU A  1 335 ? -8.123  -7.102  44.655   1.00 159.27 ? 335  GLU A O   1 
ATOM   2570  C  CB  . GLU A  1 335 ? -6.331  -5.437  46.669   1.00 171.89 ? 335  GLU A CB  1 
ATOM   2571  C  CG  . GLU A  1 335 ? -5.675  -4.984  47.974   1.00 167.47 ? 335  GLU A CG  1 
ATOM   2572  C  CD  . GLU A  1 335 ? -4.891  -3.695  47.822   1.00 182.80 ? 335  GLU A CD  1 
ATOM   2573  O  OE1 . GLU A  1 335 ? -3.863  -3.537  48.515   1.00 192.10 ? 335  GLU A OE1 1 
ATOM   2574  O  OE2 . GLU A  1 335 ? -5.301  -2.839  47.008   1.00 190.47 ? 335  GLU A OE2 1 
ATOM   2575  N  N   . VAL A  1 336 ? -9.527  -5.785  45.857   1.00 170.04 ? 336  VAL A N   1 
ATOM   2576  C  CA  . VAL A  1 336 ? -10.539 -5.668  44.808   1.00 165.55 ? 336  VAL A CA  1 
ATOM   2577  C  C   . VAL A  1 336 ? -9.995  -4.851  43.642   1.00 154.12 ? 336  VAL A C   1 
ATOM   2578  O  O   . VAL A  1 336 ? -9.368  -3.801  43.838   1.00 168.87 ? 336  VAL A O   1 
ATOM   2579  C  CB  . VAL A  1 336 ? -11.820 -5.040  45.378   1.00 156.11 ? 336  VAL A CB  1 
ATOM   2580  C  CG1 . VAL A  1 336 ? -12.990 -5.264  44.440   1.00 154.14 ? 336  VAL A CG1 1 
ATOM   2581  C  CG2 . VAL A  1 336 ? -12.123 -5.618  46.755   1.00 157.90 ? 336  VAL A CG2 1 
ATOM   2582  N  N   . PHE A  1 337 ? -10.231 -5.335  42.422   1.00 150.45 ? 337  PHE A N   1 
ATOM   2583  C  CA  . PHE A  1 337 ? -9.831  -4.686  41.174   1.00 149.69 ? 337  PHE A CA  1 
ATOM   2584  C  C   . PHE A  1 337 ? -8.319  -4.582  41.016   1.00 180.89 ? 337  PHE A C   1 
ATOM   2585  O  O   . PHE A  1 337 ? -7.840  -3.903  40.097   1.00 173.03 ? 337  PHE A O   1 
ATOM   2586  C  CB  . PHE A  1 337 ? -10.466 -3.299  41.030   1.00 151.85 ? 337  PHE A CB  1 
ATOM   2587  C  CG  . PHE A  1 337 ? -11.960 -3.333  40.956   1.00 151.67 ? 337  PHE A CG  1 
ATOM   2588  C  CD1 . PHE A  1 337 ? -12.617 -4.466  40.507   1.00 149.03 ? 337  PHE A CD1 1 
ATOM   2589  C  CD2 . PHE A  1 337 ? -12.710 -2.241  41.350   1.00 166.46 ? 337  PHE A CD2 1 
ATOM   2590  C  CE1 . PHE A  1 337 ? -13.999 -4.504  40.443   1.00 158.13 ? 337  PHE A CE1 1 
ATOM   2591  C  CE2 . PHE A  1 337 ? -14.089 -2.273  41.289   1.00 165.13 ? 337  PHE A CE2 1 
ATOM   2592  C  CZ  . PHE A  1 337 ? -14.735 -3.407  40.835   1.00 160.74 ? 337  PHE A CZ  1 
ATOM   2593  N  N   . ALA A  1 338 ? -7.552  -5.240  41.890   1.00 168.21 ? 338  ALA A N   1 
ATOM   2594  C  CA  . ALA A  1 338 ? -6.101  -5.213  41.803   1.00 151.44 ? 338  ALA A CA  1 
ATOM   2595  C  C   . ALA A  1 338 ? -5.584  -6.089  40.683   1.00 148.93 ? 338  ALA A C   1 
ATOM   2596  O  O   . ALA A  1 338 ? -4.431  -5.927  40.270   1.00 181.23 ? 338  ALA A O   1 
ATOM   2597  C  CB  . ALA A  1 338 ? -5.491  -5.670  43.129   1.00 153.24 ? 338  ALA A CB  1 
ATOM   2598  N  N   . ARG A  1 339 ? -6.415  -7.000  40.184   1.00 146.41 ? 339  ARG A N   1 
ATOM   2599  C  CA  . ARG A  1 339 ? -6.024  -7.934  39.138   1.00 144.27 ? 339  ARG A CA  1 
ATOM   2600  C  C   . ARG A  1 339 ? -4.825  -8.764  39.592   1.00 159.60 ? 339  ARG A C   1 
ATOM   2601  O  O   . ARG A  1 339 ? -3.807  -8.873  38.901   1.00 159.17 ? 339  ARG A O   1 
ATOM   2602  C  CB  . ARG A  1 339 ? -5.746  -7.208  37.820   1.00 143.92 ? 339  ARG A CB  1 
ATOM   2603  C  CG  . ARG A  1 339 ? -6.970  -6.523  37.252   1.00 143.32 ? 339  ARG A CG  1 
ATOM   2604  C  CD  . ARG A  1 339 ? -6.739  -6.035  35.837   1.00 142.84 ? 339  ARG A CD  1 
ATOM   2605  N  NE  . ARG A  1 339 ? -7.868  -5.253  35.337   1.00 142.84 ? 339  ARG A NE  1 
ATOM   2606  C  CZ  . ARG A  1 339 ? -7.949  -4.759  34.105   1.00 142.60 ? 339  ARG A CZ  1 
ATOM   2607  N  NH1 . ARG A  1 339 ? -6.970  -4.968  33.237   1.00 142.31 ? 339  ARG A NH1 1 
ATOM   2608  N  NH2 . ARG A  1 339 ? -9.010  -4.060  33.736   1.00 142.96 ? 339  ARG A NH2 1 
ATOM   2609  N  N   . PHE A  1 340 ? -4.950  -9.327  40.794   1.00 169.88 ? 340  PHE A N   1 
ATOM   2610  C  CA  . PHE A  1 340 ? -3.997  -10.311 41.291   1.00 146.39 ? 340  PHE A CA  1 
ATOM   2611  C  C   . PHE A  1 340 ? -3.851  -11.448 40.289   1.00 144.40 ? 340  PHE A C   1 
ATOM   2612  O  O   . PHE A  1 340 ? -4.840  -12.053 39.872   1.00 158.99 ? 340  PHE A O   1 
ATOM   2613  C  CB  . PHE A  1 340 ? -4.488  -10.833 42.645   1.00 147.32 ? 340  PHE A CB  1 
ATOM   2614  C  CG  . PHE A  1 340 ? -3.628  -11.903 43.247   1.00 156.26 ? 340  PHE A CG  1 
ATOM   2615  C  CD1 . PHE A  1 340 ? -2.566  -11.574 44.068   1.00 156.48 ? 340  PHE A CD1 1 
ATOM   2616  C  CD2 . PHE A  1 340 ? -3.907  -13.241 43.022   1.00 152.92 ? 340  PHE A CD2 1 
ATOM   2617  C  CE1 . PHE A  1 340 ? -1.780  -12.559 44.631   1.00 152.34 ? 340  PHE A CE1 1 
ATOM   2618  C  CE2 . PHE A  1 340 ? -3.129  -14.228 43.582   1.00 148.13 ? 340  PHE A CE2 1 
ATOM   2619  C  CZ  . PHE A  1 340 ? -2.062  -13.887 44.388   1.00 150.88 ? 340  PHE A CZ  1 
ATOM   2620  N  N   . GLY A  1 341 ? -2.616  -11.757 39.921   1.00 145.26 ? 341  GLY A N   1 
ATOM   2621  C  CA  . GLY A  1 341 ? -2.370  -12.775 38.925   1.00 143.95 ? 341  GLY A CA  1 
ATOM   2622  C  C   . GLY A  1 341 ? -2.060  -12.256 37.542   1.00 143.34 ? 341  GLY A C   1 
ATOM   2623  O  O   . GLY A  1 341 ? -2.049  -13.047 36.592   1.00 142.23 ? 341  GLY A O   1 
ATOM   2624  N  N   . SER A  1 342 ? -1.869  -10.947 37.387   1.00 144.25 ? 342  SER A N   1 
ATOM   2625  C  CA  . SER A  1 342 ? -1.537  -10.397 36.081   1.00 144.06 ? 342  SER A CA  1 
ATOM   2626  C  C   . SER A  1 342 ? -0.151  -10.823 35.622   1.00 145.58 ? 342  SER A C   1 
ATOM   2627  O  O   . SER A  1 342 ? 0.067   -11.037 34.424   1.00 145.10 ? 342  SER A O   1 
ATOM   2628  C  CB  . SER A  1 342 ? -1.622  -8.879  36.132   1.00 145.20 ? 342  SER A CB  1 
ATOM   2629  O  OG  . SER A  1 342 ? -2.939  -8.476  36.444   1.00 169.12 ? 342  SER A OG  1 
ATOM   2630  N  N   . ALA A  1 343 ? 0.792   -10.956 36.550   1.00 150.63 ? 343  ALA A N   1 
ATOM   2631  C  CA  . ALA A  1 343 ? 2.143   -11.386 36.231   1.00 155.33 ? 343  ALA A CA  1 
ATOM   2632  C  C   . ALA A  1 343 ? 2.608   -12.402 37.262   1.00 150.99 ? 343  ALA A C   1 
ATOM   2633  O  O   . ALA A  1 343 ? 2.363   -12.241 38.462   1.00 151.59 ? 343  ALA A O   1 
ATOM   2634  C  CB  . ALA A  1 343 ? 3.109   -10.198 36.184   1.00 160.16 ? 343  ALA A CB  1 
ATOM   2635  N  N   . ILE A  1 344 ? 3.273   -13.449 36.781   1.00 151.66 ? 344  ILE A N   1 
ATOM   2636  C  CA  . ILE A  1 344 ? 3.769   -14.543 37.607   1.00 153.15 ? 344  ILE A CA  1 
ATOM   2637  C  C   . ILE A  1 344 ? 5.215   -14.797 37.198   1.00 185.88 ? 344  ILE A C   1 
ATOM   2638  O  O   . ILE A  1 344 ? 5.478   -15.194 36.055   1.00 189.76 ? 344  ILE A O   1 
ATOM   2639  C  CB  . ILE A  1 344 ? 2.922   -15.813 37.453   1.00 151.16 ? 344  ILE A CB  1 
ATOM   2640  C  CG1 . ILE A  1 344 ? 1.435   -15.487 37.635   1.00 156.56 ? 344  ILE A CG1 1 
ATOM   2641  C  CG2 . ILE A  1 344 ? 3.361   -16.870 38.451   1.00 152.98 ? 344  ILE A CG2 1 
ATOM   2642  C  CD1 . ILE A  1 344 ? 0.505   -16.651 37.358   1.00 159.47 ? 344  ILE A CD1 1 
ATOM   2643  N  N   . ALA A  1 345 ? 6.150   -14.540 38.110   1.00 191.84 ? 345  ALA A N   1 
ATOM   2644  C  CA  . ALA A  1 345 ? 7.584   -14.689 37.843   1.00 162.64 ? 345  ALA A CA  1 
ATOM   2645  C  C   . ALA A  1 345 ? 8.195   -15.731 38.765   1.00 165.08 ? 345  ALA A C   1 
ATOM   2646  O  O   . ALA A  1 345 ? 8.214   -15.526 39.994   1.00 166.21 ? 345  ALA A O   1 
ATOM   2647  C  CB  . ALA A  1 345 ? 8.310   -13.356 38.017   1.00 164.88 ? 345  ALA A CB  1 
ATOM   2648  N  N   . PRO A  1 346 ? 8.681   -16.857 38.244   1.00 166.24 ? 346  PRO A N   1 
ATOM   2649  C  CA  . PRO A  1 346 ? 9.441   -17.788 39.087   1.00 169.42 ? 346  PRO A CA  1 
ATOM   2650  C  C   . PRO A  1 346 ? 10.695  -17.114 39.617   1.00 173.46 ? 346  PRO A C   1 
ATOM   2651  O  O   . PRO A  1 346 ? 11.423  -16.454 38.873   1.00 174.96 ? 346  PRO A O   1 
ATOM   2652  C  CB  . PRO A  1 346 ? 9.775   -18.942 38.136   1.00 170.25 ? 346  PRO A CB  1 
ATOM   2653  C  CG  . PRO A  1 346 ? 8.796   -18.818 37.013   1.00 170.38 ? 346  PRO A CG  1 
ATOM   2654  C  CD  . PRO A  1 346 ? 8.548   -17.346 36.863   1.00 165.09 ? 346  PRO A CD  1 
ATOM   2655  N  N   . LEU A  1 347 ? 10.937  -17.269 40.916   1.00 175.48 ? 347  LEU A N   1 
ATOM   2656  C  CA  . LEU A  1 347 ? 12.030  -16.577 41.589   1.00 181.01 ? 347  LEU A CA  1 
ATOM   2657  C  C   . LEU A  1 347 ? 13.241  -17.463 41.853   1.00 184.09 ? 347  LEU A C   1 
ATOM   2658  O  O   . LEU A  1 347 ? 14.247  -16.975 42.380   1.00 188.02 ? 347  LEU A O   1 
ATOM   2659  C  CB  . LEU A  1 347 ? 11.534  -15.990 42.914   1.00 181.16 ? 347  LEU A CB  1 
ATOM   2660  C  CG  . LEU A  1 347 ? 10.297  -15.099 42.845   1.00 175.36 ? 347  LEU A CG  1 
ATOM   2661  C  CD1 . LEU A  1 347 ? 9.902   -14.626 44.234   1.00 176.06 ? 347  LEU A CD1 1 
ATOM   2662  C  CD2 . LEU A  1 347 ? 10.556  -13.919 41.928   1.00 175.11 ? 347  LEU A CD2 1 
ATOM   2663  N  N   . GLY A  1 348 ? 13.176  -18.746 41.505   1.00 184.08 ? 348  GLY A N   1 
ATOM   2664  C  CA  . GLY A  1 348 ? 14.208  -19.632 41.988   1.00 188.73 ? 348  GLY A CA  1 
ATOM   2665  C  C   . GLY A  1 348 ? 13.983  -19.888 43.466   1.00 189.74 ? 348  GLY A C   1 
ATOM   2666  O  O   . GLY A  1 348 ? 12.857  -19.852 43.965   1.00 186.40 ? 348  GLY A O   1 
ATOM   2667  N  N   . ASP A  1 349 ? 15.070  -20.143 44.186   1.00 198.51 ? 349  ASP A N   1 
ATOM   2668  C  CA  . ASP A  1 349 ? 15.003  -20.298 45.637   1.00 201.93 ? 349  ASP A CA  1 
ATOM   2669  C  C   . ASP A  1 349 ? 15.434  -18.964 46.234   1.00 205.77 ? 349  ASP A C   1 
ATOM   2670  O  O   . ASP A  1 349 ? 16.598  -18.765 46.584   1.00 206.77 ? 349  ASP A O   1 
ATOM   2671  C  CB  . ASP A  1 349 ? 15.874  -21.448 46.119   1.00 205.28 ? 349  ASP A CB  1 
ATOM   2672  C  CG  . ASP A  1 349 ? 15.465  -21.947 47.490   1.00 211.04 ? 349  ASP A CG  1 
ATOM   2673  O  OD1 . ASP A  1 349 ? 14.708  -21.233 48.192   1.00 215.83 ? 349  ASP A OD1 1 
ATOM   2674  O  OD2 . ASP A  1 349 ? 15.898  -23.056 47.864   1.00 219.78 ? 349  ASP A OD2 1 
ATOM   2675  N  N   . LEU A  1 350 ? 14.469  -18.045 46.343   1.00 201.32 ? 350  LEU A N   1 
ATOM   2676  C  CA  . LEU A  1 350 ? 14.754  -16.681 46.781   1.00 202.63 ? 350  LEU A CA  1 
ATOM   2677  C  C   . LEU A  1 350 ? 15.466  -16.646 48.128   1.00 207.43 ? 350  LEU A C   1 
ATOM   2678  O  O   . LEU A  1 350 ? 16.328  -15.789 48.351   1.00 210.88 ? 350  LEU A O   1 
ATOM   2679  C  CB  . LEU A  1 350 ? 13.454  -15.880 46.853   1.00 198.12 ? 350  LEU A CB  1 
ATOM   2680  C  CG  . LEU A  1 350 ? 13.567  -14.390 47.184   1.00 207.45 ? 350  LEU A CG  1 
ATOM   2681  C  CD1 . LEU A  1 350 ? 14.355  -13.659 46.109   1.00 200.11 ? 350  LEU A CD1 1 
ATOM   2682  C  CD2 . LEU A  1 350 ? 12.196  -13.757 47.378   1.00 212.94 ? 350  LEU A CD2 1 
ATOM   2683  N  N   . ASP A  1 351 ? 15.140  -17.569 49.030   1.00 212.25 ? 351  ASP A N   1 
ATOM   2684  C  CA  . ASP A  1 351 ? 15.712  -17.560 50.369   1.00 216.85 ? 351  ASP A CA  1 
ATOM   2685  C  C   . ASP A  1 351 ? 16.623  -18.755 50.615   1.00 229.96 ? 351  ASP A C   1 
ATOM   2686  O  O   . ASP A  1 351 ? 17.108  -18.932 51.738   1.00 244.44 ? 351  ASP A O   1 
ATOM   2687  C  CB  . ASP A  1 351 ? 14.603  -17.481 51.426   1.00 226.42 ? 351  ASP A CB  1 
ATOM   2688  C  CG  . ASP A  1 351 ? 13.495  -18.498 51.208   1.00 235.53 ? 351  ASP A CG  1 
ATOM   2689  O  OD1 . ASP A  1 351 ? 13.104  -18.724 50.042   1.00 241.21 ? 351  ASP A OD1 1 
ATOM   2690  O  OD2 . ASP A  1 351 ? 12.989  -19.047 52.213   1.00 232.90 ? 351  ASP A OD2 1 
ATOM   2691  N  N   . GLN A  1 352 ? 16.888  -19.557 49.581   1.00 213.26 ? 352  GLN A N   1 
ATOM   2692  C  CA  . GLN A  1 352 ? 17.825  -20.677 49.657   1.00 226.95 ? 352  GLN A CA  1 
ATOM   2693  C  C   . GLN A  1 352 ? 17.470  -21.630 50.797   1.00 231.43 ? 352  GLN A C   1 
ATOM   2694  O  O   . GLN A  1 352 ? 18.299  -21.964 51.646   1.00 230.79 ? 352  GLN A O   1 
ATOM   2695  C  CB  . GLN A  1 352 ? 19.264  -20.174 49.788   1.00 223.58 ? 352  GLN A CB  1 
ATOM   2696  C  CG  . GLN A  1 352 ? 19.805  -19.420 48.571   1.00 226.27 ? 352  GLN A CG  1 
ATOM   2697  C  CD  . GLN A  1 352 ? 19.927  -20.278 47.316   1.00 223.48 ? 352  GLN A CD  1 
ATOM   2698  O  OE1 . GLN A  1 352 ? 18.935  -20.786 46.789   1.00 217.73 ? 352  GLN A OE1 1 
ATOM   2699  N  NE2 . GLN A  1 352 ? 21.154  -20.447 46.838   1.00 227.13 ? 352  GLN A NE2 1 
ATOM   2700  N  N   . ASP A  1 353 ? 16.213  -22.073 50.811   1.00 229.96 ? 353  ASP A N   1 
ATOM   2701  C  CA  . ASP A  1 353 ? 15.740  -23.030 51.801   1.00 223.29 ? 353  ASP A CA  1 
ATOM   2702  C  C   . ASP A  1 353 ? 15.584  -24.438 51.238   1.00 225.89 ? 353  ASP A C   1 
ATOM   2703  O  O   . ASP A  1 353 ? 15.217  -25.354 51.981   1.00 235.13 ? 353  ASP A O   1 
ATOM   2704  C  CB  . ASP A  1 353 ? 14.406  -22.555 52.403   1.00 218.94 ? 353  ASP A CB  1 
ATOM   2705  C  CG  . ASP A  1 353 ? 13.309  -22.330 51.344   1.00 240.62 ? 353  ASP A CG  1 
ATOM   2706  O  OD1 . ASP A  1 353 ? 13.437  -22.825 50.206   1.00 248.99 ? 353  ASP A OD1 1 
ATOM   2707  O  OD2 . ASP A  1 353 ? 12.304  -21.651 51.652   1.00 235.45 ? 353  ASP A OD2 1 
ATOM   2708  N  N   . GLY A  1 354 ? 15.879  -24.639 49.955   1.00 217.18 ? 354  GLY A N   1 
ATOM   2709  C  CA  . GLY A  1 354 ? 15.734  -25.931 49.322   1.00 217.09 ? 354  GLY A CA  1 
ATOM   2710  C  C   . GLY A  1 354 ? 14.468  -26.090 48.511   1.00 211.85 ? 354  GLY A C   1 
ATOM   2711  O  O   . GLY A  1 354 ? 14.261  -27.156 47.917   1.00 211.14 ? 354  GLY A O   1 
ATOM   2712  N  N   . PHE A  1 355 ? 13.606  -25.078 48.484   1.00 200.31 ? 355  PHE A N   1 
ATOM   2713  C  CA  . PHE A  1 355 ? 12.365  -25.120 47.726   1.00 194.82 ? 355  PHE A CA  1 
ATOM   2714  C  C   . PHE A  1 355 ? 12.202  -23.819 46.960   1.00 191.63 ? 355  PHE A C   1 
ATOM   2715  O  O   . PHE A  1 355 ? 12.379  -22.734 47.523   1.00 192.04 ? 355  PHE A O   1 
ATOM   2716  C  CB  . PHE A  1 355 ? 11.163  -25.348 48.636   1.00 192.56 ? 355  PHE A CB  1 
ATOM   2717  C  CG  . PHE A  1 355 ? 11.202  -26.653 49.362   1.00 195.57 ? 355  PHE A CG  1 
ATOM   2718  C  CD1 . PHE A  1 355 ? 10.951  -27.839 48.695   1.00 195.31 ? 355  PHE A CD1 1 
ATOM   2719  C  CD2 . PHE A  1 355 ? 11.483  -26.695 50.714   1.00 198.98 ? 355  PHE A CD2 1 
ATOM   2720  C  CE1 . PHE A  1 355 ? 10.985  -29.042 49.364   1.00 198.42 ? 355  PHE A CE1 1 
ATOM   2721  C  CE2 . PHE A  1 355 ? 11.518  -27.894 51.389   1.00 202.05 ? 355  PHE A CE2 1 
ATOM   2722  C  CZ  . PHE A  1 355 ? 11.269  -29.070 50.714   1.00 201.77 ? 355  PHE A CZ  1 
ATOM   2723  N  N   . ASN A  1 356 ? 11.878  -23.931 45.679   1.00 188.81 ? 356  ASN A N   1 
ATOM   2724  C  CA  . ASN A  1 356 ? 11.687  -22.749 44.851   1.00 195.54 ? 356  ASN A CA  1 
ATOM   2725  C  C   . ASN A  1 356 ? 10.505  -21.915 45.343   1.00 197.84 ? 356  ASN A C   1 
ATOM   2726  O  O   . ASN A  1 356 ? 9.575   -22.418 45.983   1.00 180.47 ? 356  ASN A O   1 
ATOM   2727  C  CB  . ASN A  1 356 ? 11.476  -23.155 43.395   1.00 201.64 ? 356  ASN A CB  1 
ATOM   2728  C  CG  . ASN A  1 356 ? 12.754  -23.627 42.739   1.00 188.57 ? 356  ASN A CG  1 
ATOM   2729  O  OD1 . ASN A  1 356 ? 13.844  -23.184 43.096   1.00 208.93 ? 356  ASN A OD1 1 
ATOM   2730  N  ND2 . ASN A  1 356 ? 12.630  -24.538 41.781   1.00 187.58 ? 356  ASN A ND2 1 
ATOM   2731  N  N   . ASP A  1 357 ? 10.568  -20.618 45.057   1.00 192.31 ? 357  ASP A N   1 
ATOM   2732  C  CA  . ASP A  1 357 ? 9.571   -19.641 45.464   1.00 177.84 ? 357  ASP A CA  1 
ATOM   2733  C  C   . ASP A  1 357 ? 9.070   -18.897 44.231   1.00 174.31 ? 357  ASP A C   1 
ATOM   2734  O  O   . ASP A  1 357 ? 9.639   -19.005 43.140   1.00 174.63 ? 357  ASP A O   1 
ATOM   2735  C  CB  . ASP A  1 357 ? 10.155  -18.673 46.497   1.00 193.70 ? 357  ASP A CB  1 
ATOM   2736  C  CG  . ASP A  1 357 ? 10.898  -19.395 47.607   1.00 196.84 ? 357  ASP A CG  1 
ATOM   2737  O  OD1 . ASP A  1 357 ? 10.355  -20.382 48.151   1.00 190.41 ? 357  ASP A OD1 1 
ATOM   2738  O  OD2 . ASP A  1 357 ? 12.032  -18.988 47.930   1.00 192.29 ? 357  ASP A OD2 1 
ATOM   2739  N  N   . ILE A  1 358 ? 7.994   -18.128 44.403   1.00 176.14 ? 358  ILE A N   1 
ATOM   2740  C  CA  . ILE A  1 358 ? 7.346   -17.475 43.271   1.00 167.80 ? 358  ILE A CA  1 
ATOM   2741  C  C   . ILE A  1 358 ? 6.759   -16.134 43.695   1.00 166.66 ? 358  ILE A C   1 
ATOM   2742  O  O   . ILE A  1 358 ? 6.391   -15.931 44.856   1.00 167.39 ? 358  ILE A O   1 
ATOM   2743  C  CB  . ILE A  1 358 ? 6.267   -18.392 42.654   1.00 164.48 ? 358  ILE A CB  1 
ATOM   2744  C  CG1 . ILE A  1 358 ? 6.007   -17.998 41.199   1.00 162.04 ? 358  ILE A CG1 1 
ATOM   2745  C  CG2 . ILE A  1 358 ? 5.000   -18.365 43.490   1.00 162.41 ? 358  ILE A CG2 1 
ATOM   2746  C  CD1 . ILE A  1 358 ? 5.586   -19.148 40.318   1.00 160.53 ? 358  ILE A CD1 1 
ATOM   2747  N  N   . ALA A  1 359 ? 6.697   -15.208 42.739   1.00 165.26 ? 359  ALA A N   1 
ATOM   2748  C  CA  . ALA A  1 359 ? 6.076   -13.904 42.921   1.00 164.16 ? 359  ALA A CA  1 
ATOM   2749  C  C   . ALA A  1 359 ? 4.835   -13.775 42.043   1.00 160.15 ? 359  ALA A C   1 
ATOM   2750  O  O   . ALA A  1 359 ? 4.818   -14.240 40.898   1.00 158.65 ? 359  ALA A O   1 
ATOM   2751  C  CB  . ALA A  1 359 ? 7.066   -12.778 42.607   1.00 166.55 ? 359  ALA A CB  1 
ATOM   2752  N  N   . ILE A  1 360 ? 3.788   -13.160 42.595   1.00 158.76 ? 360  ILE A N   1 
ATOM   2753  C  CA  . ILE A  1 360 ? 2.550   -12.863 41.877   1.00 164.10 ? 360  ILE A CA  1 
ATOM   2754  C  C   . ILE A  1 360 ? 2.202   -11.398 42.102   1.00 169.24 ? 360  ILE A C   1 
ATOM   2755  O  O   . ILE A  1 360 ? 2.194   -10.928 43.245   1.00 169.70 ? 360  ILE A O   1 
ATOM   2756  C  CB  . ILE A  1 360 ? 1.386   -13.766 42.328   1.00 166.51 ? 360  ILE A CB  1 
ATOM   2757  C  CG1 . ILE A  1 360 ? 1.761   -15.244 42.193   1.00 153.61 ? 360  ILE A CG1 1 
ATOM   2758  C  CG2 . ILE A  1 360 ? 0.134   -13.461 41.525   1.00 150.35 ? 360  ILE A CG2 1 
ATOM   2759  C  CD1 . ILE A  1 360 ? 0.724   -16.193 42.754   1.00 152.33 ? 360  ILE A CD1 1 
ATOM   2760  N  N   . ALA A  1 361 ? 1.914   -10.677 41.021   1.00 154.38 ? 361  ALA A N   1 
ATOM   2761  C  CA  . ALA A  1 361 ? 1.705   -9.238  41.087   1.00 155.22 ? 361  ALA A CA  1 
ATOM   2762  C  C   . ALA A  1 361 ? 0.232   -8.862  40.974   1.00 175.28 ? 361  ALA A C   1 
ATOM   2763  O  O   . ALA A  1 361 ? -0.542  -9.514  40.265   1.00 196.27 ? 361  ALA A O   1 
ATOM   2764  C  CB  . ALA A  1 361 ? 2.497   -8.526  39.993   1.00 156.00 ? 361  ALA A CB  1 
ATOM   2765  N  N   . ALA A  1 362 ? -0.150  -7.801  41.690   1.00 195.23 ? 362  ALA A N   1 
ATOM   2766  C  CA  . ALA A  1 362 ? -1.452  -7.152  41.553   1.00 185.97 ? 362  ALA A CA  1 
ATOM   2767  C  C   . ALA A  1 362 ? -1.191  -5.715  41.112   1.00 184.78 ? 362  ALA A C   1 
ATOM   2768  O  O   . ALA A  1 362 ? -1.180  -4.791  41.943   1.00 176.32 ? 362  ALA A O   1 
ATOM   2769  C  CB  . ALA A  1 362 ? -2.251  -7.213  42.854   1.00 167.72 ? 362  ALA A CB  1 
ATOM   2770  N  N   . PRO A  1 363 ? -1.016  -5.483  39.806   1.00 155.20 ? 363  PRO A N   1 
ATOM   2771  C  CA  . PRO A  1 363 ? -0.468  -4.196  39.342   1.00 165.40 ? 363  PRO A CA  1 
ATOM   2772  C  C   . PRO A  1 363 ? -1.307  -2.993  39.714   1.00 164.19 ? 363  PRO A C   1 
ATOM   2773  O  O   . PRO A  1 363 ? -0.816  -1.861  39.614   1.00 188.55 ? 363  PRO A O   1 
ATOM   2774  C  CB  . PRO A  1 363 ? -0.406  -4.367  37.815   1.00 155.44 ? 363  PRO A CB  1 
ATOM   2775  C  CG  . PRO A  1 363 ? -0.442  -5.844  37.592   1.00 153.12 ? 363  PRO A CG  1 
ATOM   2776  C  CD  . PRO A  1 363 ? -1.309  -6.389  38.685   1.00 152.31 ? 363  PRO A CD  1 
ATOM   2777  N  N   . TYR A  1 364 ? -2.547  -3.192  40.152   1.00 155.66 ? 364  TYR A N   1 
ATOM   2778  C  CA  . TYR A  1 364 ? -3.445  -2.085  40.446   1.00 157.09 ? 364  TYR A CA  1 
ATOM   2779  C  C   . TYR A  1 364 ? -3.919  -2.102  41.896   1.00 170.11 ? 364  TYR A C   1 
ATOM   2780  O  O   . TYR A  1 364 ? -4.918  -1.456  42.227   1.00 181.54 ? 364  TYR A O   1 
ATOM   2781  C  CB  . TYR A  1 364 ? -4.632  -2.117  39.484   1.00 154.67 ? 364  TYR A CB  1 
ATOM   2782  C  CG  . TYR A  1 364 ? -4.219  -2.324  38.042   1.00 163.14 ? 364  TYR A CG  1 
ATOM   2783  C  CD1 . TYR A  1 364 ? -3.523  -1.344  37.348   1.00 156.57 ? 364  TYR A CD1 1 
ATOM   2784  C  CD2 . TYR A  1 364 ? -4.522  -3.507  37.376   1.00 168.30 ? 364  TYR A CD2 1 
ATOM   2785  C  CE1 . TYR A  1 364 ? -3.143  -1.536  36.029   1.00 173.81 ? 364  TYR A CE1 1 
ATOM   2786  C  CE2 . TYR A  1 364 ? -4.145  -3.706  36.057   1.00 159.61 ? 364  TYR A CE2 1 
ATOM   2787  C  CZ  . TYR A  1 364 ? -3.458  -2.717  35.388   1.00 150.39 ? 364  TYR A CZ  1 
ATOM   2788  O  OH  . TYR A  1 364 ? -3.083  -2.910  34.077   1.00 149.49 ? 364  TYR A OH  1 
ATOM   2789  N  N   . GLY A  1 365 ? -3.215  -2.822  42.769   1.00 165.51 ? 365  GLY A N   1 
ATOM   2790  C  CA  . GLY A  1 365 ? -3.538  -2.863  44.178   1.00 167.49 ? 365  GLY A CA  1 
ATOM   2791  C  C   . GLY A  1 365 ? -2.802  -1.795  44.962   1.00 171.68 ? 365  GLY A C   1 
ATOM   2792  O  O   . GLY A  1 365 ? -2.138  -0.915  44.411   1.00 188.21 ? 365  GLY A O   1 
ATOM   2793  N  N   . GLY A  1 366 ? -2.945  -1.869  46.284   1.00 179.05 ? 366  GLY A N   1 
ATOM   2794  C  CA  . GLY A  1 366 ? -2.260  -0.941  47.161   1.00 188.28 ? 366  GLY A CA  1 
ATOM   2795  C  C   . GLY A  1 366 ? -2.909  0.429   47.154   1.00 190.87 ? 366  GLY A C   1 
ATOM   2796  O  O   . GLY A  1 366 ? -3.871  0.701   46.435   1.00 184.78 ? 366  GLY A O   1 
ATOM   2797  N  N   . GLU A  1 367 ? -2.372  1.305   48.001   1.00 182.60 ? 367  GLU A N   1 
ATOM   2798  C  CA  . GLU A  1 367 ? -2.869  2.672   48.077   1.00 192.52 ? 367  GLU A CA  1 
ATOM   2799  C  C   . GLU A  1 367 ? -2.699  3.385   46.741   1.00 185.58 ? 367  GLU A C   1 
ATOM   2800  O  O   . GLU A  1 367 ? -1.674  3.244   46.068   1.00 185.35 ? 367  GLU A O   1 
ATOM   2801  C  CB  . GLU A  1 367 ? -2.134  3.439   49.175   1.00 210.54 ? 367  GLU A CB  1 
ATOM   2802  C  CG  . GLU A  1 367 ? -0.621  3.451   49.021   1.00 213.37 ? 367  GLU A CG  1 
ATOM   2803  C  CD  . GLU A  1 367 ? 0.062   4.284   50.082   1.00 218.90 ? 367  GLU A CD  1 
ATOM   2804  O  OE1 . GLU A  1 367 ? 1.199   4.736   49.844   1.00 211.72 ? 367  GLU A OE1 1 
ATOM   2805  O  OE2 . GLU A  1 367 ? -0.550  4.510   51.147   1.00 236.21 ? 367  GLU A OE2 1 
ATOM   2806  N  N   . ASP A  1 368 ? -3.718  4.153   46.357   1.00 188.26 ? 368  ASP A N   1 
ATOM   2807  C  CA  . ASP A  1 368 ? -3.717  4.938   45.125   1.00 190.83 ? 368  ASP A CA  1 
ATOM   2808  C  C   . ASP A  1 368 ? -3.556  4.067   43.885   1.00 196.90 ? 368  ASP A C   1 
ATOM   2809  O  O   . ASP A  1 368 ? -3.116  4.556   42.838   1.00 204.14 ? 368  ASP A O   1 
ATOM   2810  C  CB  . ASP A  1 368 ? -2.623  6.013   45.154   1.00 195.06 ? 368  ASP A CB  1 
ATOM   2811  C  CG  . ASP A  1 368 ? -2.970  7.223   44.312   1.00 217.01 ? 368  ASP A CG  1 
ATOM   2812  O  OD1 . ASP A  1 368 ? -3.831  7.103   43.416   1.00 239.44 ? 368  ASP A OD1 1 
ATOM   2813  O  OD2 . ASP A  1 368 ? -2.378  8.297   44.546   1.00 219.46 ? 368  ASP A OD2 1 
ATOM   2814  N  N   . LYS A  1 369 ? -3.898  2.782   43.991   1.00 197.83 ? 369  LYS A N   1 
ATOM   2815  C  CA  . LYS A  1 369 ? -3.793  1.829   42.885   1.00 197.09 ? 369  LYS A CA  1 
ATOM   2816  C  C   . LYS A  1 369 ? -2.423  1.911   42.210   1.00 193.82 ? 369  LYS A C   1 
ATOM   2817  O  O   . LYS A  1 369 ? -2.304  2.029   40.987   1.00 169.41 ? 369  LYS A O   1 
ATOM   2818  C  CB  . LYS A  1 369 ? -4.924  2.032   41.877   1.00 194.91 ? 369  LYS A CB  1 
ATOM   2819  C  CG  . LYS A  1 369 ? -6.319  1.967   42.489   1.00 178.34 ? 369  LYS A CG  1 
ATOM   2820  C  CD  . LYS A  1 369 ? -7.326  1.345   41.524   1.00 164.95 ? 369  LYS A CD  1 
ATOM   2821  C  CE  . LYS A  1 369 ? -7.367  2.078   40.189   1.00 164.68 ? 369  LYS A CE  1 
ATOM   2822  N  NZ  . LYS A  1 369 ? -8.286  1.411   39.224   1.00 172.00 ? 369  LYS A NZ  1 
ATOM   2823  N  N   . LYS A  1 370 ? -1.375  1.839   43.030   1.00 186.13 ? 370  LYS A N   1 
ATOM   2824  C  CA  . LYS A  1 370 ? -0.008  1.986   42.545   1.00 177.92 ? 370  LYS A CA  1 
ATOM   2825  C  C   . LYS A  1 370 ? 0.604   0.654   42.151   1.00 173.75 ? 370  LYS A C   1 
ATOM   2826  O  O   . LYS A  1 370 ? 1.278   0.564   41.122   1.00 173.01 ? 370  LYS A O   1 
ATOM   2827  C  CB  . LYS A  1 370 ? 0.863   2.653   43.616   1.00 186.06 ? 370  LYS A CB  1 
ATOM   2828  C  CG  . LYS A  1 370 ? 0.605   4.138   43.808   1.00 205.64 ? 370  LYS A CG  1 
ATOM   2829  C  CD  . LYS A  1 370 ? 1.585   4.748   44.806   1.00 221.75 ? 370  LYS A CD  1 
ATOM   2830  C  CE  . LYS A  1 370 ? 1.091   6.096   45.325   1.00 231.01 ? 370  LYS A CE  1 
ATOM   2831  N  NZ  . LYS A  1 370 ? 2.069   6.743   46.249   1.00 226.14 ? 370  LYS A NZ  1 
ATOM   2832  N  N   . GLY A  1 371 ? 0.359   -0.386  42.938   1.00 176.33 ? 371  GLY A N   1 
ATOM   2833  C  CA  . GLY A  1 371 ? 0.796   -1.729  42.601   1.00 173.79 ? 371  GLY A CA  1 
ATOM   2834  C  C   . GLY A  1 371 ? 1.421   -2.456  43.776   1.00 175.33 ? 371  GLY A C   1 
ATOM   2835  O  O   . GLY A  1 371 ? 2.050   -1.854  44.650   1.00 184.00 ? 371  GLY A O   1 
ATOM   2836  N  N   . ILE A  1 372 ? 1.233   -3.775  43.802   1.00 165.24 ? 372  ILE A N   1 
ATOM   2837  C  CA  . ILE A  1 372 ? 1.748   -4.640  44.860   1.00 166.51 ? 372  ILE A CA  1 
ATOM   2838  C  C   . ILE A  1 372 ? 2.296   -5.909  44.218   1.00 164.54 ? 372  ILE A C   1 
ATOM   2839  O  O   . ILE A  1 372 ? 1.725   -6.422  43.249   1.00 161.32 ? 372  ILE A O   1 
ATOM   2840  C  CB  . ILE A  1 372 ? 0.656   -4.991  45.895   1.00 196.31 ? 372  ILE A CB  1 
ATOM   2841  C  CG1 . ILE A  1 372 ? 0.045   -3.730  46.506   1.00 188.98 ? 372  ILE A CG1 1 
ATOM   2842  C  CG2 . ILE A  1 372 ? 1.225   -5.862  47.006   1.00 202.23 ? 372  ILE A CG2 1 
ATOM   2843  C  CD1 . ILE A  1 372 ? 0.970   -3.006  47.450   1.00 192.43 ? 372  ILE A CD1 1 
ATOM   2844  N  N   . VAL A  1 373 ? 3.406   -6.418  44.753   1.00 166.80 ? 373  VAL A N   1 
ATOM   2845  C  CA  . VAL A  1 373 ? 3.938   -7.721  44.370   1.00 165.68 ? 373  VAL A CA  1 
ATOM   2846  C  C   . VAL A  1 373 ? 4.028   -8.579  45.623   1.00 168.70 ? 373  VAL A C   1 
ATOM   2847  O  O   . VAL A  1 373 ? 4.637   -8.170  46.618   1.00 204.22 ? 373  VAL A O   1 
ATOM   2848  C  CB  . VAL A  1 373 ? 5.314   -7.611  43.687   1.00 167.62 ? 373  VAL A CB  1 
ATOM   2849  C  CG1 . VAL A  1 373 ? 5.867   -8.997  43.404   1.00 176.85 ? 373  VAL A CG1 1 
ATOM   2850  C  CG2 . VAL A  1 373 ? 5.218   -6.805  42.405   1.00 166.42 ? 373  VAL A CG2 1 
ATOM   2851  N  N   . TYR A  1 374 ? 3.444   -9.769  45.564   1.00 164.77 ? 374  TYR A N   1 
ATOM   2852  C  CA  . TYR A  1 374 ? 3.413   -10.684 46.695   1.00 165.95 ? 374  TYR A CA  1 
ATOM   2853  C  C   . TYR A  1 374 ? 4.431   -11.798 46.484   1.00 190.21 ? 374  TYR A C   1 
ATOM   2854  O  O   . TYR A  1 374 ? 4.560   -12.331 45.376   1.00 198.05 ? 374  TYR A O   1 
ATOM   2855  C  CB  . TYR A  1 374 ? 2.013   -11.271 46.889   1.00 163.22 ? 374  TYR A CB  1 
ATOM   2856  C  CG  . TYR A  1 374 ? 0.924   -10.253 47.187   1.00 169.97 ? 374  TYR A CG  1 
ATOM   2857  C  CD1 . TYR A  1 374 ? 0.669   -9.831  48.488   1.00 169.84 ? 374  TYR A CD1 1 
ATOM   2858  C  CD2 . TYR A  1 374 ? 0.122   -9.744  46.168   1.00 181.93 ? 374  TYR A CD2 1 
ATOM   2859  C  CE1 . TYR A  1 374 ? -0.342  -8.909  48.765   1.00 165.26 ? 374  TYR A CE1 1 
ATOM   2860  C  CE2 . TYR A  1 374 ? -0.892  -8.825  46.435   1.00 181.21 ? 374  TYR A CE2 1 
ATOM   2861  C  CZ  . TYR A  1 374 ? -1.119  -8.411  47.733   1.00 169.77 ? 374  TYR A CZ  1 
ATOM   2862  O  OH  . TYR A  1 374 ? -2.123  -7.501  47.989   1.00 163.00 ? 374  TYR A OH  1 
ATOM   2863  N  N   . ILE A  1 375 ? 5.186   -12.108 47.535   1.00 186.33 ? 375  ILE A N   1 
ATOM   2864  C  CA  . ILE A  1 375 ? 6.201   -13.156 47.512   1.00 171.94 ? 375  ILE A CA  1 
ATOM   2865  C  C   . ILE A  1 375 ? 5.664   -14.390 48.226   1.00 171.56 ? 375  ILE A C   1 
ATOM   2866  O  O   . ILE A  1 375 ? 5.248   -14.310 49.388   1.00 184.96 ? 375  ILE A O   1 
ATOM   2867  C  CB  . ILE A  1 375 ? 7.500   -12.667 48.165   1.00 176.56 ? 375  ILE A CB  1 
ATOM   2868  C  CG1 . ILE A  1 375 ? 7.903   -11.318 47.561   1.00 177.19 ? 375  ILE A CG1 1 
ATOM   2869  C  CG2 . ILE A  1 375 ? 8.584   -13.712 48.023   1.00 178.72 ? 375  ILE A CG2 1 
ATOM   2870  C  CD1 . ILE A  1 375 ? 8.029   -11.335 46.055   1.00 174.85 ? 375  ILE A CD1 1 
ATOM   2871  N  N   . PHE A  1 376 ? 5.686   -15.534 47.548   1.00 173.47 ? 376  PHE A N   1 
ATOM   2872  C  CA  . PHE A  1 376 ? 5.209   -16.787 48.119   1.00 173.31 ? 376  PHE A CA  1 
ATOM   2873  C  C   . PHE A  1 376 ? 6.333   -17.810 48.123   1.00 176.10 ? 376  PHE A C   1 
ATOM   2874  O  O   . PHE A  1 376 ? 7.050   -17.959 47.127   1.00 179.41 ? 376  PHE A O   1 
ATOM   2875  C  CB  . PHE A  1 376 ? 4.007   -17.334 47.351   1.00 169.25 ? 376  PHE A CB  1 
ATOM   2876  C  CG  . PHE A  1 376 ? 2.797   -16.449 47.406   1.00 166.81 ? 376  PHE A CG  1 
ATOM   2877  C  CD1 . PHE A  1 376 ? 1.969   -16.446 48.515   1.00 183.54 ? 376  PHE A CD1 1 
ATOM   2878  C  CD2 . PHE A  1 376 ? 2.488   -15.618 46.346   1.00 183.47 ? 376  PHE A CD2 1 
ATOM   2879  C  CE1 . PHE A  1 376 ? 0.849   -15.632 48.559   1.00 178.59 ? 376  PHE A CE1 1 
ATOM   2880  C  CE2 . PHE A  1 376 ? 1.372   -14.801 46.386   1.00 178.61 ? 376  PHE A CE2 1 
ATOM   2881  C  CZ  . PHE A  1 376 ? 0.553   -14.809 47.494   1.00 166.70 ? 376  PHE A CZ  1 
ATOM   2882  N  N   . ASN A  1 377 ? 6.479   -18.512 49.242   1.00 177.53 ? 377  ASN A N   1 
ATOM   2883  C  CA  . ASN A  1 377 ? 7.523   -19.509 49.421   1.00 183.64 ? 377  ASN A CA  1 
ATOM   2884  C  C   . ASN A  1 377 ? 6.974   -20.919 49.216   1.00 196.84 ? 377  ASN A C   1 
ATOM   2885  O  O   . ASN A  1 377 ? 5.804   -21.200 49.495   1.00 203.84 ? 377  ASN A O   1 
ATOM   2886  C  CB  . ASN A  1 377 ? 8.151   -19.381 50.814   1.00 189.80 ? 377  ASN A CB  1 
ATOM   2887  C  CG  . ASN A  1 377 ? 8.880   -18.054 51.011   1.00 193.82 ? 377  ASN A CG  1 
ATOM   2888  O  OD1 . ASN A  1 377 ? 8.284   -17.062 51.431   1.00 197.52 ? 377  ASN A OD1 1 
ATOM   2889  N  ND2 . ASN A  1 377 ? 10.181  -18.044 50.738   1.00 190.50 ? 377  ASN A ND2 1 
ATOM   2890  N  N   . GLY A  1 378 ? 7.830   -21.800 48.675   1.00 179.32 ? 378  GLY A N   1 
ATOM   2891  C  CA  . GLY A  1 378 ? 7.485   -23.196 48.525   1.00 179.17 ? 378  GLY A CA  1 
ATOM   2892  C  C   . GLY A  1 378 ? 7.756   -24.002 49.782   1.00 182.89 ? 378  GLY A C   1 
ATOM   2893  O  O   . GLY A  1 378 ? 8.457   -23.571 50.694   1.00 186.20 ? 378  GLY A O   1 
ATOM   2894  N  N   . ARG A  1 379 ? 7.181   -25.200 49.819   1.00 184.40 ? 379  ARG A N   1 
ATOM   2895  C  CA  . ARG A  1 379 ? 7.413   -26.145 50.905   1.00 186.32 ? 379  ARG A CA  1 
ATOM   2896  C  C   . ARG A  1 379 ? 7.130   -27.545 50.373   1.00 186.31 ? 379  ARG A C   1 
ATOM   2897  O  O   . ARG A  1 379 ? 6.776   -27.726 49.203   1.00 183.48 ? 379  ARG A O   1 
ATOM   2898  C  CB  . ARG A  1 379 ? 6.559   -25.812 52.138   1.00 186.12 ? 379  ARG A CB  1 
ATOM   2899  C  CG  . ARG A  1 379 ? 5.109   -25.467 51.824   1.00 181.43 ? 379  ARG A CG  1 
ATOM   2900  C  CD  . ARG A  1 379 ? 4.342   -24.859 52.999   1.00 181.54 ? 379  ARG A CD  1 
ATOM   2901  N  NE  . ARG A  1 379 ? 2.948   -24.611 52.624   1.00 195.86 ? 379  ARG A NE  1 
ATOM   2902  C  CZ  . ARG A  1 379 ? 2.024   -24.066 53.414   1.00 193.18 ? 379  ARG A CZ  1 
ATOM   2903  N  NH1 . ARG A  1 379 ? 2.329   -23.699 54.652   1.00 187.26 ? 379  ARG A NH1 1 
ATOM   2904  N  NH2 . ARG A  1 379 ? 0.785   -23.892 52.962   1.00 173.28 ? 379  ARG A NH2 1 
ATOM   2905  N  N   . SER A  1 380 ? 7.343   -28.543 51.236   1.00 189.94 ? 380  SER A N   1 
ATOM   2906  C  CA  . SER A  1 380 ? 7.195   -29.934 50.822   1.00 190.91 ? 380  SER A CA  1 
ATOM   2907  C  C   . SER A  1 380 ? 5.811   -30.208 50.249   1.00 186.54 ? 380  SER A C   1 
ATOM   2908  O  O   . SER A  1 380 ? 5.668   -30.976 49.292   1.00 200.53 ? 380  SER A O   1 
ATOM   2909  C  CB  . SER A  1 380 ? 7.477   -30.863 52.003   1.00 195.54 ? 380  SER A CB  1 
ATOM   2910  O  OG  . SER A  1 380 ? 6.525   -30.682 53.037   1.00 194.68 ? 380  SER A OG  1 
ATOM   2911  N  N   . THR A  1 381 ? 4.781   -29.577 50.806   1.00 184.73 ? 381  THR A N   1 
ATOM   2912  C  CA  . THR A  1 381 ? 3.408   -29.796 50.366   1.00 180.95 ? 381  THR A CA  1 
ATOM   2913  C  C   . THR A  1 381 ? 2.999   -28.842 49.256   1.00 176.57 ? 381  THR A C   1 
ATOM   2914  O  O   . THR A  1 381 ? 1.875   -28.935 48.754   1.00 180.82 ? 381  THR A O   1 
ATOM   2915  C  CB  . THR A  1 381 ? 2.452   -29.664 51.557   1.00 199.14 ? 381  THR A CB  1 
ATOM   2916  O  OG1 . THR A  1 381 ? 3.035   -30.302 52.701   1.00 218.02 ? 381  THR A OG1 1 
ATOM   2917  C  CG2 . THR A  1 381 ? 1.110   -30.338 51.265   1.00 178.52 ? 381  THR A CG2 1 
ATOM   2918  N  N   . GLY A  1 382 ? 3.886   -27.943 48.844   1.00 175.81 ? 382  GLY A N   1 
ATOM   2919  C  CA  . GLY A  1 382 ? 3.566   -27.023 47.774   1.00 172.07 ? 382  GLY A CA  1 
ATOM   2920  C  C   . GLY A  1 382 ? 3.849   -25.572 48.092   1.00 171.54 ? 382  GLY A C   1 
ATOM   2921  O  O   . GLY A  1 382 ? 4.804   -25.259 48.804   1.00 174.70 ? 382  GLY A O   1 
ATOM   2922  N  N   . LEU A  1 383 ? 3.044   -24.671 47.539   1.00 173.94 ? 383  LEU A N   1 
ATOM   2923  C  CA  . LEU A  1 383 ? 3.238   -23.241 47.722   1.00 173.42 ? 383  LEU A CA  1 
ATOM   2924  C  C   . LEU A  1 383 ? 2.527   -22.745 48.975   1.00 182.79 ? 383  LEU A C   1 
ATOM   2925  O  O   . LEU A  1 383 ? 1.378   -23.112 49.239   1.00 177.41 ? 383  LEU A O   1 
ATOM   2926  C  CB  . LEU A  1 383 ? 2.728   -22.481 46.500   1.00 193.68 ? 383  LEU A CB  1 
ATOM   2927  C  CG  . LEU A  1 383 ? 3.054   -20.991 46.478   1.00 192.57 ? 383  LEU A CG  1 
ATOM   2928  C  CD1 . LEU A  1 383 ? 4.559   -20.801 46.436   1.00 172.70 ? 383  LEU A CD1 1 
ATOM   2929  C  CD2 . LEU A  1 383 ? 2.389   -20.327 45.285   1.00 185.40 ? 383  LEU A CD2 1 
ATOM   2930  N  N   . ASN A  1 384 ? 3.210   -21.891 49.733   1.00 170.81 ? 384  ASN A N   1 
ATOM   2931  C  CA  . ASN A  1 384 ? 2.611   -21.268 50.909   1.00 171.59 ? 384  ASN A CA  1 
ATOM   2932  C  C   . ASN A  1 384 ? 1.593   -20.218 50.489   1.00 168.31 ? 384  ASN A C   1 
ATOM   2933  O  O   . ASN A  1 384 ? 1.945   -19.226 49.843   1.00 176.06 ? 384  ASN A O   1 
ATOM   2934  C  CB  . ASN A  1 384 ? 3.690   -20.642 51.784   1.00 179.14 ? 384  ASN A CB  1 
ATOM   2935  C  CG  . ASN A  1 384 ? 3.149   -20.134 53.103   1.00 180.17 ? 384  ASN A CG  1 
ATOM   2936  O  OD1 . ASN A  1 384 ? 3.594   -19.103 53.606   1.00 178.97 ? 384  ASN A OD1 1 
ATOM   2937  N  ND2 . ASN A  1 384 ? 2.179   -20.846 53.666   1.00 184.01 ? 384  ASN A ND2 1 
ATOM   2938  N  N   . ALA A  1 385 ? 0.329   -20.437 50.860   1.00 178.47 ? 385  ALA A N   1 
ATOM   2939  C  CA  . ALA A  1 385 ? -0.744  -19.548 50.426   1.00 188.71 ? 385  ALA A CA  1 
ATOM   2940  C  C   . ALA A  1 385 ? -0.611  -18.146 51.008   1.00 186.79 ? 385  ALA A C   1 
ATOM   2941  O  O   . ALA A  1 385 ? -1.124  -17.186 50.421   1.00 184.92 ? 385  ALA A O   1 
ATOM   2942  C  CB  . ALA A  1 385 ? -2.101  -20.140 50.800   1.00 179.21 ? 385  ALA A CB  1 
ATOM   2943  N  N   . VAL A  1 386 ? 0.050   -18.001 52.153   1.00 179.27 ? 386  VAL A N   1 
ATOM   2944  C  CA  . VAL A  1 386 ? 0.210   -16.685 52.773   1.00 179.26 ? 386  VAL A CA  1 
ATOM   2945  C  C   . VAL A  1 386 ? 1.526   -16.055 52.329   1.00 186.24 ? 386  VAL A C   1 
ATOM   2946  O  O   . VAL A  1 386 ? 2.570   -16.725 52.335   1.00 198.29 ? 386  VAL A O   1 
ATOM   2947  C  CB  . VAL A  1 386 ? 0.109   -16.770 54.305   1.00 197.16 ? 386  VAL A CB  1 
ATOM   2948  C  CG1 . VAL A  1 386 ? -1.330  -17.052 54.720   1.00 213.78 ? 386  VAL A CG1 1 
ATOM   2949  C  CG2 . VAL A  1 386 ? 1.034   -17.843 54.856   1.00 191.38 ? 386  VAL A CG2 1 
ATOM   2950  N  N   . PRO A  1 387 ? 1.515   -14.793 51.895   1.00 176.89 ? 387  PRO A N   1 
ATOM   2951  C  CA  . PRO A  1 387 ? 2.760   -14.161 51.445   1.00 189.42 ? 387  PRO A CA  1 
ATOM   2952  C  C   . PRO A  1 387 ? 3.673   -13.823 52.612   1.00 195.44 ? 387  PRO A C   1 
ATOM   2953  O  O   . PRO A  1 387 ? 3.225   -13.395 53.678   1.00 198.80 ? 387  PRO A O   1 
ATOM   2954  C  CB  . PRO A  1 387 ? 2.277   -12.892 50.735   1.00 182.49 ? 387  PRO A CB  1 
ATOM   2955  C  CG  . PRO A  1 387 ? 0.987   -12.567 51.405   1.00 174.92 ? 387  PRO A CG  1 
ATOM   2956  C  CD  . PRO A  1 387 ? 0.356   -13.892 51.751   1.00 173.90 ? 387  PRO A CD  1 
ATOM   2957  N  N   . SER A  1 388 ? 4.974   -13.984 52.386   1.00 204.53 ? 388  SER A N   1 
ATOM   2958  C  CA  . SER A  1 388 ? 5.973   -13.678 53.394   1.00 193.29 ? 388  SER A CA  1 
ATOM   2959  C  C   . SER A  1 388 ? 6.552   -12.283 53.239   1.00 208.51 ? 388  SER A C   1 
ATOM   2960  O  O   . SER A  1 388 ? 7.295   -11.834 54.119   1.00 214.90 ? 388  SER A O   1 
ATOM   2961  C  CB  . SER A  1 388 ? 7.106   -14.709 53.340   1.00 195.46 ? 388  SER A CB  1 
ATOM   2962  O  OG  . SER A  1 388 ? 7.730   -14.702 52.067   1.00 194.06 ? 388  SER A OG  1 
ATOM   2963  N  N   . GLN A  1 389 ? 6.228   -11.590 52.151   1.00 205.58 ? 389  GLN A N   1 
ATOM   2964  C  CA  . GLN A  1 389 ? 6.708   -10.234 51.935   1.00 206.85 ? 389  GLN A CA  1 
ATOM   2965  C  C   . GLN A  1 389 ? 5.774   -9.515  50.972   1.00 208.56 ? 389  GLN A C   1 
ATOM   2966  O  O   . GLN A  1 389 ? 5.255   -10.119 50.028   1.00 193.53 ? 389  GLN A O   1 
ATOM   2967  C  CB  . GLN A  1 389 ? 8.135   -10.224 51.388   1.00 187.73 ? 389  GLN A CB  1 
ATOM   2968  C  CG  . GLN A  1 389 ? 8.781   -8.854  51.419   1.00 190.69 ? 389  GLN A CG  1 
ATOM   2969  C  CD  . GLN A  1 389 ? 10.254  -8.916  51.119   1.00 193.91 ? 389  GLN A CD  1 
ATOM   2970  O  OE1 . GLN A  1 389 ? 10.765  -9.951  50.696   1.00 211.23 ? 389  GLN A OE1 1 
ATOM   2971  N  NE2 . GLN A  1 389 ? 10.949  -7.803  51.325   1.00 197.45 ? 389  GLN A NE2 1 
ATOM   2972  N  N   . ILE A  1 390 ? 5.577   -8.222  51.214   1.00 220.54 ? 390  ILE A N   1 
ATOM   2973  C  CA  . ILE A  1 390 ? 4.707   -7.384  50.397   1.00 218.63 ? 390  ILE A CA  1 
ATOM   2974  C  C   . ILE A  1 390 ? 5.547   -6.266  49.797   1.00 213.45 ? 390  ILE A C   1 
ATOM   2975  O  O   . ILE A  1 390 ? 6.116   -5.445  50.529   1.00 217.23 ? 390  ILE A O   1 
ATOM   2976  C  CB  . ILE A  1 390 ? 3.535   -6.812  51.208   1.00 218.52 ? 390  ILE A CB  1 
ATOM   2977  C  CG1 . ILE A  1 390 ? 2.691   -7.936  51.821   1.00 228.91 ? 390  ILE A CG1 1 
ATOM   2978  C  CG2 . ILE A  1 390 ? 2.677   -5.922  50.327   1.00 208.82 ? 390  ILE A CG2 1 
ATOM   2979  C  CD1 . ILE A  1 390 ? 3.154   -8.384  53.206   1.00 225.50 ? 390  ILE A CD1 1 
ATOM   2980  N  N   . LEU A  1 391 ? 5.625   -6.235  48.470   1.00 209.80 ? 391  LEU A N   1 
ATOM   2981  C  CA  . LEU A  1 391 ? 6.337   -5.185  47.755   1.00 202.82 ? 391  LEU A CA  1 
ATOM   2982  C  C   . LEU A  1 391 ? 5.350   -4.081  47.397   1.00 193.35 ? 391  LEU A C   1 
ATOM   2983  O  O   . LEU A  1 391 ? 4.372   -4.326  46.685   1.00 179.92 ? 391  LEU A O   1 
ATOM   2984  C  CB  . LEU A  1 391 ? 6.998   -5.747  46.498   1.00 183.21 ? 391  LEU A CB  1 
ATOM   2985  C  CG  . LEU A  1 391 ? 8.416   -6.309  46.619   1.00 186.19 ? 391  LEU A CG  1 
ATOM   2986  C  CD1 . LEU A  1 391 ? 8.521   -7.339  47.733   1.00 195.40 ? 391  LEU A CD1 1 
ATOM   2987  C  CD2 . LEU A  1 391 ? 8.830   -6.924  45.299   1.00 184.22 ? 391  LEU A CD2 1 
ATOM   2988  N  N   . GLU A  1 392 ? 5.608   -2.869  47.878   1.00 204.73 ? 392  GLU A N   1 
ATOM   2989  C  CA  . GLU A  1 392 ? 4.698   -1.750  47.684   1.00 203.01 ? 392  GLU A CA  1 
ATOM   2990  C  C   . GLU A  1 392 ? 5.232   -0.802  46.618   1.00 202.72 ? 392  GLU A C   1 
ATOM   2991  O  O   . GLU A  1 392 ? 6.434   -0.521  46.565   1.00 213.48 ? 392  GLU A O   1 
ATOM   2992  C  CB  . GLU A  1 392 ? 4.482   -0.989  48.996   1.00 212.91 ? 392  GLU A CB  1 
ATOM   2993  C  CG  . GLU A  1 392 ? 3.708   -1.765  50.052   1.00 225.63 ? 392  GLU A CG  1 
ATOM   2994  C  CD  . GLU A  1 392 ? 2.260   -1.312  50.165   1.00 244.11 ? 392  GLU A CD  1 
ATOM   2995  O  OE1 . GLU A  1 392 ? 1.846   -0.428  49.384   1.00 243.60 ? 392  GLU A OE1 1 
ATOM   2996  O  OE2 . GLU A  1 392 ? 1.532   -1.848  51.029   1.00 259.16 ? 392  GLU A OE2 1 
ATOM   2997  N  N   . GLY A  1 393 ? 4.326   -0.316  45.770   1.00 194.16 ? 393  GLY A N   1 
ATOM   2998  C  CA  . GLY A  1 393 ? 4.674   0.720   44.807   1.00 194.79 ? 393  GLY A CA  1 
ATOM   2999  C  C   . GLY A  1 393 ? 4.765   2.085   45.474   1.00 213.15 ? 393  GLY A C   1 
ATOM   3000  O  O   . GLY A  1 393 ? 3.991   2.421   46.370   1.00 238.35 ? 393  GLY A O   1 
ATOM   3001  N  N   . GLN A  1 394 ? 5.728   2.880   45.014   1.00 196.20 ? 394  GLN A N   1 
ATOM   3002  C  CA  . GLN A  1 394 ? 6.005   4.187   45.587   1.00 199.19 ? 394  GLN A CA  1 
ATOM   3003  C  C   . GLN A  1 394 ? 5.627   5.339   44.670   1.00 205.69 ? 394  GLN A C   1 
ATOM   3004  O  O   . GLN A  1 394 ? 5.694   6.495   45.099   1.00 218.20 ? 394  GLN A O   1 
ATOM   3005  C  CB  . GLN A  1 394 ? 7.498   4.299   45.939   1.00 198.90 ? 394  GLN A CB  1 
ATOM   3006  C  CG  . GLN A  1 394 ? 8.045   3.168   46.802   1.00 198.12 ? 394  GLN A CG  1 
ATOM   3007  C  CD  . GLN A  1 394 ? 7.472   3.141   48.205   1.00 199.71 ? 394  GLN A CD  1 
ATOM   3008  O  OE1 . GLN A  1 394 ? 6.917   4.128   48.686   1.00 205.30 ? 394  GLN A OE1 1 
ATOM   3009  N  NE2 . GLN A  1 394 ? 7.613   2.003   48.875   1.00 198.79 ? 394  GLN A NE2 1 
ATOM   3010  N  N   . TRP A  1 395 ? 5.256   5.061   43.425   1.00 204.45 ? 395  TRP A N   1 
ATOM   3011  C  CA  . TRP A  1 395 ? 5.122   6.079   42.389   1.00 208.81 ? 395  TRP A CA  1 
ATOM   3012  C  C   . TRP A  1 395 ? 3.651   6.314   42.067   1.00 211.81 ? 395  TRP A C   1 
ATOM   3013  O  O   . TRP A  1 395 ? 2.953   5.396   41.623   1.00 216.63 ? 395  TRP A O   1 
ATOM   3014  C  CB  . TRP A  1 395 ? 5.908   5.667   41.146   1.00 197.66 ? 395  TRP A CB  1 
ATOM   3015  C  CG  . TRP A  1 395 ? 7.338   5.342   41.470   1.00 216.31 ? 395  TRP A CG  1 
ATOM   3016  C  CD1 . TRP A  1 395 ? 8.416   6.175   41.366   1.00 230.94 ? 395  TRP A CD1 1 
ATOM   3017  C  CD2 . TRP A  1 395 ? 7.839   4.104   41.992   1.00 217.81 ? 395  TRP A CD2 1 
ATOM   3018  N  NE1 . TRP A  1 395 ? 9.559   5.526   41.771   1.00 234.16 ? 395  TRP A NE1 1 
ATOM   3019  C  CE2 . TRP A  1 395 ? 9.230   4.255   42.161   1.00 222.38 ? 395  TRP A CE2 1 
ATOM   3020  C  CE3 . TRP A  1 395 ? 7.247   2.881   42.321   1.00 216.07 ? 395  TRP A CE3 1 
ATOM   3021  C  CZ2 . TRP A  1 395 ? 10.036  3.230   42.647   1.00 212.21 ? 395  TRP A CZ2 1 
ATOM   3022  C  CZ3 . TRP A  1 395 ? 8.050   1.866   42.807   1.00 215.03 ? 395  TRP A CZ3 1 
ATOM   3023  C  CH2 . TRP A  1 395 ? 9.427   2.047   42.966   1.00 212.63 ? 395  TRP A CH2 1 
ATOM   3024  N  N   . ALA A  1 396 ? 3.189   7.540   42.305   1.00 217.97 ? 396  ALA A N   1 
ATOM   3025  C  CA  . ALA A  1 396 ? 1.813   7.926   42.031   1.00 223.94 ? 396  ALA A CA  1 
ATOM   3026  C  C   . ALA A  1 396 ? 1.546   8.007   40.527   1.00 231.40 ? 396  ALA A C   1 
ATOM   3027  O  O   . ALA A  1 396 ? 2.461   8.063   39.699   1.00 225.82 ? 396  ALA A O   1 
ATOM   3028  C  CB  . ALA A  1 396 ? 1.488   9.265   42.698   1.00 217.61 ? 396  ALA A CB  1 
ATOM   3029  N  N   . ALA A  1 397 ? 0.259   8.017   40.186   1.00 220.02 ? 397  ALA A N   1 
ATOM   3030  C  CA  . ALA A  1 397 ? -0.191  8.017   38.800   1.00 194.61 ? 397  ALA A CA  1 
ATOM   3031  C  C   . ALA A  1 397 ? -0.320  9.464   38.344   1.00 204.88 ? 397  ALA A C   1 
ATOM   3032  O  O   . ALA A  1 397 ? -1.221  10.185  38.783   1.00 207.81 ? 397  ALA A O   1 
ATOM   3033  C  CB  . ALA A  1 397 ? -1.518  7.274   38.661   1.00 179.38 ? 397  ALA A CB  1 
ATOM   3034  N  N   . ARG A  1 398 ? 0.581   9.883   37.461   1.00 197.74 ? 398  ARG A N   1 
ATOM   3035  C  CA  . ARG A  1 398 ? 0.511   11.189  36.821   1.00 201.98 ? 398  ARG A CA  1 
ATOM   3036  C  C   . ARG A  1 398 ? -0.787  11.392  36.046   1.00 206.65 ? 398  ARG A C   1 
ATOM   3037  O  O   . ARG A  1 398 ? -1.646  12.170  36.470   1.00 220.75 ? 398  ARG A O   1 
ATOM   3038  C  CB  . ARG A  1 398 ? 1.714   11.358  35.895   1.00 205.98 ? 398  ARG A CB  1 
ATOM   3039  C  CG  . ARG A  1 398 ? 2.048   10.087  35.122   1.00 204.43 ? 398  ARG A CG  1 
ATOM   3040  C  CD  . ARG A  1 398 ? 3.282   10.240  34.272   1.00 204.24 ? 398  ARG A CD  1 
ATOM   3041  N  NE  . ARG A  1 398 ? 4.492   10.209  35.080   1.00 211.94 ? 398  ARG A NE  1 
ATOM   3042  C  CZ  . ARG A  1 398 ? 5.719   10.196  34.576   1.00 199.67 ? 398  ARG A CZ  1 
ATOM   3043  N  NH1 . ARG A  1 398 ? 5.895   10.210  33.262   1.00 195.84 ? 398  ARG A NH1 1 
ATOM   3044  N  NH2 . ARG A  1 398 ? 6.769   10.166  35.385   1.00 197.66 ? 398  ARG A NH2 1 
ATOM   3045  N  N   . SER A  1 399 ? -0.941  10.697  34.919   1.00 210.40 ? 399  SER A N   1 
ATOM   3046  C  CA  . SER A  1 399 ? -2.099  10.838  34.047   1.00 213.27 ? 399  SER A CA  1 
ATOM   3047  C  C   . SER A  1 399 ? -2.020  9.787   32.952   1.00 195.18 ? 399  SER A C   1 
ATOM   3048  O  O   . SER A  1 399 ? -0.964  9.624   32.332   1.00 197.16 ? 399  SER A O   1 
ATOM   3049  C  CB  . SER A  1 399 ? -2.145  12.240  33.436   1.00 227.47 ? 399  SER A CB  1 
ATOM   3050  O  OG  . SER A  1 399 ? -0.891  12.567  32.861   1.00 228.59 ? 399  SER A OG  1 
ATOM   3051  N  N   . GLY A  1 400 ? -3.106  9.052   32.724   1.00 193.42 ? 400  GLY A N   1 
ATOM   3052  C  CA  . GLY A  1 400 ? -3.121  8.096   31.638   1.00 184.86 ? 400  GLY A CA  1 
ATOM   3053  C  C   . GLY A  1 400 ? -3.219  6.709   32.225   1.00 181.12 ? 400  GLY A C   1 
ATOM   3054  O  O   . GLY A  1 400 ? -4.193  6.378   32.910   1.00 180.50 ? 400  GLY A O   1 
ATOM   3055  N  N   . CYS A  1 401 ? -2.209  5.878   31.940   1.00 188.02 ? 401  CYS A N   1 
ATOM   3056  C  CA  . CYS A  1 401 ? -2.158  4.554   32.531   1.00 187.15 ? 401  CYS A CA  1 
ATOM   3057  C  C   . CYS A  1 401 ? -1.767  4.654   34.002   1.00 197.78 ? 401  CYS A C   1 
ATOM   3058  O  O   . CYS A  1 401 ? -0.985  5.528   34.388   1.00 202.39 ? 401  CYS A O   1 
ATOM   3059  C  CB  . CYS A  1 401 ? -1.143  3.674   31.813   1.00 163.72 ? 401  CYS A CB  1 
ATOM   3060  S  SG  . CYS A  1 401 ? -1.751  2.696   30.435   1.00 160.06 ? 401  CYS A SG  1 
ATOM   3061  N  N   . PRO A  1 402 ? -2.299  3.768   34.837   1.00 190.39 ? 402  PRO A N   1 
ATOM   3062  C  CA  . PRO A  1 402 ? -1.840  3.678   36.218   1.00 181.47 ? 402  PRO A CA  1 
ATOM   3063  C  C   . PRO A  1 402 ? -0.390  3.236   36.266   1.00 167.05 ? 402  PRO A C   1 
ATOM   3064  O  O   . PRO A  1 402 ? 0.160   2.782   35.249   1.00 165.78 ? 402  PRO A O   1 
ATOM   3065  C  CB  . PRO A  1 402 ? -2.777  2.627   36.837   1.00 163.39 ? 402  PRO A CB  1 
ATOM   3066  C  CG  . PRO A  1 402 ? -3.254  1.830   35.705   1.00 195.65 ? 402  PRO A CG  1 
ATOM   3067  C  CD  . PRO A  1 402 ? -3.356  2.787   34.547   1.00 194.89 ? 402  PRO A CD  1 
ATOM   3068  N  N   . PRO A  1 403 ? 0.277   3.395   37.409   1.00 169.55 ? 403  PRO A N   1 
ATOM   3069  C  CA  . PRO A  1 403 ? 1.700   3.035   37.476   1.00 170.88 ? 403  PRO A CA  1 
ATOM   3070  C  C   . PRO A  1 403 ? 1.982   1.617   37.025   1.00 177.83 ? 403  PRO A C   1 
ATOM   3071  O  O   . PRO A  1 403 ? 3.039   1.365   36.431   1.00 195.82 ? 403  PRO A O   1 
ATOM   3072  C  CB  . PRO A  1 403 ? 2.040   3.243   38.958   1.00 182.02 ? 403  PRO A CB  1 
ATOM   3073  C  CG  . PRO A  1 403 ? 1.009   4.193   39.455   1.00 175.09 ? 403  PRO A CG  1 
ATOM   3074  C  CD  . PRO A  1 403 ? -0.233  3.869   38.706   1.00 171.58 ? 403  PRO A CD  1 
ATOM   3075  N  N   . SER A  1 404 ? 1.069   0.678   37.283   1.00 164.45 ? 404  SER A N   1 
ATOM   3076  C  CA  . SER A  1 404 ? 1.201   -0.700  36.807   1.00 161.45 ? 404  SER A CA  1 
ATOM   3077  C  C   . SER A  1 404 ? 2.467   -1.367  37.344   1.00 162.88 ? 404  SER A C   1 
ATOM   3078  O  O   . SER A  1 404 ? 3.118   -2.148  36.646   1.00 162.06 ? 404  SER A O   1 
ATOM   3079  C  CB  . SER A  1 404 ? 1.179   -0.751  35.278   1.00 159.97 ? 404  SER A CB  1 
ATOM   3080  O  OG  . SER A  1 404 ? 0.053   -0.073  34.743   1.00 159.11 ? 404  SER A OG  1 
ATOM   3081  N  N   . PHE A  1 405 ? 2.830   -1.042  38.586   1.00 165.44 ? 405  PHE A N   1 
ATOM   3082  C  CA  . PHE A  1 405 ? 3.968   -1.678  39.244   1.00 167.19 ? 405  PHE A CA  1 
ATOM   3083  C  C   . PHE A  1 405 ? 3.715   -3.172  39.389   1.00 195.85 ? 405  PHE A C   1 
ATOM   3084  O  O   . PHE A  1 405 ? 2.758   -3.582  40.048   1.00 183.35 ? 405  PHE A O   1 
ATOM   3085  C  CB  . PHE A  1 405 ? 4.206   -1.032  40.612   1.00 170.54 ? 405  PHE A CB  1 
ATOM   3086  C  CG  . PHE A  1 405 ? 5.302   -1.683  41.423   1.00 190.81 ? 405  PHE A CG  1 
ATOM   3087  C  CD1 . PHE A  1 405 ? 6.626   -1.303  41.265   1.00 206.89 ? 405  PHE A CD1 1 
ATOM   3088  C  CD2 . PHE A  1 405 ? 5.002   -2.661  42.360   1.00 184.59 ? 405  PHE A CD2 1 
ATOM   3089  C  CE1 . PHE A  1 405 ? 7.631   -1.897  42.019   1.00 200.00 ? 405  PHE A CE1 1 
ATOM   3090  C  CE2 . PHE A  1 405 ? 6.000   -3.258  43.113   1.00 181.19 ? 405  PHE A CE2 1 
ATOM   3091  C  CZ  . PHE A  1 405 ? 7.314   -2.874  42.943   1.00 177.38 ? 405  PHE A CZ  1 
ATOM   3092  N  N   . GLY A  1 406 ? 4.561   -3.988  38.755   1.00 203.16 ? 406  GLY A N   1 
ATOM   3093  C  CA  . GLY A  1 406 ? 4.410   -5.428  38.797   1.00 188.47 ? 406  GLY A CA  1 
ATOM   3094  C  C   . GLY A  1 406 ? 3.845   -6.050  37.537   1.00 168.55 ? 406  GLY A C   1 
ATOM   3095  O  O   . GLY A  1 406 ? 3.762   -7.282  37.464   1.00 159.67 ? 406  GLY A O   1 
ATOM   3096  N  N   . TYR A  1 407 ? 3.428   -5.238  36.561   1.00 158.04 ? 407  TYR A N   1 
ATOM   3097  C  CA  . TYR A  1 407 ? 2.767   -5.770  35.375   1.00 155.19 ? 407  TYR A CA  1 
ATOM   3098  C  C   . TYR A  1 407 ? 3.615   -6.806  34.647   1.00 155.24 ? 407  TYR A C   1 
ATOM   3099  O  O   . TYR A  1 407 ? 3.067   -7.738  34.048   1.00 157.84 ? 407  TYR A O   1 
ATOM   3100  C  CB  . TYR A  1 407 ? 2.412   -4.639  34.422   1.00 155.31 ? 407  TYR A CB  1 
ATOM   3101  C  CG  . TYR A  1 407 ? 1.668   -5.133  33.209   1.00 162.22 ? 407  TYR A CG  1 
ATOM   3102  C  CD1 . TYR A  1 407 ? 0.297   -5.358  33.258   1.00 153.63 ? 407  TYR A CD1 1 
ATOM   3103  C  CD2 . TYR A  1 407 ? 2.335   -5.390  32.019   1.00 153.04 ? 407  TYR A CD2 1 
ATOM   3104  C  CE1 . TYR A  1 407 ? -0.392  -5.817  32.153   1.00 147.91 ? 407  TYR A CE1 1 
ATOM   3105  C  CE2 . TYR A  1 407 ? 1.652   -5.851  30.908   1.00 163.17 ? 407  TYR A CE2 1 
ATOM   3106  C  CZ  . TYR A  1 407 ? 0.289   -6.060  30.981   1.00 148.33 ? 407  TYR A CZ  1 
ATOM   3107  O  OH  . TYR A  1 407 ? -0.390  -6.515  29.878   1.00 146.52 ? 407  TYR A OH  1 
ATOM   3108  N  N   . SER A  1 408 ? 4.941   -6.666  34.682   1.00 168.01 ? 408  SER A N   1 
ATOM   3109  C  CA  . SER A  1 408 ? 5.861   -7.668  34.155   1.00 159.11 ? 408  SER A CA  1 
ATOM   3110  C  C   . SER A  1 408 ? 7.007   -7.839  35.138   1.00 162.29 ? 408  SER A C   1 
ATOM   3111  O  O   . SER A  1 408 ? 7.430   -6.869  35.773   1.00 164.65 ? 408  SER A O   1 
ATOM   3112  C  CB  . SER A  1 408 ? 6.426   -7.276  32.786   1.00 160.22 ? 408  SER A CB  1 
ATOM   3113  O  OG  . SER A  1 408 ? 7.146   -6.059  32.869   1.00 163.20 ? 408  SER A OG  1 
ATOM   3114  N  N   . MET A  1 409 ? 7.506   -9.067  35.263   1.00 162.70 ? 409  MET A N   1 
ATOM   3115  C  CA  . MET A  1 409 ? 8.636   -9.323  36.146   1.00 166.09 ? 409  MET A CA  1 
ATOM   3116  C  C   . MET A  1 409 ? 9.296   -10.642 35.765   1.00 195.25 ? 409  MET A C   1 
ATOM   3117  O  O   . MET A  1 409 ? 8.697   -11.487 35.094   1.00 192.18 ? 409  MET A O   1 
ATOM   3118  C  CB  . MET A  1 409 ? 8.213   -9.337  37.619   1.00 166.03 ? 409  MET A CB  1 
ATOM   3119  C  CG  . MET A  1 409 ? 6.950   -10.112 37.912   1.00 162.50 ? 409  MET A CG  1 
ATOM   3120  S  SD  . MET A  1 409 ? 6.438   -9.838  39.613   1.00 163.02 ? 409  MET A SD  1 
ATOM   3121  C  CE  . MET A  1 409 ? 5.199   -11.113 39.804   1.00 159.51 ? 409  MET A CE  1 
ATOM   3122  N  N   . LYS A  1 410 ? 10.552  -10.795 36.197   1.00 196.54 ? 410  LYS A N   1 
ATOM   3123  C  CA  . LYS A  1 410 ? 11.339  -11.998 35.952   1.00 183.02 ? 410  LYS A CA  1 
ATOM   3124  C  C   . LYS A  1 410 ? 12.297  -12.229 37.118   1.00 176.44 ? 410  LYS A C   1 
ATOM   3125  O  O   . LYS A  1 410 ? 12.899  -11.282 37.628   1.00 179.05 ? 410  LYS A O   1 
ATOM   3126  C  CB  . LYS A  1 410 ? 12.122  -11.884 34.639   1.00 174.60 ? 410  LYS A CB  1 
ATOM   3127  C  CG  . LYS A  1 410 ? 12.744  -13.183 34.193   1.00 176.31 ? 410  LYS A CG  1 
ATOM   3128  C  CD  . LYS A  1 410 ? 11.682  -14.144 33.682   1.00 172.65 ? 410  LYS A CD  1 
ATOM   3129  C  CE  . LYS A  1 410 ? 12.100  -15.593 33.892   1.00 190.17 ? 410  LYS A CE  1 
ATOM   3130  N  NZ  . LYS A  1 410 ? 13.482  -15.880 33.401   1.00 217.13 ? 410  LYS A NZ  1 
ATOM   3131  N  N   . GLY A  1 411 ? 12.444  -13.489 37.530   1.00 177.02 ? 411  GLY A N   1 
ATOM   3132  C  CA  . GLY A  1 411 ? 13.344  -13.810 38.620   1.00 180.83 ? 411  GLY A CA  1 
ATOM   3133  C  C   . GLY A  1 411 ? 14.287  -14.964 38.339   1.00 183.95 ? 411  GLY A C   1 
ATOM   3134  O  O   . GLY A  1 411 ? 14.548  -15.293 37.177   1.00 184.17 ? 411  GLY A O   1 
ATOM   3135  N  N   . ALA A  1 412 ? 14.794  -15.580 39.412   1.00 186.72 ? 412  ALA A N   1 
ATOM   3136  C  CA  . ALA A  1 412 ? 15.643  -16.774 39.366   1.00 193.64 ? 412  ALA A CA  1 
ATOM   3137  C  C   . ALA A  1 412 ? 17.036  -16.505 38.793   1.00 208.69 ? 412  ALA A C   1 
ATOM   3138  O  O   . ALA A  1 412 ? 17.664  -17.410 38.235   1.00 213.17 ? 412  ALA A O   1 
ATOM   3139  C  CB  . ALA A  1 412 ? 14.968  -17.913 38.592   1.00 189.29 ? 412  ALA A CB  1 
ATOM   3140  N  N   . THR A  1 413 ? 17.532  -15.274 38.916   1.00 196.66 ? 413  THR A N   1 
ATOM   3141  C  CA  . THR A  1 413 ? 18.882  -14.923 38.489   1.00 201.76 ? 413  THR A CA  1 
ATOM   3142  C  C   . THR A  1 413 ? 19.561  -14.110 39.584   1.00 205.30 ? 413  THR A C   1 
ATOM   3143  O  O   . THR A  1 413 ? 19.031  -13.080 40.011   1.00 215.80 ? 413  THR A O   1 
ATOM   3144  C  CB  . THR A  1 413 ? 18.856  -14.145 37.171   1.00 200.67 ? 413  THR A CB  1 
ATOM   3145  O  OG1 . THR A  1 413 ? 18.335  -14.983 36.130   1.00 198.15 ? 413  THR A OG1 1 
ATOM   3146  C  CG2 . THR A  1 413 ? 20.253  -13.687 36.797   1.00 208.26 ? 413  THR A CG2 1 
ATOM   3147  N  N   . ASP A  1 414 ? 20.737  -14.564 40.029   1.00 210.78 ? 414  ASP A N   1 
ATOM   3148  C  CA  . ASP A  1 414 ? 21.492  -13.883 41.086   1.00 214.98 ? 414  ASP A CA  1 
ATOM   3149  C  C   . ASP A  1 414 ? 22.427  -12.876 40.427   1.00 218.52 ? 414  ASP A C   1 
ATOM   3150  O  O   . ASP A  1 414 ? 23.551  -13.197 40.035   1.00 223.38 ? 414  ASP A O   1 
ATOM   3151  C  CB  . ASP A  1 414 ? 22.258  -14.885 41.939   1.00 219.43 ? 414  ASP A CB  1 
ATOM   3152  C  CG  . ASP A  1 414 ? 22.925  -14.239 43.142   1.00 223.70 ? 414  ASP A CG  1 
ATOM   3153  O  OD1 . ASP A  1 414 ? 22.493  -13.141 43.567   1.00 222.19 ? 414  ASP A OD1 1 
ATOM   3154  O  OD2 . ASP A  1 414 ? 23.888  -14.838 43.663   1.00 228.92 ? 414  ASP A OD2 1 
ATOM   3155  N  N   . ILE A  1 415 ? 21.955  -11.631 40.315   1.00 216.40 ? 415  ILE A N   1 
ATOM   3156  C  CA  . ILE A  1 415 ? 22.649  -10.628 39.510   1.00 226.90 ? 415  ILE A CA  1 
ATOM   3157  C  C   . ILE A  1 415 ? 23.865  -10.038 40.219   1.00 225.44 ? 415  ILE A C   1 
ATOM   3158  O  O   . ILE A  1 415 ? 24.742  -9.469  39.556   1.00 229.20 ? 415  ILE A O   1 
ATOM   3159  C  CB  . ILE A  1 415 ? 21.661  -9.519  39.097   1.00 214.64 ? 415  ILE A CB  1 
ATOM   3160  C  CG1 . ILE A  1 415 ? 22.140  -8.787  37.839   1.00 216.12 ? 415  ILE A CG1 1 
ATOM   3161  C  CG2 . ILE A  1 415 ? 21.440  -8.533  40.231   1.00 215.20 ? 415  ILE A CG2 1 
ATOM   3162  C  CD1 . ILE A  1 415 ? 21.180  -7.740  37.332   1.00 212.13 ? 415  ILE A CD1 1 
ATOM   3163  N  N   . ASP A  1 416 ? 23.971  -10.188 41.539   1.00 227.20 ? 416  ASP A N   1 
ATOM   3164  C  CA  . ASP A  1 416 ? 25.069  -9.604  42.297   1.00 233.46 ? 416  ASP A CA  1 
ATOM   3165  C  C   . ASP A  1 416 ? 25.990  -10.652 42.909   1.00 238.31 ? 416  ASP A C   1 
ATOM   3166  O  O   . ASP A  1 416 ? 26.821  -10.306 43.756   1.00 243.58 ? 416  ASP A O   1 
ATOM   3167  C  CB  . ASP A  1 416 ? 24.526  -8.673  43.383   1.00 232.63 ? 416  ASP A CB  1 
ATOM   3168  C  CG  . ASP A  1 416 ? 23.709  -9.404  44.437   1.00 229.85 ? 416  ASP A CG  1 
ATOM   3169  O  OD1 . ASP A  1 416 ? 23.155  -10.488 44.147   1.00 226.46 ? 416  ASP A OD1 1 
ATOM   3170  O  OD2 . ASP A  1 416 ? 23.609  -8.877  45.567   1.00 231.32 ? 416  ASP A OD2 1 
ATOM   3171  N  N   . LYS A  1 417 ? 25.865  -11.917 42.501   1.00 236.99 ? 417  LYS A N   1 
ATOM   3172  C  CA  . LYS A  1 417 ? 26.750  -12.990 42.965   1.00 241.93 ? 417  LYS A CA  1 
ATOM   3173  C  C   . LYS A  1 417 ? 26.776  -13.065 44.488   1.00 243.91 ? 417  LYS A C   1 
ATOM   3174  O  O   . LYS A  1 417 ? 27.799  -13.362 45.108   1.00 250.00 ? 417  LYS A O   1 
ATOM   3175  C  CB  . LYS A  1 417 ? 28.157  -12.822 42.397   1.00 248.58 ? 417  LYS A CB  1 
ATOM   3176  C  CG  . LYS A  1 417 ? 28.200  -12.854 40.879   1.00 249.01 ? 417  LYS A CG  1 
ATOM   3177  C  CD  . LYS A  1 417 ? 27.920  -14.250 40.342   1.00 245.64 ? 417  LYS A CD  1 
ATOM   3178  C  CE  . LYS A  1 417 ? 28.971  -15.240 40.817   1.00 252.01 ? 417  LYS A CE  1 
ATOM   3179  N  NZ  . LYS A  1 417 ? 28.727  -16.612 40.294   1.00 250.95 ? 417  LYS A NZ  1 
ATOM   3180  N  N   . ASN A  1 418 ? 25.625  -12.799 45.090   1.00 248.60 ? 418  ASN A N   1 
ATOM   3181  C  CA  . ASN A  1 418 ? 25.430  -12.779 46.531   1.00 248.40 ? 418  ASN A CA  1 
ATOM   3182  C  C   . ASN A  1 418 ? 24.973  -14.120 47.084   1.00 238.76 ? 418  ASN A C   1 
ATOM   3183  O  O   . ASN A  1 418 ? 24.805  -14.253 48.301   1.00 239.95 ? 418  ASN A O   1 
ATOM   3184  C  CB  . ASN A  1 418 ? 24.393  -11.710 46.865   1.00 249.43 ? 418  ASN A CB  1 
ATOM   3185  C  CG  . ASN A  1 418 ? 22.971  -12.193 46.617   1.00 228.75 ? 418  ASN A CG  1 
ATOM   3186  O  OD1 . ASN A  1 418 ? 22.737  -13.012 45.726   1.00 226.22 ? 418  ASN A OD1 1 
ATOM   3187  N  ND2 . ASN A  1 418 ? 22.009  -11.625 47.335   1.00 225.76 ? 418  ASN A ND2 1 
ATOM   3188  N  N   . GLY A  1 419 ? 24.759  -15.111 46.222   1.00 236.56 ? 419  GLY A N   1 
ATOM   3189  C  CA  . GLY A  1 419 ? 24.303  -16.412 46.647   1.00 235.37 ? 419  GLY A CA  1 
ATOM   3190  C  C   . GLY A  1 419 ? 22.804  -16.561 46.620   1.00 228.33 ? 419  GLY A C   1 
ATOM   3191  O  O   . GLY A  1 419 ? 22.302  -17.660 46.882   1.00 226.88 ? 419  GLY A O   1 
ATOM   3192  N  N   . TYR A  1 420 ? 22.074  -15.486 46.314   1.00 224.54 ? 420  TYR A N   1 
ATOM   3193  C  CA  . TYR A  1 420 ? 20.624  -15.485 46.307   1.00 231.54 ? 420  TYR A CA  1 
ATOM   3194  C  C   . TYR A  1 420 ? 20.085  -14.884 45.016   1.00 221.26 ? 420  TYR A C   1 
ATOM   3195  O  O   . TYR A  1 420 ? 20.561  -13.831 44.567   1.00 232.36 ? 420  TYR A O   1 
ATOM   3196  C  CB  . TYR A  1 420 ? 20.073  -14.689 47.496   1.00 235.65 ? 420  TYR A CB  1 
ATOM   3197  C  CG  . TYR A  1 420 ? 20.480  -15.227 48.844   1.00 242.07 ? 420  TYR A CG  1 
ATOM   3198  C  CD1 . TYR A  1 420 ? 21.717  -14.915 49.397   1.00 232.98 ? 420  TYR A CD1 1 
ATOM   3199  C  CD2 . TYR A  1 420 ? 19.622  -16.042 49.568   1.00 228.51 ? 420  TYR A CD2 1 
ATOM   3200  C  CE1 . TYR A  1 420 ? 22.089  -15.404 50.631   1.00 231.75 ? 420  TYR A CE1 1 
ATOM   3201  C  CE2 . TYR A  1 420 ? 19.984  -16.535 50.802   1.00 223.91 ? 420  TYR A CE2 1 
ATOM   3202  C  CZ  . TYR A  1 420 ? 21.216  -16.211 51.330   1.00 229.42 ? 420  TYR A CZ  1 
ATOM   3203  O  OH  . TYR A  1 420 ? 21.571  -16.707 52.562   1.00 233.64 ? 420  TYR A OH  1 
ATOM   3204  N  N   . PRO A  1 421 ? 19.073  -15.509 44.416   1.00 208.66 ? 421  PRO A N   1 
ATOM   3205  C  CA  . PRO A  1 421 ? 18.483  -14.948 43.195   1.00 220.10 ? 421  PRO A CA  1 
ATOM   3206  C  C   . PRO A  1 421 ? 17.686  -13.686 43.499   1.00 223.50 ? 421  PRO A C   1 
ATOM   3207  O  O   . PRO A  1 421 ? 17.051  -13.566 44.548   1.00 221.46 ? 421  PRO A O   1 
ATOM   3208  C  CB  . PRO A  1 421 ? 17.579  -16.079 42.687   1.00 221.87 ? 421  PRO A CB  1 
ATOM   3209  C  CG  . PRO A  1 421 ? 17.234  -16.856 43.918   1.00 221.25 ? 421  PRO A CG  1 
ATOM   3210  C  CD  . PRO A  1 421 ? 18.464  -16.799 44.786   1.00 206.99 ? 421  PRO A CD  1 
ATOM   3211  N  N   . ASP A  1 422 ? 17.742  -12.729 42.576   1.00 219.62 ? 422  ASP A N   1 
ATOM   3212  C  CA  . ASP A  1 422 ? 17.126  -11.420 42.746   1.00 199.11 ? 422  ASP A CA  1 
ATOM   3213  C  C   . ASP A  1 422 ? 15.947  -11.274 41.784   1.00 193.61 ? 422  ASP A C   1 
ATOM   3214  O  O   . ASP A  1 422 ? 15.627  -12.187 41.016   1.00 191.32 ? 422  ASP A O   1 
ATOM   3215  C  CB  . ASP A  1 422 ? 18.177  -10.323 42.565   1.00 203.39 ? 422  ASP A CB  1 
ATOM   3216  C  CG  . ASP A  1 422 ? 19.427  -10.574 43.408   1.00 209.35 ? 422  ASP A CG  1 
ATOM   3217  O  OD1 . ASP A  1 422 ? 20.296  -11.359 42.973   1.00 212.13 ? 422  ASP A OD1 1 
ATOM   3218  O  OD2 . ASP A  1 422 ? 19.534  -10.001 44.513   1.00 211.55 ? 422  ASP A OD2 1 
ATOM   3219  N  N   . LEU A  1 423 ? 15.295  -10.109 41.831   1.00 198.40 ? 423  LEU A N   1 
ATOM   3220  C  CA  . LEU A  1 423 ? 14.014  -9.909  41.159   1.00 206.42 ? 423  LEU A CA  1 
ATOM   3221  C  C   . LEU A  1 423 ? 13.901  -8.516  40.552   1.00 202.63 ? 423  LEU A C   1 
ATOM   3222  O  O   . LEU A  1 423 ? 14.113  -7.515  41.243   1.00 208.21 ? 423  LEU A O   1 
ATOM   3223  C  CB  . LEU A  1 423 ? 12.864  -10.136 42.146   1.00 183.93 ? 423  LEU A CB  1 
ATOM   3224  C  CG  . LEU A  1 423 ? 11.472  -9.706  41.704   1.00 179.27 ? 423  LEU A CG  1 
ATOM   3225  C  CD1 . LEU A  1 423 ? 11.003  -10.543 40.530   1.00 198.40 ? 423  LEU A CD1 1 
ATOM   3226  C  CD2 . LEU A  1 423 ? 10.510  -9.814  42.869   1.00 179.40 ? 423  LEU A CD2 1 
ATOM   3227  N  N   . ILE A  1 424 ? 13.548  -8.456  39.266   1.00 184.09 ? 424  ILE A N   1 
ATOM   3228  C  CA  . ILE A  1 424 ? 13.264  -7.201  38.572   1.00 183.50 ? 424  ILE A CA  1 
ATOM   3229  C  C   . ILE A  1 424 ? 11.755  -7.038  38.436   1.00 205.64 ? 424  ILE A C   1 
ATOM   3230  O  O   . ILE A  1 424 ? 11.055  -7.980  38.042   1.00 193.56 ? 424  ILE A O   1 
ATOM   3231  C  CB  . ILE A  1 424 ? 13.940  -7.156  37.192   1.00 184.63 ? 424  ILE A CB  1 
ATOM   3232  C  CG1 . ILE A  1 424 ? 15.442  -7.385  37.326   1.00 209.06 ? 424  ILE A CG1 1 
ATOM   3233  C  CG2 . ILE A  1 424 ? 13.694  -5.819  36.517   1.00 184.54 ? 424  ILE A CG2 1 
ATOM   3234  C  CD1 . ILE A  1 424 ? 16.146  -7.558  35.999   1.00 225.25 ? 424  ILE A CD1 1 
ATOM   3235  N  N   . VAL A  1 425 ? 11.254  -5.839  38.741   1.00 216.69 ? 425  VAL A N   1 
ATOM   3236  C  CA  . VAL A  1 425 ? 9.825   -5.535  38.682   1.00 203.89 ? 425  VAL A CA  1 
ATOM   3237  C  C   . VAL A  1 425 ? 9.600   -4.312  37.799   1.00 197.68 ? 425  VAL A C   1 
ATOM   3238  O  O   . VAL A  1 425 ? 10.109  -3.225  38.096   1.00 188.86 ? 425  VAL A O   1 
ATOM   3239  C  CB  . VAL A  1 425 ? 9.238   -5.292  40.079   1.00 204.22 ? 425  VAL A CB  1 
ATOM   3240  C  CG1 . VAL A  1 425 ? 7.771   -4.911  39.964   1.00 196.66 ? 425  VAL A CG1 1 
ATOM   3241  C  CG2 . VAL A  1 425 ? 9.426   -6.520  40.955   1.00 200.71 ? 425  VAL A CG2 1 
ATOM   3242  N  N   . GLY A  1 426 ? 8.820   -4.485  36.733   1.00 197.30 ? 426  GLY A N   1 
ATOM   3243  C  CA  . GLY A  1 426 ? 8.513   -3.395  35.830   1.00 189.58 ? 426  GLY A CA  1 
ATOM   3244  C  C   . GLY A  1 426 ? 7.231   -2.657  36.181   1.00 169.69 ? 426  GLY A C   1 
ATOM   3245  O  O   . GLY A  1 426 ? 6.258   -3.246  36.646   1.00 166.90 ? 426  GLY A O   1 
ATOM   3246  N  N   . ALA A  1 427 ? 7.240   -1.333  35.940   1.00 172.23 ? 427  ALA A N   1 
ATOM   3247  C  CA  . ALA A  1 427 ? 6.070   -0.459  36.125   1.00 170.60 ? 427  ALA A CA  1 
ATOM   3248  C  C   . ALA A  1 427 ? 5.997   0.495   34.928   1.00 171.27 ? 427  ALA A C   1 
ATOM   3249  O  O   . ALA A  1 427 ? 6.416   1.651   35.001   1.00 183.01 ? 427  ALA A O   1 
ATOM   3250  C  CB  . ALA A  1 427 ? 6.146   0.307   37.444   1.00 173.42 ? 427  ALA A CB  1 
ATOM   3251  N  N   . PHE A  1 428 ? 5.414   0.021   33.826   1.00 168.35 ? 428  PHE A N   1 
ATOM   3252  C  CA  . PHE A  1 428 ? 5.493   0.778   32.581   1.00 169.25 ? 428  PHE A CA  1 
ATOM   3253  C  C   . PHE A  1 428 ? 4.700   2.079   32.628   1.00 170.22 ? 428  PHE A C   1 
ATOM   3254  O  O   . PHE A  1 428 ? 5.027   3.012   31.888   1.00 172.52 ? 428  PHE A O   1 
ATOM   3255  C  CB  . PHE A  1 428 ? 5.016   -0.092  31.414   1.00 166.11 ? 428  PHE A CB  1 
ATOM   3256  C  CG  . PHE A  1 428 ? 3.545   -0.394  31.442   1.00 162.58 ? 428  PHE A CG  1 
ATOM   3257  C  CD1 . PHE A  1 428 ? 2.619   0.478   30.880   1.00 162.24 ? 428  PHE A CD1 1 
ATOM   3258  C  CD2 . PHE A  1 428 ? 3.087   -1.550  32.043   1.00 163.89 ? 428  PHE A CD2 1 
ATOM   3259  C  CE1 . PHE A  1 428 ? 1.262   0.199   30.922   1.00 159.37 ? 428  PHE A CE1 1 
ATOM   3260  C  CE2 . PHE A  1 428 ? 1.732   -1.839  32.080   1.00 193.35 ? 428  PHE A CE2 1 
ATOM   3261  C  CZ  . PHE A  1 428 ? 0.815   -0.961  31.520   1.00 156.74 ? 428  PHE A CZ  1 
ATOM   3262  N  N   . GLY A  1 429 ? 3.684   2.169   33.489   1.00 168.91 ? 429  GLY A N   1 
ATOM   3263  C  CA  . GLY A  1 429 ? 2.859   3.365   33.553   1.00 185.14 ? 429  GLY A CA  1 
ATOM   3264  C  C   . GLY A  1 429 ? 3.595   4.599   34.028   1.00 188.80 ? 429  GLY A C   1 
ATOM   3265  O  O   . GLY A  1 429 ? 3.147   5.720   33.760   1.00 196.00 ? 429  GLY A O   1 
ATOM   3266  N  N   . VAL A  1 430 ? 4.709   4.419   34.734   1.00 176.93 ? 430  VAL A N   1 
ATOM   3267  C  CA  . VAL A  1 430 ? 5.555   5.514   35.176   1.00 181.73 ? 430  VAL A CA  1 
ATOM   3268  C  C   . VAL A  1 430 ? 6.958   5.407   34.596   1.00 184.00 ? 430  VAL A C   1 
ATOM   3269  O  O   . VAL A  1 430 ? 7.864   6.109   35.043   1.00 188.23 ? 430  VAL A O   1 
ATOM   3270  C  CB  . VAL A  1 430 ? 5.597   5.604   36.714   1.00 184.83 ? 430  VAL A CB  1 
ATOM   3271  C  CG1 . VAL A  1 430 ? 4.266   6.112   37.259   1.00 182.83 ? 430  VAL A CG1 1 
ATOM   3272  C  CG2 . VAL A  1 430 ? 5.931   4.251   37.318   1.00 183.53 ? 430  VAL A CG2 1 
ATOM   3273  N  N   . ASP A  1 431 ? 7.149   4.529   33.609   1.00 189.53 ? 431  ASP A N   1 
ATOM   3274  C  CA  . ASP A  1 431 ? 8.418   4.341   32.900   1.00 183.73 ? 431  ASP A CA  1 
ATOM   3275  C  C   . ASP A  1 431 ? 9.563   4.065   33.873   1.00 186.61 ? 431  ASP A C   1 
ATOM   3276  O  O   . ASP A  1 431 ? 10.557  4.794   33.926   1.00 197.60 ? 431  ASP A O   1 
ATOM   3277  C  CB  . ASP A  1 431 ? 8.732   5.556   32.024   1.00 191.71 ? 431  ASP A CB  1 
ATOM   3278  C  CG  . ASP A  1 431 ? 7.598   5.905   31.080   1.00 211.24 ? 431  ASP A CG  1 
ATOM   3279  O  OD1 . ASP A  1 431 ? 7.386   5.163   30.098   1.00 221.81 ? 431  ASP A OD1 1 
ATOM   3280  O  OD2 . ASP A  1 431 ? 6.904   6.912   31.330   1.00 229.89 ? 431  ASP A OD2 1 
ATOM   3281  N  N   . ARG A  1 432 ? 9.416   2.984   34.639   1.00 184.36 ? 432  ARG A N   1 
ATOM   3282  C  CA  . ARG A  1 432 ? 10.384  2.678   35.678   1.00 187.09 ? 432  ARG A CA  1 
ATOM   3283  C  C   . ARG A  1 432 ? 10.540  1.171   35.853   1.00 184.74 ? 432  ARG A C   1 
ATOM   3284  O  O   . ARG A  1 432 ? 9.600   0.396   35.651   1.00 180.44 ? 432  ARG A O   1 
ATOM   3285  C  CB  . ARG A  1 432 ? 9.972   3.334   36.999   1.00 188.58 ? 432  ARG A CB  1 
ATOM   3286  C  CG  . ARG A  1 432 ? 11.135  3.857   37.804   1.00 197.10 ? 432  ARG A CG  1 
ATOM   3287  C  CD  . ARG A  1 432 ? 11.643  5.151   37.208   1.00 202.55 ? 432  ARG A CD  1 
ATOM   3288  N  NE  . ARG A  1 432 ? 10.650  6.223   37.177   1.00 202.56 ? 432  ARG A NE  1 
ATOM   3289  C  CZ  . ARG A  1 432 ? 10.625  7.246   38.027   1.00 201.25 ? 432  ARG A CZ  1 
ATOM   3290  N  NH1 . ARG A  1 432 ? 11.537  7.342   38.985   1.00 204.95 ? 432  ARG A NH1 1 
ATOM   3291  N  NH2 . ARG A  1 432 ? 9.687   8.178   37.919   1.00 211.37 ? 432  ARG A NH2 1 
ATOM   3292  N  N   . ALA A  1 433 ? 11.751  0.772   36.243   1.00 205.03 ? 433  ALA A N   1 
ATOM   3293  C  CA  . ALA A  1 433 ? 12.065  -0.594  36.635   1.00 198.97 ? 433  ALA A CA  1 
ATOM   3294  C  C   . ALA A  1 433 ? 12.912  -0.567  37.901   1.00 190.25 ? 433  ALA A C   1 
ATOM   3295  O  O   . ALA A  1 433 ? 13.834  0.247   38.026   1.00 194.69 ? 433  ALA A O   1 
ATOM   3296  C  CB  . ALA A  1 433 ? 12.796  -1.344  35.518   1.00 196.51 ? 433  ALA A CB  1 
ATOM   3297  N  N   . ILE A  1 434 ? 12.597  -1.460  38.837   1.00 188.75 ? 434  ILE A N   1 
ATOM   3298  C  CA  . ILE A  1 434 ? 13.202  -1.465  40.163   1.00 192.10 ? 434  ILE A CA  1 
ATOM   3299  C  C   . ILE A  1 434 ? 13.792  -2.842  40.444   1.00 196.94 ? 434  ILE A C   1 
ATOM   3300  O  O   . ILE A  1 434 ? 13.106  -3.859  40.292   1.00 194.54 ? 434  ILE A O   1 
ATOM   3301  C  CB  . ILE A  1 434 ? 12.179  -1.085  41.249   1.00 190.96 ? 434  ILE A CB  1 
ATOM   3302  C  CG1 . ILE A  1 434 ? 11.484  0.233   40.891   1.00 208.97 ? 434  ILE A CG1 1 
ATOM   3303  C  CG2 . ILE A  1 434 ? 12.856  -0.980  42.601   1.00 195.06 ? 434  ILE A CG2 1 
ATOM   3304  C  CD1 . ILE A  1 434 ? 10.152  0.060   40.162   1.00 201.70 ? 434  ILE A CD1 1 
ATOM   3305  N  N   . LEU A  1 435 ? 15.055  -2.871  40.872   1.00 204.97 ? 435  LEU A N   1 
ATOM   3306  C  CA  . LEU A  1 435 ? 15.744  -4.104  41.244   1.00 201.07 ? 435  LEU A CA  1 
ATOM   3307  C  C   . LEU A  1 435 ? 15.708  -4.284  42.760   1.00 199.67 ? 435  LEU A C   1 
ATOM   3308  O  O   . LEU A  1 435 ? 16.238  -3.448  43.500   1.00 208.54 ? 435  LEU A O   1 
ATOM   3309  C  CB  . LEU A  1 435 ? 17.191  -4.091  40.749   1.00 202.67 ? 435  LEU A CB  1 
ATOM   3310  C  CG  . LEU A  1 435 ? 18.053  -5.296  41.141   1.00 204.99 ? 435  LEU A CG  1 
ATOM   3311  C  CD1 . LEU A  1 435 ? 17.597  -6.557  40.424   1.00 201.22 ? 435  LEU A CD1 1 
ATOM   3312  C  CD2 . LEU A  1 435 ? 19.520  -5.023  40.869   1.00 210.72 ? 435  LEU A CD2 1 
ATOM   3313  N  N   . TYR A  1 436 ? 15.099  -5.377  43.218   1.00 196.89 ? 436  TYR A N   1 
ATOM   3314  C  CA  . TYR A  1 436 ? 15.093  -5.745  44.630   1.00 198.55 ? 436  TYR A CA  1 
ATOM   3315  C  C   . TYR A  1 436 ? 16.114  -6.854  44.856   1.00 201.31 ? 436  TYR A C   1 
ATOM   3316  O  O   . TYR A  1 436 ? 16.045  -7.908  44.213   1.00 199.14 ? 436  TYR A O   1 
ATOM   3317  C  CB  . TYR A  1 436 ? 13.701  -6.194  45.076   1.00 194.13 ? 436  TYR A CB  1 
ATOM   3318  C  CG  . TYR A  1 436 ? 12.669  -5.087  45.096   1.00 192.21 ? 436  TYR A CG  1 
ATOM   3319  C  CD1 . TYR A  1 436 ? 12.559  -4.239  46.189   1.00 194.88 ? 436  TYR A CD1 1 
ATOM   3320  C  CD2 . TYR A  1 436 ? 11.821  -4.877  44.015   1.00 188.18 ? 436  TYR A CD2 1 
ATOM   3321  C  CE1 . TYR A  1 436 ? 11.623  -3.224  46.217   1.00 193.63 ? 436  TYR A CE1 1 
ATOM   3322  C  CE2 . TYR A  1 436 ? 10.881  -3.858  44.031   1.00 191.50 ? 436  TYR A CE2 1 
ATOM   3323  C  CZ  . TYR A  1 436 ? 10.787  -3.035  45.137   1.00 196.04 ? 436  TYR A CZ  1 
ATOM   3324  O  OH  . TYR A  1 436 ? 9.854   -2.020  45.167   1.00 194.45 ? 436  TYR A OH  1 
ATOM   3325  N  N   . ARG A  1 437 ? 17.043  -6.621  45.776   1.00 206.38 ? 437  ARG A N   1 
ATOM   3326  C  CA  . ARG A  1 437 ? 18.116  -7.559  46.068   1.00 210.01 ? 437  ARG A CA  1 
ATOM   3327  C  C   . ARG A  1 437 ? 17.763  -8.403  47.284   1.00 210.05 ? 437  ARG A C   1 
ATOM   3328  O  O   . ARG A  1 437 ? 17.279  -7.882  48.293   1.00 210.52 ? 437  ARG A O   1 
ATOM   3329  C  CB  . ARG A  1 437 ? 19.428  -6.817  46.314   1.00 216.21 ? 437  ARG A CB  1 
ATOM   3330  C  CG  . ARG A  1 437 ? 19.947  -6.066  45.109   1.00 217.06 ? 437  ARG A CG  1 
ATOM   3331  C  CD  . ARG A  1 437 ? 21.287  -5.442  45.424   1.00 223.73 ? 437  ARG A CD  1 
ATOM   3332  N  NE  . ARG A  1 437 ? 21.163  -4.331  46.365   1.00 230.93 ? 437  ARG A NE  1 
ATOM   3333  C  CZ  . ARG A  1 437 ? 22.055  -4.054  47.311   1.00 231.78 ? 437  ARG A CZ  1 
ATOM   3334  N  NH1 . ARG A  1 437 ? 23.125  -4.819  47.448   1.00 235.75 ? 437  ARG A NH1 1 
ATOM   3335  N  NH2 . ARG A  1 437 ? 21.874  -3.024  48.129   1.00 233.90 ? 437  ARG A NH2 1 
ATOM   3336  N  N   . ALA A  1 438 ? 18.014  -9.706  47.188   1.00 209.92 ? 438  ALA A N   1 
ATOM   3337  C  CA  . ALA A  1 438 ? 17.710  -10.611 48.286   1.00 210.20 ? 438  ALA A CA  1 
ATOM   3338  C  C   . ALA A  1 438 ? 18.754  -10.480 49.388   1.00 232.22 ? 438  ALA A C   1 
ATOM   3339  O  O   . ALA A  1 438 ? 19.954  -10.632 49.140   1.00 232.62 ? 438  ALA A O   1 
ATOM   3340  C  CB  . ALA A  1 438 ? 17.652  -12.052 47.783   1.00 208.45 ? 438  ALA A CB  1 
ATOM   3341  N  N   . ARG A  1 439 ? 18.293  -10.221 50.611   1.00 209.31 ? 439  ARG A N   1 
ATOM   3342  C  CA  . ARG A  1 439 ? 19.206  -10.134 51.740   1.00 213.35 ? 439  ARG A CA  1 
ATOM   3343  C  C   . ARG A  1 439 ? 19.527  -11.535 52.254   1.00 216.98 ? 439  ARG A C   1 
ATOM   3344  O  O   . ARG A  1 439 ? 18.655  -12.407 52.259   1.00 212.09 ? 439  ARG A O   1 
ATOM   3345  C  CB  . ARG A  1 439 ? 18.594  -9.298  52.865   1.00 214.98 ? 439  ARG A CB  1 
ATOM   3346  C  CG  . ARG A  1 439 ? 18.313  -7.859  52.474   1.00 216.83 ? 439  ARG A CG  1 
ATOM   3347  C  CD  . ARG A  1 439 ? 17.349  -7.179  53.438   1.00 219.04 ? 439  ARG A CD  1 
ATOM   3348  N  NE  . ARG A  1 439 ? 17.863  -7.107  54.804   1.00 220.78 ? 439  ARG A NE  1 
ATOM   3349  C  CZ  . ARG A  1 439 ? 17.168  -6.636  55.835   1.00 224.53 ? 439  ARG A CZ  1 
ATOM   3350  N  NH1 . ARG A  1 439 ? 15.930  -6.198  55.657   1.00 225.70 ? 439  ARG A NH1 1 
ATOM   3351  N  NH2 . ARG A  1 439 ? 17.708  -6.606  57.046   1.00 230.50 ? 439  ARG A NH2 1 
ATOM   3352  N  N   . PRO A  1 440 ? 20.765  -11.778 52.686   1.00 232.52 ? 440  PRO A N   1 
ATOM   3353  C  CA  . PRO A  1 440 ? 21.106  -13.096 53.233   1.00 234.37 ? 440  PRO A CA  1 
ATOM   3354  C  C   . PRO A  1 440 ? 20.283  -13.398 54.477   1.00 236.18 ? 440  PRO A C   1 
ATOM   3355  O  O   . PRO A  1 440 ? 19.955  -12.510 55.265   1.00 244.49 ? 440  PRO A O   1 
ATOM   3356  C  CB  . PRO A  1 440 ? 22.601  -12.972 53.560   1.00 233.84 ? 440  PRO A CB  1 
ATOM   3357  C  CG  . PRO A  1 440 ? 23.084  -11.833 52.712   1.00 228.15 ? 440  PRO A CG  1 
ATOM   3358  C  CD  . PRO A  1 440 ? 21.932  -10.881 52.628   1.00 227.95 ? 440  PRO A CD  1 
ATOM   3359  N  N   . VAL A  1 441 ? 19.948  -14.673 54.648   1.00 230.55 ? 441  VAL A N   1 
ATOM   3360  C  CA  . VAL A  1 441 ? 19.066  -15.118 55.723   1.00 230.51 ? 441  VAL A CA  1 
ATOM   3361  C  C   . VAL A  1 441 ? 19.910  -15.821 56.777   1.00 240.30 ? 441  VAL A C   1 
ATOM   3362  O  O   . VAL A  1 441 ? 20.581  -16.819 56.488   1.00 245.53 ? 441  VAL A O   1 
ATOM   3363  C  CB  . VAL A  1 441 ? 17.946  -16.029 55.202   1.00 226.24 ? 441  VAL A CB  1 
ATOM   3364  C  CG1 . VAL A  1 441 ? 17.041  -16.460 56.345   1.00 219.97 ? 441  VAL A CG1 1 
ATOM   3365  C  CG2 . VAL A  1 441 ? 17.138  -15.306 54.135   1.00 226.31 ? 441  VAL A CG2 1 
ATOM   3366  N  N   . ILE A  1 442 ? 19.891  -15.283 57.993   1.00 239.35 ? 442  ILE A N   1 
ATOM   3367  C  CA  . ILE A  1 442 ? 20.632  -15.825 59.125   1.00 231.15 ? 442  ILE A CA  1 
ATOM   3368  C  C   . ILE A  1 442 ? 19.673  -16.664 59.960   1.00 227.26 ? 442  ILE A C   1 
ATOM   3369  O  O   . ILE A  1 442 ? 18.630  -16.170 60.406   1.00 234.45 ? 442  ILE A O   1 
ATOM   3370  C  CB  . ILE A  1 442 ? 21.263  -14.706 59.968   1.00 224.01 ? 442  ILE A CB  1 
ATOM   3371  C  CG1 . ILE A  1 442 ? 21.989  -13.696 59.077   1.00 217.08 ? 442  ILE A CG1 1 
ATOM   3372  C  CG2 . ILE A  1 442 ? 22.224  -15.285 60.996   1.00 226.62 ? 442  ILE A CG2 1 
ATOM   3373  C  CD1 . ILE A  1 442 ? 23.160  -14.271 58.339   1.00 214.86 ? 442  ILE A CD1 1 
ATOM   3374  N  N   . THR A  1 443 ? 19.995  -17.941 60.140   1.00 217.54 ? 443  THR A N   1 
ATOM   3375  C  CA  . THR A  1 443 ? 19.268  -18.808 61.059   1.00 218.70 ? 443  THR A CA  1 
ATOM   3376  C  C   . THR A  1 443 ? 20.021  -18.842 62.387   1.00 233.71 ? 443  THR A C   1 
ATOM   3377  O  O   . THR A  1 443 ? 21.199  -19.214 62.429   1.00 245.37 ? 443  THR A O   1 
ATOM   3378  C  CB  . THR A  1 443 ? 19.113  -20.210 60.471   1.00 217.11 ? 443  THR A CB  1 
ATOM   3379  O  OG1 . THR A  1 443 ? 18.250  -20.153 59.327   1.00 214.67 ? 443  THR A OG1 1 
ATOM   3380  C  CG2 . THR A  1 443 ? 18.519  -21.159 61.493   1.00 221.94 ? 443  THR A CG2 1 
ATOM   3381  N  N   . VAL A  1 444 ? 19.346  -18.449 63.464   1.00 239.17 ? 444  VAL A N   1 
ATOM   3382  C  CA  . VAL A  1 444 ? 19.952  -18.348 64.789   1.00 236.44 ? 444  VAL A CA  1 
ATOM   3383  C  C   . VAL A  1 444 ? 19.295  -19.362 65.718   1.00 242.02 ? 444  VAL A C   1 
ATOM   3384  O  O   . VAL A  1 444 ? 18.062  -19.456 65.776   1.00 253.50 ? 444  VAL A O   1 
ATOM   3385  C  CB  . VAL A  1 444 ? 19.835  -16.918 65.345   1.00 235.37 ? 444  VAL A CB  1 
ATOM   3386  C  CG1 . VAL A  1 444 ? 18.414  -16.389 65.182   1.00 244.78 ? 444  VAL A CG1 1 
ATOM   3387  C  CG2 . VAL A  1 444 ? 20.252  -16.875 66.805   1.00 235.84 ? 444  VAL A CG2 1 
ATOM   3388  N  N   . ASN A  1 445 ? 20.119  -20.124 66.438   1.00 239.18 ? 445  ASN A N   1 
ATOM   3389  C  CA  . ASN A  1 445 ? 19.656  -21.049 67.473   1.00 248.71 ? 445  ASN A CA  1 
ATOM   3390  C  C   . ASN A  1 445 ? 20.185  -20.573 68.828   1.00 256.48 ? 445  ASN A C   1 
ATOM   3391  O  O   . ASN A  1 445 ? 21.382  -20.697 69.115   1.00 257.75 ? 445  ASN A O   1 
ATOM   3392  C  CB  . ASN A  1 445 ? 20.098  -22.479 67.166   1.00 249.84 ? 445  ASN A CB  1 
ATOM   3393  C  CG  . ASN A  1 445 ? 19.290  -23.117 66.044   1.00 239.78 ? 445  ASN A CG  1 
ATOM   3394  O  OD1 . ASN A  1 445 ? 19.852  -23.607 65.066   1.00 234.76 ? 445  ASN A OD1 1 
ATOM   3395  N  ND2 . ASN A  1 445 ? 17.966  -23.121 66.187   1.00 238.46 ? 445  ASN A ND2 1 
ATOM   3396  N  N   . ALA A  1 446 ? 19.303  -19.990 69.642   1.00 256.32 ? 446  ALA A N   1 
ATOM   3397  C  CA  . ALA A  1 446 ? 19.662  -19.513 70.969   1.00 255.72 ? 446  ALA A CA  1 
ATOM   3398  C  C   . ALA A  1 446 ? 19.249  -20.512 72.047   1.00 256.33 ? 446  ALA A C   1 
ATOM   3399  O  O   . ALA A  1 446 ? 18.204  -21.162 71.956   1.00 250.96 ? 446  ALA A O   1 
ATOM   3400  C  CB  . ALA A  1 446 ? 19.020  -18.153 71.251   1.00 248.16 ? 446  ALA A CB  1 
ATOM   3401  N  N   . GLY A  1 447 ? 20.081  -20.612 73.078   1.00 271.48 ? 447  GLY A N   1 
ATOM   3402  C  CA  . GLY A  1 447 ? 19.817  -21.502 74.193   1.00 281.60 ? 447  GLY A CA  1 
ATOM   3403  C  C   . GLY A  1 447 ? 19.912  -20.771 75.516   1.00 290.45 ? 447  GLY A C   1 
ATOM   3404  O  O   . GLY A  1 447 ? 20.583  -19.746 75.635   1.00 301.56 ? 447  GLY A O   1 
ATOM   3405  N  N   . LEU A  1 448 ? 19.224  -21.316 76.522   1.00 270.03 ? 448  LEU A N   1 
ATOM   3406  C  CA  . LEU A  1 448 ? 19.235  -20.703 77.852   1.00 256.04 ? 448  LEU A CA  1 
ATOM   3407  C  C   . LEU A  1 448 ? 19.036  -21.781 78.911   1.00 249.33 ? 448  LEU A C   1 
ATOM   3408  O  O   . LEU A  1 448 ? 17.987  -22.433 78.949   1.00 247.63 ? 448  LEU A O   1 
ATOM   3409  C  CB  . LEU A  1 448 ? 18.168  -19.616 77.969   1.00 249.57 ? 448  LEU A CB  1 
ATOM   3410  C  CG  . LEU A  1 448 ? 18.251  -18.782 79.251   1.00 248.24 ? 448  LEU A CG  1 
ATOM   3411  C  CD1 . LEU A  1 448 ? 19.615  -18.122 79.361   1.00 252.90 ? 448  LEU A CD1 1 
ATOM   3412  C  CD2 . LEU A  1 448 ? 17.146  -17.745 79.285   1.00 245.04 ? 448  LEU A CD2 1 
ATOM   3413  N  N   . GLU A  1 449 ? 20.050  -21.980 79.749   1.00 261.14 ? 449  GLU A N   1 
ATOM   3414  C  CA  . GLU A  1 449 ? 19.990  -22.901 80.875   1.00 265.57 ? 449  GLU A CA  1 
ATOM   3415  C  C   . GLU A  1 449 ? 20.091  -22.120 82.178   1.00 270.56 ? 449  GLU A C   1 
ATOM   3416  O  O   . GLU A  1 449 ? 20.923  -21.217 82.306   1.00 272.73 ? 449  GLU A O   1 
ATOM   3417  C  CB  . GLU A  1 449 ? 21.110  -23.943 80.809   1.00 267.09 ? 449  GLU A CB  1 
ATOM   3418  C  CG  . GLU A  1 449 ? 21.093  -24.793 79.556   1.00 271.58 ? 449  GLU A CG  1 
ATOM   3419  C  CD  . GLU A  1 449 ? 22.287  -25.716 79.469   1.00 272.69 ? 449  GLU A CD  1 
ATOM   3420  O  OE1 . GLU A  1 449 ? 22.603  -26.177 78.351   1.00 281.40 ? 449  GLU A OE1 1 
ATOM   3421  O  OE2 . GLU A  1 449 ? 22.913  -25.973 80.519   1.00 260.08 ? 449  GLU A OE2 1 
ATOM   3422  N  N   . VAL A  1 450 ? 19.249  -22.478 83.144   1.00 264.54 ? 450  VAL A N   1 
ATOM   3423  C  CA  . VAL A  1 450 ? 19.260  -21.880 84.475   1.00 260.96 ? 450  VAL A CA  1 
ATOM   3424  C  C   . VAL A  1 450 ? 19.385  -23.010 85.489   1.00 267.23 ? 450  VAL A C   1 
ATOM   3425  O  O   . VAL A  1 450 ? 18.418  -23.744 85.729   1.00 261.51 ? 450  VAL A O   1 
ATOM   3426  C  CB  . VAL A  1 450 ? 18.006  -21.039 84.749   1.00 256.11 ? 450  VAL A CB  1 
ATOM   3427  C  CG1 . VAL A  1 450 ? 18.051  -20.471 86.161   1.00 261.29 ? 450  VAL A CG1 1 
ATOM   3428  C  CG2 . VAL A  1 450 ? 17.882  -19.921 83.725   1.00 252.95 ? 450  VAL A CG2 1 
ATOM   3429  N  N   . TYR A  1 451 ? 20.568  -23.152 86.080   1.00 278.51 ? 451  TYR A N   1 
ATOM   3430  C  CA  . TYR A  1 451 ? 20.809  -24.172 87.098   1.00 282.44 ? 451  TYR A CA  1 
ATOM   3431  C  C   . TYR A  1 451 ? 21.482  -23.546 88.322   1.00 294.61 ? 451  TYR A C   1 
ATOM   3432  O  O   . TYR A  1 451 ? 22.514  -22.889 88.195   1.00 306.79 ? 451  TYR A O   1 
ATOM   3433  C  CB  . TYR A  1 451 ? 21.660  -25.321 86.534   1.00 273.12 ? 451  TYR A CB  1 
ATOM   3434  C  CG  . TYR A  1 451 ? 22.870  -24.893 85.724   1.00 267.21 ? 451  TYR A CG  1 
ATOM   3435  C  CD1 . TYR A  1 451 ? 22.775  -24.680 84.355   1.00 266.99 ? 451  TYR A CD1 1 
ATOM   3436  C  CD2 . TYR A  1 451 ? 24.111  -24.726 86.327   1.00 267.19 ? 451  TYR A CD2 1 
ATOM   3437  C  CE1 . TYR A  1 451 ? 23.876  -24.294 83.614   1.00 268.63 ? 451  TYR A CE1 1 
ATOM   3438  C  CE2 . TYR A  1 451 ? 25.216  -24.341 85.595   1.00 266.47 ? 451  TYR A CE2 1 
ATOM   3439  C  CZ  . TYR A  1 451 ? 25.094  -24.127 84.240   1.00 270.25 ? 451  TYR A CZ  1 
ATOM   3440  O  OH  . TYR A  1 451 ? 26.196  -23.746 83.511   1.00 275.50 ? 451  TYR A OH  1 
ATOM   3441  N  N   . PRO A  1 452 ? 20.905  -23.755 89.519   1.00 278.84 ? 452  PRO A N   1 
ATOM   3442  C  CA  . PRO A  1 452 ? 19.690  -24.535 89.780   1.00 271.53 ? 452  PRO A CA  1 
ATOM   3443  C  C   . PRO A  1 452 ? 18.387  -23.828 89.421   1.00 264.53 ? 452  PRO A C   1 
ATOM   3444  O  O   . PRO A  1 452 ? 18.342  -22.604 89.288   1.00 254.89 ? 452  PRO A O   1 
ATOM   3445  C  CB  . PRO A  1 452 ? 19.751  -24.765 91.290   1.00 261.51 ? 452  PRO A CB  1 
ATOM   3446  C  CG  . PRO A  1 452 ? 20.448  -23.558 91.802   1.00 263.25 ? 452  PRO A CG  1 
ATOM   3447  C  CD  . PRO A  1 452 ? 21.473  -23.200 90.762   1.00 270.58 ? 452  PRO A CD  1 
ATOM   3448  N  N   . SER A  1 453 ? 17.323  -24.627 89.281   1.00 269.66 ? 453  SER A N   1 
ATOM   3449  C  CA  . SER A  1 453 ? 15.987  -24.078 89.091   1.00 254.80 ? 453  SER A CA  1 
ATOM   3450  C  C   . SER A  1 453 ? 15.443  -23.496 90.386   1.00 255.56 ? 453  SER A C   1 
ATOM   3451  O  O   . SER A  1 453 ? 14.692  -22.515 90.360   1.00 245.00 ? 453  SER A O   1 
ATOM   3452  C  CB  . SER A  1 453 ? 15.041  -25.158 88.557   1.00 245.04 ? 453  SER A CB  1 
ATOM   3453  O  OG  . SER A  1 453 ? 14.988  -26.283 89.418   1.00 241.16 ? 453  SER A OG  1 
ATOM   3454  N  N   . ILE A  1 454 ? 15.793  -24.095 91.518   1.00 269.65 ? 454  ILE A N   1 
ATOM   3455  C  CA  . ILE A  1 454 ? 15.248  -23.720 92.816   1.00 269.63 ? 454  ILE A CA  1 
ATOM   3456  C  C   . ILE A  1 454 ? 16.349  -23.001 93.581   1.00 269.35 ? 454  ILE A C   1 
ATOM   3457  O  O   . ILE A  1 454 ? 17.373  -23.600 93.933   1.00 271.57 ? 454  ILE A O   1 
ATOM   3458  C  CB  . ILE A  1 454 ? 14.725  -24.937 93.593   1.00 267.83 ? 454  ILE A CB  1 
ATOM   3459  C  CG1 . ILE A  1 454 ? 15.687  -26.120 93.468   1.00 264.13 ? 454  ILE A CG1 1 
ATOM   3460  C  CG2 . ILE A  1 454 ? 13.354  -25.336 93.086   1.00 261.17 ? 454  ILE A CG2 1 
ATOM   3461  C  CD1 . ILE A  1 454 ? 15.221  -27.364 94.184   1.00 254.01 ? 454  ILE A CD1 1 
ATOM   3462  N  N   . LEU A  1 455 ? 16.152  -21.709 93.822   1.00 274.21 ? 455  LEU A N   1 
ATOM   3463  C  CA  . LEU A  1 455 ? 17.117  -20.908 94.564   1.00 282.55 ? 455  LEU A CA  1 
ATOM   3464  C  C   . LEU A  1 455 ? 16.755  -20.900 96.046   1.00 281.31 ? 455  LEU A C   1 
ATOM   3465  O  O   . LEU A  1 455 ? 15.659  -20.466 96.424   1.00 287.87 ? 455  LEU A O   1 
ATOM   3466  C  CB  . LEU A  1 455 ? 17.178  -19.486 94.006   1.00 281.49 ? 455  LEU A CB  1 
ATOM   3467  C  CG  . LEU A  1 455 ? 17.442  -19.364 92.499   1.00 275.50 ? 455  LEU A CG  1 
ATOM   3468  C  CD1 . LEU A  1 455 ? 17.482  -17.902 92.081   1.00 278.62 ? 455  LEU A CD1 1 
ATOM   3469  C  CD2 . LEU A  1 455 ? 18.726  -20.073 92.098   1.00 272.43 ? 455  LEU A CD2 1 
ATOM   3470  N  N   . ASN A  1 456 ? 17.665  -21.402 96.876   1.00 267.52 ? 456  ASN A N   1 
ATOM   3471  C  CA  . ASN A  1 456 ? 17.468  -21.371 98.314   1.00 254.62 ? 456  ASN A CA  1 
ATOM   3472  C  C   . ASN A  1 456 ? 17.496  -19.926 98.800   1.00 261.26 ? 456  ASN A C   1 
ATOM   3473  O  O   . ASN A  1 456 ? 18.087  -19.045 98.170   1.00 259.32 ? 456  ASN A O   1 
ATOM   3474  C  CB  . ASN A  1 456 ? 18.553  -22.194 99.014   1.00 250.01 ? 456  ASN A CB  1 
ATOM   3475  C  CG  . ASN A  1 456 ? 18.286  -22.384 100.496  1.00 254.43 ? 456  ASN A CG  1 
ATOM   3476  O  OD1 . ASN A  1 456 ? 18.743  -21.602 101.329  1.00 270.01 ? 456  ASN A OD1 1 
ATOM   3477  N  ND2 . ASN A  1 456 ? 17.556  -23.440 100.831  1.00 247.17 ? 456  ASN A ND2 1 
ATOM   3478  N  N   . GLN A  1 457 ? 16.855  -19.684 99.945   1.00 277.22 ? 457  GLN A N   1 
ATOM   3479  C  CA  . GLN A  1 457 ? 16.857  -18.337 100.500  1.00 280.53 ? 457  GLN A CA  1 
ATOM   3480  C  C   . GLN A  1 457 ? 18.205  -17.979 101.112  1.00 279.18 ? 457  GLN A C   1 
ATOM   3481  O  O   . GLN A  1 457 ? 18.485  -16.795 101.332  1.00 281.14 ? 457  GLN A O   1 
ATOM   3482  C  CB  . GLN A  1 457 ? 15.738  -18.192 101.540  1.00 278.76 ? 457  GLN A CB  1 
ATOM   3483  C  CG  . GLN A  1 457 ? 15.579  -16.781 102.083  1.00 271.06 ? 457  GLN A CG  1 
ATOM   3484  C  CD  . GLN A  1 457 ? 15.485  -15.753 100.974  1.00 259.12 ? 457  GLN A CD  1 
ATOM   3485  O  OE1 . GLN A  1 457 ? 14.628  -15.850 100.097  1.00 255.70 ? 457  GLN A OE1 1 
ATOM   3486  N  NE2 . GLN A  1 457 ? 16.389  -14.779 100.987  1.00 258.40 ? 457  GLN A NE2 1 
ATOM   3487  N  N   . ASP A  1 458 ? 19.058  -18.974 101.359  1.00 260.13 ? 458  ASP A N   1 
ATOM   3488  C  CA  . ASP A  1 458 ? 20.379  -18.731 101.943  1.00 244.54 ? 458  ASP A CA  1 
ATOM   3489  C  C   . ASP A  1 458 ? 21.309  -19.856 101.481  1.00 240.19 ? 458  ASP A C   1 
ATOM   3490  O  O   . ASP A  1 458 ? 21.464  -20.870 102.164  1.00 238.87 ? 458  ASP A O   1 
ATOM   3491  C  CB  . ASP A  1 458 ? 20.308  -18.644 103.460  1.00 240.85 ? 458  ASP A CB  1 
ATOM   3492  C  CG  . ASP A  1 458 ? 21.651  -18.334 104.086  1.00 240.22 ? 458  ASP A CG  1 
ATOM   3493  O  OD1 . ASP A  1 458 ? 22.032  -17.145 104.125  1.00 241.49 ? 458  ASP A OD1 1 
ATOM   3494  O  OD2 . ASP A  1 458 ? 22.327  -19.279 104.536  1.00 240.25 ? 458  ASP A OD2 1 
ATOM   3495  N  N   . ASN A  1 459 ? 21.910  -19.668 100.307  1.00 245.82 ? 459  ASN A N   1 
ATOM   3496  C  CA  . ASN A  1 459 ? 22.867  -20.620 99.741   1.00 254.80 ? 459  ASN A CA  1 
ATOM   3497  C  C   . ASN A  1 459 ? 24.087  -19.819 99.298   1.00 260.32 ? 459  ASN A C   1 
ATOM   3498  O  O   . ASN A  1 459 ? 24.196  -19.423 98.136   1.00 263.90 ? 459  ASN A O   1 
ATOM   3499  C  CB  . ASN A  1 459 ? 22.267  -21.409 98.585   1.00 263.66 ? 459  ASN A CB  1 
ATOM   3500  C  CG  . ASN A  1 459 ? 23.287  -22.303 97.910   1.00 283.41 ? 459  ASN A CG  1 
ATOM   3501  O  OD1 . ASN A  1 459 ? 24.265  -22.721 98.532   1.00 259.50 ? 459  ASN A OD1 1 
ATOM   3502  N  ND2 . ASN A  1 459 ? 23.077  -22.587 96.628   1.00 381.85 ? 459  ASN A ND2 1 
ATOM   3503  N  N   . LYS A  1 460 ? 25.020  -19.617 100.220  1.00 265.30 ? 460  LYS A N   1 
ATOM   3504  C  CA  . LYS A  1 460 ? 26.215  -18.826 99.967   1.00 264.99 ? 460  LYS A CA  1 
ATOM   3505  C  C   . LYS A  1 460 ? 27.320  -19.733 99.435   1.00 261.93 ? 460  LYS A C   1 
ATOM   3506  O  O   . LYS A  1 460 ? 27.779  -20.638 100.141  1.00 266.04 ? 460  LYS A O   1 
ATOM   3507  C  CB  . LYS A  1 460 ? 26.641  -18.116 101.251  1.00 273.90 ? 460  LYS A CB  1 
ATOM   3508  C  CG  . LYS A  1 460 ? 25.599  -17.121 101.753  1.00 267.16 ? 460  LYS A CG  1 
ATOM   3509  C  CD  . LYS A  1 460 ? 25.856  -16.677 103.190  1.00 262.00 ? 460  LYS A CD  1 
ATOM   3510  C  CE  . LYS A  1 460 ? 25.752  -17.834 104.180  1.00 253.77 ? 460  LYS A CE  1 
ATOM   3511  N  NZ  . LYS A  1 460 ? 25.865  -17.363 105.593  1.00 250.90 ? 460  LYS A NZ  1 
ATOM   3512  N  N   . THR A  1 461 ? 27.749  -19.494 98.193   1.00 264.14 ? 461  THR A N   1 
ATOM   3513  C  CA  . THR A  1 461 ? 28.728  -20.379 97.569   1.00 263.80 ? 461  THR A CA  1 
ATOM   3514  C  C   . THR A  1 461 ? 29.799  -19.634 96.776   1.00 264.58 ? 461  THR A C   1 
ATOM   3515  O  O   . THR A  1 461 ? 30.994  -19.779 97.059   1.00 267.05 ? 461  THR A O   1 
ATOM   3516  C  CB  . THR A  1 461 ? 28.016  -21.379 96.659   1.00 270.88 ? 461  THR A CB  1 
ATOM   3517  O  OG1 . THR A  1 461 ? 27.034  -22.100 97.412   1.00 270.96 ? 461  THR A OG1 1 
ATOM   3518  C  CG2 . THR A  1 461 ? 29.015  -22.358 96.057   1.00 277.99 ? 461  THR A CG2 1 
ATOM   3519  N  N   . CYS A  1 462 ? 29.390  -18.843 95.782   1.00 271.98 ? 462  CYS A N   1 
ATOM   3520  C  CA  . CYS A  1 462 ? 30.353  -18.075 95.002   1.00 284.11 ? 462  CYS A CA  1 
ATOM   3521  C  C   . CYS A  1 462 ? 31.110  -17.099 95.895   1.00 270.24 ? 462  CYS A C   1 
ATOM   3522  O  O   . CYS A  1 462 ? 30.576  -16.567 96.871   1.00 270.20 ? 462  CYS A O   1 
ATOM   3523  C  CB  . CYS A  1 462 ? 29.658  -17.310 93.876   1.00 301.13 ? 462  CYS A CB  1 
ATOM   3524  S  SG  . CYS A  1 462 ? 28.312  -16.282 94.460   1.00 327.69 ? 462  CYS A SG  1 
ATOM   3525  N  N   . SER A  1 463 ? 32.366  -16.851 95.536   1.00 265.81 ? 463  SER A N   1 
ATOM   3526  C  CA  . SER A  1 463 ? 33.223  -15.999 96.347   1.00 271.16 ? 463  SER A CA  1 
ATOM   3527  C  C   . SER A  1 463 ? 32.754  -14.544 96.334   1.00 270.40 ? 463  SER A C   1 
ATOM   3528  O  O   . SER A  1 463 ? 32.409  -13.986 95.287   1.00 264.94 ? 463  SER A O   1 
ATOM   3529  C  CB  . SER A  1 463 ? 34.667  -16.091 95.855   1.00 272.01 ? 463  SER A CB  1 
ATOM   3530  O  OG  . SER A  1 463 ? 35.552  -15.443 96.750   1.00 284.66 ? 463  SER A OG  1 
ATOM   3531  N  N   . LEU A  1 464 ? 32.739  -13.940 97.524   1.00 265.63 ? 464  LEU A N   1 
ATOM   3532  C  CA  . LEU A  1 464 ? 32.378  -12.551 97.783   1.00 253.36 ? 464  LEU A CA  1 
ATOM   3533  C  C   . LEU A  1 464 ? 32.847  -12.235 99.202   1.00 256.46 ? 464  LEU A C   1 
ATOM   3534  O  O   . LEU A  1 464 ? 32.912  -13.147 100.037  1.00 254.75 ? 464  LEU A O   1 
ATOM   3535  C  CB  . LEU A  1 464 ? 30.869  -12.345 97.620   1.00 236.26 ? 464  LEU A CB  1 
ATOM   3536  C  CG  . LEU A  1 464 ? 30.277  -10.938 97.720   1.00 237.31 ? 464  LEU A CG  1 
ATOM   3537  C  CD1 . LEU A  1 464 ? 30.609  -10.113 96.483   1.00 237.12 ? 464  LEU A CD1 1 
ATOM   3538  C  CD2 . LEU A  1 464 ? 28.778  -11.008 97.931   1.00 236.78 ? 464  LEU A CD2 1 
ATOM   3539  N  N   . PRO A  1 465 ? 33.194  -10.976 99.530   1.00 252.33 ? 465  PRO A N   1 
ATOM   3540  C  CA  . PRO A  1 465 ? 33.578  -10.733 100.927  1.00 243.25 ? 465  PRO A CA  1 
ATOM   3541  C  C   . PRO A  1 465 ? 32.419  -10.893 101.909  1.00 243.85 ? 465  PRO A C   1 
ATOM   3542  O  O   . PRO A  1 465 ? 31.891  -9.895  102.398  1.00 245.06 ? 465  PRO A O   1 
ATOM   3543  C  CB  . PRO A  1 465 ? 34.082  -9.283  100.909  1.00 245.92 ? 465  PRO A CB  1 
ATOM   3544  C  CG  . PRO A  1 465 ? 33.511  -8.682  99.670   1.00 246.54 ? 465  PRO A CG  1 
ATOM   3545  C  CD  . PRO A  1 465 ? 33.457  -9.805  98.678   1.00 249.49 ? 465  PRO A CD  1 
ATOM   3546  N  N   . LYS A  1 470 ? 30.007  -13.873 100.538  1.00 269.87 ? 470  LYS A N   1 
ATOM   3547  C  CA  . LYS A  1 470 ? 29.202  -14.960 99.991   1.00 263.26 ? 470  LYS A CA  1 
ATOM   3548  C  C   . LYS A  1 470 ? 27.715  -14.682 100.185  1.00 259.51 ? 470  LYS A C   1 
ATOM   3549  O  O   . LYS A  1 470 ? 27.260  -14.428 101.300  1.00 261.83 ? 470  LYS A O   1 
ATOM   3550  C  CB  . LYS A  1 470 ? 29.569  -16.304 100.639  1.00 262.91 ? 470  LYS A CB  1 
ATOM   3551  C  CG  . LYS A  1 470 ? 30.823  -17.004 100.103  1.00 261.61 ? 470  LYS A CG  1 
ATOM   3552  C  CD  . LYS A  1 470 ? 32.083  -16.171 100.241  1.00 261.46 ? 470  LYS A CD  1 
ATOM   3553  C  CE  . LYS A  1 470 ? 32.512  -16.074 101.692  1.00 254.61 ? 470  LYS A CE  1 
ATOM   3554  N  NZ  . LYS A  1 470 ? 33.751  -15.267 101.864  1.00 248.87 ? 470  LYS A NZ  1 
ATOM   3555  N  N   . VAL A  1 471 ? 26.958  -14.716 99.087   1.00 254.15 ? 471  VAL A N   1 
ATOM   3556  C  CA  . VAL A  1 471 ? 25.512  -14.537 99.118   1.00 253.74 ? 471  VAL A CA  1 
ATOM   3557  C  C   . VAL A  1 471 ? 24.874  -15.564 98.190   1.00 262.50 ? 471  VAL A C   1 
ATOM   3558  O  O   . VAL A  1 471 ? 25.534  -16.160 97.337   1.00 269.57 ? 471  VAL A O   1 
ATOM   3559  C  CB  . VAL A  1 471 ? 25.087  -13.109 98.715   1.00 255.85 ? 471  VAL A CB  1 
ATOM   3560  C  CG1 . VAL A  1 471 ? 25.556  -12.095 99.755   1.00 253.75 ? 471  VAL A CG1 1 
ATOM   3561  C  CG2 . VAL A  1 471 ? 25.640  -12.770 97.343   1.00 268.25 ? 471  VAL A CG2 1 
ATOM   3562  N  N   . SER A  1 472 ? 23.571  -15.780 98.381   1.00 262.35 ? 472  SER A N   1 
ATOM   3563  C  CA  . SER A  1 472 ? 22.800  -16.713 97.561   1.00 255.68 ? 472  SER A CA  1 
ATOM   3564  C  C   . SER A  1 472 ? 22.910  -16.430 96.063   1.00 254.60 ? 472  SER A C   1 
ATOM   3565  O  O   . SER A  1 472 ? 22.255  -15.516 95.552   1.00 248.89 ? 472  SER A O   1 
ATOM   3566  C  CB  . SER A  1 472 ? 21.332  -16.681 97.985   1.00 249.58 ? 472  SER A CB  1 
ATOM   3567  O  OG  . SER A  1 472 ? 20.572  -17.619 97.247   1.00 247.38 ? 472  SER A OG  1 
ATOM   3568  N  N   . CYS A  1 473 ? 23.718  -17.220 95.349   1.00 270.21 ? 473  CYS A N   1 
ATOM   3569  C  CA  . CYS A  1 473 ? 24.013  -16.986 93.940   1.00 278.59 ? 473  CYS A CA  1 
ATOM   3570  C  C   . CYS A  1 473 ? 23.811  -18.247 93.106   1.00 273.70 ? 473  CYS A C   1 
ATOM   3571  O  O   . CYS A  1 473 ? 23.743  -19.363 93.628   1.00 265.65 ? 473  CYS A O   1 
ATOM   3572  C  CB  . CYS A  1 473 ? 25.438  -16.464 93.747   1.00 288.65 ? 473  CYS A CB  1 
ATOM   3573  S  SG  . CYS A  1 473 ? 26.709  -17.518 94.428   1.00 318.14 ? 473  CYS A SG  1 
ATOM   3574  N  N   . PHE A  1 474 ? 23.744  -18.044 91.787   1.00 283.83 ? 474  PHE A N   1 
ATOM   3575  C  CA  . PHE A  1 474 ? 23.496  -19.107 90.820   1.00 290.31 ? 474  PHE A CA  1 
ATOM   3576  C  C   . PHE A  1 474 ? 24.198  -18.774 89.507   1.00 297.13 ? 474  PHE A C   1 
ATOM   3577  O  O   . PHE A  1 474 ? 24.588  -17.629 89.262   1.00 298.11 ? 474  PHE A O   1 
ATOM   3578  C  CB  . PHE A  1 474 ? 21.988  -19.306 90.603   1.00 287.21 ? 474  PHE A CB  1 
ATOM   3579  C  CG  . PHE A  1 474 ? 21.279  -18.061 90.149   1.00 282.03 ? 474  PHE A CG  1 
ATOM   3580  C  CD1 . PHE A  1 474 ? 20.843  -17.124 91.073   1.00 280.50 ? 474  PHE A CD1 1 
ATOM   3581  C  CD2 . PHE A  1 474 ? 21.038  -17.830 88.807   1.00 279.70 ? 474  PHE A CD2 1 
ATOM   3582  C  CE1 . PHE A  1 474 ? 20.193  -15.975 90.665   1.00 279.45 ? 474  PHE A CE1 1 
ATOM   3583  C  CE2 . PHE A  1 474 ? 20.384  -16.685 88.392   1.00 275.54 ? 474  PHE A CE2 1 
ATOM   3584  C  CZ  . PHE A  1 474 ? 19.961  -15.756 89.322   1.00 279.39 ? 474  PHE A CZ  1 
ATOM   3585  N  N   . ASN A  1 475 ? 24.370  -19.797 88.668   1.00 302.40 ? 475  ASN A N   1 
ATOM   3586  C  CA  . ASN A  1 475 ? 25.074  -19.680 87.394   1.00 299.66 ? 475  ASN A CA  1 
ATOM   3587  C  C   . ASN A  1 475 ? 24.092  -19.493 86.244   1.00 298.09 ? 475  ASN A C   1 
ATOM   3588  O  O   . ASN A  1 475 ? 23.110  -20.234 86.133   1.00 304.86 ? 475  ASN A O   1 
ATOM   3589  C  CB  . ASN A  1 475 ? 25.936  -20.918 87.139   1.00 300.45 ? 475  ASN A CB  1 
ATOM   3590  C  CG  . ASN A  1 475 ? 26.998  -21.113 88.199   1.00 307.50 ? 475  ASN A CG  1 
ATOM   3591  O  OD1 . ASN A  1 475 ? 26.763  -21.772 89.210   1.00 312.78 ? 475  ASN A OD1 1 
ATOM   3592  N  ND2 . ASN A  1 475 ? 28.177  -20.542 87.971   1.00 307.52 ? 475  ASN A ND2 1 
ATOM   3593  N  N   . VAL A  1 476 ? 24.365  -18.511 85.387   1.00 297.71 ? 476  VAL A N   1 
ATOM   3594  C  CA  . VAL A  1 476 ? 23.575  -18.256 84.184   1.00 295.10 ? 476  VAL A CA  1 
ATOM   3595  C  C   . VAL A  1 476 ? 24.436  -18.605 82.975   1.00 296.91 ? 476  VAL A C   1 
ATOM   3596  O  O   . VAL A  1 476 ? 25.411  -17.906 82.675   1.00 295.75 ? 476  VAL A O   1 
ATOM   3597  C  CB  . VAL A  1 476 ? 23.088  -16.805 84.120   1.00 296.51 ? 476  VAL A CB  1 
ATOM   3598  C  CG1 . VAL A  1 476 ? 22.265  -16.586 82.861   1.00 298.52 ? 476  VAL A CG1 1 
ATOM   3599  C  CG2 . VAL A  1 476 ? 22.278  -16.464 85.361   1.00 295.76 ? 476  VAL A CG2 1 
ATOM   3600  N  N   . ARG A  1 477 ? 24.096  -19.692 82.284   1.00 302.91 ? 477  ARG A N   1 
ATOM   3601  C  CA  . ARG A  1 477 ? 24.827  -20.129 81.098   1.00 301.38 ? 477  ARG A CA  1 
ATOM   3602  C  C   . ARG A  1 477 ? 23.938  -19.975 79.868   1.00 296.59 ? 477  ARG A C   1 
ATOM   3603  O  O   . ARG A  1 477 ? 22.879  -20.606 79.782   1.00 294.18 ? 477  ARG A O   1 
ATOM   3604  C  CB  . ARG A  1 477 ? 25.301  -21.575 81.251   1.00 300.53 ? 477  ARG A CB  1 
ATOM   3605  C  CG  . ARG A  1 477 ? 26.166  -22.077 80.097   1.00 299.50 ? 477  ARG A CG  1 
ATOM   3606  C  CD  . ARG A  1 477 ? 26.776  -23.441 80.399   1.00 300.97 ? 477  ARG A CD  1 
ATOM   3607  N  NE  . ARG A  1 477 ? 27.630  -23.924 79.317   1.00 306.05 ? 477  ARG A NE  1 
ATOM   3608  C  CZ  . ARG A  1 477 ? 27.215  -24.724 78.339   1.00 308.16 ? 477  ARG A CZ  1 
ATOM   3609  N  NH1 . ARG A  1 477 ? 25.954  -25.135 78.308   1.00 309.04 ? 477  ARG A NH1 1 
ATOM   3610  N  NH2 . ARG A  1 477 ? 28.060  -25.117 77.394   1.00 306.77 ? 477  ARG A NH2 1 
ATOM   3611  N  N   . PHE A  1 478 ? 24.371  -19.140 78.923   1.00 302.55 ? 478  PHE A N   1 
ATOM   3612  C  CA  . PHE A  1 478 ? 23.654  -18.893 77.677   1.00 303.42 ? 478  PHE A CA  1 
ATOM   3613  C  C   . PHE A  1 478 ? 24.560  -19.226 76.498   1.00 303.55 ? 478  PHE A C   1 
ATOM   3614  O  O   . PHE A  1 478 ? 25.717  -18.793 76.461   1.00 309.56 ? 478  PHE A O   1 
ATOM   3615  C  CB  . PHE A  1 478 ? 23.189  -17.433 77.592   1.00 307.59 ? 478  PHE A CB  1 
ATOM   3616  C  CG  . PHE A  1 478 ? 24.313  -16.432 77.649   1.00 312.77 ? 478  PHE A CG  1 
ATOM   3617  C  CD1 . PHE A  1 478 ? 24.845  -16.034 78.865   1.00 312.12 ? 478  PHE A CD1 1 
ATOM   3618  C  CD2 . PHE A  1 478 ? 24.838  -15.893 76.484   1.00 316.33 ? 478  PHE A CD2 1 
ATOM   3619  C  CE1 . PHE A  1 478 ? 25.882  -15.120 78.919   1.00 314.85 ? 478  PHE A CE1 1 
ATOM   3620  C  CE2 . PHE A  1 478 ? 25.874  -14.981 76.531   1.00 320.39 ? 478  PHE A CE2 1 
ATOM   3621  C  CZ  . PHE A  1 478 ? 26.396  -14.593 77.750   1.00 318.97 ? 478  PHE A CZ  1 
ATOM   3622  N  N   . CYS A  1 479 ? 24.039  -19.989 75.539   1.00 293.53 ? 479  CYS A N   1 
ATOM   3623  C  CA  . CYS A  1 479 ? 24.790  -20.386 74.357   1.00 292.29 ? 479  CYS A CA  1 
ATOM   3624  C  C   . CYS A  1 479 ? 24.199  -19.726 73.117   1.00 280.72 ? 479  CYS A C   1 
ATOM   3625  O  O   . CYS A  1 479 ? 22.999  -19.445 73.058   1.00 267.84 ? 479  CYS A O   1 
ATOM   3626  C  CB  . CYS A  1 479 ? 24.787  -21.904 74.174   1.00 290.39 ? 479  CYS A CB  1 
ATOM   3627  S  SG  . CYS A  1 479 ? 25.541  -22.877 75.511   1.00 300.46 ? 479  CYS A SG  1 
ATOM   3628  N  N   . LEU A  1 480 ? 25.048  -19.499 72.115   1.00 282.71 ? 480  LEU A N   1 
ATOM   3629  C  CA  . LEU A  1 480 ? 24.655  -18.770 70.917   1.00 268.56 ? 480  LEU A CA  1 
ATOM   3630  C  C   . LEU A  1 480 ? 25.325  -19.368 69.689   1.00 258.76 ? 480  LEU A C   1 
ATOM   3631  O  O   . LEU A  1 480 ? 26.543  -19.574 69.679   1.00 265.00 ? 480  LEU A O   1 
ATOM   3632  C  CB  . LEU A  1 480 ? 25.017  -17.286 71.039   1.00 278.33 ? 480  LEU A CB  1 
ATOM   3633  C  CG  . LEU A  1 480 ? 24.225  -16.334 70.145   1.00 268.33 ? 480  LEU A CG  1 
ATOM   3634  C  CD1 . LEU A  1 480 ? 22.740  -16.554 70.346   1.00 259.25 ? 480  LEU A CD1 1 
ATOM   3635  C  CD2 . LEU A  1 480 ? 24.603  -14.887 70.418   1.00 275.92 ? 480  LEU A CD2 1 
ATOM   3636  N  N   . LYS A  1 481 ? 24.529  -19.651 68.660   1.00 253.28 ? 481  LYS A N   1 
ATOM   3637  C  CA  . LYS A  1 481 ? 25.028  -20.224 67.418   1.00 272.24 ? 481  LYS A CA  1 
ATOM   3638  C  C   . LYS A  1 481 ? 24.235  -19.658 66.247   1.00 282.66 ? 481  LYS A C   1 
ATOM   3639  O  O   . LYS A  1 481 ? 23.010  -19.527 66.328   1.00 278.87 ? 481  LYS A O   1 
ATOM   3640  C  CB  . LYS A  1 481 ? 24.932  -21.754 67.434   1.00 279.74 ? 481  LYS A CB  1 
ATOM   3641  C  CG  . LYS A  1 481 ? 25.548  -22.435 66.223   1.00 291.44 ? 481  LYS A CG  1 
ATOM   3642  C  CD  . LYS A  1 481 ? 25.518  -23.943 66.383   1.00 295.17 ? 481  LYS A CD  1 
ATOM   3643  C  CE  . LYS A  1 481 ? 24.097  -24.479 66.249   1.00 288.92 ? 481  LYS A CE  1 
ATOM   3644  N  NZ  . LYS A  1 481 ? 23.505  -24.211 64.902   1.00 274.60 ? 481  LYS A NZ  1 
ATOM   3645  N  N   . ALA A  1 482 ? 24.938  -19.312 65.167   1.00 275.52 ? 482  ALA A N   1 
ATOM   3646  C  CA  . ALA A  1 482 ? 24.318  -18.715 63.992   1.00 252.04 ? 482  ALA A CA  1 
ATOM   3647  C  C   . ALA A  1 482 ? 24.947  -19.285 62.727   1.00 241.63 ? 482  ALA A C   1 
ATOM   3648  O  O   . ALA A  1 482 ? 26.058  -19.821 62.745   1.00 248.06 ? 482  ALA A O   1 
ATOM   3649  C  CB  . ALA A  1 482 ? 24.440  -17.185 64.000   1.00 249.65 ? 482  ALA A CB  1 
ATOM   3650  N  N   . ASP A  1 483 ? 24.207  -19.180 61.624   1.00 231.01 ? 483  ASP A N   1 
ATOM   3651  C  CA  . ASP A  1 483 ? 24.697  -19.635 60.330   1.00 234.27 ? 483  ASP A CA  1 
ATOM   3652  C  C   . ASP A  1 483 ? 23.856  -19.019 59.220   1.00 238.16 ? 483  ASP A C   1 
ATOM   3653  O  O   . ASP A  1 483 ? 22.748  -18.526 59.450   1.00 245.39 ? 483  ASP A O   1 
ATOM   3654  C  CB  . ASP A  1 483 ? 24.684  -21.164 60.230   1.00 233.84 ? 483  ASP A CB  1 
ATOM   3655  C  CG  . ASP A  1 483 ? 25.556  -21.679 59.101   1.00 228.79 ? 483  ASP A CG  1 
ATOM   3656  O  OD1 . ASP A  1 483 ? 26.619  -21.074 58.843   1.00 220.93 ? 483  ASP A OD1 1 
ATOM   3657  O  OD2 . ASP A  1 483 ? 25.176  -22.688 58.471   1.00 234.82 ? 483  ASP A OD2 1 
ATOM   3658  N  N   . GLY A  1 484 ? 24.409  -19.057 58.008   1.00 238.37 ? 484  GLY A N   1 
ATOM   3659  C  CA  . GLY A  1 484 ? 23.730  -18.557 56.831   1.00 229.17 ? 484  GLY A CA  1 
ATOM   3660  C  C   . GLY A  1 484 ? 24.093  -19.423 55.645   1.00 222.30 ? 484  GLY A C   1 
ATOM   3661  O  O   . GLY A  1 484 ? 24.979  -20.277 55.723   1.00 235.56 ? 484  GLY A O   1 
ATOM   3662  N  N   . LYS A  1 485 ? 23.389  -19.202 54.534   1.00 208.10 ? 485  LYS A N   1 
ATOM   3663  C  CA  . LYS A  1 485 ? 23.563  -20.036 53.338   1.00 209.22 ? 485  LYS A CA  1 
ATOM   3664  C  C   . LYS A  1 485 ? 23.586  -19.118 52.115   1.00 225.87 ? 485  LYS A C   1 
ATOM   3665  O  O   . LYS A  1 485 ? 22.545  -18.811 51.528   1.00 222.04 ? 485  LYS A O   1 
ATOM   3666  C  CB  . LYS A  1 485 ? 22.476  -21.096 53.234   1.00 203.87 ? 485  LYS A CB  1 
ATOM   3667  C  CG  . LYS A  1 485 ? 22.802  -22.209 52.242   1.00 206.37 ? 485  LYS A CG  1 
ATOM   3668  C  CD  . LYS A  1 485 ? 21.846  -23.386 52.390   1.00 200.82 ? 485  LYS A CD  1 
ATOM   3669  C  CE  . LYS A  1 485 ? 22.243  -24.543 51.481   1.00 204.52 ? 485  LYS A CE  1 
ATOM   3670  N  NZ  . LYS A  1 485 ? 21.332  -25.715 51.618   1.00 203.41 ? 485  LYS A NZ  1 
ATOM   3671  N  N   . GLY A  1 486 ? 24.787  -18.711 51.727   1.00 242.73 ? 486  GLY A N   1 
ATOM   3672  C  CA  . GLY A  1 486 ? 25.024  -17.787 50.625   1.00 245.93 ? 486  GLY A CA  1 
ATOM   3673  C  C   . GLY A  1 486 ? 26.428  -17.209 50.733   1.00 241.56 ? 486  GLY A C   1 
ATOM   3674  O  O   . GLY A  1 486 ? 27.330  -17.842 51.283   1.00 238.91 ? 486  GLY A O   1 
ATOM   3675  N  N   . VAL A  1 487 ? 26.597  -16.000 50.204   1.00 236.85 ? 487  VAL A N   1 
ATOM   3676  C  CA  . VAL A  1 487 ? 27.867  -15.279 50.302   1.00 235.38 ? 487  VAL A CA  1 
ATOM   3677  C  C   . VAL A  1 487 ? 27.720  -14.253 51.421   1.00 231.22 ? 487  VAL A C   1 
ATOM   3678  O  O   . VAL A  1 487 ? 27.104  -13.200 51.242   1.00 228.49 ? 487  VAL A O   1 
ATOM   3679  C  CB  . VAL A  1 487 ? 28.264  -14.625 48.977   1.00 230.05 ? 487  VAL A CB  1 
ATOM   3680  C  CG1 . VAL A  1 487 ? 29.515  -13.774 49.157   1.00 241.16 ? 487  VAL A CG1 1 
ATOM   3681  C  CG2 . VAL A  1 487 ? 28.501  -15.684 47.909   1.00 224.30 ? 487  VAL A CG2 1 
ATOM   3682  N  N   . LEU A  1 488 ? 28.285  -14.563 52.583   1.00 249.38 ? 488  LEU A N   1 
ATOM   3683  C  CA  . LEU A  1 488 ? 28.287  -13.682 53.740   1.00 260.44 ? 488  LEU A CA  1 
ATOM   3684  C  C   . LEU A  1 488 ? 29.610  -13.853 54.471   1.00 259.57 ? 488  LEU A C   1 
ATOM   3685  O  O   . LEU A  1 488 ? 30.258  -14.900 54.354   1.00 251.70 ? 488  LEU A O   1 
ATOM   3686  C  CB  . LEU A  1 488 ? 27.099  -13.971 54.676   1.00 262.06 ? 488  LEU A CB  1 
ATOM   3687  C  CG  . LEU A  1 488 ? 26.835  -15.358 55.271   1.00 264.42 ? 488  LEU A CG  1 
ATOM   3688  C  CD1 . LEU A  1 488 ? 26.027  -15.223 56.550   1.00 264.23 ? 488  LEU A CD1 1 
ATOM   3689  C  CD2 . LEU A  1 488 ? 26.097  -16.260 54.295   1.00 245.37 ? 488  LEU A CD2 1 
ATOM   3690  N  N   . PRO A  1 489 ? 30.048  -12.839 55.219   1.00 257.92 ? 489  PRO A N   1 
ATOM   3691  C  CA  . PRO A  1 489 ? 31.293  -12.971 55.991   1.00 250.14 ? 489  PRO A CA  1 
ATOM   3692  C  C   . PRO A  1 489 ? 31.172  -14.034 57.071   1.00 249.86 ? 489  PRO A C   1 
ATOM   3693  O  O   . PRO A  1 489 ? 30.082  -14.490 57.423   1.00 249.57 ? 489  PRO A O   1 
ATOM   3694  C  CB  . PRO A  1 489 ? 31.493  -11.579 56.598   1.00 247.46 ? 489  PRO A CB  1 
ATOM   3695  C  CG  . PRO A  1 489 ? 30.138  -10.967 56.599   1.00 250.43 ? 489  PRO A CG  1 
ATOM   3696  C  CD  . PRO A  1 489 ? 29.445  -11.506 55.383   1.00 259.75 ? 489  PRO A CD  1 
ATOM   3697  N  N   . ARG A  1 490 ? 32.328  -14.431 57.610   1.00 244.12 ? 490  ARG A N   1 
ATOM   3698  C  CA  . ARG A  1 490 ? 32.334  -15.428 58.678   1.00 241.86 ? 490  ARG A CA  1 
ATOM   3699  C  C   . ARG A  1 490 ? 32.016  -14.800 60.030   1.00 239.31 ? 490  ARG A C   1 
ATOM   3700  O  O   . ARG A  1 490 ? 31.228  -15.349 60.809   1.00 242.42 ? 490  ARG A O   1 
ATOM   3701  C  CB  . ARG A  1 490 ? 33.691  -16.144 58.734   1.00 247.60 ? 490  ARG A CB  1 
ATOM   3702  C  CG  . ARG A  1 490 ? 33.830  -17.307 57.755   1.00 257.53 ? 490  ARG A CG  1 
ATOM   3703  C  CD  . ARG A  1 490 ? 32.847  -18.432 58.065   1.00 253.18 ? 490  ARG A CD  1 
ATOM   3704  N  NE  . ARG A  1 490 ? 32.864  -19.471 57.037   1.00 257.19 ? 490  ARG A NE  1 
ATOM   3705  C  CZ  . ARG A  1 490 ? 32.003  -20.483 56.978   1.00 256.84 ? 490  ARG A CZ  1 
ATOM   3706  N  NH1 . ARG A  1 490 ? 31.046  -20.600 57.890   1.00 256.22 ? 490  ARG A NH1 1 
ATOM   3707  N  NH2 . ARG A  1 490 ? 32.096  -21.377 56.003   1.00 262.27 ? 490  ARG A NH2 1 
ATOM   3708  N  N   . LYS A  1 491 ? 32.608  -13.644 60.317   1.00 235.29 ? 491  LYS A N   1 
ATOM   3709  C  CA  . LYS A  1 491 ? 32.498  -13.025 61.635   1.00 240.76 ? 491  LYS A CA  1 
ATOM   3710  C  C   . LYS A  1 491 ? 31.237  -12.169 61.701   1.00 242.02 ? 491  LYS A C   1 
ATOM   3711  O  O   . LYS A  1 491 ? 31.166  -11.102 61.081   1.00 242.39 ? 491  LYS A O   1 
ATOM   3712  C  CB  . LYS A  1 491 ? 33.748  -12.206 61.928   1.00 245.42 ? 491  LYS A CB  1 
ATOM   3713  C  CG  . LYS A  1 491 ? 35.035  -13.013 61.825   1.00 248.43 ? 491  LYS A CG  1 
ATOM   3714  C  CD  . LYS A  1 491 ? 35.003  -14.199 62.765   1.00 246.13 ? 491  LYS A CD  1 
ATOM   3715  C  CE  . LYS A  1 491 ? 36.232  -15.069 62.599   1.00 260.24 ? 491  LYS A CE  1 
ATOM   3716  N  NZ  . LYS A  1 491 ? 36.202  -16.228 63.531   1.00 262.70 ? 491  LYS A NZ  1 
ATOM   3717  N  N   . LEU A  1 492 ? 30.236  -12.645 62.441   1.00 240.35 ? 492  LEU A N   1 
ATOM   3718  C  CA  . LEU A  1 492 ? 29.005  -11.904 62.697   1.00 242.21 ? 492  LEU A CA  1 
ATOM   3719  C  C   . LEU A  1 492 ? 29.027  -11.360 64.124   1.00 243.46 ? 492  LEU A C   1 
ATOM   3720  O  O   . LEU A  1 492 ? 29.083  -12.134 65.087   1.00 248.18 ? 492  LEU A O   1 
ATOM   3721  C  CB  . LEU A  1 492 ? 27.783  -12.798 62.479   1.00 239.55 ? 492  LEU A CB  1 
ATOM   3722  C  CG  . LEU A  1 492 ? 27.646  -13.513 61.129   1.00 237.99 ? 492  LEU A CG  1 
ATOM   3723  C  CD1 . LEU A  1 492 ? 26.501  -14.520 61.177   1.00 242.54 ? 492  LEU A CD1 1 
ATOM   3724  C  CD2 . LEU A  1 492 ? 27.445  -12.519 59.992   1.00 234.48 ? 492  LEU A CD2 1 
ATOM   3725  N  N   . ASN A  1 493 ? 28.984  -10.033 64.257   1.00 242.68 ? 493  ASN A N   1 
ATOM   3726  C  CA  . ASN A  1 493 ? 29.022  -9.368  65.558   1.00 254.92 ? 493  ASN A CA  1 
ATOM   3727  C  C   . ASN A  1 493 ? 27.616  -9.246  66.139   1.00 248.41 ? 493  ASN A C   1 
ATOM   3728  O  O   . ASN A  1 493 ? 26.757  -8.570  65.563   1.00 246.55 ? 493  ASN A O   1 
ATOM   3729  C  CB  . ASN A  1 493 ? 29.663  -7.986  65.438   1.00 263.46 ? 493  ASN A CB  1 
ATOM   3730  C  CG  . ASN A  1 493 ? 31.171  -8.048  65.313   1.00 266.81 ? 493  ASN A CG  1 
ATOM   3731  O  OD1 . ASN A  1 493 ? 31.732  -9.069  64.914   1.00 278.21 ? 493  ASN A OD1 1 
ATOM   3732  N  ND2 . ASN A  1 493 ? 31.838  -6.953  65.661   1.00 250.58 ? 493  ASN A ND2 1 
ATOM   3733  N  N   . PHE A  1 494 ? 27.398  -9.861  67.299   1.00 249.90 ? 494  PHE A N   1 
ATOM   3734  C  CA  . PHE A  1 494 ? 26.114  -9.838  67.988   1.00 247.58 ? 494  PHE A CA  1 
ATOM   3735  C  C   . PHE A  1 494 ? 26.164  -8.916  69.198   1.00 259.70 ? 494  PHE A C   1 
ATOM   3736  O  O   . PHE A  1 494 ? 27.193  -8.814  69.875   1.00 274.42 ? 494  PHE A O   1 
ATOM   3737  C  CB  . PHE A  1 494 ? 25.710  -11.242 68.433   1.00 246.01 ? 494  PHE A CB  1 
ATOM   3738  C  CG  . PHE A  1 494 ? 25.196  -12.097 67.325   1.00 243.82 ? 494  PHE A CG  1 
ATOM   3739  C  CD1 . PHE A  1 494 ? 26.072  -12.720 66.458   1.00 249.36 ? 494  PHE A CD1 1 
ATOM   3740  C  CD2 . PHE A  1 494 ? 23.837  -12.285 67.154   1.00 243.82 ? 494  PHE A CD2 1 
ATOM   3741  C  CE1 . PHE A  1 494 ? 25.605  -13.504 65.432   1.00 252.63 ? 494  PHE A CE1 1 
ATOM   3742  C  CE2 . PHE A  1 494 ? 23.363  -13.073 66.132   1.00 246.90 ? 494  PHE A CE2 1 
ATOM   3743  C  CZ  . PHE A  1 494 ? 24.249  -13.685 65.270   1.00 248.73 ? 494  PHE A CZ  1 
ATOM   3744  N  N   . GLN A  1 495 ? 25.041  -8.255  69.470   1.00 264.47 ? 495  GLN A N   1 
ATOM   3745  C  CA  . GLN A  1 495 ? 24.849  -7.463  70.681   1.00 278.76 ? 495  GLN A CA  1 
ATOM   3746  C  C   . GLN A  1 495 ? 23.803  -8.166  71.537   1.00 274.52 ? 495  GLN A C   1 
ATOM   3747  O  O   . GLN A  1 495 ? 22.634  -8.251  71.148   1.00 275.76 ? 495  GLN A O   1 
ATOM   3748  C  CB  . GLN A  1 495 ? 24.409  -6.039  70.351   1.00 284.57 ? 495  GLN A CB  1 
ATOM   3749  C  CG  . GLN A  1 495 ? 25.399  -5.234  69.527   1.00 296.37 ? 495  GLN A CG  1 
ATOM   3750  C  CD  . GLN A  1 495 ? 24.979  -3.783  69.382   1.00 298.58 ? 495  GLN A CD  1 
ATOM   3751  O  OE1 . GLN A  1 495 ? 25.620  -3.006  68.675   1.00 312.50 ? 495  GLN A OE1 1 
ATOM   3752  N  NE2 . GLN A  1 495 ? 23.897  -3.412  70.058   1.00 288.87 ? 495  GLN A NE2 1 
ATOM   3753  N  N   . VAL A  1 496 ? 24.220  -8.682  72.691   1.00 266.61 ? 496  VAL A N   1 
ATOM   3754  C  CA  . VAL A  1 496 ? 23.353  -9.477  73.556   1.00 256.09 ? 496  VAL A CA  1 
ATOM   3755  C  C   . VAL A  1 496 ? 23.075  -8.695  74.835   1.00 257.64 ? 496  VAL A C   1 
ATOM   3756  O  O   . VAL A  1 496 ? 24.004  -8.184  75.474   1.00 261.55 ? 496  VAL A O   1 
ATOM   3757  C  CB  . VAL A  1 496 ? 23.980  -10.846 73.864   1.00 250.23 ? 496  VAL A CB  1 
ATOM   3758  C  CG1 . VAL A  1 496 ? 23.050  -11.670 74.728   1.00 248.69 ? 496  VAL A CG1 1 
ATOM   3759  C  CG2 . VAL A  1 496 ? 24.303  -11.582 72.571   1.00 253.41 ? 496  VAL A CG2 1 
ATOM   3760  N  N   . GLU A  1 497 ? 21.796  -8.602  75.205   1.00 253.30 ? 497  GLU A N   1 
ATOM   3761  C  CA  . GLU A  1 497 ? 21.361  -7.975  76.446   1.00 250.13 ? 497  GLU A CA  1 
ATOM   3762  C  C   . GLU A  1 497 ? 20.624  -8.995  77.301   1.00 248.34 ? 497  GLU A C   1 
ATOM   3763  O  O   . GLU A  1 497 ? 19.813  -9.776  76.794   1.00 251.40 ? 497  GLU A O   1 
ATOM   3764  C  CB  . GLU A  1 497 ? 20.449  -6.763  76.187   1.00 250.35 ? 497  GLU A CB  1 
ATOM   3765  C  CG  . GLU A  1 497 ? 20.862  -5.891  75.011   1.00 256.46 ? 497  GLU A CG  1 
ATOM   3766  C  CD  . GLU A  1 497 ? 22.175  -5.165  75.244   1.00 251.94 ? 497  GLU A CD  1 
ATOM   3767  O  OE1 . GLU A  1 497 ? 22.944  -5.003  74.274   1.00 254.09 ? 497  GLU A OE1 1 
ATOM   3768  O  OE2 . GLU A  1 497 ? 22.445  -4.766  76.396   1.00 249.52 ? 497  GLU A OE2 1 
ATOM   3769  N  N   . LEU A  1 498 ? 20.901  -8.984  78.601   1.00 253.59 ? 498  LEU A N   1 
ATOM   3770  C  CA  . LEU A  1 498 ? 20.227  -9.854  79.555   1.00 257.02 ? 498  LEU A CA  1 
ATOM   3771  C  C   . LEU A  1 498 ? 19.585  -9.001  80.639   1.00 267.82 ? 498  LEU A C   1 
ATOM   3772  O  O   . LEU A  1 498 ? 20.212  -8.068  81.152   1.00 271.22 ? 498  LEU A O   1 
ATOM   3773  C  CB  . LEU A  1 498 ? 21.204  -10.865 80.169   1.00 255.40 ? 498  LEU A CB  1 
ATOM   3774  C  CG  . LEU A  1 498 ? 21.336  -12.241 79.507   1.00 250.57 ? 498  LEU A CG  1 
ATOM   3775  C  CD1 . LEU A  1 498 ? 21.814  -12.130 78.071   1.00 248.99 ? 498  LEU A CD1 1 
ATOM   3776  C  CD2 . LEU A  1 498 ? 22.289  -13.109 80.307   1.00 253.11 ? 498  LEU A CD2 1 
ATOM   3777  N  N   . LEU A  1 499 ? 18.333  -9.313  80.979   1.00 279.86 ? 499  LEU A N   1 
ATOM   3778  C  CA  . LEU A  1 499 ? 17.606  -8.612  82.034   1.00 282.98 ? 499  LEU A CA  1 
ATOM   3779  C  C   . LEU A  1 499 ? 17.053  -9.621  83.028   1.00 272.73 ? 499  LEU A C   1 
ATOM   3780  O  O   . LEU A  1 499 ? 16.259  -10.493 82.658   1.00 272.02 ? 499  LEU A O   1 
ATOM   3781  C  CB  . LEU A  1 499 ? 16.473  -7.757  81.459   1.00 293.73 ? 499  LEU A CB  1 
ATOM   3782  C  CG  . LEU A  1 499 ? 16.828  -6.770  80.344   1.00 300.51 ? 499  LEU A CG  1 
ATOM   3783  C  CD1 . LEU A  1 499 ? 15.568  -6.313  79.612   1.00 300.18 ? 499  LEU A CD1 1 
ATOM   3784  C  CD2 . LEU A  1 499 ? 17.581  -5.587  80.917   1.00 300.66 ? 499  LEU A CD2 1 
ATOM   3785  N  N   . LEU A  1 500 ? 17.464  -9.494  84.285   1.00 265.37 ? 500  LEU A N   1 
ATOM   3786  C  CA  . LEU A  1 500 ? 16.970  -10.347 85.355   1.00 267.23 ? 500  LEU A CA  1 
ATOM   3787  C  C   . LEU A  1 500 ? 15.697  -9.762  85.952   1.00 273.53 ? 500  LEU A C   1 
ATOM   3788  O  O   . LEU A  1 500 ? 15.578  -8.543  86.111   1.00 280.61 ? 500  LEU A O   1 
ATOM   3789  C  CB  . LEU A  1 500 ? 18.029  -10.504 86.447   1.00 267.07 ? 500  LEU A CB  1 
ATOM   3790  C  CG  . LEU A  1 500 ? 19.351  -11.169 86.062   1.00 273.54 ? 500  LEU A CG  1 
ATOM   3791  C  CD1 . LEU A  1 500 ? 20.385  -10.972 87.155   1.00 277.83 ? 500  LEU A CD1 1 
ATOM   3792  C  CD2 . LEU A  1 500 ? 19.147  -12.649 85.786   1.00 280.53 ? 500  LEU A CD2 1 
ATOM   3793  N  N   . ASP A  1 501 ? 14.749  -10.637 86.282   1.00 267.61 ? 501  ASP A N   1 
ATOM   3794  C  CA  . ASP A  1 501 ? 13.518  -10.238 86.960   1.00 261.54 ? 501  ASP A CA  1 
ATOM   3795  C  C   . ASP A  1 501 ? 12.799  -9.124  86.204   1.00 259.70 ? 501  ASP A C   1 
ATOM   3796  O  O   . ASP A  1 501 ? 12.455  -8.079  86.762   1.00 257.21 ? 501  ASP A O   1 
ATOM   3797  C  CB  . ASP A  1 501 ? 13.808  -9.816  88.399   1.00 266.41 ? 501  ASP A CB  1 
ATOM   3798  C  CG  . ASP A  1 501 ? 12.557  -9.727  89.239   1.00 270.62 ? 501  ASP A CG  1 
ATOM   3799  O  OD1 . ASP A  1 501 ? 11.602  -10.480 88.957   1.00 259.05 ? 501  ASP A OD1 1 
ATOM   3800  O  OD2 . ASP A  1 501 ? 12.529  -8.898  90.172   1.00 287.37 ? 501  ASP A OD2 1 
ATOM   3801  N  N   . LYS A  1 502 ? 12.583  -9.347  84.906   1.00 254.91 ? 502  LYS A N   1 
ATOM   3802  C  CA  . LYS A  1 502 ? 11.949  -8.316  84.090   1.00 256.18 ? 502  LYS A CA  1 
ATOM   3803  C  C   . LYS A  1 502 ? 10.507  -8.063  84.512   1.00 258.91 ? 502  LYS A C   1 
ATOM   3804  O  O   . LYS A  1 502 ? 10.045  -6.916  84.488   1.00 259.86 ? 502  LYS A O   1 
ATOM   3805  C  CB  . LYS A  1 502 ? 11.988  -8.687  82.612   1.00 252.92 ? 502  LYS A CB  1 
ATOM   3806  C  CG  . LYS A  1 502 ? 11.371  -7.587  81.781   1.00 254.24 ? 502  LYS A CG  1 
ATOM   3807  C  CD  . LYS A  1 502 ? 11.210  -7.925  80.329   1.00 247.14 ? 502  LYS A CD  1 
ATOM   3808  C  CE  . LYS A  1 502 ? 10.605  -6.730  79.626   1.00 248.44 ? 502  LYS A CE  1 
ATOM   3809  N  NZ  . LYS A  1 502 ? 11.511  -5.553  79.673   1.00 249.86 ? 502  LYS A NZ  1 
ATOM   3810  N  N   . LEU A  1 503 ? 9.776   -9.121  84.874   1.00 262.50 ? 503  LEU A N   1 
ATOM   3811  C  CA  . LEU A  1 503 ? 8.357   -9.044  85.216   1.00 265.61 ? 503  LEU A CA  1 
ATOM   3812  C  C   . LEU A  1 503 ? 8.028   -7.850  86.106   1.00 274.12 ? 503  LEU A C   1 
ATOM   3813  O  O   . LEU A  1 503 ? 6.924   -7.300  86.033   1.00 276.14 ? 503  LEU A O   1 
ATOM   3814  C  CB  . LEU A  1 503 ? 7.906   -10.340 85.895   1.00 267.72 ? 503  LEU A CB  1 
ATOM   3815  C  CG  . LEU A  1 503 ? 7.267   -11.419 85.014   1.00 264.71 ? 503  LEU A CG  1 
ATOM   3816  C  CD1 . LEU A  1 503 ? 8.014   -11.585 83.694   1.00 262.30 ? 503  LEU A CD1 1 
ATOM   3817  C  CD2 . LEU A  1 503 ? 7.182   -12.743 85.760   1.00 263.46 ? 503  LEU A CD2 1 
ATOM   3818  N  N   . LYS A  1 504 ? 8.979   -7.441  86.946   1.00 279.39 ? 504  LYS A N   1 
ATOM   3819  C  CA  . LYS A  1 504 ? 8.848   -6.224  87.744   1.00 281.10 ? 504  LYS A CA  1 
ATOM   3820  C  C   . LYS A  1 504 ? 9.075   -5.009  86.848   1.00 282.44 ? 504  LYS A C   1 
ATOM   3821  O  O   . LYS A  1 504 ? 10.193  -4.777  86.375   1.00 279.24 ? 504  LYS A O   1 
ATOM   3822  C  CB  . LYS A  1 504 ? 9.833   -6.241  88.908   1.00 276.65 ? 504  LYS A CB  1 
ATOM   3823  C  CG  . LYS A  1 504 ? 9.520   -7.271  89.987   1.00 273.66 ? 504  LYS A CG  1 
ATOM   3824  C  CD  . LYS A  1 504 ? 8.215   -6.953  90.702   1.00 269.46 ? 504  LYS A CD  1 
ATOM   3825  C  CE  . LYS A  1 504 ? 7.993   -7.884  91.883   1.00 265.99 ? 504  LYS A CE  1 
ATOM   3826  N  NZ  . LYS A  1 504 ? 6.743   -7.553  92.618   1.00 266.24 ? 504  LYS A NZ  1 
ATOM   3827  N  N   . GLN A  1 505 ? 8.011   -4.245  86.602   1.00 288.64 ? 505  GLN A N   1 
ATOM   3828  C  CA  . GLN A  1 505 ? 8.102   -3.039  85.791   1.00 288.03 ? 505  GLN A CA  1 
ATOM   3829  C  C   . GLN A  1 505 ? 9.007   -2.004  86.461   1.00 294.57 ? 505  GLN A C   1 
ATOM   3830  O  O   . GLN A  1 505 ? 9.284   -2.063  87.662   1.00 308.96 ? 505  GLN A O   1 
ATOM   3831  C  CB  . GLN A  1 505 ? 6.709   -2.450  85.555   1.00 282.00 ? 505  GLN A CB  1 
ATOM   3832  C  CG  . GLN A  1 505 ? 5.756   -3.362  84.777   1.00 274.76 ? 505  GLN A CG  1 
ATOM   3833  C  CD  . GLN A  1 505 ? 6.093   -3.469  83.297   1.00 264.39 ? 505  GLN A CD  1 
ATOM   3834  O  OE1 . GLN A  1 505 ? 6.939   -2.739  82.782   1.00 266.63 ? 505  GLN A OE1 1 
ATOM   3835  N  NE2 . GLN A  1 505 ? 5.420   -4.382  82.606   1.00 258.07 ? 505  GLN A NE2 1 
ATOM   3836  N  N   . LYS A  1 506 ? 9.470   -1.042  85.659   1.00 271.64 ? 506  LYS A N   1 
ATOM   3837  C  CA  . LYS A  1 506 ? 10.348  0.017   86.145   1.00 258.98 ? 506  LYS A CA  1 
ATOM   3838  C  C   . LYS A  1 506 ? 9.691   0.831   87.254   1.00 268.32 ? 506  LYS A C   1 
ATOM   3839  O  O   . LYS A  1 506 ? 8.830   1.678   86.991   1.00 277.18 ? 506  LYS A O   1 
ATOM   3840  C  CB  . LYS A  1 506 ? 10.766  0.931   84.993   1.00 247.55 ? 506  LYS A CB  1 
ATOM   3841  C  CG  . LYS A  1 506 ? 11.853  1.911   85.371   1.00 249.01 ? 506  LYS A CG  1 
ATOM   3842  C  CD  . LYS A  1 506 ? 13.043  1.183   85.977   1.00 248.37 ? 506  LYS A CD  1 
ATOM   3843  C  CE  . LYS A  1 506 ? 14.149  2.154   86.351   1.00 251.31 ? 506  LYS A CE  1 
ATOM   3844  N  NZ  . LYS A  1 506 ? 14.663  2.883   85.161   1.00 254.01 ? 506  LYS A NZ  1 
ATOM   3845  N  N   . GLY A  1 507 ? 10.093  0.573   88.496   1.00 256.78 ? 507  GLY A N   1 
ATOM   3846  C  CA  . GLY A  1 507 ? 9.573   1.284   89.648   1.00 250.08 ? 507  GLY A CA  1 
ATOM   3847  C  C   . GLY A  1 507 ? 9.273   0.334   90.788   1.00 243.11 ? 507  GLY A C   1 
ATOM   3848  O  O   . GLY A  1 507 ? 9.129   0.746   91.943   1.00 242.12 ? 507  GLY A O   1 
ATOM   3849  N  N   . ALA A  1 508 ? 9.171   -0.952  90.460   1.00 248.21 ? 508  ALA A N   1 
ATOM   3850  C  CA  . ALA A  1 508 ? 8.855   -1.984  91.438   1.00 246.62 ? 508  ALA A CA  1 
ATOM   3851  C  C   . ALA A  1 508 ? 10.058  -2.303  92.313   1.00 249.40 ? 508  ALA A C   1 
ATOM   3852  O  O   . ALA A  1 508 ? 10.978  -1.488  92.443   1.00 246.98 ? 508  ALA A O   1 
ATOM   3853  C  CB  . ALA A  1 508 ? 8.361   -3.252  90.742   1.00 243.13 ? 508  ALA A CB  1 
ATOM   3854  N  N   . ILE A  1 509 ? 10.051  -3.484  92.924   1.00 263.18 ? 509  ILE A N   1 
ATOM   3855  C  CA  . ILE A  1 509 ? 11.140  -3.950  93.774   1.00 271.14 ? 509  ILE A CA  1 
ATOM   3856  C  C   . ILE A  1 509 ? 11.836  -5.103  93.055   1.00 267.14 ? 509  ILE A C   1 
ATOM   3857  O  O   . ILE A  1 509 ? 11.239  -6.163  92.823   1.00 259.88 ? 509  ILE A O   1 
ATOM   3858  C  CB  . ILE A  1 509 ? 10.636  -4.363  95.162   1.00 266.61 ? 509  ILE A CB  1 
ATOM   3859  C  CG1 . ILE A  1 509 ? 11.729  -5.111  95.928   1.00 258.78 ? 509  ILE A CG1 1 
ATOM   3860  C  CG2 . ILE A  1 509 ? 9.342   -5.169  95.062   1.00 267.20 ? 509  ILE A CG2 1 
ATOM   3861  C  CD1 . ILE A  1 509 ? 12.917  -4.255  96.290   1.00 255.20 ? 509  ILE A CD1 1 
ATOM   3862  N  N   . ARG A  1 510 ? 13.092  -4.884  92.673   1.00 275.99 ? 510  ARG A N   1 
ATOM   3863  C  CA  . ARG A  1 510 ? 13.872  -5.856  91.921   1.00 276.90 ? 510  ARG A CA  1 
ATOM   3864  C  C   . ARG A  1 510 ? 14.578  -6.791  92.896   1.00 282.61 ? 510  ARG A C   1 
ATOM   3865  O  O   . ARG A  1 510 ? 14.808  -6.445  94.056   1.00 292.19 ? 510  ARG A O   1 
ATOM   3866  C  CB  . ARG A  1 510 ? 14.888  -5.148  91.015   1.00 275.10 ? 510  ARG A CB  1 
ATOM   3867  C  CG  . ARG A  1 510 ? 15.431  -5.993  89.864   1.00 269.18 ? 510  ARG A CG  1 
ATOM   3868  C  CD  . ARG A  1 510 ? 14.392  -6.159  88.761   1.00 265.51 ? 510  ARG A CD  1 
ATOM   3869  N  NE  . ARG A  1 510 ? 14.004  -4.875  88.183   1.00 267.00 ? 510  ARG A NE  1 
ATOM   3870  C  CZ  . ARG A  1 510 ? 13.316  -4.737  87.054   1.00 264.07 ? 510  ARG A CZ  1 
ATOM   3871  N  NH1 . ARG A  1 510 ? 12.933  -5.807  86.371   1.00 259.23 ? 510  ARG A NH1 1 
ATOM   3872  N  NH2 . ARG A  1 510 ? 13.012  -3.527  86.603   1.00 267.73 ? 510  ARG A NH2 1 
ATOM   3873  N  N   . ARG A  1 511 ? 14.920  -7.994  92.418   1.00 280.99 ? 511  ARG A N   1 
ATOM   3874  C  CA  . ARG A  1 511 ? 15.489  -9.013  93.292   1.00 275.66 ? 511  ARG A CA  1 
ATOM   3875  C  C   . ARG A  1 511 ? 16.737  -9.711  92.761   1.00 275.43 ? 511  ARG A C   1 
ATOM   3876  O  O   . ARG A  1 511 ? 17.284  -10.568 93.467   1.00 269.17 ? 511  ARG A O   1 
ATOM   3877  C  CB  . ARG A  1 511 ? 14.429  -10.079 93.615   1.00 269.60 ? 511  ARG A CB  1 
ATOM   3878  C  CG  . ARG A  1 511 ? 13.207  -9.523  94.326   1.00 271.24 ? 511  ARG A CG  1 
ATOM   3879  C  CD  . ARG A  1 511 ? 12.000  -10.413 94.131   1.00 269.40 ? 511  ARG A CD  1 
ATOM   3880  N  NE  . ARG A  1 511 ? 11.652  -10.545 92.723   1.00 276.74 ? 511  ARG A NE  1 
ATOM   3881  C  CZ  . ARG A  1 511 ? 10.656  -11.296 92.272   1.00 289.29 ? 511  ARG A CZ  1 
ATOM   3882  N  NH1 . ARG A  1 511 ? 9.909   -11.987 93.123   1.00 288.03 ? 511  ARG A NH1 1 
ATOM   3883  N  NH2 . ARG A  1 511 ? 10.408  -11.360 90.970   1.00 294.29 ? 511  ARG A NH2 1 
ATOM   3884  N  N   . ALA A  1 512 ? 17.202  -9.393  91.556   1.00 285.55 ? 512  ALA A N   1 
ATOM   3885  C  CA  . ALA A  1 512 ? 18.387  -10.035 91.007   1.00 283.64 ? 512  ALA A CA  1 
ATOM   3886  C  C   . ALA A  1 512 ? 19.306  -9.000  90.373   1.00 297.71 ? 512  ALA A C   1 
ATOM   3887  O  O   . ALA A  1 512 ? 18.857  -7.949  89.905   1.00 310.57 ? 512  ALA A O   1 
ATOM   3888  C  CB  . ALA A  1 512 ? 18.015  -11.107 89.976   1.00 271.58 ? 512  ALA A CB  1 
ATOM   3889  N  N   . LEU A  1 513 ? 20.598  -9.326  90.344   1.00 290.08 ? 513  LEU A N   1 
ATOM   3890  C  CA  . LEU A  1 513 ? 21.626  -8.493  89.734   1.00 289.77 ? 513  LEU A CA  1 
ATOM   3891  C  C   . LEU A  1 513 ? 22.935  -9.271  89.742   1.00 285.95 ? 513  LEU A C   1 
ATOM   3892  O  O   . LEU A  1 513 ? 23.212  -10.010 90.690   1.00 280.02 ? 513  LEU A O   1 
ATOM   3893  C  CB  . LEU A  1 513 ? 21.786  -7.146  90.463   1.00 283.67 ? 513  LEU A CB  1 
ATOM   3894  C  CG  . LEU A  1 513 ? 22.310  -7.070  91.898   1.00 270.45 ? 513  LEU A CG  1 
ATOM   3895  C  CD1 . LEU A  1 513 ? 23.807  -6.815  91.908   1.00 271.04 ? 513  LEU A CD1 1 
ATOM   3896  C  CD2 . LEU A  1 513 ? 21.585  -5.980  92.662   1.00 270.03 ? 513  LEU A CD2 1 
ATOM   3897  N  N   . PHE A  1 514 ? 23.712  -9.122  88.669   1.00 283.16 ? 514  PHE A N   1 
ATOM   3898  C  CA  . PHE A  1 514 ? 24.907  -9.929  88.466   1.00 280.37 ? 514  PHE A CA  1 
ATOM   3899  C  C   . PHE A  1 514 ? 25.916  -9.730  89.597   1.00 285.74 ? 514  PHE A C   1 
ATOM   3900  O  O   . PHE A  1 514 ? 25.894  -8.736  90.328   1.00 286.29 ? 514  PHE A O   1 
ATOM   3901  C  CB  . PHE A  1 514 ? 25.551  -9.607  87.116   1.00 270.03 ? 514  PHE A CB  1 
ATOM   3902  C  CG  . PHE A  1 514 ? 24.747  -10.074 85.929   1.00 264.68 ? 514  PHE A CG  1 
ATOM   3903  C  CD1 . PHE A  1 514 ? 23.548  -9.466  85.591   1.00 263.15 ? 514  PHE A CD1 1 
ATOM   3904  C  CD2 . PHE A  1 514 ? 25.189  -11.138 85.161   1.00 260.89 ? 514  PHE A CD2 1 
ATOM   3905  C  CE1 . PHE A  1 514 ? 22.812  -9.906  84.503   1.00 255.28 ? 514  PHE A CE1 1 
ATOM   3906  C  CE2 . PHE A  1 514 ? 24.460  -11.581 84.074   1.00 255.52 ? 514  PHE A CE2 1 
ATOM   3907  C  CZ  . PHE A  1 514 ? 23.269  -10.965 83.745   1.00 252.37 ? 514  PHE A CZ  1 
ATOM   3908  N  N   . LEU A  1 515 ? 26.823  -10.703 89.721   1.00 284.09 ? 515  LEU A N   1 
ATOM   3909  C  CA  . LEU A  1 515 ? 27.728  -10.748 90.867   1.00 275.59 ? 515  LEU A CA  1 
ATOM   3910  C  C   . LEU A  1 515 ? 28.768  -9.636  90.800   1.00 268.44 ? 515  LEU A C   1 
ATOM   3911  O  O   . LEU A  1 515 ? 28.964  -8.898  91.772   1.00 272.52 ? 515  LEU A O   1 
ATOM   3912  C  CB  . LEU A  1 515 ? 28.404  -12.118 90.940   1.00 275.55 ? 515  LEU A CB  1 
ATOM   3913  C  CG  . LEU A  1 515 ? 29.312  -12.393 92.141   1.00 277.45 ? 515  LEU A CG  1 
ATOM   3914  C  CD1 . LEU A  1 515 ? 28.525  -12.332 93.441   1.00 275.19 ? 515  LEU A CD1 1 
ATOM   3915  C  CD2 . LEU A  1 515 ? 29.998  -13.742 91.995   1.00 281.43 ? 515  LEU A CD2 1 
ATOM   3916  N  N   . TYR A  1 516 ? 29.444  -9.496  89.660   1.00 265.52 ? 516  TYR A N   1 
ATOM   3917  C  CA  . TYR A  1 516 ? 30.487  -8.490  89.511   1.00 269.83 ? 516  TYR A CA  1 
ATOM   3918  C  C   . TYR A  1 516 ? 29.995  -7.224  88.827   1.00 274.72 ? 516  TYR A C   1 
ATOM   3919  O  O   . TYR A  1 516 ? 30.490  -6.134  89.136   1.00 279.53 ? 516  TYR A O   1 
ATOM   3920  C  CB  . TYR A  1 516 ? 31.674  -9.064  88.724   1.00 272.98 ? 516  TYR A CB  1 
ATOM   3921  C  CG  . TYR A  1 516 ? 33.010  -8.411  89.033   1.00 273.72 ? 516  TYR A CG  1 
ATOM   3922  C  CD1 . TYR A  1 516 ? 33.126  -7.436  90.020   1.00 269.65 ? 516  TYR A CD1 1 
ATOM   3923  C  CD2 . TYR A  1 516 ? 34.155  -8.769  88.333   1.00 275.03 ? 516  TYR A CD2 1 
ATOM   3924  C  CE1 . TYR A  1 516 ? 34.346  -6.840  90.299   1.00 270.18 ? 516  TYR A CE1 1 
ATOM   3925  C  CE2 . TYR A  1 516 ? 35.375  -8.178  88.605   1.00 273.07 ? 516  TYR A CE2 1 
ATOM   3926  C  CZ  . TYR A  1 516 ? 35.466  -7.215  89.589   1.00 267.41 ? 516  TYR A CZ  1 
ATOM   3927  O  OH  . TYR A  1 516 ? 36.681  -6.626  89.861   1.00 261.69 ? 516  TYR A OH  1 
ATOM   3928  N  N   . SER A  1 517 ? 29.033  -7.340  87.908   1.00 273.76 ? 517  SER A N   1 
ATOM   3929  C  CA  . SER A  1 517 ? 28.505  -6.166  87.224   1.00 276.07 ? 517  SER A CA  1 
ATOM   3930  C  C   . SER A  1 517 ? 27.729  -5.251  88.163   1.00 282.99 ? 517  SER A C   1 
ATOM   3931  O  O   . SER A  1 517 ? 27.588  -4.059  87.864   1.00 289.42 ? 517  SER A O   1 
ATOM   3932  C  CB  . SER A  1 517 ? 27.616  -6.590  86.051   1.00 266.38 ? 517  SER A CB  1 
ATOM   3933  O  OG  . SER A  1 517 ? 27.119  -5.462  85.349   1.00 264.48 ? 517  SER A OG  1 
ATOM   3934  N  N   . ARG A  1 518 ? 27.224  -5.780  89.280   1.00 274.47 ? 518  ARG A N   1 
ATOM   3935  C  CA  . ARG A  1 518 ? 26.444  -5.010  90.253   1.00 268.93 ? 518  ARG A CA  1 
ATOM   3936  C  C   . ARG A  1 518 ? 25.278  -4.285  89.587   1.00 267.87 ? 518  ARG A C   1 
ATOM   3937  O  O   . ARG A  1 518 ? 24.916  -3.168  89.962   1.00 264.14 ? 518  ARG A O   1 
ATOM   3938  C  CB  . ARG A  1 518 ? 27.325  -4.016  91.011   1.00 278.85 ? 518  ARG A CB  1 
ATOM   3939  C  CG  . ARG A  1 518 ? 28.699  -4.539  91.386   1.00 284.18 ? 518  ARG A CG  1 
ATOM   3940  C  CD  . ARG A  1 518 ? 28.600  -5.771  92.260   1.00 277.76 ? 518  ARG A CD  1 
ATOM   3941  N  NE  . ARG A  1 518 ? 29.818  -5.982  93.035   1.00 275.99 ? 518  ARG A NE  1 
ATOM   3942  C  CZ  . ARG A  1 518 ? 30.033  -5.441  94.228   1.00 271.64 ? 518  ARG A CZ  1 
ATOM   3943  N  NH1 . ARG A  1 518 ? 29.108  -4.660  94.766   1.00 271.53 ? 518  ARG A NH1 1 
ATOM   3944  N  NH2 . ARG A  1 518 ? 31.164  -5.678  94.878   1.00 267.33 ? 518  ARG A NH2 1 
ATOM   3945  N  N   . SER A  1 519 ? 24.673  -4.932  88.597   1.00 279.36 ? 519  SER A N   1 
ATOM   3946  C  CA  . SER A  1 519 ? 23.651  -4.280  87.792   1.00 281.03 ? 519  SER A CA  1 
ATOM   3947  C  C   . SER A  1 519 ? 22.716  -5.333  87.213   1.00 277.57 ? 519  SER A C   1 
ATOM   3948  O  O   . SER A  1 519 ? 23.179  -6.301  86.594   1.00 269.89 ? 519  SER A O   1 
ATOM   3949  C  CB  . SER A  1 519 ? 24.301  -3.445  86.684   1.00 279.34 ? 519  SER A CB  1 
ATOM   3950  O  OG  . SER A  1 519 ? 23.330  -2.780  85.895   1.00 269.46 ? 519  SER A OG  1 
ATOM   3951  N  N   . PRO A  1 520 ? 21.390  -5.183  87.413   1.00 285.77 ? 520  PRO A N   1 
ATOM   3952  C  CA  . PRO A  1 520 ? 20.431  -6.210  86.977   1.00 281.74 ? 520  PRO A CA  1 
ATOM   3953  C  C   . PRO A  1 520 ? 20.552  -6.594  85.510   1.00 274.45 ? 520  PRO A C   1 
ATOM   3954  O  O   . PRO A  1 520 ? 20.001  -7.615  85.086   1.00 268.96 ? 520  PRO A O   1 
ATOM   3955  C  CB  . PRO A  1 520 ? 19.073  -5.554  87.264   1.00 277.83 ? 520  PRO A CB  1 
ATOM   3956  C  CG  . PRO A  1 520 ? 19.339  -4.631  88.407   1.00 277.79 ? 520  PRO A CG  1 
ATOM   3957  C  CD  . PRO A  1 520 ? 20.753  -4.133  88.227   1.00 283.48 ? 520  PRO A CD  1 
ATOM   3958  N  N   . SER A  1 521 ? 21.256  -5.782  84.727   1.00 269.56 ? 521  SER A N   1 
ATOM   3959  C  CA  . SER A  1 521 ? 21.445  -6.035  83.309   1.00 267.82 ? 521  SER A CA  1 
ATOM   3960  C  C   . SER A  1 521 ? 22.934  -6.096  82.996   1.00 272.88 ? 521  SER A C   1 
ATOM   3961  O  O   . SER A  1 521 ? 23.747  -5.412  83.625   1.00 272.21 ? 521  SER A O   1 
ATOM   3962  C  CB  . SER A  1 521 ? 20.774  -4.953  82.445   1.00 266.80 ? 521  SER A CB  1 
ATOM   3963  O  OG  . SER A  1 521 ? 21.178  -3.648  82.825   1.00 269.08 ? 521  SER A OG  1 
ATOM   3964  N  N   . HIS A  1 522 ? 23.285  -6.934  82.023   1.00 274.25 ? 522  HIS A N   1 
ATOM   3965  C  CA  . HIS A  1 522 ? 24.667  -7.087  81.590   1.00 276.60 ? 522  HIS A CA  1 
ATOM   3966  C  C   . HIS A  1 522 ? 24.705  -7.036  80.073   1.00 268.40 ? 522  HIS A C   1 
ATOM   3967  O  O   . HIS A  1 522 ? 24.017  -7.812  79.403   1.00 253.77 ? 522  HIS A O   1 
ATOM   3968  C  CB  . HIS A  1 522 ? 25.280  -8.404  82.094   1.00 270.74 ? 522  HIS A CB  1 
ATOM   3969  C  CG  . HIS A  1 522 ? 26.686  -8.637  81.627   1.00 268.11 ? 522  HIS A CG  1 
ATOM   3970  N  ND1 . HIS A  1 522 ? 26.988  -9.383  80.507   1.00 260.62 ? 522  HIS A ND1 1 
ATOM   3971  C  CD2 . HIS A  1 522 ? 27.872  -8.215  82.127   1.00 271.11 ? 522  HIS A CD2 1 
ATOM   3972  C  CE1 . HIS A  1 522 ? 28.298  -9.415  80.341   1.00 262.57 ? 522  HIS A CE1 1 
ATOM   3973  N  NE2 . HIS A  1 522 ? 28.858  -8.713  81.310   1.00 270.64 ? 522  HIS A NE2 1 
ATOM   3974  N  N   . SER A  1 523 ? 25.504  -6.123  79.538   1.00 268.82 ? 523  SER A N   1 
ATOM   3975  C  CA  . SER A  1 523 ? 25.686  -5.993  78.104   1.00 255.17 ? 523  SER A CA  1 
ATOM   3976  C  C   . SER A  1 523 ? 27.004  -6.641  77.708   1.00 261.56 ? 523  SER A C   1 
ATOM   3977  O  O   . SER A  1 523 ? 27.986  -6.593  78.453   1.00 267.41 ? 523  SER A O   1 
ATOM   3978  C  CB  . SER A  1 523 ? 25.675  -4.522  77.684   1.00 253.15 ? 523  SER A CB  1 
ATOM   3979  O  OG  . SER A  1 523 ? 25.796  -4.390  76.281   1.00 254.55 ? 523  SER A OG  1 
ATOM   3980  N  N   . LYS A  1 524 ? 27.017  -7.248  76.524   1.00 261.26 ? 524  LYS A N   1 
ATOM   3981  C  CA  . LYS A  1 524 ? 28.214  -7.907  76.025   1.00 262.89 ? 524  LYS A CA  1 
ATOM   3982  C  C   . LYS A  1 524 ? 28.181  -7.904  74.508   1.00 261.14 ? 524  LYS A C   1 
ATOM   3983  O  O   . LYS A  1 524 ? 27.194  -8.326  73.896   1.00 244.72 ? 524  LYS A O   1 
ATOM   3984  C  CB  . LYS A  1 524 ? 28.335  -9.342  76.550   1.00 251.00 ? 524  LYS A CB  1 
ATOM   3985  C  CG  . LYS A  1 524 ? 29.551  -10.092 76.013   1.00 246.16 ? 524  LYS A CG  1 
ATOM   3986  C  CD  . LYS A  1 524 ? 30.858  -9.417  76.418   1.00 240.39 ? 524  LYS A CD  1 
ATOM   3987  C  CE  . LYS A  1 524 ? 32.048  -9.996  75.664   1.00 237.35 ? 524  LYS A CE  1 
ATOM   3988  N  NZ  . LYS A  1 524 ? 32.280  -11.432 75.966   1.00 235.85 ? 524  LYS A NZ  1 
ATOM   3989  N  N   . ASN A  1 525 ? 29.264  -7.419  73.914   1.00 271.04 ? 525  ASN A N   1 
ATOM   3990  C  CA  . ASN A  1 525 ? 29.431  -7.404  72.470   1.00 260.50 ? 525  ASN A CA  1 
ATOM   3991  C  C   . ASN A  1 525 ? 30.069  -8.727  72.070   1.00 261.41 ? 525  ASN A C   1 
ATOM   3992  O  O   . ASN A  1 525 ? 31.131  -9.091  72.588   1.00 270.25 ? 525  ASN A O   1 
ATOM   3993  C  CB  . ASN A  1 525 ? 30.296  -6.203  72.081   1.00 270.52 ? 525  ASN A CB  1 
ATOM   3994  C  CG  . ASN A  1 525 ? 29.578  -4.893  72.337   1.00 296.78 ? 525  ASN A CG  1 
ATOM   3995  O  OD1 . ASN A  1 525 ? 28.355  -4.821  72.201   1.00 262.29 ? 525  ASN A OD1 1 
ATOM   3996  N  ND2 . ASN A  1 525 ? 30.309  -3.867  72.749   1.00 410.05 ? 525  ASN A ND2 1 
ATOM   3997  N  N   . MET A  1 526 ? 29.447  -9.427  71.122   1.00 252.08 ? 526  MET A N   1 
ATOM   3998  C  CA  . MET A  1 526 ? 29.807  -10.814 70.837   1.00 251.92 ? 526  MET A CA  1 
ATOM   3999  C  C   . MET A  1 526 ? 30.077  -11.014 69.355   1.00 246.39 ? 526  MET A C   1 
ATOM   4000  O  O   . MET A  1 526 ? 29.155  -10.968 68.536   1.00 249.20 ? 526  MET A O   1 
ATOM   4001  C  CB  . MET A  1 526 ? 28.710  -11.770 71.311   1.00 253.33 ? 526  MET A CB  1 
ATOM   4002  C  CG  . MET A  1 526 ? 29.249  -13.109 71.787   1.00 261.18 ? 526  MET A CG  1 
ATOM   4003  S  SD  . MET A  1 526 ? 27.997  -14.352 72.157   1.00 265.24 ? 526  MET A SD  1 
ATOM   4004  C  CE  . MET A  1 526 ? 29.028  -15.806 72.359   1.00 260.62 ? 526  MET A CE  1 
ATOM   4005  N  N   . THR A  1 527 ? 31.344  -11.227 69.017   1.00 252.73 ? 527  THR A N   1 
ATOM   4006  C  CA  . THR A  1 527 ? 31.727  -11.716 67.702   1.00 253.34 ? 527  THR A CA  1 
ATOM   4007  C  C   . THR A  1 527 ? 31.694  -13.239 67.718   1.00 256.55 ? 527  THR A C   1 
ATOM   4008  O  O   . THR A  1 527 ? 32.458  -13.876 68.452   1.00 265.74 ? 527  THR A O   1 
ATOM   4009  C  CB  . THR A  1 527 ? 33.115  -11.211 67.316   1.00 259.30 ? 527  THR A CB  1 
ATOM   4010  O  OG1 . THR A  1 527 ? 33.071  -9.790  67.139   1.00 262.77 ? 527  THR A OG1 1 
ATOM   4011  C  CG2 . THR A  1 527 ? 33.588  -11.882 66.038   1.00 251.53 ? 527  THR A CG2 1 
ATOM   4012  N  N   . ILE A  1 528 ? 30.803  -13.821 66.922   1.00 246.10 ? 528  ILE A N   1 
ATOM   4013  C  CA  . ILE A  1 528 ? 30.754  -15.265 66.757   1.00 242.92 ? 528  ILE A CA  1 
ATOM   4014  C  C   . ILE A  1 528 ? 30.930  -15.571 65.280   1.00 248.09 ? 528  ILE A C   1 
ATOM   4015  O  O   . ILE A  1 528 ? 30.579  -14.768 64.408   1.00 246.23 ? 528  ILE A O   1 
ATOM   4016  C  CB  . ILE A  1 528 ? 29.449  -15.891 67.298   1.00 227.53 ? 528  ILE A CB  1 
ATOM   4017  C  CG1 . ILE A  1 528 ? 28.288  -15.662 66.333   1.00 226.88 ? 528  ILE A CG1 1 
ATOM   4018  C  CG2 . ILE A  1 528 ? 29.108  -15.320 68.658   1.00 230.35 ? 528  ILE A CG2 1 
ATOM   4019  C  CD1 . ILE A  1 528 ? 27.019  -16.346 66.765   1.00 228.05 ? 528  ILE A CD1 1 
ATOM   4020  N  N   . SER A  1 529 ? 31.466  -16.754 65.000   1.00 255.30 ? 529  SER A N   1 
ATOM   4021  C  CA  . SER A  1 529 ? 31.700  -17.203 63.636   1.00 254.16 ? 529  SER A CA  1 
ATOM   4022  C  C   . SER A  1 529 ? 30.647  -18.228 63.258   1.00 231.66 ? 529  SER A C   1 
ATOM   4023  O  O   . SER A  1 529 ? 30.365  -19.157 64.025   1.00 227.03 ? 529  SER A O   1 
ATOM   4024  C  CB  . SER A  1 529 ? 33.097  -17.808 63.476   1.00 265.00 ? 529  SER A CB  1 
ATOM   4025  O  OG  . SER A  1 529 ? 33.217  -19.003 64.225   1.00 262.65 ? 529  SER A OG  1 
ATOM   4026  N  N   . ARG A  1 530 ? 30.060  -18.046 62.088   1.00 229.31 ? 530  ARG A N   1 
ATOM   4027  C  CA  . ARG A  1 530 ? 29.067  -18.984 61.609   1.00 230.15 ? 530  ARG A CA  1 
ATOM   4028  C  C   . ARG A  1 530 ? 29.739  -20.264 61.127   1.00 228.51 ? 530  ARG A C   1 
ATOM   4029  O  O   . ARG A  1 530 ? 30.887  -20.257 60.673   1.00 226.70 ? 530  ARG A O   1 
ATOM   4030  C  CB  . ARG A  1 530 ? 28.238  -18.337 60.494   1.00 241.14 ? 530  ARG A CB  1 
ATOM   4031  C  CG  . ARG A  1 530 ? 28.776  -18.548 59.090   1.00 241.37 ? 530  ARG A CG  1 
ATOM   4032  C  CD  . ARG A  1 530 ? 27.947  -17.784 58.066   1.00 224.84 ? 530  ARG A CD  1 
ATOM   4033  N  NE  . ARG A  1 530 ? 28.298  -18.159 56.699   1.00 221.81 ? 530  ARG A NE  1 
ATOM   4034  C  CZ  . ARG A  1 530 ? 29.366  -17.699 56.053   1.00 231.12 ? 530  ARG A CZ  1 
ATOM   4035  N  NH1 . ARG A  1 530 ? 30.202  -16.871 56.659   1.00 243.54 ? 530  ARG A NH1 1 
ATOM   4036  N  NH2 . ARG A  1 530 ? 29.616  -18.091 54.811   1.00 227.69 ? 530  ARG A NH2 1 
ATOM   4037  N  N   . GLY A  1 531 ? 29.019  -21.376 61.267   1.00 233.44 ? 531  GLY A N   1 
ATOM   4038  C  CA  . GLY A  1 531 ? 29.455  -22.652 60.732   1.00 237.75 ? 531  GLY A CA  1 
ATOM   4039  C  C   . GLY A  1 531 ? 30.414  -23.463 61.579   1.00 235.66 ? 531  GLY A C   1 
ATOM   4040  O  O   . GLY A  1 531 ? 30.423  -24.697 61.500   1.00 230.76 ? 531  GLY A O   1 
ATOM   4041  N  N   . GLY A  1 532 ? 31.223  -22.793 62.395   1.00 248.21 ? 532  GLY A N   1 
ATOM   4042  C  CA  . GLY A  1 532 ? 32.259  -23.482 63.141   1.00 254.82 ? 532  GLY A CA  1 
ATOM   4043  C  C   . GLY A  1 532 ? 31.750  -24.319 64.295   1.00 254.40 ? 532  GLY A C   1 
ATOM   4044  O  O   . GLY A  1 532 ? 31.591  -25.534 64.162   1.00 255.93 ? 532  GLY A O   1 
ATOM   4045  N  N   . LEU A  1 533 ? 31.457  -23.671 65.419   1.00 253.29 ? 533  LEU A N   1 
ATOM   4046  C  CA  . LEU A  1 533 ? 30.965  -24.337 66.616   1.00 249.03 ? 533  LEU A CA  1 
ATOM   4047  C  C   . LEU A  1 533 ? 30.120  -23.332 67.381   1.00 249.82 ? 533  LEU A C   1 
ATOM   4048  O  O   . LEU A  1 533 ? 30.135  -22.134 67.092   1.00 259.19 ? 533  LEU A O   1 
ATOM   4049  C  CB  . LEU A  1 533 ? 32.102  -24.865 67.514   1.00 232.64 ? 533  LEU A CB  1 
ATOM   4050  C  CG  . LEU A  1 533 ? 33.216  -25.810 67.042   1.00 221.21 ? 533  LEU A CG  1 
ATOM   4051  C  CD1 . LEU A  1 533 ? 34.291  -25.940 68.115   1.00 224.45 ? 533  LEU A CD1 1 
ATOM   4052  C  CD2 . LEU A  1 533 ? 32.663  -27.179 66.690   1.00 222.30 ? 533  LEU A CD2 1 
ATOM   4053  N  N   . MET A  1 534 ? 29.357  -23.827 68.346   1.00 238.53 ? 534  MET A N   1 
ATOM   4054  C  CA  . MET A  1 534 ? 28.543  -22.944 69.167   1.00 236.71 ? 534  MET A CA  1 
ATOM   4055  C  C   . MET A  1 534 ? 29.406  -22.313 70.252   1.00 244.49 ? 534  MET A C   1 
ATOM   4056  O  O   . MET A  1 534 ? 30.068  -23.020 71.016   1.00 247.06 ? 534  MET A O   1 
ATOM   4057  C  CB  . MET A  1 534 ? 27.380  -23.717 69.787   1.00 237.54 ? 534  MET A CB  1 
ATOM   4058  C  CG  . MET A  1 534 ? 26.416  -22.860 70.586   1.00 242.85 ? 534  MET A CG  1 
ATOM   4059  S  SD  . MET A  1 534 ? 25.184  -23.868 71.428   1.00 246.32 ? 534  MET A SD  1 
ATOM   4060  C  CE  . MET A  1 534 ? 24.496  -24.787 70.056   1.00 245.06 ? 534  MET A CE  1 
ATOM   4061  N  N   . GLN A  1 535 ? 29.401  -20.983 70.322   1.00 244.05 ? 535  GLN A N   1 
ATOM   4062  C  CA  . GLN A  1 535 ? 30.131  -20.269 71.365   1.00 243.91 ? 535  GLN A CA  1 
ATOM   4063  C  C   . GLN A  1 535 ? 29.190  -19.961 72.522   1.00 248.06 ? 535  GLN A C   1 
ATOM   4064  O  O   . GLN A  1 535 ? 28.148  -19.327 72.331   1.00 244.99 ? 535  GLN A O   1 
ATOM   4065  C  CB  . GLN A  1 535 ? 30.754  -18.982 70.829   1.00 239.56 ? 535  GLN A CB  1 
ATOM   4066  C  CG  . GLN A  1 535 ? 32.102  -19.174 70.160   1.00 236.57 ? 535  GLN A CG  1 
ATOM   4067  C  CD  . GLN A  1 535 ? 32.619  -17.899 69.534   1.00 236.41 ? 535  GLN A CD  1 
ATOM   4068  O  OE1 . GLN A  1 535 ? 31.845  -17.008 69.192   1.00 241.31 ? 535  GLN A OE1 1 
ATOM   4069  N  NE2 . GLN A  1 535 ? 33.932  -17.803 69.381   1.00 234.60 ? 535  GLN A NE2 1 
ATOM   4070  N  N   . CYS A  1 536 ? 29.565  -20.402 73.718   1.00 263.32 ? 536  CYS A N   1 
ATOM   4071  C  CA  . CYS A  1 536 ? 28.757  -20.246 74.916   1.00 267.87 ? 536  CYS A CA  1 
ATOM   4072  C  C   . CYS A  1 536 ? 29.559  -19.488 75.971   1.00 266.96 ? 536  CYS A C   1 
ATOM   4073  O  O   . CYS A  1 536 ? 30.789  -19.427 75.909   1.00 269.46 ? 536  CYS A O   1 
ATOM   4074  C  CB  . CYS A  1 536 ? 28.310  -21.622 75.432   1.00 283.08 ? 536  CYS A CB  1 
ATOM   4075  S  SG  . CYS A  1 536 ? 26.848  -21.646 76.475   1.00 305.18 ? 536  CYS A SG  1 
ATOM   4076  N  N   . GLU A  1 537 ? 28.856  -18.906 76.947   1.00 267.56 ? 537  GLU A N   1 
ATOM   4077  C  CA  . GLU A  1 537 ? 29.520  -18.136 77.996   1.00 274.76 ? 537  GLU A CA  1 
ATOM   4078  C  C   . GLU A  1 537 ? 28.726  -18.193 79.296   1.00 278.02 ? 537  GLU A C   1 
ATOM   4079  O  O   . GLU A  1 537 ? 27.504  -18.012 79.291   1.00 278.35 ? 537  GLU A O   1 
ATOM   4080  C  CB  . GLU A  1 537 ? 29.708  -16.679 77.556   1.00 272.37 ? 537  GLU A CB  1 
ATOM   4081  C  CG  . GLU A  1 537 ? 30.061  -15.725 78.681   1.00 286.40 ? 537  GLU A CG  1 
ATOM   4082  C  CD  . GLU A  1 537 ? 30.370  -14.328 78.181   1.00 294.20 ? 537  GLU A CD  1 
ATOM   4083  O  OE1 . GLU A  1 537 ? 30.955  -14.202 77.084   1.00 296.82 ? 537  GLU A OE1 1 
ATOM   4084  O  OE2 . GLU A  1 537 ? 30.034  -13.356 78.889   1.00 296.47 ? 537  GLU A OE2 1 
ATOM   4085  N  N   . GLU A  1 538 ? 29.424  -18.441 80.404   1.00 274.53 ? 538  GLU A N   1 
ATOM   4086  C  CA  . GLU A  1 538 ? 28.825  -18.527 81.728   1.00 272.89 ? 538  GLU A CA  1 
ATOM   4087  C  C   . GLU A  1 538 ? 29.128  -17.276 82.556   1.00 280.50 ? 538  GLU A C   1 
ATOM   4088  O  O   . GLU A  1 538 ? 30.137  -16.597 82.348   1.00 280.28 ? 538  GLU A O   1 
ATOM   4089  C  CB  . GLU A  1 538 ? 29.328  -19.781 82.449   1.00 273.10 ? 538  GLU A CB  1 
ATOM   4090  C  CG  . GLU A  1 538 ? 28.543  -20.165 83.691   1.00 278.07 ? 538  GLU A CG  1 
ATOM   4091  C  CD  . GLU A  1 538 ? 29.217  -21.271 84.481   1.00 287.25 ? 538  GLU A CD  1 
ATOM   4092  O  OE1 . GLU A  1 538 ? 30.268  -21.768 84.028   1.00 293.65 ? 538  GLU A OE1 1 
ATOM   4093  O  OE2 . GLU A  1 538 ? 28.697  -21.642 85.554   1.00 288.56 ? 538  GLU A OE2 1 
ATOM   4094  N  N   . LEU A  1 539 ? 28.234  -16.975 83.501   1.00 284.97 ? 539  LEU A N   1 
ATOM   4095  C  CA  . LEU A  1 539 ? 28.377  -15.819 84.380   1.00 289.92 ? 539  LEU A CA  1 
ATOM   4096  C  C   . LEU A  1 539 ? 27.502  -16.047 85.608   1.00 282.67 ? 539  LEU A C   1 
ATOM   4097  O  O   . LEU A  1 539 ? 26.525  -16.798 85.550   1.00 286.23 ? 539  LEU A O   1 
ATOM   4098  C  CB  . LEU A  1 539 ? 28.000  -14.521 83.657   1.00 286.55 ? 539  LEU A CB  1 
ATOM   4099  C  CG  . LEU A  1 539 ? 28.609  -13.210 84.163   1.00 287.53 ? 539  LEU A CG  1 
ATOM   4100  C  CD1 . LEU A  1 539 ? 30.135  -13.248 84.102   1.00 285.45 ? 539  LEU A CD1 1 
ATOM   4101  C  CD2 . LEU A  1 539 ? 28.078  -12.041 83.349   1.00 286.47 ? 539  LEU A CD2 1 
ATOM   4102  N  N   . ILE A  1 540 ? 27.853  -15.398 86.720   1.00 251.72 ? 540  ILE A N   1 
ATOM   4103  C  CA  . ILE A  1 540 ? 27.192  -15.631 88.004   1.00 239.64 ? 540  ILE A CA  1 
ATOM   4104  C  C   . ILE A  1 540 ? 26.316  -14.440 88.378   1.00 241.70 ? 540  ILE A C   1 
ATOM   4105  O  O   . ILE A  1 540 ? 26.772  -13.291 88.358   1.00 241.66 ? 540  ILE A O   1 
ATOM   4106  C  CB  . ILE A  1 540 ? 28.209  -15.923 89.118   1.00 240.30 ? 540  ILE A CB  1 
ATOM   4107  C  CG1 . ILE A  1 540 ? 28.975  -17.211 88.816   1.00 239.35 ? 540  ILE A CG1 1 
ATOM   4108  C  CG2 . ILE A  1 540 ? 27.522  -16.015 90.464   1.00 241.72 ? 540  ILE A CG2 1 
ATOM   4109  C  CD1 . ILE A  1 540 ? 29.952  -17.602 89.901   1.00 239.93 ? 540  ILE A CD1 1 
ATOM   4110  N  N   . ALA A  1 541 ? 25.054  -14.723 88.707   1.00 265.10 ? 541  ALA A N   1 
ATOM   4111  C  CA  . ALA A  1 541 ? 24.117  -13.755 89.261   1.00 266.29 ? 541  ALA A CA  1 
ATOM   4112  C  C   . ALA A  1 541 ? 23.600  -14.265 90.602   1.00 262.95 ? 541  ALA A C   1 
ATOM   4113  O  O   . ALA A  1 541 ? 23.584  -15.472 90.855   1.00 264.30 ? 541  ALA A O   1 
ATOM   4114  C  CB  . ALA A  1 541 ? 22.951  -13.478 88.305   1.00 269.61 ? 541  ALA A CB  1 
ATOM   4115  N  N   . TYR A  1 542 ? 23.195  -13.342 91.476   1.00 265.10 ? 542  TYR A N   1 
ATOM   4116  C  CA  . TYR A  1 542 ? 22.719  -13.713 92.801   1.00 272.62 ? 542  TYR A CA  1 
ATOM   4117  C  C   . TYR A  1 542 ? 21.386  -13.056 93.140   1.00 267.15 ? 542  TYR A C   1 
ATOM   4118  O  O   . TYR A  1 542 ? 20.975  -12.065 92.529   1.00 264.58 ? 542  TYR A O   1 
ATOM   4119  C  CB  . TYR A  1 542 ? 23.744  -13.345 93.876   1.00 283.32 ? 542  TYR A CB  1 
ATOM   4120  C  CG  . TYR A  1 542 ? 23.873  -11.867 94.139   1.00 289.59 ? 542  TYR A CG  1 
ATOM   4121  C  CD1 . TYR A  1 542 ? 24.684  -11.066 93.348   1.00 294.59 ? 542  TYR A CD1 1 
ATOM   4122  C  CD2 . TYR A  1 542 ? 23.189  -11.273 95.191   1.00 289.75 ? 542  TYR A CD2 1 
ATOM   4123  C  CE1 . TYR A  1 542 ? 24.809  -9.713  93.597   1.00 294.65 ? 542  TYR A CE1 1 
ATOM   4124  C  CE2 . TYR A  1 542 ? 23.304  -9.922  95.447   1.00 293.59 ? 542  TYR A CE2 1 
ATOM   4125  C  CZ  . TYR A  1 542 ? 24.117  -9.146  94.646   1.00 293.25 ? 542  TYR A CZ  1 
ATOM   4126  O  OH  . TYR A  1 542 ? 24.242  -7.798  94.892   1.00 292.68 ? 542  TYR A OH  1 
ATOM   4127  N  N   . LEU A  1 543 ? 20.712  -13.649 94.127   1.00 271.81 ? 543  LEU A N   1 
ATOM   4128  C  CA  . LEU A  1 543 ? 19.474  -13.135 94.693   1.00 273.71 ? 543  LEU A CA  1 
ATOM   4129  C  C   . LEU A  1 543 ? 19.763  -12.193 95.863   1.00 281.72 ? 543  LEU A C   1 
ATOM   4130  O  O   . LEU A  1 543 ? 20.756  -12.345 96.578   1.00 285.25 ? 543  LEU A O   1 
ATOM   4131  C  CB  . LEU A  1 543 ? 18.586  -14.294 95.157   1.00 273.31 ? 543  LEU A CB  1 
ATOM   4132  C  CG  . LEU A  1 543 ? 17.273  -13.983 95.882   1.00 276.18 ? 543  LEU A CG  1 
ATOM   4133  C  CD1 . LEU A  1 543 ? 16.283  -13.269 94.961   1.00 277.99 ? 543  LEU A CD1 1 
ATOM   4134  C  CD2 . LEU A  1 543 ? 16.655  -15.249 96.460   1.00 279.33 ? 543  LEU A CD2 1 
ATOM   4135  N  N   . ARG A  1 544 ? 18.857  -11.237 96.072   1.00 284.68 ? 544  ARG A N   1 
ATOM   4136  C  CA  . ARG A  1 544 ? 18.913  -10.347 97.225   1.00 292.91 ? 544  ARG A CA  1 
ATOM   4137  C  C   . ARG A  1 544 ? 18.506  -11.053 98.524   1.00 290.21 ? 544  ARG A C   1 
ATOM   4138  O  O   . ARG A  1 544 ? 17.821  -12.079 98.529   1.00 285.58 ? 544  ARG A O   1 
ATOM   4139  C  CB  . ARG A  1 544 ? 18.026  -9.120  97.012   1.00 293.91 ? 544  ARG A CB  1 
ATOM   4140  C  CG  . ARG A  1 544 ? 18.562  -8.097  96.011   1.00 288.34 ? 544  ARG A CG  1 
ATOM   4141  C  CD  . ARG A  1 544 ? 17.842  -6.764  96.203   1.00 283.14 ? 544  ARG A CD  1 
ATOM   4142  N  NE  . ARG A  1 544 ? 18.410  -5.668  95.422   1.00 284.24 ? 544  ARG A NE  1 
ATOM   4143  C  CZ  . ARG A  1 544 ? 18.276  -5.527  94.108   1.00 291.84 ? 544  ARG A CZ  1 
ATOM   4144  N  NH1 . ARG A  1 544 ? 17.606  -6.427  93.401   1.00 295.61 ? 544  ARG A NH1 1 
ATOM   4145  N  NH2 . ARG A  1 544 ? 18.824  -4.486  93.497   1.00 293.34 ? 544  ARG A NH2 1 
ATOM   4146  N  N   . ASP A  1 545 ? 18.956  -10.472 99.639   1.00 292.06 ? 545  ASP A N   1 
ATOM   4147  C  CA  . ASP A  1 545 ? 18.654  -10.946 100.986  1.00 285.02 ? 545  ASP A CA  1 
ATOM   4148  C  C   . ASP A  1 545 ? 17.146  -11.014 101.247  1.00 296.87 ? 545  ASP A C   1 
ATOM   4149  O  O   . ASP A  1 545 ? 16.337  -10.344 100.598  1.00 301.47 ? 545  ASP A O   1 
ATOM   4150  C  CB  . ASP A  1 545 ? 19.329  -10.040 102.013  1.00 281.22 ? 545  ASP A CB  1 
ATOM   4151  C  CG  . ASP A  1 545 ? 19.141  -10.524 103.432  1.00 290.26 ? 545  ASP A CG  1 
ATOM   4152  O  OD1 . ASP A  1 545 ? 19.936  -11.373 103.882  1.00 293.80 ? 545  ASP A OD1 1 
ATOM   4153  O  OD2 . ASP A  1 545 ? 18.190  -10.060 104.095  1.00 296.95 ? 545  ASP A OD2 1 
ATOM   4154  N  N   . GLU A  1 546 ? 16.781  -11.859 102.218  1.00 312.05 ? 546  GLU A N   1 
ATOM   4155  C  CA  . GLU A  1 546 ? 15.378  -12.038 102.591  1.00 315.91 ? 546  GLU A CA  1 
ATOM   4156  C  C   . GLU A  1 546 ? 14.759  -10.748 103.121  1.00 312.11 ? 546  GLU A C   1 
ATOM   4157  O  O   . GLU A  1 546 ? 13.623  -10.409 102.768  1.00 307.10 ? 546  GLU A O   1 
ATOM   4158  C  CB  . GLU A  1 546 ? 15.255  -13.148 103.639  1.00 314.19 ? 546  GLU A CB  1 
ATOM   4159  C  CG  . GLU A  1 546 ? 13.822  -13.460 104.063  1.00 309.66 ? 546  GLU A CG  1 
ATOM   4160  C  CD  . GLU A  1 546 ? 13.746  -14.581 105.081  1.00 303.68 ? 546  GLU A CD  1 
ATOM   4161  O  OE1 . GLU A  1 546 ? 14.815  -15.094 105.468  1.00 298.47 ? 546  GLU A OE1 1 
ATOM   4162  O  OE2 . GLU A  1 546 ? 12.626  -14.942 105.507  1.00 302.23 ? 546  GLU A OE2 1 
ATOM   4163  N  N   . SER A  1 547 ? 15.492  -10.008 103.959  1.00 312.02 ? 547  SER A N   1 
ATOM   4164  C  CA  . SER A  1 547 ? 14.941  -8.827  104.617  1.00 309.82 ? 547  SER A CA  1 
ATOM   4165  C  C   . SER A  1 547 ? 14.806  -7.630  103.683  1.00 319.58 ? 547  SER A C   1 
ATOM   4166  O  O   . SER A  1 547 ? 14.195  -6.627  104.073  1.00 325.20 ? 547  SER A O   1 
ATOM   4167  C  CB  . SER A  1 547 ? 15.804  -8.444  105.830  1.00 288.07 ? 547  SER A CB  1 
ATOM   4168  O  OG  . SER A  1 547 ? 15.771  -9.441  106.838  1.00 278.29 ? 547  SER A OG  1 
ATOM   4169  N  N   . GLU A  1 548 ? 15.356  -7.710  102.473  1.00 307.00 ? 548  GLU A N   1 
ATOM   4170  C  CA  . GLU A  1 548 ? 15.336  -6.610  101.518  1.00 294.69 ? 548  GLU A CA  1 
ATOM   4171  C  C   . GLU A  1 548 ? 14.068  -6.569  100.675  1.00 280.92 ? 548  GLU A C   1 
ATOM   4172  O  O   . GLU A  1 548 ? 13.815  -5.553  100.015  1.00 280.64 ? 548  GLU A O   1 
ATOM   4173  C  CB  . GLU A  1 548 ? 16.568  -6.693  100.607  1.00 287.03 ? 548  GLU A CB  1 
ATOM   4174  C  CG  . GLU A  1 548 ? 17.888  -6.559  101.360  1.00 281.42 ? 548  GLU A CG  1 
ATOM   4175  C  CD  . GLU A  1 548 ? 19.091  -6.449  100.441  1.00 274.05 ? 548  GLU A CD  1 
ATOM   4176  O  OE1 . GLU A  1 548 ? 20.194  -6.142  100.939  1.00 275.56 ? 548  GLU A OE1 1 
ATOM   4177  O  OE2 . GLU A  1 548 ? 18.935  -6.664  99.223   1.00 273.36 ? 548  GLU A OE2 1 
ATOM   4178  N  N   . PHE A  1 549 ? 13.277  -7.639  100.670  1.00 276.47 ? 549  PHE A N   1 
ATOM   4179  C  CA  . PHE A  1 549 ? 12.024  -7.661  99.919   1.00 283.95 ? 549  PHE A CA  1 
ATOM   4180  C  C   . PHE A  1 549 ? 11.135  -8.757  100.487  1.00 292.19 ? 549  PHE A C   1 
ATOM   4181  O  O   . PHE A  1 549 ? 11.570  -9.907  100.607  1.00 291.67 ? 549  PHE A O   1 
ATOM   4182  C  CB  . PHE A  1 549 ? 12.281  -7.871  98.422   1.00 279.40 ? 549  PHE A CB  1 
ATOM   4183  C  CG  . PHE A  1 549 ? 12.908  -9.194  98.090   1.00 284.35 ? 549  PHE A CG  1 
ATOM   4184  C  CD1 . PHE A  1 549 ? 14.278  -9.363  98.183   1.00 294.67 ? 549  PHE A CD1 1 
ATOM   4185  C  CD2 . PHE A  1 549 ? 12.132  -10.267 97.682   1.00 286.24 ? 549  PHE A CD2 1 
ATOM   4186  C  CE1 . PHE A  1 549 ? 14.865  -10.575 97.882   1.00 303.78 ? 549  PHE A CE1 1 
ATOM   4187  C  CE2 . PHE A  1 549 ? 12.715  -11.488 97.381   1.00 296.71 ? 549  PHE A CE2 1 
ATOM   4188  C  CZ  . PHE A  1 549 ? 14.086  -11.639 97.480   1.00 305.54 ? 549  PHE A CZ  1 
ATOM   4189  N  N   . ARG A  1 550 ? 9.910   -8.395  100.877  1.00 294.60 ? 550  ARG A N   1 
ATOM   4190  C  CA  . ARG A  1 550 ? 8.946   -9.372  101.372  1.00 290.40 ? 550  ARG A CA  1 
ATOM   4191  C  C   . ARG A  1 550 ? 8.275   -10.146 100.247  1.00 289.47 ? 550  ARG A C   1 
ATOM   4192  O  O   . ARG A  1 550 ? 7.572   -11.127 100.519  1.00 290.82 ? 550  ARG A O   1 
ATOM   4193  C  CB  . ARG A  1 550 ? 7.883   -8.682  102.237  1.00 282.26 ? 550  ARG A CB  1 
ATOM   4194  C  CG  . ARG A  1 550 ? 7.294   -7.414  101.632  1.00 277.18 ? 550  ARG A CG  1 
ATOM   4195  C  CD  . ARG A  1 550 ? 6.258   -6.788  102.560  1.00 271.80 ? 550  ARG A CD  1 
ATOM   4196  N  NE  . ARG A  1 550 ? 5.521   -5.697  101.926  1.00 267.06 ? 550  ARG A NE  1 
ATOM   4197  C  CZ  . ARG A  1 550 ? 5.815   -4.408  102.067  1.00 268.08 ? 550  ARG A CZ  1 
ATOM   4198  N  NH1 . ARG A  1 550 ? 6.836   -4.032  102.826  1.00 268.26 ? 550  ARG A NH1 1 
ATOM   4199  N  NH2 . ARG A  1 550 ? 5.081   -3.490  101.451  1.00 269.32 ? 550  ARG A NH2 1 
ATOM   4200  N  N   . ASP A  1 551 ? 8.475   -9.726  99.001   1.00 287.81 ? 551  ASP A N   1 
ATOM   4201  C  CA  . ASP A  1 551 ? 7.823   -10.317 97.835   1.00 282.70 ? 551  ASP A CA  1 
ATOM   4202  C  C   . ASP A  1 551 ? 8.615   -11.545 97.398   1.00 285.36 ? 551  ASP A C   1 
ATOM   4203  O  O   . ASP A  1 551 ? 9.531   -11.463 96.578   1.00 288.65 ? 551  ASP A O   1 
ATOM   4204  C  CB  . ASP A  1 551 ? 7.722   -9.286  96.717   1.00 279.40 ? 551  ASP A CB  1 
ATOM   4205  C  CG  . ASP A  1 551 ? 6.731   -9.682  95.639   1.00 286.53 ? 551  ASP A CG  1 
ATOM   4206  O  OD1 . ASP A  1 551 ? 6.411   -10.883 95.512   1.00 285.80 ? 551  ASP A OD1 1 
ATOM   4207  O  OD2 . ASP A  1 551 ? 6.275   -8.779  94.906   1.00 294.50 ? 551  ASP A OD2 1 
ATOM   4208  N  N   . LYS A  1 552 ? 8.248   -12.709 97.940   1.00 290.42 ? 552  LYS A N   1 
ATOM   4209  C  CA  . LYS A  1 552 ? 8.878   -13.975 97.579   1.00 291.73 ? 552  LYS A CA  1 
ATOM   4210  C  C   . LYS A  1 552 ? 7.951   -14.857 96.752   1.00 293.90 ? 552  LYS A C   1 
ATOM   4211  O  O   . LYS A  1 552 ? 8.204   -16.058 96.608   1.00 300.69 ? 552  LYS A O   1 
ATOM   4212  C  CB  . LYS A  1 552 ? 9.341   -14.734 98.824   1.00 289.50 ? 552  LYS A CB  1 
ATOM   4213  C  CG  . LYS A  1 552 ? 10.561  -14.159 99.522   1.00 283.95 ? 552  LYS A CG  1 
ATOM   4214  C  CD  . LYS A  1 552 ? 10.160  -13.245 100.657  1.00 279.82 ? 552  LYS A CD  1 
ATOM   4215  C  CE  . LYS A  1 552 ? 11.337  -12.953 101.561  1.00 280.27 ? 552  LYS A CE  1 
ATOM   4216  N  NZ  . LYS A  1 552 ? 10.961  -12.055 102.685  1.00 291.19 ? 552  LYS A NZ  1 
ATOM   4217  N  N   . LEU A  1 553 ? 6.886   -14.280 96.199   1.00 284.84 ? 553  LEU A N   1 
ATOM   4218  C  CA  . LEU A  1 553 ? 5.901   -15.027 95.431   1.00 279.49 ? 553  LEU A CA  1 
ATOM   4219  C  C   . LEU A  1 553 ? 5.990   -14.779 93.934   1.00 277.20 ? 553  LEU A C   1 
ATOM   4220  O  O   . LEU A  1 553 ? 5.569   -15.634 93.153   1.00 276.01 ? 553  LEU A O   1 
ATOM   4221  C  CB  . LEU A  1 553 ? 4.479   -14.689 95.905   1.00 276.30 ? 553  LEU A CB  1 
ATOM   4222  C  CG  . LEU A  1 553 ? 4.106   -14.872 97.382   1.00 268.17 ? 553  LEU A CG  1 
ATOM   4223  C  CD1 . LEU A  1 553 ? 4.726   -16.141 97.955   1.00 271.85 ? 553  LEU A CD1 1 
ATOM   4224  C  CD2 . LEU A  1 553 ? 4.470   -13.651 98.217   1.00 264.48 ? 553  LEU A CD2 1 
ATOM   4225  N  N   . THR A  1 554 ? 6.514   -13.631 93.519   1.00 271.39 ? 554  THR A N   1 
ATOM   4226  C  CA  . THR A  1 554 ? 6.609   -13.250 92.115   1.00 268.16 ? 554  THR A CA  1 
ATOM   4227  C  C   . THR A  1 554 ? 7.756   -14.002 91.446   1.00 277.87 ? 554  THR A C   1 
ATOM   4228  O  O   . THR A  1 554 ? 8.924   -13.677 91.696   1.00 297.63 ? 554  THR A O   1 
ATOM   4229  C  CB  . THR A  1 554 ? 6.811   -11.739 91.984   1.00 265.07 ? 554  THR A CB  1 
ATOM   4230  O  OG1 . THR A  1 554 ? 5.728   -11.051 92.621   1.00 265.19 ? 554  THR A OG1 1 
ATOM   4231  C  CG2 . THR A  1 554 ? 6.866   -11.336 90.522   1.00 262.71 ? 554  THR A CG2 1 
ATOM   4232  N  N   . PRO A  1 555 ? 7.477   -15.044 90.656   1.00 261.43 ? 555  PRO A N   1 
ATOM   4233  C  CA  . PRO A  1 555 ? 8.562   -15.809 90.021   1.00 256.57 ? 555  PRO A CA  1 
ATOM   4234  C  C   . PRO A  1 555 ? 9.534   -14.921 89.251   1.00 251.79 ? 555  PRO A C   1 
ATOM   4235  O  O   . PRO A  1 555 ? 9.133   -13.996 88.543   1.00 252.55 ? 555  PRO A O   1 
ATOM   4236  C  CB  . PRO A  1 555 ? 7.816   -16.773 89.092   1.00 253.04 ? 555  PRO A CB  1 
ATOM   4237  C  CG  . PRO A  1 555 ? 6.516   -16.108 88.825   1.00 253.02 ? 555  PRO A CG  1 
ATOM   4238  C  CD  . PRO A  1 555 ? 6.159   -15.402 90.100   1.00 253.22 ? 555  PRO A CD  1 
ATOM   4239  N  N   . ILE A  1 556 ? 10.825  -15.228 89.379   1.00 250.50 ? 556  ILE A N   1 
ATOM   4240  C  CA  . ILE A  1 556 ? 11.891  -14.407 88.807   1.00 251.03 ? 556  ILE A CA  1 
ATOM   4241  C  C   . ILE A  1 556 ? 12.191  -14.949 87.415   1.00 256.66 ? 556  ILE A C   1 
ATOM   4242  O  O   . ILE A  1 556 ? 12.808  -16.005 87.261   1.00 261.83 ? 556  ILE A O   1 
ATOM   4243  C  CB  . ILE A  1 556 ? 13.142  -14.398 89.686   1.00 252.73 ? 556  ILE A CB  1 
ATOM   4244  C  CG1 . ILE A  1 556 ? 12.797  -13.910 91.094   1.00 263.64 ? 556  ILE A CG1 1 
ATOM   4245  C  CG2 . ILE A  1 556 ? 14.227  -13.537 89.049   1.00 252.77 ? 556  ILE A CG2 1 
ATOM   4246  C  CD1 . ILE A  1 556 ? 13.990  -13.819 92.025   1.00 272.85 ? 556  ILE A CD1 1 
ATOM   4247  N  N   . THR A  1 557 ? 11.734  -14.229 86.397   1.00 258.42 ? 557  THR A N   1 
ATOM   4248  C  CA  . THR A  1 557 ? 11.949  -14.616 85.011   1.00 253.67 ? 557  THR A CA  1 
ATOM   4249  C  C   . THR A  1 557 ? 13.271  -14.030 84.530   1.00 249.46 ? 557  THR A C   1 
ATOM   4250  O  O   . THR A  1 557 ? 13.470  -12.810 84.582   1.00 243.80 ? 557  THR A O   1 
ATOM   4251  C  CB  . THR A  1 557 ? 10.791  -14.141 84.134   1.00 250.24 ? 557  THR A CB  1 
ATOM   4252  O  OG1 . THR A  1 557 ? 9.588   -14.818 84.520   1.00 252.10 ? 557  THR A OG1 1 
ATOM   4253  C  CG2 . THR A  1 557 ? 11.079  -14.426 82.673   1.00 251.75 ? 557  THR A CG2 1 
ATOM   4254  N  N   . ILE A  1 558 ? 14.169  -14.897 84.071   1.00 260.46 ? 558  ILE A N   1 
ATOM   4255  C  CA  . ILE A  1 558 ? 15.422  -14.474 83.453   1.00 259.66 ? 558  ILE A CA  1 
ATOM   4256  C  C   . ILE A  1 558 ? 15.156  -14.255 81.971   1.00 268.74 ? 558  ILE A C   1 
ATOM   4257  O  O   . ILE A  1 558 ? 14.792  -15.192 81.251   1.00 271.61 ? 558  ILE A O   1 
ATOM   4258  C  CB  . ILE A  1 558 ? 16.538  -15.512 83.659   1.00 250.16 ? 558  ILE A CB  1 
ATOM   4259  C  CG1 . ILE A  1 558 ? 16.932  -15.641 85.137   1.00 249.68 ? 558  ILE A CG1 1 
ATOM   4260  C  CG2 . ILE A  1 558 ? 17.750  -15.166 82.807   1.00 245.84 ? 558  ILE A CG2 1 
ATOM   4261  C  CD1 . ILE A  1 558 ? 16.090  -16.621 85.929   1.00 248.35 ? 558  ILE A CD1 1 
ATOM   4262  N  N   . PHE A  1 559 ? 15.354  -13.026 81.507   1.00 271.41 ? 559  PHE A N   1 
ATOM   4263  C  CA  . PHE A  1 559 ? 15.080  -12.665 80.124   1.00 270.73 ? 559  PHE A CA  1 
ATOM   4264  C  C   . PHE A  1 559 ? 16.395  -12.490 79.379   1.00 264.44 ? 559  PHE A C   1 
ATOM   4265  O  O   . PHE A  1 559 ? 17.297  -11.792 79.856   1.00 279.28 ? 559  PHE A O   1 
ATOM   4266  C  CB  . PHE A  1 559 ? 14.241  -11.386 80.045   1.00 270.99 ? 559  PHE A CB  1 
ATOM   4267  C  CG  . PHE A  1 559 ? 13.989  -10.915 78.641   1.00 264.12 ? 559  PHE A CG  1 
ATOM   4268  C  CD1 . PHE A  1 559 ? 13.046  -11.548 77.847   1.00 259.49 ? 559  PHE A CD1 1 
ATOM   4269  C  CD2 . PHE A  1 559 ? 14.699  -9.851  78.112   1.00 262.63 ? 559  PHE A CD2 1 
ATOM   4270  C  CE1 . PHE A  1 559 ? 12.813  -11.126 76.556   1.00 258.57 ? 559  PHE A CE1 1 
ATOM   4271  C  CE2 . PHE A  1 559 ? 14.470  -9.425  76.821   1.00 263.31 ? 559  PHE A CE2 1 
ATOM   4272  C  CZ  . PHE A  1 559 ? 13.531  -10.068 76.041   1.00 264.71 ? 559  PHE A CZ  1 
ATOM   4273  N  N   . MET A  1 560 ? 16.504  -13.129 78.219   1.00 250.87 ? 560  MET A N   1 
ATOM   4274  C  CA  . MET A  1 560 ? 17.681  -13.028 77.369   1.00 254.41 ? 560  MET A CA  1 
ATOM   4275  C  C   . MET A  1 560 ? 17.273  -12.484 76.010   1.00 264.86 ? 560  MET A C   1 
ATOM   4276  O  O   . MET A  1 560 ? 16.403  -13.056 75.346   1.00 273.93 ? 560  MET A O   1 
ATOM   4277  C  CB  . MET A  1 560 ? 18.360  -14.384 77.200   1.00 253.68 ? 560  MET A CB  1 
ATOM   4278  C  CG  . MET A  1 560 ? 19.444  -14.375 76.148   1.00 255.79 ? 560  MET A CG  1 
ATOM   4279  S  SD  . MET A  1 560 ? 20.129  -16.012 75.877   1.00 262.52 ? 560  MET A SD  1 
ATOM   4280  C  CE  . MET A  1 560 ? 21.092  -15.731 74.392   1.00 260.48 ? 560  MET A CE  1 
ATOM   4281  N  N   . GLU A  1 561 ? 17.917  -11.398 75.592   1.00 264.55 ? 561  GLU A N   1 
ATOM   4282  C  CA  . GLU A  1 561 ? 17.644  -10.743 74.321   1.00 262.39 ? 561  GLU A CA  1 
ATOM   4283  C  C   . GLU A  1 561 ? 18.924  -10.691 73.496   1.00 264.14 ? 561  GLU A C   1 
ATOM   4284  O  O   . GLU A  1 561 ? 20.015  -10.495 74.041   1.00 277.96 ? 561  GLU A O   1 
ATOM   4285  C  CB  . GLU A  1 561 ? 17.096  -9.327  74.549   1.00 259.29 ? 561  GLU A CB  1 
ATOM   4286  C  CG  . GLU A  1 561 ? 16.815  -8.529  73.286   1.00 257.83 ? 561  GLU A CG  1 
ATOM   4287  C  CD  . GLU A  1 561 ? 16.406  -7.098  73.588   1.00 261.71 ? 561  GLU A CD  1 
ATOM   4288  O  OE1 . GLU A  1 561 ? 16.536  -6.676  74.759   1.00 259.32 ? 561  GLU A OE1 1 
ATOM   4289  O  OE2 . GLU A  1 561 ? 15.955  -6.397  72.658   1.00 266.44 ? 561  GLU A OE2 1 
ATOM   4290  N  N   . TYR A  1 562 ? 18.797  -10.881 72.183   1.00 255.41 ? 562  TYR A N   1 
ATOM   4291  C  CA  . TYR A  1 562 ? 19.955  -10.862 71.302   1.00 257.39 ? 562  TYR A CA  1 
ATOM   4292  C  C   . TYR A  1 562 ? 19.615  -10.164 69.992   1.00 258.03 ? 562  TYR A C   1 
ATOM   4293  O  O   . TYR A  1 562 ? 18.484  -10.236 69.504   1.00 257.36 ? 562  TYR A O   1 
ATOM   4294  C  CB  . TYR A  1 562 ? 20.484  -12.283 71.041   1.00 255.05 ? 562  TYR A CB  1 
ATOM   4295  C  CG  . TYR A  1 562 ? 19.464  -13.251 70.484   1.00 257.93 ? 562  TYR A CG  1 
ATOM   4296  C  CD1 . TYR A  1 562 ? 19.278  -13.389 69.114   1.00 264.09 ? 562  TYR A CD1 1 
ATOM   4297  C  CD2 . TYR A  1 562 ? 18.692  -14.035 71.332   1.00 259.60 ? 562  TYR A CD2 1 
ATOM   4298  C  CE1 . TYR A  1 562 ? 18.348  -14.280 68.605   1.00 266.17 ? 562  TYR A CE1 1 
ATOM   4299  C  CE2 . TYR A  1 562 ? 17.760  -14.924 70.833   1.00 262.12 ? 562  TYR A CE2 1 
ATOM   4300  C  CZ  . TYR A  1 562 ? 17.594  -15.045 69.470   1.00 264.25 ? 562  TYR A CZ  1 
ATOM   4301  O  OH  . TYR A  1 562 ? 16.666  -15.932 68.972   1.00 260.95 ? 562  TYR A OH  1 
ATOM   4302  N  N   . ARG A  1 563 ? 20.621  -9.496  69.424   1.00 275.52 ? 563  ARG A N   1 
ATOM   4303  C  CA  . ARG A  1 563 ? 20.477  -8.754  68.178   1.00 280.08 ? 563  ARG A CA  1 
ATOM   4304  C  C   . ARG A  1 563 ? 21.781  -8.836  67.395   1.00 280.07 ? 563  ARG A C   1 
ATOM   4305  O  O   . ARG A  1 563 ? 22.793  -9.354  67.878   1.00 281.08 ? 563  ARG A O   1 
ATOM   4306  C  CB  . ARG A  1 563 ? 20.095  -7.283  68.410   1.00 291.07 ? 563  ARG A CB  1 
ATOM   4307  C  CG  . ARG A  1 563 ? 18.796  -7.046  69.178   1.00 298.57 ? 563  ARG A CG  1 
ATOM   4308  C  CD  . ARG A  1 563 ? 18.492  -5.554  69.298   1.00 312.44 ? 563  ARG A CD  1 
ATOM   4309  N  NE  . ARG A  1 563 ? 17.119  -5.283  69.726   1.00 313.98 ? 563  ARG A NE  1 
ATOM   4310  C  CZ  . ARG A  1 563 ? 16.627  -4.064  69.936   1.00 312.50 ? 563  ARG A CZ  1 
ATOM   4311  N  NH1 . ARG A  1 563 ? 17.399  -2.998  69.765   1.00 322.32 ? 563  ARG A NH1 1 
ATOM   4312  N  NH2 . ARG A  1 563 ? 15.367  -3.909  70.323   1.00 299.43 ? 563  ARG A NH2 1 
ATOM   4313  N  N   . LEU A  1 564 ? 21.736  -8.323  66.166   1.00 274.90 ? 564  LEU A N   1 
ATOM   4314  C  CA  . LEU A  1 564 ? 22.859  -8.295  65.242   1.00 273.89 ? 564  LEU A CA  1 
ATOM   4315  C  C   . LEU A  1 564 ? 23.263  -6.846  64.972   1.00 288.31 ? 564  LEU A C   1 
ATOM   4316  O  O   . LEU A  1 564 ? 22.468  -5.916  65.131   1.00 288.63 ? 564  LEU A O   1 
ATOM   4317  C  CB  . LEU A  1 564 ? 22.509  -9.022  63.934   1.00 257.10 ? 564  LEU A CB  1 
ATOM   4318  C  CG  . LEU A  1 564 ? 23.588  -9.158  62.856   1.00 255.52 ? 564  LEU A CG  1 
ATOM   4319  C  CD1 . LEU A  1 564 ? 24.827  -9.807  63.452   1.00 262.22 ? 564  LEU A CD1 1 
ATOM   4320  C  CD2 . LEU A  1 564 ? 23.095  -9.960  61.664   1.00 262.79 ? 564  LEU A CD2 1 
ATOM   4321  N  N   . ASP A  1 565 ? 24.519  -6.666  64.551   1.00 298.58 ? 565  ASP A N   1 
ATOM   4322  C  CA  . ASP A  1 565 ? 25.029  -5.356  64.147   1.00 292.88 ? 565  ASP A CA  1 
ATOM   4323  C  C   . ASP A  1 565 ? 24.587  -4.927  62.745   1.00 281.18 ? 565  ASP A C   1 
ATOM   4324  O  O   . ASP A  1 565 ? 24.501  -3.724  62.476   1.00 275.71 ? 565  ASP A O   1 
ATOM   4325  C  CB  . ASP A  1 565 ? 26.555  -5.380  64.203   1.00 292.79 ? 565  ASP A CB  1 
ATOM   4326  C  CG  . ASP A  1 565 ? 27.169  -3.992  64.236   1.00 294.59 ? 565  ASP A CG  1 
ATOM   4327  O  OD1 . ASP A  1 565 ? 27.388  -3.447  65.341   1.00 295.66 ? 565  ASP A OD1 1 
ATOM   4328  O  OD2 . ASP A  1 565 ? 27.440  -3.446  63.150   1.00 298.64 ? 565  ASP A OD2 1 
ATOM   4329  N  N   . TYR A  1 566 ? 24.304  -5.874  61.846   1.00 265.81 ? 566  TYR A N   1 
ATOM   4330  C  CA  . TYR A  1 566 ? 24.018  -5.611  60.430   1.00 262.44 ? 566  TYR A CA  1 
ATOM   4331  C  C   . TYR A  1 566 ? 25.081  -4.781  59.708   1.00 264.00 ? 566  TYR A C   1 
ATOM   4332  O  O   . TYR A  1 566 ? 25.492  -5.145  58.602   1.00 269.64 ? 566  TYR A O   1 
ATOM   4333  C  CB  . TYR A  1 566 ? 22.673  -4.895  60.240   1.00 263.51 ? 566  TYR A CB  1 
ATOM   4334  C  CG  . TYR A  1 566 ? 21.426  -5.615  60.707   1.00 270.44 ? 566  TYR A CG  1 
ATOM   4335  C  CD1 . TYR A  1 566 ? 21.388  -6.999  60.814   1.00 271.85 ? 566  TYR A CD1 1 
ATOM   4336  C  CD2 . TYR A  1 566 ? 20.263  -4.906  60.990   1.00 268.47 ? 566  TYR A CD2 1 
ATOM   4337  C  CE1 . TYR A  1 566 ? 20.235  -7.655  61.223   1.00 262.28 ? 566  TYR A CE1 1 
ATOM   4338  C  CE2 . TYR A  1 566 ? 19.108  -5.551  61.398   1.00 256.94 ? 566  TYR A CE2 1 
ATOM   4339  C  CZ  . TYR A  1 566 ? 19.099  -6.926  61.513   1.00 250.58 ? 566  TYR A CZ  1 
ATOM   4340  O  OH  . TYR A  1 566 ? 17.956  -7.576  61.917   1.00 244.14 ? 566  TYR A OH  1 
ATOM   4341  N  N   . ARG A  1 567 ? 25.517  -3.662  60.298   1.00 261.74 ? 567  ARG A N   1 
ATOM   4342  C  CA  . ARG A  1 567 ? 26.474  -2.790  59.619   1.00 258.71 ? 567  ARG A CA  1 
ATOM   4343  C  C   . ARG A  1 567 ? 27.791  -3.504  59.335   1.00 250.59 ? 567  ARG A C   1 
ATOM   4344  O  O   . ARG A  1 567 ? 28.358  -3.366  58.245   1.00 249.05 ? 567  ARG A O   1 
ATOM   4345  C  CB  . ARG A  1 567 ? 26.710  -1.519  60.433   1.00 268.87 ? 567  ARG A CB  1 
ATOM   4346  C  CG  . ARG A  1 567 ? 25.450  -0.706  60.677   1.00 275.28 ? 567  ARG A CG  1 
ATOM   4347  C  CD  . ARG A  1 567 ? 25.790  0.690   61.169   1.00 283.44 ? 567  ARG A CD  1 
ATOM   4348  N  NE  . ARG A  1 567 ? 24.601  1.454   61.533   1.00 283.17 ? 567  ARG A NE  1 
ATOM   4349  C  CZ  . ARG A  1 567 ? 24.609  2.749   61.832   1.00 276.22 ? 567  ARG A CZ  1 
ATOM   4350  N  NH1 . ARG A  1 567 ? 25.748  3.430   61.807   1.00 265.05 ? 567  ARG A NH1 1 
ATOM   4351  N  NH2 . ARG A  1 567 ? 23.479  3.364   62.155   1.00 275.12 ? 567  ARG A NH2 1 
ATOM   4352  N  N   . THR A  1 568 ? 28.299  -4.265  60.304   1.00 256.53 ? 568  THR A N   1 
ATOM   4353  C  CA  . THR A  1 568 ? 29.531  -5.022  60.119   1.00 259.72 ? 568  THR A CA  1 
ATOM   4354  C  C   . THR A  1 568 ? 29.304  -6.362  59.437   1.00 258.43 ? 568  THR A C   1 
ATOM   4355  O  O   . THR A  1 568 ? 30.276  -7.077  59.174   1.00 259.88 ? 568  THR A O   1 
ATOM   4356  C  CB  . THR A  1 568 ? 30.228  -5.253  61.461   1.00 265.02 ? 568  THR A CB  1 
ATOM   4357  O  OG1 . THR A  1 568 ? 31.570  -5.696  61.231   1.00 281.54 ? 568  THR A OG1 1 
ATOM   4358  C  CG2 . THR A  1 568 ? 29.493  -6.314  62.260   1.00 255.25 ? 568  THR A CG2 1 
ATOM   4359  N  N   . ALA A  1 569 ? 28.055  -6.727  59.162   1.00 259.18 ? 569  ALA A N   1 
ATOM   4360  C  CA  . ALA A  1 569 ? 27.737  -7.941  58.423   1.00 266.89 ? 569  ALA A CA  1 
ATOM   4361  C  C   . ALA A  1 569 ? 27.211  -7.636  57.025   1.00 277.38 ? 569  ALA A C   1 
ATOM   4362  O  O   . ALA A  1 569 ? 26.760  -8.551  56.327   1.00 277.41 ? 569  ALA A O   1 
ATOM   4363  C  CB  . ALA A  1 569 ? 26.727  -8.788  59.201   1.00 263.14 ? 569  ALA A CB  1 
ATOM   4364  N  N   . ALA A  1 570 ? 27.254  -6.373  56.604   1.00 284.27 ? 570  ALA A N   1 
ATOM   4365  C  CA  . ALA A  1 570 ? 26.807  -5.979  55.279   1.00 275.63 ? 570  ALA A CA  1 
ATOM   4366  C  C   . ALA A  1 570 ? 27.848  -6.371  54.235   1.00 269.55 ? 570  ALA A C   1 
ATOM   4367  O  O   . ALA A  1 570 ? 28.977  -6.754  54.552   1.00 273.64 ? 570  ALA A O   1 
ATOM   4368  C  CB  . ALA A  1 570 ? 26.534  -4.475  55.224   1.00 276.68 ? 570  ALA A CB  1 
ATOM   4369  N  N   . ASP A  1 571 ? 27.456  -6.282  52.970   1.00 258.08 ? 571  ASP A N   1 
ATOM   4370  C  CA  . ASP A  1 571 ? 28.335  -6.659  51.879   1.00 262.52 ? 571  ASP A CA  1 
ATOM   4371  C  C   . ASP A  1 571 ? 28.956  -5.412  51.244   1.00 257.83 ? 571  ASP A C   1 
ATOM   4372  O  O   . ASP A  1 571 ? 28.680  -4.275  51.639   1.00 257.56 ? 571  ASP A O   1 
ATOM   4373  C  CB  . ASP A  1 571 ? 27.561  -7.489  50.857   1.00 261.77 ? 571  ASP A CB  1 
ATOM   4374  C  CG  . ASP A  1 571 ? 28.458  -8.389  50.041   1.00 268.33 ? 571  ASP A CG  1 
ATOM   4375  O  OD1 . ASP A  1 571 ? 29.494  -8.836  50.576   1.00 257.75 ? 571  ASP A OD1 1 
ATOM   4376  O  OD2 . ASP A  1 571 ? 28.119  -8.655  48.868   1.00 267.90 ? 571  ASP A OD2 1 
ATOM   4377  N  N   . THR A  1 572 ? 29.817  -5.637  50.243   1.00 252.59 ? 572  THR A N   1 
ATOM   4378  C  CA  . THR A  1 572 ? 30.426  -4.527  49.514   1.00 253.13 ? 572  THR A CA  1 
ATOM   4379  C  C   . THR A  1 572 ? 29.370  -3.672  48.830   1.00 256.64 ? 572  THR A C   1 
ATOM   4380  O  O   . THR A  1 572 ? 29.593  -2.479  48.592   1.00 261.12 ? 572  THR A O   1 
ATOM   4381  C  CB  . THR A  1 572 ? 31.435  -5.054  48.485   1.00 254.97 ? 572  THR A CB  1 
ATOM   4382  O  OG1 . THR A  1 572 ? 31.985  -3.959  47.740   1.00 249.92 ? 572  THR A OG1 1 
ATOM   4383  C  CG2 . THR A  1 572 ? 30.771  -6.033  47.524   1.00 254.11 ? 572  THR A CG2 1 
ATOM   4384  N  N   . THR A  1 573 ? 28.224  -4.262  48.505   1.00 242.21 ? 573  THR A N   1 
ATOM   4385  C  CA  . THR A  1 573 ? 27.112  -3.554  47.894   1.00 228.89 ? 573  THR A CA  1 
ATOM   4386  C  C   . THR A  1 573 ? 26.153  -2.955  48.917   1.00 240.92 ? 573  THR A C   1 
ATOM   4387  O  O   . THR A  1 573 ? 25.130  -2.388  48.522   1.00 264.44 ? 573  THR A O   1 
ATOM   4388  C  CB  . THR A  1 573 ? 26.344  -4.494  46.959   1.00 220.51 ? 573  THR A CB  1 
ATOM   4389  O  OG1 . THR A  1 573 ? 25.759  -5.554  47.725   1.00 219.22 ? 573  THR A OG1 1 
ATOM   4390  C  CG2 . THR A  1 573 ? 27.269  -5.086  45.911   1.00 217.60 ? 573  THR A CG2 1 
ATOM   4391  N  N   . GLY A  1 574 ? 26.451  -3.058  50.212   1.00 230.24 ? 574  GLY A N   1 
ATOM   4392  C  CA  . GLY A  1 574 ? 25.579  -2.484  51.219   1.00 225.64 ? 574  GLY A CA  1 
ATOM   4393  C  C   . GLY A  1 574 ? 24.348  -3.296  51.541   1.00 222.13 ? 574  GLY A C   1 
ATOM   4394  O  O   . GLY A  1 574 ? 23.381  -2.753  52.087   1.00 224.13 ? 574  GLY A O   1 
ATOM   4395  N  N   . LEU A  1 575 ? 24.344  -4.579  51.201   1.00 217.73 ? 575  LEU A N   1 
ATOM   4396  C  CA  . LEU A  1 575 ? 23.195  -5.448  51.418   1.00 216.43 ? 575  LEU A CA  1 
ATOM   4397  C  C   . LEU A  1 575 ? 23.272  -6.037  52.820   1.00 226.38 ? 575  LEU A C   1 
ATOM   4398  O  O   . LEU A  1 575 ? 24.130  -6.881  53.100   1.00 235.24 ? 575  LEU A O   1 
ATOM   4399  C  CB  . LEU A  1 575 ? 23.158  -6.545  50.362   1.00 214.80 ? 575  LEU A CB  1 
ATOM   4400  C  CG  . LEU A  1 575 ? 21.786  -7.156  50.127   1.00 212.81 ? 575  LEU A CG  1 
ATOM   4401  C  CD1 . LEU A  1 575 ? 20.800  -6.048  49.831   1.00 232.44 ? 575  LEU A CD1 1 
ATOM   4402  C  CD2 . LEU A  1 575 ? 21.871  -8.123  48.962   1.00 210.62 ? 575  LEU A CD2 1 
ATOM   4403  N  N   . GLN A  1 576 ? 22.375  -5.594  53.700   1.00 227.60 ? 576  GLN A N   1 
ATOM   4404  C  CA  . GLN A  1 576 ? 22.392  -6.068  55.082   1.00 228.54 ? 576  GLN A CA  1 
ATOM   4405  C  C   . GLN A  1 576 ? 21.592  -7.358  55.212   1.00 226.51 ? 576  GLN A C   1 
ATOM   4406  O  O   . GLN A  1 576 ? 20.482  -7.446  54.676   1.00 224.83 ? 576  GLN A O   1 
ATOM   4407  C  CB  . GLN A  1 576 ? 21.826  -5.021  56.027   1.00 230.41 ? 576  GLN A CB  1 
ATOM   4408  C  CG  . GLN A  1 576 ? 22.333  -3.615  55.785   1.00 242.81 ? 576  GLN A CG  1 
ATOM   4409  C  CD  . GLN A  1 576 ? 21.681  -2.606  56.707   1.00 252.50 ? 576  GLN A CD  1 
ATOM   4410  O  OE1 . GLN A  1 576 ? 20.756  -2.934  57.451   1.00 247.91 ? 576  GLN A OE1 1 
ATOM   4411  N  NE2 . GLN A  1 576 ? 22.170  -1.374  56.673   1.00 267.25 ? 576  GLN A NE2 1 
ATOM   4412  N  N   . PRO A  1 577 ? 22.123  -8.374  55.906   1.00 238.79 ? 577  PRO A N   1 
ATOM   4413  C  CA  . PRO A  1 577 ? 21.387  -9.636  56.073   1.00 238.73 ? 577  PRO A CA  1 
ATOM   4414  C  C   . PRO A  1 577 ? 20.107  -9.479  56.881   1.00 245.27 ? 577  PRO A C   1 
ATOM   4415  O  O   . PRO A  1 577 ? 19.779  -8.380  57.340   1.00 254.94 ? 577  PRO A O   1 
ATOM   4416  C  CB  . PRO A  1 577 ? 22.398  -10.537 56.799   1.00 234.38 ? 577  PRO A CB  1 
ATOM   4417  C  CG  . PRO A  1 577 ? 23.735  -9.925  56.518   1.00 244.80 ? 577  PRO A CG  1 
ATOM   4418  C  CD  . PRO A  1 577 ? 23.475  -8.447  56.481   1.00 249.81 ? 577  PRO A CD  1 
ATOM   4419  N  N   . ILE A  1 578 ? 19.375  -10.579 57.064   1.00 238.75 ? 578  ILE A N   1 
ATOM   4420  C  CA  . ILE A  1 578 ? 18.116  -10.555 57.798   1.00 234.56 ? 578  ILE A CA  1 
ATOM   4421  C  C   . ILE A  1 578 ? 17.874  -11.929 58.411   1.00 234.29 ? 578  ILE A C   1 
ATOM   4422  O  O   . ILE A  1 578 ? 18.265  -12.956 57.850   1.00 235.42 ? 578  ILE A O   1 
ATOM   4423  C  CB  . ILE A  1 578 ? 16.939  -10.125 56.892   1.00 222.06 ? 578  ILE A CB  1 
ATOM   4424  C  CG1 . ILE A  1 578 ? 15.686  -9.856  57.729   1.00 223.19 ? 578  ILE A CG1 1 
ATOM   4425  C  CG2 . ILE A  1 578 ? 16.670  -11.177 55.820   1.00 213.80 ? 578  ILE A CG2 1 
ATOM   4426  C  CD1 . ILE A  1 578 ? 15.876  -8.785  58.793   1.00 220.50 ? 578  ILE A CD1 1 
ATOM   4427  N  N   . LEU A  1 579 ? 17.234  -11.937 59.580   1.00 230.07 ? 579  LEU A N   1 
ATOM   4428  C  CA  . LEU A  1 579 ? 16.930  -13.166 60.303   1.00 222.11 ? 579  LEU A CA  1 
ATOM   4429  C  C   . LEU A  1 579 ? 15.757  -13.916 59.679   1.00 213.93 ? 579  LEU A C   1 
ATOM   4430  O  O   . LEU A  1 579 ? 14.863  -13.322 59.062   1.00 210.62 ? 579  LEU A O   1 
ATOM   4431  C  CB  . LEU A  1 579 ? 16.616  -12.861 61.769   1.00 218.50 ? 579  LEU A CB  1 
ATOM   4432  C  CG  . LEU A  1 579 ? 17.747  -12.293 62.634   1.00 219.20 ? 579  LEU A CG  1 
ATOM   4433  C  CD1 . LEU A  1 579 ? 17.222  -11.906 64.008   1.00 219.81 ? 579  LEU A CD1 1 
ATOM   4434  C  CD2 . LEU A  1 579 ? 18.880  -13.293 62.766   1.00 222.10 ? 579  LEU A CD2 1 
ATOM   4435  N  N   . ASN A  1 580 ? 15.792  -15.243 59.811   1.00 211.63 ? 580  ASN A N   1 
ATOM   4436  C  CA  . ASN A  1 580 ? 14.655  -16.047 59.391   1.00 210.34 ? 580  ASN A CA  1 
ATOM   4437  C  C   . ASN A  1 580 ? 13.443  -15.641 60.218   1.00 214.36 ? 580  ASN A C   1 
ATOM   4438  O  O   . ASN A  1 580 ? 13.555  -15.303 61.398   1.00 219.01 ? 580  ASN A O   1 
ATOM   4439  C  CB  . ASN A  1 580 ? 14.958  -17.541 59.544   1.00 210.32 ? 580  ASN A CB  1 
ATOM   4440  C  CG  . ASN A  1 580 ? 13.854  -18.424 58.975   1.00 208.20 ? 580  ASN A CG  1 
ATOM   4441  O  OD1 . ASN A  1 580 ? 13.032  -18.968 59.710   1.00 211.29 ? 580  ASN A OD1 1 
ATOM   4442  N  ND2 . ASN A  1 580 ? 13.825  -18.549 57.653   1.00 205.72 ? 580  ASN A ND2 1 
ATOM   4443  N  N   . GLN A  1 581 ? 12.272  -15.716 59.598   1.00 209.82 ? 581  GLN A N   1 
ATOM   4444  C  CA  . GLN A  1 581 ? 11.125  -14.964 60.093   1.00 210.62 ? 581  GLN A CA  1 
ATOM   4445  C  C   . GLN A  1 581 ? 10.406  -15.631 61.264   1.00 200.62 ? 581  GLN A C   1 
ATOM   4446  O  O   . GLN A  1 581 ? 9.938   -14.939 62.174   1.00 201.85 ? 581  GLN A O   1 
ATOM   4447  C  CB  . GLN A  1 581 ? 10.174  -14.717 58.929   1.00 221.82 ? 581  GLN A CB  1 
ATOM   4448  C  CG  . GLN A  1 581 ? 9.803   -15.961 58.115   1.00 216.16 ? 581  GLN A CG  1 
ATOM   4449  C  CD  . GLN A  1 581 ? 8.349   -15.974 57.674   1.00 205.73 ? 581  GLN A CD  1 
ATOM   4450  O  OE1 . GLN A  1 581 ? 7.522   -15.226 58.193   1.00 217.41 ? 581  GLN A OE1 1 
ATOM   4451  N  NE2 . GLN A  1 581 ? 8.048   -16.780 56.659   1.00 194.25 ? 581  GLN A NE2 1 
ATOM   4452  N  N   . PHE A  1 582 ? 10.263  -16.954 61.266   1.00 213.31 ? 582  PHE A N   1 
ATOM   4453  C  CA  . PHE A  1 582 ? 9.555   -17.561 62.390   1.00 219.86 ? 582  PHE A CA  1 
ATOM   4454  C  C   . PHE A  1 582 ? 10.446  -17.803 63.607   1.00 237.66 ? 582  PHE A C   1 
ATOM   4455  O  O   . PHE A  1 582 ? 9.919   -18.141 64.672   1.00 246.51 ? 582  PHE A O   1 
ATOM   4456  C  CB  . PHE A  1 582 ? 8.814   -18.826 61.956   1.00 219.95 ? 582  PHE A CB  1 
ATOM   4457  C  CG  . PHE A  1 582 ? 7.322   -18.621 61.871   1.00 226.51 ? 582  PHE A CG  1 
ATOM   4458  C  CD1 . PHE A  1 582 ? 6.792   -17.762 60.922   1.00 229.05 ? 582  PHE A CD1 1 
ATOM   4459  C  CD2 . PHE A  1 582 ? 6.456   -19.226 62.773   1.00 226.66 ? 582  PHE A CD2 1 
ATOM   4460  C  CE1 . PHE A  1 582 ? 5.425   -17.531 60.842   1.00 226.71 ? 582  PHE A CE1 1 
ATOM   4461  C  CE2 . PHE A  1 582 ? 5.081   -19.000 62.699   1.00 222.22 ? 582  PHE A CE2 1 
ATOM   4462  C  CZ  . PHE A  1 582 ? 4.568   -18.152 61.731   1.00 220.34 ? 582  PHE A CZ  1 
ATOM   4463  N  N   . THR A  1 583 ? 11.782  -17.683 63.483   1.00 235.17 ? 583  THR A N   1 
ATOM   4464  C  CA  . THR A  1 583 ? 12.652  -17.959 64.627   1.00 238.61 ? 583  THR A CA  1 
ATOM   4465  C  C   . THR A  1 583 ? 13.651  -16.847 64.961   1.00 229.05 ? 583  THR A C   1 
ATOM   4466  O  O   . THR A  1 583 ? 14.820  -17.147 65.241   1.00 231.30 ? 583  THR A O   1 
ATOM   4467  C  CB  . THR A  1 583 ? 13.453  -19.242 64.374   1.00 243.55 ? 583  THR A CB  1 
ATOM   4468  O  OG1 . THR A  1 583 ? 14.427  -19.011 63.340   1.00 246.98 ? 583  THR A OG1 1 
ATOM   4469  C  CG2 . THR A  1 583 ? 12.536  -20.382 63.950   1.00 240.23 ? 583  THR A CG2 1 
ATOM   4470  N  N   . PRO A  1 584 ? 13.264  -15.550 64.951   1.00 217.36 ? 584  PRO A N   1 
ATOM   4471  C  CA  . PRO A  1 584 ? 14.235  -14.515 65.338   1.00 225.29 ? 584  PRO A CA  1 
ATOM   4472  C  C   . PRO A  1 584 ? 14.255  -14.183 66.827   1.00 233.51 ? 584  PRO A C   1 
ATOM   4473  O  O   . PRO A  1 584 ? 15.265  -13.697 67.342   1.00 244.23 ? 584  PRO A O   1 
ATOM   4474  C  CB  . PRO A  1 584 ? 13.779  -13.306 64.519   1.00 223.19 ? 584  PRO A CB  1 
ATOM   4475  C  CG  . PRO A  1 584 ? 12.307  -13.445 64.538   1.00 217.97 ? 584  PRO A CG  1 
ATOM   4476  C  CD  . PRO A  1 584 ? 12.048  -14.926 64.388   1.00 212.53 ? 584  PRO A CD  1 
ATOM   4477  N  N   . ALA A  1 585 ? 13.143  -14.418 67.521   1.00 211.79 ? 585  ALA A N   1 
ATOM   4478  C  CA  . ALA A  1 585 ? 12.908  -13.855 68.844   1.00 213.93 ? 585  ALA A CA  1 
ATOM   4479  C  C   . ALA A  1 585 ? 13.926  -14.284 69.909   1.00 234.75 ? 585  ALA A C   1 
ATOM   4480  O  O   . ALA A  1 585 ? 14.575  -15.335 69.841   1.00 241.94 ? 585  ALA A O   1 
ATOM   4481  C  CB  . ALA A  1 585 ? 11.512  -14.231 69.323   1.00 211.59 ? 585  ALA A CB  1 
ATOM   4482  N  N   . ASN A  1 586 ? 14.031  -13.418 70.916   1.00 236.35 ? 586  ASN A N   1 
ATOM   4483  C  CA  . ASN A  1 586 ? 14.615  -13.647 72.231   1.00 228.31 ? 586  ASN A CA  1 
ATOM   4484  C  C   . ASN A  1 586 ? 13.935  -14.835 72.926   1.00 232.20 ? 586  ASN A C   1 
ATOM   4485  O  O   . ASN A  1 586 ? 12.890  -15.327 72.494   1.00 245.79 ? 586  ASN A O   1 
ATOM   4486  C  CB  . ASN A  1 586 ? 14.457  -12.365 73.048   1.00 223.43 ? 586  ASN A CB  1 
ATOM   4487  C  CG  . ASN A  1 586 ? 13.061  -11.833 72.942   1.00 243.82 ? 586  ASN A CG  1 
ATOM   4488  O  OD1 . ASN A  1 586 ? 12.112  -12.615 72.954   1.00 227.13 ? 586  ASN A OD1 1 
ATOM   4489  N  ND2 . ASN A  1 586 ? 12.899  -10.528 72.798   1.00 323.50 ? 586  ASN A ND2 1 
ATOM   4490  N  N   . ILE A  1 587 ? 14.537  -15.294 74.030   1.00 230.59 ? 587  ILE A N   1 
ATOM   4491  C  CA  . ILE A  1 587 ? 13.977  -16.394 74.808   1.00 232.62 ? 587  ILE A CA  1 
ATOM   4492  C  C   . ILE A  1 587 ? 14.062  -16.101 76.303   1.00 237.52 ? 587  ILE A C   1 
ATOM   4493  O  O   . ILE A  1 587 ? 14.897  -15.319 76.765   1.00 243.38 ? 587  ILE A O   1 
ATOM   4494  C  CB  . ILE A  1 587 ? 14.660  -17.745 74.499   1.00 239.61 ? 587  ILE A CB  1 
ATOM   4495  C  CG1 . ILE A  1 587 ? 16.181  -17.599 74.505   1.00 233.21 ? 587  ILE A CG1 1 
ATOM   4496  C  CG2 . ILE A  1 587 ? 14.172  -18.294 73.165   1.00 251.38 ? 587  ILE A CG2 1 
ATOM   4497  C  CD1 . ILE A  1 587 ? 16.907  -18.902 74.247   1.00 233.16 ? 587  ILE A CD1 1 
ATOM   4498  N  N   . SER A  1 588 ? 13.173  -16.751 77.061   1.00 239.01 ? 588  SER A N   1 
ATOM   4499  C  CA  . SER A  1 588 ? 13.054  -16.546 78.498   1.00 235.98 ? 588  SER A CA  1 
ATOM   4500  C  C   . SER A  1 588 ? 12.901  -17.875 79.236   1.00 230.43 ? 588  SER A C   1 
ATOM   4501  O  O   . SER A  1 588 ? 12.338  -18.842 78.711   1.00 231.98 ? 588  SER A O   1 
ATOM   4502  C  CB  . SER A  1 588 ? 11.868  -15.633 78.824   1.00 239.65 ? 588  SER A CB  1 
ATOM   4503  O  OG  . SER A  1 588 ? 10.648  -16.210 78.391   1.00 243.76 ? 588  SER A OG  1 
ATOM   4504  N  N   . ARG A  1 589 ? 13.419  -17.909 80.469   1.00 226.19 ? 589  ARG A N   1 
ATOM   4505  C  CA  . ARG A  1 589 ? 13.249  -19.026 81.396   1.00 228.15 ? 589  ARG A CA  1 
ATOM   4506  C  C   . ARG A  1 589 ? 13.037  -18.440 82.790   1.00 248.29 ? 589  ARG A C   1 
ATOM   4507  O  O   . ARG A  1 589 ? 12.963  -17.219 82.953   1.00 264.01 ? 589  ARG A O   1 
ATOM   4508  C  CB  . ARG A  1 589 ? 14.435  -19.995 81.333   1.00 228.59 ? 589  ARG A CB  1 
ATOM   4509  C  CG  . ARG A  1 589 ? 14.093  -21.410 81.788   1.00 229.57 ? 589  ARG A CG  1 
ATOM   4510  C  CD  . ARG A  1 589 ? 15.317  -22.297 81.881   1.00 231.56 ? 589  ARG A CD  1 
ATOM   4511  N  NE  . ARG A  1 589 ? 15.006  -23.580 82.505   1.00 231.24 ? 589  ARG A NE  1 
ATOM   4512  C  CZ  . ARG A  1 589 ? 15.899  -24.537 82.738   1.00 231.84 ? 589  ARG A CZ  1 
ATOM   4513  N  NH1 . ARG A  1 589 ? 17.168  -24.369 82.392   1.00 239.90 ? 589  ARG A NH1 1 
ATOM   4514  N  NH2 . ARG A  1 589 ? 15.519  -25.668 83.314   1.00 231.71 ? 589  ARG A NH2 1 
ATOM   4515  N  N   . GLN A  1 590 ? 12.928  -19.295 83.810   1.00 247.73 ? 590  GLN A N   1 
ATOM   4516  C  CA  . GLN A  1 590 ? 12.585  -18.794 85.139   1.00 247.58 ? 590  GLN A CA  1 
ATOM   4517  C  C   . GLN A  1 590 ? 13.029  -19.766 86.230   1.00 250.87 ? 590  GLN A C   1 
ATOM   4518  O  O   . GLN A  1 590 ? 13.087  -20.979 86.017   1.00 261.31 ? 590  GLN A O   1 
ATOM   4519  C  CB  . GLN A  1 590 ? 11.076  -18.537 85.246   1.00 239.76 ? 590  GLN A CB  1 
ATOM   4520  C  CG  . GLN A  1 590 ? 10.221  -19.768 84.966   1.00 234.10 ? 590  GLN A CG  1 
ATOM   4521  C  CD  . GLN A  1 590 ? 8.739   -19.457 84.942   1.00 228.88 ? 590  GLN A CD  1 
ATOM   4522  O  OE1 . GLN A  1 590 ? 8.339   -18.293 84.969   1.00 228.56 ? 590  GLN A OE1 1 
ATOM   4523  N  NE2 . GLN A  1 590 ? 7.914   -20.498 84.869   1.00 228.17 ? 590  GLN A NE2 1 
ATOM   4524  N  N   . ALA A  1 591 ? 13.329  -19.212 87.407   1.00 241.74 ? 591  ALA A N   1 
ATOM   4525  C  CA  . ALA A  1 591 ? 13.674  -19.978 88.598   1.00 235.92 ? 591  ALA A CA  1 
ATOM   4526  C  C   . ALA A  1 591 ? 12.728  -19.582 89.725   1.00 230.66 ? 591  ALA A C   1 
ATOM   4527  O  O   . ALA A  1 591 ? 12.163  -18.486 89.712   1.00 228.67 ? 591  ALA A O   1 
ATOM   4528  C  CB  . ALA A  1 591 ? 15.139  -19.751 89.010   1.00 235.90 ? 591  ALA A CB  1 
ATOM   4529  N  N   . HIS A  1 592 ? 12.551  -20.472 90.705   1.00 227.95 ? 592  HIS A N   1 
ATOM   4530  C  CA  . HIS A  1 592 ? 11.504  -20.294 91.706   1.00 228.79 ? 592  HIS A CA  1 
ATOM   4531  C  C   . HIS A  1 592 ? 12.015  -20.524 93.124   1.00 241.95 ? 592  HIS A C   1 
ATOM   4532  O  O   . HIS A  1 592 ? 12.956  -21.291 93.350   1.00 246.46 ? 592  HIS A O   1 
ATOM   4533  C  CB  . HIS A  1 592 ? 10.330  -21.235 91.432   1.00 224.92 ? 592  HIS A CB  1 
ATOM   4534  C  CG  . HIS A  1 592 ? 9.737   -21.069 90.069   1.00 225.32 ? 592  HIS A CG  1 
ATOM   4535  N  ND1 . HIS A  1 592 ? 8.794   -20.107 89.782   1.00 228.87 ? 592  HIS A ND1 1 
ATOM   4536  C  CD2 . HIS A  1 592 ? 9.961   -21.734 88.911   1.00 228.28 ? 592  HIS A CD2 1 
ATOM   4537  C  CE1 . HIS A  1 592 ? 8.457   -20.190 88.508   1.00 235.36 ? 592  HIS A CE1 1 
ATOM   4538  N  NE2 . HIS A  1 592 ? 9.151   -21.169 87.957   1.00 235.62 ? 592  HIS A NE2 1 
ATOM   4539  N  N   . ILE A  1 593 ? 11.361  -19.854 94.077   1.00 242.52 ? 593  ILE A N   1 
ATOM   4540  C  CA  . ILE A  1 593 ? 11.624  -19.992 95.508   1.00 228.49 ? 593  ILE A CA  1 
ATOM   4541  C  C   . ILE A  1 593 ? 10.440  -20.721 96.124   1.00 222.82 ? 593  ILE A C   1 
ATOM   4542  O  O   . ILE A  1 593 ? 9.306   -20.221 96.095   1.00 225.63 ? 593  ILE A O   1 
ATOM   4543  C  CB  . ILE A  1 593 ? 11.837  -18.630 96.192   1.00 220.05 ? 593  ILE A CB  1 
ATOM   4544  C  CG1 . ILE A  1 593 ? 12.793  -17.749 95.388   1.00 221.41 ? 593  ILE A CG1 1 
ATOM   4545  C  CG2 . ILE A  1 593 ? 12.342  -18.819 97.618   1.00 220.94 ? 593  ILE A CG2 1 
ATOM   4546  C  CD1 . ILE A  1 593 ? 12.088  -16.728 94.516   1.00 221.24 ? 593  ILE A CD1 1 
ATOM   4547  N  N   . LEU A  1 594 ? 10.700  -21.896 96.681   1.00 210.92 ? 594  LEU A N   1 
ATOM   4548  C  CA  . LEU A  1 594 ? 9.642   -22.723 97.236   1.00 222.44 ? 594  LEU A CA  1 
ATOM   4549  C  C   . LEU A  1 594 ? 9.781   -22.840 98.749   1.00 279.50 ? 594  LEU A C   1 
ATOM   4550  O  O   . LEU A  1 594 ? 10.660  -22.249 99.392   1.00 207.32 ? 594  LEU A O   1 
ATOM   4551  C  CB  . LEU A  1 594 ? 9.627   -24.116 96.600   1.00 222.18 ? 594  LEU A CB  1 
ATOM   4552  C  CG  . LEU A  1 594 ? 9.066   -24.309 95.181   1.00 201.73 ? 594  LEU A CG  1 
ATOM   4553  C  CD1 . LEU A  1 594 ? 10.147  -24.114 94.124   1.00 200.22 ? 594  LEU A CD1 1 
ATOM   4554  C  CD2 . LEU A  1 594 ? 8.406   -25.680 95.028   1.00 202.14 ? 594  LEU A CD2 1 
ATOM   4555  N  N   . LEU A  1 595 ? 8.892   -23.650 99.301   1.00 186.46 ? 595  LEU A N   1 
ATOM   4556  C  CA  . LEU A  1 595 ? 8.583   -23.659 100.721  1.00 222.03 ? 595  LEU A CA  1 
ATOM   4557  C  C   . LEU A  1 595 ? 7.539   -24.745 100.940  1.00 211.34 ? 595  LEU A C   1 
ATOM   4558  O  O   . LEU A  1 595 ? 6.755   -25.048 100.033  1.00 179.45 ? 595  LEU A O   1 
ATOM   4559  C  CB  . LEU A  1 595 ? 8.093   -22.261 101.209  1.00 224.55 ? 595  LEU A CB  1 
ATOM   4560  C  CG  . LEU A  1 595 ? 6.715   -21.556 101.160  1.00 218.70 ? 595  LEU A CG  1 
ATOM   4561  C  CD1 . LEU A  1 595 ? 6.803   -20.155 101.893  1.00 216.88 ? 595  LEU A CD1 1 
ATOM   4562  C  CD2 . LEU A  1 595 ? 6.114   -21.461 99.747   1.00 200.59 ? 595  LEU A CD2 1 
ATOM   4563  N  N   . ASP A  1 596 ? 7.564   -25.342 102.136  1.00 175.48 ? 596  ASP A N   1 
ATOM   4564  C  CA  . ASP A  1 596 ? 6.569   -26.328 102.630  1.00 151.81 ? 596  ASP A CA  1 
ATOM   4565  C  C   . ASP A  1 596 ? 6.495   -27.637 101.822  1.00 158.38 ? 596  ASP A C   1 
ATOM   4566  O  O   . ASP A  1 596 ? 5.551   -28.437 101.935  1.00 163.74 ? 596  ASP A O   1 
ATOM   4567  C  CB  . ASP A  1 596 ? 5.168   -25.708 102.693  1.00 191.42 ? 596  ASP A CB  1 
ATOM   4568  C  CG  . ASP A  1 596 ? 5.116   -24.345 103.497  1.00 169.24 ? 596  ASP A CG  1 
ATOM   4569  O  OD1 . ASP A  1 596 ? 6.153   -23.575 103.545  1.00 167.84 ? 596  ASP A OD1 1 
ATOM   4570  O  OD2 . ASP A  1 596 ? 4.002   -24.056 104.083  1.00 159.33 ? 596  ASP A OD2 1 
ATOM   4571  N  N   . ASP B  2 3   ? -48.611 2.916   38.685   1.00 282.12 ? 113  ASP B N   1 
ATOM   4572  C  CA  . ASP B  2 3   ? -48.070 4.025   37.910   1.00 279.20 ? 113  ASP B CA  1 
ATOM   4573  C  C   . ASP B  2 3   ? -46.688 4.419   38.416   1.00 265.79 ? 113  ASP B C   1 
ATOM   4574  O  O   . ASP B  2 3   ? -46.533 4.815   39.572   1.00 265.39 ? 113  ASP B O   1 
ATOM   4575  C  CB  . ASP B  2 3   ? -49.011 5.225   37.966   1.00 292.61 ? 113  ASP B CB  1 
ATOM   4576  C  CG  . ASP B  2 3   ? -48.572 6.344   37.053   1.00 291.42 ? 113  ASP B CG  1 
ATOM   4577  O  OD1 . ASP B  2 3   ? -47.871 6.063   36.058   1.00 283.52 ? 113  ASP B OD1 1 
ATOM   4578  O  OD2 . ASP B  2 3   ? -48.922 7.507   37.336   1.00 298.77 ? 113  ASP B OD2 1 
ATOM   4579  N  N   . TYR B  2 4   ? -45.682 4.322   37.541   1.00 270.75 ? 114  TYR B N   1 
ATOM   4580  C  CA  . TYR B  2 4   ? -44.316 4.576   37.974   1.00 258.03 ? 114  TYR B CA  1 
ATOM   4581  C  C   . TYR B  2 4   ? -43.436 4.919   36.785   1.00 253.14 ? 114  TYR B C   1 
ATOM   4582  O  O   . TYR B  2 4   ? -43.568 4.284   35.729   1.00 250.71 ? 114  TYR B O   1 
ATOM   4583  C  CB  . TYR B  2 4   ? -43.755 3.363   38.722   1.00 249.31 ? 114  TYR B CB  1 
ATOM   4584  C  CG  . TYR B  2 4   ? -42.413 3.607   39.362   1.00 252.21 ? 114  TYR B CG  1 
ATOM   4585  C  CD1 . TYR B  2 4   ? -42.314 4.283   40.569   1.00 256.74 ? 114  TYR B CD1 1 
ATOM   4586  C  CD2 . TYR B  2 4   ? -41.245 3.144   38.770   1.00 238.19 ? 114  TYR B CD2 1 
ATOM   4587  C  CE1 . TYR B  2 4   ? -41.087 4.506   41.162   1.00 260.09 ? 114  TYR B CE1 1 
ATOM   4588  C  CE2 . TYR B  2 4   ? -40.012 3.361   39.356   1.00 218.05 ? 114  TYR B CE2 1 
ATOM   4589  C  CZ  . TYR B  2 4   ? -39.939 4.042   40.553   1.00 244.47 ? 114  TYR B CZ  1 
ATOM   4590  O  OH  . TYR B  2 4   ? -38.715 4.263   41.144   1.00 221.99 ? 114  TYR B OH  1 
ATOM   4591  N  N   . PRO B  2 5   ? -42.571 5.928   36.904   1.00 258.53 ? 115  PRO B N   1 
ATOM   4592  C  CA  . PRO B  2 5   ? -41.694 6.317   35.788   1.00 260.07 ? 115  PRO B CA  1 
ATOM   4593  C  C   . PRO B  2 5   ? -40.729 5.214   35.370   1.00 224.45 ? 115  PRO B C   1 
ATOM   4594  O  O   . PRO B  2 5   ? -40.222 4.456   36.198   1.00 217.39 ? 115  PRO B O   1 
ATOM   4595  C  CB  . PRO B  2 5   ? -40.940 7.531   36.344   1.00 256.89 ? 115  PRO B CB  1 
ATOM   4596  C  CG  . PRO B  2 5   ? -41.841 8.073   37.421   1.00 264.98 ? 115  PRO B CG  1 
ATOM   4597  C  CD  . PRO B  2 5   ? -42.483 6.863   38.037   1.00 260.47 ? 115  PRO B CD  1 
ATOM   4598  N  N   . VAL B  2 6   ? -40.459 5.148   34.065   1.00 211.03 ? 116  VAL B N   1 
ATOM   4599  C  CA  . VAL B  2 6   ? -39.593 4.125   33.485   1.00 200.98 ? 116  VAL B CA  1 
ATOM   4600  C  C   . VAL B  2 6   ? -38.741 4.741   32.382   1.00 207.83 ? 116  VAL B C   1 
ATOM   4601  O  O   . VAL B  2 6   ? -39.250 5.491   31.542   1.00 209.47 ? 116  VAL B O   1 
ATOM   4602  C  CB  . VAL B  2 6   ? -40.409 2.942   32.934   1.00 204.98 ? 116  VAL B CB  1 
ATOM   4603  C  CG1 . VAL B  2 6   ? -39.570 2.115   31.985   1.00 196.47 ? 116  VAL B CG1 1 
ATOM   4604  C  CG2 . VAL B  2 6   ? -40.895 2.073   34.078   1.00 205.93 ? 116  VAL B CG2 1 
ATOM   4605  N  N   . ASP B  2 7   ? -37.442 4.432   32.392   1.00 185.54 ? 117  ASP B N   1 
ATOM   4606  C  CA  . ASP B  2 7   ? -36.509 4.813   31.339   1.00 180.78 ? 117  ASP B CA  1 
ATOM   4607  C  C   . ASP B  2 7   ? -35.987 3.569   30.632   1.00 173.80 ? 117  ASP B C   1 
ATOM   4608  O  O   . ASP B  2 7   ? -35.717 2.550   31.275   1.00 167.93 ? 117  ASP B O   1 
ATOM   4609  C  CB  . ASP B  2 7   ? -35.324 5.601   31.895   1.00 211.47 ? 117  ASP B CB  1 
ATOM   4610  C  CG  . ASP B  2 7   ? -35.739 6.884   32.561   1.00 202.45 ? 117  ASP B CG  1 
ATOM   4611  O  OD1 . ASP B  2 7   ? -36.836 7.398   32.248   1.00 194.74 ? 117  ASP B OD1 1 
ATOM   4612  O  OD2 . ASP B  2 7   ? -34.958 7.375   33.399   1.00 176.19 ? 117  ASP B OD2 1 
ATOM   4613  N  N   . LEU B  2 8   ? -35.853 3.648   29.309   1.00 174.94 ? 118  LEU B N   1 
ATOM   4614  C  CA  . LEU B  2 8   ? -35.367 2.524   28.507   1.00 169.21 ? 118  LEU B CA  1 
ATOM   4615  C  C   . LEU B  2 8   ? -34.364 3.038   27.479   1.00 169.19 ? 118  LEU B C   1 
ATOM   4616  O  O   . LEU B  2 8   ? -34.726 3.830   26.606   1.00 198.43 ? 118  LEU B O   1 
ATOM   4617  C  CB  . LEU B  2 8   ? -36.531 1.793   27.833   1.00 201.70 ? 118  LEU B CB  1 
ATOM   4618  C  CG  . LEU B  2 8   ? -36.280 0.460   27.113   1.00 192.46 ? 118  LEU B CG  1 
ATOM   4619  C  CD1 . LEU B  2 8   ? -35.906 0.666   25.654   1.00 190.91 ? 118  LEU B CD1 1 
ATOM   4620  C  CD2 . LEU B  2 8   ? -35.197 -0.332  27.820   1.00 162.45 ? 118  LEU B CD2 1 
ATOM   4621  N  N   . TYR B  2 9   ? -33.104 2.614   27.592   1.00 176.67 ? 119  TYR B N   1 
ATOM   4622  C  CA  . TYR B  2 9   ? -32.070 2.960   26.619   1.00 160.65 ? 119  TYR B CA  1 
ATOM   4623  C  C   . TYR B  2 9   ? -31.889 1.807   25.640   1.00 148.53 ? 119  TYR B C   1 
ATOM   4624  O  O   . TYR B  2 9   ? -31.784 0.647   26.050   1.00 173.70 ? 119  TYR B O   1 
ATOM   4625  C  CB  . TYR B  2 9   ? -30.738 3.281   27.300   1.00 142.63 ? 119  TYR B CB  1 
ATOM   4626  C  CG  . TYR B  2 9   ? -29.770 4.051   26.422   1.00 141.16 ? 119  TYR B CG  1 
ATOM   4627  C  CD1 . TYR B  2 9   ? -29.778 5.442   26.396   1.00 158.64 ? 119  TYR B CD1 1 
ATOM   4628  C  CD2 . TYR B  2 9   ? -28.855 3.393   25.614   1.00 145.96 ? 119  TYR B CD2 1 
ATOM   4629  C  CE1 . TYR B  2 9   ? -28.892 6.155   25.595   1.00 147.91 ? 119  TYR B CE1 1 
ATOM   4630  C  CE2 . TYR B  2 9   ? -27.963 4.099   24.809   1.00 134.75 ? 119  TYR B CE2 1 
ATOM   4631  C  CZ  . TYR B  2 9   ? -27.989 5.477   24.804   1.00 139.93 ? 119  TYR B CZ  1 
ATOM   4632  O  OH  . TYR B  2 9   ? -27.113 6.181   24.008   1.00 140.03 ? 119  TYR B OH  1 
ATOM   4633  N  N   . TYR B  2 10  ? -31.840 2.129   24.353   1.00 152.09 ? 120  TYR B N   1 
ATOM   4634  C  CA  . TYR B  2 10  ? -31.777 1.126   23.295   1.00 151.24 ? 120  TYR B CA  1 
ATOM   4635  C  C   . TYR B  2 10  ? -30.363 1.097   22.725   1.00 143.76 ? 120  TYR B C   1 
ATOM   4636  O  O   . TYR B  2 10  ? -29.965 2.001   21.985   1.00 146.16 ? 120  TYR B O   1 
ATOM   4637  C  CB  . TYR B  2 10  ? -32.814 1.420   22.220   1.00 161.80 ? 120  TYR B CB  1 
ATOM   4638  C  CG  . TYR B  2 10  ? -33.134 0.235   21.345   1.00 162.98 ? 120  TYR B CG  1 
ATOM   4639  C  CD1 . TYR B  2 10  ? -33.909 -0.810  21.821   1.00 164.21 ? 120  TYR B CD1 1 
ATOM   4640  C  CD2 . TYR B  2 10  ? -32.670 0.166   20.041   1.00 163.52 ? 120  TYR B CD2 1 
ATOM   4641  C  CE1 . TYR B  2 10  ? -34.205 -1.898  21.026   1.00 184.67 ? 120  TYR B CE1 1 
ATOM   4642  C  CE2 . TYR B  2 10  ? -32.962 -0.914  19.239   1.00 165.06 ? 120  TYR B CE2 1 
ATOM   4643  C  CZ  . TYR B  2 10  ? -33.730 -1.946  19.735   1.00 185.88 ? 120  TYR B CZ  1 
ATOM   4644  O  OH  . TYR B  2 10  ? -34.028 -3.030  18.938   1.00 200.19 ? 120  TYR B OH  1 
ATOM   4645  N  N   . LEU B  2 11  ? -29.607 0.055   23.078   1.00 135.28 ? 121  LEU B N   1 
ATOM   4646  C  CA  . LEU B  2 11  ? -28.215 -0.111  22.653   1.00 127.94 ? 121  LEU B CA  1 
ATOM   4647  C  C   . LEU B  2 11  ? -28.144 -1.103  21.492   1.00 127.90 ? 121  LEU B C   1 
ATOM   4648  O  O   . LEU B  2 11  ? -28.230 -2.318  21.692   1.00 124.66 ? 121  LEU B O   1 
ATOM   4649  C  CB  . LEU B  2 11  ? -27.365 -0.571  23.828   1.00 119.13 ? 121  LEU B CB  1 
ATOM   4650  C  CG  . LEU B  2 11  ? -25.867 -0.406  23.623   1.00 117.87 ? 121  LEU B CG  1 
ATOM   4651  C  CD1 . LEU B  2 11  ? -25.571 1.056   23.320   1.00 116.09 ? 121  LEU B CD1 1 
ATOM   4652  C  CD2 . LEU B  2 11  ? -25.127 -0.877  24.863   1.00 148.82 ? 121  LEU B CD2 1 
ATOM   4653  N  N   . MET B  2 12  ? -27.948 -0.588  20.279   1.00 157.62 ? 122  MET B N   1 
ATOM   4654  C  CA  . MET B  2 12  ? -27.943 -1.407  19.073   1.00 139.88 ? 122  MET B CA  1 
ATOM   4655  C  C   . MET B  2 12  ? -26.525 -1.668  18.574   1.00 126.50 ? 122  MET B C   1 
ATOM   4656  O  O   . MET B  2 12  ? -25.691 -0.758  18.525   1.00 125.03 ? 122  MET B O   1 
ATOM   4657  C  CB  . MET B  2 12  ? -28.749 -0.735  17.961   1.00 150.66 ? 122  MET B CB  1 
ATOM   4658  C  CG  . MET B  2 12  ? -29.068 -1.650  16.798   1.00 146.65 ? 122  MET B CG  1 
ATOM   4659  S  SD  . MET B  2 12  ? -29.212 -0.751  15.242   1.00 196.43 ? 122  MET B SD  1 
ATOM   4660  C  CE  . MET B  2 12  ? -30.606 0.328   15.550   1.00 197.89 ? 122  MET B CE  1 
ATOM   4661  N  N   . ASP B  2 13  ? -26.283 -2.905  18.148   1.00 123.40 ? 123  ASP B N   1 
ATOM   4662  C  CA  . ASP B  2 13  ? -25.025 -3.302  17.526   1.00 118.24 ? 123  ASP B CA  1 
ATOM   4663  C  C   . ASP B  2 13  ? -25.092 -3.033  16.033   1.00 124.53 ? 123  ASP B C   1 
ATOM   4664  O  O   . ASP B  2 13  ? -25.897 -3.642  15.324   1.00 168.37 ? 123  ASP B O   1 
ATOM   4665  C  CB  . ASP B  2 13  ? -24.750 -4.784  17.759   1.00 112.60 ? 123  ASP B CB  1 
ATOM   4666  C  CG  . ASP B  2 13  ? -23.566 -5.291  16.966   1.00 108.68 ? 123  ASP B CG  1 
ATOM   4667  O  OD1 . ASP B  2 13  ? -22.634 -4.510  16.694   1.00 107.38 ? 123  ASP B OD1 1 
ATOM   4668  O  OD2 . ASP B  2 13  ? -23.597 -6.476  16.577   1.00 107.65 ? 123  ASP B OD2 1 
ATOM   4669  N  N   . LEU B  2 14  ? -24.242 -2.142  15.550   1.00 124.73 ? 124  LEU B N   1 
ATOM   4670  C  CA  . LEU B  2 14  ? -24.232 -1.832  14.136   1.00 131.08 ? 124  LEU B CA  1 
ATOM   4671  C  C   . LEU B  2 14  ? -23.171 -2.611  13.381   1.00 129.08 ? 124  LEU B C   1 
ATOM   4672  O  O   . LEU B  2 14  ? -22.900 -2.295  12.221   1.00 149.03 ? 124  LEU B O   1 
ATOM   4673  C  CB  . LEU B  2 14  ? -24.027 -0.333  13.934   1.00 135.48 ? 124  LEU B CB  1 
ATOM   4674  C  CG  . LEU B  2 14  ? -25.267 0.513   14.199   1.00 142.85 ? 124  LEU B CG  1 
ATOM   4675  C  CD1 . LEU B  2 14  ? -24.996 1.970   13.900   1.00 154.64 ? 124  LEU B CD1 1 
ATOM   4676  C  CD2 . LEU B  2 14  ? -26.391 0.006   13.328   1.00 150.44 ? 124  LEU B CD2 1 
ATOM   4677  N  N   . SER B  2 15  ? -22.596 -3.646  13.987   1.00 122.03 ? 125  SER B N   1 
ATOM   4678  C  CA  . SER B  2 15  ? -21.491 -4.348  13.351   1.00 121.57 ? 125  SER B CA  1 
ATOM   4679  C  C   . SER B  2 15  ? -21.958 -5.072  12.086   1.00 129.91 ? 125  SER B C   1 
ATOM   4680  O  O   . SER B  2 15  ? -23.143 -5.095  11.736   1.00 135.87 ? 125  SER B O   1 
ATOM   4681  C  CB  . SER B  2 15  ? -20.837 -5.315  14.336   1.00 112.90 ? 125  SER B CB  1 
ATOM   4682  O  OG  . SER B  2 15  ? -21.727 -6.347  14.721   1.00 112.32 ? 125  SER B OG  1 
ATOM   4683  N  N   . ALA B  2 16  ? -20.997 -5.704  11.409   1.00 130.70 ? 126  ALA B N   1 
ATOM   4684  C  CA  . ALA B  2 16  ? -21.264 -6.255  10.088   1.00 139.38 ? 126  ALA B CA  1 
ATOM   4685  C  C   . ALA B  2 16  ? -22.202 -7.448  10.159   1.00 140.76 ? 126  ALA B C   1 
ATOM   4686  O  O   . ALA B  2 16  ? -22.972 -7.686  9.224    1.00 149.11 ? 126  ALA B O   1 
ATOM   4687  C  CB  . ALA B  2 16  ? -19.952 -6.640  9.404    1.00 139.92 ? 126  ALA B CB  1 
ATOM   4688  N  N   . SER B  2 17  ? -22.184 -8.187  11.257   1.00 133.28 ? 127  SER B N   1 
ATOM   4689  C  CA  . SER B  2 17  ? -23.006 -9.381  11.355   1.00 134.65 ? 127  SER B CA  1 
ATOM   4690  C  C   . SER B  2 17  ? -24.466 -9.052  11.595   1.00 138.15 ? 127  SER B C   1 
ATOM   4691  O  O   . SER B  2 17  ? -25.275 -9.965  11.817   1.00 139.31 ? 127  SER B O   1 
ATOM   4692  C  CB  . SER B  2 17  ? -22.477 -10.301 12.464   1.00 136.22 ? 127  SER B CB  1 
ATOM   4693  O  OG  . SER B  2 17  ? -22.294 -9.606  13.691   1.00 118.41 ? 127  SER B OG  1 
ATOM   4694  N  N   . MET B  2 18  ? -24.826 -7.774  11.516   1.00 140.72 ? 128  MET B N   1 
ATOM   4695  C  CA  . MET B  2 18  ? -26.160 -7.320  11.867   1.00 144.01 ? 128  MET B CA  1 
ATOM   4696  C  C   . MET B  2 18  ? -27.000 -6.935  10.655   1.00 155.56 ? 128  MET B C   1 
ATOM   4697  O  O   . MET B  2 18  ? -28.133 -6.468  10.825   1.00 160.00 ? 128  MET B O   1 
ATOM   4698  C  CB  . MET B  2 18  ? -26.050 -6.139  12.830   1.00 138.73 ? 128  MET B CB  1 
ATOM   4699  C  CG  . MET B  2 18  ? -25.533 -6.505  14.205   1.00 128.09 ? 128  MET B CG  1 
ATOM   4700  S  SD  . MET B  2 18  ? -26.705 -7.473  15.160   1.00 126.54 ? 128  MET B SD  1 
ATOM   4701  C  CE  . MET B  2 18  ? -28.087 -6.335  15.210   1.00 135.87 ? 128  MET B CE  1 
ATOM   4702  N  N   . ASP B  2 19  ? -26.494 -7.146  9.435    1.00 161.20 ? 129  ASP B N   1 
ATOM   4703  C  CA  . ASP B  2 19  ? -27.289 -6.829  8.253    1.00 172.89 ? 129  ASP B CA  1 
ATOM   4704  C  C   . ASP B  2 19  ? -28.461 -7.787  8.115    1.00 178.53 ? 129  ASP B C   1 
ATOM   4705  O  O   . ASP B  2 19  ? -29.528 -7.403  7.621    1.00 208.98 ? 129  ASP B O   1 
ATOM   4706  C  CB  . ASP B  2 19  ? -26.418 -6.862  6.995    1.00 192.24 ? 129  ASP B CB  1 
ATOM   4707  C  CG  . ASP B  2 19  ? -27.213 -6.586  5.724    1.00 215.98 ? 129  ASP B CG  1 
ATOM   4708  O  OD1 . ASP B  2 19  ? -27.477 -5.401  5.423    1.00 195.55 ? 129  ASP B OD1 1 
ATOM   4709  O  OD2 . ASP B  2 19  ? -27.579 -7.557  5.025    1.00 218.97 ? 129  ASP B OD2 1 
ATOM   4710  N  N   . ASP B  2 20  ? -28.286 -9.028  8.561    1.00 173.41 ? 130  ASP B N   1 
ATOM   4711  C  CA  . ASP B  2 20  ? -29.355 -10.013 8.556    1.00 183.59 ? 130  ASP B CA  1 
ATOM   4712  C  C   . ASP B  2 20  ? -30.322 -9.805  9.705    1.00 174.99 ? 130  ASP B C   1 
ATOM   4713  O  O   . ASP B  2 20  ? -31.395 -10.417 9.724    1.00 180.14 ? 130  ASP B O   1 
ATOM   4714  C  CB  . ASP B  2 20  ? -28.767 -11.427 8.627    1.00 193.80 ? 130  ASP B CB  1 
ATOM   4715  C  CG  . ASP B  2 20  ? -27.765 -11.591 9.763    1.00 161.72 ? 130  ASP B CG  1 
ATOM   4716  O  OD1 . ASP B  2 20  ? -27.025 -10.629 10.055   1.00 157.02 ? 130  ASP B OD1 1 
ATOM   4717  O  OD2 . ASP B  2 20  ? -27.711 -12.678 10.372   1.00 157.40 ? 130  ASP B OD2 1 
ATOM   4718  N  N   . ASP B  2 21  ? -29.966 -8.963  10.660   1.00 167.61 ? 131  ASP B N   1 
ATOM   4719  C  CA  . ASP B  2 21  ? -30.769 -8.758  11.844   1.00 164.52 ? 131  ASP B CA  1 
ATOM   4720  C  C   . ASP B  2 21  ? -31.253 -7.322  11.917   1.00 168.00 ? 131  ASP B C   1 
ATOM   4721  O  O   . ASP B  2 21  ? -31.904 -6.945  12.898   1.00 167.83 ? 131  ASP B O   1 
ATOM   4722  C  CB  . ASP B  2 21  ? -29.948 -9.089  13.092   1.00 152.48 ? 131  ASP B CB  1 
ATOM   4723  C  CG  . ASP B  2 21  ? -28.891 -10.162 12.836   1.00 157.55 ? 131  ASP B CG  1 
ATOM   4724  O  OD1 . ASP B  2 21  ? -29.157 -11.201 12.193   1.00 152.91 ? 131  ASP B OD1 1 
ATOM   4725  O  OD2 . ASP B  2 21  ? -27.744 -9.934  13.262   1.00 168.02 ? 131  ASP B OD2 1 
ATOM   4726  N  N   . LEU B  2 22  ? -30.905 -6.503  10.922   1.00 173.24 ? 132  LEU B N   1 
ATOM   4727  C  CA  . LEU B  2 22  ? -31.234 -5.081  10.942   1.00 181.13 ? 132  LEU B CA  1 
ATOM   4728  C  C   . LEU B  2 22  ? -32.741 -4.852  10.973   1.00 193.61 ? 132  LEU B C   1 
ATOM   4729  O  O   . LEU B  2 22  ? -33.252 -4.117  11.827   1.00 203.08 ? 132  LEU B O   1 
ATOM   4730  C  CB  . LEU B  2 22  ? -30.616 -4.402  9.720    1.00 199.66 ? 132  LEU B CB  1 
ATOM   4731  C  CG  . LEU B  2 22  ? -30.891 -2.911  9.521    1.00 209.78 ? 132  LEU B CG  1 
ATOM   4732  C  CD1 . LEU B  2 22  ? -30.330 -2.108  10.682   1.00 184.71 ? 132  LEU B CD1 1 
ATOM   4733  C  CD2 . LEU B  2 22  ? -30.323 -2.431  8.190    1.00 207.30 ? 132  LEU B CD2 1 
ATOM   4734  N  N   . ASN B  2 23  ? -33.474 -5.488  10.053   1.00 195.07 ? 133  ASN B N   1 
ATOM   4735  C  CA  . ASN B  2 23  ? -34.909 -5.253  9.945    1.00 206.02 ? 133  ASN B CA  1 
ATOM   4736  C  C   . ASN B  2 23  ? -35.652 -5.698  11.193   1.00 204.98 ? 133  ASN B C   1 
ATOM   4737  O  O   . ASN B  2 23  ? -36.771 -5.234  11.437   1.00 213.66 ? 133  ASN B O   1 
ATOM   4738  C  CB  . ASN B  2 23  ? -35.474 -5.975  8.722    1.00 216.06 ? 133  ASN B CB  1 
ATOM   4739  C  CG  . ASN B  2 23  ? -35.237 -7.466  8.772    1.00 216.68 ? 133  ASN B CG  1 
ATOM   4740  O  OD1 . ASN B  2 23  ? -34.231 -7.926  9.312    1.00 210.08 ? 133  ASN B OD1 1 
ATOM   4741  N  ND2 . ASN B  2 23  ? -36.169 -8.233  8.220    1.00 221.34 ? 133  ASN B ND2 1 
ATOM   4742  N  N   . THR B  2 24  ? -35.050 -6.580  11.991   1.00 195.41 ? 134  THR B N   1 
ATOM   4743  C  CA  . THR B  2 24  ? -35.673 -7.002  13.237   1.00 193.82 ? 134  THR B CA  1 
ATOM   4744  C  C   . THR B  2 24  ? -35.553 -5.922  14.297   1.00 190.48 ? 134  THR B C   1 
ATOM   4745  O  O   . THR B  2 24  ? -36.428 -5.795  15.160   1.00 194.18 ? 134  THR B O   1 
ATOM   4746  C  CB  . THR B  2 24  ? -35.018 -8.287  13.750   1.00 184.61 ? 134  THR B CB  1 
ATOM   4747  O  OG1 . THR B  2 24  ? -35.033 -9.295  12.730   1.00 187.51 ? 134  THR B OG1 1 
ATOM   4748  C  CG2 . THR B  2 24  ? -35.757 -8.795  14.953   1.00 184.90 ? 134  THR B CG2 1 
ATOM   4749  N  N   . ILE B  2 25  ? -34.493 -5.123  14.223   1.00 190.09 ? 135  ILE B N   1 
ATOM   4750  C  CA  . ILE B  2 25  ? -34.261 -4.091  15.222   1.00 180.80 ? 135  ILE B CA  1 
ATOM   4751  C  C   . ILE B  2 25  ? -35.158 -2.889  14.973   1.00 191.19 ? 135  ILE B C   1 
ATOM   4752  O  O   . ILE B  2 25  ? -35.689 -2.290  15.915   1.00 199.37 ? 135  ILE B O   1 
ATOM   4753  C  CB  . ILE B  2 25  ? -32.772 -3.713  15.227   1.00 171.02 ? 135  ILE B CB  1 
ATOM   4754  C  CG1 . ILE B  2 25  ? -31.932 -4.944  15.566   1.00 161.29 ? 135  ILE B CG1 1 
ATOM   4755  C  CG2 . ILE B  2 25  ? -32.510 -2.609  16.213   1.00 172.56 ? 135  ILE B CG2 1 
ATOM   4756  C  CD1 . ILE B  2 25  ? -32.523 -5.779  16.672   1.00 159.60 ? 135  ILE B CD1 1 
ATOM   4757  N  N   . LYS B  2 26  ? -35.356 -2.529  13.705   1.00 198.73 ? 136  LYS B N   1 
ATOM   4758  C  CA  . LYS B  2 26  ? -36.259 -1.431  13.385   1.00 213.77 ? 136  LYS B CA  1 
ATOM   4759  C  C   . LYS B  2 26  ? -37.702 -1.808  13.692   1.00 229.37 ? 136  LYS B C   1 
ATOM   4760  O  O   . LYS B  2 26  ? -38.490 -0.954  14.115   1.00 240.49 ? 136  LYS B O   1 
ATOM   4761  C  CB  . LYS B  2 26  ? -36.093 -1.038  11.915   1.00 224.23 ? 136  LYS B CB  1 
ATOM   4762  C  CG  . LYS B  2 26  ? -34.672 -0.608  11.548   1.00 208.23 ? 136  LYS B CG  1 
ATOM   4763  C  CD  . LYS B  2 26  ? -34.561 -0.162  10.097   1.00 216.52 ? 136  LYS B CD  1 
ATOM   4764  C  CE  . LYS B  2 26  ? -33.120 0.156   9.730    1.00 208.07 ? 136  LYS B CE  1 
ATOM   4765  N  NZ  . LYS B  2 26  ? -32.977 0.554   8.306    1.00 215.72 ? 136  LYS B NZ  1 
ATOM   4766  N  N   . GLU B  2 27  ? -38.059 -3.080  13.496   1.00 227.75 ? 137  GLU B N   1 
ATOM   4767  C  CA  . GLU B  2 27  ? -39.374 -3.564  13.889   1.00 235.82 ? 137  GLU B CA  1 
ATOM   4768  C  C   . GLU B  2 27  ? -39.482 -3.751  15.391   1.00 222.79 ? 137  GLU B C   1 
ATOM   4769  O  O   . GLU B  2 27  ? -40.595 -3.882  15.910   1.00 230.40 ? 137  GLU B O   1 
ATOM   4770  C  CB  . GLU B  2 27  ? -39.691 -4.885  13.182   1.00 232.70 ? 137  GLU B CB  1 
ATOM   4771  C  CG  . GLU B  2 27  ? -40.271 -4.730  11.788   1.00 242.93 ? 137  GLU B CG  1 
ATOM   4772  C  CD  . GLU B  2 27  ? -40.913 -6.009  11.286   1.00 253.05 ? 137  GLU B CD  1 
ATOM   4773  O  OE1 . GLU B  2 27  ? -41.181 -6.100  10.069   1.00 262.03 ? 137  GLU B OE1 1 
ATOM   4774  O  OE2 . GLU B  2 27  ? -41.141 -6.926  12.106   1.00 245.52 ? 137  GLU B OE2 1 
ATOM   4775  N  N   . LEU B  2 28  ? -38.351 -3.779  16.091   1.00 210.36 ? 138  LEU B N   1 
ATOM   4776  C  CA  . LEU B  2 28  ? -38.347 -3.792  17.545   1.00 205.02 ? 138  LEU B CA  1 
ATOM   4777  C  C   . LEU B  2 28  ? -38.406 -2.385  18.119   1.00 206.60 ? 138  LEU B C   1 
ATOM   4778  O  O   . LEU B  2 28  ? -39.026 -2.170  19.163   1.00 208.85 ? 138  LEU B O   1 
ATOM   4779  C  CB  . LEU B  2 28  ? -37.108 -4.522  18.062   1.00 191.55 ? 138  LEU B CB  1 
ATOM   4780  C  CG  . LEU B  2 28  ? -36.946 -4.538  19.579   1.00 185.30 ? 138  LEU B CG  1 
ATOM   4781  C  CD1 . LEU B  2 28  ? -38.213 -5.039  20.246   1.00 192.72 ? 138  LEU B CD1 1 
ATOM   4782  C  CD2 . LEU B  2 28  ? -35.777 -5.412  19.955   1.00 173.30 ? 138  LEU B CD2 1 
ATOM   4783  N  N   . GLY B  2 29  ? -37.767 -1.423  17.460   1.00 205.93 ? 139  GLY B N   1 
ATOM   4784  C  CA  . GLY B  2 29  ? -37.826 -0.045  17.893   1.00 208.47 ? 139  GLY B CA  1 
ATOM   4785  C  C   . GLY B  2 29  ? -39.224 0.536   17.837   1.00 221.94 ? 139  GLY B C   1 
ATOM   4786  O  O   . GLY B  2 29  ? -39.738 1.026   18.847   1.00 224.21 ? 139  GLY B O   1 
ATOM   4787  N  N   . SER B  2 30  ? -39.850 0.490   16.657   1.00 231.53 ? 140  SER B N   1 
ATOM   4788  C  CA  . SER B  2 30  ? -41.182 1.067   16.504   1.00 245.56 ? 140  SER B CA  1 
ATOM   4789  C  C   . SER B  2 30  ? -42.203 0.334   17.362   1.00 249.68 ? 140  SER B C   1 
ATOM   4790  O  O   . SER B  2 30  ? -43.103 0.955   17.939   1.00 257.78 ? 140  SER B O   1 
ATOM   4791  C  CB  . SER B  2 30  ? -41.602 1.033   15.035   1.00 255.10 ? 140  SER B CB  1 
ATOM   4792  O  OG  . SER B  2 30  ? -41.775 -0.301  14.588   1.00 254.84 ? 140  SER B OG  1 
ATOM   4793  N  N   . ARG B  2 31  ? -42.068 -0.990  17.471   1.00 244.62 ? 141  ARG B N   1 
ATOM   4794  C  CA  . ARG B  2 31  ? -43.003 -1.764  18.280   1.00 248.77 ? 141  ARG B CA  1 
ATOM   4795  C  C   . ARG B  2 31  ? -42.824 -1.453  19.759   1.00 242.86 ? 141  ARG B C   1 
ATOM   4796  O  O   . ARG B  2 31  ? -43.804 -1.384  20.511   1.00 250.12 ? 141  ARG B O   1 
ATOM   4797  C  CB  . ARG B  2 31  ? -42.808 -3.255  18.008   1.00 244.63 ? 141  ARG B CB  1 
ATOM   4798  C  CG  . ARG B  2 31  ? -43.901 -4.152  18.557   1.00 251.66 ? 141  ARG B CG  1 
ATOM   4799  C  CD  . ARG B  2 31  ? -43.709 -5.584  18.084   1.00 248.89 ? 141  ARG B CD  1 
ATOM   4800  N  NE  . ARG B  2 31  ? -44.811 -6.450  18.496   1.00 257.26 ? 141  ARG B NE  1 
ATOM   4801  C  CZ  . ARG B  2 31  ? -44.924 -7.728  18.151   1.00 257.89 ? 141  ARG B CZ  1 
ATOM   4802  N  NH1 . ARG B  2 31  ? -44.004 -8.292  17.382   1.00 250.50 ? 141  ARG B NH1 1 
ATOM   4803  N  NH2 . ARG B  2 31  ? -45.959 -8.442  18.569   1.00 266.49 ? 141  ARG B NH2 1 
ATOM   4804  N  N   . LEU B  2 32  ? -41.577 -1.259  20.189   1.00 230.28 ? 142  LEU B N   1 
ATOM   4805  C  CA  . LEU B  2 32  ? -41.311 -0.847  21.562   1.00 224.73 ? 142  LEU B CA  1 
ATOM   4806  C  C   . LEU B  2 32  ? -41.710 0.606   21.784   1.00 231.39 ? 142  LEU B C   1 
ATOM   4807  O  O   . LEU B  2 32  ? -42.040 0.994   22.911   1.00 232.32 ? 142  LEU B O   1 
ATOM   4808  C  CB  . LEU B  2 32  ? -39.828 -1.074  21.883   1.00 215.16 ? 142  LEU B CB  1 
ATOM   4809  C  CG  . LEU B  2 32  ? -39.160 -0.648  23.194   1.00 212.86 ? 142  LEU B CG  1 
ATOM   4810  C  CD1 . LEU B  2 32  ? -38.140 -1.693  23.649   1.00 189.71 ? 142  LEU B CD1 1 
ATOM   4811  C  CD2 . LEU B  2 32  ? -38.484 0.703   23.025   1.00 209.38 ? 142  LEU B CD2 1 
ATOM   4812  N  N   . SER B  2 33  ? -41.713 1.414   20.724   1.00 236.78 ? 143  SER B N   1 
ATOM   4813  C  CA  . SER B  2 33  ? -42.103 2.813   20.830   1.00 244.11 ? 143  SER B CA  1 
ATOM   4814  C  C   . SER B  2 33  ? -43.617 2.958   20.763   1.00 259.02 ? 143  SER B C   1 
ATOM   4815  O  O   . SER B  2 33  ? -44.133 4.011   20.371   1.00 268.52 ? 143  SER B O   1 
ATOM   4816  C  CB  . SER B  2 33  ? -41.441 3.640   19.726   1.00 244.21 ? 143  SER B CB  1 
ATOM   4817  O  OG  . SER B  2 33  ? -41.830 4.998   19.809   1.00 251.99 ? 143  SER B OG  1 
ATOM   4818  N  N   . LYS B  2 34  ? -44.336 1.905   21.145   1.00 261.75 ? 144  LYS B N   1 
ATOM   4819  C  CA  . LYS B  2 34  ? -45.791 1.916   21.143   1.00 276.38 ? 144  LYS B CA  1 
ATOM   4820  C  C   . LYS B  2 34  ? -46.319 1.306   22.435   1.00 276.38 ? 144  LYS B C   1 
ATOM   4821  O  O   . LYS B  2 34  ? -47.136 1.917   23.130   1.00 284.63 ? 144  LYS B O   1 
ATOM   4822  C  CB  . LYS B  2 34  ? -46.327 1.153   19.928   1.00 283.68 ? 144  LYS B CB  1 
ATOM   4823  C  CG  . LYS B  2 34  ? -47.809 0.787   20.001   1.00 298.20 ? 144  LYS B CG  1 
ATOM   4824  C  CD  . LYS B  2 34  ? -48.713 2.018   20.036   1.00 311.20 ? 144  LYS B CD  1 
ATOM   4825  C  CE  . LYS B  2 34  ? -50.182 1.629   20.197   1.00 326.10 ? 144  LYS B CE  1 
ATOM   4826  N  NZ  . LYS B  2 34  ? -51.079 2.817   20.292   1.00 339.36 ? 144  LYS B NZ  1 
ATOM   4827  N  N   . GLU B  2 35  ? -45.829 0.116   22.784   1.00 267.36 ? 145  GLU B N   1 
ATOM   4828  C  CA  . GLU B  2 35  ? -46.340 -0.588  23.952   1.00 267.94 ? 145  GLU B CA  1 
ATOM   4829  C  C   . GLU B  2 35  ? -45.874 0.038   25.260   1.00 261.44 ? 145  GLU B C   1 
ATOM   4830  O  O   . GLU B  2 35  ? -46.413 -0.303  26.319   1.00 263.92 ? 145  GLU B O   1 
ATOM   4831  C  CB  . GLU B  2 35  ? -45.921 -2.061  23.889   1.00 260.60 ? 145  GLU B CB  1 
ATOM   4832  C  CG  . GLU B  2 35  ? -46.245 -2.768  22.567   1.00 265.99 ? 145  GLU B CG  1 
ATOM   4833  C  CD  . GLU B  2 35  ? -47.735 -2.951  22.322   1.00 282.19 ? 145  GLU B CD  1 
ATOM   4834  O  OE1 . GLU B  2 35  ? -48.506 -2.988  23.303   1.00 287.97 ? 145  GLU B OE1 1 
ATOM   4835  O  OE2 . GLU B  2 35  ? -48.132 -3.066  21.142   1.00 289.68 ? 145  GLU B OE2 1 
ATOM   4836  N  N   . MET B  2 36  ? -44.891 0.939   25.213   1.00 253.80 ? 146  MET B N   1 
ATOM   4837  C  CA  . MET B  2 36  ? -44.388 1.563   26.431   1.00 247.77 ? 146  MET B CA  1 
ATOM   4838  C  C   . MET B  2 36  ? -45.391 2.537   27.023   1.00 259.12 ? 146  MET B C   1 
ATOM   4839  O  O   . MET B  2 36  ? -45.482 2.667   28.249   1.00 258.05 ? 146  MET B O   1 
ATOM   4840  C  CB  . MET B  2 36  ? -43.081 2.296   26.141   1.00 237.78 ? 146  MET B CB  1 
ATOM   4841  C  CG  . MET B  2 36  ? -41.859 1.406   26.088   1.00 224.12 ? 146  MET B CG  1 
ATOM   4842  S  SD  . MET B  2 36  ? -41.583 0.499   27.621   1.00 216.23 ? 146  MET B SD  1 
ATOM   4843  C  CE  . MET B  2 36  ? -41.343 1.826   28.801   1.00 215.45 ? 146  MET B CE  1 
ATOM   4844  N  N   . SER B  2 37  ? -46.152 3.222   26.174   1.00 270.56 ? 147  SER B N   1 
ATOM   4845  C  CA  . SER B  2 37  ? -47.116 4.198   26.654   1.00 282.36 ? 147  SER B CA  1 
ATOM   4846  C  C   . SER B  2 37  ? -48.326 3.549   27.306   1.00 291.99 ? 147  SER B C   1 
ATOM   4847  O  O   . SER B  2 37  ? -49.150 4.262   27.889   1.00 301.87 ? 147  SER B O   1 
ATOM   4848  C  CB  . SER B  2 37  ? -47.557 5.097   25.496   1.00 292.38 ? 147  SER B CB  1 
ATOM   4849  O  OG  . SER B  2 37  ? -48.514 6.052   25.918   1.00 304.71 ? 147  SER B OG  1 
ATOM   4850  N  N   . LYS B  2 38  ? -48.453 2.224   27.227   1.00 289.91 ? 148  LYS B N   1 
ATOM   4851  C  CA  . LYS B  2 38  ? -49.606 1.530   27.784   1.00 299.81 ? 148  LYS B CA  1 
ATOM   4852  C  C   . LYS B  2 38  ? -49.550 1.461   29.305   1.00 296.34 ? 148  LYS B C   1 
ATOM   4853  O  O   . LYS B  2 38  ? -50.375 2.072   29.992   1.00 306.06 ? 148  LYS B O   1 
ATOM   4854  C  CB  . LYS B  2 38  ? -49.711 0.117   27.201   1.00 298.82 ? 148  LYS B CB  1 
ATOM   4855  C  CG  . LYS B  2 38  ? -50.054 0.067   25.716   1.00 305.71 ? 148  LYS B CG  1 
ATOM   4856  C  CD  . LYS B  2 38  ? -51.432 0.660   25.435   1.00 323.62 ? 148  LYS B CD  1 
ATOM   4857  C  CE  . LYS B  2 38  ? -51.781 0.597   23.952   1.00 331.21 ? 148  LYS B CE  1 
ATOM   4858  N  NZ  . LYS B  2 38  ? -51.820 -0.798  23.430   1.00 329.96 ? 148  LYS B NZ  1 
ATOM   4859  N  N   . LEU B  2 39  ? -48.574 0.733   29.842   1.00 283.02 ? 149  LEU B N   1 
ATOM   4860  C  CA  . LEU B  2 39  ? -48.522 0.470   31.274   1.00 279.91 ? 149  LEU B CA  1 
ATOM   4861  C  C   . LEU B  2 39  ? -47.982 1.640   32.088   1.00 275.81 ? 149  LEU B C   1 
ATOM   4862  O  O   . LEU B  2 39  ? -47.966 1.554   33.321   1.00 274.19 ? 149  LEU B O   1 
ATOM   4863  C  CB  . LEU B  2 39  ? -47.679 -0.778  31.545   1.00 267.84 ? 149  LEU B CB  1 
ATOM   4864  C  CG  . LEU B  2 39  ? -48.444 -2.006  32.039   1.00 273.27 ? 149  LEU B CG  1 
ATOM   4865  C  CD1 . LEU B  2 39  ? -47.490 -3.167  32.243   1.00 260.79 ? 149  LEU B CD1 1 
ATOM   4866  C  CD2 . LEU B  2 39  ? -49.183 -1.683  33.328   1.00 280.80 ? 149  LEU B CD2 1 
ATOM   4867  N  N   . THR B  2 40  ? -47.549 2.724   31.448   1.00 274.67 ? 150  THR B N   1 
ATOM   4868  C  CA  . THR B  2 40  ? -47.052 3.882   32.175   1.00 271.73 ? 150  THR B CA  1 
ATOM   4869  C  C   . THR B  2 40  ? -47.219 5.125   31.317   1.00 278.16 ? 150  THR B C   1 
ATOM   4870  O  O   . THR B  2 40  ? -47.194 5.059   30.085   1.00 279.47 ? 150  THR B O   1 
ATOM   4871  C  CB  . THR B  2 40  ? -45.578 3.727   32.569   1.00 255.79 ? 150  THR B CB  1 
ATOM   4872  O  OG1 . THR B  2 40  ? -45.149 4.892   33.285   1.00 254.20 ? 150  THR B OG1 1 
ATOM   4873  C  CG2 . THR B  2 40  ? -44.709 3.553   31.331   1.00 248.12 ? 150  THR B CG2 1 
ATOM   4874  N  N   . SER B  2 41  ? -47.373 6.264   31.988   1.00 282.48 ? 151  SER B N   1 
ATOM   4875  C  CA  . SER B  2 41  ? -47.472 7.549   31.314   1.00 288.68 ? 151  SER B CA  1 
ATOM   4876  C  C   . SER B  2 41  ? -46.167 8.323   31.338   1.00 278.01 ? 151  SER B C   1 
ATOM   4877  O  O   . SER B  2 41  ? -45.922 9.137   30.441   1.00 279.89 ? 151  SER B O   1 
ATOM   4878  C  CB  . SER B  2 41  ? -48.574 8.399   31.956   1.00 302.45 ? 151  SER B CB  1 
ATOM   4879  O  OG  . SER B  2 41  ? -48.400 8.463   33.360   1.00 299.16 ? 151  SER B OG  1 
ATOM   4880  N  N   . ASN B  2 42  ? -45.332 8.093   32.347   1.00 267.56 ? 152  ASN B N   1 
ATOM   4881  C  CA  . ASN B  2 42  ? -44.032 8.749   32.448   1.00 257.28 ? 152  ASN B CA  1 
ATOM   4882  C  C   . ASN B  2 42  ? -42.990 7.864   31.765   1.00 254.64 ? 152  ASN B C   1 
ATOM   4883  O  O   . ASN B  2 42  ? -42.262 7.093   32.397   1.00 247.69 ? 152  ASN B O   1 
ATOM   4884  C  CB  . ASN B  2 42  ? -43.687 9.025   33.904   1.00 253.53 ? 152  ASN B CB  1 
ATOM   4885  C  CG  . ASN B  2 42  ? -42.712 10.165  34.054   1.00 248.80 ? 152  ASN B CG  1 
ATOM   4886  O  OD1 . ASN B  2 42  ? -42.375 10.838  33.081   1.00 249.47 ? 152  ASN B OD1 1 
ATOM   4887  N  ND2 . ASN B  2 42  ? -42.254 10.396  35.275   1.00 245.09 ? 152  ASN B ND2 1 
ATOM   4888  N  N   . PHE B  2 43  ? -42.922 7.982   30.440   1.00 272.88 ? 153  PHE B N   1 
ATOM   4889  C  CA  . PHE B  2 43  ? -42.074 7.133   29.610   1.00 257.66 ? 153  PHE B CA  1 
ATOM   4890  C  C   . PHE B  2 43  ? -41.103 7.973   28.789   1.00 251.92 ? 153  PHE B C   1 
ATOM   4891  O  O   . PHE B  2 43  ? -41.524 8.829   28.003   1.00 271.83 ? 153  PHE B O   1 
ATOM   4892  C  CB  . PHE B  2 43  ? -42.920 6.252   28.691   1.00 248.00 ? 153  PHE B CB  1 
ATOM   4893  C  CG  . PHE B  2 43  ? -42.212 5.840   27.433   1.00 258.98 ? 153  PHE B CG  1 
ATOM   4894  C  CD1 . PHE B  2 43  ? -41.144 4.955   27.481   1.00 262.36 ? 153  PHE B CD1 1 
ATOM   4895  C  CD2 . PHE B  2 43  ? -42.616 6.332   26.201   1.00 251.01 ? 153  PHE B CD2 1 
ATOM   4896  C  CE1 . PHE B  2 43  ? -40.485 4.573   26.327   1.00 263.06 ? 153  PHE B CE1 1 
ATOM   4897  C  CE2 . PHE B  2 43  ? -41.963 5.950   25.040   1.00 270.87 ? 153  PHE B CE2 1 
ATOM   4898  C  CZ  . PHE B  2 43  ? -40.898 5.067   25.105   1.00 273.51 ? 153  PHE B CZ  1 
ATOM   4899  N  N   . ARG B  2 44  ? -39.807 7.721   28.972   1.00 220.80 ? 154  ARG B N   1 
ATOM   4900  C  CA  . ARG B  2 44  ? -38.750 8.337   28.181   1.00 215.88 ? 154  ARG B CA  1 
ATOM   4901  C  C   . ARG B  2 44  ? -37.778 7.259   27.731   1.00 204.86 ? 154  ARG B C   1 
ATOM   4902  O  O   . ARG B  2 44  ? -37.385 6.407   28.534   1.00 197.17 ? 154  ARG B O   1 
ATOM   4903  C  CB  . ARG B  2 44  ? -38.016 9.413   28.980   1.00 212.85 ? 154  ARG B CB  1 
ATOM   4904  C  CG  . ARG B  2 44  ? -38.899 10.570  29.378   1.00 224.01 ? 154  ARG B CG  1 
ATOM   4905  C  CD  . ARG B  2 44  ? -38.097 11.681  30.010   1.00 221.41 ? 154  ARG B CD  1 
ATOM   4906  N  NE  . ARG B  2 44  ? -38.967 12.721  30.546   1.00 232.13 ? 154  ARG B NE  1 
ATOM   4907  C  CZ  . ARG B  2 44  ? -38.542 13.736  31.288   1.00 232.36 ? 154  ARG B CZ  1 
ATOM   4908  N  NH1 . ARG B  2 44  ? -37.253 13.848  31.584   1.00 231.21 ? 154  ARG B NH1 1 
ATOM   4909  N  NH2 . ARG B  2 44  ? -39.405 14.637  31.736   1.00 242.95 ? 154  ARG B NH2 1 
ATOM   4910  N  N   . LEU B  2 45  ? -37.414 7.275   26.447   1.00 204.71 ? 155  LEU B N   1 
ATOM   4911  C  CA  . LEU B  2 45  ? -36.510 6.279   25.883   1.00 196.69 ? 155  LEU B CA  1 
ATOM   4912  C  C   . LEU B  2 45  ? -35.391 6.946   25.082   1.00 191.35 ? 155  LEU B C   1 
ATOM   4913  O  O   . LEU B  2 45  ? -35.575 8.022   24.507   1.00 208.30 ? 155  LEU B O   1 
ATOM   4914  C  CB  . LEU B  2 45  ? -37.278 5.279   25.003   1.00 199.67 ? 155  LEU B CB  1 
ATOM   4915  C  CG  . LEU B  2 45  ? -37.567 5.625   23.541   1.00 206.82 ? 155  LEU B CG  1 
ATOM   4916  C  CD1 . LEU B  2 45  ? -38.202 4.427   22.860   1.00 209.58 ? 155  LEU B CD1 1 
ATOM   4917  C  CD2 . LEU B  2 45  ? -38.448 6.864   23.392   1.00 218.82 ? 155  LEU B CD2 1 
ATOM   4918  N  N   . GLY B  2 46  ? -34.224 6.290   25.047   1.00 180.66 ? 156  GLY B N   1 
ATOM   4919  C  CA  . GLY B  2 46  ? -33.066 6.800   24.322   1.00 176.49 ? 156  GLY B CA  1 
ATOM   4920  C  C   . GLY B  2 46  ? -32.450 5.823   23.336   1.00 171.25 ? 156  GLY B C   1 
ATOM   4921  O  O   . GLY B  2 46  ? -33.030 4.766   23.075   1.00 171.91 ? 156  GLY B O   1 
ATOM   4922  N  N   . PHE B  2 47  ? -31.276 6.145   22.783   1.00 166.51 ? 157  PHE B N   1 
ATOM   4923  C  CA  . PHE B  2 47  ? -30.662 5.275   21.783   1.00 162.26 ? 157  PHE B CA  1 
ATOM   4924  C  C   . PHE B  2 47  ? -29.158 5.522   21.689   1.00 156.00 ? 157  PHE B C   1 
ATOM   4925  O  O   . PHE B  2 47  ? -28.682 6.650   21.848   1.00 155.99 ? 157  PHE B O   1 
ATOM   4926  C  CB  . PHE B  2 47  ? -31.302 5.457   20.401   1.00 171.06 ? 157  PHE B CB  1 
ATOM   4927  C  CG  . PHE B  2 47  ? -30.639 4.649   19.321   1.00 167.45 ? 157  PHE B CG  1 
ATOM   4928  C  CD1 . PHE B  2 47  ? -30.879 3.292   19.210   1.00 164.45 ? 157  PHE B CD1 1 
ATOM   4929  C  CD2 . PHE B  2 47  ? -29.776 5.246   18.418   1.00 167.63 ? 157  PHE B CD2 1 
ATOM   4930  C  CE1 . PHE B  2 47  ? -30.270 2.543   18.220   1.00 161.52 ? 157  PHE B CE1 1 
ATOM   4931  C  CE2 . PHE B  2 47  ? -29.166 4.504   17.424   1.00 164.83 ? 157  PHE B CE2 1 
ATOM   4932  C  CZ  . PHE B  2 47  ? -29.412 3.151   17.325   1.00 161.69 ? 157  PHE B CZ  1 
ATOM   4933  N  N   . GLY B  2 48  ? -28.431 4.437   21.427   1.00 172.64 ? 158  GLY B N   1 
ATOM   4934  C  CA  . GLY B  2 48  ? -26.990 4.481   21.242   1.00 140.41 ? 158  GLY B CA  1 
ATOM   4935  C  C   . GLY B  2 48  ? -26.537 3.317   20.388   1.00 136.46 ? 158  GLY B C   1 
ATOM   4936  O  O   . GLY B  2 48  ? -27.161 2.251   20.377   1.00 136.01 ? 158  GLY B O   1 
ATOM   4937  N  N   . SER B  2 49  ? -25.447 3.526   19.658   1.00 134.19 ? 159  SER B N   1 
ATOM   4938  C  CA  . SER B  2 49  ? -24.923 2.531   18.734   1.00 131.21 ? 159  SER B CA  1 
ATOM   4939  C  C   . SER B  2 49  ? -23.434 2.306   18.971   1.00 123.08 ? 159  SER B C   1 
ATOM   4940  O  O   . SER B  2 49  ? -22.728 3.184   19.472   1.00 121.69 ? 159  SER B O   1 
ATOM   4941  C  CB  . SER B  2 49  ? -25.179 2.956   17.293   1.00 138.90 ? 159  SER B CB  1 
ATOM   4942  O  OG  . SER B  2 49  ? -24.670 4.256   17.066   1.00 153.86 ? 159  SER B OG  1 
ATOM   4943  N  N   . PHE B  2 50  ? -22.968 1.108   18.620   1.00 118.22 ? 160  PHE B N   1 
ATOM   4944  C  CA  . PHE B  2 50  ? -21.567 0.739   18.786   1.00 110.94 ? 160  PHE B CA  1 
ATOM   4945  C  C   . PHE B  2 50  ? -21.160 -0.193  17.656   1.00 110.20 ? 160  PHE B C   1 
ATOM   4946  O  O   . PHE B  2 50  ? -22.006 -0.726  16.933   1.00 114.28 ? 160  PHE B O   1 
ATOM   4947  C  CB  . PHE B  2 50  ? -21.304 0.080   20.151   1.00 114.18 ? 160  PHE B CB  1 
ATOM   4948  C  CG  . PHE B  2 50  ? -21.986 -1.258  20.335   1.00 143.77 ? 160  PHE B CG  1 
ATOM   4949  C  CD1 . PHE B  2 50  ? -23.297 -1.325  20.780   1.00 123.24 ? 160  PHE B CD1 1 
ATOM   4950  C  CD2 . PHE B  2 50  ? -21.311 -2.447  20.091   1.00 127.88 ? 160  PHE B CD2 1 
ATOM   4951  C  CE1 . PHE B  2 50  ? -23.932 -2.549  20.961   1.00 104.45 ? 160  PHE B CE1 1 
ATOM   4952  C  CE2 . PHE B  2 50  ? -21.945 -3.675  20.269   1.00 95.20  ? 160  PHE B CE2 1 
ATOM   4953  C  CZ  . PHE B  2 50  ? -23.253 -3.722  20.708   1.00 99.25  ? 160  PHE B CZ  1 
ATOM   4954  N  N   . VAL B  2 51  ? -19.845 -0.324  17.462   1.00 105.84 ? 161  VAL B N   1 
ATOM   4955  C  CA  . VAL B  2 51  ? -19.292 -1.298  16.522   1.00 104.31 ? 161  VAL B CA  1 
ATOM   4956  C  C   . VAL B  2 51  ? -18.096 -2.023  17.140   1.00 96.32  ? 161  VAL B C   1 
ATOM   4957  O  O   . VAL B  2 51  ? -18.216 -3.175  17.570   1.00 91.96  ? 161  VAL B O   1 
ATOM   4958  C  CB  . VAL B  2 51  ? -18.897 -0.638  15.188   1.00 110.06 ? 161  VAL B CB  1 
ATOM   4959  C  CG1 . VAL B  2 51  ? -18.408 -1.687  14.216   1.00 111.94 ? 161  VAL B CG1 1 
ATOM   4960  C  CG2 . VAL B  2 51  ? -20.068 0.091   14.587   1.00 118.58 ? 161  VAL B CG2 1 
ATOM   4961  N  N   . GLU B  2 52  ? -16.953 -1.338  17.226   1.00 103.67 ? 162  GLU B N   1 
ATOM   4962  C  CA  . GLU B  2 52  ? -15.664 -1.917  17.606   1.00 88.77  ? 162  GLU B CA  1 
ATOM   4963  C  C   . GLU B  2 52  ? -14.662 -0.783  17.804   1.00 107.72 ? 162  GLU B C   1 
ATOM   4964  O  O   . GLU B  2 52  ? -14.832 0.310   17.254   1.00 150.07 ? 162  GLU B O   1 
ATOM   4965  C  CB  . GLU B  2 52  ? -15.166 -2.890  16.522   1.00 91.73  ? 162  GLU B CB  1 
ATOM   4966  C  CG  . GLU B  2 52  ? -13.915 -3.707  16.847   1.00 122.17 ? 162  GLU B CG  1 
ATOM   4967  C  CD  . GLU B  2 52  ? -14.133 -4.780  17.897   1.00 117.00 ? 162  GLU B CD  1 
ATOM   4968  O  OE1 . GLU B  2 52  ? -13.305 -4.876  18.821   1.00 76.96  ? 162  GLU B OE1 1 
ATOM   4969  O  OE2 . GLU B  2 52  ? -15.118 -5.538  17.790   1.00 111.38 ? 162  GLU B OE2 1 
ATOM   4970  N  N   . LYS B  2 53  ? -13.587 -1.066  18.550   1.00 118.60 ? 163  LYS B N   1 
ATOM   4971  C  CA  . LYS B  2 53  ? -12.531 -0.064  18.756   1.00 124.51 ? 163  LYS B CA  1 
ATOM   4972  C  C   . LYS B  2 53  ? -11.783 0.167   17.453   1.00 93.33  ? 163  LYS B C   1 
ATOM   4973  O  O   . LYS B  2 53  ? -11.283 -0.795  16.854   1.00 137.06 ? 163  LYS B O   1 
ATOM   4974  C  CB  . LYS B  2 53  ? -11.551 -0.478  19.843   1.00 106.43 ? 163  LYS B CB  1 
ATOM   4975  C  CG  . LYS B  2 53  ? -12.119 -0.475  21.246   1.00 102.59 ? 163  LYS B CG  1 
ATOM   4976  C  CD  . LYS B  2 53  ? -11.007 -0.727  22.264   1.00 130.53 ? 163  LYS B CD  1 
ATOM   4977  C  CE  . LYS B  2 53  ? -11.490 -0.686  23.720   1.00 68.64  ? 163  LYS B CE  1 
ATOM   4978  N  NZ  . LYS B  2 53  ? -12.030 0.622   24.168   1.00 72.52  ? 163  LYS B NZ  1 
ATOM   4979  N  N   . PRO B  2 54  ? -11.695 1.400   16.972   1.00 122.93 ? 164  PRO B N   1 
ATOM   4980  C  CA  . PRO B  2 54  ? -11.111 1.637   15.645   1.00 140.29 ? 164  PRO B CA  1 
ATOM   4981  C  C   . PRO B  2 54  ? -9.592  1.511   15.576   1.00 159.71 ? 164  PRO B C   1 
ATOM   4982  O  O   . PRO B  2 54  ? -8.923  2.443   15.119   1.00 105.97 ? 164  PRO B O   1 
ATOM   4983  C  CB  . PRO B  2 54  ? -11.563 3.069   15.332   1.00 163.00 ? 164  PRO B CB  1 
ATOM   4984  C  CG  . PRO B  2 54  ? -11.693 3.716   16.675   1.00 168.29 ? 164  PRO B CG  1 
ATOM   4985  C  CD  . PRO B  2 54  ? -12.166 2.641   17.613   1.00 98.85  ? 164  PRO B CD  1 
ATOM   4986  N  N   . VAL B  2 55  ? -9.024  0.389   16.022   1.00 190.84 ? 165  VAL B N   1 
ATOM   4987  C  CA  . VAL B  2 55  ? -7.581  0.184   15.979   1.00 127.97 ? 165  VAL B CA  1 
ATOM   4988  C  C   . VAL B  2 55  ? -7.289  -1.255  15.572   1.00 119.78 ? 165  VAL B C   1 
ATOM   4989  O  O   . VAL B  2 55  ? -8.065  -2.173  15.857   1.00 110.14 ? 165  VAL B O   1 
ATOM   4990  C  CB  . VAL B  2 55  ? -6.930  0.539   17.332   1.00 107.58 ? 165  VAL B CB  1 
ATOM   4991  C  CG1 . VAL B  2 55  ? -7.520  -0.316  18.438   1.00 87.86  ? 165  VAL B CG1 1 
ATOM   4992  C  CG2 . VAL B  2 55  ? -5.414  0.412   17.264   1.00 98.74  ? 165  VAL B CG2 1 
ATOM   4993  N  N   . SER B  2 56  ? -6.173  -1.437  14.874   1.00 124.58 ? 166  SER B N   1 
ATOM   4994  C  CA  . SER B  2 56  ? -5.666  -2.764  14.541   1.00 159.83 ? 166  SER B CA  1 
ATOM   4995  C  C   . SER B  2 56  ? -5.414  -3.539  15.852   1.00 127.22 ? 166  SER B C   1 
ATOM   4996  O  O   . SER B  2 56  ? -5.053  -2.948  16.868   1.00 90.70  ? 166  SER B O   1 
ATOM   4997  C  CB  . SER B  2 56  ? -4.389  -2.637  13.691   1.00 106.86 ? 166  SER B CB  1 
ATOM   4998  O  OG  . SER B  2 56  ? -4.136  -3.787  12.892   1.00 109.92 ? 166  SER B OG  1 
ATOM   4999  N  N   . PRO B  2 57  ? -5.619  -4.865  15.842   1.00 112.12 ? 167  PRO B N   1 
ATOM   5000  C  CA  . PRO B  2 57  ? -5.979  -5.731  14.713   1.00 165.05 ? 167  PRO B CA  1 
ATOM   5001  C  C   . PRO B  2 57  ? -7.482  -5.904  14.482   1.00 123.81 ? 167  PRO B C   1 
ATOM   5002  O  O   . PRO B  2 57  ? -7.890  -6.690  13.628   1.00 136.63 ? 167  PRO B O   1 
ATOM   5003  C  CB  . PRO B  2 57  ? -5.345  -7.062  15.104   1.00 142.39 ? 167  PRO B CB  1 
ATOM   5004  C  CG  . PRO B  2 57  ? -5.467  -7.081  16.592   1.00 108.02 ? 167  PRO B CG  1 
ATOM   5005  C  CD  . PRO B  2 57  ? -5.333  -5.651  17.056   1.00 90.33  ? 167  PRO B CD  1 
ATOM   5006  N  N   . PHE B  2 58  ? -8.302  -5.192  15.249   1.00 98.22  ? 168  PHE B N   1 
ATOM   5007  C  CA  . PHE B  2 58  ? -9.741  -5.378  15.127   1.00 98.44  ? 168  PHE B CA  1 
ATOM   5008  C  C   . PHE B  2 58  ? -10.277 -4.855  13.806   1.00 122.35 ? 168  PHE B C   1 
ATOM   5009  O  O   . PHE B  2 58  ? -11.293 -5.362  13.317   1.00 116.75 ? 168  PHE B O   1 
ATOM   5010  C  CB  . PHE B  2 58  ? -10.433 -4.705  16.298   1.00 120.58 ? 168  PHE B CB  1 
ATOM   5011  C  CG  . PHE B  2 58  ? -9.925  -5.180  17.613   1.00 172.05 ? 168  PHE B CG  1 
ATOM   5012  C  CD1 . PHE B  2 58  ? -9.623  -6.521  17.799   1.00 163.57 ? 168  PHE B CD1 1 
ATOM   5013  C  CD2 . PHE B  2 58  ? -9.694  -4.294  18.646   1.00 169.97 ? 168  PHE B CD2 1 
ATOM   5014  C  CE1 . PHE B  2 58  ? -9.129  -6.970  19.000   1.00 116.64 ? 168  PHE B CE1 1 
ATOM   5015  C  CE2 . PHE B  2 58  ? -9.200  -4.739  19.848   1.00 77.31  ? 168  PHE B CE2 1 
ATOM   5016  C  CZ  . PHE B  2 58  ? -8.918  -6.080  20.023   1.00 76.25  ? 168  PHE B CZ  1 
ATOM   5017  N  N   . VAL B  2 59  ? -9.623  -3.843  13.226   1.00 134.18 ? 169  VAL B N   1 
ATOM   5018  C  CA  . VAL B  2 59  ? -9.973  -3.290  11.922   1.00 149.48 ? 169  VAL B CA  1 
ATOM   5019  C  C   . VAL B  2 59  ? -8.714  -3.229  11.067   1.00 161.83 ? 169  VAL B C   1 
ATOM   5020  O  O   . VAL B  2 59  ? -7.617  -2.985  11.583   1.00 116.24 ? 169  VAL B O   1 
ATOM   5021  C  CB  . VAL B  2 59  ? -10.605 -1.886  12.036   1.00 155.58 ? 169  VAL B CB  1 
ATOM   5022  C  CG1 . VAL B  2 59  ? -11.250 -1.483  10.708   1.00 171.94 ? 169  VAL B CG1 1 
ATOM   5023  C  CG2 . VAL B  2 59  ? -11.613 -1.826  13.180   1.00 109.13 ? 169  VAL B CG2 1 
ATOM   5024  N  N   . LYS B  2 60  ? -8.868  -3.481  9.768    1.00 176.77 ? 170  LYS B N   1 
ATOM   5025  C  CA  . LYS B  2 60  ? -7.744  -3.339  8.852    1.00 163.42 ? 170  LYS B CA  1 
ATOM   5026  C  C   . LYS B  2 60  ? -7.330  -1.876  8.734    1.00 163.15 ? 170  LYS B C   1 
ATOM   5027  O  O   . LYS B  2 60  ? -8.173  -0.973  8.722    1.00 140.18 ? 170  LYS B O   1 
ATOM   5028  C  CB  . LYS B  2 60  ? -8.086  -3.909  7.477    1.00 144.09 ? 170  LYS B CB  1 
ATOM   5029  C  CG  . LYS B  2 60  ? -7.869  -5.406  7.383    1.00 143.27 ? 170  LYS B CG  1 
ATOM   5030  C  CD  . LYS B  2 60  ? -7.948  -5.896  5.956    1.00 152.19 ? 170  LYS B CD  1 
ATOM   5031  C  CE  . LYS B  2 60  ? -7.593  -7.369  5.859    1.00 151.88 ? 170  LYS B CE  1 
ATOM   5032  N  NZ  . LYS B  2 60  ? -8.470  -8.221  6.707    1.00 146.11 ? 170  LYS B NZ  1 
ATOM   5033  N  N   . THR B  2 61  ? -6.014  -1.654  8.636    1.00 188.35 ? 171  THR B N   1 
ATOM   5034  C  CA  . THR B  2 61  ? -5.410  -0.327  8.631    1.00 195.02 ? 171  THR B CA  1 
ATOM   5035  C  C   . THR B  2 61  ? -5.000  0.128   7.230    1.00 163.73 ? 171  THR B C   1 
ATOM   5036  O  O   . THR B  2 61  ? -4.061  0.919   7.081    1.00 159.36 ? 171  THR B O   1 
ATOM   5037  C  CB  . THR B  2 61  ? -4.203  -0.289  9.575    1.00 184.10 ? 171  THR B CB  1 
ATOM   5038  O  OG1 . THR B  2 61  ? -3.420  -1.482  9.419    1.00 165.74 ? 171  THR B OG1 1 
ATOM   5039  C  CG2 . THR B  2 61  ? -4.647  -0.165  11.024   1.00 157.13 ? 171  THR B CG2 1 
ATOM   5040  N  N   . THR B  2 62  ? -5.680  -0.345  6.210    1.00 153.40 ? 172  THR B N   1 
ATOM   5041  C  CA  . THR B  2 62  ? -5.426  0.151   4.864    1.00 173.41 ? 172  THR B CA  1 
ATOM   5042  C  C   . THR B  2 62  ? -6.285  1.386   4.592    1.00 198.45 ? 172  THR B C   1 
ATOM   5043  O  O   . THR B  2 62  ? -7.444  1.434   5.013    1.00 208.81 ? 172  THR B O   1 
ATOM   5044  C  CB  . THR B  2 62  ? -5.726  -0.927  3.828    1.00 189.26 ? 172  THR B CB  1 
ATOM   5045  O  OG1 . THR B  2 62  ? -7.087  -1.360  3.961    1.00 173.54 ? 172  THR B OG1 1 
ATOM   5046  C  CG2 . THR B  2 62  ? -4.800  -2.124  4.029    1.00 178.69 ? 172  THR B CG2 1 
ATOM   5047  N  N   . PRO B  2 63  ? -5.731  2.397   3.914    1.00 175.49 ? 173  PRO B N   1 
ATOM   5048  C  CA  . PRO B  2 63  ? -6.454  3.674   3.753    1.00 179.91 ? 173  PRO B CA  1 
ATOM   5049  C  C   . PRO B  2 63  ? -7.866  3.546   3.200    1.00 183.52 ? 173  PRO B C   1 
ATOM   5050  O  O   . PRO B  2 63  ? -8.716  4.391   3.510    1.00 183.89 ? 173  PRO B O   1 
ATOM   5051  C  CB  . PRO B  2 63  ? -5.548  4.467   2.799    1.00 216.11 ? 173  PRO B CB  1 
ATOM   5052  C  CG  . PRO B  2 63  ? -4.643  3.448   2.172    1.00 211.67 ? 173  PRO B CG  1 
ATOM   5053  C  CD  . PRO B  2 63  ? -4.439  2.402   3.212    1.00 181.28 ? 173  PRO B CD  1 
ATOM   5054  N  N   . GLU B  2 64  ? -8.151  2.523   2.392    1.00 186.82 ? 174  GLU B N   1 
ATOM   5055  C  CA  . GLU B  2 64  ? -9.494  2.370   1.841    1.00 191.20 ? 174  GLU B CA  1 
ATOM   5056  C  C   . GLU B  2 64  ? -10.443 1.718   2.841    1.00 182.62 ? 174  GLU B C   1 
ATOM   5057  O  O   . GLU B  2 64  ? -11.616 2.099   2.928    1.00 184.01 ? 174  GLU B O   1 
ATOM   5058  C  CB  . GLU B  2 64  ? -9.443  1.561   0.544    1.00 199.22 ? 174  GLU B CB  1 
ATOM   5059  C  CG  . GLU B  2 64  ? -10.809 1.265   -0.062   1.00 211.08 ? 174  GLU B CG  1 
ATOM   5060  C  CD  . GLU B  2 64  ? -10.722 0.445   -1.334   1.00 215.99 ? 174  GLU B CD  1 
ATOM   5061  O  OE1 . GLU B  2 64  ? -9.603  0.274   -1.860   1.00 215.68 ? 174  GLU B OE1 1 
ATOM   5062  O  OE2 . GLU B  2 64  ? -11.775 -0.039  -1.801   1.00 216.67 ? 174  GLU B OE2 1 
ATOM   5063  N  N   . GLU B  2 65  ? -9.955  0.739   3.603    1.00 217.89 ? 175  GLU B N   1 
ATOM   5064  C  CA  . GLU B  2 65  ? -10.773 -0.009  4.552    1.00 185.55 ? 175  GLU B CA  1 
ATOM   5065  C  C   . GLU B  2 65  ? -10.928 0.708   5.888    1.00 161.11 ? 175  GLU B C   1 
ATOM   5066  O  O   . GLU B  2 65  ? -11.531 0.155   6.818    1.00 153.41 ? 175  GLU B O   1 
ATOM   5067  C  CB  . GLU B  2 65  ? -10.174 -1.403  4.764    1.00 163.82 ? 175  GLU B CB  1 
ATOM   5068  C  CG  . GLU B  2 65  ? -11.162 -2.454  5.263    1.00 211.88 ? 175  GLU B CG  1 
ATOM   5069  C  CD  . GLU B  2 65  ? -10.641 -3.862  5.085    1.00 211.86 ? 175  GLU B CD  1 
ATOM   5070  O  OE1 . GLU B  2 65  ? -9.923  -4.095  4.088    1.00 200.06 ? 175  GLU B OE1 1 
ATOM   5071  O  OE2 . GLU B  2 65  ? -10.939 -4.725  5.942    1.00 203.85 ? 175  GLU B OE2 1 
ATOM   5072  N  N   . ILE B  2 66  ? -10.384 1.911   6.013    1.00 160.00 ? 176  ILE B N   1 
ATOM   5073  C  CA  . ILE B  2 66  ? -10.641 2.745   7.177    1.00 154.19 ? 176  ILE B CA  1 
ATOM   5074  C  C   . ILE B  2 66  ? -11.917 3.550   6.987    1.00 162.46 ? 176  ILE B C   1 
ATOM   5075  O  O   . ILE B  2 66  ? -12.802 3.547   7.845    1.00 186.12 ? 176  ILE B O   1 
ATOM   5076  C  CB  . ILE B  2 66  ? -9.428  3.663   7.448    1.00 154.20 ? 176  ILE B CB  1 
ATOM   5077  C  CG1 . ILE B  2 66  ? -8.170  2.836   7.726    1.00 149.91 ? 176  ILE B CG1 1 
ATOM   5078  C  CG2 . ILE B  2 66  ? -9.726  4.601   8.607    1.00 149.33 ? 176  ILE B CG2 1 
ATOM   5079  C  CD1 . ILE B  2 66  ? -6.912  3.661   7.903    1.00 151.72 ? 176  ILE B CD1 1 
ATOM   5080  N  N   . ALA B  2 67  ? -12.034 4.227   5.841    1.00 168.78 ? 177  ALA B N   1 
ATOM   5081  C  CA  . ALA B  2 67  ? -13.233 4.981   5.505    1.00 174.94 ? 177  ALA B CA  1 
ATOM   5082  C  C   . ALA B  2 67  ? -14.356 4.092   4.998    1.00 177.70 ? 177  ALA B C   1 
ATOM   5083  O  O   . ALA B  2 67  ? -15.517 4.515   5.003    1.00 181.02 ? 177  ALA B O   1 
ATOM   5084  C  CB  . ALA B  2 67  ? -12.903 6.044   4.459    1.00 185.58 ? 177  ALA B CB  1 
ATOM   5085  N  N   . ASN B  2 68  ? -14.036 2.879   4.552    1.00 177.10 ? 178  ASN B N   1 
ATOM   5086  C  CA  . ASN B  2 68  ? -15.034 1.926   4.073    1.00 179.94 ? 178  ASN B CA  1 
ATOM   5087  C  C   . ASN B  2 68  ? -14.622 0.528   4.504    1.00 172.78 ? 178  ASN B C   1 
ATOM   5088  O  O   . ASN B  2 68  ? -13.989 -0.213  3.739    1.00 175.85 ? 178  ASN B O   1 
ATOM   5089  C  CB  . ASN B  2 68  ? -15.193 1.991   2.556    1.00 191.95 ? 178  ASN B CB  1 
ATOM   5090  C  CG  . ASN B  2 68  ? -16.247 1.030   2.048    1.00 195.71 ? 178  ASN B CG  1 
ATOM   5091  O  OD1 . ASN B  2 68  ? -17.265 0.806   2.701    1.00 192.42 ? 178  ASN B OD1 1 
ATOM   5092  N  ND2 . ASN B  2 68  ? -15.992 0.432   0.891    1.00 202.92 ? 178  ASN B ND2 1 
ATOM   5093  N  N   . PRO B  2 69  ? -14.980 0.123   5.729    1.00 163.65 ? 179  PRO B N   1 
ATOM   5094  C  CA  . PRO B  2 69  ? -14.592 -1.214  6.209    1.00 168.40 ? 179  PRO B CA  1 
ATOM   5095  C  C   . PRO B  2 69  ? -15.322 -2.353  5.517    1.00 174.81 ? 179  PRO B C   1 
ATOM   5096  O  O   . PRO B  2 69  ? -14.978 -3.520  5.765    1.00 157.26 ? 179  PRO B O   1 
ATOM   5097  C  CB  . PRO B  2 69  ? -14.921 -1.160  7.709    1.00 156.65 ? 179  PRO B CB  1 
ATOM   5098  C  CG  . PRO B  2 69  ? -15.966 -0.122  7.832    1.00 150.23 ? 179  PRO B CG  1 
ATOM   5099  C  CD  . PRO B  2 69  ? -15.659 0.908   6.774    1.00 159.13 ? 179  PRO B CD  1 
ATOM   5100  N  N   . CYS B  2 70  ? -16.322 -2.063  4.677    1.00 169.76 ? 180  CYS B N   1 
ATOM   5101  C  CA  . CYS B  2 70  ? -16.982 -3.079  3.871    1.00 175.47 ? 180  CYS B CA  1 
ATOM   5102  C  C   . CYS B  2 70  ? -16.353 -3.206  2.503    1.00 184.22 ? 180  CYS B C   1 
ATOM   5103  O  O   . CYS B  2 70  ? -17.008 -3.683  1.568    1.00 192.11 ? 180  CYS B O   1 
ATOM   5104  C  CB  . CYS B  2 70  ? -18.472 -2.778  3.720    1.00 180.59 ? 180  CYS B CB  1 
ATOM   5105  S  SG  . CYS B  2 70  ? -19.361 -2.757  5.255    1.00 222.32 ? 180  CYS B SG  1 
ATOM   5106  N  N   . SER B  2 71  ? -15.096 -2.798  2.363    1.00 183.46 ? 181  SER B N   1 
ATOM   5107  C  CA  . SER B  2 71  ? -14.406 -2.945  1.102    1.00 191.72 ? 181  SER B CA  1 
ATOM   5108  C  C   . SER B  2 71  ? -14.142 -4.426  0.853    1.00 191.07 ? 181  SER B C   1 
ATOM   5109  O  O   . SER B  2 71  ? -14.404 -5.281  1.705    1.00 183.89 ? 181  SER B O   1 
ATOM   5110  C  CB  . SER B  2 71  ? -13.110 -2.131  1.111    1.00 190.95 ? 181  SER B CB  1 
ATOM   5111  O  OG  . SER B  2 71  ? -12.428 -2.253  -0.119   1.00 199.49 ? 181  SER B OG  1 
ATOM   5112  N  N   . SER B  2 72  ? -13.652 -4.733  -0.350   1.00 224.03 ? 182  SER B N   1 
ATOM   5113  C  CA  . SER B  2 72  ? -13.312 -6.075  -0.840   1.00 233.76 ? 182  SER B CA  1 
ATOM   5114  C  C   . SER B  2 72  ? -14.526 -6.991  -0.985   1.00 228.67 ? 182  SER B C   1 
ATOM   5115  O  O   . SER B  2 72  ? -14.364 -8.150  -1.401   1.00 224.40 ? 182  SER B O   1 
ATOM   5116  C  CB  . SER B  2 72  ? -12.270 -6.780  0.039    1.00 210.65 ? 182  SER B CB  1 
ATOM   5117  O  OG  . SER B  2 72  ? -12.090 -8.126  -0.378   1.00 211.94 ? 182  SER B OG  1 
ATOM   5118  N  N   . ILE B  2 73  ? -15.732 -6.518  -0.690   1.00 213.50 ? 183  ILE B N   1 
ATOM   5119  C  CA  . ILE B  2 73  ? -16.935 -7.332  -0.828   1.00 206.47 ? 183  ILE B CA  1 
ATOM   5120  C  C   . ILE B  2 73  ? -17.531 -7.190  -2.231   1.00 219.40 ? 183  ILE B C   1 
ATOM   5121  O  O   . ILE B  2 73  ? -17.757 -8.195  -2.906   1.00 224.59 ? 183  ILE B O   1 
ATOM   5122  C  CB  . ILE B  2 73  ? -17.978 -6.979  0.263    1.00 203.80 ? 183  ILE B CB  1 
ATOM   5123  C  CG1 . ILE B  2 73  ? -17.357 -7.093  1.657    1.00 209.71 ? 183  ILE B CG1 1 
ATOM   5124  C  CG2 . ILE B  2 73  ? -19.217 -7.868  0.133    1.00 204.54 ? 183  ILE B CG2 1 
ATOM   5125  C  CD1 . ILE B  2 73  ? -18.273 -6.648  2.779    1.00 211.17 ? 183  ILE B CD1 1 
ATOM   5126  N  N   . PRO B  2 74  ? -17.788 -5.947  -2.689   1.00 225.25 ? 184  PRO B N   1 
ATOM   5127  C  CA  . PRO B  2 74  ? -17.698 -4.605  -2.095   1.00 221.88 ? 184  PRO B CA  1 
ATOM   5128  C  C   . PRO B  2 74  ? -19.034 -4.097  -1.543   1.00 221.55 ? 184  PRO B C   1 
ATOM   5129  O  O   . PRO B  2 74  ? -20.083 -4.588  -1.958   1.00 227.25 ? 184  PRO B O   1 
ATOM   5130  C  CB  . PRO B  2 74  ? -17.237 -3.750  -3.268   1.00 231.98 ? 184  PRO B CB  1 
ATOM   5131  C  CG  . PRO B  2 74  ? -17.910 -4.383  -4.442   1.00 242.77 ? 184  PRO B CG  1 
ATOM   5132  C  CD  . PRO B  2 74  ? -18.033 -5.865  -4.141   1.00 238.32 ? 184  PRO B CD  1 
ATOM   5133  N  N   . TYR B  2 75  ? -18.990 -3.135  -0.621   1.00 215.39 ? 185  TYR B N   1 
ATOM   5134  C  CA  . TYR B  2 75  ? -20.199 -2.515  -0.088   1.00 215.62 ? 185  TYR B CA  1 
ATOM   5135  C  C   . TYR B  2 75  ? -19.813 -1.223  0.620    1.00 211.22 ? 185  TYR B C   1 
ATOM   5136  O  O   . TYR B  2 75  ? -18.695 -1.085  1.122    1.00 204.34 ? 185  TYR B O   1 
ATOM   5137  C  CB  . TYR B  2 75  ? -20.950 -3.449  0.870    1.00 208.58 ? 185  TYR B CB  1 
ATOM   5138  C  CG  . TYR B  2 75  ? -22.292 -2.916  1.342    1.00 210.14 ? 185  TYR B CG  1 
ATOM   5139  C  CD1 . TYR B  2 75  ? -23.370 -2.815  0.468    1.00 221.19 ? 185  TYR B CD1 1 
ATOM   5140  C  CD2 . TYR B  2 75  ? -22.486 -2.529  2.662    1.00 201.63 ? 185  TYR B CD2 1 
ATOM   5141  C  CE1 . TYR B  2 75  ? -24.601 -2.332  0.894    1.00 223.38 ? 185  TYR B CE1 1 
ATOM   5142  C  CE2 . TYR B  2 75  ? -23.715 -2.047  3.097    1.00 204.64 ? 185  TYR B CE2 1 
ATOM   5143  C  CZ  . TYR B  2 75  ? -24.767 -1.951  2.209    1.00 214.29 ? 185  TYR B CZ  1 
ATOM   5144  O  OH  . TYR B  2 75  ? -25.985 -1.472  2.641    1.00 216.94 ? 185  TYR B OH  1 
ATOM   5145  N  N   . PHE B  2 76  ? -20.748 -0.278  0.645    1.00 215.89 ? 186  PHE B N   1 
ATOM   5146  C  CA  . PHE B  2 76  ? -20.554 1.010   1.297    1.00 213.03 ? 186  PHE B CA  1 
ATOM   5147  C  C   . PHE B  2 76  ? -21.159 0.968   2.693    1.00 203.81 ? 186  PHE B C   1 
ATOM   5148  O  O   . PHE B  2 76  ? -22.364 0.734   2.844    1.00 206.14 ? 186  PHE B O   1 
ATOM   5149  C  CB  . PHE B  2 76  ? -21.183 2.140   0.483    1.00 224.57 ? 186  PHE B CB  1 
ATOM   5150  C  CG  . PHE B  2 76  ? -21.003 3.495   1.101    1.00 222.75 ? 186  PHE B CG  1 
ATOM   5151  C  CD1 . PHE B  2 76  ? -19.819 4.192   0.934    1.00 222.45 ? 186  PHE B CD1 1 
ATOM   5152  C  CD2 . PHE B  2 76  ? -22.016 4.072   1.852    1.00 221.87 ? 186  PHE B CD2 1 
ATOM   5153  C  CE1 . PHE B  2 76  ? -19.645 5.437   1.505    1.00 221.25 ? 186  PHE B CE1 1 
ATOM   5154  C  CE2 . PHE B  2 76  ? -21.849 5.319   2.426    1.00 220.65 ? 186  PHE B CE2 1 
ATOM   5155  C  CZ  . PHE B  2 76  ? -20.661 6.002   2.251    1.00 220.33 ? 186  PHE B CZ  1 
ATOM   5156  N  N   . CYS B  2 77  ? -20.331 1.196   3.709    1.00 193.89 ? 187  CYS B N   1 
ATOM   5157  C  CA  . CYS B  2 77  ? -20.816 1.235   5.077    1.00 186.79 ? 187  CYS B CA  1 
ATOM   5158  C  C   . CYS B  2 77  ? -20.038 2.266   5.887    1.00 179.39 ? 187  CYS B C   1 
ATOM   5159  O  O   . CYS B  2 77  ? -18.983 2.756   5.474    1.00 180.70 ? 187  CYS B O   1 
ATOM   5160  C  CB  . CYS B  2 77  ? -20.734 -0.148  5.723    1.00 182.60 ? 187  CYS B CB  1 
ATOM   5161  S  SG  . CYS B  2 77  ? -19.089 -0.841  5.844    1.00 174.89 ? 187  CYS B SG  1 
ATOM   5162  N  N   . LEU B  2 78  ? -20.590 2.586   7.057    1.00 177.25 ? 188  LEU B N   1 
ATOM   5163  C  CA  . LEU B  2 78  ? -20.001 3.551   7.975    1.00 170.16 ? 188  LEU B CA  1 
ATOM   5164  C  C   . LEU B  2 78  ? -18.650 3.057   8.503    1.00 186.61 ? 188  LEU B C   1 
ATOM   5165  O  O   . LEU B  2 78  ? -18.418 1.848   8.609    1.00 197.39 ? 188  LEU B O   1 
ATOM   5166  C  CB  . LEU B  2 78  ? -20.952 3.797   9.147    1.00 178.53 ? 188  LEU B CB  1 
ATOM   5167  C  CG  . LEU B  2 78  ? -22.412 4.143   8.838    1.00 195.28 ? 188  LEU B CG  1 
ATOM   5168  C  CD1 . LEU B  2 78  ? -23.192 4.406   10.124   1.00 178.12 ? 188  LEU B CD1 1 
ATOM   5169  C  CD2 . LEU B  2 78  ? -22.519 5.327   7.886    1.00 203.18 ? 188  LEU B CD2 1 
ATOM   5170  N  N   . PRO B  2 79  ? -17.741 3.971   8.845    1.00 164.75 ? 189  PRO B N   1 
ATOM   5171  C  CA  . PRO B  2 79  ? -16.458 3.568   9.440    1.00 154.31 ? 189  PRO B CA  1 
ATOM   5172  C  C   . PRO B  2 79  ? -16.656 2.920   10.805   1.00 138.70 ? 189  PRO B C   1 
ATOM   5173  O  O   . PRO B  2 79  ? -17.734 2.964   11.397   1.00 137.36 ? 189  PRO B O   1 
ATOM   5174  C  CB  . PRO B  2 79  ? -15.692 4.890   9.557    1.00 158.40 ? 189  PRO B CB  1 
ATOM   5175  C  CG  . PRO B  2 79  ? -16.759 5.939   9.605    1.00 155.67 ? 189  PRO B CG  1 
ATOM   5176  C  CD  . PRO B  2 79  ? -17.850 5.434   8.710    1.00 162.57 ? 189  PRO B CD  1 
ATOM   5177  N  N   . THR B  2 80  ? -15.588 2.290   11.304   1.00 131.92 ? 190  THR B N   1 
ATOM   5178  C  CA  . THR B  2 80  ? -15.639 1.617   12.601   1.00 166.22 ? 190  THR B CA  1 
ATOM   5179  C  C   . THR B  2 80  ? -15.501 2.626   13.734   1.00 152.51 ? 190  THR B C   1 
ATOM   5180  O  O   . THR B  2 80  ? -14.581 3.451   13.737   1.00 172.34 ? 190  THR B O   1 
ATOM   5181  C  CB  . THR B  2 80  ? -14.546 0.555   12.726   1.00 131.56 ? 190  THR B CB  1 
ATOM   5182  O  OG1 . THR B  2 80  ? -14.630 -0.361  11.628   1.00 162.82 ? 190  THR B OG1 1 
ATOM   5183  C  CG2 . THR B  2 80  ? -14.689 -0.205  14.042   1.00 108.73 ? 190  THR B CG2 1 
ATOM   5184  N  N   . PHE B  2 81  ? -16.426 2.573   14.686   1.00 116.54 ? 191  PHE B N   1 
ATOM   5185  C  CA  . PHE B  2 81  ? -16.387 3.456   15.838   1.00 115.40 ? 191  PHE B CA  1 
ATOM   5186  C  C   . PHE B  2 81  ? -16.697 2.652   17.085   1.00 108.45 ? 191  PHE B C   1 
ATOM   5187  O  O   . PHE B  2 81  ? -17.414 1.651   17.030   1.00 106.77 ? 191  PHE B O   1 
ATOM   5188  C  CB  . PHE B  2 81  ? -17.386 4.608   15.715   1.00 122.96 ? 191  PHE B CB  1 
ATOM   5189  C  CG  . PHE B  2 81  ? -18.802 4.157   15.558   1.00 125.62 ? 191  PHE B CG  1 
ATOM   5190  C  CD1 . PHE B  2 81  ? -19.312 3.859   14.311   1.00 130.96 ? 191  PHE B CD1 1 
ATOM   5191  C  CD2 . PHE B  2 81  ? -19.621 4.023   16.662   1.00 123.42 ? 191  PHE B CD2 1 
ATOM   5192  C  CE1 . PHE B  2 81  ? -20.614 3.446   14.163   1.00 134.22 ? 191  PHE B CE1 1 
ATOM   5193  C  CE2 . PHE B  2 81  ? -20.923 3.608   16.523   1.00 126.67 ? 191  PHE B CE2 1 
ATOM   5194  C  CZ  . PHE B  2 81  ? -21.422 3.317   15.270   1.00 132.15 ? 191  PHE B CZ  1 
ATOM   5195  N  N   . GLY B  2 82  ? -16.143 3.097   18.209   1.00 122.02 ? 192  GLY B N   1 
ATOM   5196  C  CA  . GLY B  2 82  ? -16.369 2.437   19.479   1.00 98.88  ? 192  GLY B CA  1 
ATOM   5197  C  C   . GLY B  2 82  ? -17.807 2.511   19.954   1.00 101.28 ? 192  GLY B C   1 
ATOM   5198  O  O   . GLY B  2 82  ? -18.486 1.484   20.051   1.00 100.74 ? 192  GLY B O   1 
ATOM   5199  N  N   . PHE B  2 83  ? -18.291 3.717   20.251   1.00 106.22 ? 193  PHE B N   1 
ATOM   5200  C  CA  . PHE B  2 83  ? -19.660 3.889   20.723   1.00 109.52 ? 193  PHE B CA  1 
ATOM   5201  C  C   . PHE B  2 83  ? -20.089 5.332   20.517   1.00 117.19 ? 193  PHE B C   1 
ATOM   5202  O  O   . PHE B  2 83  ? -19.346 6.262   20.851   1.00 117.73 ? 193  PHE B O   1 
ATOM   5203  C  CB  . PHE B  2 83  ? -19.807 3.499   22.198   1.00 104.35 ? 193  PHE B CB  1 
ATOM   5204  C  CG  . PHE B  2 83  ? -21.006 4.110   22.865   1.00 108.87 ? 193  PHE B CG  1 
ATOM   5205  C  CD1 . PHE B  2 83  ? -22.290 3.700   22.533   1.00 112.92 ? 193  PHE B CD1 1 
ATOM   5206  C  CD2 . PHE B  2 83  ? -20.848 5.101   23.819   1.00 120.38 ? 193  PHE B CD2 1 
ATOM   5207  C  CE1 . PHE B  2 83  ? -23.395 4.262   23.143   1.00 117.80 ? 193  PHE B CE1 1 
ATOM   5208  C  CE2 . PHE B  2 83  ? -21.948 5.670   24.432   1.00 146.92 ? 193  PHE B CE2 1 
ATOM   5209  C  CZ  . PHE B  2 83  ? -23.226 5.248   24.094   1.00 128.68 ? 193  PHE B CZ  1 
ATOM   5210  N  N   . LYS B  2 84  ? -21.281 5.510   19.956   1.00 123.68 ? 194  LYS B N   1 
ATOM   5211  C  CA  . LYS B  2 84  ? -21.862 6.823   19.717   1.00 132.03 ? 194  LYS B CA  1 
ATOM   5212  C  C   . LYS B  2 84  ? -23.184 6.930   20.464   1.00 135.19 ? 194  LYS B C   1 
ATOM   5213  O  O   . LYS B  2 84  ? -24.103 6.139   20.225   1.00 136.45 ? 194  LYS B O   1 
ATOM   5214  C  CB  . LYS B  2 84  ? -22.071 7.053   18.219   1.00 157.38 ? 194  LYS B CB  1 
ATOM   5215  C  CG  . LYS B  2 84  ? -20.778 7.198   17.427   1.00 137.70 ? 194  LYS B CG  1 
ATOM   5216  C  CD  . LYS B  2 84  ? -21.062 7.478   15.960   1.00 145.47 ? 194  LYS B CD  1 
ATOM   5217  C  CE  . LYS B  2 84  ? -19.773 7.667   15.174   1.00 145.21 ? 194  LYS B CE  1 
ATOM   5218  N  NZ  . LYS B  2 84  ? -20.030 7.976   13.736   1.00 180.95 ? 194  LYS B NZ  1 
ATOM   5219  N  N   . HIS B  2 85  ? -23.286 7.916   21.350   1.00 137.17 ? 195  HIS B N   1 
ATOM   5220  C  CA  . HIS B  2 85  ? -24.543 8.231   22.021   1.00 143.29 ? 195  HIS B CA  1 
ATOM   5221  C  C   . HIS B  2 85  ? -25.346 9.155   21.112   1.00 174.34 ? 195  HIS B C   1 
ATOM   5222  O  O   . HIS B  2 85  ? -25.004 10.331  20.943   1.00 156.74 ? 195  HIS B O   1 
ATOM   5223  C  CB  . HIS B  2 85  ? -24.300 8.873   23.383   1.00 158.24 ? 195  HIS B CB  1 
ATOM   5224  C  CG  . HIS B  2 85  ? -25.551 9.351   24.056   1.00 156.18 ? 195  HIS B CG  1 
ATOM   5225  N  ND1 . HIS B  2 85  ? -26.619 8.521   24.323   1.00 146.49 ? 195  HIS B ND1 1 
ATOM   5226  C  CD2 . HIS B  2 85  ? -25.910 10.579  24.498   1.00 178.73 ? 195  HIS B CD2 1 
ATOM   5227  C  CE1 . HIS B  2 85  ? -27.577 9.215   24.911   1.00 152.86 ? 195  HIS B CE1 1 
ATOM   5228  N  NE2 . HIS B  2 85  ? -27.172 10.466  25.029   1.00 156.22 ? 195  HIS B NE2 1 
ATOM   5229  N  N   . ILE B  2 86  ? -26.406 8.619   20.516   1.00 176.99 ? 196  ILE B N   1 
ATOM   5230  C  CA  . ILE B  2 86  ? -27.163 9.366   19.522   1.00 167.01 ? 196  ILE B CA  1 
ATOM   5231  C  C   . ILE B  2 86  ? -28.328 10.097  20.174   1.00 174.24 ? 196  ILE B C   1 
ATOM   5232  O  O   . ILE B  2 86  ? -28.424 11.326  20.087   1.00 184.91 ? 196  ILE B O   1 
ATOM   5233  C  CB  . ILE B  2 86  ? -27.639 8.438   18.392   1.00 173.12 ? 196  ILE B CB  1 
ATOM   5234  C  CG1 . ILE B  2 86  ? -26.432 7.734   17.761   1.00 162.23 ? 196  ILE B CG1 1 
ATOM   5235  C  CG2 . ILE B  2 86  ? -28.412 9.226   17.350   1.00 192.53 ? 196  ILE B CG2 1 
ATOM   5236  C  CD1 . ILE B  2 86  ? -26.760 6.870   16.561   1.00 164.62 ? 196  ILE B CD1 1 
ATOM   5237  N  N   . LEU B  2 87  ? -29.206 9.359   20.843   1.00 173.48 ? 197  LEU B N   1 
ATOM   5238  C  CA  . LEU B  2 87  ? -30.442 9.933   21.381   1.00 181.48 ? 197  LEU B CA  1 
ATOM   5239  C  C   . LEU B  2 87  ? -30.488 9.889   22.903   1.00 177.07 ? 197  LEU B C   1 
ATOM   5240  O  O   . LEU B  2 87  ? -30.561 8.791   23.486   1.00 171.06 ? 197  LEU B O   1 
ATOM   5241  C  CB  . LEU B  2 87  ? -31.655 9.212   20.798   1.00 187.41 ? 197  LEU B CB  1 
ATOM   5242  C  CG  . LEU B  2 87  ? -33.002 9.735   21.295   1.00 196.79 ? 197  LEU B CG  1 
ATOM   5243  C  CD1 . LEU B  2 87  ? -33.187 11.188  20.902   1.00 205.91 ? 197  LEU B CD1 1 
ATOM   5244  C  CD2 . LEU B  2 87  ? -34.129 8.886   20.748   1.00 202.39 ? 197  LEU B CD2 1 
ATOM   5245  N  N   . PRO B  2 88  ? -30.418 11.033  23.587   1.00 192.73 ? 198  PRO B N   1 
ATOM   5246  C  CA  . PRO B  2 88  ? -30.723 11.055  25.021   1.00 178.23 ? 198  PRO B CA  1 
ATOM   5247  C  C   . PRO B  2 88  ? -32.181 10.707  25.263   1.00 184.92 ? 198  PRO B C   1 
ATOM   5248  O  O   . PRO B  2 88  ? -33.063 11.091  24.492   1.00 194.25 ? 198  PRO B O   1 
ATOM   5249  C  CB  . PRO B  2 88  ? -30.421 12.501  25.432   1.00 182.38 ? 198  PRO B CB  1 
ATOM   5250  C  CG  . PRO B  2 88  ? -29.503 13.015  24.381   1.00 193.88 ? 198  PRO B CG  1 
ATOM   5251  C  CD  . PRO B  2 88  ? -29.943 12.342  23.109   1.00 209.03 ? 198  PRO B CD  1 
ATOM   5252  N  N   . LEU B  2 89  ? -32.429 9.979   26.348   1.00 180.73 ? 199  LEU B N   1 
ATOM   5253  C  CA  . LEU B  2 89  ? -33.769 9.470   26.605   1.00 198.65 ? 199  LEU B CA  1 
ATOM   5254  C  C   . LEU B  2 89  ? -34.751 10.611  26.847   1.00 200.34 ? 199  LEU B C   1 
ATOM   5255  O  O   . LEU B  2 89  ? -34.541 11.458  27.720   1.00 198.44 ? 199  LEU B O   1 
ATOM   5256  C  CB  . LEU B  2 89  ? -33.752 8.498   27.787   1.00 180.16 ? 199  LEU B CB  1 
ATOM   5257  C  CG  . LEU B  2 89  ? -33.274 8.938   29.170   1.00 176.28 ? 199  LEU B CG  1 
ATOM   5258  C  CD1 . LEU B  2 89  ? -34.458 9.312   30.038   1.00 187.32 ? 199  LEU B CD1 1 
ATOM   5259  C  CD2 . LEU B  2 89  ? -32.481 7.820   29.820   1.00 165.57 ? 199  LEU B CD2 1 
ATOM   5260  N  N   . THR B  2 90  ? -35.829 10.628  26.062   1.00 210.00 ? 200  THR B N   1 
ATOM   5261  C  CA  . THR B  2 90  ? -36.838 11.675  26.138   1.00 229.77 ? 200  THR B CA  1 
ATOM   5262  C  C   . THR B  2 90  ? -38.206 11.069  25.864   1.00 232.49 ? 200  THR B C   1 
ATOM   5263  O  O   . THR B  2 90  ? -38.329 9.936   25.390   1.00 225.06 ? 200  THR B O   1 
ATOM   5264  C  CB  . THR B  2 90  ? -36.579 12.808  25.131   1.00 238.68 ? 200  THR B CB  1 
ATOM   5265  O  OG1 . THR B  2 90  ? -36.473 12.264  23.809   1.00 236.48 ? 200  THR B OG1 1 
ATOM   5266  C  CG2 . THR B  2 90  ? -35.310 13.582  25.470   1.00 234.50 ? 200  THR B CG2 1 
ATOM   5267  N  N   . ASN B  2 91  ? -39.246 11.851  26.163   1.00 239.00 ? 201  ASN B N   1 
ATOM   5268  C  CA  . ASN B  2 91  ? -40.602 11.383  25.908   1.00 248.83 ? 201  ASN B CA  1 
ATOM   5269  C  C   . ASN B  2 91  ? -40.921 11.390  24.418   1.00 255.36 ? 201  ASN B C   1 
ATOM   5270  O  O   . ASN B  2 91  ? -41.726 10.571  23.960   1.00 260.44 ? 201  ASN B O   1 
ATOM   5271  C  CB  . ASN B  2 91  ? -41.616 12.211  26.702   1.00 259.46 ? 201  ASN B CB  1 
ATOM   5272  C  CG  . ASN B  2 91  ? -41.500 13.694  26.440   1.00 265.96 ? 201  ASN B CG  1 
ATOM   5273  O  OD1 . ASN B  2 91  ? -41.384 14.131  25.298   1.00 281.99 ? 201  ASN B OD1 1 
ATOM   5274  N  ND2 . ASN B  2 91  ? -41.537 14.483  27.506   1.00 267.68 ? 201  ASN B ND2 1 
ATOM   5275  N  N   . ASP B  2 92  ? -40.318 12.305  23.654   1.00 256.46 ? 202  ASP B N   1 
ATOM   5276  C  CA  . ASP B  2 92  ? -40.548 12.371  22.214   1.00 262.96 ? 202  ASP B CA  1 
ATOM   5277  C  C   . ASP B  2 92  ? -40.247 11.014  21.588   1.00 256.13 ? 202  ASP B C   1 
ATOM   5278  O  O   . ASP B  2 92  ? -39.080 10.650  21.414   1.00 245.33 ? 202  ASP B O   1 
ATOM   5279  C  CB  . ASP B  2 92  ? -39.686 13.460  21.561   1.00 263.01 ? 202  ASP B CB  1 
ATOM   5280  C  CG  . ASP B  2 92  ? -40.159 14.870  21.889   1.00 274.43 ? 202  ASP B CG  1 
ATOM   5281  O  OD1 . ASP B  2 92  ? -40.229 15.216  23.085   1.00 279.61 ? 202  ASP B OD1 1 
ATOM   5282  O  OD2 . ASP B  2 92  ? -40.453 15.638  20.947   1.00 282.55 ? 202  ASP B OD2 1 
ATOM   5283  N  N   . ALA B  2 93  ? -41.294 10.260  21.244   1.00 262.95 ? 203  ALA B N   1 
ATOM   5284  C  CA  . ALA B  2 93  ? -41.136 8.873   20.830   1.00 257.05 ? 203  ALA B CA  1 
ATOM   5285  C  C   . ALA B  2 93  ? -41.033 8.683   19.324   1.00 260.44 ? 203  ALA B C   1 
ATOM   5286  O  O   . ALA B  2 93  ? -40.446 7.687   18.887   1.00 252.85 ? 203  ALA B O   1 
ATOM   5287  C  CB  . ALA B  2 93  ? -42.307 8.033   21.361   1.00 262.47 ? 203  ALA B CB  1 
ATOM   5288  N  N   . GLU B  2 94  ? -41.560 9.603   18.517   1.00 271.86 ? 204  GLU B N   1 
ATOM   5289  C  CA  . GLU B  2 94  ? -41.376 9.471   17.079   1.00 275.12 ? 204  GLU B CA  1 
ATOM   5290  C  C   . GLU B  2 94  ? -40.013 9.954   16.633   1.00 267.16 ? 204  GLU B C   1 
ATOM   5291  O  O   . GLU B  2 94  ? -39.580 9.613   15.528   1.00 266.55 ? 204  GLU B O   1 
ATOM   5292  C  CB  . GLU B  2 94  ? -42.469 10.204  16.305   1.00 291.26 ? 204  GLU B CB  1 
ATOM   5293  C  CG  . GLU B  2 94  ? -43.820 9.547   16.422   1.00 300.56 ? 204  GLU B CG  1 
ATOM   5294  C  CD  . GLU B  2 94  ? -44.716 9.889   15.259   1.00 315.53 ? 204  GLU B CD  1 
ATOM   5295  O  OE1 . GLU B  2 94  ? -44.364 10.814  14.494   1.00 319.54 ? 204  GLU B OE1 1 
ATOM   5296  O  OE2 . GLU B  2 94  ? -45.774 9.242   15.118   1.00 323.89 ? 204  GLU B OE2 1 
ATOM   5297  N  N   . ARG B  2 95  ? -39.326 10.724  17.473   1.00 261.55 ? 205  ARG B N   1 
ATOM   5298  C  CA  . ARG B  2 95  ? -37.936 11.039  17.189   1.00 252.87 ? 205  ARG B CA  1 
ATOM   5299  C  C   . ARG B  2 95  ? -37.072 9.806   17.374   1.00 239.79 ? 205  ARG B C   1 
ATOM   5300  O  O   . ARG B  2 95  ? -36.056 9.648   16.688   1.00 234.08 ? 205  ARG B O   1 
ATOM   5301  C  CB  . ARG B  2 95  ? -37.463 12.175  18.097   1.00 251.06 ? 205  ARG B CB  1 
ATOM   5302  C  CG  . ARG B  2 95  ? -36.083 12.709  17.778   1.00 244.48 ? 205  ARG B CG  1 
ATOM   5303  C  CD  . ARG B  2 95  ? -36.012 13.202  16.349   1.00 252.13 ? 205  ARG B CD  1 
ATOM   5304  N  NE  . ARG B  2 95  ? -34.680 13.693  16.020   1.00 249.23 ? 205  ARG B NE  1 
ATOM   5305  C  CZ  . ARG B  2 95  ? -34.282 14.945  16.214   1.00 249.63 ? 205  ARG B CZ  1 
ATOM   5306  N  NH1 . ARG B  2 95  ? -35.115 15.837  16.735   1.00 258.16 ? 205  ARG B NH1 1 
ATOM   5307  N  NH2 . ARG B  2 95  ? -33.050 15.305  15.886   1.00 244.79 ? 205  ARG B NH2 1 
ATOM   5308  N  N   . PHE B  2 96  ? -37.466 8.924   18.295   1.00 235.54 ? 206  PHE B N   1 
ATOM   5309  C  CA  . PHE B  2 96  ? -36.758 7.663   18.474   1.00 224.14 ? 206  PHE B CA  1 
ATOM   5310  C  C   . PHE B  2 96  ? -36.850 6.803   17.223   1.00 226.03 ? 206  PHE B C   1 
ATOM   5311  O  O   . PHE B  2 96  ? -35.843 6.267   16.749   1.00 218.10 ? 206  PHE B O   1 
ATOM   5312  C  CB  . PHE B  2 96  ? -37.323 6.916   19.684   1.00 221.33 ? 206  PHE B CB  1 
ATOM   5313  C  CG  . PHE B  2 96  ? -36.835 5.495   19.808   1.00 218.03 ? 206  PHE B CG  1 
ATOM   5314  C  CD1 . PHE B  2 96  ? -35.592 5.218   20.358   1.00 203.70 ? 206  PHE B CD1 1 
ATOM   5315  C  CD2 . PHE B  2 96  ? -37.626 4.436   19.388   1.00 235.60 ? 206  PHE B CD2 1 
ATOM   5316  C  CE1 . PHE B  2 96  ? -35.143 3.910   20.478   1.00 191.27 ? 206  PHE B CE1 1 
ATOM   5317  C  CE2 . PHE B  2 96  ? -37.181 3.124   19.508   1.00 235.26 ? 206  PHE B CE2 1 
ATOM   5318  C  CZ  . PHE B  2 96  ? -35.939 2.863   20.053   1.00 195.56 ? 206  PHE B CZ  1 
ATOM   5319  N  N   . ASN B  2 97  ? -38.055 6.669   16.667   1.00 237.16 ? 207  ASN B N   1 
ATOM   5320  C  CA  . ASN B  2 97  ? -38.240 5.812   15.501   1.00 240.02 ? 207  ASN B CA  1 
ATOM   5321  C  C   . ASN B  2 97  ? -37.457 6.329   14.301   1.00 240.78 ? 207  ASN B C   1 
ATOM   5322  O  O   . ASN B  2 97  ? -36.834 5.545   13.575   1.00 236.02 ? 207  ASN B O   1 
ATOM   5323  C  CB  . ASN B  2 97  ? -39.726 5.700   15.174   1.00 253.34 ? 207  ASN B CB  1 
ATOM   5324  C  CG  . ASN B  2 97  ? -40.499 4.982   16.257   1.00 253.01 ? 207  ASN B CG  1 
ATOM   5325  O  OD1 . ASN B  2 97  ? -39.942 4.182   17.008   1.00 242.46 ? 207  ASN B OD1 1 
ATOM   5326  N  ND2 . ASN B  2 97  ? -41.791 5.272   16.352   1.00 265.21 ? 207  ASN B ND2 1 
ATOM   5327  N  N   . GLU B  2 98  ? -37.464 7.647   14.086   1.00 247.09 ? 208  GLU B N   1 
ATOM   5328  C  CA  . GLU B  2 98  ? -36.784 8.235   12.936   1.00 249.45 ? 208  GLU B CA  1 
ATOM   5329  C  C   . GLU B  2 98  ? -35.282 7.985   12.957   1.00 237.01 ? 208  GLU B C   1 
ATOM   5330  O  O   . GLU B  2 98  ? -34.625 8.116   11.919   1.00 237.68 ? 208  GLU B O   1 
ATOM   5331  C  CB  . GLU B  2 98  ? -37.065 9.738   12.884   1.00 258.51 ? 208  GLU B CB  1 
ATOM   5332  C  CG  . GLU B  2 98  ? -38.515 10.091  12.588   1.00 273.01 ? 208  GLU B CG  1 
ATOM   5333  C  CD  . GLU B  2 98  ? -38.851 11.524  12.956   1.00 280.75 ? 208  GLU B CD  1 
ATOM   5334  O  OE1 . GLU B  2 98  ? -37.916 12.306  13.230   1.00 275.78 ? 208  GLU B OE1 1 
ATOM   5335  O  OE2 . GLU B  2 98  ? -40.052 11.867  12.989   1.00 292.24 ? 208  GLU B OE2 1 
ATOM   5336  N  N   . ILE B  2 99  ? -34.723 7.638   14.115   1.00 231.75 ? 209  ILE B N   1 
ATOM   5337  C  CA  . ILE B  2 99  ? -33.296 7.354   14.197   1.00 214.83 ? 209  ILE B CA  1 
ATOM   5338  C  C   . ILE B  2 99  ? -33.016 5.912   13.809   1.00 208.71 ? 209  ILE B C   1 
ATOM   5339  O  O   . ILE B  2 99  ? -32.064 5.631   13.074   1.00 204.53 ? 209  ILE B O   1 
ATOM   5340  C  CB  . ILE B  2 99  ? -32.781 7.672   15.609   1.00 206.78 ? 209  ILE B CB  1 
ATOM   5341  C  CG1 . ILE B  2 99  ? -32.951 9.163   15.909   1.00 213.21 ? 209  ILE B CG1 1 
ATOM   5342  C  CG2 . ILE B  2 99  ? -31.329 7.242   15.755   1.00 195.05 ? 209  ILE B CG2 1 
ATOM   5343  C  CD1 . ILE B  2 99  ? -32.634 9.540   17.332   1.00 207.23 ? 209  ILE B CD1 1 
ATOM   5344  N  N   . VAL B  2 100 ? -33.843 4.981   14.284   1.00 208.83 ? 210  VAL B N   1 
ATOM   5345  C  CA  . VAL B  2 100 ? -33.630 3.569   13.993   1.00 207.55 ? 210  VAL B CA  1 
ATOM   5346  C  C   . VAL B  2 100 ? -33.805 3.280   12.508   1.00 210.14 ? 210  VAL B C   1 
ATOM   5347  O  O   . VAL B  2 100 ? -33.144 2.389   11.961   1.00 204.94 ? 210  VAL B O   1 
ATOM   5348  C  CB  . VAL B  2 100 ? -34.574 2.713   14.855   1.00 214.01 ? 210  VAL B CB  1 
ATOM   5349  C  CG1 . VAL B  2 100 ? -34.197 1.246   14.758   1.00 206.35 ? 210  VAL B CG1 1 
ATOM   5350  C  CG2 . VAL B  2 100 ? -34.538 3.180   16.301   1.00 211.97 ? 210  VAL B CG2 1 
ATOM   5351  N  N   . LYS B  2 101 ? -34.681 4.022   11.830   1.00 222.09 ? 211  LYS B N   1 
ATOM   5352  C  CA  . LYS B  2 101 ? -34.937 3.772   10.415   1.00 229.84 ? 211  LYS B CA  1 
ATOM   5353  C  C   . LYS B  2 101 ? -33.705 4.070   9.566    1.00 226.35 ? 211  LYS B C   1 
ATOM   5354  O  O   . LYS B  2 101 ? -33.381 3.313   8.643    1.00 226.04 ? 211  LYS B O   1 
ATOM   5355  C  CB  . LYS B  2 101 ? -36.123 4.615   9.952    1.00 244.17 ? 211  LYS B CB  1 
ATOM   5356  C  CG  . LYS B  2 101 ? -37.413 4.362   10.725   1.00 249.46 ? 211  LYS B CG  1 
ATOM   5357  C  CD  . LYS B  2 101 ? -38.352 5.558   10.603   1.00 262.18 ? 211  LYS B CD  1 
ATOM   5358  C  CE  . LYS B  2 101 ? -39.589 5.417   11.479   1.00 267.71 ? 211  LYS B CE  1 
ATOM   5359  N  NZ  . LYS B  2 101 ? -40.463 6.624   11.391   1.00 280.36 ? 211  LYS B NZ  1 
ATOM   5360  N  N   . ASN B  2 102 ? -33.008 5.165   9.862    1.00 224.25 ? 212  ASN B N   1 
ATOM   5361  C  CA  . ASN B  2 102 ? -31.889 5.617   9.045    1.00 222.82 ? 212  ASN B CA  1 
ATOM   5362  C  C   . ASN B  2 102 ? -30.586 4.904   9.370    1.00 210.04 ? 212  ASN B C   1 
ATOM   5363  O  O   . ASN B  2 102 ? -29.562 5.220   8.755    1.00 208.33 ? 212  ASN B O   1 
ATOM   5364  C  CB  . ASN B  2 102 ? -31.689 7.124   9.215    1.00 226.98 ? 212  ASN B CB  1 
ATOM   5365  C  CG  . ASN B  2 102 ? -32.962 7.904   9.011    1.00 239.82 ? 212  ASN B CG  1 
ATOM   5366  O  OD1 . ASN B  2 102 ? -34.054 7.337   9.019    1.00 244.79 ? 212  ASN B OD1 1 
ATOM   5367  N  ND2 . ASN B  2 102 ? -32.836 9.213   8.836    1.00 245.87 ? 212  ASN B ND2 1 
ATOM   5368  N  N   . GLN B  2 103 ? -30.594 3.969   10.317   1.00 201.71 ? 213  GLN B N   1 
ATOM   5369  C  CA  . GLN B  2 103 ? -29.364 3.308   10.732   1.00 189.82 ? 213  GLN B CA  1 
ATOM   5370  C  C   . GLN B  2 103 ? -28.811 2.416   9.628    1.00 188.77 ? 213  GLN B C   1 
ATOM   5371  O  O   . GLN B  2 103 ? -29.514 1.551   9.096    1.00 193.22 ? 213  GLN B O   1 
ATOM   5372  C  CB  . GLN B  2 103 ? -29.609 2.491   11.996   1.00 182.37 ? 213  GLN B CB  1 
ATOM   5373  C  CG  . GLN B  2 103 ? -29.833 3.333   13.240   1.00 181.16 ? 213  GLN B CG  1 
ATOM   5374  C  CD  . GLN B  2 103 ? -28.628 4.184   13.598   1.00 175.81 ? 213  GLN B CD  1 
ATOM   5375  O  OE1 . GLN B  2 103 ? -27.492 3.864   13.242   1.00 169.93 ? 213  GLN B OE1 1 
ATOM   5376  N  NE2 . GLN B  2 103 ? -28.871 5.274   14.316   1.00 178.34 ? 213  GLN B NE2 1 
ATOM   5377  N  N   . LYS B  2 104 ? -27.548 2.636   9.285    1.00 185.07 ? 214  LYS B N   1 
ATOM   5378  C  CA  . LYS B  2 104 ? -26.830 1.824   8.317    1.00 186.24 ? 214  LYS B CA  1 
ATOM   5379  C  C   . LYS B  2 104 ? -25.845 0.905   9.033    1.00 174.62 ? 214  LYS B C   1 
ATOM   5380  O  O   . LYS B  2 104 ? -25.531 1.085   10.213   1.00 165.73 ? 214  LYS B O   1 
ATOM   5381  C  CB  . LYS B  2 104 ? -26.089 2.702   7.303    1.00 192.50 ? 214  LYS B CB  1 
ATOM   5382  C  CG  . LYS B  2 104 ? -26.983 3.617   6.476    1.00 205.18 ? 214  LYS B CG  1 
ATOM   5383  C  CD  . LYS B  2 104 ? -26.175 4.365   5.420    1.00 211.63 ? 214  LYS B CD  1 
ATOM   5384  C  CE  . LYS B  2 104 ? -27.017 5.401   4.681    1.00 224.44 ? 214  LYS B CE  1 
ATOM   5385  N  NZ  . LYS B  2 104 ? -27.524 6.489   5.568    1.00 223.89 ? 214  LYS B NZ  1 
ATOM   5386  N  N   . ILE B  2 105 ? -25.362 -0.092  8.294    1.00 175.40 ? 215  ILE B N   1 
ATOM   5387  C  CA  . ILE B  2 105 ? -24.436 -1.088  8.824    1.00 165.93 ? 215  ILE B CA  1 
ATOM   5388  C  C   . ILE B  2 105 ? -23.021 -0.528  8.805    1.00 161.95 ? 215  ILE B C   1 
ATOM   5389  O  O   . ILE B  2 105 ? -22.675 0.312   7.970    1.00 168.31 ? 215  ILE B O   1 
ATOM   5390  C  CB  . ILE B  2 105 ? -24.525 -2.399  8.016    1.00 170.74 ? 215  ILE B CB  1 
ATOM   5391  C  CG1 . ILE B  2 105 ? -25.978 -2.700  7.634    1.00 192.96 ? 215  ILE B CG1 1 
ATOM   5392  C  CG2 . ILE B  2 105 ? -23.933 -3.560  8.805    1.00 159.84 ? 215  ILE B CG2 1 
ATOM   5393  C  CD1 . ILE B  2 105 ? -26.349 -2.296  6.206    1.00 189.92 ? 215  ILE B CD1 1 
ATOM   5394  N  N   . SER B  2 106 ? -22.206 -0.967  9.762    1.00 151.80 ? 216  SER B N   1 
ATOM   5395  C  CA  . SER B  2 106 ? -20.772 -0.733  9.779    1.00 147.63 ? 216  SER B CA  1 
ATOM   5396  C  C   . SER B  2 106 ? -20.055 -2.062  9.558    1.00 144.67 ? 216  SER B C   1 
ATOM   5397  O  O   . SER B  2 106 ? -20.654 -3.030  9.068    1.00 148.13 ? 216  SER B O   1 
ATOM   5398  C  CB  . SER B  2 106 ? -20.360 -0.075  11.092   1.00 139.10 ? 216  SER B CB  1 
ATOM   5399  O  OG  . SER B  2 106 ? -21.035 1.146   11.291   1.00 142.45 ? 216  SER B OG  1 
ATOM   5400  N  N   . ALA B  2 107 ? -18.787 -2.121  9.946    1.00 138.70 ? 217  ALA B N   1 
ATOM   5401  C  CA  . ALA B  2 107 ? -18.035 -3.352  9.775    1.00 136.28 ? 217  ALA B CA  1 
ATOM   5402  C  C   . ALA B  2 107 ? -16.793 -3.323  10.650   1.00 129.59 ? 217  ALA B C   1 
ATOM   5403  O  O   . ALA B  2 107 ? -16.406 -2.290  11.201   1.00 136.69 ? 217  ALA B O   1 
ATOM   5404  C  CB  . ALA B  2 107 ? -17.649 -3.574  8.313    1.00 144.82 ? 217  ALA B CB  1 
ATOM   5405  N  N   . ASN B  2 108 ? -16.190 -4.496  10.782   1.00 124.86 ? 218  ASN B N   1 
ATOM   5406  C  CA  . ASN B  2 108 ? -14.899 -4.704  11.419   1.00 118.70 ? 218  ASN B CA  1 
ATOM   5407  C  C   . ASN B  2 108 ? -14.419 -6.079  10.955   1.00 138.74 ? 218  ASN B C   1 
ATOM   5408  O  O   . ASN B  2 108 ? -14.882 -6.580  9.924    1.00 130.76 ? 218  ASN B O   1 
ATOM   5409  C  CB  . ASN B  2 108 ? -15.009 -4.548  12.948   1.00 114.71 ? 218  ASN B CB  1 
ATOM   5410  C  CG  . ASN B  2 108 ? -15.865 -5.623  13.589   1.00 108.93 ? 218  ASN B CG  1 
ATOM   5411  O  OD1 . ASN B  2 108 ? -15.345 -6.547  14.202   1.00 101.89 ? 218  ASN B OD1 1 
ATOM   5412  N  ND2 . ASN B  2 108 ? -17.182 -5.490  13.479   1.00 128.85 ? 218  ASN B ND2 1 
ATOM   5413  N  N   . ILE B  2 109 ? -13.503 -6.698  11.703   1.00 148.97 ? 219  ILE B N   1 
ATOM   5414  C  CA  . ILE B  2 109 ? -12.930 -7.985  11.319   1.00 115.26 ? 219  ILE B CA  1 
ATOM   5415  C  C   . ILE B  2 109 ? -13.367 -9.103  12.259   1.00 110.11 ? 219  ILE B C   1 
ATOM   5416  O  O   . ILE B  2 109 ? -13.903 -10.121 11.816   1.00 113.23 ? 219  ILE B O   1 
ATOM   5417  C  CB  . ILE B  2 109 ? -11.386 -7.917  11.236   1.00 114.66 ? 219  ILE B CB  1 
ATOM   5418  C  CG1 . ILE B  2 109 ? -10.921 -6.692  10.462   1.00 179.34 ? 219  ILE B CG1 1 
ATOM   5419  C  CG2 . ILE B  2 109 ? -10.848 -9.171  10.565   1.00 118.17 ? 219  ILE B CG2 1 
ATOM   5420  C  CD1 . ILE B  2 109 ? -9.412  -6.576  10.414   1.00 119.18 ? 219  ILE B CD1 1 
ATOM   5421  N  N   . ASP B  2 110 ? -13.185 -8.913  13.564   1.00 135.27 ? 220  ASP B N   1 
ATOM   5422  C  CA  . ASP B  2 110 ? -13.268 -10.003 14.530   1.00 118.42 ? 220  ASP B CA  1 
ATOM   5423  C  C   . ASP B  2 110 ? -14.680 -10.073 15.099   1.00 96.04  ? 220  ASP B C   1 
ATOM   5424  O  O   . ASP B  2 110 ? -15.251 -9.047  15.489   1.00 94.42  ? 220  ASP B O   1 
ATOM   5425  C  CB  . ASP B  2 110 ? -12.222 -9.838  15.641   1.00 91.47  ? 220  ASP B CB  1 
ATOM   5426  C  CG  . ASP B  2 110 ? -12.551 -8.726  16.627   1.00 86.48  ? 220  ASP B CG  1 
ATOM   5427  O  OD1 . ASP B  2 110 ? -13.305 -7.785  16.313   1.00 105.22 ? 220  ASP B OD1 1 
ATOM   5428  O  OD2 . ASP B  2 110 ? -12.000 -8.777  17.729   1.00 81.07  ? 220  ASP B OD2 1 
ATOM   5429  N  N   . THR B  2 111 ? -15.259 -11.279 15.069   1.00 97.32  ? 221  THR B N   1 
ATOM   5430  C  CA  . THR B  2 111 ? -16.674 -11.488 15.386   1.00 97.49  ? 221  THR B CA  1 
ATOM   5431  C  C   . THR B  2 111 ? -17.127 -10.860 16.703   1.00 91.11  ? 221  THR B C   1 
ATOM   5432  O  O   . THR B  2 111 ? -18.211 -10.254 16.720   1.00 92.53  ? 221  THR B O   1 
ATOM   5433  C  CB  . THR B  2 111 ? -16.976 -12.991 15.339   1.00 118.70 ? 221  THR B CB  1 
ATOM   5434  O  OG1 . THR B  2 111 ? -16.451 -13.540 14.127   1.00 165.21 ? 221  THR B OG1 1 
ATOM   5435  C  CG2 . THR B  2 111 ? -18.473 -13.218 15.345   1.00 101.38 ? 221  THR B CG2 1 
ATOM   5436  N  N   . PRO B  2 112 ? -16.402 -10.983 17.825   1.00 166.69 ? 222  PRO B N   1 
ATOM   5437  C  CA  . PRO B  2 112 ? -16.826 -10.285 19.046   1.00 79.38  ? 222  PRO B CA  1 
ATOM   5438  C  C   . PRO B  2 112 ? -16.606 -8.787  18.937   1.00 79.16  ? 222  PRO B C   1 
ATOM   5439  O  O   . PRO B  2 112 ? -15.661 -8.313  18.299   1.00 81.05  ? 222  PRO B O   1 
ATOM   5440  C  CB  . PRO B  2 112 ? -15.931 -10.890 20.125   1.00 73.90  ? 222  PRO B CB  1 
ATOM   5441  C  CG  . PRO B  2 112 ? -14.725 -11.318 19.394   1.00 76.42  ? 222  PRO B CG  1 
ATOM   5442  C  CD  . PRO B  2 112 ? -15.205 -11.809 18.079   1.00 83.04  ? 222  PRO B CD  1 
ATOM   5443  N  N   . GLU B  2 113 ? -17.445 -8.042  19.641   1.00 76.53  ? 223  GLU B N   1 
ATOM   5444  C  CA  . GLU B  2 113 ? -17.509 -6.604  19.446   1.00 87.95  ? 223  GLU B CA  1 
ATOM   5445  C  C   . GLU B  2 113 ? -17.245 -5.866  20.756   1.00 72.95  ? 223  GLU B C   1 
ATOM   5446  O  O   . GLU B  2 113 ? -17.006 -6.458  21.806   1.00 159.29 ? 223  GLU B O   1 
ATOM   5447  C  CB  . GLU B  2 113 ? -18.868 -6.216  18.841   1.00 83.21  ? 223  GLU B CB  1 
ATOM   5448  C  CG  . GLU B  2 113 ? -19.360 -7.075  17.637   1.00 90.04  ? 223  GLU B CG  1 
ATOM   5449  C  CD  . GLU B  2 113 ? -18.512 -6.960  16.353   1.00 127.09 ? 223  GLU B CD  1 
ATOM   5450  O  OE1 . GLU B  2 113 ? -17.422 -6.349  16.377   1.00 117.92 ? 223  GLU B OE1 1 
ATOM   5451  O  OE2 . GLU B  2 113 ? -18.951 -7.481  15.301   1.00 110.08 ? 223  GLU B OE2 1 
ATOM   5452  N  N   . GLY B  2 114 ? -17.277 -4.546  20.674   1.00 115.41 ? 224  GLY B N   1 
ATOM   5453  C  CA  . GLY B  2 114 ? -17.059 -3.712  21.833   1.00 74.74  ? 224  GLY B CA  1 
ATOM   5454  C  C   . GLY B  2 114 ? -18.388 -3.417  22.496   1.00 125.68 ? 224  GLY B C   1 
ATOM   5455  O  O   . GLY B  2 114 ? -18.766 -2.247  22.657   1.00 81.40  ? 224  GLY B O   1 
ATOM   5456  N  N   . GLY B  2 115 ? -19.138 -4.482  22.810   1.00 76.52  ? 225  GLY B N   1 
ATOM   5457  C  CA  . GLY B  2 115 ? -20.436 -4.299  23.435   1.00 79.88  ? 225  GLY B CA  1 
ATOM   5458  C  C   . GLY B  2 115 ? -20.352 -3.698  24.824   1.00 78.00  ? 225  GLY B C   1 
ATOM   5459  O  O   . GLY B  2 115 ? -21.166 -2.845  25.191   1.00 82.26  ? 225  GLY B O   1 
ATOM   5460  N  N   . PHE B  2 116 ? -19.359 -4.112  25.607   1.00 72.13  ? 226  PHE B N   1 
ATOM   5461  C  CA  . PHE B  2 116 ? -19.284 -3.655  26.989   1.00 70.52  ? 226  PHE B CA  1 
ATOM   5462  C  C   . PHE B  2 116 ? -18.935 -2.177  27.094   1.00 72.96  ? 226  PHE B C   1 
ATOM   5463  O  O   . PHE B  2 116 ? -19.401 -1.507  28.023   1.00 74.73  ? 226  PHE B O   1 
ATOM   5464  C  CB  . PHE B  2 116 ? -18.284 -4.505  27.759   1.00 64.29  ? 226  PHE B CB  1 
ATOM   5465  C  CG  . PHE B  2 116 ? -18.713 -5.933  27.927   1.00 62.33  ? 226  PHE B CG  1 
ATOM   5466  C  CD1 . PHE B  2 116 ? -20.019 -6.300  27.677   1.00 101.11 ? 226  PHE B CD1 1 
ATOM   5467  C  CD2 . PHE B  2 116 ? -17.822 -6.904  28.370   1.00 92.16  ? 226  PHE B CD2 1 
ATOM   5468  C  CE1 . PHE B  2 116 ? -20.427 -7.607  27.829   1.00 94.20  ? 226  PHE B CE1 1 
ATOM   5469  C  CE2 . PHE B  2 116 ? -18.227 -8.222  28.536   1.00 55.97  ? 226  PHE B CE2 1 
ATOM   5470  C  CZ  . PHE B  2 116 ? -19.525 -8.571  28.266   1.00 77.16  ? 226  PHE B CZ  1 
ATOM   5471  N  N   . ASP B  2 117 ? -18.142 -1.654  26.146   1.00 73.71  ? 227  ASP B N   1 
ATOM   5472  C  CA  . ASP B  2 117 ? -17.800 -0.229  26.120   1.00 76.94  ? 227  ASP B CA  1 
ATOM   5473  C  C   . ASP B  2 117 ? -19.045 0.647   26.060   1.00 83.32  ? 227  ASP B C   1 
ATOM   5474  O  O   . ASP B  2 117 ? -19.089 1.725   26.665   1.00 85.80  ? 227  ASP B O   1 
ATOM   5475  C  CB  . ASP B  2 117 ? -16.893 0.080   24.924   1.00 134.94 ? 227  ASP B CB  1 
ATOM   5476  C  CG  . ASP B  2 117 ? -15.416 -0.102  25.236   1.00 141.52 ? 227  ASP B CG  1 
ATOM   5477  O  OD1 . ASP B  2 117 ? -15.088 -0.887  26.148   1.00 100.09 ? 227  ASP B OD1 1 
ATOM   5478  O  OD2 . ASP B  2 117 ? -14.587 0.574   24.579   1.00 108.38 ? 227  ASP B OD2 1 
ATOM   5479  N  N   . ALA B  2 118 ? -20.016 0.249   25.237   1.00 86.79  ? 228  ALA B N   1 
ATOM   5480  C  CA  . ALA B  2 118 ? -21.283 0.968   25.131   1.00 115.31 ? 228  ALA B CA  1 
ATOM   5481  C  C   . ALA B  2 118 ? -22.130 0.808   26.392   1.00 100.08 ? 228  ALA B C   1 
ATOM   5482  O  O   . ALA B  2 118 ? -22.818 1.747   26.812   1.00 104.03 ? 228  ALA B O   1 
ATOM   5483  C  CB  . ALA B  2 118 ? -22.044 0.478   23.901   1.00 131.12 ? 228  ALA B CB  1 
ATOM   5484  N  N   . ILE B  2 119 ? -22.125 -0.384  26.984   1.00 94.05  ? 229  ILE B N   1 
ATOM   5485  C  CA  . ILE B  2 119 ? -22.864 -0.595  28.220   1.00 89.43  ? 229  ILE B CA  1 
ATOM   5486  C  C   . ILE B  2 119 ? -22.294 0.293   29.321   1.00 88.10  ? 229  ILE B C   1 
ATOM   5487  O  O   . ILE B  2 119 ? -23.037 0.969   30.043   1.00 99.15  ? 229  ILE B O   1 
ATOM   5488  C  CB  . ILE B  2 119 ? -22.811 -2.088  28.595   1.00 84.70  ? 229  ILE B CB  1 
ATOM   5489  C  CG1 . ILE B  2 119 ? -23.395 -2.942  27.478   1.00 86.76  ? 229  ILE B CG1 1 
ATOM   5490  C  CG2 . ILE B  2 119 ? -23.543 -2.371  29.881   1.00 85.37  ? 229  ILE B CG2 1 
ATOM   5491  C  CD1 . ILE B  2 119 ? -23.341 -4.407  27.803   1.00 83.98  ? 229  ILE B CD1 1 
ATOM   5492  N  N   . MET B  2 120 ? -20.960 0.365   29.408   1.00 83.27  ? 230  MET B N   1 
ATOM   5493  C  CA  . MET B  2 120 ? -20.289 1.138   30.455   1.00 82.56  ? 230  MET B CA  1 
ATOM   5494  C  C   . MET B  2 120 ? -20.528 2.641   30.301   1.00 87.84  ? 230  MET B C   1 
ATOM   5495  O  O   . MET B  2 120 ? -20.727 3.351   31.295   1.00 90.97  ? 230  MET B O   1 
ATOM   5496  C  CB  . MET B  2 120 ? -18.791 0.821   30.437   1.00 106.58 ? 230  MET B CB  1 
ATOM   5497  C  CG  . MET B  2 120 ? -17.933 1.624   31.406   1.00 106.23 ? 230  MET B CG  1 
ATOM   5498  S  SD  . MET B  2 120 ? -18.304 1.387   33.146   1.00 81.26  ? 230  MET B SD  1 
ATOM   5499  C  CE  . MET B  2 120 ? -17.650 -0.249  33.422   1.00 75.29  ? 230  MET B CE  1 
ATOM   5500  N  N   . GLN B  2 121 ? -20.445 3.162   29.076   1.00 90.98  ? 231  GLN B N   1 
ATOM   5501  C  CA  . GLN B  2 121 ? -20.633 4.597   28.899   1.00 97.02  ? 231  GLN B CA  1 
ATOM   5502  C  C   . GLN B  2 121 ? -22.079 5.001   29.114   1.00 103.27 ? 231  GLN B C   1 
ATOM   5503  O  O   . GLN B  2 121 ? -22.347 6.054   29.703   1.00 107.43 ? 231  GLN B O   1 
ATOM   5504  C  CB  . GLN B  2 121 ? -20.140 5.043   27.525   1.00 123.79 ? 231  GLN B CB  1 
ATOM   5505  C  CG  . GLN B  2 121 ? -18.642 4.927   27.385   1.00 115.19 ? 231  GLN B CG  1 
ATOM   5506  C  CD  . GLN B  2 121 ? -17.934 5.687   28.491   1.00 93.92  ? 231  GLN B CD  1 
ATOM   5507  O  OE1 . GLN B  2 121 ? -18.240 6.853   28.757   1.00 99.05  ? 231  GLN B OE1 1 
ATOM   5508  N  NE2 . GLN B  2 121 ? -16.989 5.023   29.151   1.00 110.69 ? 231  GLN B NE2 1 
ATOM   5509  N  N   . ALA B  2 122 ? -23.022 4.161   28.677   1.00 126.68 ? 232  ALA B N   1 
ATOM   5510  C  CA  . ALA B  2 122 ? -24.436 4.477   28.849   1.00 111.23 ? 232  ALA B CA  1 
ATOM   5511  C  C   . ALA B  2 122 ? -24.843 4.360   30.303   1.00 110.52 ? 232  ALA B C   1 
ATOM   5512  O  O   . ALA B  2 122 ? -25.755 5.060   30.748   1.00 116.61 ? 232  ALA B O   1 
ATOM   5513  C  CB  . ALA B  2 122 ? -25.294 3.555   27.985   1.00 113.23 ? 232  ALA B CB  1 
ATOM   5514  N  N   . ALA B  2 123 ? -24.135 3.529   31.063   1.00 107.80 ? 233  ALA B N   1 
ATOM   5515  C  CA  . ALA B  2 123 ? -24.443 3.333   32.471   1.00 108.02 ? 233  ALA B CA  1 
ATOM   5516  C  C   . ALA B  2 123 ? -23.954 4.501   33.316   1.00 110.38 ? 233  ALA B C   1 
ATOM   5517  O  O   . ALA B  2 123 ? -24.734 5.113   34.054   1.00 115.64 ? 233  ALA B O   1 
ATOM   5518  C  CB  . ALA B  2 123 ? -23.805 2.031   32.963   1.00 103.00 ? 233  ALA B CB  1 
ATOM   5519  N  N   . VAL B  2 124 ? -22.668 4.840   33.202   1.00 126.16 ? 234  VAL B N   1 
ATOM   5520  C  CA  . VAL B  2 124 ? -22.073 5.825   34.099   1.00 127.59 ? 234  VAL B CA  1 
ATOM   5521  C  C   . VAL B  2 124 ? -22.576 7.228   33.788   1.00 110.47 ? 234  VAL B C   1 
ATOM   5522  O  O   . VAL B  2 124 ? -22.844 8.021   34.700   1.00 114.79 ? 234  VAL B O   1 
ATOM   5523  C  CB  . VAL B  2 124 ? -20.543 5.741   34.023   1.00 100.86 ? 234  VAL B CB  1 
ATOM   5524  C  CG1 . VAL B  2 124 ? -19.922 6.670   35.054   1.00 167.73 ? 234  VAL B CG1 1 
ATOM   5525  C  CG2 . VAL B  2 124 ? -20.092 4.315   34.232   1.00 95.58  ? 234  VAL B CG2 1 
ATOM   5526  N  N   . CYS B  2 125 ? -22.683 7.570   32.503   1.00 111.40 ? 235  CYS B N   1 
ATOM   5527  C  CA  . CYS B  2 125 ? -23.130 8.904   32.114   1.00 124.36 ? 235  CYS B CA  1 
ATOM   5528  C  C   . CYS B  2 125 ? -24.581 9.137   32.510   1.00 125.55 ? 235  CYS B C   1 
ATOM   5529  O  O   . CYS B  2 125 ? -25.492 8.934   31.701   1.00 129.53 ? 235  CYS B O   1 
ATOM   5530  C  CB  . CYS B  2 125 ? -22.962 9.123   30.604   1.00 137.52 ? 235  CYS B CB  1 
ATOM   5531  S  SG  . CYS B  2 125 ? -21.260 9.039   29.970   1.00 115.65 ? 235  CYS B SG  1 
ATOM   5532  N  N   . LYS B  2 126 ? -24.805 9.593   33.741   1.00 128.70 ? 236  LYS B N   1 
ATOM   5533  C  CA  . LYS B  2 126 ? -26.155 9.916   34.178   1.00 156.49 ? 236  LYS B CA  1 
ATOM   5534  C  C   . LYS B  2 126 ? -26.618 11.255  33.640   1.00 143.00 ? 236  LYS B C   1 
ATOM   5535  O  O   . LYS B  2 126 ? -27.788 11.609  33.814   1.00 150.16 ? 236  LYS B O   1 
ATOM   5536  C  CB  . LYS B  2 126 ? -26.230 9.942   35.708   1.00 165.10 ? 236  LYS B CB  1 
ATOM   5537  C  CG  . LYS B  2 126 ? -26.101 8.594   36.394   1.00 129.05 ? 236  LYS B CG  1 
ATOM   5538  C  CD  . LYS B  2 126 ? -26.120 8.760   37.911   1.00 131.79 ? 236  LYS B CD  1 
ATOM   5539  C  CE  . LYS B  2 126 ? -26.080 7.416   38.625   1.00 129.00 ? 236  LYS B CE  1 
ATOM   5540  N  NZ  . LYS B  2 126 ? -26.041 7.550   40.113   1.00 131.60 ? 236  LYS B NZ  1 
ATOM   5541  N  N   . GLU B  2 127 ? -25.730 12.000  32.991   1.00 143.03 ? 237  GLU B N   1 
ATOM   5542  C  CA  . GLU B  2 127 ? -26.030 13.338  32.509   1.00 179.20 ? 237  GLU B CA  1 
ATOM   5543  C  C   . GLU B  2 127 ? -26.236 13.356  31.001   1.00 187.43 ? 237  GLU B C   1 
ATOM   5544  O  O   . GLU B  2 127 ? -27.305 13.754  30.526   1.00 211.94 ? 237  GLU B O   1 
ATOM   5545  C  CB  . GLU B  2 127 ? -24.901 14.299  32.912   1.00 201.47 ? 237  GLU B CB  1 
ATOM   5546  C  CG  . GLU B  2 127 ? -24.579 14.307  34.404   1.00 190.39 ? 237  GLU B CG  1 
ATOM   5547  C  CD  . GLU B  2 127 ? -23.292 15.049  34.725   1.00 196.52 ? 237  GLU B CD  1 
ATOM   5548  O  OE1 . GLU B  2 127 ? -22.972 15.196  35.925   1.00 202.69 ? 237  GLU B OE1 1 
ATOM   5549  O  OE2 . GLU B  2 127 ? -22.607 15.498  33.781   1.00 182.83 ? 237  GLU B OE2 1 
ATOM   5550  N  N   . LYS B  2 128 ? -25.232 12.927  30.230   1.00 171.11 ? 238  LYS B N   1 
ATOM   5551  C  CA  . LYS B  2 128 ? -25.343 12.946  28.778   1.00 151.99 ? 238  LYS B CA  1 
ATOM   5552  C  C   . LYS B  2 128 ? -26.336 11.912  28.281   1.00 161.11 ? 238  LYS B C   1 
ATOM   5553  O  O   . LYS B  2 128 ? -26.808 12.015  27.146   1.00 181.41 ? 238  LYS B O   1 
ATOM   5554  C  CB  . LYS B  2 128 ? -23.972 12.725  28.144   1.00 146.30 ? 238  LYS B CB  1 
ATOM   5555  C  CG  . LYS B  2 128 ? -22.896 13.627  28.730   1.00 157.54 ? 238  LYS B CG  1 
ATOM   5556  C  CD  . LYS B  2 128 ? -21.622 13.610  27.907   1.00 169.17 ? 238  LYS B CD  1 
ATOM   5557  C  CE  . LYS B  2 128 ? -21.812 14.327  26.586   1.00 154.83 ? 238  LYS B CE  1 
ATOM   5558  N  NZ  . LYS B  2 128 ? -20.527 14.439  25.851   1.00 147.98 ? 238  LYS B NZ  1 
ATOM   5559  N  N   . ILE B  2 129 ? -26.652 10.915  29.100   1.00 147.43 ? 239  ILE B N   1 
ATOM   5560  C  CA  . ILE B  2 129 ? -27.752 10.007  28.800   1.00 149.23 ? 239  ILE B CA  1 
ATOM   5561  C  C   . ILE B  2 129 ? -29.026 10.470  29.481   1.00 156.85 ? 239  ILE B C   1 
ATOM   5562  O  O   . ILE B  2 129 ? -30.104 10.438  28.884   1.00 174.19 ? 239  ILE B O   1 
ATOM   5563  C  CB  . ILE B  2 129 ? -27.390 8.565   29.195   1.00 140.48 ? 239  ILE B CB  1 
ATOM   5564  C  CG1 . ILE B  2 129 ? -26.641 7.872   28.057   1.00 135.83 ? 239  ILE B CG1 1 
ATOM   5565  C  CG2 . ILE B  2 129 ? -28.633 7.793   29.593   1.00 143.13 ? 239  ILE B CG2 1 
ATOM   5566  C  CD1 . ILE B  2 129 ? -25.245 8.378   27.859   1.00 131.82 ? 239  ILE B CD1 1 
ATOM   5567  N  N   . GLY B  2 130 ? -28.917 10.919  30.727   1.00 156.39 ? 240  GLY B N   1 
ATOM   5568  C  CA  . GLY B  2 130 ? -30.051 11.497  31.417   1.00 165.50 ? 240  GLY B CA  1 
ATOM   5569  C  C   . GLY B  2 130 ? -30.896 10.468  32.133   1.00 163.70 ? 240  GLY B C   1 
ATOM   5570  O  O   . GLY B  2 130 ? -32.066 10.273  31.798   1.00 170.33 ? 240  GLY B O   1 
ATOM   5571  N  N   . TRP B  2 131 ? -30.313 9.797   33.119   1.00 156.35 ? 241  TRP B N   1 
ATOM   5572  C  CA  . TRP B  2 131 ? -31.063 8.834   33.905   1.00 156.05 ? 241  TRP B CA  1 
ATOM   5573  C  C   . TRP B  2 131 ? -31.908 9.537   34.954   1.00 176.87 ? 241  TRP B C   1 
ATOM   5574  O  O   . TRP B  2 131 ? -31.437 10.442  35.650   1.00 163.79 ? 241  TRP B O   1 
ATOM   5575  C  CB  . TRP B  2 131 ? -30.128 7.836   34.577   1.00 151.48 ? 241  TRP B CB  1 
ATOM   5576  C  CG  . TRP B  2 131 ? -29.428 6.952   33.611   1.00 154.11 ? 241  TRP B CG  1 
ATOM   5577  C  CD1 . TRP B  2 131 ? -28.127 7.024   33.227   1.00 133.04 ? 241  TRP B CD1 1 
ATOM   5578  C  CD2 . TRP B  2 131 ? -30.011 5.868   32.875   1.00 182.93 ? 241  TRP B CD2 1 
ATOM   5579  N  NE1 . TRP B  2 131 ? -27.853 6.039   32.311   1.00 128.77 ? 241  TRP B NE1 1 
ATOM   5580  C  CE2 . TRP B  2 131 ? -28.993 5.315   32.076   1.00 132.50 ? 241  TRP B CE2 1 
ATOM   5581  C  CE3 . TRP B  2 131 ? -31.296 5.307   32.820   1.00 145.16 ? 241  TRP B CE3 1 
ATOM   5582  C  CZ2 . TRP B  2 131 ? -29.214 4.226   31.231   1.00 130.90 ? 241  TRP B CZ2 1 
ATOM   5583  C  CZ3 . TRP B  2 131 ? -31.514 4.231   31.981   1.00 143.70 ? 241  TRP B CZ3 1 
ATOM   5584  C  CH2 . TRP B  2 131 ? -30.475 3.701   31.196   1.00 136.51 ? 241  TRP B CH2 1 
ATOM   5585  N  N   . ARG B  2 132 ? -33.159 9.096   35.074   1.00 196.12 ? 242  ARG B N   1 
ATOM   5586  C  CA  . ARG B  2 132 ? -34.072 9.666   36.049   1.00 177.14 ? 242  ARG B CA  1 
ATOM   5587  C  C   . ARG B  2 132 ? -33.591 9.358   37.463   1.00 172.21 ? 242  ARG B C   1 
ATOM   5588  O  O   . ARG B  2 132 ? -32.832 8.417   37.704   1.00 163.54 ? 242  ARG B O   1 
ATOM   5589  C  CB  . ARG B  2 132 ? -35.475 9.108   35.847   1.00 184.74 ? 242  ARG B CB  1 
ATOM   5590  C  CG  . ARG B  2 132 ? -36.347 9.907   34.903   1.00 196.20 ? 242  ARG B CG  1 
ATOM   5591  C  CD  . ARG B  2 132 ? -37.694 9.223   34.746   1.00 214.01 ? 242  ARG B CD  1 
ATOM   5592  N  NE  . ARG B  2 132 ? -38.564 9.930   33.818   1.00 213.41 ? 242  ARG B NE  1 
ATOM   5593  C  CZ  . ARG B  2 132 ? -39.521 9.344   33.108   1.00 218.88 ? 242  ARG B CZ  1 
ATOM   5594  N  NH1 . ARG B  2 132 ? -39.730 8.039   33.218   1.00 215.52 ? 242  ARG B NH1 1 
ATOM   5595  N  NH2 . ARG B  2 132 ? -40.263 10.063  32.280   1.00 228.87 ? 242  ARG B NH2 1 
ATOM   5596  N  N   . ASN B  2 133 ? -34.085 10.149  38.412   1.00 185.44 ? 243  ASN B N   1 
ATOM   5597  C  CA  . ASN B  2 133 ? -33.682 9.991   39.806   1.00 182.96 ? 243  ASN B CA  1 
ATOM   5598  C  C   . ASN B  2 133 ? -34.227 8.693   40.390   1.00 177.53 ? 243  ASN B C   1 
ATOM   5599  O  O   . ASN B  2 133 ? -33.467 7.826   40.834   1.00 171.96 ? 243  ASN B O   1 
ATOM   5600  C  CB  . ASN B  2 133 ? -34.135 11.217  40.600   1.00 187.07 ? 243  ASN B CB  1 
ATOM   5601  C  CG  . ASN B  2 133 ? -33.145 12.361  40.485   1.00 190.83 ? 243  ASN B CG  1 
ATOM   5602  O  OD1 . ASN B  2 133 ? -32.039 12.175  39.979   1.00 177.69 ? 243  ASN B OD1 1 
ATOM   5603  N  ND2 . ASN B  2 133 ? -33.537 13.551  40.917   1.00 214.77 ? 243  ASN B ND2 1 
ATOM   5604  N  N   . ASP B  2 134 ? -35.546 8.538   40.401   1.00 195.63 ? 244  ASP B N   1 
ATOM   5605  C  CA  . ASP B  2 134 ? -36.190 7.345   40.943   1.00 210.01 ? 244  ASP B CA  1 
ATOM   5606  C  C   . ASP B  2 134 ? -37.009 6.714   39.823   1.00 195.59 ? 244  ASP B C   1 
ATOM   5607  O  O   . ASP B  2 134 ? -38.185 7.035   39.635   1.00 205.63 ? 244  ASP B O   1 
ATOM   5608  C  CB  . ASP B  2 134 ? -37.039 7.687   42.157   1.00 218.38 ? 244  ASP B CB  1 
ATOM   5609  C  CG  . ASP B  2 134 ? -36.270 8.483   43.193   1.00 247.92 ? 244  ASP B CG  1 
ATOM   5610  O  OD1 . ASP B  2 134 ? -36.255 9.729   43.098   1.00 272.99 ? 244  ASP B OD1 1 
ATOM   5611  O  OD2 . ASP B  2 134 ? -35.666 7.862   44.094   1.00 242.71 ? 244  ASP B OD2 1 
ATOM   5612  N  N   . SER B  2 135 ? -36.372 5.833   39.057   1.00 200.99 ? 245  SER B N   1 
ATOM   5613  C  CA  . SER B  2 135 ? -37.053 5.133   37.980   1.00 195.78 ? 245  SER B CA  1 
ATOM   5614  C  C   . SER B  2 135 ? -36.342 3.814   37.721   1.00 198.16 ? 245  SER B C   1 
ATOM   5615  O  O   . SER B  2 135 ? -35.311 3.504   38.323   1.00 183.96 ? 245  SER B O   1 
ATOM   5616  C  CB  . SER B  2 135 ? -37.108 5.967   36.700   1.00 189.28 ? 245  SER B CB  1 
ATOM   5617  O  OG  . SER B  2 135 ? -35.830 6.046   36.099   1.00 180.19 ? 245  SER B OG  1 
ATOM   5618  N  N   . LEU B  2 136 ? -36.921 3.034   36.816   1.00 198.82 ? 246  LEU B N   1 
ATOM   5619  C  CA  . LEU B  2 136 ? -36.365 1.749   36.401   1.00 168.98 ? 246  LEU B CA  1 
ATOM   5620  C  C   . LEU B  2 136 ? -35.435 2.001   35.220   1.00 161.50 ? 246  LEU B C   1 
ATOM   5621  O  O   . LEU B  2 136 ? -35.888 2.216   34.094   1.00 165.67 ? 246  LEU B O   1 
ATOM   5622  C  CB  . LEU B  2 136 ? -37.484 0.781   36.041   1.00 178.91 ? 246  LEU B CB  1 
ATOM   5623  C  CG  . LEU B  2 136 ? -38.506 0.518   37.149   1.00 183.99 ? 246  LEU B CG  1 
ATOM   5624  C  CD1 . LEU B  2 136 ? -39.524 -0.520  36.702   1.00 191.96 ? 246  LEU B CD1 1 
ATOM   5625  C  CD2 . LEU B  2 136 ? -37.809 0.081   38.429   1.00 195.69 ? 246  LEU B CD2 1 
ATOM   5626  N  N   . HIS B  2 137 ? -34.129 2.008   35.481   1.00 159.71 ? 247  HIS B N   1 
ATOM   5627  C  CA  . HIS B  2 137 ? -33.117 2.248   34.449   1.00 178.74 ? 247  HIS B CA  1 
ATOM   5628  C  C   . HIS B  2 137 ? -32.875 0.956   33.674   1.00 174.47 ? 247  HIS B C   1 
ATOM   5629  O  O   . HIS B  2 137 ? -32.042 0.128   34.045   1.00 163.89 ? 247  HIS B O   1 
ATOM   5630  C  CB  . HIS B  2 137 ? -31.833 2.760   35.081   1.00 140.18 ? 247  HIS B CB  1 
ATOM   5631  C  CG  . HIS B  2 137 ? -32.039 3.919   36.000   1.00 144.76 ? 247  HIS B CG  1 
ATOM   5632  N  ND1 . HIS B  2 137 ? -31.254 4.137   37.112   1.00 164.95 ? 247  HIS B ND1 1 
ATOM   5633  C  CD2 . HIS B  2 137 ? -32.939 4.929   35.971   1.00 152.27 ? 247  HIS B CD2 1 
ATOM   5634  C  CE1 . HIS B  2 137 ? -31.665 5.229   37.732   1.00 185.76 ? 247  HIS B CE1 1 
ATOM   5635  N  NE2 . HIS B  2 137 ? -32.687 5.728   37.060   1.00 188.18 ? 247  HIS B NE2 1 
ATOM   5636  N  N   . LEU B  2 138 ? -33.585 0.797   32.559   1.00 180.32 ? 248  LEU B N   1 
ATOM   5637  C  CA  . LEU B  2 138 ? -33.517 -0.412  31.744   1.00 152.92 ? 248  LEU B CA  1 
ATOM   5638  C  C   . LEU B  2 138 ? -32.691 -0.158  30.489   1.00 142.62 ? 248  LEU B C   1 
ATOM   5639  O  O   . LEU B  2 138 ? -32.911 0.834   29.787   1.00 158.76 ? 248  LEU B O   1 
ATOM   5640  C  CB  . LEU B  2 138 ? -34.921 -0.877  31.359   1.00 167.80 ? 248  LEU B CB  1 
ATOM   5641  C  CG  . LEU B  2 138 ? -35.978 -0.959  32.461   1.00 180.04 ? 248  LEU B CG  1 
ATOM   5642  C  CD1 . LEU B  2 138 ? -37.284 -1.466  31.881   1.00 171.56 ? 248  LEU B CD1 1 
ATOM   5643  C  CD2 . LEU B  2 138 ? -35.511 -1.853  33.598   1.00 170.27 ? 248  LEU B CD2 1 
ATOM   5644  N  N   . LEU B  2 139 ? -31.761 -1.071  30.197   1.00 132.20 ? 249  LEU B N   1 
ATOM   5645  C  CA  . LEU B  2 139 ? -30.821 -0.928  29.080   1.00 141.07 ? 249  LEU B CA  1 
ATOM   5646  C  C   . LEU B  2 139 ? -30.883 -2.174  28.200   1.00 126.83 ? 249  LEU B C   1 
ATOM   5647  O  O   . LEU B  2 139 ? -30.318 -3.214  28.548   1.00 120.50 ? 249  LEU B O   1 
ATOM   5648  C  CB  . LEU B  2 139 ? -29.407 -0.679  29.595   1.00 119.52 ? 249  LEU B CB  1 
ATOM   5649  C  CG  . LEU B  2 139 ? -28.472 0.236   28.806   1.00 117.77 ? 249  LEU B CG  1 
ATOM   5650  C  CD1 . LEU B  2 139 ? -27.298 0.580   29.691   1.00 126.67 ? 249  LEU B CD1 1 
ATOM   5651  C  CD2 . LEU B  2 139 ? -28.008 -0.431  27.527   1.00 115.45 ? 249  LEU B CD2 1 
ATOM   5652  N  N   . VAL B  2 140 ? -31.589 -2.074  27.077   1.00 133.43 ? 250  VAL B N   1 
ATOM   5653  C  CA  . VAL B  2 140 ? -31.699 -3.180  26.131   1.00 133.43 ? 250  VAL B CA  1 
ATOM   5654  C  C   . VAL B  2 140 ? -30.420 -3.278  25.308   1.00 126.72 ? 250  VAL B C   1 
ATOM   5655  O  O   . VAL B  2 140 ? -30.058 -2.338  24.592   1.00 128.17 ? 250  VAL B O   1 
ATOM   5656  C  CB  . VAL B  2 140 ? -32.927 -3.006  25.227   1.00 143.83 ? 250  VAL B CB  1 
ATOM   5657  C  CG1 . VAL B  2 140 ? -32.842 -3.927  24.022   1.00 143.96 ? 250  VAL B CG1 1 
ATOM   5658  C  CG2 . VAL B  2 140 ? -34.191 -3.287  26.020   1.00 150.52 ? 250  VAL B CG2 1 
ATOM   5659  N  N   . PHE B  2 141 ? -29.754 -4.431  25.385   1.00 120.07 ? 251  PHE B N   1 
ATOM   5660  C  CA  . PHE B  2 141 ? -28.510 -4.694  24.667   1.00 157.97 ? 251  PHE B CA  1 
ATOM   5661  C  C   . PHE B  2 141 ? -28.766 -5.708  23.559   1.00 115.68 ? 251  PHE B C   1 
ATOM   5662  O  O   . PHE B  2 141 ? -29.170 -6.842  23.834   1.00 115.46 ? 251  PHE B O   1 
ATOM   5663  C  CB  . PHE B  2 141 ? -27.429 -5.213  25.617   1.00 155.07 ? 251  PHE B CB  1 
ATOM   5664  C  CG  . PHE B  2 141 ? -26.141 -5.552  24.931   1.00 122.55 ? 251  PHE B CG  1 
ATOM   5665  C  CD1 . PHE B  2 141 ? -25.247 -4.555  24.574   1.00 96.98  ? 251  PHE B CD1 1 
ATOM   5666  C  CD2 . PHE B  2 141 ? -25.831 -6.868  24.624   1.00 112.99 ? 251  PHE B CD2 1 
ATOM   5667  C  CE1 . PHE B  2 141 ? -24.064 -4.862  23.930   1.00 92.17  ? 251  PHE B CE1 1 
ATOM   5668  C  CE2 . PHE B  2 141 ? -24.652 -7.182  23.980   1.00 111.47 ? 251  PHE B CE2 1 
ATOM   5669  C  CZ  . PHE B  2 141 ? -23.766 -6.176  23.630   1.00 88.86  ? 251  PHE B CZ  1 
ATOM   5670  N  N   . VAL B  2 142 ? -28.481 -5.316  22.317   1.00 117.77 ? 252  VAL B N   1 
ATOM   5671  C  CA  . VAL B  2 142 ? -28.739 -6.138  21.137   1.00 120.80 ? 252  VAL B CA  1 
ATOM   5672  C  C   . VAL B  2 142 ? -27.440 -6.294  20.357   1.00 115.30 ? 252  VAL B C   1 
ATOM   5673  O  O   . VAL B  2 142 ? -26.827 -5.292  19.967   1.00 115.08 ? 252  VAL B O   1 
ATOM   5674  C  CB  . VAL B  2 142 ? -29.823 -5.532  20.229   1.00 130.99 ? 252  VAL B CB  1 
ATOM   5675  C  CG1 . VAL B  2 142 ? -29.922 -6.334  18.955   1.00 133.93 ? 252  VAL B CG1 1 
ATOM   5676  C  CG2 . VAL B  2 142 ? -31.167 -5.477  20.935   1.00 137.56 ? 252  VAL B CG2 1 
ATOM   5677  N  N   . SER B  2 143 ? -27.025 -7.542  20.129   1.00 111.48 ? 253  SER B N   1 
ATOM   5678  C  CA  . SER B  2 143 ? -25.902 -7.869  19.255   1.00 107.54 ? 253  SER B CA  1 
ATOM   5679  C  C   . SER B  2 143 ? -25.999 -9.344  18.898   1.00 106.85 ? 253  SER B C   1 
ATOM   5680  O  O   . SER B  2 143 ? -26.412 -10.161 19.722   1.00 107.47 ? 253  SER B O   1 
ATOM   5681  C  CB  . SER B  2 143 ? -24.545 -7.577  19.910   1.00 99.40  ? 253  SER B CB  1 
ATOM   5682  O  OG  . SER B  2 143 ? -24.297 -8.452  20.997   1.00 141.49 ? 253  SER B OG  1 
ATOM   5683  N  N   . ASP B  2 144 ? -25.592 -9.689  17.674   1.00 108.08 ? 254  ASP B N   1 
ATOM   5684  C  CA  . ASP B  2 144 ? -25.693 -11.069 17.210   1.00 128.02 ? 254  ASP B CA  1 
ATOM   5685  C  C   . ASP B  2 144 ? -24.359 -11.801 17.294   1.00 140.37 ? 254  ASP B C   1 
ATOM   5686  O  O   . ASP B  2 144 ? -24.126 -12.763 16.551   1.00 164.33 ? 254  ASP B O   1 
ATOM   5687  C  CB  . ASP B  2 144 ? -26.245 -11.127 15.786   1.00 119.69 ? 254  ASP B CB  1 
ATOM   5688  C  CG  . ASP B  2 144 ? -25.257 -10.637 14.752   1.00 121.75 ? 254  ASP B CG  1 
ATOM   5689  O  OD1 . ASP B  2 144 ? -24.376 -9.819  15.107   1.00 116.81 ? 254  ASP B OD1 1 
ATOM   5690  O  OD2 . ASP B  2 144 ? -25.372 -11.076 13.581   1.00 128.82 ? 254  ASP B OD2 1 
ATOM   5691  N  N   . ALA B  2 145 ? -23.480 -11.367 18.193   1.00 97.53  ? 255  ALA B N   1 
ATOM   5692  C  CA  . ALA B  2 145 ? -22.185 -12.000 18.370   1.00 93.16  ? 255  ALA B CA  1 
ATOM   5693  C  C   . ALA B  2 145 ? -21.703 -11.769 19.801   1.00 86.95  ? 255  ALA B C   1 
ATOM   5694  O  O   . ALA B  2 145 ? -22.367 -11.116 20.613   1.00 82.76  ? 255  ALA B O   1 
ATOM   5695  C  CB  . ALA B  2 145 ? -21.176 -11.460 17.352   1.00 95.56  ? 255  ALA B CB  1 
ATOM   5696  N  N   . ASP B  2 146 ? -20.514 -12.294 20.091   1.00 81.43  ? 256  ASP B N   1 
ATOM   5697  C  CA  . ASP B  2 146 ? -19.888 -12.123 21.388   1.00 74.22  ? 256  ASP B CA  1 
ATOM   5698  C  C   . ASP B  2 146 ? -19.452 -10.668 21.553   1.00 71.85  ? 256  ASP B C   1 
ATOM   5699  O  O   . ASP B  2 146 ? -19.610 -9.833  20.659   1.00 129.74 ? 256  ASP B O   1 
ATOM   5700  C  CB  . ASP B  2 146 ? -18.701 -13.078 21.513   1.00 72.54  ? 256  ASP B CB  1 
ATOM   5701  C  CG  . ASP B  2 146 ? -18.303 -13.356 22.959   1.00 180.72 ? 256  ASP B CG  1 
ATOM   5702  O  OD1 . ASP B  2 146 ? -18.499 -12.482 23.835   1.00 142.01 ? 256  ASP B OD1 1 
ATOM   5703  O  OD2 . ASP B  2 146 ? -17.772 -14.457 23.213   1.00 152.43 ? 256  ASP B OD2 1 
ATOM   5704  N  N   . SER B  2 147 ? -18.897 -10.348 22.714   1.00 128.91 ? 257  SER B N   1 
ATOM   5705  C  CA  . SER B  2 147 ? -18.376 -9.010  22.927   1.00 64.98  ? 257  SER B CA  1 
ATOM   5706  C  C   . SER B  2 147 ? -17.086 -9.093  23.738   1.00 65.61  ? 257  SER B C   1 
ATOM   5707  O  O   . SER B  2 147 ? -16.873 -10.019 24.532   1.00 56.24  ? 257  SER B O   1 
ATOM   5708  C  CB  . SER B  2 147 ? -19.414 -8.057  23.562   1.00 68.51  ? 257  SER B CB  1 
ATOM   5709  O  OG  . SER B  2 147 ? -19.964 -8.564  24.759   1.00 67.13  ? 257  SER B OG  1 
ATOM   5710  N  N   . HIS B  2 148 ? -16.195 -8.151  23.434   1.00 112.34 ? 258  HIS B N   1 
ATOM   5711  C  CA  . HIS B  2 148 ? -14.898 -8.049  24.078   1.00 55.65  ? 258  HIS B CA  1 
ATOM   5712  C  C   . HIS B  2 148 ? -15.020 -7.484  25.476   1.00 53.61  ? 258  HIS B C   1 
ATOM   5713  O  O   . HIS B  2 148 ? -15.808 -6.571  25.733   1.00 56.69  ? 258  HIS B O   1 
ATOM   5714  C  CB  . HIS B  2 148 ? -13.975 -7.147  23.263   1.00 102.65 ? 258  HIS B CB  1 
ATOM   5715  C  CG  . HIS B  2 148 ? -13.443 -7.783  22.025   1.00 62.86  ? 258  HIS B CG  1 
ATOM   5716  N  ND1 . HIS B  2 148 ? -12.435 -8.718  22.048   1.00 63.00  ? 258  HIS B ND1 1 
ATOM   5717  C  CD2 . HIS B  2 148 ? -13.788 -7.633  20.729   1.00 68.20  ? 258  HIS B CD2 1 
ATOM   5718  C  CE1 . HIS B  2 148 ? -12.169 -9.109  20.818   1.00 67.93  ? 258  HIS B CE1 1 
ATOM   5719  N  NE2 . HIS B  2 148 ? -12.982 -8.470  19.997   1.00 124.88 ? 258  HIS B NE2 1 
ATOM   5720  N  N   . PHE B  2 149 ? -14.202 -8.014  26.373   1.00 49.44  ? 259  PHE B N   1 
ATOM   5721  C  CA  . PHE B  2 149 ? -14.079 -7.463  27.711   1.00 127.73 ? 259  PHE B CA  1 
ATOM   5722  C  C   . PHE B  2 149 ? -12.636 -7.025  27.952   1.00 144.33 ? 259  PHE B C   1 
ATOM   5723  O  O   . PHE B  2 149 ? -11.871 -6.806  26.997   1.00 48.15  ? 259  PHE B O   1 
ATOM   5724  C  CB  . PHE B  2 149 ? -14.558 -8.490  28.753   1.00 46.02  ? 259  PHE B CB  1 
ATOM   5725  C  CG  . PHE B  2 149 ? -14.049 -9.896  28.512   1.00 71.43  ? 259  PHE B CG  1 
ATOM   5726  C  CD1 . PHE B  2 149 ? -14.726 -10.774 27.668   1.00 46.68  ? 259  PHE B CD1 1 
ATOM   5727  C  CD2 . PHE B  2 149 ? -12.916 -10.353 29.166   1.00 119.93 ? 259  PHE B CD2 1 
ATOM   5728  C  CE1 . PHE B  2 149 ? -14.254 -12.064 27.453   1.00 48.75  ? 259  PHE B CE1 1 
ATOM   5729  C  CE2 . PHE B  2 149 ? -12.451 -11.637 28.960   1.00 174.32 ? 259  PHE B CE2 1 
ATOM   5730  C  CZ  . PHE B  2 149 ? -13.119 -12.495 28.099   1.00 148.41 ? 259  PHE B CZ  1 
ATOM   5731  N  N   . GLY B  2 150 ? -12.278 -6.851  29.222   1.00 166.79 ? 260  GLY B N   1 
ATOM   5732  C  CA  . GLY B  2 150 ? -10.978 -6.365  29.623   1.00 46.70  ? 260  GLY B CA  1 
ATOM   5733  C  C   . GLY B  2 150 ? -9.835  -7.153  29.026   1.00 46.98  ? 260  GLY B C   1 
ATOM   5734  O  O   . GLY B  2 150 ? -9.978  -8.340  28.711   1.00 46.72  ? 260  GLY B O   1 
ATOM   5735  N  N   . MET B  2 151 ? -8.698  -6.481  28.842   1.00 51.05  ? 261  MET B N   1 
ATOM   5736  C  CA  . MET B  2 151 ? -7.400  -7.039  28.475   1.00 52.81  ? 261  MET B CA  1 
ATOM   5737  C  C   . MET B  2 151 ? -7.408  -7.630  27.083   1.00 117.05 ? 261  MET B C   1 
ATOM   5738  O  O   . MET B  2 151 ? -6.347  -8.044  26.582   1.00 143.57 ? 261  MET B O   1 
ATOM   5739  C  CB  . MET B  2 151 ? -6.918  -8.083  29.487   1.00 58.58  ? 261  MET B CB  1 
ATOM   5740  C  CG  . MET B  2 151 ? -6.549  -7.469  30.826   1.00 51.82  ? 261  MET B CG  1 
ATOM   5741  S  SD  . MET B  2 151 ? -6.653  -8.716  32.093   1.00 50.51  ? 261  MET B SD  1 
ATOM   5742  C  CE  . MET B  2 151 ? -5.443  -8.108  33.260   1.00 172.58 ? 261  MET B CE  1 
ATOM   5743  N  N   . ASP B  2 152 ? -8.564  -7.651  26.421   1.00 113.21 ? 262  ASP B N   1 
ATOM   5744  C  CA  . ASP B  2 152 ? -8.629  -8.058  25.031   1.00 55.59  ? 262  ASP B CA  1 
ATOM   5745  C  C   . ASP B  2 152 ? -8.017  -6.997  24.140   1.00 58.58  ? 262  ASP B C   1 
ATOM   5746  O  O   . ASP B  2 152 ? -7.557  -7.309  23.039   1.00 62.28  ? 262  ASP B O   1 
ATOM   5747  C  CB  . ASP B  2 152 ? -10.089 -8.295  24.618   1.00 55.35  ? 262  ASP B CB  1 
ATOM   5748  C  CG  . ASP B  2 152 ? -10.642 -9.627  25.086   1.00 54.30  ? 262  ASP B CG  1 
ATOM   5749  O  OD1 . ASP B  2 152 ? -9.879  -10.604 25.201   1.00 55.33  ? 262  ASP B OD1 1 
ATOM   5750  O  OD2 . ASP B  2 152 ? -11.865 -9.693  25.297   1.00 53.01  ? 262  ASP B OD2 1 
ATOM   5751  N  N   . SER B  2 153 ? -7.959  -5.763  24.627   1.00 62.56  ? 263  SER B N   1 
ATOM   5752  C  CA  . SER B  2 153 ? -7.373  -4.647  23.909   1.00 160.23 ? 263  SER B CA  1 
ATOM   5753  C  C   . SER B  2 153 ? -5.853  -4.646  23.982   1.00 220.89 ? 263  SER B C   1 
ATOM   5754  O  O   . SER B  2 153 ? -5.207  -3.870  23.259   1.00 71.97  ? 263  SER B O   1 
ATOM   5755  C  CB  . SER B  2 153 ? -7.956  -3.353  24.484   1.00 65.49  ? 263  SER B CB  1 
ATOM   5756  O  OG  . SER B  2 153 ? -7.804  -3.335  25.895   1.00 63.23  ? 263  SER B OG  1 
ATOM   5757  N  N   . LYS B  2 154 ? -5.275  -5.560  24.769   1.00 205.44 ? 264  LYS B N   1 
ATOM   5758  C  CA  . LYS B  2 154 ? -3.825  -5.654  24.879   1.00 166.73 ? 264  LYS B CA  1 
ATOM   5759  C  C   . LYS B  2 154 ? -3.189  -5.939  23.527   1.00 69.14  ? 264  LYS B C   1 
ATOM   5760  O  O   . LYS B  2 154 ? -2.068  -5.494  23.263   1.00 72.60  ? 264  LYS B O   1 
ATOM   5761  C  CB  . LYS B  2 154 ? -3.450  -6.743  25.884   1.00 112.78 ? 264  LYS B CB  1 
ATOM   5762  C  CG  . LYS B  2 154 ? -1.954  -6.922  26.101   1.00 120.58 ? 264  LYS B CG  1 
ATOM   5763  C  CD  . LYS B  2 154 ? -1.702  -7.929  27.213   1.00 97.49  ? 264  LYS B CD  1 
ATOM   5764  C  CE  . LYS B  2 154 ? -0.244  -8.351  27.292   1.00 67.61  ? 264  LYS B CE  1 
ATOM   5765  N  NZ  . LYS B  2 154 ? 0.623   -7.171  27.457   1.00 70.13  ? 264  LYS B NZ  1 
ATOM   5766  N  N   . LEU B  2 155 ? -3.888  -6.694  22.675   1.00 69.03  ? 265  LEU B N   1 
ATOM   5767  C  CA  . LEU B  2 155 ? -3.411  -6.953  21.324   1.00 113.45 ? 265  LEU B CA  1 
ATOM   5768  C  C   . LEU B  2 155 ? -3.336  -5.669  20.514   1.00 169.46 ? 265  LEU B C   1 
ATOM   5769  O  O   . LEU B  2 155 ? -2.432  -5.494  19.688   1.00 155.01 ? 265  LEU B O   1 
ATOM   5770  C  CB  . LEU B  2 155 ? -4.330  -7.954  20.638   1.00 108.73 ? 265  LEU B CB  1 
ATOM   5771  C  CG  . LEU B  2 155 ? -4.590  -9.208  21.457   1.00 102.11 ? 265  LEU B CG  1 
ATOM   5772  C  CD1 . LEU B  2 155 ? -5.589  -10.040 20.706   1.00 135.95 ? 265  LEU B CD1 1 
ATOM   5773  C  CD2 . LEU B  2 155 ? -3.305  -9.973  21.692   1.00 117.43 ? 265  LEU B CD2 1 
ATOM   5774  N  N   . ALA B  2 156 ? -4.284  -4.763  20.729   1.00 130.10 ? 266  ALA B N   1 
ATOM   5775  C  CA  . ALA B  2 156 ? -4.285  -3.503  20.006   1.00 137.44 ? 266  ALA B CA  1 
ATOM   5776  C  C   . ALA B  2 156 ? -3.244  -2.532  20.532   1.00 111.78 ? 266  ALA B C   1 
ATOM   5777  O  O   . ALA B  2 156 ? -2.947  -1.540  19.857   1.00 85.24  ? 266  ALA B O   1 
ATOM   5778  C  CB  . ALA B  2 156 ? -5.668  -2.861  20.087   1.00 118.04 ? 266  ALA B CB  1 
ATOM   5779  N  N   . GLY B  2 157 ? -2.689  -2.804  21.705   1.00 130.38 ? 267  GLY B N   1 
ATOM   5780  C  CA  . GLY B  2 157 ? -1.757  -1.923  22.353   1.00 132.29 ? 267  GLY B CA  1 
ATOM   5781  C  C   . GLY B  2 157 ? -2.377  -1.004  23.370   1.00 78.57  ? 267  GLY B C   1 
ATOM   5782  O  O   . GLY B  2 157 ? -1.777  0.029   23.697   1.00 82.33  ? 267  GLY B O   1 
ATOM   5783  N  N   . ILE B  2 158 ? -3.530  -1.373  23.923   1.00 95.33  ? 268  ILE B N   1 
ATOM   5784  C  CA  . ILE B  2 158 ? -4.238  -0.570  24.915   1.00 103.23 ? 268  ILE B CA  1 
ATOM   5785  C  C   . ILE B  2 158 ? -4.136  -1.322  26.231   1.00 69.15  ? 268  ILE B C   1 
ATOM   5786  O  O   . ILE B  2 158 ? -4.672  -2.428  26.376   1.00 65.05  ? 268  ILE B O   1 
ATOM   5787  C  CB  . ILE B  2 158 ? -5.697  -0.318  24.526   1.00 92.78  ? 268  ILE B CB  1 
ATOM   5788  C  CG1 . ILE B  2 158 ? -5.794  0.085   23.044   1.00 97.98  ? 268  ILE B CG1 1 
ATOM   5789  C  CG2 . ILE B  2 158 ? -6.264  0.774   25.422   1.00 72.43  ? 268  ILE B CG2 1 
ATOM   5790  C  CD1 . ILE B  2 158 ? -7.215  0.206   22.522   1.00 73.82  ? 268  ILE B CD1 1 
ATOM   5791  N  N   . VAL B  2 159 ? -3.421  -0.730  27.183   1.00 71.48  ? 269  VAL B N   1 
ATOM   5792  C  CA  . VAL B  2 159 ? -3.135  -1.351  28.467   1.00 159.55 ? 269  VAL B CA  1 
ATOM   5793  C  C   . VAL B  2 159 ? -3.624  -0.514  29.641   1.00 165.55 ? 269  VAL B C   1 
ATOM   5794  O  O   . VAL B  2 159 ? -3.508  -0.952  30.791   1.00 69.10  ? 269  VAL B O   1 
ATOM   5795  C  CB  . VAL B  2 159 ? -1.621  -1.627  28.605   1.00 106.10 ? 269  VAL B CB  1 
ATOM   5796  C  CG1 . VAL B  2 159 ? -1.173  -2.748  27.661   1.00 70.93  ? 269  VAL B CG1 1 
ATOM   5797  C  CG2 . VAL B  2 159 ? -0.850  -0.370  28.283   1.00 78.02  ? 269  VAL B CG2 1 
ATOM   5798  N  N   . CYS B  2 160 ? -4.236  0.643   29.381   1.00 160.66 ? 270  CYS B N   1 
ATOM   5799  C  CA  . CYS B  2 160 ? -4.798  1.480   30.434   1.00 75.41  ? 270  CYS B CA  1 
ATOM   5800  C  C   . CYS B  2 160 ? -6.204  0.987   30.718   1.00 71.65  ? 270  CYS B C   1 
ATOM   5801  O  O   . CYS B  2 160 ? -7.019  0.931   29.787   1.00 70.33  ? 270  CYS B O   1 
ATOM   5802  C  CB  . CYS B  2 160 ? -4.832  2.948   30.024   1.00 146.09 ? 270  CYS B CB  1 
ATOM   5803  S  SG  . CYS B  2 160 ? -3.246  3.792   29.600   1.00 238.57 ? 270  CYS B SG  1 
ATOM   5804  N  N   . PRO B  2 161 ? -6.505  0.553   31.952   1.00 148.69 ? 271  PRO B N   1 
ATOM   5805  C  CA  . PRO B  2 161 ? -7.821  -0.036  32.265   1.00 80.43  ? 271  PRO B CA  1 
ATOM   5806  C  C   . PRO B  2 161 ? -8.982  0.937   32.116   1.00 69.88  ? 271  PRO B C   1 
ATOM   5807  O  O   . PRO B  2 161 ? -8.828  2.155   32.100   1.00 74.42  ? 271  PRO B O   1 
ATOM   5808  C  CB  . PRO B  2 161 ? -7.673  -0.468  33.727   1.00 66.58  ? 271  PRO B CB  1 
ATOM   5809  C  CG  . PRO B  2 161 ? -6.190  -0.564  33.967   1.00 67.53  ? 271  PRO B CG  1 
ATOM   5810  C  CD  . PRO B  2 161 ? -5.592  0.510   33.109   1.00 103.55 ? 271  PRO B CD  1 
ATOM   5811  N  N   . ASN B  2 162 ? -10.177 0.389   32.054   1.00 67.67  ? 272  ASN B N   1 
ATOM   5812  C  CA  . ASN B  2 162 ? -11.337 1.261   31.957   1.00 128.10 ? 272  ASN B CA  1 
ATOM   5813  C  C   . ASN B  2 162 ? -11.689 1.817   33.336   1.00 159.43 ? 272  ASN B C   1 
ATOM   5814  O  O   . ASN B  2 162 ? -11.954 1.047   34.265   1.00 160.80 ? 272  ASN B O   1 
ATOM   5815  C  CB  . ASN B  2 162 ? -12.546 0.531   31.399   1.00 68.41  ? 272  ASN B CB  1 
ATOM   5816  C  CG  . ASN B  2 162 ? -13.616 1.494   30.991   1.00 72.18  ? 272  ASN B CG  1 
ATOM   5817  O  OD1 . ASN B  2 162 ? -14.348 2.003   31.831   1.00 75.35  ? 272  ASN B OD1 1 
ATOM   5818  N  ND2 . ASN B  2 162 ? -13.739 1.731   29.695   1.00 72.13  ? 272  ASN B ND2 1 
ATOM   5819  N  N   . ASP B  2 163 ? -11.703 3.146   33.476   1.00 169.51 ? 273  ASP B N   1 
ATOM   5820  C  CA  . ASP B  2 163 ? -12.064 3.734   34.761   1.00 130.54 ? 273  ASP B CA  1 
ATOM   5821  C  C   . ASP B  2 163 ? -13.561 3.672   35.038   1.00 112.38 ? 273  ASP B C   1 
ATOM   5822  O  O   . ASP B  2 163 ? -13.977 3.882   36.184   1.00 105.12 ? 273  ASP B O   1 
ATOM   5823  C  CB  . ASP B  2 163 ? -11.596 5.193   34.854   1.00 88.94  ? 273  ASP B CB  1 
ATOM   5824  C  CG  . ASP B  2 163 ? -12.012 6.019   33.657   1.00 93.60  ? 273  ASP B CG  1 
ATOM   5825  O  OD1 . ASP B  2 163 ? -12.772 5.504   32.816   1.00 88.76  ? 273  ASP B OD1 1 
ATOM   5826  O  OD2 . ASP B  2 163 ? -11.602 7.194   33.570   1.00 132.20 ? 273  ASP B OD2 1 
ATOM   5827  N  N   . GLY B  2 164 ? -14.380 3.382   34.036   1.00 82.31  ? 274  GLY B N   1 
ATOM   5828  C  CA  . GLY B  2 164 ? -15.795 3.364   34.292   1.00 112.30 ? 274  GLY B CA  1 
ATOM   5829  C  C   . GLY B  2 164 ? -16.317 4.748   34.590   1.00 124.68 ? 274  GLY B C   1 
ATOM   5830  O  O   . GLY B  2 164 ? -16.965 4.975   35.615   1.00 167.76 ? 274  GLY B O   1 
ATOM   5831  N  N   . LEU B  2 165 ? -16.000 5.693   33.719   1.00 95.11  ? 275  LEU B N   1 
ATOM   5832  C  CA  . LEU B  2 165 ? -16.442 7.063   33.874   1.00 100.80 ? 275  LEU B CA  1 
ATOM   5833  C  C   . LEU B  2 165 ? -17.097 7.515   32.577   1.00 107.39 ? 275  LEU B C   1 
ATOM   5834  O  O   . LEU B  2 165 ? -17.163 6.771   31.594   1.00 114.95 ? 275  LEU B O   1 
ATOM   5835  C  CB  . LEU B  2 165 ? -15.275 7.975   34.268   1.00 103.35 ? 275  LEU B CB  1 
ATOM   5836  C  CG  . LEU B  2 165 ? -14.657 7.658   35.629   1.00 102.96 ? 275  LEU B CG  1 
ATOM   5837  C  CD1 . LEU B  2 165 ? -13.476 8.572   35.924   1.00 106.04 ? 275  LEU B CD1 1 
ATOM   5838  C  CD2 . LEU B  2 165 ? -15.721 7.764   36.716   1.00 135.41 ? 275  LEU B CD2 1 
ATOM   5839  N  N   . CYS B  2 166 ? -17.608 8.742   32.585   1.00 130.20 ? 276  CYS B N   1 
ATOM   5840  C  CA  . CYS B  2 166 ? -18.284 9.293   31.417   1.00 148.46 ? 276  CYS B CA  1 
ATOM   5841  C  C   . CYS B  2 166 ? -17.242 9.885   30.474   1.00 129.80 ? 276  CYS B C   1 
ATOM   5842  O  O   . CYS B  2 166 ? -16.641 10.923  30.773   1.00 122.91 ? 276  CYS B O   1 
ATOM   5843  C  CB  . CYS B  2 166 ? -19.306 10.343  31.837   1.00 155.51 ? 276  CYS B CB  1 
ATOM   5844  S  SG  . CYS B  2 166 ? -20.439 10.814  30.513   1.00 192.32 ? 276  CYS B SG  1 
ATOM   5845  N  N   . HIS B  2 167 ? -17.035 9.235   29.327   1.00 105.70 ? 277  HIS B N   1 
ATOM   5846  C  CA  . HIS B  2 167 ? -16.057 9.706   28.353   1.00 123.42 ? 277  HIS B CA  1 
ATOM   5847  C  C   . HIS B  2 167 ? -16.713 9.963   27.003   1.00 120.14 ? 277  HIS B C   1 
ATOM   5848  O  O   . HIS B  2 167 ? -16.326 9.362   25.995   1.00 124.85 ? 277  HIS B O   1 
ATOM   5849  C  CB  . HIS B  2 167 ? -14.915 8.695   28.199   1.00 130.64 ? 277  HIS B CB  1 
ATOM   5850  C  CG  . HIS B  2 167 ? -14.050 8.564   29.415   1.00 142.75 ? 277  HIS B CG  1 
ATOM   5851  N  ND1 . HIS B  2 167 ? -13.242 9.586   29.870   1.00 136.49 ? 277  HIS B ND1 1 
ATOM   5852  C  CD2 . HIS B  2 167 ? -13.866 7.531   30.271   1.00 126.78 ? 277  HIS B CD2 1 
ATOM   5853  C  CE1 . HIS B  2 167 ? -12.598 9.187   30.952   1.00 127.65 ? 277  HIS B CE1 1 
ATOM   5854  N  NE2 . HIS B  2 167 ? -12.960 7.945   31.218   1.00 165.96 ? 277  HIS B NE2 1 
ATOM   5855  N  N   . LEU B  2 168 ? -17.698 10.857  26.970   1.00 119.10 ? 278  LEU B N   1 
ATOM   5856  C  CA  . LEU B  2 168 ? -18.378 11.234  25.739   1.00 125.24 ? 278  LEU B CA  1 
ATOM   5857  C  C   . LEU B  2 168 ? -17.982 12.658  25.379   1.00 164.18 ? 278  LEU B C   1 
ATOM   5858  O  O   . LEU B  2 168 ? -18.183 13.582  26.174   1.00 191.07 ? 278  LEU B O   1 
ATOM   5859  C  CB  . LEU B  2 168 ? -19.893 11.107  25.883   1.00 128.48 ? 278  LEU B CB  1 
ATOM   5860  C  CG  . LEU B  2 168 ? -20.412 9.697   26.185   1.00 136.21 ? 278  LEU B CG  1 
ATOM   5861  C  CD1 . LEU B  2 168 ? -21.922 9.713   26.370   1.00 144.36 ? 278  LEU B CD1 1 
ATOM   5862  C  CD2 . LEU B  2 168 ? -20.009 8.707   25.097   1.00 119.24 ? 278  LEU B CD2 1 
ATOM   5863  N  N   . ASP B  2 169 ? -17.403 12.824  24.189   1.00 134.79 ? 279  ASP B N   1 
ATOM   5864  C  CA  . ASP B  2 169 ? -16.921 14.121  23.729   1.00 142.01 ? 279  ASP B CA  1 
ATOM   5865  C  C   . ASP B  2 169 ? -18.056 15.010  23.235   1.00 150.93 ? 279  ASP B C   1 
ATOM   5866  O  O   . ASP B  2 169 ? -19.234 14.723  23.473   1.00 151.66 ? 279  ASP B O   1 
ATOM   5867  C  CB  . ASP B  2 169 ? -15.879 13.936  22.618   1.00 189.42 ? 279  ASP B CB  1 
ATOM   5868  C  CG  . ASP B  2 169 ? -16.338 12.977  21.520   1.00 176.38 ? 279  ASP B CG  1 
ATOM   5869  O  OD1 . ASP B  2 169 ? -17.554 12.721  21.403   1.00 142.34 ? 279  ASP B OD1 1 
ATOM   5870  O  OD2 . ASP B  2 169 ? -15.473 12.471  20.773   1.00 186.92 ? 279  ASP B OD2 1 
ATOM   5871  N  N   . SER B  2 170 ? -17.708 16.083  22.521   1.00 158.39 ? 280  SER B N   1 
ATOM   5872  C  CA  . SER B  2 170 ? -18.723 16.978  21.985   1.00 167.80 ? 280  SER B CA  1 
ATOM   5873  C  C   . SER B  2 170 ? -19.543 16.311  20.893   1.00 188.66 ? 280  SER B C   1 
ATOM   5874  O  O   . SER B  2 170 ? -20.655 16.762  20.603   1.00 211.64 ? 280  SER B O   1 
ATOM   5875  C  CB  . SER B  2 170 ? -18.065 18.249  21.451   1.00 175.73 ? 280  SER B CB  1 
ATOM   5876  O  OG  . SER B  2 170 ? -17.064 17.923  20.505   1.00 174.53 ? 280  SER B OG  1 
ATOM   5877  N  N   . LYS B  2 171 ? -19.027 15.244  20.292   1.00 189.84 ? 281  LYS B N   1 
ATOM   5878  C  CA  . LYS B  2 171 ? -19.765 14.488  19.293   1.00 165.71 ? 281  LYS B CA  1 
ATOM   5879  C  C   . LYS B  2 171 ? -20.651 13.420  19.918   1.00 160.32 ? 281  LYS B C   1 
ATOM   5880  O  O   . LYS B  2 171 ? -21.289 12.656  19.183   1.00 161.08 ? 281  LYS B O   1 
ATOM   5881  C  CB  . LYS B  2 171 ? -18.786 13.844  18.298   1.00 170.09 ? 281  LYS B CB  1 
ATOM   5882  C  CG  . LYS B  2 171 ? -17.967 14.848  17.480   1.00 184.94 ? 281  LYS B CG  1 
ATOM   5883  C  CD  . LYS B  2 171 ? -16.989 14.169  16.524   1.00 173.55 ? 281  LYS B CD  1 
ATOM   5884  C  CE  . LYS B  2 171 ? -16.192 15.199  15.726   1.00 189.62 ? 281  LYS B CE  1 
ATOM   5885  N  NZ  . LYS B  2 171 ? -15.214 14.572  14.791   1.00 185.15 ? 281  LYS B NZ  1 
ATOM   5886  N  N   . ASN B  2 172 ? -20.720 13.372  21.250   1.00 155.04 ? 282  ASN B N   1 
ATOM   5887  C  CA  . ASN B  2 172 ? -21.464 12.344  21.980   1.00 149.82 ? 282  ASN B CA  1 
ATOM   5888  C  C   . ASN B  2 172 ? -20.975 10.941  21.625   1.00 142.10 ? 282  ASN B C   1 
ATOM   5889  O  O   . ASN B  2 172 ? -21.759 9.997   21.541   1.00 140.42 ? 282  ASN B O   1 
ATOM   5890  C  CB  . ASN B  2 172 ? -22.971 12.469  21.749   1.00 156.58 ? 282  ASN B CB  1 
ATOM   5891  C  CG  . ASN B  2 172 ? -23.605 13.545  22.606   1.00 191.44 ? 282  ASN B CG  1 
ATOM   5892  O  OD1 . ASN B  2 172 ? -23.203 13.758  23.749   1.00 185.99 ? 282  ASN B OD1 1 
ATOM   5893  N  ND2 . ASN B  2 172 ? -24.614 14.219  22.064   1.00 216.37 ? 282  ASN B ND2 1 
ATOM   5894  N  N   . GLU B  2 173 ? -19.670 10.806  21.410   1.00 147.56 ? 283  GLU B N   1 
ATOM   5895  C  CA  . GLU B  2 173 ? -19.036 9.538   21.082   1.00 140.53 ? 283  GLU B CA  1 
ATOM   5896  C  C   . GLU B  2 173 ? -18.099 9.121   22.209   1.00 139.57 ? 283  GLU B C   1 
ATOM   5897  O  O   . GLU B  2 173 ? -17.719 9.928   23.058   1.00 151.51 ? 283  GLU B O   1 
ATOM   5898  C  CB  . GLU B  2 173 ? -18.247 9.641   19.769   1.00 133.41 ? 283  GLU B CB  1 
ATOM   5899  C  CG  . GLU B  2 173 ? -19.037 10.249  18.617   1.00 171.58 ? 283  GLU B CG  1 
ATOM   5900  C  CD  . GLU B  2 173 ? -18.221 10.385  17.341   1.00 184.87 ? 283  GLU B CD  1 
ATOM   5901  O  OE1 . GLU B  2 173 ? -17.175 9.711   17.229   1.00 183.59 ? 283  GLU B OE1 1 
ATOM   5902  O  OE2 . GLU B  2 173 ? -18.627 11.164  16.448   1.00 185.23 ? 283  GLU B OE2 1 
ATOM   5903  N  N   . TYR B  2 174 ? -17.735 7.840   22.216   1.00 121.60 ? 284  TYR B N   1 
ATOM   5904  C  CA  . TYR B  2 174 ? -16.730 7.357   23.155   1.00 109.21 ? 284  TYR B CA  1 
ATOM   5905  C  C   . TYR B  2 174 ? -15.351 7.854   22.738   1.00 113.38 ? 284  TYR B C   1 
ATOM   5906  O  O   . TYR B  2 174 ? -14.696 7.228   21.900   1.00 107.99 ? 284  TYR B O   1 
ATOM   5907  C  CB  . TYR B  2 174 ? -16.740 5.836   23.217   1.00 115.43 ? 284  TYR B CB  1 
ATOM   5908  C  CG  . TYR B  2 174 ? -15.981 5.254   24.379   1.00 95.66  ? 284  TYR B CG  1 
ATOM   5909  C  CD1 . TYR B  2 174 ? -15.401 6.069   25.342   1.00 95.73  ? 284  TYR B CD1 1 
ATOM   5910  C  CD2 . TYR B  2 174 ? -15.817 3.883   24.494   1.00 89.65  ? 284  TYR B CD2 1 
ATOM   5911  C  CE1 . TYR B  2 174 ? -14.702 5.529   26.394   1.00 90.08  ? 284  TYR B CE1 1 
ATOM   5912  C  CE2 . TYR B  2 174 ? -15.123 3.338   25.539   1.00 83.97  ? 284  TYR B CE2 1 
ATOM   5913  C  CZ  . TYR B  2 174 ? -14.566 4.160   26.484   1.00 84.22  ? 284  TYR B CZ  1 
ATOM   5914  O  OH  . TYR B  2 174 ? -13.872 3.592   27.520   1.00 79.08  ? 284  TYR B OH  1 
ATOM   5915  N  N   . SER B  2 175 ? -14.905 8.980   23.307   1.00 144.76 ? 285  SER B N   1 
ATOM   5916  C  CA  . SER B  2 175 ? -13.623 9.560   22.912   1.00 131.38 ? 285  SER B CA  1 
ATOM   5917  C  C   . SER B  2 175 ? -12.441 8.748   23.425   1.00 137.02 ? 285  SER B C   1 
ATOM   5918  O  O   . SER B  2 175 ? -11.393 8.699   22.766   1.00 108.39 ? 285  SER B O   1 
ATOM   5919  C  CB  . SER B  2 175 ? -13.522 11.000  23.412   1.00 151.40 ? 285  SER B CB  1 
ATOM   5920  O  OG  . SER B  2 175 ? -13.579 11.045  24.827   1.00 117.16 ? 285  SER B OG  1 
ATOM   5921  N  N   . MET B  2 176 ? -12.579 8.120   24.588   1.00 108.35 ? 286  MET B N   1 
ATOM   5922  C  CA  . MET B  2 176 ? -11.502 7.326   25.186   1.00 96.24  ? 286  MET B CA  1 
ATOM   5923  C  C   . MET B  2 176 ? -11.668 5.843   24.876   1.00 90.55  ? 286  MET B C   1 
ATOM   5924  O  O   . MET B  2 176 ? -11.421 4.988   25.723   1.00 103.84 ? 286  MET B O   1 
ATOM   5925  C  CB  . MET B  2 176 ? -11.456 7.567   26.690   1.00 94.22  ? 286  MET B CB  1 
ATOM   5926  C  CG  . MET B  2 176 ? -11.412 9.028   27.085   1.00 100.24 ? 286  MET B CG  1 
ATOM   5927  S  SD  . MET B  2 176 ? -9.879  9.843   26.606   1.00 265.47 ? 286  MET B SD  1 
ATOM   5928  C  CE  . MET B  2 176 ? -8.738  9.109   27.770   1.00 186.01 ? 286  MET B CE  1 
ATOM   5929  N  N   . SER B  2 177 ? -12.008 5.518   23.628   1.00 92.37  ? 287  SER B N   1 
ATOM   5930  C  CA  . SER B  2 177 ? -12.198 4.136   23.204   1.00 87.92  ? 287  SER B CA  1 
ATOM   5931  C  C   . SER B  2 177 ? -10.889 3.476   22.820   1.00 85.02  ? 287  SER B C   1 
ATOM   5932  O  O   . SER B  2 177 ? -10.659 2.311   23.150   1.00 139.69 ? 287  SER B O   1 
ATOM   5933  C  CB  . SER B  2 177 ? -13.154 4.076   22.010   1.00 91.92  ? 287  SER B CB  1 
ATOM   5934  O  OG  . SER B  2 177 ? -13.373 2.736   21.597   1.00 151.15 ? 287  SER B OG  1 
ATOM   5935  N  N   . THR B  2 178 ? -10.022 4.217   22.142   1.00 108.40 ? 288  THR B N   1 
ATOM   5936  C  CA  . THR B  2 178 ? -8.690  3.773   21.768   1.00 87.87  ? 288  THR B CA  1 
ATOM   5937  C  C   . THR B  2 178 ? -7.686  4.063   22.866   1.00 87.18  ? 288  THR B C   1 
ATOM   5938  O  O   . THR B  2 178 ? -6.483  3.862   22.665   1.00 86.84  ? 288  THR B O   1 
ATOM   5939  C  CB  . THR B  2 178 ? -8.253  4.457   20.472   1.00 107.67 ? 288  THR B CB  1 
ATOM   5940  O  OG1 . THR B  2 178 ? -8.013  5.846   20.727   1.00 133.38 ? 288  THR B OG1 1 
ATOM   5941  C  CG2 . THR B  2 178 ? -9.334  4.325   19.407   1.00 134.10 ? 288  THR B CG2 1 
ATOM   5942  N  N   . VAL B  2 179 ? -8.165  4.571   24.002   1.00 98.01  ? 289  VAL B N   1 
ATOM   5943  C  CA  . VAL B  2 179 ? -7.321  4.920   25.126   1.00 86.75  ? 289  VAL B CA  1 
ATOM   5944  C  C   . VAL B  2 179 ? -7.515  3.983   26.307   1.00 81.91  ? 289  VAL B C   1 
ATOM   5945  O  O   . VAL B  2 179 ? -6.562  3.752   27.060   1.00 81.98  ? 289  VAL B O   1 
ATOM   5946  C  CB  . VAL B  2 179 ? -7.575  6.379   25.552   1.00 92.33  ? 289  VAL B CB  1 
ATOM   5947  C  CG1 . VAL B  2 179 ? -6.433  6.878   26.437   1.00 134.82 ? 289  VAL B CG1 1 
ATOM   5948  C  CG2 . VAL B  2 179 ? -7.769  7.265   24.326   1.00 96.97  ? 289  VAL B CG2 1 
ATOM   5949  N  N   . LEU B  2 180 ? -8.716  3.457   26.503   1.00 78.39  ? 290  LEU B N   1 
ATOM   5950  C  CA  . LEU B  2 180 ? -9.016  2.621   27.650   1.00 76.69  ? 290  LEU B CA  1 
ATOM   5951  C  C   . LEU B  2 180 ? -9.323  1.196   27.222   1.00 76.01  ? 290  LEU B C   1 
ATOM   5952  O  O   . LEU B  2 180 ? -9.867  0.951   26.140   1.00 92.68  ? 290  LEU B O   1 
ATOM   5953  C  CB  . LEU B  2 180 ? -10.202 3.173   28.444   1.00 76.18  ? 290  LEU B CB  1 
ATOM   5954  C  CG  . LEU B  2 180 ? -10.123 4.639   28.843   1.00 82.09  ? 290  LEU B CG  1 
ATOM   5955  C  CD1 . LEU B  2 180 ? -11.359 5.036   29.612   1.00 83.62  ? 290  LEU B CD1 1 
ATOM   5956  C  CD2 . LEU B  2 180 ? -8.879  4.885   29.668   1.00 109.77 ? 290  LEU B CD2 1 
ATOM   5957  N  N   . GLU B  2 181 ? -8.998  0.258   28.105   1.00 78.56  ? 291  GLU B N   1 
ATOM   5958  C  CA  . GLU B  2 181 ? -9.345  -1.125  27.857   1.00 90.62  ? 291  GLU B CA  1 
ATOM   5959  C  C   . GLU B  2 181 ? -10.863 -1.296  27.897   1.00 78.07  ? 291  GLU B C   1 
ATOM   5960  O  O   . GLU B  2 181 ? -11.616 -0.434  28.366   1.00 62.93  ? 291  GLU B O   1 
ATOM   5961  C  CB  . GLU B  2 181 ? -8.699  -2.046  28.894   1.00 58.73  ? 291  GLU B CB  1 
ATOM   5962  C  CG  . GLU B  2 181 ? -7.179  -2.100  28.923   1.00 119.54 ? 291  GLU B CG  1 
ATOM   5963  C  CD  . GLU B  2 181 ? -6.678  -3.006  30.037   1.00 89.70  ? 291  GLU B CD  1 
ATOM   5964  O  OE1 . GLU B  2 181 ? -7.520  -3.437  30.847   1.00 55.87  ? 291  GLU B OE1 1 
ATOM   5965  O  OE2 . GLU B  2 181 ? -5.456  -3.274  30.120   1.00 58.97  ? 291  GLU B OE2 1 
ATOM   5966  N  N   . TYR B  2 182 ? -11.309 -2.436  27.402   1.00 74.03  ? 292  TYR B N   1 
ATOM   5967  C  CA  . TYR B  2 182 ? -12.685 -2.813  27.614   1.00 102.68 ? 292  TYR B CA  1 
ATOM   5968  C  C   . TYR B  2 182 ? -12.925 -3.082  29.101   1.00 129.97 ? 292  TYR B C   1 
ATOM   5969  O  O   . TYR B  2 182 ? -11.991 -3.439  29.836   1.00 54.13  ? 292  TYR B O   1 
ATOM   5970  C  CB  . TYR B  2 182 ? -13.033 -4.057  26.827   1.00 55.10  ? 292  TYR B CB  1 
ATOM   5971  C  CG  . TYR B  2 182 ? -12.822 -4.027  25.351   1.00 63.42  ? 292  TYR B CG  1 
ATOM   5972  C  CD1 . TYR B  2 182 ? -11.672 -4.557  24.778   1.00 55.69  ? 292  TYR B CD1 1 
ATOM   5973  C  CD2 . TYR B  2 182 ? -13.813 -3.545  24.520   1.00 136.12 ? 292  TYR B CD2 1 
ATOM   5974  C  CE1 . TYR B  2 182 ? -11.505 -4.566  23.408   1.00 58.74  ? 292  TYR B CE1 1 
ATOM   5975  C  CE2 . TYR B  2 182 ? -13.659 -3.547  23.165   1.00 161.46 ? 292  TYR B CE2 1 
ATOM   5976  C  CZ  . TYR B  2 182 ? -12.509 -4.052  22.608   1.00 118.20 ? 292  TYR B CZ  1 
ATOM   5977  O  OH  . TYR B  2 182 ? -12.399 -4.029  21.241   1.00 66.68  ? 292  TYR B OH  1 
ATOM   5978  N  N   . PRO B  2 183 ? -14.155 -2.865  29.577   1.00 174.45 ? 293  PRO B N   1 
ATOM   5979  C  CA  . PRO B  2 183 ? -14.488 -3.201  30.963   1.00 94.53  ? 293  PRO B CA  1 
ATOM   5980  C  C   . PRO B  2 183 ? -14.729 -4.688  31.148   1.00 54.36  ? 293  PRO B C   1 
ATOM   5981  O  O   . PRO B  2 183 ? -15.125 -5.405  30.227   1.00 52.16  ? 293  PRO B O   1 
ATOM   5982  C  CB  . PRO B  2 183 ? -15.767 -2.399  31.217   1.00 62.80  ? 293  PRO B CB  1 
ATOM   5983  C  CG  . PRO B  2 183 ? -16.381 -2.297  29.912   1.00 62.98  ? 293  PRO B CG  1 
ATOM   5984  C  CD  . PRO B  2 183 ? -15.296 -2.220  28.900   1.00 60.86  ? 293  PRO B CD  1 
ATOM   5985  N  N   . THR B  2 184 ? -14.438 -5.151  32.360   1.00 61.80  ? 294  THR B N   1 
ATOM   5986  C  CA  . THR B  2 184 ? -14.650 -6.533  32.750   1.00 86.96  ? 294  THR B CA  1 
ATOM   5987  C  C   . THR B  2 184 ? -16.050 -6.679  33.331   1.00 79.48  ? 294  THR B C   1 
ATOM   5988  O  O   . THR B  2 184 ? -16.756 -5.697  33.560   1.00 154.93 ? 294  THR B O   1 
ATOM   5989  C  CB  . THR B  2 184 ? -13.602 -6.978  33.773   1.00 120.68 ? 294  THR B CB  1 
ATOM   5990  O  OG1 . THR B  2 184 ? -13.917 -6.395  35.038   1.00 52.78  ? 294  THR B OG1 1 
ATOM   5991  C  CG2 . THR B  2 184 ? -12.176 -6.512  33.358   1.00 48.49  ? 294  THR B CG2 1 
ATOM   5992  N  N   . ILE B  2 185 ? -16.464 -7.928  33.550   1.00 62.50  ? 295  ILE B N   1 
ATOM   5993  C  CA  . ILE B  2 185 ? -17.745 -8.184  34.211   1.00 56.21  ? 295  ILE B CA  1 
ATOM   5994  C  C   . ILE B  2 185 ? -17.735 -7.630  35.641   1.00 86.15  ? 295  ILE B C   1 
ATOM   5995  O  O   . ILE B  2 185 ? -18.768 -7.179  36.156   1.00 64.19  ? 295  ILE B O   1 
ATOM   5996  C  CB  . ILE B  2 185 ? -18.069 -9.688  34.154   1.00 122.13 ? 295  ILE B CB  1 
ATOM   5997  C  CG1 . ILE B  2 185 ? -18.236 -10.115 32.688   1.00 56.09  ? 295  ILE B CG1 1 
ATOM   5998  C  CG2 . ILE B  2 185 ? -19.330 -10.015 34.960   1.00 178.11 ? 295  ILE B CG2 1 
ATOM   5999  C  CD1 . ILE B  2 185 ? -18.737 -11.521 32.500   1.00 50.82  ? 295  ILE B CD1 1 
ATOM   6000  N  N   . GLY B  2 186 ? -16.578 -7.681  36.314   1.00 102.88 ? 296  GLY B N   1 
ATOM   6001  C  CA  . GLY B  2 186 ? -16.449 -7.035  37.613   1.00 59.95  ? 296  GLY B CA  1 
ATOM   6002  C  C   . GLY B  2 186 ? -16.633 -5.527  37.555   1.00 108.60 ? 296  GLY B C   1 
ATOM   6003  O  O   . GLY B  2 186 ? -17.333 -4.948  38.390   1.00 145.18 ? 296  GLY B O   1 
ATOM   6004  N  N   . GLN B  2 187 ? -16.002 -4.866  36.570   1.00 62.83  ? 297  GLN B N   1 
ATOM   6005  C  CA  . GLN B  2 187 ? -16.148 -3.417  36.423   1.00 80.86  ? 297  GLN B CA  1 
ATOM   6006  C  C   . GLN B  2 187 ? -17.587 -3.049  36.079   1.00 85.16  ? 297  GLN B C   1 
ATOM   6007  O  O   . GLN B  2 187 ? -18.146 -2.096  36.634   1.00 129.30 ? 297  GLN B O   1 
ATOM   6008  C  CB  . GLN B  2 187 ? -15.199 -2.880  35.337   1.00 113.81 ? 297  GLN B CB  1 
ATOM   6009  C  CG  . GLN B  2 187 ? -13.683 -3.077  35.568   1.00 136.96 ? 297  GLN B CG  1 
ATOM   6010  C  CD  . GLN B  2 187 ? -12.793 -2.411  34.492   1.00 62.04  ? 297  GLN B CD  1 
ATOM   6011  O  OE1 . GLN B  2 187 ? -13.094 -1.330  33.983   1.00 65.18  ? 297  GLN B OE1 1 
ATOM   6012  N  NE2 . GLN B  2 187 ? -11.715 -3.093  34.124   1.00 104.38 ? 297  GLN B NE2 1 
ATOM   6013  N  N   . LEU B  2 188 ? -18.193 -3.798  35.158   1.00 69.08  ? 298  LEU B N   1 
ATOM   6014  C  CA  . LEU B  2 188 ? -19.579 -3.575  34.770   1.00 73.13  ? 298  LEU B CA  1 
ATOM   6015  C  C   . LEU B  2 188 ? -20.519 -3.801  35.947   1.00 77.16  ? 298  LEU B C   1 
ATOM   6016  O  O   . LEU B  2 188 ? -21.456 -3.022  36.161   1.00 145.76 ? 298  LEU B O   1 
ATOM   6017  C  CB  . LEU B  2 188 ? -19.919 -4.499  33.600   1.00 70.52  ? 298  LEU B CB  1 
ATOM   6018  C  CG  . LEU B  2 188 ? -19.307 -4.137  32.247   1.00 67.87  ? 298  LEU B CG  1 
ATOM   6019  C  CD1 . LEU B  2 188 ? -19.476 -5.253  31.259   1.00 64.68  ? 298  LEU B CD1 1 
ATOM   6020  C  CD2 . LEU B  2 188 ? -19.918 -2.862  31.686   1.00 72.23  ? 298  LEU B CD2 1 
ATOM   6021  N  N   . ILE B  2 189 ? -20.285 -4.862  36.725   1.00 75.03  ? 299  ILE B N   1 
ATOM   6022  C  CA  . ILE B  2 189 ? -21.114 -5.109  37.900   1.00 103.24 ? 299  ILE B CA  1 
ATOM   6023  C  C   . ILE B  2 189 ? -20.964 -3.978  38.906   1.00 85.92  ? 299  ILE B C   1 
ATOM   6024  O  O   . ILE B  2 189 ? -21.931 -3.601  39.580   1.00 110.04 ? 299  ILE B O   1 
ATOM   6025  C  CB  . ILE B  2 189 ? -20.770 -6.478  38.518   1.00 150.43 ? 299  ILE B CB  1 
ATOM   6026  C  CG1 . ILE B  2 189 ? -21.276 -7.611  37.622   1.00 127.02 ? 299  ILE B CG1 1 
ATOM   6027  C  CG2 . ILE B  2 189 ? -21.360 -6.613  39.915   1.00 181.26 ? 299  ILE B CG2 1 
ATOM   6028  C  CD1 . ILE B  2 189 ? -20.915 -8.986  38.127   1.00 70.97  ? 299  ILE B CD1 1 
ATOM   6029  N  N   . ASP B  2 190 ? -19.768 -3.399  39.008   1.00 103.91 ? 300  ASP B N   1 
ATOM   6030  C  CA  . ASP B  2 190 ? -19.541 -2.334  39.977   1.00 129.07 ? 300  ASP B CA  1 
ATOM   6031  C  C   . ASP B  2 190 ? -20.164 -1.007  39.563   1.00 147.18 ? 300  ASP B C   1 
ATOM   6032  O  O   . ASP B  2 190 ? -20.357 -0.140  40.420   1.00 154.66 ? 300  ASP B O   1 
ATOM   6033  C  CB  . ASP B  2 190 ? -18.041 -2.139  40.201   1.00 81.06  ? 300  ASP B CB  1 
ATOM   6034  C  CG  . ASP B  2 190 ? -17.743 -1.175  41.327   1.00 157.27 ? 300  ASP B CG  1 
ATOM   6035  O  OD1 . ASP B  2 190 ? -18.467 -1.196  42.346   1.00 188.00 ? 300  ASP B OD1 1 
ATOM   6036  O  OD2 . ASP B  2 190 ? -16.811 -0.364  41.166   1.00 84.56  ? 300  ASP B OD2 1 
ATOM   6037  N  N   . LYS B  2 191 ? -20.511 -0.829  38.289   1.00 153.17 ? 301  LYS B N   1 
ATOM   6038  C  CA  . LYS B  2 191 ? -21.067 0.430   37.815   1.00 123.77 ? 301  LYS B CA  1 
ATOM   6039  C  C   . LYS B  2 191 ? -22.527 0.326   37.417   1.00 101.41 ? 301  LYS B C   1 
ATOM   6040  O  O   . LYS B  2 191 ? -23.188 1.361   37.276   1.00 102.51 ? 301  LYS B O   1 
ATOM   6041  C  CB  . LYS B  2 191 ? -20.263 0.959   36.618   1.00 121.32 ? 301  LYS B CB  1 
ATOM   6042  C  CG  . LYS B  2 191 ? -18.923 1.603   36.973   1.00 90.01  ? 301  LYS B CG  1 
ATOM   6043  C  CD  . LYS B  2 191 ? -19.076 2.846   37.843   1.00 95.58  ? 301  LYS B CD  1 
ATOM   6044  C  CE  . LYS B  2 191 ? -17.712 3.342   38.296   1.00 94.40  ? 301  LYS B CE  1 
ATOM   6045  N  NZ  . LYS B  2 191 ? -17.798 4.575   39.116   1.00 99.65  ? 301  LYS B NZ  1 
ATOM   6046  N  N   . LEU B  2 192 ? -23.048 -0.886  37.253   1.00 101.67 ? 302  LEU B N   1 
ATOM   6047  C  CA  . LEU B  2 192 ? -24.454 -1.099  36.952   1.00 102.03 ? 302  LEU B CA  1 
ATOM   6048  C  C   . LEU B  2 192 ? -25.308 -1.095  38.209   1.00 141.30 ? 302  LEU B C   1 
ATOM   6049  O  O   . LEU B  2 192 ? -26.543 -1.122  38.121   1.00 148.73 ? 302  LEU B O   1 
ATOM   6050  C  CB  . LEU B  2 192 ? -24.621 -2.425  36.199   1.00 98.83  ? 302  LEU B CB  1 
ATOM   6051  C  CG  . LEU B  2 192 ? -24.200 -2.452  34.728   1.00 99.17  ? 302  LEU B CG  1 
ATOM   6052  C  CD1 . LEU B  2 192 ? -24.442 -3.827  34.148   1.00 108.74 ? 302  LEU B CD1 1 
ATOM   6053  C  CD2 . LEU B  2 192 ? -24.960 -1.407  33.933   1.00 117.42 ? 302  LEU B CD2 1 
ATOM   6054  N  N   . VAL B  2 193 ? -24.670 -1.060  39.372   1.00 106.31 ? 303  VAL B N   1 
ATOM   6055  C  CA  . VAL B  2 193 ? -25.358 -0.962  40.640   1.00 109.10 ? 303  VAL B CA  1 
ATOM   6056  C  C   . VAL B  2 193 ? -25.224 0.435   41.228   1.00 135.64 ? 303  VAL B C   1 
ATOM   6057  O  O   . VAL B  2 193 ? -26.178 0.962   41.802   1.00 159.91 ? 303  VAL B O   1 
ATOM   6058  C  CB  . VAL B  2 193 ? -24.836 -2.032  41.623   1.00 119.43 ? 303  VAL B CB  1 
ATOM   6059  C  CG1 . VAL B  2 193 ? -25.613 -1.979  42.941   1.00 161.50 ? 303  VAL B CG1 1 
ATOM   6060  C  CG2 . VAL B  2 193 ? -24.916 -3.411  40.996   1.00 102.82 ? 303  VAL B CG2 1 
ATOM   6061  N  N   . GLN B  2 194 ? -24.049 1.057   41.067   1.00 120.98 ? 304  GLN B N   1 
ATOM   6062  C  CA  . GLN B  2 194 ? -23.889 2.451   41.466   1.00 141.16 ? 304  GLN B CA  1 
ATOM   6063  C  C   . GLN B  2 194 ? -24.881 3.338   40.739   1.00 160.76 ? 304  GLN B C   1 
ATOM   6064  O  O   . GLN B  2 194 ? -25.260 4.399   41.248   1.00 155.89 ? 304  GLN B O   1 
ATOM   6065  C  CB  . GLN B  2 194 ? -22.471 2.929   41.177   1.00 120.30 ? 304  GLN B CB  1 
ATOM   6066  C  CG  . GLN B  2 194 ? -21.407 2.356   42.074   1.00 146.65 ? 304  GLN B CG  1 
ATOM   6067  C  CD  . GLN B  2 194 ? -20.037 2.881   41.699   1.00 148.82 ? 304  GLN B CD  1 
ATOM   6068  O  OE1 . GLN B  2 194 ? -19.922 3.807   40.895   1.00 118.15 ? 304  GLN B OE1 1 
ATOM   6069  N  NE2 . GLN B  2 194 ? -18.991 2.287   42.265   1.00 142.47 ? 304  GLN B NE2 1 
ATOM   6070  N  N   . ASN B  2 195 ? -25.285 2.936   39.537   1.00 158.96 ? 305  ASN B N   1 
ATOM   6071  C  CA  . ASN B  2 195 ? -26.317 3.630   38.792   1.00 151.09 ? 305  ASN B CA  1 
ATOM   6072  C  C   . ASN B  2 195 ? -27.636 2.883   38.796   1.00 124.47 ? 305  ASN B C   1 
ATOM   6073  O  O   . ASN B  2 195 ? -28.648 3.444   38.357   1.00 129.70 ? 305  ASN B O   1 
ATOM   6074  C  CB  . ASN B  2 195 ? -25.854 3.852   37.348   1.00 134.63 ? 305  ASN B CB  1 
ATOM   6075  C  CG  . ASN B  2 195 ? -24.409 4.284   37.276   1.00 145.08 ? 305  ASN B CG  1 
ATOM   6076  O  OD1 . ASN B  2 195 ? -23.953 5.092   38.086   1.00 151.63 ? 305  ASN B OD1 1 
ATOM   6077  N  ND2 . ASN B  2 195 ? -23.671 3.732   36.324   1.00 151.14 ? 305  ASN B ND2 1 
ATOM   6078  N  N   . ASN B  2 196 ? -27.652 1.654   39.318   1.00 122.70 ? 306  ASN B N   1 
ATOM   6079  C  CA  . ASN B  2 196 ? -28.839 0.814   39.360   1.00 126.77 ? 306  ASN B CA  1 
ATOM   6080  C  C   . ASN B  2 196 ? -29.410 0.643   37.960   1.00 127.13 ? 306  ASN B C   1 
ATOM   6081  O  O   . ASN B  2 196 ? -30.393 1.300   37.602   1.00 133.01 ? 306  ASN B O   1 
ATOM   6082  C  CB  . ASN B  2 196 ? -29.890 1.405   40.303   1.00 162.91 ? 306  ASN B CB  1 
ATOM   6083  C  CG  . ASN B  2 196 ? -31.077 0.478   40.504   1.00 146.83 ? 306  ASN B CG  1 
ATOM   6084  O  OD1 . ASN B  2 196 ? -30.942 -0.742  40.438   1.00 152.94 ? 306  ASN B OD1 1 
ATOM   6085  N  ND2 . ASN B  2 196 ? -32.251 1.057   40.735   1.00 149.57 ? 306  ASN B ND2 1 
ATOM   6086  N  N   . VAL B  2 197 ? -28.793 -0.222  37.157   1.00 121.13 ? 307  VAL B N   1 
ATOM   6087  C  CA  . VAL B  2 197 ? -29.184 -0.445  35.769   1.00 120.78 ? 307  VAL B CA  1 
ATOM   6088  C  C   . VAL B  2 197 ? -29.487 -1.928  35.601   1.00 119.58 ? 307  VAL B C   1 
ATOM   6089  O  O   . VAL B  2 197 ? -28.693 -2.775  36.028   1.00 114.49 ? 307  VAL B O   1 
ATOM   6090  C  CB  . VAL B  2 197 ? -28.082 0.023   34.796   1.00 146.05 ? 307  VAL B CB  1 
ATOM   6091  C  CG1 . VAL B  2 197 ? -28.496 -0.158  33.351   1.00 144.00 ? 307  VAL B CG1 1 
ATOM   6092  C  CG2 . VAL B  2 197 ? -27.730 1.483   35.045   1.00 128.93 ? 307  VAL B CG2 1 
ATOM   6093  N  N   . LEU B  2 198 ? -30.662 -2.238  35.040   1.00 159.42 ? 308  LEU B N   1 
ATOM   6094  C  CA  . LEU B  2 198 ? -31.061 -3.610  34.717   1.00 124.89 ? 308  LEU B CA  1 
ATOM   6095  C  C   . LEU B  2 198 ? -30.746 -3.893  33.253   1.00 129.57 ? 308  LEU B C   1 
ATOM   6096  O  O   . LEU B  2 198 ? -31.360 -3.310  32.354   1.00 124.62 ? 308  LEU B O   1 
ATOM   6097  C  CB  . LEU B  2 198 ? -32.541 -3.836  35.004   1.00 134.07 ? 308  LEU B CB  1 
ATOM   6098  C  CG  . LEU B  2 198 ? -32.991 -3.747  36.460   1.00 164.83 ? 308  LEU B CG  1 
ATOM   6099  C  CD1 . LEU B  2 198 ? -34.472 -4.069  36.540   1.00 173.69 ? 308  LEU B CD1 1 
ATOM   6100  C  CD2 . LEU B  2 198 ? -32.179 -4.686  37.340   1.00 163.20 ? 308  LEU B CD2 1 
ATOM   6101  N  N   . LEU B  2 199 ? -29.806 -4.806  33.017   1.00 154.18 ? 309  LEU B N   1 
ATOM   6102  C  CA  . LEU B  2 199 ? -29.272 -5.060  31.681   1.00 143.79 ? 309  LEU B CA  1 
ATOM   6103  C  C   . LEU B  2 199 ? -30.002 -6.239  31.044   1.00 111.65 ? 309  LEU B C   1 
ATOM   6104  O  O   . LEU B  2 199 ? -29.937 -7.368  31.539   1.00 110.38 ? 309  LEU B O   1 
ATOM   6105  C  CB  . LEU B  2 199 ? -27.765 -5.308  31.735   1.00 100.70 ? 309  LEU B CB  1 
ATOM   6106  C  CG  . LEU B  2 199 ? -27.073 -5.388  30.375   1.00 95.77  ? 309  LEU B CG  1 
ATOM   6107  C  CD1 . LEU B  2 199 ? -27.260 -4.106  29.584   1.00 99.73  ? 309  LEU B CD1 1 
ATOM   6108  C  CD2 . LEU B  2 199 ? -25.636 -5.692  30.569   1.00 88.20  ? 309  LEU B CD2 1 
ATOM   6109  N  N   . ILE B  2 200 ? -30.716 -5.968  29.964   1.00 115.99 ? 310  ILE B N   1 
ATOM   6110  C  CA  . ILE B  2 200 ? -31.410 -6.994  29.201   1.00 140.38 ? 310  ILE B CA  1 
ATOM   6111  C  C   . ILE B  2 200 ? -30.523 -7.386  28.029   1.00 115.18 ? 310  ILE B C   1 
ATOM   6112  O  O   . ILE B  2 200 ? -30.177 -6.542  27.194   1.00 115.58 ? 310  ILE B O   1 
ATOM   6113  C  CB  . ILE B  2 200 ? -32.781 -6.499  28.713   1.00 130.37 ? 310  ILE B CB  1 
ATOM   6114  C  CG1 . ILE B  2 200 ? -33.689 -6.192  29.901   1.00 135.65 ? 310  ILE B CG1 1 
ATOM   6115  C  CG2 . ILE B  2 200 ? -33.425 -7.529  27.806   1.00 134.76 ? 310  ILE B CG2 1 
ATOM   6116  C  CD1 . ILE B  2 200 ? -35.002 -5.601  29.501   1.00 146.61 ? 310  ILE B CD1 1 
ATOM   6117  N  N   . PHE B  2 201 ? -30.144 -8.658  27.974   1.00 111.22 ? 311  PHE B N   1 
ATOM   6118  C  CA  . PHE B  2 201 ? -29.420 -9.211  26.837   1.00 107.87 ? 311  PHE B CA  1 
ATOM   6119  C  C   . PHE B  2 201 ? -30.428 -9.697  25.800   1.00 134.14 ? 311  PHE B C   1 
ATOM   6120  O  O   . PHE B  2 201 ? -31.272 -10.547 26.104   1.00 132.54 ? 311  PHE B O   1 
ATOM   6121  C  CB  . PHE B  2 201 ? -28.520 -10.362 27.281   1.00 100.59 ? 311  PHE B CB  1 
ATOM   6122  C  CG  . PHE B  2 201 ? -27.308 -9.922  28.047   1.00 133.46 ? 311  PHE B CG  1 
ATOM   6123  C  CD1 . PHE B  2 201 ? -26.596 -8.799  27.655   1.00 115.92 ? 311  PHE B CD1 1 
ATOM   6124  C  CD2 . PHE B  2 201 ? -26.888 -10.621 29.166   1.00 122.82 ? 311  PHE B CD2 1 
ATOM   6125  C  CE1 . PHE B  2 201 ? -25.498 -8.393  28.353   1.00 84.99  ? 311  PHE B CE1 1 
ATOM   6126  C  CE2 . PHE B  2 201 ? -25.785 -10.211 29.871   1.00 82.56  ? 311  PHE B CE2 1 
ATOM   6127  C  CZ  . PHE B  2 201 ? -25.094 -9.097  29.463   1.00 80.72  ? 311  PHE B CZ  1 
ATOM   6128  N  N   . ALA B  2 202 ? -30.350 -9.158  24.584   1.00 130.93 ? 312  ALA B N   1 
ATOM   6129  C  CA  . ALA B  2 202 ? -31.233 -9.545  23.481   1.00 125.45 ? 312  ALA B CA  1 
ATOM   6130  C  C   . ALA B  2 202 ? -30.370 -9.973  22.295   1.00 122.14 ? 312  ALA B C   1 
ATOM   6131  O  O   . ALA B  2 202 ? -30.103 -9.179  21.390   1.00 123.68 ? 312  ALA B O   1 
ATOM   6132  C  CB  . ALA B  2 202 ? -32.164 -8.397  23.109   1.00 133.94 ? 312  ALA B CB  1 
ATOM   6133  N  N   . VAL B  2 203 ? -29.995 -11.254 22.267   1.00 134.02 ? 313  VAL B N   1 
ATOM   6134  C  CA  . VAL B  2 203 ? -29.055 -11.763 21.273   1.00 152.33 ? 313  VAL B CA  1 
ATOM   6135  C  C   . VAL B  2 203 ? -29.725 -12.819 20.404   1.00 125.68 ? 313  VAL B C   1 
ATOM   6136  O  O   . VAL B  2 203 ? -30.947 -12.997 20.450   1.00 128.03 ? 313  VAL B O   1 
ATOM   6137  C  CB  . VAL B  2 203 ? -27.784 -12.329 21.942   1.00 136.44 ? 313  VAL B CB  1 
ATOM   6138  C  CG1 . VAL B  2 203 ? -27.047 -11.245 22.718   1.00 100.06 ? 313  VAL B CG1 1 
ATOM   6139  C  CG2 . VAL B  2 203 ? -28.135 -13.478 22.861   1.00 113.63 ? 313  VAL B CG2 1 
ATOM   6140  N  N   . THR B  2 204 ? -28.929 -13.494 19.580   1.00 149.59 ? 314  THR B N   1 
ATOM   6141  C  CA  . THR B  2 204 ? -29.375 -14.581 18.722   1.00 159.71 ? 314  THR B CA  1 
ATOM   6142  C  C   . THR B  2 204 ? -29.280 -15.924 19.447   1.00 143.55 ? 314  THR B C   1 
ATOM   6143  O  O   . THR B  2 204 ? -28.687 -16.038 20.520   1.00 130.25 ? 314  THR B O   1 
ATOM   6144  C  CB  . THR B  2 204 ? -28.543 -14.600 17.444   1.00 157.53 ? 314  THR B CB  1 
ATOM   6145  O  OG1 . THR B  2 204 ? -27.148 -14.601 17.784   1.00 138.03 ? 314  THR B OG1 1 
ATOM   6146  C  CG2 . THR B  2 204 ? -28.857 -13.378 16.603   1.00 126.81 ? 314  THR B CG2 1 
ATOM   6147  N  N   . GLN B  2 205 ? -29.880 -16.953 18.839   1.00 124.32 ? 315  GLN B N   1 
ATOM   6148  C  CA  . GLN B  2 205 ? -29.928 -18.266 19.476   1.00 123.00 ? 315  GLN B CA  1 
ATOM   6149  C  C   . GLN B  2 205 ? -28.540 -18.755 19.868   1.00 132.09 ? 315  GLN B C   1 
ATOM   6150  O  O   . GLN B  2 205 ? -28.305 -19.127 21.022   1.00 157.77 ? 315  GLN B O   1 
ATOM   6151  C  CB  . GLN B  2 205 ? -30.594 -19.283 18.557   1.00 143.56 ? 315  GLN B CB  1 
ATOM   6152  C  CG  . GLN B  2 205 ? -32.036 -18.979 18.247   1.00 173.52 ? 315  GLN B CG  1 
ATOM   6153  C  CD  . GLN B  2 205 ? -32.751 -20.175 17.667   1.00 168.20 ? 315  GLN B CD  1 
ATOM   6154  O  OE1 . GLN B  2 205 ? -32.319 -21.317 17.842   1.00 159.81 ? 315  GLN B OE1 1 
ATOM   6155  N  NE2 . GLN B  2 205 ? -33.849 -19.923 16.968   1.00 196.45 ? 315  GLN B NE2 1 
ATOM   6156  N  N   . GLU B  2 206 ? -27.597 -18.740 18.922   1.00 143.18 ? 316  GLU B N   1 
ATOM   6157  C  CA  . GLU B  2 206 ? -26.268 -19.280 19.189   1.00 135.56 ? 316  GLU B CA  1 
ATOM   6158  C  C   . GLU B  2 206 ? -25.514 -18.474 20.229   1.00 110.30 ? 316  GLU B C   1 
ATOM   6159  O  O   . GLU B  2 206 ? -24.489 -18.948 20.728   1.00 112.16 ? 316  GLU B O   1 
ATOM   6160  C  CB  . GLU B  2 206 ? -25.435 -19.340 17.910   1.00 140.25 ? 316  GLU B CB  1 
ATOM   6161  C  CG  . GLU B  2 206 ? -25.133 -17.983 17.316   1.00 136.36 ? 316  GLU B CG  1 
ATOM   6162  C  CD  . GLU B  2 206 ? -26.283 -17.450 16.493   1.00 166.16 ? 316  GLU B CD  1 
ATOM   6163  O  OE1 . GLU B  2 206 ? -27.306 -18.157 16.370   1.00 163.68 ? 316  GLU B OE1 1 
ATOM   6164  O  OE2 . GLU B  2 206 ? -26.170 -16.322 15.974   1.00 197.81 ? 316  GLU B OE2 1 
ATOM   6165  N  N   . GLN B  2 207 ? -25.995 -17.282 20.566   1.00 98.66  ? 317  GLN B N   1 
ATOM   6166  C  CA  . GLN B  2 207 ? -25.330 -16.426 21.530   1.00 137.85 ? 317  GLN B CA  1 
ATOM   6167  C  C   . GLN B  2 207 ? -26.030 -16.419 22.883   1.00 138.65 ? 317  GLN B C   1 
ATOM   6168  O  O   . GLN B  2 207 ? -25.531 -15.798 23.826   1.00 86.93  ? 317  GLN B O   1 
ATOM   6169  C  CB  . GLN B  2 207 ? -25.230 -15.003 20.966   1.00 92.31  ? 317  GLN B CB  1 
ATOM   6170  C  CG  . GLN B  2 207 ? -23.861 -14.410 21.150   1.00 86.52  ? 317  GLN B CG  1 
ATOM   6171  C  CD  . GLN B  2 207 ? -22.816 -15.145 20.350   1.00 113.24 ? 317  GLN B CD  1 
ATOM   6172  O  OE1 . GLN B  2 207 ? -23.126 -15.761 19.329   1.00 149.72 ? 317  GLN B OE1 1 
ATOM   6173  N  NE2 . GLN B  2 207 ? -21.575 -15.123 20.829   1.00 82.52  ? 317  GLN B NE2 1 
ATOM   6174  N  N   . VAL B  2 208 ? -27.121 -17.166 23.035   1.00 148.99 ? 318  VAL B N   1 
ATOM   6175  C  CA  . VAL B  2 208 ? -27.845 -17.151 24.300   1.00 98.80  ? 318  VAL B CA  1 
ATOM   6176  C  C   . VAL B  2 208 ? -27.088 -17.943 25.354   1.00 92.70  ? 318  VAL B C   1 
ATOM   6177  O  O   . VAL B  2 208 ? -26.872 -17.463 26.472   1.00 89.62  ? 318  VAL B O   1 
ATOM   6178  C  CB  . VAL B  2 208 ? -29.273 -17.690 24.112   1.00 107.92 ? 318  VAL B CB  1 
ATOM   6179  C  CG1 . VAL B  2 208 ? -29.953 -17.812 25.456   1.00 109.87 ? 318  VAL B CG1 1 
ATOM   6180  C  CG2 . VAL B  2 208 ? -30.069 -16.778 23.201   1.00 114.68 ? 318  VAL B CG2 1 
ATOM   6181  N  N   . HIS B  2 209 ? -26.644 -19.155 25.004   1.00 142.62 ? 319  HIS B N   1 
ATOM   6182  C  CA  . HIS B  2 209 ? -25.968 -20.006 25.978   1.00 143.84 ? 319  HIS B CA  1 
ATOM   6183  C  C   . HIS B  2 209 ? -24.771 -19.291 26.575   1.00 123.66 ? 319  HIS B C   1 
ATOM   6184  O  O   . HIS B  2 209 ? -24.379 -19.579 27.711   1.00 75.55  ? 319  HIS B O   1 
ATOM   6185  C  CB  . HIS B  2 209 ? -25.547 -21.325 25.318   1.00 160.72 ? 319  HIS B CB  1 
ATOM   6186  C  CG  . HIS B  2 209 ? -25.074 -22.379 26.278   1.00 152.51 ? 319  HIS B CG  1 
ATOM   6187  N  ND1 . HIS B  2 209 ? -23.778 -22.442 26.746   1.00 170.89 ? 319  HIS B ND1 1 
ATOM   6188  C  CD2 . HIS B  2 209 ? -25.722 -23.433 26.830   1.00 110.76 ? 319  HIS B CD2 1 
ATOM   6189  C  CE1 . HIS B  2 209 ? -23.653 -23.479 27.555   1.00 115.32 ? 319  HIS B CE1 1 
ATOM   6190  N  NE2 . HIS B  2 209 ? -24.818 -24.097 27.623   1.00 96.92  ? 319  HIS B NE2 1 
ATOM   6191  N  N   . LEU B  2 210 ? -24.201 -18.337 25.835   1.00 96.23  ? 320  LEU B N   1 
ATOM   6192  C  CA  . LEU B  2 210 ? -23.108 -17.517 26.351   1.00 116.86 ? 320  LEU B CA  1 
ATOM   6193  C  C   . LEU B  2 210 ? -23.614 -16.447 27.317   1.00 111.83 ? 320  LEU B C   1 
ATOM   6194  O  O   . LEU B  2 210 ? -23.221 -16.410 28.486   1.00 68.36  ? 320  LEU B O   1 
ATOM   6195  C  CB  . LEU B  2 210 ? -22.359 -16.865 25.181   1.00 139.90 ? 320  LEU B CB  1 
ATOM   6196  C  CG  . LEU B  2 210 ? -20.994 -16.172 25.305   1.00 120.77 ? 320  LEU B CG  1 
ATOM   6197  C  CD1 . LEU B  2 210 ? -20.423 -15.965 23.920   1.00 116.19 ? 320  LEU B CD1 1 
ATOM   6198  C  CD2 . LEU B  2 210 ? -21.090 -14.828 25.978   1.00 119.71 ? 320  LEU B CD2 1 
ATOM   6199  N  N   . TYR B  2 211 ? -24.480 -15.557 26.836   1.00 76.52  ? 321  TYR B N   1 
ATOM   6200  C  CA  . TYR B  2 211 ? -24.858 -14.395 27.625   1.00 77.61  ? 321  TYR B CA  1 
ATOM   6201  C  C   . TYR B  2 211 ? -25.709 -14.748 28.831   1.00 80.37  ? 321  TYR B C   1 
ATOM   6202  O  O   . TYR B  2 211 ? -25.765 -13.956 29.773   1.00 79.93  ? 321  TYR B O   1 
ATOM   6203  C  CB  . TYR B  2 211 ? -25.595 -13.400 26.739   1.00 83.04  ? 321  TYR B CB  1 
ATOM   6204  C  CG  . TYR B  2 211 ? -24.685 -12.579 25.859   1.00 80.40  ? 321  TYR B CG  1 
ATOM   6205  C  CD1 . TYR B  2 211 ? -23.980 -13.175 24.823   1.00 78.43  ? 321  TYR B CD1 1 
ATOM   6206  C  CD2 . TYR B  2 211 ? -24.561 -11.208 26.029   1.00 130.27 ? 321  TYR B CD2 1 
ATOM   6207  C  CE1 . TYR B  2 211 ? -23.150 -12.439 24.003   1.00 76.73  ? 321  TYR B CE1 1 
ATOM   6208  C  CE2 . TYR B  2 211 ? -23.736 -10.456 25.204   1.00 146.57 ? 321  TYR B CE2 1 
ATOM   6209  C  CZ  . TYR B  2 211 ? -23.033 -11.079 24.191   1.00 134.62 ? 321  TYR B CZ  1 
ATOM   6210  O  OH  . TYR B  2 211 ? -22.214 -10.343 23.360   1.00 109.16 ? 321  TYR B OH  1 
ATOM   6211  N  N   . GLU B  2 212 ? -26.370 -15.911 28.830   1.00 128.80 ? 322  GLU B N   1 
ATOM   6212  C  CA  . GLU B  2 212 ? -27.168 -16.303 29.988   1.00 100.08 ? 322  GLU B CA  1 
ATOM   6213  C  C   . GLU B  2 212 ? -26.282 -16.596 31.176   1.00 82.00  ? 322  GLU B C   1 
ATOM   6214  O  O   . GLU B  2 212 ? -26.707 -16.435 32.324   1.00 85.16  ? 322  GLU B O   1 
ATOM   6215  C  CB  . GLU B  2 212 ? -28.020 -17.531 29.682   1.00 92.41  ? 322  GLU B CB  1 
ATOM   6216  C  CG  . GLU B  2 212 ? -28.942 -17.895 30.832   1.00 109.49 ? 322  GLU B CG  1 
ATOM   6217  C  CD  . GLU B  2 212 ? -29.770 -19.124 30.552   1.00 138.59 ? 322  GLU B CD  1 
ATOM   6218  O  OE1 . GLU B  2 212 ? -29.647 -19.680 29.442   1.00 183.64 ? 322  GLU B OE1 1 
ATOM   6219  O  OE2 . GLU B  2 212 ? -30.549 -19.529 31.441   1.00 147.22 ? 322  GLU B OE2 1 
ATOM   6220  N  N   . ASN B  2 213 ? -25.074 -17.088 30.916   1.00 75.18  ? 323  ASN B N   1 
ATOM   6221  C  CA  . ASN B  2 213 ? -24.112 -17.270 31.988   1.00 112.44 ? 323  ASN B CA  1 
ATOM   6222  C  C   . ASN B  2 213 ? -23.531 -15.934 32.433   1.00 138.39 ? 323  ASN B C   1 
ATOM   6223  O  O   . ASN B  2 213 ? -23.102 -15.802 33.583   1.00 118.75 ? 323  ASN B O   1 
ATOM   6224  C  CB  . ASN B  2 213 ? -23.022 -18.240 31.537   1.00 142.82 ? 323  ASN B CB  1 
ATOM   6225  C  CG  . ASN B  2 213 ? -23.567 -19.640 31.260   1.00 137.89 ? 323  ASN B CG  1 
ATOM   6226  O  OD1 . ASN B  2 213 ? -23.297 -20.229 30.213   1.00 109.59 ? 323  ASN B OD1 1 
ATOM   6227  N  ND2 . ASN B  2 213 ? -24.337 -20.174 32.202   1.00 146.95 ? 323  ASN B ND2 1 
ATOM   6228  N  N   . TYR B  2 214 ? -23.527 -14.932 31.548   1.00 135.69 ? 324  TYR B N   1 
ATOM   6229  C  CA  . TYR B  2 214 ? -23.161 -13.584 31.972   1.00 67.00  ? 324  TYR B CA  1 
ATOM   6230  C  C   . TYR B  2 214 ? -24.230 -12.989 32.871   1.00 101.49 ? 324  TYR B C   1 
ATOM   6231  O  O   . TYR B  2 214 ? -23.919 -12.375 33.898   1.00 158.14 ? 324  TYR B O   1 
ATOM   6232  C  CB  . TYR B  2 214 ? -22.963 -12.674 30.767   1.00 66.29  ? 324  TYR B CB  1 
ATOM   6233  C  CG  . TYR B  2 214 ? -21.690 -12.889 29.993   1.00 61.43  ? 324  TYR B CG  1 
ATOM   6234  C  CD1 . TYR B  2 214 ? -20.744 -13.823 30.409   1.00 113.42 ? 324  TYR B CD1 1 
ATOM   6235  C  CD2 . TYR B  2 214 ? -21.436 -12.153 28.836   1.00 62.13  ? 324  TYR B CD2 1 
ATOM   6236  C  CE1 . TYR B  2 214 ? -19.577 -14.016 29.690   1.00 163.09 ? 324  TYR B CE1 1 
ATOM   6237  C  CE2 . TYR B  2 214 ? -20.287 -12.340 28.115   1.00 58.44  ? 324  TYR B CE2 1 
ATOM   6238  C  CZ  . TYR B  2 214 ? -19.353 -13.271 28.543   1.00 130.47 ? 324  TYR B CZ  1 
ATOM   6239  O  OH  . TYR B  2 214 ? -18.194 -13.462 27.819   1.00 77.91  ? 324  TYR B OH  1 
ATOM   6240  N  N   . ALA B  2 215 ? -25.497 -13.168 32.501   1.00 80.05  ? 325  ALA B N   1 
ATOM   6241  C  CA  . ALA B  2 215 ? -26.593 -12.656 33.309   1.00 108.75 ? 325  ALA B CA  1 
ATOM   6242  C  C   . ALA B  2 215 ? -26.631 -13.311 34.677   1.00 114.42 ? 325  ALA B C   1 
ATOM   6243  O  O   . ALA B  2 215 ? -27.193 -12.737 35.615   1.00 145.75 ? 325  ALA B O   1 
ATOM   6244  C  CB  . ALA B  2 215 ? -27.924 -12.869 32.581   1.00 116.79 ? 325  ALA B CB  1 
ATOM   6245  N  N   . LYS B  2 216 ? -26.064 -14.510 34.804   1.00 133.65 ? 326  LYS B N   1 
ATOM   6246  C  CA  . LYS B  2 216 ? -25.986 -15.137 36.113   1.00 153.49 ? 326  LYS B CA  1 
ATOM   6247  C  C   . LYS B  2 216 ? -24.985 -14.401 36.989   1.00 142.36 ? 326  LYS B C   1 
ATOM   6248  O  O   . LYS B  2 216 ? -25.185 -14.281 38.203   1.00 199.33 ? 326  LYS B O   1 
ATOM   6249  C  CB  . LYS B  2 216 ? -25.614 -16.615 35.974   1.00 141.97 ? 326  LYS B CB  1 
ATOM   6250  C  CG  . LYS B  2 216 ? -26.675 -17.470 35.279   1.00 87.18  ? 326  LYS B CG  1 
ATOM   6251  C  CD  . LYS B  2 216 ? -26.242 -18.929 35.221   1.00 84.30  ? 326  LYS B CD  1 
ATOM   6252  C  CE  . LYS B  2 216 ? -27.265 -19.793 34.504   1.00 90.12  ? 326  LYS B CE  1 
ATOM   6253  N  NZ  . LYS B  2 216 ? -26.886 -21.237 34.494   1.00 88.13  ? 326  LYS B NZ  1 
ATOM   6254  N  N   . LEU B  2 217 ? -23.897 -13.909 36.392   1.00 77.53  ? 327  LEU B N   1 
ATOM   6255  C  CA  . LEU B  2 217 ? -22.940 -13.119 37.158   1.00 98.43  ? 327  LEU B CA  1 
ATOM   6256  C  C   . LEU B  2 217 ? -23.494 -11.737 37.458   1.00 148.99 ? 327  LEU B C   1 
ATOM   6257  O  O   . LEU B  2 217 ? -23.501 -11.293 38.612   1.00 169.71 ? 327  LEU B O   1 
ATOM   6258  C  CB  . LEU B  2 217 ? -21.608 -13.006 36.419   1.00 67.55  ? 327  LEU B CB  1 
ATOM   6259  C  CG  . LEU B  2 217 ? -20.925 -14.318 36.033   1.00 62.29  ? 327  LEU B CG  1 
ATOM   6260  C  CD1 . LEU B  2 217 ? -19.573 -14.053 35.379   1.00 55.95  ? 327  LEU B CD1 1 
ATOM   6261  C  CD2 . LEU B  2 217 ? -20.785 -15.237 37.233   1.00 135.02 ? 327  LEU B CD2 1 
ATOM   6262  N  N   . ILE B  2 218 ? -23.937 -11.032 36.426   1.00 117.50 ? 328  ILE B N   1 
ATOM   6263  C  CA  . ILE B  2 218 ? -24.452 -9.675  36.569   1.00 91.03  ? 328  ILE B CA  1 
ATOM   6264  C  C   . ILE B  2 218 ? -25.775 -9.688  37.326   1.00 103.39 ? 328  ILE B C   1 
ATOM   6265  O  O   . ILE B  2 218 ? -26.760 -10.256 36.834   1.00 149.81 ? 328  ILE B O   1 
ATOM   6266  C  CB  . ILE B  2 218 ? -24.596 -9.016  35.193   1.00 102.04 ? 328  ILE B CB  1 
ATOM   6267  C  CG1 . ILE B  2 218 ? -23.310 -9.232  34.405   1.00 82.14  ? 328  ILE B CG1 1 
ATOM   6268  C  CG2 . ILE B  2 218 ? -24.880 -7.534  35.330   1.00 149.70 ? 328  ILE B CG2 1 
ATOM   6269  C  CD1 . ILE B  2 218 ? -23.339 -8.632  33.033   1.00 80.59  ? 328  ILE B CD1 1 
ATOM   6270  N  N   . PRO B  2 219 ? -25.852 -9.076  38.510   1.00 125.93 ? 329  PRO B N   1 
ATOM   6271  C  CA  . PRO B  2 219 ? -27.113 -9.101  39.265   1.00 136.05 ? 329  PRO B CA  1 
ATOM   6272  C  C   . PRO B  2 219 ? -28.199 -8.297  38.566   1.00 139.91 ? 329  PRO B C   1 
ATOM   6273  O  O   . PRO B  2 219 ? -27.971 -7.177  38.105   1.00 131.26 ? 329  PRO B O   1 
ATOM   6274  C  CB  . PRO B  2 219 ? -26.731 -8.486  40.618   1.00 162.51 ? 329  PRO B CB  1 
ATOM   6275  C  CG  . PRO B  2 219 ? -25.532 -7.648  40.330   1.00 130.91 ? 329  PRO B CG  1 
ATOM   6276  C  CD  . PRO B  2 219 ? -24.782 -8.374  39.244   1.00 90.60  ? 329  PRO B CD  1 
ATOM   6277  N  N   . GLY B  2 220 ? -29.386 -8.882  38.495   1.00 113.51 ? 330  GLY B N   1 
ATOM   6278  C  CA  . GLY B  2 220 ? -30.520 -8.211  37.902   1.00 145.33 ? 330  GLY B CA  1 
ATOM   6279  C  C   . GLY B  2 220 ? -30.563 -8.317  36.395   1.00 130.43 ? 330  GLY B C   1 
ATOM   6280  O  O   . GLY B  2 220 ? -31.640 -8.220  35.800   1.00 181.01 ? 330  GLY B O   1 
ATOM   6281  N  N   . ALA B  2 221 ? -29.407 -8.513  35.766   1.00 110.26 ? 331  ALA B N   1 
ATOM   6282  C  CA  . ALA B  2 221 ? -29.361 -8.620  34.314   1.00 108.17 ? 331  ALA B CA  1 
ATOM   6283  C  C   . ALA B  2 221 ? -29.949 -9.948  33.845   1.00 136.76 ? 331  ALA B C   1 
ATOM   6284  O  O   . ALA B  2 221 ? -29.558 -11.020 34.318   1.00 107.20 ? 331  ALA B O   1 
ATOM   6285  C  CB  . ALA B  2 221 ? -27.930 -8.468  33.810   1.00 107.44 ? 331  ALA B CB  1 
ATOM   6286  N  N   . THR B  2 222 ? -30.863 -9.867  32.884   1.00 169.64 ? 332  THR B N   1 
ATOM   6287  C  CA  . THR B  2 222 ? -31.576 -10.990 32.290   1.00 118.50 ? 332  THR B CA  1 
ATOM   6288  C  C   . THR B  2 222 ? -31.191 -11.111 30.820   1.00 141.90 ? 332  THR B C   1 
ATOM   6289  O  O   . THR B  2 222 ? -30.387 -10.332 30.300   1.00 155.33 ? 332  THR B O   1 
ATOM   6290  C  CB  . THR B  2 222 ? -33.084 -10.803 32.437   1.00 129.13 ? 332  THR B CB  1 
ATOM   6291  O  OG1 . THR B  2 222 ? -33.507 -9.750  31.564   1.00 132.10 ? 332  THR B OG1 1 
ATOM   6292  C  CG2 . THR B  2 222 ? -33.426 -10.428 33.871   1.00 132.93 ? 332  THR B CG2 1 
ATOM   6293  N  N   . VAL B  2 223 ? -31.740 -12.129 30.160   1.00 140.14 ? 333  VAL B N   1 
ATOM   6294  C  CA  . VAL B  2 223 ? -31.445 -12.417 28.763   1.00 134.56 ? 333  VAL B CA  1 
ATOM   6295  C  C   . VAL B  2 223 ? -32.746 -12.427 27.962   1.00 125.34 ? 333  VAL B C   1 
ATOM   6296  O  O   . VAL B  2 223 ? -33.841 -12.440 28.517   1.00 132.63 ? 333  VAL B O   1 
ATOM   6297  C  CB  . VAL B  2 223 ? -30.675 -13.739 28.595   1.00 113.07 ? 333  VAL B CB  1 
ATOM   6298  C  CG1 . VAL B  2 223 ? -29.221 -13.529 28.959   1.00 100.45 ? 333  VAL B CG1 1 
ATOM   6299  C  CG2 . VAL B  2 223 ? -31.280 -14.815 29.486   1.00 113.97 ? 333  VAL B CG2 1 
ATOM   6300  N  N   . GLY B  2 224 ? -32.603 -12.386 26.637   1.00 128.63 ? 334  GLY B N   1 
ATOM   6301  C  CA  . GLY B  2 224 ? -33.744 -12.413 25.738   1.00 138.32 ? 334  GLY B CA  1 
ATOM   6302  C  C   . GLY B  2 224 ? -33.356 -12.942 24.376   1.00 137.82 ? 334  GLY B C   1 
ATOM   6303  O  O   . GLY B  2 224 ? -32.185 -12.904 23.987   1.00 166.04 ? 334  GLY B O   1 
ATOM   6304  N  N   . LEU B  2 225 ? -34.352 -13.446 23.649   1.00 144.19 ? 335  LEU B N   1 
ATOM   6305  C  CA  . LEU B  2 225 ? -34.146 -14.010 22.321   1.00 145.44 ? 335  LEU B CA  1 
ATOM   6306  C  C   . LEU B  2 225 ? -34.711 -13.097 21.239   1.00 156.87 ? 335  LEU B C   1 
ATOM   6307  O  O   . LEU B  2 225 ? -35.799 -12.530 21.393   1.00 200.64 ? 335  LEU B O   1 
ATOM   6308  C  CB  . LEU B  2 225 ? -34.797 -15.386 22.196   1.00 150.44 ? 335  LEU B CB  1 
ATOM   6309  C  CG  . LEU B  2 225 ? -34.481 -16.069 20.862   1.00 182.40 ? 335  LEU B CG  1 
ATOM   6310  C  CD1 . LEU B  2 225 ? -32.969 -16.282 20.690   1.00 140.45 ? 335  LEU B CD1 1 
ATOM   6311  C  CD2 . LEU B  2 225 ? -35.275 -17.362 20.668   1.00 192.65 ? 335  LEU B CD2 1 
ATOM   6312  N  N   . LEU B  2 226 ? -34.002 -13.025 20.113   1.00 151.02 ? 336  LEU B N   1 
ATOM   6313  C  CA  . LEU B  2 226 ? -34.394 -12.209 18.970   1.00 169.34 ? 336  LEU B CA  1 
ATOM   6314  C  C   . LEU B  2 226 ? -35.113 -13.062 17.931   1.00 165.96 ? 336  LEU B C   1 
ATOM   6315  O  O   . LEU B  2 226 ? -34.589 -14.092 17.495   1.00 162.82 ? 336  LEU B O   1 
ATOM   6316  C  CB  . LEU B  2 226 ? -33.168 -11.550 18.332   1.00 151.19 ? 336  LEU B CB  1 
ATOM   6317  C  CG  . LEU B  2 226 ? -33.120 -10.022 18.307   1.00 152.44 ? 336  LEU B CG  1 
ATOM   6318  C  CD1 . LEU B  2 226 ? -34.512 -9.457  18.148   1.00 193.26 ? 336  LEU B CD1 1 
ATOM   6319  C  CD2 . LEU B  2 226 ? -32.482 -9.482  19.554   1.00 144.74 ? 336  LEU B CD2 1 
ATOM   6320  N  N   . GLN B  2 227 ? -36.307 -12.631 17.535   1.00 176.39 ? 337  GLN B N   1 
ATOM   6321  C  CA  . GLN B  2 227 ? -37.046 -13.296 16.476   1.00 185.65 ? 337  GLN B CA  1 
ATOM   6322  C  C   . GLN B  2 227 ? -37.612 -12.231 15.554   1.00 194.29 ? 337  GLN B C   1 
ATOM   6323  O  O   . GLN B  2 227 ? -37.535 -11.035 15.843   1.00 193.54 ? 337  GLN B O   1 
ATOM   6324  C  CB  . GLN B  2 227 ? -38.165 -14.177 17.031   1.00 206.17 ? 337  GLN B CB  1 
ATOM   6325  C  CG  . GLN B  2 227 ? -37.668 -15.380 17.803   1.00 195.13 ? 337  GLN B CG  1 
ATOM   6326  C  CD  . GLN B  2 227 ? -38.796 -16.302 18.207   1.00 216.85 ? 337  GLN B CD  1 
ATOM   6327  O  OE1 . GLN B  2 227 ? -39.973 -15.981 18.010   1.00 229.57 ? 337  GLN B OE1 1 
ATOM   6328  N  NE2 . GLN B  2 227 ? -38.452 -17.436 18.810   1.00 196.74 ? 337  GLN B NE2 1 
ATOM   6329  N  N   . LYS B  2 228 ? -38.186 -12.674 14.430   1.00 203.10 ? 338  LYS B N   1 
ATOM   6330  C  CA  . LYS B  2 228 ? -38.837 -11.735 13.520   1.00 215.95 ? 338  LYS B CA  1 
ATOM   6331  C  C   . LYS B  2 228 ? -39.961 -10.984 14.219   1.00 220.87 ? 338  LYS B C   1 
ATOM   6332  O  O   . LYS B  2 228 ? -40.107 -9.767  14.050   1.00 225.24 ? 338  LYS B O   1 
ATOM   6333  C  CB  . LYS B  2 228 ? -39.365 -12.465 12.286   1.00 222.26 ? 338  LYS B CB  1 
ATOM   6334  C  CG  . LYS B  2 228 ? -38.281 -13.036 11.394   1.00 216.17 ? 338  LYS B CG  1 
ATOM   6335  C  CD  . LYS B  2 228 ? -38.884 -13.697 10.172   1.00 226.55 ? 338  LYS B CD  1 
ATOM   6336  C  CE  . LYS B  2 228 ? -37.809 -14.255 9.261    1.00 222.90 ? 338  LYS B CE  1 
ATOM   6337  N  NZ  . LYS B  2 228 ? -38.406 -14.904 8.062    1.00 238.67 ? 338  LYS B NZ  1 
ATOM   6338  N  N   . ASP B  2 229 ? -40.775 -11.695 14.997   1.00 224.77 ? 339  ASP B N   1 
ATOM   6339  C  CA  . ASP B  2 229 ? -41.753 -11.062 15.880   1.00 231.16 ? 339  ASP B CA  1 
ATOM   6340  C  C   . ASP B  2 229 ? -41.036 -10.735 17.180   1.00 220.07 ? 339  ASP B C   1 
ATOM   6341  O  O   . ASP B  2 229 ? -41.012 -11.525 18.123   1.00 216.12 ? 339  ASP B O   1 
ATOM   6342  C  CB  . ASP B  2 229 ? -42.958 -11.964 16.100   1.00 241.44 ? 339  ASP B CB  1 
ATOM   6343  C  CG  . ASP B  2 229 ? -43.824 -12.076 14.868   1.00 254.61 ? 339  ASP B CG  1 
ATOM   6344  O  OD1 . ASP B  2 229 ? -43.918 -11.082 14.116   1.00 259.15 ? 339  ASP B OD1 1 
ATOM   6345  O  OD2 . ASP B  2 229 ? -44.404 -13.156 14.645   1.00 270.46 ? 339  ASP B OD2 1 
ATOM   6346  N  N   . SER B  2 230 ? -40.444 -9.543  17.227   1.00 215.55 ? 340  SER B N   1 
ATOM   6347  C  CA  . SER B  2 230 ? -39.628 -9.138  18.364   1.00 214.54 ? 340  SER B CA  1 
ATOM   6348  C  C   . SER B  2 230 ? -40.478 -8.781  19.579   1.00 228.08 ? 340  SER B C   1 
ATOM   6349  O  O   . SER B  2 230 ? -39.975 -8.178  20.533   1.00 231.57 ? 340  SER B O   1 
ATOM   6350  C  CB  . SER B  2 230 ? -38.729 -7.960  17.964   1.00 209.92 ? 340  SER B CB  1 
ATOM   6351  O  OG  . SER B  2 230 ? -39.480 -6.891  17.403   1.00 229.13 ? 340  SER B OG  1 
ATOM   6352  N  N   . GLY B  2 231 ? -41.756 -9.169  19.577   1.00 220.51 ? 341  GLY B N   1 
ATOM   6353  C  CA  . GLY B  2 231 ? -42.577 -8.988  20.762   1.00 225.05 ? 341  GLY B CA  1 
ATOM   6354  C  C   . GLY B  2 231 ? -42.150 -9.853  21.922   1.00 217.02 ? 341  GLY B C   1 
ATOM   6355  O  O   . GLY B  2 231 ? -42.613 -9.626  23.049   1.00 218.83 ? 341  GLY B O   1 
ATOM   6356  N  N   . ASN B  2 232 ? -41.273 -10.828 21.647   1.00 208.72 ? 342  ASN B N   1 
ATOM   6357  C  CA  . ASN B  2 232 ? -40.698 -11.690 22.673   1.00 200.29 ? 342  ASN B CA  1 
ATOM   6358  C  C   . ASN B  2 232 ? -39.957 -10.861 23.722   1.00 191.62 ? 342  ASN B C   1 
ATOM   6359  O  O   . ASN B  2 232 ? -40.168 -11.032 24.926   1.00 190.84 ? 342  ASN B O   1 
ATOM   6360  C  CB  . ASN B  2 232 ? -39.739 -12.718 22.012   1.00 192.73 ? 342  ASN B CB  1 
ATOM   6361  C  CG  . ASN B  2 232 ? -40.501 -13.907 21.230   1.00 205.16 ? 342  ASN B CG  1 
ATOM   6362  O  OD1 . ASN B  2 232 ? -41.728 -14.195 21.442   1.00 235.35 ? 342  ASN B OD1 1 
ATOM   6363  N  ND2 . ASN B  2 232 ? -39.734 -14.597 20.336   1.00 198.40 ? 342  ASN B ND2 1 
ATOM   6364  N  N   . ILE B  2 233 ? -39.138 -9.903  23.278   1.00 186.11 ? 343  ILE B N   1 
ATOM   6365  C  CA  . ILE B  2 233 ? -38.400 -9.044  24.204   1.00 189.70 ? 343  ILE B CA  1 
ATOM   6366  C  C   . ILE B  2 233 ? -39.340 -8.093  24.936   1.00 190.22 ? 343  ILE B C   1 
ATOM   6367  O  O   . ILE B  2 233 ? -39.075 -7.689  26.077   1.00 200.34 ? 343  ILE B O   1 
ATOM   6368  C  CB  . ILE B  2 233 ? -37.311 -8.289  23.427   1.00 172.45 ? 343  ILE B CB  1 
ATOM   6369  C  CG1 . ILE B  2 233 ? -36.618 -9.268  22.481   1.00 192.86 ? 343  ILE B CG1 1 
ATOM   6370  C  CG2 . ILE B  2 233 ? -36.302 -7.687  24.387   1.00 162.43 ? 343  ILE B CG2 1 
ATOM   6371  C  CD1 . ILE B  2 233 ? -35.539 -8.664  21.633   1.00 190.28 ? 343  ILE B CD1 1 
ATOM   6372  N  N   . LEU B  2 234 ? -40.447 -7.722  24.301   1.00 197.62 ? 344  LEU B N   1 
ATOM   6373  C  CA  . LEU B  2 234 ? -41.416 -6.881  24.978   1.00 206.03 ? 344  LEU B CA  1 
ATOM   6374  C  C   . LEU B  2 234 ? -42.030 -7.612  26.158   1.00 208.52 ? 344  LEU B C   1 
ATOM   6375  O  O   . LEU B  2 234 ? -42.306 -6.995  27.190   1.00 209.96 ? 344  LEU B O   1 
ATOM   6376  C  CB  . LEU B  2 234 ? -42.490 -6.449  23.984   1.00 218.89 ? 344  LEU B CB  1 
ATOM   6377  C  CG  . LEU B  2 234 ? -41.957 -5.668  22.781   1.00 217.90 ? 344  LEU B CG  1 
ATOM   6378  C  CD1 . LEU B  2 234 ? -43.093 -5.145  21.925   1.00 231.80 ? 344  LEU B CD1 1 
ATOM   6379  C  CD2 . LEU B  2 234 ? -41.050 -4.534  23.223   1.00 210.26 ? 344  LEU B CD2 1 
ATOM   6380  N  N   . GLN B  2 235 ? -42.215 -8.930  26.034   1.00 209.19 ? 345  GLN B N   1 
ATOM   6381  C  CA  . GLN B  2 235 ? -42.762 -9.713  27.138   1.00 228.14 ? 345  GLN B CA  1 
ATOM   6382  C  C   . GLN B  2 235 ? -41.840 -9.690  28.351   1.00 227.90 ? 345  GLN B C   1 
ATOM   6383  O  O   . GLN B  2 235 ? -42.310 -9.794  29.490   1.00 261.78 ? 345  GLN B O   1 
ATOM   6384  C  CB  . GLN B  2 235 ? -43.015 -11.157 26.691   1.00 222.11 ? 345  GLN B CB  1 
ATOM   6385  C  CG  . GLN B  2 235 ? -44.222 -11.352 25.779   1.00 227.79 ? 345  GLN B CG  1 
ATOM   6386  C  CD  . GLN B  2 235 ? -44.506 -12.822 25.488   1.00 230.82 ? 345  GLN B CD  1 
ATOM   6387  O  OE1 . GLN B  2 235 ? -43.879 -13.714 26.062   1.00 223.31 ? 345  GLN B OE1 1 
ATOM   6388  N  NE2 . GLN B  2 235 ? -45.449 -13.077 24.587   1.00 244.90 ? 345  GLN B NE2 1 
ATOM   6389  N  N   . LEU B  2 236 ? -40.531 -9.559  28.129   1.00 199.12 ? 346  LEU B N   1 
ATOM   6390  C  CA  . LEU B  2 236 ? -39.597 -9.400  29.240   1.00 211.53 ? 346  LEU B CA  1 
ATOM   6391  C  C   . LEU B  2 236 ? -39.910 -8.139  30.034   1.00 200.14 ? 346  LEU B C   1 
ATOM   6392  O  O   . LEU B  2 236 ? -40.055 -8.176  31.262   1.00 194.15 ? 346  LEU B O   1 
ATOM   6393  C  CB  . LEU B  2 236 ? -38.165 -9.352  28.709   1.00 185.74 ? 346  LEU B CB  1 
ATOM   6394  C  CG  . LEU B  2 236 ? -37.566 -10.661 28.204   1.00 172.53 ? 346  LEU B CG  1 
ATOM   6395  C  CD1 . LEU B  2 236 ? -36.305 -10.377 27.435   1.00 163.64 ? 346  LEU B CD1 1 
ATOM   6396  C  CD2 . LEU B  2 236 ? -37.258 -11.567 29.374   1.00 169.26 ? 346  LEU B CD2 1 
ATOM   6397  N  N   . ILE B  2 237 ? -40.005 -7.006  29.341   1.00 185.61 ? 347  ILE B N   1 
ATOM   6398  C  CA  . ILE B  2 237 ? -40.139 -5.721  30.013   1.00 187.59 ? 347  ILE B CA  1 
ATOM   6399  C  C   . ILE B  2 237 ? -41.480 -5.622  30.736   1.00 198.94 ? 347  ILE B C   1 
ATOM   6400  O  O   . ILE B  2 237 ? -41.555 -5.106  31.857   1.00 199.45 ? 347  ILE B O   1 
ATOM   6401  C  CB  . ILE B  2 237 ? -39.940 -4.591  28.990   1.00 188.91 ? 347  ILE B CB  1 
ATOM   6402  C  CG1 . ILE B  2 237 ? -38.757 -4.929  28.076   1.00 179.57 ? 347  ILE B CG1 1 
ATOM   6403  C  CG2 . ILE B  2 237 ? -39.676 -3.285  29.701   1.00 187.87 ? 347  ILE B CG2 1 
ATOM   6404  C  CD1 . ILE B  2 237 ? -38.481 -3.898  27.000   1.00 180.85 ? 347  ILE B CD1 1 
ATOM   6405  N  N   . ILE B  2 238 ? -42.557 -6.112  30.108   1.00 210.44 ? 348  ILE B N   1 
ATOM   6406  C  CA  . ILE B  2 238 ? -43.886 -6.065  30.722   1.00 225.09 ? 348  ILE B CA  1 
ATOM   6407  C  C   . ILE B  2 238 ? -43.929 -6.912  31.989   1.00 225.13 ? 348  ILE B C   1 
ATOM   6408  O  O   . ILE B  2 238 ? -44.541 -6.527  32.994   1.00 227.41 ? 348  ILE B O   1 
ATOM   6409  C  CB  . ILE B  2 238 ? -44.958 -6.515  29.714   1.00 232.70 ? 348  ILE B CB  1 
ATOM   6410  C  CG1 . ILE B  2 238 ? -44.930 -5.621  28.475   1.00 235.29 ? 348  ILE B CG1 1 
ATOM   6411  C  CG2 . ILE B  2 238 ? -46.336 -6.490  30.358   1.00 246.15 ? 348  ILE B CG2 1 
ATOM   6412  C  CD1 . ILE B  2 238 ? -45.962 -5.985  27.434   1.00 247.14 ? 348  ILE B CD1 1 
ATOM   6413  N  N   . SER B  2 239 ? -43.302 -8.085  31.957   1.00 252.63 ? 349  SER B N   1 
ATOM   6414  C  CA  . SER B  2 239 ? -43.188 -8.919  33.144   1.00 241.31 ? 349  SER B CA  1 
ATOM   6415  C  C   . SER B  2 239 ? -42.024 -8.496  34.033   1.00 210.11 ? 349  SER B C   1 
ATOM   6416  O  O   . SER B  2 239 ? -41.710 -9.193  35.004   1.00 201.48 ? 349  SER B O   1 
ATOM   6417  C  CB  . SER B  2 239 ? -43.041 -10.390 32.744   1.00 241.61 ? 349  SER B CB  1 
ATOM   6418  O  OG  . SER B  2 239 ? -41.945 -10.573 31.862   1.00 226.40 ? 349  SER B OG  1 
ATOM   6419  N  N   . ALA B  2 240 ? -41.377 -7.374  33.714   1.00 197.87 ? 350  ALA B N   1 
ATOM   6420  C  CA  . ALA B  2 240 ? -40.395 -6.754  34.587   1.00 190.18 ? 350  ALA B CA  1 
ATOM   6421  C  C   . ALA B  2 240 ? -40.951 -5.520  35.279   1.00 196.30 ? 350  ALA B C   1 
ATOM   6422  O  O   . ALA B  2 240 ? -40.304 -4.985  36.186   1.00 192.01 ? 350  ALA B O   1 
ATOM   6423  C  CB  . ALA B  2 240 ? -39.130 -6.384  33.797   1.00 178.98 ? 350  ALA B CB  1 
ATOM   6424  N  N   . TYR B  2 241 ? -42.143 -5.083  34.894   1.00 210.10 ? 351  TYR B N   1 
ATOM   6425  C  CA  . TYR B  2 241 ? -42.851 -4.001  35.555   1.00 233.32 ? 351  TYR B CA  1 
ATOM   6426  C  C   . TYR B  2 241 ? -43.633 -4.503  36.762   1.00 237.24 ? 351  TYR B C   1 
ATOM   6427  O  O   . TYR B  2 241 ? -44.449 -3.762  37.320   1.00 231.40 ? 351  TYR B O   1 
ATOM   6428  C  CB  . TYR B  2 241 ? -43.786 -3.315  34.551   1.00 248.53 ? 351  TYR B CB  1 
ATOM   6429  C  CG  . TYR B  2 241 ? -44.264 -1.926  34.929   1.00 253.57 ? 351  TYR B CG  1 
ATOM   6430  C  CD1 . TYR B  2 241 ? -43.397 -0.838  34.889   1.00 222.27 ? 351  TYR B CD1 1 
ATOM   6431  C  CD2 . TYR B  2 241 ? -45.591 -1.696  35.279   1.00 241.86 ? 351  TYR B CD2 1 
ATOM   6432  C  CE1 . TYR B  2 241 ? -43.833 0.431   35.215   1.00 229.79 ? 351  TYR B CE1 1 
ATOM   6433  C  CE2 . TYR B  2 241 ? -46.034 -0.427  35.607   1.00 248.16 ? 351  TYR B CE2 1 
ATOM   6434  C  CZ  . TYR B  2 241 ? -45.149 0.631   35.572   1.00 253.17 ? 351  TYR B CZ  1 
ATOM   6435  O  OH  . TYR B  2 241 ? -45.576 1.899   35.894   1.00 254.80 ? 351  TYR B OH  1 
ATOM   6436  N  N   . GLU B  2 242 ? -43.411 -5.759  37.158   1.00 220.40 ? 352  GLU B N   1 
ATOM   6437  C  CA  . GLU B  2 242 ? -44.080 -6.317  38.328   1.00 227.95 ? 352  GLU B CA  1 
ATOM   6438  C  C   . GLU B  2 242 ? -43.695 -5.571  39.598   1.00 226.38 ? 352  GLU B C   1 
ATOM   6439  O  O   . GLU B  2 242 ? -44.532 -5.368  40.485   1.00 242.63 ? 352  GLU B O   1 
ATOM   6440  C  CB  . GLU B  2 242 ? -43.730 -7.797  38.456   1.00 224.40 ? 352  GLU B CB  1 
ATOM   6441  C  CG  . GLU B  2 242 ? -44.128 -8.628  37.253   1.00 246.60 ? 352  GLU B CG  1 
ATOM   6442  C  CD  . GLU B  2 242 ? -43.567 -10.034 37.313   1.00 258.19 ? 352  GLU B CD  1 
ATOM   6443  O  OE1 . GLU B  2 242 ? -42.738 -10.304 38.211   1.00 253.29 ? 352  GLU B OE1 1 
ATOM   6444  O  OE2 . GLU B  2 242 ? -43.950 -10.866 36.464   1.00 268.36 ? 352  GLU B OE2 1 
ATOM   6445  N  N   . GLU B  2 243 ? -42.428 -5.164  39.702   1.00 243.75 ? 353  GLU B N   1 
ATOM   6446  C  CA  . GLU B  2 243 ? -41.901 -4.443  40.857   1.00 245.53 ? 353  GLU B CA  1 
ATOM   6447  C  C   . GLU B  2 243 ? -42.123 -5.224  42.149   1.00 253.88 ? 353  GLU B C   1 
ATOM   6448  O  O   . GLU B  2 243 ? -41.548 -6.303  42.331   1.00 258.31 ? 353  GLU B O   1 
ATOM   6449  C  CB  . GLU B  2 243 ? -42.526 -3.048  40.948   1.00 238.78 ? 353  GLU B CB  1 
ATOM   6450  C  CG  . GLU B  2 243 ? -42.388 -2.222  39.673   1.00 231.54 ? 353  GLU B CG  1 
ATOM   6451  C  CD  . GLU B  2 243 ? -42.817 -0.778  39.855   1.00 237.81 ? 353  GLU B CD  1 
ATOM   6452  O  OE1 . GLU B  2 243 ? -43.772 -0.349  39.175   1.00 250.22 ? 353  GLU B OE1 1 
ATOM   6453  O  OE2 . GLU B  2 243 ? -42.213 -0.078  40.694   1.00 245.09 ? 353  GLU B OE2 1 
ATOM   6454  N  N   . LEU B  2 244 ? -42.948 -4.685  43.046   1.00 249.74 ? 354  LEU B N   1 
ATOM   6455  C  CA  . LEU B  2 244 ? -43.244 -5.303  44.343   1.00 243.32 ? 354  LEU B CA  1 
ATOM   6456  C  C   . LEU B  2 244 ? -41.981 -5.578  45.155   1.00 241.79 ? 354  LEU B C   1 
ATOM   6457  O  O   . LEU B  2 244 ? -41.994 -6.390  46.082   1.00 229.36 ? 354  LEU B O   1 
ATOM   6458  C  CB  . LEU B  2 244 ? -44.032 -6.604  44.157   1.00 241.26 ? 354  LEU B CB  1 
ATOM   6459  C  CG  . LEU B  2 244 ? -45.434 -6.481  43.558   1.00 253.59 ? 354  LEU B CG  1 
ATOM   6460  C  CD1 . LEU B  2 244 ? -46.105 -7.844  43.446   1.00 259.86 ? 354  LEU B CD1 1 
ATOM   6461  C  CD2 . LEU B  2 244 ? -46.273 -5.532  44.393   1.00 264.50 ? 354  LEU B CD2 1 
ATOM   6462  N  N   . ASP C  3 10  ? -61.596 14.308  -51.805  1.00 265.53 ? 8    ASP C N   1 
ATOM   6463  C  CA  . ASP C  3 10  ? -60.771 14.664  -50.658  1.00 261.69 ? 8    ASP C CA  1 
ATOM   6464  C  C   . ASP C  3 10  ? -59.868 13.505  -50.261  1.00 260.91 ? 8    ASP C C   1 
ATOM   6465  O  O   . ASP C  3 10  ? -58.813 13.704  -49.664  1.00 250.76 ? 8    ASP C O   1 
ATOM   6466  C  CB  . ASP C  3 10  ? -61.645 15.085  -49.476  1.00 252.59 ? 8    ASP C CB  1 
ATOM   6467  C  CG  . ASP C  3 10  ? -62.301 16.434  -49.693  1.00 257.03 ? 8    ASP C CG  1 
ATOM   6468  O  OD1 . ASP C  3 10  ? -61.667 17.303  -50.329  1.00 266.89 ? 8    ASP C OD1 1 
ATOM   6469  O  OD2 . ASP C  3 10  ? -63.448 16.627  -49.236  1.00 254.13 ? 8    ASP C OD2 1 
ATOM   6470  N  N   . MET C  3 11  ? -60.288 12.291  -50.600  1.00 277.66 ? 9    MET C N   1 
ATOM   6471  C  CA  . MET C  3 11  ? -59.486 11.109  -50.322  1.00 277.87 ? 9    MET C CA  1 
ATOM   6472  C  C   . MET C  3 11  ? -58.493 10.805  -51.434  1.00 276.44 ? 9    MET C C   1 
ATOM   6473  O  O   . MET C  3 11  ? -57.498 10.110  -51.194  1.00 263.98 ? 9    MET C O   1 
ATOM   6474  C  CB  . MET C  3 11  ? -60.403 9.903   -50.088  1.00 284.96 ? 9    MET C CB  1 
ATOM   6475  C  CG  . MET C  3 11  ? -59.697 8.662   -49.573  1.00 281.69 ? 9    MET C CG  1 
ATOM   6476  S  SD  . MET C  3 11  ? -58.904 8.899   -47.969  1.00 275.52 ? 9    MET C SD  1 
ATOM   6477  C  CE  . MET C  3 11  ? -60.330 9.140   -46.916  1.00 273.01 ? 9    MET C CE  1 
ATOM   6478  N  N   . GLU C  3 12  ? -58.736 11.312  -52.641  1.00 293.93 ? 10   GLU C N   1 
ATOM   6479  C  CA  . GLU C  3 12  ? -57.781 11.185  -53.732  1.00 295.58 ? 10   GLU C CA  1 
ATOM   6480  C  C   . GLU C  3 12  ? -56.783 12.332  -53.768  1.00 298.58 ? 10   GLU C C   1 
ATOM   6481  O  O   . GLU C  3 12  ? -55.738 12.208  -54.418  1.00 298.77 ? 10   GLU C O   1 
ATOM   6482  C  CB  . GLU C  3 12  ? -58.515 11.101  -55.077  1.00 301.13 ? 10   GLU C CB  1 
ATOM   6483  C  CG  . GLU C  3 12  ? -59.301 9.814   -55.286  1.00 300.79 ? 10   GLU C CG  1 
ATOM   6484  C  CD  . GLU C  3 12  ? -58.426 8.638   -55.694  1.00 301.28 ? 10   GLU C CD  1 
ATOM   6485  O  OE1 . GLU C  3 12  ? -57.280 8.863   -56.135  1.00 306.90 ? 10   GLU C OE1 1 
ATOM   6486  O  OE2 . GLU C  3 12  ? -58.891 7.484   -55.574  1.00 299.52 ? 10   GLU C OE2 1 
ATOM   6487  N  N   . LEU C  3 13  ? -57.083 13.443  -53.092  1.00 289.01 ? 11   LEU C N   1 
ATOM   6488  C  CA  . LEU C  3 13  ? -56.136 14.545  -53.011  1.00 271.12 ? 11   LEU C CA  1 
ATOM   6489  C  C   . LEU C  3 13  ? -55.057 14.277  -51.974  1.00 254.23 ? 11   LEU C C   1 
ATOM   6490  O  O   . LEU C  3 13  ? -53.945 14.805  -52.090  1.00 248.64 ? 11   LEU C O   1 
ATOM   6491  C  CB  . LEU C  3 13  ? -56.869 15.845  -52.683  1.00 264.81 ? 11   LEU C CB  1 
ATOM   6492  C  CG  . LEU C  3 13  ? -58.023 16.227  -53.611  1.00 258.32 ? 11   LEU C CG  1 
ATOM   6493  C  CD1 . LEU C  3 13  ? -58.670 17.520  -53.145  1.00 253.40 ? 11   LEU C CD1 1 
ATOM   6494  C  CD2 . LEU C  3 13  ? -57.530 16.351  -55.043  1.00 264.86 ? 11   LEU C CD2 1 
ATOM   6495  N  N   . VAL C  3 14  ? -55.369 13.463  -50.962  1.00 258.60 ? 12   VAL C N   1 
ATOM   6496  C  CA  . VAL C  3 14  ? -54.380 13.121  -49.948  1.00 259.41 ? 12   VAL C CA  1 
ATOM   6497  C  C   . VAL C  3 14  ? -53.281 12.257  -50.550  1.00 269.81 ? 12   VAL C C   1 
ATOM   6498  O  O   . VAL C  3 14  ? -52.097 12.418  -50.230  1.00 270.57 ? 12   VAL C O   1 
ATOM   6499  C  CB  . VAL C  3 14  ? -55.062 12.421  -48.760  1.00 256.97 ? 12   VAL C CB  1 
ATOM   6500  C  CG1 . VAL C  3 14  ? -54.027 12.006  -47.733  1.00 255.39 ? 12   VAL C CG1 1 
ATOM   6501  C  CG2 . VAL C  3 14  ? -56.099 13.329  -48.128  1.00 254.87 ? 12   VAL C CG2 1 
ATOM   6502  N  N   . LYS C  3 15  ? -53.651 11.340  -51.447  1.00 276.96 ? 13   LYS C N   1 
ATOM   6503  C  CA  . LYS C  3 15  ? -52.691 10.375  -51.971  1.00 281.06 ? 13   LYS C CA  1 
ATOM   6504  C  C   . LYS C  3 15  ? -51.721 11.008  -52.964  1.00 279.23 ? 13   LYS C C   1 
ATOM   6505  O  O   . LYS C  3 15  ? -50.579 10.550  -53.084  1.00 272.13 ? 13   LYS C O   1 
ATOM   6506  C  CB  . LYS C  3 15  ? -53.441 9.211   -52.619  1.00 285.77 ? 13   LYS C CB  1 
ATOM   6507  C  CG  . LYS C  3 15  ? -54.466 8.558   -51.702  1.00 284.14 ? 13   LYS C CG  1 
ATOM   6508  C  CD  . LYS C  3 15  ? -55.251 7.468   -52.411  1.00 278.74 ? 13   LYS C CD  1 
ATOM   6509  C  CE  . LYS C  3 15  ? -56.214 6.784   -51.453  1.00 270.82 ? 13   LYS C CE  1 
ATOM   6510  N  NZ  . LYS C  3 15  ? -56.979 5.695   -52.115  1.00 272.30 ? 13   LYS C NZ  1 
ATOM   6511  N  N   . ARG C  3 16  ? -52.142 12.060  -53.676  1.00 281.51 ? 14   ARG C N   1 
ATOM   6512  C  CA  . ARG C  3 16  ? -51.303 12.644  -54.721  1.00 275.94 ? 14   ARG C CA  1 
ATOM   6513  C  C   . ARG C  3 16  ? -50.126 13.441  -54.165  1.00 272.67 ? 14   ARG C C   1 
ATOM   6514  O  O   . ARG C  3 16  ? -49.136 13.633  -54.879  1.00 269.34 ? 14   ARG C O   1 
ATOM   6515  C  CB  . ARG C  3 16  ? -52.144 13.541  -55.633  1.00 272.12 ? 14   ARG C CB  1 
ATOM   6516  C  CG  . ARG C  3 16  ? -53.163 12.802  -56.491  1.00 268.27 ? 14   ARG C CG  1 
ATOM   6517  C  CD  . ARG C  3 16  ? -52.483 11.829  -57.439  1.00 263.49 ? 14   ARG C CD  1 
ATOM   6518  N  NE  . ARG C  3 16  ? -51.460 12.486  -58.245  1.00 262.33 ? 14   ARG C NE  1 
ATOM   6519  C  CZ  . ARG C  3 16  ? -50.710 11.867  -59.150  1.00 262.98 ? 14   ARG C CZ  1 
ATOM   6520  N  NH1 . ARG C  3 16  ? -50.867 10.569  -59.370  1.00 264.85 ? 14   ARG C NH1 1 
ATOM   6521  N  NH2 . ARG C  3 16  ? -49.802 12.546  -59.836  1.00 262.63 ? 14   ARG C NH2 1 
ATOM   6522  N  N   . LYS C  3 17  ? -50.207 13.913  -52.917  1.00 274.21 ? 15   LYS C N   1 
ATOM   6523  C  CA  . LYS C  3 17  ? -49.121 14.711  -52.354  1.00 269.15 ? 15   LYS C CA  1 
ATOM   6524  C  C   . LYS C  3 17  ? -47.926 13.848  -51.958  1.00 260.56 ? 15   LYS C C   1 
ATOM   6525  O  O   . LYS C  3 17  ? -46.776 14.271  -52.118  1.00 260.46 ? 15   LYS C O   1 
ATOM   6526  C  CB  . LYS C  3 17  ? -49.623 15.509  -51.152  1.00 270.08 ? 15   LYS C CB  1 
ATOM   6527  C  CG  . LYS C  3 17  ? -48.528 16.272  -50.418  1.00 263.33 ? 15   LYS C CG  1 
ATOM   6528  C  CD  . LYS C  3 17  ? -49.103 17.266  -49.427  1.00 262.36 ? 15   LYS C CD  1 
ATOM   6529  C  CE  . LYS C  3 17  ? -49.816 18.397  -50.145  1.00 266.06 ? 15   LYS C CE  1 
ATOM   6530  N  NZ  . LYS C  3 17  ? -50.296 19.441  -49.199  1.00 259.94 ? 15   LYS C NZ  1 
ATOM   6531  N  N   . ARG C  3 18  ? -48.176 12.639  -51.442  1.00 254.93 ? 16   ARG C N   1 
ATOM   6532  C  CA  . ARG C  3 18  ? -47.082 11.752  -51.051  1.00 254.90 ? 16   ARG C CA  1 
ATOM   6533  C  C   . ARG C  3 18  ? -46.267 11.291  -52.251  1.00 260.74 ? 16   ARG C C   1 
ATOM   6534  O  O   . ARG C  3 18  ? -45.052 11.093  -52.133  1.00 263.70 ? 16   ARG C O   1 
ATOM   6535  C  CB  . ARG C  3 18  ? -47.627 10.536  -50.303  1.00 254.55 ? 16   ARG C CB  1 
ATOM   6536  C  CG  . ARG C  3 18  ? -46.548 9.563   -49.833  1.00 252.41 ? 16   ARG C CG  1 
ATOM   6537  C  CD  . ARG C  3 18  ? -47.144 8.313   -49.204  1.00 254.72 ? 16   ARG C CD  1 
ATOM   6538  N  NE  . ARG C  3 18  ? -46.147 7.540   -48.466  1.00 250.04 ? 16   ARG C NE  1 
ATOM   6539  C  CZ  . ARG C  3 18  ? -45.354 6.625   -49.014  1.00 251.70 ? 16   ARG C CZ  1 
ATOM   6540  N  NH1 . ARG C  3 18  ? -45.436 6.367   -50.311  1.00 266.78 ? 16   ARG C NH1 1 
ATOM   6541  N  NH2 . ARG C  3 18  ? -44.477 5.970   -48.266  1.00 248.56 ? 16   ARG C NH2 1 
ATOM   6542  N  N   . ILE C  3 19  ? -46.911 11.112  -53.407  1.00 262.37 ? 17   ILE C N   1 
ATOM   6543  C  CA  . ILE C  3 19  ? -46.211 10.598  -54.581  1.00 263.07 ? 17   ILE C CA  1 
ATOM   6544  C  C   . ILE C  3 19  ? -45.095 11.547  -54.999  1.00 264.47 ? 17   ILE C C   1 
ATOM   6545  O  O   . ILE C  3 19  ? -43.982 11.115  -55.325  1.00 258.90 ? 17   ILE C O   1 
ATOM   6546  C  CB  . ILE C  3 19  ? -47.208 10.349  -55.728  1.00 276.03 ? 17   ILE C CB  1 
ATOM   6547  C  CG1 . ILE C  3 19  ? -48.259 9.321   -55.299  1.00 279.21 ? 17   ILE C CG1 1 
ATOM   6548  C  CG2 . ILE C  3 19  ? -46.480 9.881   -56.980  1.00 286.12 ? 17   ILE C CG2 1 
ATOM   6549  C  CD1 . ILE C  3 19  ? -49.289 9.003   -56.368  1.00 286.90 ? 17   ILE C CD1 1 
ATOM   6550  N  N   . GLU C  3 20  ? -45.368 12.856  -54.992  1.00 280.48 ? 18   GLU C N   1 
ATOM   6551  C  CA  . GLU C  3 20  ? -44.341 13.827  -55.354  1.00 285.35 ? 18   GLU C CA  1 
ATOM   6552  C  C   . GLU C  3 20  ? -43.237 13.914  -54.310  1.00 288.81 ? 18   GLU C C   1 
ATOM   6553  O  O   . GLU C  3 20  ? -42.138 14.386  -54.626  1.00 288.61 ? 18   GLU C O   1 
ATOM   6554  C  CB  . GLU C  3 20  ? -44.965 15.207  -55.578  1.00 283.79 ? 18   GLU C CB  1 
ATOM   6555  C  CG  . GLU C  3 20  ? -45.766 15.323  -56.869  1.00 280.03 ? 18   GLU C CG  1 
ATOM   6556  C  CD  . GLU C  3 20  ? -44.909 15.142  -58.111  1.00 276.67 ? 18   GLU C CD  1 
ATOM   6557  O  OE1 . GLU C  3 20  ? -43.718 15.520  -58.080  1.00 266.06 ? 18   GLU C OE1 1 
ATOM   6558  O  OE2 . GLU C  3 20  ? -45.426 14.616  -59.120  1.00 283.07 ? 18   GLU C OE2 1 
ATOM   6559  N  N   . ALA C  3 21  ? -43.503 13.478  -53.076  1.00 286.26 ? 19   ALA C N   1 
ATOM   6560  C  CA  . ALA C  3 21  ? -42.437 13.354  -52.090  1.00 276.72 ? 19   ALA C CA  1 
ATOM   6561  C  C   . ALA C  3 21  ? -41.632 12.079  -52.299  1.00 279.60 ? 19   ALA C C   1 
ATOM   6562  O  O   . ALA C  3 21  ? -40.444 12.039  -51.961  1.00 279.95 ? 19   ALA C O   1 
ATOM   6563  C  CB  . ALA C  3 21  ? -43.016 13.389  -50.673  1.00 265.91 ? 19   ALA C CB  1 
ATOM   6564  N  N   . ILE C  3 22  ? -42.258 11.037  -52.851  1.00 277.50 ? 20   ILE C N   1 
ATOM   6565  C  CA  . ILE C  3 22  ? -41.526 9.826   -53.208  1.00 270.16 ? 20   ILE C CA  1 
ATOM   6566  C  C   . ILE C  3 22  ? -40.607 10.091  -54.394  1.00 266.65 ? 20   ILE C C   1 
ATOM   6567  O  O   . ILE C  3 22  ? -39.472 9.598   -54.443  1.00 259.58 ? 20   ILE C O   1 
ATOM   6568  C  CB  . ILE C  3 22  ? -42.510 8.678   -53.496  1.00 266.41 ? 20   ILE C CB  1 
ATOM   6569  C  CG1 . ILE C  3 22  ? -43.243 8.259   -52.219  1.00 267.68 ? 20   ILE C CG1 1 
ATOM   6570  C  CG2 . ILE C  3 22  ? -41.786 7.494   -54.111  1.00 264.17 ? 20   ILE C CG2 1 
ATOM   6571  C  CD1 . ILE C  3 22  ? -42.347 7.622   -51.174  1.00 262.19 ? 20   ILE C CD1 1 
ATOM   6572  N  N   . ARG C  3 23  ? -41.083 10.875  -55.367  1.00 268.31 ? 21   ARG C N   1 
ATOM   6573  C  CA  . ARG C  3 23  ? -40.263 11.232  -56.520  1.00 267.96 ? 21   ARG C CA  1 
ATOM   6574  C  C   . ARG C  3 23  ? -38.989 11.945  -56.086  1.00 270.14 ? 21   ARG C C   1 
ATOM   6575  O  O   . ARG C  3 23  ? -37.887 11.597  -56.525  1.00 273.25 ? 21   ARG C O   1 
ATOM   6576  C  CB  . ARG C  3 23  ? -41.070 12.108  -57.479  1.00 266.97 ? 21   ARG C CB  1 
ATOM   6577  C  CG  . ARG C  3 23  ? -40.247 12.739  -58.589  1.00 266.82 ? 21   ARG C CG  1 
ATOM   6578  C  CD  . ARG C  3 23  ? -41.088 13.701  -59.410  1.00 267.23 ? 21   ARG C CD  1 
ATOM   6579  N  NE  . ARG C  3 23  ? -42.152 13.012  -60.133  1.00 266.03 ? 21   ARG C NE  1 
ATOM   6580  C  CZ  . ARG C  3 23  ? -42.035 12.552  -61.375  1.00 269.88 ? 21   ARG C CZ  1 
ATOM   6581  N  NH1 . ARG C  3 23  ? -40.898 12.708  -62.040  1.00 275.78 ? 21   ARG C NH1 1 
ATOM   6582  N  NH2 . ARG C  3 23  ? -43.056 11.935  -61.956  1.00 266.32 ? 21   ARG C NH2 1 
ATOM   6583  N  N   . GLY C  3 24  ? -39.121 12.951  -55.217  1.00 260.25 ? 22   GLY C N   1 
ATOM   6584  C  CA  . GLY C  3 24  ? -37.953 13.636  -54.692  1.00 253.91 ? 22   GLY C CA  1 
ATOM   6585  C  C   . GLY C  3 24  ? -37.123 12.797  -53.745  1.00 248.82 ? 22   GLY C C   1 
ATOM   6586  O  O   . GLY C  3 24  ? -35.951 13.116  -53.519  1.00 247.72 ? 22   GLY C O   1 
ATOM   6587  N  N   . GLN C  3 25  ? -37.701 11.730  -53.189  1.00 253.04 ? 23   GLN C N   1 
ATOM   6588  C  CA  . GLN C  3 25  ? -36.958 10.851  -52.292  1.00 260.40 ? 23   GLN C CA  1 
ATOM   6589  C  C   . GLN C  3 25  ? -36.095 9.866   -53.072  1.00 255.88 ? 23   GLN C C   1 
ATOM   6590  O  O   . GLN C  3 25  ? -34.891 9.749   -52.820  1.00 252.29 ? 23   GLN C O   1 
ATOM   6591  C  CB  . GLN C  3 25  ? -37.924 10.098  -51.371  1.00 266.69 ? 23   GLN C CB  1 
ATOM   6592  C  CG  . GLN C  3 25  ? -37.242 9.229   -50.319  1.00 264.72 ? 23   GLN C CG  1 
ATOM   6593  C  CD  . GLN C  3 25  ? -38.214 8.316   -49.589  1.00 260.32 ? 23   GLN C CD  1 
ATOM   6594  O  OE1 . GLN C  3 25  ? -39.288 7.998   -50.099  1.00 250.60 ? 23   GLN C OE1 1 
ATOM   6595  N  NE2 . GLN C  3 25  ? -37.838 7.891   -48.387  1.00 260.73 ? 23   GLN C NE2 1 
ATOM   6596  N  N   . ILE C  3 26  ? -36.700 9.151   -54.026  1.00 241.79 ? 24   ILE C N   1 
ATOM   6597  C  CA  . ILE C  3 26  ? -35.972 8.141   -54.793  1.00 239.25 ? 24   ILE C CA  1 
ATOM   6598  C  C   . ILE C  3 26  ? -34.795 8.774   -55.524  1.00 244.82 ? 24   ILE C C   1 
ATOM   6599  O  O   . ILE C  3 26  ? -33.684 8.231   -55.538  1.00 241.78 ? 24   ILE C O   1 
ATOM   6600  C  CB  . ILE C  3 26  ? -36.924 7.429   -55.770  1.00 241.39 ? 24   ILE C CB  1 
ATOM   6601  C  CG1 . ILE C  3 26  ? -38.054 6.734   -55.010  1.00 239.35 ? 24   ILE C CG1 1 
ATOM   6602  C  CG2 . ILE C  3 26  ? -36.161 6.432   -56.623  1.00 249.07 ? 24   ILE C CG2 1 
ATOM   6603  C  CD1 . ILE C  3 26  ? -39.040 6.023   -55.911  1.00 243.20 ? 24   ILE C CD1 1 
ATOM   6604  N  N   . LEU C  3 27  ? -35.025 9.935   -56.146  1.00 265.69 ? 25   LEU C N   1 
ATOM   6605  C  CA  . LEU C  3 27  ? -33.953 10.623  -56.857  1.00 273.86 ? 25   LEU C CA  1 
ATOM   6606  C  C   . LEU C  3 27  ? -32.848 11.070  -55.908  1.00 267.58 ? 25   LEU C C   1 
ATOM   6607  O  O   . LEU C  3 27  ? -31.673 11.096  -56.292  1.00 270.32 ? 25   LEU C O   1 
ATOM   6608  C  CB  . LEU C  3 27  ? -34.519 11.820  -57.623  1.00 281.01 ? 25   LEU C CB  1 
ATOM   6609  C  CG  . LEU C  3 27  ? -35.530 11.510  -58.732  1.00 277.75 ? 25   LEU C CG  1 
ATOM   6610  C  CD1 . LEU C  3 27  ? -36.017 12.795  -59.387  1.00 276.00 ? 25   LEU C CD1 1 
ATOM   6611  C  CD2 . LEU C  3 27  ? -34.936 10.564  -59.767  1.00 276.31 ? 25   LEU C CD2 1 
ATOM   6612  N  N   . SER C  3 28  ? -33.201 11.424  -54.670  1.00 258.26 ? 26   SER C N   1 
ATOM   6613  C  CA  . SER C  3 28  ? -32.191 11.774  -53.679  1.00 255.37 ? 26   SER C CA  1 
ATOM   6614  C  C   . SER C  3 28  ? -31.513 10.540  -53.102  1.00 257.66 ? 26   SER C C   1 
ATOM   6615  O  O   . SER C  3 28  ? -30.329 10.597  -52.749  1.00 261.09 ? 26   SER C O   1 
ATOM   6616  C  CB  . SER C  3 28  ? -32.820 12.594  -52.551  1.00 256.10 ? 26   SER C CB  1 
ATOM   6617  O  OG  . SER C  3 28  ? -33.788 11.830  -51.850  1.00 256.64 ? 26   SER C OG  1 
ATOM   6618  N  N   . LYS C  3 29  ? -32.239 9.427   -52.991  1.00 252.01 ? 27   LYS C N   1 
ATOM   6619  C  CA  . LYS C  3 29  ? -31.632 8.207   -52.473  1.00 252.19 ? 27   LYS C CA  1 
ATOM   6620  C  C   . LYS C  3 29  ? -30.708 7.574   -53.506  1.00 256.91 ? 27   LYS C C   1 
ATOM   6621  O  O   . LYS C  3 29  ? -29.678 6.991   -53.149  1.00 260.65 ? 27   LYS C O   1 
ATOM   6622  C  CB  . LYS C  3 29  ? -32.722 7.226   -52.040  1.00 253.94 ? 27   LYS C CB  1 
ATOM   6623  C  CG  . LYS C  3 29  ? -33.583 7.730   -50.888  1.00 247.31 ? 27   LYS C CG  1 
ATOM   6624  C  CD  . LYS C  3 29  ? -34.716 6.766   -50.577  1.00 250.63 ? 27   LYS C CD  1 
ATOM   6625  C  CE  . LYS C  3 29  ? -34.201 5.495   -49.926  1.00 255.76 ? 27   LYS C CE  1 
ATOM   6626  N  NZ  . LYS C  3 29  ? -33.702 5.747   -48.546  1.00 245.74 ? 27   LYS C NZ  1 
ATOM   6627  N  N   . LEU C  3 30  ? -31.053 7.685   -54.789  1.00 244.05 ? 28   LEU C N   1 
ATOM   6628  C  CA  . LEU C  3 30  ? -30.225 7.182   -55.878  1.00 237.55 ? 28   LEU C CA  1 
ATOM   6629  C  C   . LEU C  3 30  ? -29.213 8.206   -56.374  1.00 241.91 ? 28   LEU C C   1 
ATOM   6630  O  O   . LEU C  3 30  ? -28.416 7.886   -57.264  1.00 241.91 ? 28   LEU C O   1 
ATOM   6631  C  CB  . LEU C  3 30  ? -31.110 6.735   -57.044  1.00 240.40 ? 28   LEU C CB  1 
ATOM   6632  C  CG  . LEU C  3 30  ? -32.077 5.590   -56.755  1.00 240.43 ? 28   LEU C CG  1 
ATOM   6633  C  CD1 . LEU C  3 30  ? -32.929 5.305   -57.977  1.00 246.52 ? 28   LEU C CD1 1 
ATOM   6634  C  CD2 . LEU C  3 30  ? -31.313 4.348   -56.329  1.00 247.13 ? 28   LEU C CD2 1 
ATOM   6635  N  N   . ARG C  3 31  ? -29.225 9.418   -55.816  1.00 258.57 ? 29   ARG C N   1 
ATOM   6636  C  CA  . ARG C  3 31  ? -28.368 10.513  -56.269  1.00 260.04 ? 29   ARG C CA  1 
ATOM   6637  C  C   . ARG C  3 31  ? -28.526 10.748  -57.768  1.00 265.69 ? 29   ARG C C   1 
ATOM   6638  O  O   . ARG C  3 31  ? -27.550 10.936  -58.498  1.00 265.03 ? 29   ARG C O   1 
ATOM   6639  C  CB  . ARG C  3 31  ? -26.904 10.265  -55.903  1.00 249.84 ? 29   ARG C CB  1 
ATOM   6640  C  CG  . ARG C  3 31  ? -26.628 10.265  -54.409  1.00 244.79 ? 29   ARG C CG  1 
ATOM   6641  C  CD  . ARG C  3 31  ? -25.154 10.499  -54.133  1.00 250.76 ? 29   ARG C CD  1 
ATOM   6642  N  NE  . ARG C  3 31  ? -24.752 9.996   -52.823  1.00 261.21 ? 29   ARG C NE  1 
ATOM   6643  C  CZ  . ARG C  3 31  ? -24.686 10.738  -51.723  1.00 260.65 ? 29   ARG C CZ  1 
ATOM   6644  N  NH1 . ARG C  3 31  ? -24.997 12.025  -51.770  1.00 257.29 ? 29   ARG C NH1 1 
ATOM   6645  N  NH2 . ARG C  3 31  ? -24.306 10.191  -50.575  1.00 258.29 ? 29   ARG C NH2 1 
ATOM   6646  N  N   . LEU C  3 32  ? -29.772 10.729  -58.233  1.00 265.96 ? 30   LEU C N   1 
ATOM   6647  C  CA  . LEU C  3 32  ? -30.105 10.981  -59.627  1.00 264.40 ? 30   LEU C CA  1 
ATOM   6648  C  C   . LEU C  3 32  ? -30.898 12.273  -59.743  1.00 266.88 ? 30   LEU C C   1 
ATOM   6649  O  O   . LEU C  3 32  ? -31.727 12.586  -58.882  1.00 270.84 ? 30   LEU C O   1 
ATOM   6650  C  CB  . LEU C  3 32  ? -30.916 9.827   -60.225  1.00 268.97 ? 30   LEU C CB  1 
ATOM   6651  C  CG  . LEU C  3 32  ? -30.196 8.503   -60.469  1.00 275.10 ? 30   LEU C CG  1 
ATOM   6652  C  CD1 . LEU C  3 32  ? -31.147 7.493   -61.094  1.00 275.64 ? 30   LEU C CD1 1 
ATOM   6653  C  CD2 . LEU C  3 32  ? -28.981 8.715   -61.355  1.00 282.02 ? 30   LEU C CD2 1 
ATOM   6654  N  N   . ALA C  3 33  ? -30.637 13.025  -60.807  1.00 265.40 ? 31   ALA C N   1 
ATOM   6655  C  CA  . ALA C  3 33  ? -31.462 14.184  -61.113  1.00 269.72 ? 31   ALA C CA  1 
ATOM   6656  C  C   . ALA C  3 33  ? -32.596 13.838  -62.064  1.00 267.53 ? 31   ALA C C   1 
ATOM   6657  O  O   . ALA C  3 33  ? -33.673 14.439  -61.984  1.00 271.74 ? 31   ALA C O   1 
ATOM   6658  C  CB  . ALA C  3 33  ? -30.604 15.306  -61.710  1.00 277.54 ? 31   ALA C CB  1 
ATOM   6659  N  N   . SER C  3 34  ? -32.388 12.866  -62.946  1.00 270.32 ? 32   SER C N   1 
ATOM   6660  C  CA  . SER C  3 34  ? -33.395 12.483  -63.919  1.00 279.85 ? 32   SER C CA  1 
ATOM   6661  C  C   . SER C  3 34  ? -33.187 11.020  -64.276  1.00 282.92 ? 32   SER C C   1 
ATOM   6662  O  O   . SER C  3 34  ? -32.053 10.533  -64.231  1.00 284.36 ? 32   SER C O   1 
ATOM   6663  C  CB  . SER C  3 34  ? -33.313 13.356  -65.179  1.00 290.38 ? 32   SER C CB  1 
ATOM   6664  O  OG  . SER C  3 34  ? -34.231 12.915  -66.162  1.00 299.86 ? 32   SER C OG  1 
ATOM   6665  N  N   . PRO C  3 35  ? -34.258 10.293  -64.615  1.00 277.30 ? 33   PRO C N   1 
ATOM   6666  C  CA  . PRO C  3 35  ? -34.095 8.892   -65.011  1.00 271.42 ? 33   PRO C CA  1 
ATOM   6667  C  C   . PRO C  3 35  ? -33.336 8.762   -66.325  1.00 273.30 ? 33   PRO C C   1 
ATOM   6668  O  O   . PRO C  3 35  ? -33.447 9.624   -67.212  1.00 273.03 ? 33   PRO C O   1 
ATOM   6669  C  CB  . PRO C  3 35  ? -35.544 8.389   -65.148  1.00 267.57 ? 33   PRO C CB  1 
ATOM   6670  C  CG  . PRO C  3 35  ? -36.411 9.591   -65.119  1.00 268.67 ? 33   PRO C CG  1 
ATOM   6671  C  CD  . PRO C  3 35  ? -35.666 10.654  -64.388  1.00 270.39 ? 33   PRO C CD  1 
ATOM   6672  N  N   . PRO C  3 36  ? -32.570 7.685   -66.490  1.00 270.03 ? 34   PRO C N   1 
ATOM   6673  C  CA  . PRO C  3 36  ? -31.692 7.534   -67.658  1.00 272.56 ? 34   PRO C CA  1 
ATOM   6674  C  C   . PRO C  3 36  ? -32.437 7.011   -68.883  1.00 268.17 ? 34   PRO C C   1 
ATOM   6675  O  O   . PRO C  3 36  ? -33.624 6.695   -68.843  1.00 261.02 ? 34   PRO C O   1 
ATOM   6676  C  CB  . PRO C  3 36  ? -30.653 6.520   -67.175  1.00 277.39 ? 34   PRO C CB  1 
ATOM   6677  C  CG  . PRO C  3 36  ? -31.389 5.700   -66.151  1.00 271.66 ? 34   PRO C CG  1 
ATOM   6678  C  CD  . PRO C  3 36  ? -32.347 6.637   -65.478  1.00 267.44 ? 34   PRO C CD  1 
ATOM   6679  N  N   . SER C  3 37  ? -31.689 6.906   -69.989  1.00 267.59 ? 35   SER C N   1 
ATOM   6680  C  CA  . SER C  3 37  ? -32.253 6.505   -71.280  1.00 274.49 ? 35   SER C CA  1 
ATOM   6681  C  C   . SER C  3 37  ? -31.095 6.043   -72.167  1.00 277.44 ? 35   SER C C   1 
ATOM   6682  O  O   . SER C  3 37  ? -30.407 6.873   -72.768  1.00 279.49 ? 35   SER C O   1 
ATOM   6683  C  CB  . SER C  3 37  ? -33.015 7.654   -71.918  1.00 273.69 ? 35   SER C CB  1 
ATOM   6684  O  OG  . SER C  3 37  ? -32.141 8.721   -72.249  1.00 270.78 ? 35   SER C OG  1 
ATOM   6685  N  N   . GLN C  3 38  ? -30.896 4.729   -72.250  1.00 275.10 ? 36   GLN C N   1 
ATOM   6686  C  CA  . GLN C  3 38  ? -29.783 4.198   -73.029  1.00 271.84 ? 36   GLN C CA  1 
ATOM   6687  C  C   . GLN C  3 38  ? -30.200 3.063   -73.954  1.00 262.31 ? 36   GLN C C   1 
ATOM   6688  O  O   . GLN C  3 38  ? -31.395 2.793   -74.124  1.00 258.84 ? 36   GLN C O   1 
ATOM   6689  C  CB  . GLN C  3 38  ? -28.668 3.712   -72.101  1.00 271.00 ? 36   GLN C CB  1 
ATOM   6690  C  CG  . GLN C  3 38  ? -27.911 4.816   -71.393  1.00 270.07 ? 36   GLN C CG  1 
ATOM   6691  C  CD  . GLN C  3 38  ? -27.172 5.730   -72.351  1.00 277.03 ? 36   GLN C CD  1 
ATOM   6692  O  OE1 . GLN C  3 38  ? -26.958 5.394   -73.518  1.00 279.63 ? 36   GLN C OE1 1 
ATOM   6693  N  NE2 . GLN C  3 38  ? -26.775 6.896   -71.859  1.00 277.74 ? 36   GLN C NE2 1 
ATOM   6694  N  N   . GLY C  3 39  ? -29.208 2.409   -74.564  1.00 243.38 ? 37   GLY C N   1 
ATOM   6695  C  CA  . GLY C  3 39  ? -29.484 1.226   -75.362  1.00 241.69 ? 37   GLY C CA  1 
ATOM   6696  C  C   . GLY C  3 39  ? -30.076 0.114   -74.518  1.00 234.91 ? 37   GLY C C   1 
ATOM   6697  O  O   . GLY C  3 39  ? -29.779 -0.007  -73.324  1.00 233.68 ? 37   GLY C O   1 
ATOM   6698  N  N   . GLU C  3 40  ? -30.920 -0.708  -75.153  1.00 238.73 ? 38   GLU C N   1 
ATOM   6699  C  CA  . GLU C  3 40  ? -31.891 -1.547  -74.448  1.00 236.26 ? 38   GLU C CA  1 
ATOM   6700  C  C   . GLU C  3 40  ? -31.651 -3.024  -74.728  1.00 239.64 ? 38   GLU C C   1 
ATOM   6701  O  O   . GLU C  3 40  ? -31.582 -3.449  -75.889  1.00 238.71 ? 38   GLU C O   1 
ATOM   6702  C  CB  . GLU C  3 40  ? -33.346 -1.187  -74.831  1.00 220.14 ? 38   GLU C CB  1 
ATOM   6703  C  CG  . GLU C  3 40  ? -34.444 -1.722  -73.774  1.00 218.80 ? 38   GLU C CG  1 
ATOM   6704  C  CD  . GLU C  3 40  ? -36.017 -1.544  -74.186  1.00 221.27 ? 38   GLU C CD  1 
ATOM   6705  O  OE1 . GLU C  3 40  ? -36.388 -0.696  -75.098  1.00 223.47 ? 38   GLU C OE1 1 
ATOM   6706  O  OE2 . GLU C  3 40  ? -36.884 -2.275  -73.563  1.00 221.36 ? 38   GLU C OE2 1 
ATOM   6707  N  N   . VAL C  3 41  ? -31.519 -3.790  -73.656  1.00 271.41 ? 39   VAL C N   1 
ATOM   6708  C  CA  . VAL C  3 41  ? -31.416 -5.239  -73.695  1.00 275.12 ? 39   VAL C CA  1 
ATOM   6709  C  C   . VAL C  3 41  ? -32.144 -5.713  -72.443  1.00 280.91 ? 39   VAL C C   1 
ATOM   6710  O  O   . VAL C  3 41  ? -32.043 -5.060  -71.404  1.00 269.19 ? 39   VAL C O   1 
ATOM   6711  C  CB  . VAL C  3 41  ? -29.947 -5.711  -73.721  1.00 271.10 ? 39   VAL C CB  1 
ATOM   6712  C  CG1 . VAL C  3 41  ? -29.862 -7.216  -73.588  1.00 278.99 ? 39   VAL C CG1 1 
ATOM   6713  C  CG2 . VAL C  3 41  ? -29.241 -5.249  -74.994  1.00 267.35 ? 39   VAL C CG2 1 
ATOM   6714  N  N   . PRO C  3 42  ? -32.909 -6.816  -72.521  1.00 308.03 ? 40   PRO C N   1 
ATOM   6715  C  CA  . PRO C  3 42  ? -33.337 -7.649  -73.648  1.00 319.30 ? 40   PRO C CA  1 
ATOM   6716  C  C   . PRO C  3 42  ? -34.837 -7.532  -73.944  1.00 329.09 ? 40   PRO C C   1 
ATOM   6717  O  O   . PRO C  3 42  ? -35.612 -7.209  -73.040  1.00 331.34 ? 40   PRO C O   1 
ATOM   6718  C  CB  . PRO C  3 42  ? -32.991 -9.063  -73.165  1.00 309.92 ? 40   PRO C CB  1 
ATOM   6719  C  CG  . PRO C  3 42  ? -33.046 -8.974  -71.631  1.00 300.22 ? 40   PRO C CG  1 
ATOM   6720  C  CD  . PRO C  3 42  ? -33.156 -7.510  -71.246  1.00 301.15 ? 40   PRO C CD  1 
ATOM   6721  N  N   . PRO C  3 43  ? -35.247 -7.791  -75.191  1.00 340.13 ? 41   PRO C N   1 
ATOM   6722  C  CA  . PRO C  3 43  ? -36.685 -7.769  -75.503  1.00 335.60 ? 41   PRO C CA  1 
ATOM   6723  C  C   . PRO C  3 43  ? -37.460 -8.885  -74.828  1.00 329.14 ? 41   PRO C C   1 
ATOM   6724  O  O   . PRO C  3 43  ? -38.694 -8.808  -74.757  1.00 337.62 ? 41   PRO C O   1 
ATOM   6725  C  CB  . PRO C  3 43  ? -36.717 -7.907  -77.031  1.00 339.89 ? 41   PRO C CB  1 
ATOM   6726  C  CG  . PRO C  3 43  ? -35.454 -8.624  -77.363  1.00 343.10 ? 41   PRO C CG  1 
ATOM   6727  C  CD  . PRO C  3 43  ? -34.431 -8.142  -76.367  1.00 339.64 ? 41   PRO C CD  1 
ATOM   6728  N  N   . GLY C  3 44  ? -36.779 -9.920  -74.339  1.00 350.97 ? 42   GLY C N   1 
ATOM   6729  C  CA  . GLY C  3 44  ? -37.400 -10.952 -73.546  1.00 332.84 ? 42   GLY C CA  1 
ATOM   6730  C  C   . GLY C  3 44  ? -37.075 -10.783 -72.074  1.00 307.04 ? 42   GLY C C   1 
ATOM   6731  O  O   . GLY C  3 44  ? -36.709 -9.693  -71.619  1.00 293.89 ? 42   GLY C O   1 
ATOM   6732  N  N   . PRO C  3 45  ? -37.194 -11.862 -71.300  1.00 287.12 ? 43   PRO C N   1 
ATOM   6733  C  CA  . PRO C  3 45  ? -36.956 -11.762 -69.852  1.00 277.37 ? 43   PRO C CA  1 
ATOM   6734  C  C   . PRO C  3 45  ? -35.481 -11.541 -69.546  1.00 287.11 ? 43   PRO C C   1 
ATOM   6735  O  O   . PRO C  3 45  ? -34.605 -12.204 -70.108  1.00 289.87 ? 43   PRO C O   1 
ATOM   6736  C  CB  . PRO C  3 45  ? -37.455 -13.109 -69.314  1.00 276.93 ? 43   PRO C CB  1 
ATOM   6737  C  CG  . PRO C  3 45  ? -37.351 -14.037 -70.473  1.00 291.64 ? 43   PRO C CG  1 
ATOM   6738  C  CD  . PRO C  3 45  ? -37.617 -13.214 -71.703  1.00 297.90 ? 43   PRO C CD  1 
ATOM   6739  N  N   . LEU C  3 46  ? -35.220 -10.598 -68.639  1.00 277.70 ? 44   LEU C N   1 
ATOM   6740  C  CA  . LEU C  3 46  ? -33.901 -10.139 -68.217  1.00 269.62 ? 44   LEU C CA  1 
ATOM   6741  C  C   . LEU C  3 46  ? -32.978 -11.294 -67.844  1.00 269.34 ? 44   LEU C C   1 
ATOM   6742  O  O   . LEU C  3 46  ? -33.458 -12.361 -67.438  1.00 259.72 ? 44   LEU C O   1 
ATOM   6743  C  CB  . LEU C  3 46  ? -34.055 -9.188  -67.032  1.00 249.11 ? 44   LEU C CB  1 
ATOM   6744  C  CG  . LEU C  3 46  ? -35.316 -8.335  -67.111  1.00 250.59 ? 44   LEU C CG  1 
ATOM   6745  C  CD1 . LEU C  3 46  ? -36.346 -8.790  -66.089  1.00 248.57 ? 44   LEU C CD1 1 
ATOM   6746  C  CD2 . LEU C  3 46  ? -34.946 -6.892  -66.911  1.00 251.50 ? 44   LEU C CD2 1 
ATOM   6747  N  N   . PRO C  3 47  ? -31.657 -11.118 -67.953  1.00 283.91 ? 45   PRO C N   1 
ATOM   6748  C  CA  . PRO C  3 47  ? -30.739 -12.225 -67.654  1.00 285.25 ? 45   PRO C CA  1 
ATOM   6749  C  C   . PRO C  3 47  ? -30.867 -12.680 -66.209  1.00 263.66 ? 45   PRO C C   1 
ATOM   6750  O  O   . PRO C  3 47  ? -31.007 -11.868 -65.293  1.00 255.69 ? 45   PRO C O   1 
ATOM   6751  C  CB  . PRO C  3 47  ? -29.355 -11.627 -67.936  1.00 287.29 ? 45   PRO C CB  1 
ATOM   6752  C  CG  . PRO C  3 47  ? -29.544 -10.155 -67.803  1.00 275.97 ? 45   PRO C CG  1 
ATOM   6753  C  CD  . PRO C  3 47  ? -30.928 -9.890  -68.319  1.00 283.78 ? 45   PRO C CD  1 
ATOM   6754  N  N   . GLU C  3 48  ? -30.816 -13.999 -66.016  1.00 261.73 ? 46   GLU C N   1 
ATOM   6755  C  CA  . GLU C  3 48  ? -31.044 -14.606 -64.711  1.00 251.39 ? 46   GLU C CA  1 
ATOM   6756  C  C   . GLU C  3 48  ? -29.843 -14.504 -63.783  1.00 234.83 ? 46   GLU C C   1 
ATOM   6757  O  O   . GLU C  3 48  ? -29.905 -15.023 -62.662  1.00 227.98 ? 46   GLU C O   1 
ATOM   6758  C  CB  . GLU C  3 48  ? -31.442 -16.075 -64.876  1.00 248.50 ? 46   GLU C CB  1 
ATOM   6759  C  CG  . GLU C  3 48  ? -32.778 -16.271 -65.570  1.00 248.79 ? 46   GLU C CG  1 
ATOM   6760  C  CD  . GLU C  3 48  ? -33.291 -17.690 -65.461  1.00 249.74 ? 46   GLU C CD  1 
ATOM   6761  O  OE1 . GLU C  3 48  ? -32.491 -18.590 -65.133  1.00 243.59 ? 46   GLU C OE1 1 
ATOM   6762  O  OE2 . GLU C  3 48  ? -34.499 -17.902 -65.697  1.00 260.38 ? 46   GLU C OE2 1 
ATOM   6763  N  N   . ALA C  3 49  ? -28.754 -13.865 -64.214  1.00 239.34 ? 47   ALA C N   1 
ATOM   6764  C  CA  . ALA C  3 49  ? -27.662 -13.591 -63.288  1.00 241.82 ? 47   ALA C CA  1 
ATOM   6765  C  C   . ALA C  3 49  ? -28.059 -12.515 -62.287  1.00 243.35 ? 47   ALA C C   1 
ATOM   6766  O  O   . ALA C  3 49  ? -27.733 -12.614 -61.098  1.00 223.18 ? 47   ALA C O   1 
ATOM   6767  C  CB  . ALA C  3 49  ? -26.410 -13.174 -64.058  1.00 243.39 ? 47   ALA C CB  1 
ATOM   6768  N  N   . VAL C  3 50  ? -28.761 -11.479 -62.753  1.00 261.76 ? 48   VAL C N   1 
ATOM   6769  C  CA  . VAL C  3 50  ? -29.264 -10.449 -61.852  1.00 239.44 ? 48   VAL C CA  1 
ATOM   6770  C  C   . VAL C  3 50  ? -30.616 -10.829 -61.268  1.00 234.61 ? 48   VAL C C   1 
ATOM   6771  O  O   . VAL C  3 50  ? -31.007 -10.283 -60.229  1.00 240.29 ? 48   VAL C O   1 
ATOM   6772  C  CB  . VAL C  3 50  ? -29.360 -9.088  -62.561  1.00 240.22 ? 48   VAL C CB  1 
ATOM   6773  C  CG1 . VAL C  3 50  ? -28.012 -8.703  -63.148  1.00 248.63 ? 48   VAL C CG1 1 
ATOM   6774  C  CG2 . VAL C  3 50  ? -30.439 -9.115  -63.639  1.00 246.57 ? 48   VAL C CG2 1 
ATOM   6775  N  N   . LEU C  3 51  ? -31.346 -11.747 -61.912  1.00 228.99 ? 49   LEU C N   1 
ATOM   6776  C  CA  . LEU C  3 51  ? -32.580 -12.245 -61.319  1.00 225.16 ? 49   LEU C CA  1 
ATOM   6777  C  C   . LEU C  3 51  ? -32.293 -13.156 -60.134  1.00 242.41 ? 49   LEU C C   1 
ATOM   6778  O  O   . LEU C  3 51  ? -33.135 -13.285 -59.237  1.00 244.91 ? 49   LEU C O   1 
ATOM   6779  C  CB  . LEU C  3 51  ? -33.418 -12.979 -62.368  1.00 221.51 ? 49   LEU C CB  1 
ATOM   6780  C  CG  . LEU C  3 51  ? -34.040 -12.114 -63.468  1.00 233.22 ? 49   LEU C CG  1 
ATOM   6781  C  CD1 . LEU C  3 51  ? -34.887 -12.959 -64.411  1.00 249.86 ? 49   LEU C CD1 1 
ATOM   6782  C  CD2 . LEU C  3 51  ? -34.864 -10.981 -62.876  1.00 225.84 ? 49   LEU C CD2 1 
ATOM   6783  N  N   . ALA C  3 52  ? -31.118 -13.792 -60.114  1.00 249.38 ? 50   ALA C N   1 
ATOM   6784  C  CA  . ALA C  3 52  ? -30.721 -14.570 -58.947  1.00 236.81 ? 50   ALA C CA  1 
ATOM   6785  C  C   . ALA C  3 52  ? -30.408 -13.662 -57.768  1.00 217.04 ? 50   ALA C C   1 
ATOM   6786  O  O   . ALA C  3 52  ? -30.706 -14.004 -56.618  1.00 209.22 ? 50   ALA C O   1 
ATOM   6787  C  CB  . ALA C  3 52  ? -29.512 -15.448 -59.284  1.00 244.07 ? 50   ALA C CB  1 
ATOM   6788  N  N   . LEU C  3 53  ? -29.799 -12.504 -58.036  1.00 220.66 ? 51   LEU C N   1 
ATOM   6789  C  CA  . LEU C  3 53  ? -29.610 -11.504 -56.993  1.00 218.57 ? 51   LEU C CA  1 
ATOM   6790  C  C   . LEU C  3 53  ? -30.947 -10.966 -56.508  1.00 218.19 ? 51   LEU C C   1 
ATOM   6791  O  O   . LEU C  3 53  ? -31.181 -10.854 -55.299  1.00 227.06 ? 51   LEU C O   1 
ATOM   6792  C  CB  . LEU C  3 53  ? -28.737 -10.359 -57.510  1.00 227.91 ? 51   LEU C CB  1 
ATOM   6793  C  CG  . LEU C  3 53  ? -27.219 -10.478 -57.374  1.00 234.44 ? 51   LEU C CG  1 
ATOM   6794  C  CD1 . LEU C  3 53  ? -26.660 -11.555 -58.294  1.00 246.62 ? 51   LEU C CD1 1 
ATOM   6795  C  CD2 . LEU C  3 53  ? -26.564 -9.134  -57.652  1.00 230.85 ? 51   LEU C CD2 1 
ATOM   6796  N  N   . TYR C  3 54  ? -31.838 -10.624 -57.440  1.00 210.33 ? 52   TYR C N   1 
ATOM   6797  C  CA  . TYR C  3 54  ? -33.116 -10.038 -57.056  1.00 211.79 ? 52   TYR C CA  1 
ATOM   6798  C  C   . TYR C  3 54  ? -33.992 -11.048 -56.328  1.00 214.80 ? 52   TYR C C   1 
ATOM   6799  O  O   . TYR C  3 54  ? -34.740 -10.682 -55.414  1.00 227.24 ? 52   TYR C O   1 
ATOM   6800  C  CB  . TYR C  3 54  ? -33.831 -9.498  -58.291  1.00 223.20 ? 52   TYR C CB  1 
ATOM   6801  C  CG  . TYR C  3 54  ? -35.155 -8.840  -57.988  1.00 229.69 ? 52   TYR C CG  1 
ATOM   6802  C  CD1 . TYR C  3 54  ? -35.211 -7.588  -57.389  1.00 222.34 ? 52   TYR C CD1 1 
ATOM   6803  C  CD2 . TYR C  3 54  ? -36.351 -9.467  -58.309  1.00 246.13 ? 52   TYR C CD2 1 
ATOM   6804  C  CE1 . TYR C  3 54  ? -36.423 -6.983  -57.115  1.00 229.82 ? 52   TYR C CE1 1 
ATOM   6805  C  CE2 . TYR C  3 54  ? -37.564 -8.872  -58.041  1.00 249.66 ? 52   TYR C CE2 1 
ATOM   6806  C  CZ  . TYR C  3 54  ? -37.596 -7.631  -57.443  1.00 242.88 ? 52   TYR C CZ  1 
ATOM   6807  O  OH  . TYR C  3 54  ? -38.811 -7.042  -57.175  1.00 244.36 ? 52   TYR C OH  1 
ATOM   6808  N  N   . ASN C  3 55  ? -33.913 -12.324 -56.715  1.00 215.38 ? 53   ASN C N   1 
ATOM   6809  C  CA  . ASN C  3 55  ? -34.663 -13.362 -56.017  1.00 226.46 ? 53   ASN C CA  1 
ATOM   6810  C  C   . ASN C  3 55  ? -34.047 -13.706 -54.666  1.00 238.05 ? 53   ASN C C   1 
ATOM   6811  O  O   . ASN C  3 55  ? -34.740 -14.268 -53.809  1.00 236.14 ? 53   ASN C O   1 
ATOM   6812  C  CB  . ASN C  3 55  ? -34.764 -14.609 -56.897  1.00 233.21 ? 53   ASN C CB  1 
ATOM   6813  C  CG  . ASN C  3 55  ? -35.827 -14.475 -57.976  1.00 252.24 ? 53   ASN C CG  1 
ATOM   6814  O  OD1 . ASN C  3 55  ? -36.398 -13.402 -58.171  1.00 241.30 ? 53   ASN C OD1 1 
ATOM   6815  N  ND2 . ASN C  3 55  ? -36.097 -15.561 -58.684  1.00 329.34 ? 53   ASN C ND2 1 
ATOM   6816  N  N   . SER C  3 56  ? -32.770 -13.378 -54.455  1.00 249.02 ? 54   SER C N   1 
ATOM   6817  C  CA  . SER C  3 56  ? -32.123 -13.578 -53.164  1.00 235.89 ? 54   SER C CA  1 
ATOM   6818  C  C   . SER C  3 56  ? -32.297 -12.395 -52.224  1.00 223.98 ? 54   SER C C   1 
ATOM   6819  O  O   . SER C  3 56  ? -32.121 -12.557 -51.012  1.00 223.95 ? 54   SER C O   1 
ATOM   6820  C  CB  . SER C  3 56  ? -30.627 -13.847 -53.355  1.00 228.59 ? 54   SER C CB  1 
ATOM   6821  O  OG  . SER C  3 56  ? -30.406 -14.958 -54.207  1.00 233.63 ? 54   SER C OG  1 
ATOM   6822  N  N   . THR C  3 57  ? -32.634 -11.214 -52.749  1.00 211.78 ? 55   THR C N   1 
ATOM   6823  C  CA  . THR C  3 57  ? -32.825 -10.048 -51.896  1.00 206.85 ? 55   THR C CA  1 
ATOM   6824  C  C   . THR C  3 57  ? -34.245 -9.963  -51.350  1.00 214.54 ? 55   THR C C   1 
ATOM   6825  O  O   . THR C  3 57  ? -34.439 -9.521  -50.211  1.00 229.93 ? 55   THR C O   1 
ATOM   6826  C  CB  . THR C  3 57  ? -32.486 -8.772  -52.663  1.00 209.60 ? 55   THR C CB  1 
ATOM   6827  O  OG1 . THR C  3 57  ? -31.259 -8.957  -53.376  1.00 223.21 ? 55   THR C OG1 1 
ATOM   6828  C  CG2 . THR C  3 57  ? -32.321 -7.610  -51.697  1.00 210.89 ? 55   THR C CG2 1 
ATOM   6829  N  N   . ARG C  3 58  ? -35.244 -10.372 -52.136  1.00 210.52 ? 56   ARG C N   1 
ATOM   6830  C  CA  . ARG C  3 58  ? -36.609 -10.453 -51.631  1.00 212.16 ? 56   ARG C CA  1 
ATOM   6831  C  C   . ARG C  3 58  ? -36.810 -11.629 -50.688  1.00 211.98 ? 56   ARG C C   1 
ATOM   6832  O  O   . ARG C  3 58  ? -37.848 -11.700 -50.021  1.00 211.17 ? 56   ARG C O   1 
ATOM   6833  C  CB  . ARG C  3 58  ? -37.601 -10.563 -52.793  1.00 218.11 ? 56   ARG C CB  1 
ATOM   6834  C  CG  . ARG C  3 58  ? -37.538 -9.414  -53.786  1.00 215.73 ? 56   ARG C CG  1 
ATOM   6835  C  CD  . ARG C  3 58  ? -38.766 -9.375  -54.687  1.00 216.89 ? 56   ARG C CD  1 
ATOM   6836  N  NE  . ARG C  3 58  ? -38.823 -10.506 -55.608  1.00 216.65 ? 56   ARG C NE  1 
ATOM   6837  C  CZ  . ARG C  3 58  ? -39.571 -11.587 -55.419  1.00 224.40 ? 56   ARG C CZ  1 
ATOM   6838  N  NH1 . ARG C  3 58  ? -40.331 -11.690 -54.338  1.00 217.36 ? 56   ARG C NH1 1 
ATOM   6839  N  NH2 . ARG C  3 58  ? -39.560 -12.565 -56.314  1.00 242.00 ? 56   ARG C NH2 1 
ATOM   6840  N  N   . ASP C  3 59  ? -35.844 -12.546 -50.617  1.00 231.17 ? 57   ASP C N   1 
ATOM   6841  C  CA  . ASP C  3 59  ? -35.991 -13.800 -49.880  1.00 238.19 ? 57   ASP C CA  1 
ATOM   6842  C  C   . ASP C  3 59  ? -35.615 -13.564 -48.420  1.00 224.38 ? 57   ASP C C   1 
ATOM   6843  O  O   . ASP C  3 59  ? -34.486 -13.798 -47.982  1.00 228.59 ? 57   ASP C O   1 
ATOM   6844  C  CB  . ASP C  3 59  ? -35.132 -14.885 -50.521  1.00 246.62 ? 57   ASP C CB  1 
ATOM   6845  C  CG  . ASP C  3 59  ? -35.350 -16.261 -49.904  1.00 246.57 ? 57   ASP C CG  1 
ATOM   6846  O  OD1 . ASP C  3 59  ? -36.021 -16.363 -48.853  1.00 249.12 ? 57   ASP C OD1 1 
ATOM   6847  O  OD2 . ASP C  3 59  ? -34.835 -17.248 -50.473  1.00 241.93 ? 57   ASP C OD2 1 
ATOM   6848  N  N   . ARG C  3 60  ? -36.595 -13.108 -47.645  1.00 214.05 ? 58   ARG C N   1 
ATOM   6849  C  CA  . ARG C  3 60  ? -36.430 -12.963 -46.204  1.00 222.43 ? 58   ARG C CA  1 
ATOM   6850  C  C   . ARG C  3 60  ? -37.050 -14.187 -45.537  1.00 216.67 ? 58   ARG C C   1 
ATOM   6851  O  O   . ARG C  3 60  ? -38.240 -14.471 -45.716  1.00 214.53 ? 58   ARG C O   1 
ATOM   6852  C  CB  . ARG C  3 60  ? -37.033 -11.649 -45.697  1.00 243.96 ? 58   ARG C CB  1 
ATOM   6853  C  CG  . ARG C  3 60  ? -38.554 -11.492 -45.804  1.00 256.48 ? 58   ARG C CG  1 
ATOM   6854  C  CD  . ARG C  3 60  ? -39.235 -11.707 -44.448  1.00 245.63 ? 58   ARG C CD  1 
ATOM   6855  N  NE  . ARG C  3 60  ? -40.625 -12.141 -44.579  1.00 230.43 ? 58   ARG C NE  1 
ATOM   6856  C  CZ  . ARG C  3 60  ? -41.355 -12.620 -43.576  1.00 219.41 ? 58   ARG C CZ  1 
ATOM   6857  N  NH1 . ARG C  3 60  ? -40.830 -12.727 -42.362  1.00 216.79 ? 58   ARG C NH1 1 
ATOM   6858  N  NH2 . ARG C  3 60  ? -42.609 -12.995 -43.785  1.00 222.43 ? 58   ARG C NH2 1 
ATOM   6859  N  N   . VAL C  3 61  ? -36.221 -14.950 -44.826  1.00 216.76 ? 59   VAL C N   1 
ATOM   6860  C  CA  . VAL C  3 61  ? -36.701 -16.015 -43.953  1.00 227.24 ? 59   VAL C CA  1 
ATOM   6861  C  C   . VAL C  3 61  ? -35.942 -15.903 -42.636  1.00 237.40 ? 59   VAL C C   1 
ATOM   6862  O  O   . VAL C  3 61  ? -36.438 -15.304 -41.673  1.00 248.05 ? 59   VAL C O   1 
ATOM   6863  C  CB  . VAL C  3 61  ? -36.536 -17.412 -44.585  1.00 226.02 ? 59   VAL C CB  1 
ATOM   6864  C  CG1 . VAL C  3 61  ? -37.250 -18.448 -43.747  1.00 230.95 ? 59   VAL C CG1 1 
ATOM   6865  C  CG2 . VAL C  3 61  ? -37.064 -17.443 -46.015  1.00 219.95 ? 59   VAL C CG2 1 
ATOM   6866  N  N   . ALA C  3 62  ? -34.736 -16.470 -42.591  1.00 239.54 ? 60   ALA C N   1 
ATOM   6867  C  CA  . ALA C  3 62  ? -33.819 -16.345 -41.449  1.00 233.67 ? 60   ALA C CA  1 
ATOM   6868  C  C   . ALA C  3 62  ? -34.390 -16.885 -40.137  1.00 230.64 ? 60   ALA C C   1 
ATOM   6869  O  O   . ALA C  3 62  ? -35.521 -17.370 -40.078  1.00 233.12 ? 60   ALA C O   1 
ATOM   6870  C  CB  . ALA C  3 62  ? -33.397 -14.888 -41.271  1.00 226.05 ? 60   ALA C CB  1 
ATOM   6871  N  N   . ALA C  3 74  ? -29.608 8.765   -40.263  1.00 219.26 ? 72   ALA C N   1 
ATOM   6872  C  CA  . ALA C  3 74  ? -28.447 7.950   -40.597  1.00 215.17 ? 72   ALA C CA  1 
ATOM   6873  C  C   . ALA C  3 74  ? -28.292 7.802   -42.110  1.00 221.76 ? 72   ALA C C   1 
ATOM   6874  O  O   . ALA C  3 74  ? -28.385 8.783   -42.849  1.00 226.09 ? 72   ALA C O   1 
ATOM   6875  C  CB  . ALA C  3 74  ? -28.551 6.584   -39.937  1.00 206.24 ? 72   ALA C CB  1 
ATOM   6876  N  N   . ASP C  3 75  ? -28.062 6.570   -42.564  1.00 230.73 ? 73   ASP C N   1 
ATOM   6877  C  CA  . ASP C  3 75  ? -27.786 6.287   -43.973  1.00 229.56 ? 73   ASP C CA  1 
ATOM   6878  C  C   . ASP C  3 75  ? -29.100 6.076   -44.709  1.00 228.81 ? 73   ASP C C   1 
ATOM   6879  O  O   . ASP C  3 75  ? -29.661 4.978   -44.703  1.00 223.57 ? 73   ASP C O   1 
ATOM   6880  C  CB  . ASP C  3 75  ? -26.883 5.069   -44.111  1.00 236.46 ? 73   ASP C CB  1 
ATOM   6881  C  CG  . ASP C  3 75  ? -25.519 5.293   -43.510  1.00 249.84 ? 73   ASP C CG  1 
ATOM   6882  O  OD1 . ASP C  3 75  ? -25.354 5.039   -42.298  1.00 257.22 ? 73   ASP C OD1 1 
ATOM   6883  O  OD2 . ASP C  3 75  ? -24.613 5.729   -44.250  1.00 249.74 ? 73   ASP C OD2 1 
ATOM   6884  N  N   . TYR C  3 76  ? -29.584 7.130   -45.359  1.00 237.28 ? 74   TYR C N   1 
ATOM   6885  C  CA  . TYR C  3 76  ? -30.804 7.056   -46.146  1.00 243.94 ? 74   TYR C CA  1 
ATOM   6886  C  C   . TYR C  3 76  ? -30.548 6.771   -47.617  1.00 237.63 ? 74   TYR C C   1 
ATOM   6887  O  O   . TYR C  3 76  ? -31.497 6.456   -48.342  1.00 237.19 ? 74   TYR C O   1 
ATOM   6888  C  CB  . TYR C  3 76  ? -31.598 8.361   -46.017  1.00 264.54 ? 74   TYR C CB  1 
ATOM   6889  C  CG  . TYR C  3 76  ? -32.343 8.493   -44.709  1.00 277.41 ? 74   TYR C CG  1 
ATOM   6890  C  CD1 . TYR C  3 76  ? -33.573 7.872   -44.526  1.00 269.79 ? 74   TYR C CD1 1 
ATOM   6891  C  CD2 . TYR C  3 76  ? -31.821 9.239   -43.660  1.00 277.29 ? 74   TYR C CD2 1 
ATOM   6892  C  CE1 . TYR C  3 76  ? -34.261 7.987   -43.334  1.00 257.30 ? 74   TYR C CE1 1 
ATOM   6893  C  CE2 . TYR C  3 76  ? -32.503 9.361   -42.463  1.00 267.13 ? 74   TYR C CE2 1 
ATOM   6894  C  CZ  . TYR C  3 76  ? -33.722 8.733   -42.306  1.00 257.82 ? 74   TYR C CZ  1 
ATOM   6895  O  OH  . TYR C  3 76  ? -34.403 8.851   -41.118  1.00 257.23 ? 74   TYR C OH  1 
ATOM   6896  N  N   . TYR C  3 77  ? -29.303 6.864   -48.075  1.00 232.56 ? 75   TYR C N   1 
ATOM   6897  C  CA  . TYR C  3 77  ? -29.010 6.670   -49.486  1.00 239.24 ? 75   TYR C CA  1 
ATOM   6898  C  C   . TYR C  3 77  ? -29.087 5.185   -49.850  1.00 245.60 ? 75   TYR C C   1 
ATOM   6899  O  O   . TYR C  3 77  ? -29.300 4.311   -49.003  1.00 248.01 ? 75   TYR C O   1 
ATOM   6900  C  CB  . TYR C  3 77  ? -27.641 7.253   -49.827  1.00 244.46 ? 75   TYR C CB  1 
ATOM   6901  C  CG  . TYR C  3 77  ? -27.553 8.760   -49.681  1.00 253.33 ? 75   TYR C CG  1 
ATOM   6902  C  CD1 . TYR C  3 77  ? -27.908 9.603   -50.727  1.00 254.32 ? 75   TYR C CD1 1 
ATOM   6903  C  CD2 . TYR C  3 77  ? -27.107 9.338   -48.498  1.00 259.10 ? 75   TYR C CD2 1 
ATOM   6904  C  CE1 . TYR C  3 77  ? -27.826 10.980  -50.596  1.00 255.07 ? 75   TYR C CE1 1 
ATOM   6905  C  CE2 . TYR C  3 77  ? -27.020 10.712  -48.359  1.00 259.63 ? 75   TYR C CE2 1 
ATOM   6906  C  CZ  . TYR C  3 77  ? -27.380 11.527  -49.411  1.00 253.81 ? 75   TYR C CZ  1 
ATOM   6907  O  OH  . TYR C  3 77  ? -27.295 12.894  -49.273  1.00 251.39 ? 75   TYR C OH  1 
ATOM   6908  N  N   . ALA C  3 78  ? -28.908 4.899   -51.139  1.00 244.22 ? 76   ALA C N   1 
ATOM   6909  C  CA  . ALA C  3 78  ? -29.055 3.556   -51.681  1.00 236.38 ? 76   ALA C CA  1 
ATOM   6910  C  C   . ALA C  3 78  ? -27.757 2.763   -51.564  1.00 230.75 ? 76   ALA C C   1 
ATOM   6911  O  O   . ALA C  3 78  ? -26.661 3.320   -51.465  1.00 238.58 ? 76   ALA C O   1 
ATOM   6912  C  CB  . ALA C  3 78  ? -29.491 3.610   -53.145  1.00 234.44 ? 76   ALA C CB  1 
ATOM   6913  N  N   . LYS C  3 79  ? -27.897 1.440   -51.587  1.00 218.81 ? 77   LYS C N   1 
ATOM   6914  C  CA  . LYS C  3 79  ? -26.766 0.528   -51.486  1.00 215.09 ? 77   LYS C CA  1 
ATOM   6915  C  C   . LYS C  3 79  ? -26.805 -0.438  -52.660  1.00 226.86 ? 77   LYS C C   1 
ATOM   6916  O  O   . LYS C  3 79  ? -27.832 -1.080  -52.900  1.00 232.94 ? 77   LYS C O   1 
ATOM   6917  C  CB  . LYS C  3 79  ? -26.795 -0.245  -50.163  1.00 211.61 ? 77   LYS C CB  1 
ATOM   6918  C  CG  . LYS C  3 79  ? -27.071 0.619   -48.942  1.00 213.09 ? 77   LYS C CG  1 
ATOM   6919  C  CD  . LYS C  3 79  ? -25.965 1.635   -48.708  1.00 220.28 ? 77   LYS C CD  1 
ATOM   6920  C  CE  . LYS C  3 79  ? -26.241 2.464   -47.461  1.00 218.27 ? 77   LYS C CE  1 
ATOM   6921  N  NZ  . LYS C  3 79  ? -25.193 3.491   -47.205  1.00 222.98 ? 77   LYS C NZ  1 
ATOM   6922  N  N   . GLU C  3 80  ? -25.692 -0.539  -53.388  1.00 233.11 ? 78   GLU C N   1 
ATOM   6923  C  CA  . GLU C  3 80  ? -25.606 -1.436  -54.536  1.00 232.07 ? 78   GLU C CA  1 
ATOM   6924  C  C   . GLU C  3 80  ? -25.321 -2.854  -54.052  1.00 235.13 ? 78   GLU C C   1 
ATOM   6925  O  O   . GLU C  3 80  ? -24.301 -3.104  -53.401  1.00 236.95 ? 78   GLU C O   1 
ATOM   6926  C  CB  . GLU C  3 80  ? -24.525 -0.964  -55.508  1.00 226.53 ? 78   GLU C CB  1 
ATOM   6927  C  CG  . GLU C  3 80  ? -24.367 -1.844  -56.745  1.00 221.61 ? 78   GLU C CG  1 
ATOM   6928  C  CD  . GLU C  3 80  ? -23.382 -1.274  -57.752  1.00 222.14 ? 78   GLU C CD  1 
ATOM   6929  O  OE1 . GLU C  3 80  ? -23.012 -0.089  -57.626  1.00 225.66 ? 78   GLU C OE1 1 
ATOM   6930  O  OE2 . GLU C  3 80  ? -22.977 -2.014  -58.672  1.00 220.34 ? 78   GLU C OE2 1 
ATOM   6931  N  N   . VAL C  3 81  ? -26.219 -3.782  -54.377  1.00 232.86 ? 79   VAL C N   1 
ATOM   6932  C  CA  . VAL C  3 81  ? -26.175 -5.144  -53.853  1.00 229.59 ? 79   VAL C CA  1 
ATOM   6933  C  C   . VAL C  3 81  ? -25.513 -6.051  -54.882  1.00 240.04 ? 79   VAL C C   1 
ATOM   6934  O  O   . VAL C  3 81  ? -25.946 -6.117  -56.039  1.00 248.67 ? 79   VAL C O   1 
ATOM   6935  C  CB  . VAL C  3 81  ? -27.582 -5.649  -53.496  1.00 230.69 ? 79   VAL C CB  1 
ATOM   6936  C  CG1 . VAL C  3 81  ? -27.527 -7.093  -53.035  1.00 230.52 ? 79   VAL C CG1 1 
ATOM   6937  C  CG2 . VAL C  3 81  ? -28.201 -4.770  -52.422  1.00 224.24 ? 79   VAL C CG2 1 
ATOM   6938  N  N   . THR C  3 82  ? -24.469 -6.760  -54.454  1.00 239.27 ? 80   THR C N   1 
ATOM   6939  C  CA  . THR C  3 82  ? -23.777 -7.741  -55.277  1.00 237.66 ? 80   THR C CA  1 
ATOM   6940  C  C   . THR C  3 82  ? -23.482 -8.969  -54.425  1.00 225.16 ? 80   THR C C   1 
ATOM   6941  O  O   . THR C  3 82  ? -23.444 -8.898  -53.195  1.00 219.05 ? 80   THR C O   1 
ATOM   6942  C  CB  . THR C  3 82  ? -22.475 -7.179  -55.867  1.00 242.52 ? 80   THR C CB  1 
ATOM   6943  O  OG1 . THR C  3 82  ? -21.683 -6.595  -54.823  1.00 228.43 ? 80   THR C OG1 1 
ATOM   6944  C  CG2 . THR C  3 82  ? -22.774 -6.124  -56.929  1.00 248.81 ? 80   THR C CG2 1 
ATOM   6945  N  N   . ARG C  3 83  ? -23.271 -10.104 -55.089  1.00 223.91 ? 81   ARG C N   1 
ATOM   6946  C  CA  . ARG C  3 83  ? -23.044 -11.364 -54.395  1.00 215.20 ? 81   ARG C CA  1 
ATOM   6947  C  C   . ARG C  3 83  ? -21.840 -12.087 -54.988  1.00 216.87 ? 81   ARG C C   1 
ATOM   6948  O  O   . ARG C  3 83  ? -21.394 -11.792 -56.101  1.00 232.61 ? 81   ARG C O   1 
ATOM   6949  C  CB  . ARG C  3 83  ? -24.276 -12.275 -54.463  1.00 213.50 ? 81   ARG C CB  1 
ATOM   6950  C  CG  . ARG C  3 83  ? -24.408 -13.022 -55.777  1.00 228.58 ? 81   ARG C CG  1 
ATOM   6951  C  CD  . ARG C  3 83  ? -25.484 -14.090 -55.715  1.00 229.60 ? 81   ARG C CD  1 
ATOM   6952  N  NE  . ARG C  3 83  ? -25.499 -14.902 -56.928  1.00 230.15 ? 81   ARG C NE  1 
ATOM   6953  C  CZ  . ARG C  3 83  ? -26.302 -15.941 -57.124  1.00 230.30 ? 81   ARG C CZ  1 
ATOM   6954  N  NH1 . ARG C  3 83  ? -27.165 -16.304 -56.184  1.00 219.65 ? 81   ARG C NH1 1 
ATOM   6955  N  NH2 . ARG C  3 83  ? -26.241 -16.617 -58.263  1.00 241.90 ? 81   ARG C NH2 1 
ATOM   6956  N  N   . VAL C  3 84  ? -21.323 -13.052 -54.226  1.00 209.70 ? 82   VAL C N   1 
ATOM   6957  C  CA  . VAL C  3 84  ? -20.199 -13.887 -54.645  1.00 217.62 ? 82   VAL C CA  1 
ATOM   6958  C  C   . VAL C  3 84  ? -20.409 -15.299 -54.110  1.00 220.65 ? 82   VAL C C   1 
ATOM   6959  O  O   . VAL C  3 84  ? -20.641 -15.486 -52.911  1.00 210.39 ? 82   VAL C O   1 
ATOM   6960  C  CB  . VAL C  3 84  ? -18.846 -13.324 -54.161  1.00 217.55 ? 82   VAL C CB  1 
ATOM   6961  C  CG1 . VAL C  3 84  ? -18.356 -12.227 -55.095  1.00 229.80 ? 82   VAL C CG1 1 
ATOM   6962  C  CG2 . VAL C  3 84  ? -18.962 -12.800 -52.738  1.00 211.82 ? 82   VAL C CG2 1 
ATOM   6963  N  N   . LEU C  3 85  ? -20.316 -16.291 -54.995  1.00 247.82 ? 83   LEU C N   1 
ATOM   6964  C  CA  . LEU C  3 85  ? -20.470 -17.688 -54.614  1.00 244.46 ? 83   LEU C CA  1 
ATOM   6965  C  C   . LEU C  3 85  ? -19.181 -18.218 -53.983  1.00 241.86 ? 83   LEU C C   1 
ATOM   6966  O  O   . LEU C  3 85  ? -18.126 -17.579 -54.020  1.00 251.32 ? 83   LEU C O   1 
ATOM   6967  C  CB  . LEU C  3 85  ? -20.853 -18.537 -55.825  1.00 243.50 ? 83   LEU C CB  1 
ATOM   6968  C  CG  . LEU C  3 85  ? -22.153 -18.170 -56.544  1.00 236.35 ? 83   LEU C CG  1 
ATOM   6969  C  CD1 . LEU C  3 85  ? -22.279 -18.945 -57.848  1.00 251.38 ? 83   LEU C CD1 1 
ATOM   6970  C  CD2 . LEU C  3 85  ? -23.357 -18.424 -55.647  1.00 221.19 ? 83   LEU C CD2 1 
ATOM   6971  N  N   . MET C  3 86  ? -19.271 -19.415 -53.404  1.00 222.91 ? 84   MET C N   1 
ATOM   6972  C  CA  . MET C  3 86  ? -18.139 -20.007 -52.712  1.00 217.05 ? 84   MET C CA  1 
ATOM   6973  C  C   . MET C  3 86  ? -17.323 -20.880 -53.660  1.00 221.78 ? 84   MET C C   1 
ATOM   6974  O  O   . MET C  3 86  ? -17.559 -20.930 -54.869  1.00 229.57 ? 84   MET C O   1 
ATOM   6975  C  CB  . MET C  3 86  ? -18.605 -20.813 -51.501  1.00 217.95 ? 84   MET C CB  1 
ATOM   6976  C  CG  . MET C  3 86  ? -19.366 -22.086 -51.839  1.00 222.29 ? 84   MET C CG  1 
ATOM   6977  S  SD  . MET C  3 86  ? -19.596 -23.138 -50.390  1.00 221.45 ? 84   MET C SD  1 
ATOM   6978  C  CE  . MET C  3 86  ? -20.373 -24.584 -51.111  1.00 234.64 ? 84   MET C CE  1 
ATOM   6979  N  N   . VAL C  3 87  ? -16.343 -21.583 -53.097  1.00 229.18 ? 85   VAL C N   1 
ATOM   6980  C  CA  . VAL C  3 87  ? -15.457 -22.455 -53.855  1.00 248.20 ? 85   VAL C CA  1 
ATOM   6981  C  C   . VAL C  3 87  ? -15.948 -23.890 -53.728  1.00 252.01 ? 85   VAL C C   1 
ATOM   6982  O  O   . VAL C  3 87  ? -16.529 -24.292 -52.714  1.00 268.59 ? 85   VAL C O   1 
ATOM   6983  C  CB  . VAL C  3 87  ? -13.996 -22.311 -53.377  1.00 248.23 ? 85   VAL C CB  1 
ATOM   6984  C  CG1 . VAL C  3 87  ? -13.059 -23.149 -54.236  1.00 250.16 ? 85   VAL C CG1 1 
ATOM   6985  C  CG2 . VAL C  3 87  ? -13.576 -20.851 -53.408  1.00 242.93 ? 85   VAL C CG2 1 
ATOM   6986  N  N   . GLU C  3 88  ? -15.714 -24.670 -54.779  1.00 235.02 ? 86   GLU C N   1 
ATOM   6987  C  CA  . GLU C  3 88  ? -16.125 -26.062 -54.810  1.00 234.82 ? 86   GLU C CA  1 
ATOM   6988  C  C   . GLU C  3 88  ? -15.314 -26.881 -53.815  1.00 238.17 ? 86   GLU C C   1 
ATOM   6989  O  O   . GLU C  3 88  ? -14.396 -26.390 -53.156  1.00 233.03 ? 86   GLU C O   1 
ATOM   6990  C  CB  . GLU C  3 88  ? -15.977 -26.610 -56.225  1.00 244.40 ? 86   GLU C CB  1 
ATOM   6991  C  CG  . GLU C  3 88  ? -16.585 -25.705 -57.277  1.00 243.50 ? 86   GLU C CG  1 
ATOM   6992  C  CD  . GLU C  3 88  ? -16.214 -26.098 -58.687  1.00 256.31 ? 86   GLU C CD  1 
ATOM   6993  O  OE1 . GLU C  3 88  ? -15.554 -27.142 -58.864  1.00 256.09 ? 86   GLU C OE1 1 
ATOM   6994  O  OE2 . GLU C  3 88  ? -16.583 -25.355 -59.620  1.00 265.45 ? 86   GLU C OE2 1 
ATOM   6995  N  N   . THR C  3 89  ? -15.662 -28.162 -53.713  1.00 248.79 ? 87   THR C N   1 
ATOM   6996  C  CA  . THR C  3 89  ? -14.832 -29.096 -52.964  1.00 245.47 ? 87   THR C CA  1 
ATOM   6997  C  C   . THR C  3 89  ? -13.489 -29.337 -53.638  1.00 238.68 ? 87   THR C C   1 
ATOM   6998  O  O   . THR C  3 89  ? -12.660 -30.075 -53.094  1.00 232.60 ? 87   THR C O   1 
ATOM   6999  C  CB  . THR C  3 89  ? -15.576 -30.416 -52.772  1.00 241.96 ? 87   THR C CB  1 
ATOM   7000  O  OG1 . THR C  3 89  ? -16.061 -30.883 -54.040  1.00 235.52 ? 87   THR C OG1 1 
ATOM   7001  C  CG2 . THR C  3 89  ? -16.747 -30.221 -51.816  1.00 231.58 ? 87   THR C CG2 1 
ATOM   7002  N  N   . HIS C  3 90  ? -13.266 -28.735 -54.800  1.00 233.01 ? 88   HIS C N   1 
ATOM   7003  C  CA  . HIS C  3 90  ? -11.980 -28.755 -55.480  1.00 233.75 ? 88   HIS C CA  1 
ATOM   7004  C  C   . HIS C  3 90  ? -11.157 -27.558 -55.003  1.00 234.33 ? 88   HIS C C   1 
ATOM   7005  O  O   . HIS C  3 90  ? -11.442 -26.979 -53.953  1.00 234.46 ? 88   HIS C O   1 
ATOM   7006  C  CB  . HIS C  3 90  ? -12.195 -28.750 -56.995  1.00 234.06 ? 88   HIS C CB  1 
ATOM   7007  C  CG  . HIS C  3 90  ? -13.186 -29.765 -57.467  1.00 247.11 ? 88   HIS C CG  1 
ATOM   7008  N  ND1 . HIS C  3 90  ? -14.534 -29.672 -57.194  1.00 230.97 ? 88   HIS C ND1 1 
ATOM   7009  C  CD2 . HIS C  3 90  ? -13.026 -30.894 -58.196  1.00 272.29 ? 88   HIS C CD2 1 
ATOM   7010  C  CE1 . HIS C  3 90  ? -15.161 -30.702 -57.733  1.00 256.75 ? 88   HIS C CE1 1 
ATOM   7011  N  NE2 . HIS C  3 90  ? -14.269 -31.458 -58.347  1.00 275.11 ? 88   HIS C NE2 1 
ATOM   7012  N  N   . ASN C  3 91  ? -10.132 -27.178 -55.763  1.00 246.90 ? 89   ASN C N   1 
ATOM   7013  C  CA  . ASN C  3 91  ? -9.361  -25.956 -55.518  1.00 246.86 ? 89   ASN C CA  1 
ATOM   7014  C  C   . ASN C  3 91  ? -8.814  -25.902 -54.091  1.00 238.96 ? 89   ASN C C   1 
ATOM   7015  O  O   . ASN C  3 91  ? -8.952  -24.901 -53.383  1.00 228.62 ? 89   ASN C O   1 
ATOM   7016  C  CB  . ASN C  3 91  ? -10.195 -24.714 -55.834  1.00 231.88 ? 89   ASN C CB  1 
ATOM   7017  C  CG  . ASN C  3 91  ? -10.417 -24.530 -57.324  1.00 247.35 ? 89   ASN C CG  1 
ATOM   7018  O  OD1 . ASN C  3 91  ? -9.630  -25.007 -58.144  1.00 269.66 ? 89   ASN C OD1 1 
ATOM   7019  N  ND2 . ASN C  3 91  ? -11.489 -23.832 -57.683  1.00 234.48 ? 89   ASN C ND2 1 
ATOM   7020  N  N   . GLU C  3 92  ? -8.189  -27.004 -53.674  1.00 243.41 ? 90   GLU C N   1 
ATOM   7021  C  CA  . GLU C  3 92  ? -7.428  -27.126 -52.434  1.00 237.35 ? 90   GLU C CA  1 
ATOM   7022  C  C   . GLU C  3 92  ? -8.292  -27.083 -51.182  1.00 232.32 ? 90   GLU C C   1 
ATOM   7023  O  O   . GLU C  3 92  ? -7.752  -26.968 -50.072  1.00 233.93 ? 90   GLU C O   1 
ATOM   7024  C  CB  . GLU C  3 92  ? -6.337  -26.055 -52.341  1.00 237.86 ? 90   GLU C CB  1 
ATOM   7025  C  CG  . GLU C  3 92  ? -5.342  -26.104 -53.488  1.00 246.66 ? 90   GLU C CG  1 
ATOM   7026  C  CD  . GLU C  3 92  ? -4.408  -24.916 -53.498  1.00 247.33 ? 90   GLU C CD  1 
ATOM   7027  O  OE1 . GLU C  3 92  ? -4.652  -23.972 -52.720  1.00 251.98 ? 90   GLU C OE1 1 
ATOM   7028  O  OE2 . GLU C  3 92  ? -3.431  -24.927 -54.279  1.00 241.47 ? 90   GLU C OE2 1 
ATOM   7029  N  N   . ILE C  3 93  ? -9.620  -27.170 -51.317  1.00 232.56 ? 91   ILE C N   1 
ATOM   7030  C  CA  . ILE C  3 93  ? -10.488 -27.294 -50.146  1.00 233.72 ? 91   ILE C CA  1 
ATOM   7031  C  C   . ILE C  3 93  ? -10.450 -28.697 -49.564  1.00 241.81 ? 91   ILE C C   1 
ATOM   7032  O  O   . ILE C  3 93  ? -11.053 -28.945 -48.510  1.00 239.79 ? 91   ILE C O   1 
ATOM   7033  C  CB  . ILE C  3 93  ? -11.919 -26.864 -50.533  1.00 236.01 ? 91   ILE C CB  1 
ATOM   7034  C  CG1 . ILE C  3 93  ? -11.885 -25.555 -51.324  1.00 230.82 ? 91   ILE C CG1 1 
ATOM   7035  C  CG2 . ILE C  3 93  ? -12.789 -26.656 -49.305  1.00 232.21 ? 91   ILE C CG2 1 
ATOM   7036  C  CD1 . ILE C  3 93  ? -11.204 -24.414 -50.600  1.00 225.17 ? 91   ILE C CD1 1 
ATOM   7037  N  N   . TYR C  3 94  ? -9.728  -29.618 -50.203  1.00 254.94 ? 92   TYR C N   1 
ATOM   7038  C  CA  . TYR C  3 94  ? -9.690  -31.011 -49.789  1.00 261.58 ? 92   TYR C CA  1 
ATOM   7039  C  C   . TYR C  3 94  ? -8.414  -31.404 -49.055  1.00 271.58 ? 92   TYR C C   1 
ATOM   7040  O  O   . TYR C  3 94  ? -8.377  -32.484 -48.454  1.00 269.94 ? 92   TYR C O   1 
ATOM   7041  C  CB  . TYR C  3 94  ? -9.884  -31.931 -51.010  1.00 255.70 ? 92   TYR C CB  1 
ATOM   7042  C  CG  . TYR C  3 94  ? -9.044  -31.582 -52.225  1.00 244.16 ? 92   TYR C CG  1 
ATOM   7043  C  CD1 . TYR C  3 94  ? -9.436  -30.578 -53.104  1.00 242.80 ? 92   TYR C CD1 1 
ATOM   7044  C  CD2 . TYR C  3 94  ? -7.875  -32.278 -52.511  1.00 240.20 ? 92   TYR C CD2 1 
ATOM   7045  C  CE1 . TYR C  3 94  ? -8.678  -30.264 -54.216  1.00 252.88 ? 92   TYR C CE1 1 
ATOM   7046  C  CE2 . TYR C  3 94  ? -7.110  -31.971 -53.622  1.00 240.72 ? 92   TYR C CE2 1 
ATOM   7047  C  CZ  . TYR C  3 94  ? -7.517  -30.963 -54.472  1.00 244.00 ? 92   TYR C CZ  1 
ATOM   7048  O  OH  . TYR C  3 94  ? -6.764  -30.652 -55.581  1.00 234.28 ? 92   TYR C OH  1 
ATOM   7049  N  N   . ASP C  3 95  ? -7.376  -30.565 -49.071  1.00 275.30 ? 93   ASP C N   1 
ATOM   7050  C  CA  . ASP C  3 95  ? -6.119  -30.906 -48.416  1.00 274.41 ? 93   ASP C CA  1 
ATOM   7051  C  C   . ASP C  3 95  ? -6.145  -30.678 -46.911  1.00 263.63 ? 93   ASP C C   1 
ATOM   7052  O  O   . ASP C  3 95  ? -5.221  -31.124 -46.219  1.00 259.77 ? 93   ASP C O   1 
ATOM   7053  C  CB  . ASP C  3 95  ? -4.966  -30.098 -49.024  1.00 266.76 ? 93   ASP C CB  1 
ATOM   7054  C  CG  . ASP C  3 95  ? -4.767  -30.374 -50.505  1.00 265.00 ? 93   ASP C CG  1 
ATOM   7055  O  OD1 . ASP C  3 95  ? -5.423  -31.292 -51.039  1.00 264.39 ? 93   ASP C OD1 1 
ATOM   7056  O  OD2 . ASP C  3 95  ? -3.942  -29.679 -51.135  1.00 266.25 ? 93   ASP C OD2 1 
ATOM   7057  N  N   . LYS C  3 96  ? -7.167  -30.014 -46.388  1.00 263.49 ? 94   LYS C N   1 
ATOM   7058  C  CA  . LYS C  3 96  ? -7.158  -29.574 -44.999  1.00 267.41 ? 94   LYS C CA  1 
ATOM   7059  C  C   . LYS C  3 96  ? -8.289  -30.150 -44.159  1.00 280.41 ? 94   LYS C C   1 
ATOM   7060  O  O   . LYS C  3 96  ? -8.074  -30.456 -42.982  1.00 279.93 ? 94   LYS C O   1 
ATOM   7061  C  CB  . LYS C  3 96  ? -7.211  -28.042 -44.942  1.00 261.74 ? 94   LYS C CB  1 
ATOM   7062  C  CG  . LYS C  3 96  ? -6.027  -27.349 -45.591  1.00 259.02 ? 94   LYS C CG  1 
ATOM   7063  C  CD  . LYS C  3 96  ? -4.782  -27.500 -44.745  1.00 256.97 ? 94   LYS C CD  1 
ATOM   7064  C  CE  . LYS C  3 96  ? -3.749  -26.461 -45.124  1.00 253.56 ? 94   LYS C CE  1 
ATOM   7065  N  NZ  . LYS C  3 96  ? -3.463  -26.475 -46.583  1.00 254.55 ? 94   LYS C NZ  1 
ATOM   7066  N  N   . PHE C  3 97  ? -9.489  -30.311 -44.717  1.00 290.78 ? 95   PHE C N   1 
ATOM   7067  C  CA  . PHE C  3 97  ? -10.640 -30.633 -43.882  1.00 293.74 ? 95   PHE C CA  1 
ATOM   7068  C  C   . PHE C  3 97  ? -11.331 -31.922 -44.320  1.00 302.50 ? 95   PHE C C   1 
ATOM   7069  O  O   . PHE C  3 97  ? -10.791 -33.004 -44.117  1.00 319.33 ? 95   PHE C O   1 
ATOM   7070  C  CB  . PHE C  3 97  ? -11.627 -29.471 -43.898  1.00 294.95 ? 95   PHE C CB  1 
ATOM   7071  C  CG  . PHE C  3 97  ? -10.969 -28.127 -43.828  1.00 302.76 ? 95   PHE C CG  1 
ATOM   7072  C  CD1 . PHE C  3 97  ? -10.614 -27.582 -42.604  1.00 291.84 ? 95   PHE C CD1 1 
ATOM   7073  C  CD2 . PHE C  3 97  ? -10.682 -27.422 -44.985  1.00 307.21 ? 95   PHE C CD2 1 
ATOM   7074  C  CE1 . PHE C  3 97  ? -9.997  -26.354 -42.533  1.00 283.28 ? 95   PHE C CE1 1 
ATOM   7075  C  CE2 . PHE C  3 97  ? -10.061 -26.190 -44.919  1.00 301.13 ? 95   PHE C CE2 1 
ATOM   7076  C  CZ  . PHE C  3 97  ? -9.718  -25.655 -43.688  1.00 288.73 ? 95   PHE C CZ  1 
ATOM   7077  N  N   . LYS C  3 98  ? -12.540 -31.781 -44.870  1.00 300.29 ? 96   LYS C N   1 
ATOM   7078  C  CA  . LYS C  3 98  ? -13.292 -32.834 -45.557  1.00 309.59 ? 96   LYS C CA  1 
ATOM   7079  C  C   . LYS C  3 98  ? -14.070 -33.767 -44.629  1.00 313.03 ? 96   LYS C C   1 
ATOM   7080  O  O   . LYS C  3 98  ? -15.277 -33.941 -44.816  1.00 310.53 ? 96   LYS C O   1 
ATOM   7081  C  CB  . LYS C  3 98  ? -12.368 -33.655 -46.463  1.00 314.75 ? 96   LYS C CB  1 
ATOM   7082  C  CG  . LYS C  3 98  ? -13.040 -34.881 -47.075  1.00 314.25 ? 96   LYS C CG  1 
ATOM   7083  C  CD  . LYS C  3 98  ? -12.035 -35.808 -47.753  1.00 313.46 ? 96   LYS C CD  1 
ATOM   7084  C  CE  . LYS C  3 98  ? -12.686 -37.131 -48.154  1.00 318.11 ? 96   LYS C CE  1 
ATOM   7085  N  NZ  . LYS C  3 98  ? -11.736 -38.092 -48.792  1.00 328.01 ? 96   LYS C NZ  1 
ATOM   7086  N  N   . GLN C  3 99  ? -13.418 -34.371 -43.632  1.00 317.42 ? 97   GLN C N   1 
ATOM   7087  C  CA  . GLN C  3 99  ? -13.972 -35.556 -42.977  1.00 320.11 ? 97   GLN C CA  1 
ATOM   7088  C  C   . GLN C  3 99  ? -14.510 -35.312 -41.570  1.00 318.62 ? 97   GLN C C   1 
ATOM   7089  O  O   . GLN C  3 99  ? -14.822 -36.282 -40.868  1.00 322.59 ? 97   GLN C O   1 
ATOM   7090  C  CB  . GLN C  3 99  ? -12.933 -36.679 -42.914  1.00 319.48 ? 97   GLN C CB  1 
ATOM   7091  C  CG  . GLN C  3 99  ? -11.942 -36.708 -44.063  1.00 323.75 ? 97   GLN C CG  1 
ATOM   7092  C  CD  . GLN C  3 99  ? -10.628 -36.037 -43.708  1.00 320.47 ? 97   GLN C CD  1 
ATOM   7093  O  OE1 . GLN C  3 99  ? -10.488 -35.453 -42.632  1.00 327.70 ? 97   GLN C OE1 1 
ATOM   7094  N  NE2 . GLN C  3 99  ? -9.657  -36.120 -44.611  1.00 313.52 ? 97   GLN C NE2 1 
ATOM   7095  N  N   . SER C  3 100 ? -14.621 -34.064 -41.124  1.00 300.08 ? 98   SER C N   1 
ATOM   7096  C  CA  . SER C  3 100 ? -15.295 -33.815 -39.851  1.00 289.74 ? 98   SER C CA  1 
ATOM   7097  C  C   . SER C  3 100 ? -16.785 -33.825 -40.154  1.00 293.46 ? 98   SER C C   1 
ATOM   7098  O  O   . SER C  3 100 ? -17.382 -32.806 -40.504  1.00 289.09 ? 98   SER C O   1 
ATOM   7099  C  CB  . SER C  3 100 ? -14.837 -32.509 -39.216  1.00 280.80 ? 98   SER C CB  1 
ATOM   7100  O  OG  . SER C  3 100 ? -15.158 -31.404 -40.033  1.00 277.56 ? 98   SER C OG  1 
ATOM   7101  N  N   . THR C  3 101 ? -17.387 -35.015 -40.035  1.00 300.27 ? 99   THR C N   1 
ATOM   7102  C  CA  . THR C  3 101 ? -18.770 -35.211 -40.451  1.00 297.77 ? 99   THR C CA  1 
ATOM   7103  C  C   . THR C  3 101 ? -19.735 -34.317 -39.691  1.00 291.33 ? 99   THR C C   1 
ATOM   7104  O  O   . THR C  3 101 ? -20.877 -34.150 -40.130  1.00 289.34 ? 99   THR C O   1 
ATOM   7105  C  CB  . THR C  3 101 ? -19.181 -36.675 -40.270  1.00 295.49 ? 99   THR C CB  1 
ATOM   7106  O  OG1 . THR C  3 101 ? -19.207 -36.998 -38.874  1.00 290.94 ? 99   THR C OG1 1 
ATOM   7107  C  CG2 . THR C  3 101 ? -18.205 -37.596 -40.987  1.00 294.88 ? 99   THR C CG2 1 
ATOM   7108  N  N   . HIS C  3 102 ? -19.306 -33.735 -38.569  1.00 285.46 ? 100  HIS C N   1 
ATOM   7109  C  CA  . HIS C  3 102 ? -20.143 -32.860 -37.758  1.00 284.19 ? 100  HIS C CA  1 
ATOM   7110  C  C   . HIS C  3 102 ? -19.844 -31.383 -37.992  1.00 275.46 ? 100  HIS C C   1 
ATOM   7111  O  O   . HIS C  3 102 ? -20.051 -30.558 -37.094  1.00 269.35 ? 100  HIS C O   1 
ATOM   7112  C  CB  . HIS C  3 102 ? -19.981 -33.204 -36.279  1.00 288.83 ? 100  HIS C CB  1 
ATOM   7113  C  CG  . HIS C  3 102 ? -20.303 -34.627 -35.951  1.00 298.98 ? 100  HIS C CG  1 
ATOM   7114  N  ND1 . HIS C  3 102 ? -21.557 -35.032 -35.549  1.00 300.42 ? 100  HIS C ND1 1 
ATOM   7115  C  CD2 . HIS C  3 102 ? -19.536 -35.742 -35.969  1.00 302.17 ? 100  HIS C CD2 1 
ATOM   7116  C  CE1 . HIS C  3 102 ? -21.548 -36.335 -35.330  1.00 304.75 ? 100  HIS C CE1 1 
ATOM   7117  N  NE2 . HIS C  3 102 ? -20.333 -36.790 -35.576  1.00 306.74 ? 100  HIS C NE2 1 
ATOM   7118  N  N   . SER C  3 103 ? -19.362 -31.027 -39.180  1.00 283.95 ? 101  SER C N   1 
ATOM   7119  C  CA  . SER C  3 103 ? -19.025 -29.640 -39.470  1.00 278.55 ? 101  SER C CA  1 
ATOM   7120  C  C   . SER C  3 103 ? -19.045 -29.422 -40.977  1.00 281.18 ? 101  SER C C   1 
ATOM   7121  O  O   . SER C  3 103 ? -18.996 -30.372 -41.762  1.00 288.12 ? 101  SER C O   1 
ATOM   7122  C  CB  . SER C  3 103 ? -17.658 -29.264 -38.886  1.00 276.43 ? 101  SER C CB  1 
ATOM   7123  O  OG  . SER C  3 103 ? -17.612 -29.504 -37.489  1.00 273.75 ? 101  SER C OG  1 
ATOM   7124  N  N   . ILE C  3 104 ? -19.119 -28.150 -41.368  1.00 270.54 ? 102  ILE C N   1 
ATOM   7125  C  CA  . ILE C  3 104 ? -19.109 -27.749 -42.772  1.00 267.60 ? 102  ILE C CA  1 
ATOM   7126  C  C   . ILE C  3 104 ? -18.195 -26.540 -42.922  1.00 263.88 ? 102  ILE C C   1 
ATOM   7127  O  O   . ILE C  3 104 ? -18.311 -25.571 -42.164  1.00 254.59 ? 102  ILE C O   1 
ATOM   7128  C  CB  . ILE C  3 104 ? -20.525 -27.432 -43.291  1.00 259.88 ? 102  ILE C CB  1 
ATOM   7129  C  CG1 . ILE C  3 104 ? -21.270 -28.730 -43.621  1.00 266.12 ? 102  ILE C CG1 1 
ATOM   7130  C  CG2 . ILE C  3 104 ? -20.463 -26.513 -44.501  1.00 259.02 ? 102  ILE C CG2 1 
ATOM   7131  C  CD1 . ILE C  3 104 ? -22.656 -28.531 -44.197  1.00 265.45 ? 102  ILE C CD1 1 
ATOM   7132  N  N   . TYR C  3 105 ? -17.292 -26.591 -43.899  1.00 274.10 ? 103  TYR C N   1 
ATOM   7133  C  CA  . TYR C  3 105 ? -16.306 -25.541 -44.115  1.00 272.96 ? 103  TYR C CA  1 
ATOM   7134  C  C   . TYR C  3 105 ? -16.573 -24.825 -45.432  1.00 272.66 ? 103  TYR C C   1 
ATOM   7135  O  O   . TYR C  3 105 ? -16.860 -25.463 -46.449  1.00 281.45 ? 103  TYR C O   1 
ATOM   7136  C  CB  . TYR C  3 105 ? -14.889 -26.115 -44.115  1.00 277.70 ? 103  TYR C CB  1 
ATOM   7137  C  CG  . TYR C  3 105 ? -14.609 -27.011 -42.936  1.00 278.27 ? 103  TYR C CG  1 
ATOM   7138  C  CD1 . TYR C  3 105 ? -14.173 -26.484 -41.728  1.00 272.23 ? 103  TYR C CD1 1 
ATOM   7139  C  CD2 . TYR C  3 105 ? -14.788 -28.384 -43.027  1.00 281.44 ? 103  TYR C CD2 1 
ATOM   7140  C  CE1 . TYR C  3 105 ? -13.919 -27.302 -40.645  1.00 275.36 ? 103  TYR C CE1 1 
ATOM   7141  C  CE2 . TYR C  3 105 ? -14.535 -29.207 -41.954  1.00 280.93 ? 103  TYR C CE2 1 
ATOM   7142  C  CZ  . TYR C  3 105 ? -14.101 -28.663 -40.763  1.00 281.82 ? 103  TYR C CZ  1 
ATOM   7143  O  OH  . TYR C  3 105 ? -13.850 -29.485 -39.688  1.00 288.28 ? 103  TYR C OH  1 
ATOM   7144  N  N   . MET C  3 106 ? -16.461 -23.496 -45.410  1.00 266.62 ? 104  MET C N   1 
ATOM   7145  C  CA  . MET C  3 106 ? -16.730 -22.660 -46.571  1.00 261.77 ? 104  MET C CA  1 
ATOM   7146  C  C   . MET C  3 106 ? -15.576 -21.691 -46.786  1.00 255.27 ? 104  MET C C   1 
ATOM   7147  O  O   . MET C  3 106 ? -15.056 -21.115 -45.827  1.00 248.89 ? 104  MET C O   1 
ATOM   7148  C  CB  . MET C  3 106 ? -18.042 -21.892 -46.394  1.00 259.24 ? 104  MET C CB  1 
ATOM   7149  C  CG  . MET C  3 106 ? -19.228 -22.788 -46.079  1.00 263.54 ? 104  MET C CG  1 
ATOM   7150  S  SD  . MET C  3 106 ? -20.669 -21.870 -45.518  1.00 274.74 ? 104  MET C SD  1 
ATOM   7151  C  CE  . MET C  3 106 ? -20.037 -21.132 -44.012  1.00 271.25 ? 104  MET C CE  1 
ATOM   7152  N  N   . PHE C  3 107 ? -15.182 -21.507 -48.047  1.00 269.47 ? 105  PHE C N   1 
ATOM   7153  C  CA  . PHE C  3 107 ? -14.017 -20.701 -48.388  1.00 278.89 ? 105  PHE C CA  1 
ATOM   7154  C  C   . PHE C  3 107 ? -14.330 -19.769 -49.552  1.00 283.55 ? 105  PHE C C   1 
ATOM   7155  O  O   . PHE C  3 107 ? -15.163 -20.076 -50.411  1.00 286.72 ? 105  PHE C O   1 
ATOM   7156  C  CB  . PHE C  3 107 ? -12.807 -21.594 -48.733  1.00 287.80 ? 105  PHE C CB  1 
ATOM   7157  C  CG  . PHE C  3 107 ? -12.028 -22.055 -47.528  1.00 281.76 ? 105  PHE C CG  1 
ATOM   7158  C  CD1 . PHE C  3 107 ? -12.519 -23.055 -46.703  1.00 271.96 ? 105  PHE C CD1 1 
ATOM   7159  C  CD2 . PHE C  3 107 ? -10.798 -21.489 -47.228  1.00 283.87 ? 105  PHE C CD2 1 
ATOM   7160  C  CE1 . PHE C  3 107 ? -11.803 -23.473 -45.599  1.00 269.13 ? 105  PHE C CE1 1 
ATOM   7161  C  CE2 . PHE C  3 107 ? -10.076 -21.906 -46.127  1.00 284.53 ? 105  PHE C CE2 1 
ATOM   7162  C  CZ  . PHE C  3 107 ? -10.579 -22.896 -45.312  1.00 278.30 ? 105  PHE C CZ  1 
ATOM   7163  N  N   . PHE C  3 108 ? -13.647 -18.621 -49.573  1.00 282.91 ? 106  PHE C N   1 
ATOM   7164  C  CA  . PHE C  3 108 ? -13.839 -17.610 -50.606  1.00 275.27 ? 106  PHE C CA  1 
ATOM   7165  C  C   . PHE C  3 108 ? -12.491 -17.043 -51.038  1.00 271.42 ? 106  PHE C C   1 
ATOM   7166  O  O   . PHE C  3 108 ? -11.466 -17.242 -50.379  1.00 272.94 ? 106  PHE C O   1 
ATOM   7167  C  CB  . PHE C  3 108 ? -14.748 -16.473 -50.122  1.00 261.90 ? 106  PHE C CB  1 
ATOM   7168  C  CG  . PHE C  3 108 ? -16.130 -16.916 -49.736  1.00 261.09 ? 106  PHE C CG  1 
ATOM   7169  C  CD1 . PHE C  3 108 ? -17.155 -16.927 -50.670  1.00 267.13 ? 106  PHE C CD1 1 
ATOM   7170  C  CD2 . PHE C  3 108 ? -16.410 -17.308 -48.436  1.00 258.92 ? 106  PHE C CD2 1 
ATOM   7171  C  CE1 . PHE C  3 108 ? -18.430 -17.326 -50.318  1.00 270.60 ? 106  PHE C CE1 1 
ATOM   7172  C  CE2 . PHE C  3 108 ? -17.682 -17.708 -48.076  1.00 265.36 ? 106  PHE C CE2 1 
ATOM   7173  C  CZ  . PHE C  3 108 ? -18.695 -17.717 -49.019  1.00 272.68 ? 106  PHE C CZ  1 
ATOM   7174  N  N   . GLN C  3 109 ? -12.505 -16.320 -52.155  1.00 255.49 ? 107  GLN C N   1 
ATOM   7175  C  CA  . GLN C  3 109 ? -11.312 -15.698 -52.715  1.00 245.59 ? 107  GLN C CA  1 
ATOM   7176  C  C   . GLN C  3 109 ? -11.382 -14.187 -52.531  1.00 252.03 ? 107  GLN C C   1 
ATOM   7177  O  O   . GLN C  3 109 ? -12.400 -13.565 -52.854  1.00 256.68 ? 107  GLN C O   1 
ATOM   7178  C  CB  . GLN C  3 109 ? -11.159 -16.042 -54.199  1.00 241.99 ? 107  GLN C CB  1 
ATOM   7179  C  CG  . GLN C  3 109 ? -10.890 -17.516 -54.475  1.00 246.33 ? 107  GLN C CG  1 
ATOM   7180  C  CD  . GLN C  3 109 ? -10.721 -17.817 -55.956  1.00 259.73 ? 107  GLN C CD  1 
ATOM   7181  O  OE1 . GLN C  3 109 ? -10.957 -16.962 -56.810  1.00 268.01 ? 107  GLN C OE1 1 
ATOM   7182  N  NE2 . GLN C  3 109 ? -10.308 -19.041 -56.265  1.00 263.24 ? 107  GLN C NE2 1 
ATOM   7183  N  N   . THR C  3 110 ? -10.298 -13.601 -52.021  1.00 254.49 ? 108  THR C N   1 
ATOM   7184  C  CA  . THR C  3 110 ? -10.253 -12.158 -51.814  1.00 255.24 ? 108  THR C CA  1 
ATOM   7185  C  C   . THR C  3 110 ? -10.054 -11.392 -53.113  1.00 259.68 ? 108  THR C C   1 
ATOM   7186  O  O   . THR C  3 110 ? -10.394 -10.205 -53.176  1.00 247.77 ? 108  THR C O   1 
ATOM   7187  C  CB  . THR C  3 110 ? -9.134  -11.794 -50.834  1.00 255.66 ? 108  THR C CB  1 
ATOM   7188  O  OG1 . THR C  3 110 ? -9.097  -12.755 -49.771  1.00 260.32 ? 108  THR C OG1 1 
ATOM   7189  C  CG2 . THR C  3 110 ? -9.356  -10.405 -50.242  1.00 249.14 ? 108  THR C CG2 1 
ATOM   7190  N  N   . SER C  3 111 ? -9.516  -12.044 -54.148  1.00 286.07 ? 109  SER C N   1 
ATOM   7191  C  CA  . SER C  3 111 ? -9.296  -11.372 -55.423  1.00 291.02 ? 109  SER C CA  1 
ATOM   7192  C  C   . SER C  3 111 ? -10.602 -10.921 -56.067  1.00 278.62 ? 109  SER C C   1 
ATOM   7193  O  O   . SER C  3 111 ? -10.590 -10.001 -56.893  1.00 282.10 ? 109  SER C O   1 
ATOM   7194  C  CB  . SER C  3 111 ? -8.521  -12.290 -56.378  1.00 288.27 ? 109  SER C CB  1 
ATOM   7195  O  OG  . SER C  3 111 ? -7.262  -12.667 -55.839  1.00 276.93 ? 109  SER C OG  1 
ATOM   7196  N  N   . GLU C  3 112 ? -11.727 -11.541 -55.707  1.00 253.67 ? 110  GLU C N   1 
ATOM   7197  C  CA  . GLU C  3 112 ? -13.028 -11.128 -56.210  1.00 249.32 ? 110  GLU C CA  1 
ATOM   7198  C  C   . GLU C  3 112 ? -13.811 -10.292 -55.210  1.00 249.82 ? 110  GLU C C   1 
ATOM   7199  O  O   . GLU C  3 112 ? -14.746 -9.588  -55.609  1.00 251.03 ? 110  GLU C O   1 
ATOM   7200  C  CB  . GLU C  3 112 ? -13.856 -12.361 -56.597  1.00 247.29 ? 110  GLU C CB  1 
ATOM   7201  C  CG  . GLU C  3 112 ? -13.119 -13.327 -57.507  1.00 254.47 ? 110  GLU C CG  1 
ATOM   7202  C  CD  . GLU C  3 112 ? -13.949 -14.541 -57.866  1.00 258.31 ? 110  GLU C CD  1 
ATOM   7203  O  OE1 . GLU C  3 112 ? -15.135 -14.584 -57.476  1.00 241.16 ? 110  GLU C OE1 1 
ATOM   7204  O  OE2 . GLU C  3 112 ? -13.414 -15.451 -58.538  1.00 273.93 ? 110  GLU C OE2 1 
ATOM   7205  N  N   . LEU C  3 113 ? -13.451 -10.354 -53.928  1.00 242.22 ? 111  LEU C N   1 
ATOM   7206  C  CA  . LEU C  3 113 ? -14.150 -9.565  -52.921  1.00 242.35 ? 111  LEU C CA  1 
ATOM   7207  C  C   . LEU C  3 113 ? -13.804 -8.091  -53.045  1.00 247.18 ? 111  LEU C C   1 
ATOM   7208  O  O   . LEU C  3 113 ? -14.692 -7.232  -53.043  1.00 249.34 ? 111  LEU C O   1 
ATOM   7209  C  CB  . LEU C  3 113 ? -13.800 -10.074 -51.527  1.00 241.91 ? 111  LEU C CB  1 
ATOM   7210  C  CG  . LEU C  3 113 ? -14.510 -11.364 -51.144  1.00 244.72 ? 111  LEU C CG  1 
ATOM   7211  C  CD1 . LEU C  3 113 ? -14.074 -11.790 -49.760  1.00 254.30 ? 111  LEU C CD1 1 
ATOM   7212  C  CD2 . LEU C  3 113 ? -16.014 -11.161 -51.209  1.00 240.12 ? 111  LEU C CD2 1 
ATOM   7213  N  N   . ARG C  3 114 ? -12.514 -7.779  -53.144  1.00 249.41 ? 112  ARG C N   1 
ATOM   7214  C  CA  . ARG C  3 114 ? -12.066 -6.404  -53.281  1.00 254.95 ? 112  ARG C CA  1 
ATOM   7215  C  C   . ARG C  3 114 ? -12.288 -5.851  -54.685  1.00 259.76 ? 112  ARG C C   1 
ATOM   7216  O  O   . ARG C  3 114 ? -11.776 -4.771  -55.001  1.00 274.36 ? 112  ARG C O   1 
ATOM   7217  C  CB  . ARG C  3 114 ? -10.591 -6.293  -52.882  1.00 263.10 ? 112  ARG C CB  1 
ATOM   7218  C  CG  . ARG C  3 114 ? -10.337 -6.551  -51.399  1.00 254.13 ? 112  ARG C CG  1 
ATOM   7219  C  CD  . ARG C  3 114 ? -8.900  -6.229  -50.998  1.00 258.98 ? 112  ARG C CD  1 
ATOM   7220  N  NE  . ARG C  3 114 ? -7.945  -7.231  -51.466  1.00 264.23 ? 112  ARG C NE  1 
ATOM   7221  C  CZ  . ARG C  3 114 ? -6.630  -7.160  -51.278  1.00 260.73 ? 112  ARG C CZ  1 
ATOM   7222  N  NH1 . ARG C  3 114 ? -6.101  -6.131  -50.629  1.00 259.02 ? 112  ARG C NH1 1 
ATOM   7223  N  NH2 . ARG C  3 114 ? -5.840  -8.120  -51.739  1.00 255.62 ? 112  ARG C NH2 1 
ATOM   7224  N  N   . GLU C  3 115 ? -13.037 -6.560  -55.529  1.00 249.36 ? 113  GLU C N   1 
ATOM   7225  C  CA  . GLU C  3 115 ? -13.457 -6.042  -56.824  1.00 251.91 ? 113  GLU C CA  1 
ATOM   7226  C  C   . GLU C  3 115 ? -14.901 -5.562  -56.809  1.00 249.71 ? 113  GLU C C   1 
ATOM   7227  O  O   . GLU C  3 115 ? -15.226 -4.567  -57.464  1.00 259.51 ? 113  GLU C O   1 
ATOM   7228  C  CB  . GLU C  3 115 ? -13.280 -7.115  -57.909  1.00 255.15 ? 113  GLU C CB  1 
ATOM   7229  C  CG  . GLU C  3 115 ? -13.237 -6.574  -59.336  1.00 271.09 ? 113  GLU C CG  1 
ATOM   7230  C  CD  . GLU C  3 115 ? -13.043 -7.673  -60.368  1.00 276.42 ? 113  GLU C CD  1 
ATOM   7231  O  OE1 . GLU C  3 115 ? -13.018 -8.858  -59.973  1.00 282.29 ? 113  GLU C OE1 1 
ATOM   7232  O  OE2 . GLU C  3 115 ? -12.917 -7.355  -61.572  1.00 270.14 ? 113  GLU C OE2 1 
ATOM   7233  N  N   . ALA C  3 116 ? -15.774 -6.247  -56.066  1.00 223.28 ? 114  ALA C N   1 
ATOM   7234  C  CA  . ALA C  3 116 ? -17.142 -5.770  -55.914  1.00 218.48 ? 114  ALA C CA  1 
ATOM   7235  C  C   . ALA C  3 116 ? -17.199 -4.569  -54.981  1.00 221.56 ? 114  ALA C C   1 
ATOM   7236  O  O   . ALA C  3 116 ? -17.976 -3.635  -55.206  1.00 224.35 ? 114  ALA C O   1 
ATOM   7237  C  CB  . ALA C  3 116 ? -18.035 -6.899  -55.398  1.00 214.85 ? 114  ALA C CB  1 
ATOM   7238  N  N   . VAL C  3 117 ? -16.381 -4.575  -53.934  1.00 231.89 ? 115  VAL C N   1 
ATOM   7239  C  CA  . VAL C  3 117 ? -16.298 -3.456  -52.999  1.00 245.51 ? 115  VAL C CA  1 
ATOM   7240  C  C   . VAL C  3 117 ? -14.839 -3.021  -52.890  1.00 258.27 ? 115  VAL C C   1 
ATOM   7241  O  O   . VAL C  3 117 ? -14.070 -3.627  -52.129  1.00 267.82 ? 115  VAL C O   1 
ATOM   7242  C  CB  . VAL C  3 117 ? -16.878 -3.833  -51.627  1.00 241.36 ? 115  VAL C CB  1 
ATOM   7243  C  CG1 . VAL C  3 117 ? -16.911 -2.622  -50.709  1.00 241.37 ? 115  VAL C CG1 1 
ATOM   7244  C  CG2 . VAL C  3 117 ? -18.271 -4.433  -51.777  1.00 235.47 ? 115  VAL C CG2 1 
ATOM   7245  N  N   . PRO C  3 118 ? -14.411 -1.988  -53.633  1.00 260.70 ? 116  PRO C N   1 
ATOM   7246  C  CA  . PRO C  3 118 ? -13.000 -1.572  -53.593  1.00 257.16 ? 116  PRO C CA  1 
ATOM   7247  C  C   . PRO C  3 118 ? -12.543 -1.088  -52.226  1.00 258.73 ? 116  PRO C C   1 
ATOM   7248  O  O   . PRO C  3 118 ? -11.559 -1.592  -51.676  1.00 248.30 ? 116  PRO C O   1 
ATOM   7249  C  CB  . PRO C  3 118 ? -12.940 -0.439  -54.627  1.00 259.99 ? 116  PRO C CB  1 
ATOM   7250  C  CG  . PRO C  3 118 ? -14.106 -0.682  -55.528  1.00 264.39 ? 116  PRO C CG  1 
ATOM   7251  C  CD  . PRO C  3 118 ? -15.179 -1.240  -54.643  1.00 258.95 ? 116  PRO C CD  1 
ATOM   7252  N  N   . GLU C  3 119 ? -13.245 -0.110  -51.668  1.00 283.00 ? 117  GLU C N   1 
ATOM   7253  C  CA  . GLU C  3 119 ? -12.826 0.456   -50.391  1.00 294.04 ? 117  GLU C CA  1 
ATOM   7254  C  C   . GLU C  3 119 ? -13.625 -0.160  -49.252  1.00 289.88 ? 117  GLU C C   1 
ATOM   7255  O  O   . GLU C  3 119 ? -14.856 -0.274  -49.358  1.00 287.83 ? 117  GLU C O   1 
ATOM   7256  C  CB  . GLU C  3 119 ? -13.011 1.970   -50.400  1.00 304.60 ? 117  GLU C CB  1 
ATOM   7257  C  CG  . GLU C  3 119 ? -12.416 2.678   -49.200  1.00 304.23 ? 117  GLU C CG  1 
ATOM   7258  C  CD  . GLU C  3 119 ? -12.439 4.186   -49.342  1.00 308.43 ? 117  GLU C CD  1 
ATOM   7259  O  OE1 . GLU C  3 119 ? -12.899 4.686   -50.393  1.00 313.87 ? 117  GLU C OE1 1 
ATOM   7260  O  OE2 . GLU C  3 119 ? -11.994 4.871   -48.398  1.00 308.25 ? 117  GLU C OE2 1 
ATOM   7261  N  N   . PRO C  3 120 ? -12.970 -0.569  -48.159  1.00 285.16 ? 118  PRO C N   1 
ATOM   7262  C  CA  . PRO C  3 120 ? -13.705 -1.191  -47.040  1.00 287.74 ? 118  PRO C CA  1 
ATOM   7263  C  C   . PRO C  3 120 ? -14.730 -0.279  -46.384  1.00 282.36 ? 118  PRO C C   1 
ATOM   7264  O  O   . PRO C  3 120 ? -15.636 -0.778  -45.701  1.00 272.63 ? 118  PRO C O   1 
ATOM   7265  C  CB  . PRO C  3 120 ? -12.587 -1.570  -46.057  1.00 283.97 ? 118  PRO C CB  1 
ATOM   7266  C  CG  . PRO C  3 120 ? -11.351 -1.664  -46.901  1.00 279.88 ? 118  PRO C CG  1 
ATOM   7267  C  CD  . PRO C  3 120 ? -11.512 -0.604  -47.951  1.00 278.97 ? 118  PRO C CD  1 
ATOM   7268  N  N   . VAL C  3 121 ? -14.612 1.040   -46.557  1.00 280.33 ? 119  VAL C N   1 
ATOM   7269  C  CA  . VAL C  3 121 ? -15.573 1.956   -45.952  1.00 269.23 ? 119  VAL C CA  1 
ATOM   7270  C  C   . VAL C  3 121 ? -16.899 1.911   -46.699  1.00 255.45 ? 119  VAL C C   1 
ATOM   7271  O  O   . VAL C  3 121 ? -17.964 2.111   -46.101  1.00 254.40 ? 119  VAL C O   1 
ATOM   7272  C  CB  . VAL C  3 121 ? -14.990 3.382   -45.909  1.00 283.43 ? 119  VAL C CB  1 
ATOM   7273  C  CG1 . VAL C  3 121 ? -15.803 4.260   -44.967  1.00 291.02 ? 119  VAL C CG1 1 
ATOM   7274  C  CG2 . VAL C  3 121 ? -13.523 3.353   -45.489  1.00 283.42 ? 119  VAL C CG2 1 
ATOM   7275  N  N   . LEU C  3 122 ? -16.862 1.645   -48.007  1.00 242.24 ? 120  LEU C N   1 
ATOM   7276  C  CA  . LEU C  3 122 ? -18.085 1.545   -48.794  1.00 240.45 ? 120  LEU C CA  1 
ATOM   7277  C  C   . LEU C  3 122 ? -18.980 0.410   -48.324  1.00 234.37 ? 120  LEU C C   1 
ATOM   7278  O  O   . LEU C  3 122 ? -20.197 0.473   -48.526  1.00 233.02 ? 120  LEU C O   1 
ATOM   7279  C  CB  . LEU C  3 122 ? -17.744 1.351   -50.272  1.00 247.06 ? 120  LEU C CB  1 
ATOM   7280  C  CG  . LEU C  3 122 ? -16.808 2.378   -50.908  1.00 261.05 ? 120  LEU C CG  1 
ATOM   7281  C  CD1 . LEU C  3 122 ? -16.476 1.993   -52.345  1.00 270.32 ? 120  LEU C CD1 1 
ATOM   7282  C  CD2 . LEU C  3 122 ? -17.412 3.776   -50.849  1.00 260.16 ? 120  LEU C CD2 1 
ATOM   7283  N  N   . LEU C  3 123 ? -18.410 -0.620  -47.704  1.00 224.33 ? 121  LEU C N   1 
ATOM   7284  C  CA  . LEU C  3 123 ? -19.200 -1.757  -47.254  1.00 218.62 ? 121  LEU C CA  1 
ATOM   7285  C  C   . LEU C  3 123 ? -20.152 -1.320  -46.149  1.00 226.87 ? 121  LEU C C   1 
ATOM   7286  O  O   . LEU C  3 123 ? -19.733 -0.723  -45.152  1.00 234.33 ? 121  LEU C O   1 
ATOM   7287  C  CB  . LEU C  3 123 ? -18.281 -2.878  -46.765  1.00 215.46 ? 121  LEU C CB  1 
ATOM   7288  C  CG  . LEU C  3 123 ? -18.796 -4.322  -46.781  1.00 209.74 ? 121  LEU C CG  1 
ATOM   7289  C  CD1 . LEU C  3 123 ? -19.695 -4.614  -45.594  1.00 205.33 ? 121  LEU C CD1 1 
ATOM   7290  C  CD2 . LEU C  3 123 ? -19.526 -4.612  -48.080  1.00 211.22 ? 121  LEU C CD2 1 
ATOM   7291  N  N   . SER C  3 124 ? -21.440 -1.615  -46.329  1.00 229.84 ? 122  SER C N   1 
ATOM   7292  C  CA  . SER C  3 124 ? -22.463 -1.269  -45.352  1.00 231.87 ? 122  SER C CA  1 
ATOM   7293  C  C   . SER C  3 124 ? -23.023 -2.500  -44.651  1.00 231.23 ? 122  SER C C   1 
ATOM   7294  O  O   . SER C  3 124 ? -22.994 -2.578  -43.419  1.00 233.93 ? 122  SER C O   1 
ATOM   7295  C  CB  . SER C  3 124 ? -23.593 -0.477  -46.027  1.00 232.95 ? 122  SER C CB  1 
ATOM   7296  O  OG  . SER C  3 124 ? -24.240 -1.251  -47.022  1.00 234.39 ? 122  SER C OG  1 
ATOM   7297  N  N   . ARG C  3 125 ? -23.534 -3.473  -45.402  1.00 229.71 ? 123  ARG C N   1 
ATOM   7298  C  CA  . ARG C  3 125 ? -24.088 -4.690  -44.821  1.00 216.92 ? 123  ARG C CA  1 
ATOM   7299  C  C   . ARG C  3 125 ? -23.608 -5.886  -45.632  1.00 223.01 ? 123  ARG C C   1 
ATOM   7300  O  O   . ARG C  3 125 ? -23.716 -5.888  -46.862  1.00 225.79 ? 123  ARG C O   1 
ATOM   7301  C  CB  . ARG C  3 125 ? -25.622 -4.634  -44.787  1.00 199.58 ? 123  ARG C CB  1 
ATOM   7302  C  CG  . ARG C  3 125 ? -26.289 -5.832  -44.128  1.00 192.83 ? 123  ARG C CG  1 
ATOM   7303  C  CD  . ARG C  3 125 ? -27.802 -5.667  -44.068  1.00 193.61 ? 123  ARG C CD  1 
ATOM   7304  N  NE  . ARG C  3 125 ? -28.453 -6.822  -43.453  1.00 197.50 ? 123  ARG C NE  1 
ATOM   7305  C  CZ  . ARG C  3 125 ? -28.796 -6.895  -42.170  1.00 189.77 ? 123  ARG C CZ  1 
ATOM   7306  N  NH1 . ARG C  3 125 ? -28.556 -5.875  -41.360  1.00 190.13 ? 123  ARG C NH1 1 
ATOM   7307  N  NH2 . ARG C  3 125 ? -29.383 -7.986  -41.696  1.00 188.88 ? 123  ARG C NH2 1 
ATOM   7308  N  N   . ALA C  3 126 ? -23.067 -6.892  -44.943  1.00 217.52 ? 124  ALA C N   1 
ATOM   7309  C  CA  . ALA C  3 126 ? -22.545 -8.104  -45.577  1.00 209.07 ? 124  ALA C CA  1 
ATOM   7310  C  C   . ALA C  3 126 ? -23.039 -9.311  -44.784  1.00 217.21 ? 124  ALA C C   1 
ATOM   7311  O  O   . ALA C  3 126 ? -22.426 -9.694  -43.783  1.00 227.02 ? 124  ALA C O   1 
ATOM   7312  C  CB  . ALA C  3 126 ? -21.021 -8.076  -45.648  1.00 204.04 ? 124  ALA C CB  1 
ATOM   7313  N  N   . GLU C  3 127 ? -24.138 -9.914  -45.235  1.00 219.71 ? 125  GLU C N   1 
ATOM   7314  C  CA  . GLU C  3 127 ? -24.761 -11.041 -44.551  1.00 210.12 ? 125  GLU C CA  1 
ATOM   7315  C  C   . GLU C  3 127 ? -24.546 -12.322 -45.348  1.00 205.51 ? 125  GLU C C   1 
ATOM   7316  O  O   . GLU C  3 127 ? -24.797 -12.357 -46.558  1.00 198.67 ? 125  GLU C O   1 
ATOM   7317  C  CB  . GLU C  3 127 ? -26.255 -10.787 -44.333  1.00 199.91 ? 125  GLU C CB  1 
ATOM   7318  C  CG  . GLU C  3 127 ? -26.986 -10.245 -45.548  1.00 197.23 ? 125  GLU C CG  1 
ATOM   7319  C  CD  . GLU C  3 127 ? -28.428 -9.913  -45.244  1.00 197.71 ? 125  GLU C CD  1 
ATOM   7320  O  OE1 . GLU C  3 127 ? -28.921 -10.354 -44.186  1.00 196.72 ? 125  GLU C OE1 1 
ATOM   7321  O  OE2 . GLU C  3 127 ? -29.066 -9.210  -46.055  1.00 202.20 ? 125  GLU C OE2 1 
ATOM   7322  N  N   . LEU C  3 128 ? -24.083 -13.370 -44.666  1.00 217.75 ? 126  LEU C N   1 
ATOM   7323  C  CA  . LEU C  3 128 ? -23.795 -14.659 -45.290  1.00 222.66 ? 126  LEU C CA  1 
ATOM   7324  C  C   . LEU C  3 128 ? -25.053 -15.522 -45.279  1.00 235.75 ? 126  LEU C C   1 
ATOM   7325  O  O   . LEU C  3 128 ? -25.577 -15.845 -44.208  1.00 253.97 ? 126  LEU C O   1 
ATOM   7326  C  CB  . LEU C  3 128 ? -22.654 -15.363 -44.555  1.00 214.31 ? 126  LEU C CB  1 
ATOM   7327  C  CG  . LEU C  3 128 ? -22.267 -16.778 -45.001  1.00 208.49 ? 126  LEU C CG  1 
ATOM   7328  C  CD1 . LEU C  3 128 ? -21.782 -16.788 -46.446  1.00 225.77 ? 126  LEU C CD1 1 
ATOM   7329  C  CD2 . LEU C  3 128 ? -21.212 -17.369 -44.075  1.00 204.15 ? 126  LEU C CD2 1 
ATOM   7330  N  N   . ARG C  3 129 ? -25.526 -15.910 -46.462  1.00 226.77 ? 127  ARG C N   1 
ATOM   7331  C  CA  . ARG C  3 129 ? -26.767 -16.662 -46.606  1.00 212.73 ? 127  ARG C CA  1 
ATOM   7332  C  C   . ARG C  3 129 ? -26.481 -18.078 -47.098  1.00 216.41 ? 127  ARG C C   1 
ATOM   7333  O  O   . ARG C  3 129 ? -25.645 -18.281 -47.982  1.00 216.80 ? 127  ARG C O   1 
ATOM   7334  C  CB  . ARG C  3 129 ? -27.721 -15.948 -47.570  1.00 209.90 ? 127  ARG C CB  1 
ATOM   7335  C  CG  . ARG C  3 129 ? -28.091 -14.534 -47.138  1.00 208.30 ? 127  ARG C CG  1 
ATOM   7336  C  CD  . ARG C  3 129 ? -29.327 -14.030 -47.868  1.00 209.83 ? 127  ARG C CD  1 
ATOM   7337  N  NE  . ARG C  3 129 ? -29.756 -12.723 -47.376  1.00 219.24 ? 127  ARG C NE  1 
ATOM   7338  C  CZ  . ARG C  3 129 ? -30.881 -12.116 -47.743  1.00 232.13 ? 127  ARG C CZ  1 
ATOM   7339  N  NH1 . ARG C  3 129 ? -31.699 -12.699 -48.608  1.00 237.30 ? 127  ARG C NH1 1 
ATOM   7340  N  NH2 . ARG C  3 129 ? -31.192 -10.926 -47.243  1.00 234.23 ? 127  ARG C NH2 1 
ATOM   7341  N  N   . LEU C  3 130 ? -27.181 -19.061 -46.523  1.00 213.29 ? 128  LEU C N   1 
ATOM   7342  C  CA  . LEU C  3 130 ? -26.950 -20.459 -46.873  1.00 217.09 ? 128  LEU C CA  1 
ATOM   7343  C  C   . LEU C  3 130 ? -28.218 -21.117 -47.410  1.00 219.28 ? 128  LEU C C   1 
ATOM   7344  O  O   . LEU C  3 130 ? -29.147 -20.428 -47.850  1.00 220.77 ? 128  LEU C O   1 
ATOM   7345  C  CB  . LEU C  3 130 ? -26.424 -21.233 -45.662  1.00 216.10 ? 128  LEU C CB  1 
ATOM   7346  C  CG  . LEU C  3 130 ? -25.343 -20.568 -44.806  1.00 212.42 ? 128  LEU C CG  1 
ATOM   7347  C  CD1 . LEU C  3 130 ? -24.907 -21.498 -43.689  1.00 216.26 ? 128  LEU C CD1 1 
ATOM   7348  C  CD2 . LEU C  3 130 ? -24.147 -20.154 -45.647  1.00 211.91 ? 128  LEU C CD2 1 
ATOM   7349  N  N   . LEU C  3 131 ? -28.271 -22.447 -47.393  1.00 220.37 ? 129  LEU C N   1 
ATOM   7350  C  CA  . LEU C  3 131 ? -29.449 -23.160 -47.877  1.00 219.77 ? 129  LEU C CA  1 
ATOM   7351  C  C   . LEU C  3 131 ? -29.634 -24.444 -47.078  1.00 223.04 ? 129  LEU C C   1 
ATOM   7352  O  O   . LEU C  3 131 ? -28.780 -25.335 -47.116  1.00 225.44 ? 129  LEU C O   1 
ATOM   7353  C  CB  . LEU C  3 131 ? -29.319 -23.454 -49.372  1.00 223.94 ? 129  LEU C CB  1 
ATOM   7354  C  CG  . LEU C  3 131 ? -30.551 -23.975 -50.117  1.00 232.23 ? 129  LEU C CG  1 
ATOM   7355  C  CD1 . LEU C  3 131 ? -30.579 -25.499 -50.151  1.00 246.03 ? 129  LEU C CD1 1 
ATOM   7356  C  CD2 . LEU C  3 131 ? -31.837 -23.428 -49.505  1.00 228.76 ? 129  LEU C CD2 1 
ATOM   7357  N  N   . ARG C  3 132 ? -30.763 -24.541 -46.380  1.00 230.84 ? 130  ARG C N   1 
ATOM   7358  C  CA  . ARG C  3 132 ? -31.079 -25.686 -45.538  1.00 234.16 ? 130  ARG C CA  1 
ATOM   7359  C  C   . ARG C  3 132 ? -31.843 -26.745 -46.326  1.00 242.72 ? 130  ARG C C   1 
ATOM   7360  O  O   . ARG C  3 132 ? -32.660 -26.432 -47.197  1.00 259.87 ? 130  ARG C O   1 
ATOM   7361  C  CB  . ARG C  3 132 ? -31.900 -25.234 -44.326  1.00 239.11 ? 130  ARG C CB  1 
ATOM   7362  C  CG  . ARG C  3 132 ? -32.726 -26.313 -43.630  1.00 246.35 ? 130  ARG C CG  1 
ATOM   7363  C  CD  . ARG C  3 132 ? -33.768 -25.675 -42.714  1.00 246.44 ? 130  ARG C CD  1 
ATOM   7364  N  NE  . ARG C  3 132 ? -34.669 -26.644 -42.096  1.00 261.78 ? 130  ARG C NE  1 
ATOM   7365  C  CZ  . ARG C  3 132 ? -34.663 -26.953 -40.803  1.00 264.41 ? 130  ARG C CZ  1 
ATOM   7366  N  NH1 . ARG C  3 132 ? -35.522 -27.848 -40.329  1.00 266.94 ? 130  ARG C NH1 1 
ATOM   7367  N  NH2 . ARG C  3 132 ? -33.799 -26.369 -39.984  1.00 258.93 ? 130  ARG C NH2 1 
ATOM   7368  N  N   . LEU C  3 133 ? -31.564 -28.009 -46.015  1.00 246.18 ? 131  LEU C N   1 
ATOM   7369  C  CA  . LEU C  3 133 ? -32.278 -29.128 -46.619  1.00 271.80 ? 131  LEU C CA  1 
ATOM   7370  C  C   . LEU C  3 133 ? -33.090 -29.914 -45.603  1.00 282.50 ? 131  LEU C C   1 
ATOM   7371  O  O   . LEU C  3 133 ? -34.288 -30.144 -45.816  1.00 285.64 ? 131  LEU C O   1 
ATOM   7372  C  CB  . LEU C  3 133 ? -31.293 -30.071 -47.335  1.00 275.43 ? 131  LEU C CB  1 
ATOM   7373  C  CG  . LEU C  3 133 ? -30.677 -29.652 -48.673  1.00 271.57 ? 131  LEU C CG  1 
ATOM   7374  C  CD1 . LEU C  3 133 ? -29.616 -28.580 -48.492  1.00 262.22 ? 131  LEU C CD1 1 
ATOM   7375  C  CD2 . LEU C  3 133 ? -30.095 -30.864 -49.386  1.00 269.92 ? 131  LEU C CD2 1 
ATOM   7376  N  N   . LYS C  3 134 ? -32.467 -30.327 -44.498  1.00 288.02 ? 132  LYS C N   1 
ATOM   7377  C  CA  . LYS C  3 134 ? -33.132 -31.164 -43.506  1.00 289.94 ? 132  LYS C CA  1 
ATOM   7378  C  C   . LYS C  3 134 ? -34.329 -30.438 -42.905  1.00 284.56 ? 132  LYS C C   1 
ATOM   7379  O  O   . LYS C  3 134 ? -34.243 -29.265 -42.537  1.00 281.09 ? 132  LYS C O   1 
ATOM   7380  C  CB  . LYS C  3 134 ? -32.145 -31.543 -42.398  1.00 274.57 ? 132  LYS C CB  1 
ATOM   7381  C  CG  . LYS C  3 134 ? -32.339 -32.925 -41.792  1.00 277.94 ? 132  LYS C CG  1 
ATOM   7382  C  CD  . LYS C  3 134 ? -31.131 -33.302 -40.942  1.00 267.52 ? 132  LYS C CD  1 
ATOM   7383  C  CE  . LYS C  3 134 ? -31.193 -34.746 -40.472  1.00 280.65 ? 132  LYS C CE  1 
ATOM   7384  N  NZ  . LYS C  3 134 ? -29.966 -35.132 -39.716  1.00 274.91 ? 132  LYS C NZ  1 
ATOM   7385  N  N   . LEU C  3 135 ? -35.453 -31.145 -42.801  1.00 272.61 ? 133  LEU C N   1 
ATOM   7386  C  CA  . LEU C  3 135 ? -36.682 -30.555 -42.295  1.00 251.76 ? 133  LEU C CA  1 
ATOM   7387  C  C   . LEU C  3 135 ? -37.167 -31.166 -40.990  1.00 246.78 ? 133  LEU C C   1 
ATOM   7388  O  O   . LEU C  3 135 ? -38.099 -30.624 -40.385  1.00 242.49 ? 133  LEU C O   1 
ATOM   7389  C  CB  . LEU C  3 135 ? -37.795 -30.666 -43.351  1.00 250.43 ? 133  LEU C CB  1 
ATOM   7390  C  CG  . LEU C  3 135 ? -38.239 -32.044 -43.842  1.00 258.04 ? 133  LEU C CG  1 
ATOM   7391  C  CD1 . LEU C  3 135 ? -39.462 -32.530 -43.079  1.00 261.25 ? 133  LEU C CD1 1 
ATOM   7392  C  CD2 . LEU C  3 135 ? -38.526 -31.985 -45.329  1.00 260.88 ? 133  LEU C CD2 1 
ATOM   7393  N  N   . LYS C  3 136 ? -36.562 -32.259 -40.536  1.00 241.40 ? 134  LYS C N   1 
ATOM   7394  C  CA  . LYS C  3 136 ? -36.993 -32.985 -39.351  1.00 234.37 ? 134  LYS C CA  1 
ATOM   7395  C  C   . LYS C  3 136 ? -36.053 -32.683 -38.189  1.00 229.02 ? 134  LYS C C   1 
ATOM   7396  O  O   . LYS C  3 136 ? -34.856 -32.459 -38.396  1.00 228.49 ? 134  LYS C O   1 
ATOM   7397  C  CB  . LYS C  3 136 ? -37.031 -34.489 -39.638  1.00 227.71 ? 134  LYS C CB  1 
ATOM   7398  C  CG  . LYS C  3 136 ? -37.776 -34.827 -40.918  1.00 226.21 ? 134  LYS C CG  1 
ATOM   7399  C  CD  . LYS C  3 136 ? -37.499 -36.230 -41.413  1.00 228.98 ? 134  LYS C CD  1 
ATOM   7400  C  CE  . LYS C  3 136 ? -38.209 -36.459 -42.738  1.00 234.09 ? 134  LYS C CE  1 
ATOM   7401  N  NZ  . LYS C  3 136 ? -37.988 -37.823 -43.279  1.00 240.70 ? 134  LYS C NZ  1 
ATOM   7402  N  N   . VAL C  3 137 ? -36.602 -32.684 -36.967  1.00 219.87 ? 135  VAL C N   1 
ATOM   7403  C  CA  . VAL C  3 137 ? -35.853 -32.445 -35.732  1.00 219.83 ? 135  VAL C CA  1 
ATOM   7404  C  C   . VAL C  3 137 ? -35.313 -31.014 -35.712  1.00 216.95 ? 135  VAL C C   1 
ATOM   7405  O  O   . VAL C  3 137 ? -35.499 -30.251 -36.666  1.00 213.54 ? 135  VAL C O   1 
ATOM   7406  C  CB  . VAL C  3 137 ? -34.717 -33.480 -35.549  1.00 228.87 ? 135  VAL C CB  1 
ATOM   7407  C  CG1 . VAL C  3 137 ? -34.225 -33.548 -34.100  1.00 227.30 ? 135  VAL C CG1 1 
ATOM   7408  C  CG2 . VAL C  3 137 ? -35.163 -34.864 -36.001  1.00 249.80 ? 135  VAL C CG2 1 
ATOM   7409  N  N   . GLU C  3 138 ? -34.658 -30.640 -34.612  1.00 228.90 ? 136  GLU C N   1 
ATOM   7410  C  CA  . GLU C  3 138 ? -34.055 -29.331 -34.414  1.00 232.19 ? 136  GLU C CA  1 
ATOM   7411  C  C   . GLU C  3 138 ? -32.630 -29.522 -33.914  1.00 242.78 ? 136  GLU C C   1 
ATOM   7412  O  O   . GLU C  3 138 ? -32.368 -30.413 -33.101  1.00 253.11 ? 136  GLU C O   1 
ATOM   7413  C  CB  . GLU C  3 138 ? -34.878 -28.508 -33.414  1.00 228.36 ? 136  GLU C CB  1 
ATOM   7414  C  CG  . GLU C  3 138 ? -34.113 -27.446 -32.650  1.00 223.97 ? 136  GLU C CG  1 
ATOM   7415  C  CD  . GLU C  3 138 ? -35.043 -26.499 -31.918  1.00 226.78 ? 136  GLU C CD  1 
ATOM   7416  O  OE1 . GLU C  3 138 ? -35.927 -26.991 -31.185  1.00 226.73 ? 136  GLU C OE1 1 
ATOM   7417  O  OE2 . GLU C  3 138 ? -34.903 -25.269 -32.085  1.00 230.33 ? 136  GLU C OE2 1 
ATOM   7418  N  N   . GLN C  3 139 ? -31.708 -28.698 -34.410  1.00 240.59 ? 137  GLN C N   1 
ATOM   7419  C  CA  . GLN C  3 139 ? -30.301 -28.826 -34.058  1.00 235.12 ? 137  GLN C CA  1 
ATOM   7420  C  C   . GLN C  3 139 ? -29.714 -27.446 -33.782  1.00 227.02 ? 137  GLN C C   1 
ATOM   7421  O  O   . GLN C  3 139 ? -30.286 -26.417 -34.149  1.00 222.45 ? 137  GLN C O   1 
ATOM   7422  C  CB  . GLN C  3 139 ? -29.511 -29.557 -35.161  1.00 245.58 ? 137  GLN C CB  1 
ATOM   7423  C  CG  . GLN C  3 139 ? -29.698 -31.085 -35.157  1.00 258.66 ? 137  GLN C CG  1 
ATOM   7424  C  CD  . GLN C  3 139 ? -29.162 -31.770 -36.412  1.00 261.62 ? 137  GLN C CD  1 
ATOM   7425  O  OE1 . GLN C  3 139 ? -29.095 -31.166 -37.483  1.00 266.28 ? 137  GLN C OE1 1 
ATOM   7426  N  NE2 . GLN C  3 139 ? -28.783 -33.039 -36.280  1.00 252.18 ? 137  GLN C NE2 1 
ATOM   7427  N  N   . HIS C  3 140 ? -28.552 -27.443 -33.126  1.00 229.56 ? 138  HIS C N   1 
ATOM   7428  C  CA  . HIS C  3 140 ? -27.909 -26.237 -32.616  1.00 234.89 ? 138  HIS C CA  1 
ATOM   7429  C  C   . HIS C  3 140 ? -26.611 -25.990 -33.371  1.00 233.11 ? 138  HIS C C   1 
ATOM   7430  O  O   . HIS C  3 140 ? -25.787 -26.900 -33.506  1.00 240.89 ? 138  HIS C O   1 
ATOM   7431  C  CB  . HIS C  3 140 ? -27.628 -26.371 -31.119  1.00 241.08 ? 138  HIS C CB  1 
ATOM   7432  C  CG  . HIS C  3 140 ? -27.266 -25.084 -30.449  1.00 237.72 ? 138  HIS C CG  1 
ATOM   7433  N  ND1 . HIS C  3 140 ? -28.178 -24.072 -30.244  1.00 237.35 ? 138  HIS C ND1 1 
ATOM   7434  C  CD2 . HIS C  3 140 ? -26.096 -24.650 -29.923  1.00 229.73 ? 138  HIS C CD2 1 
ATOM   7435  C  CE1 . HIS C  3 140 ? -27.585 -23.067 -29.626  1.00 229.29 ? 138  HIS C CE1 1 
ATOM   7436  N  NE2 . HIS C  3 140 ? -26.321 -23.392 -29.419  1.00 224.32 ? 138  HIS C NE2 1 
ATOM   7437  N  N   . VAL C  3 141 ? -26.411 -24.753 -33.823  1.00 225.16 ? 139  VAL C N   1 
ATOM   7438  C  CA  . VAL C  3 141 ? -25.333 -24.414 -34.744  1.00 224.16 ? 139  VAL C CA  1 
ATOM   7439  C  C   . VAL C  3 141 ? -24.483 -23.299 -34.144  1.00 220.98 ? 139  VAL C C   1 
ATOM   7440  O  O   . VAL C  3 141 ? -25.018 -22.313 -33.624  1.00 216.39 ? 139  VAL C O   1 
ATOM   7441  C  CB  . VAL C  3 141 ? -25.891 -23.999 -36.117  1.00 226.99 ? 139  VAL C CB  1 
ATOM   7442  C  CG1 . VAL C  3 141 ? -24.772 -23.560 -37.037  1.00 236.70 ? 139  VAL C CG1 1 
ATOM   7443  C  CG2 . VAL C  3 141 ? -26.671 -25.146 -36.732  1.00 235.34 ? 139  VAL C CG2 1 
ATOM   7444  N  N   . GLU C  3 142 ? -23.160 -23.450 -34.238  1.00 228.55 ? 140  GLU C N   1 
ATOM   7445  C  CA  . GLU C  3 142 ? -22.200 -22.421 -33.856  1.00 237.50 ? 140  GLU C CA  1 
ATOM   7446  C  C   . GLU C  3 142 ? -21.358 -22.034 -35.069  1.00 231.78 ? 140  GLU C C   1 
ATOM   7447  O  O   . GLU C  3 142 ? -21.023 -22.884 -35.901  1.00 233.03 ? 140  GLU C O   1 
ATOM   7448  C  CB  . GLU C  3 142 ? -21.285 -22.901 -32.715  1.00 242.89 ? 140  GLU C CB  1 
ATOM   7449  C  CG  . GLU C  3 142 ? -22.014 -23.364 -31.456  1.00 239.66 ? 140  GLU C CG  1 
ATOM   7450  C  CD  . GLU C  3 142 ? -21.066 -23.921 -30.404  1.00 240.51 ? 140  GLU C CD  1 
ATOM   7451  O  OE1 . GLU C  3 142 ? -19.834 -23.850 -30.610  1.00 248.15 ? 140  GLU C OE1 1 
ATOM   7452  O  OE2 . GLU C  3 142 ? -21.552 -24.433 -29.372  1.00 234.88 ? 140  GLU C OE2 1 
ATOM   7453  N  N   . LEU C  3 143 ? -21.012 -20.751 -35.165  1.00 217.30 ? 141  LEU C N   1 
ATOM   7454  C  CA  . LEU C  3 143 ? -20.291 -20.208 -36.308  1.00 198.66 ? 141  LEU C CA  1 
ATOM   7455  C  C   . LEU C  3 143 ? -18.916 -19.711 -35.881  1.00 198.59 ? 141  LEU C C   1 
ATOM   7456  O  O   . LEU C  3 143 ? -18.763 -19.131 -34.802  1.00 209.56 ? 141  LEU C O   1 
ATOM   7457  C  CB  . LEU C  3 143 ? -21.079 -19.066 -36.951  1.00 191.80 ? 141  LEU C CB  1 
ATOM   7458  C  CG  . LEU C  3 143 ? -20.508 -18.511 -38.252  1.00 189.15 ? 141  LEU C CG  1 
ATOM   7459  C  CD1 . LEU C  3 143 ? -20.462 -19.606 -39.302  1.00 206.28 ? 141  LEU C CD1 1 
ATOM   7460  C  CD2 . LEU C  3 143 ? -21.341 -17.339 -38.728  1.00 184.68 ? 141  LEU C CD2 1 
ATOM   7461  N  N   . TYR C  3 144 ? -17.918 -19.930 -36.732  1.00 201.83 ? 142  TYR C N   1 
ATOM   7462  C  CA  . TYR C  3 144 ? -16.544 -19.570 -36.416  1.00 202.24 ? 142  TYR C CA  1 
ATOM   7463  C  C   . TYR C  3 144 ? -15.929 -18.804 -37.580  1.00 203.62 ? 142  TYR C C   1 
ATOM   7464  O  O   . TYR C  3 144 ? -16.491 -18.732 -38.675  1.00 205.56 ? 142  TYR C O   1 
ATOM   7465  C  CB  . TYR C  3 144 ? -15.705 -20.811 -36.091  1.00 211.47 ? 142  TYR C CB  1 
ATOM   7466  C  CG  . TYR C  3 144 ? -16.095 -21.494 -34.799  1.00 219.10 ? 142  TYR C CG  1 
ATOM   7467  C  CD1 . TYR C  3 144 ? -15.512 -21.124 -33.596  1.00 221.10 ? 142  TYR C CD1 1 
ATOM   7468  C  CD2 . TYR C  3 144 ? -17.041 -22.512 -34.783  1.00 224.57 ? 142  TYR C CD2 1 
ATOM   7469  C  CE1 . TYR C  3 144 ? -15.860 -21.742 -32.413  1.00 223.20 ? 142  TYR C CE1 1 
ATOM   7470  C  CE2 . TYR C  3 144 ? -17.395 -23.137 -33.602  1.00 224.53 ? 142  TYR C CE2 1 
ATOM   7471  C  CZ  . TYR C  3 144 ? -16.800 -22.747 -32.422  1.00 221.98 ? 142  TYR C CZ  1 
ATOM   7472  O  OH  . TYR C  3 144 ? -17.143 -23.362 -31.242  1.00 224.24 ? 142  TYR C OH  1 
ATOM   7473  N  N   . GLN C  3 145 ? -14.757 -18.228 -37.331  1.00 218.67 ? 143  GLN C N   1 
ATOM   7474  C  CA  . GLN C  3 145 ? -14.017 -17.473 -38.330  1.00 225.12 ? 143  GLN C CA  1 
ATOM   7475  C  C   . GLN C  3 145 ? -12.622 -18.067 -38.489  1.00 233.51 ? 143  GLN C C   1 
ATOM   7476  O  O   . GLN C  3 145 ? -12.079 -18.664 -37.555  1.00 240.86 ? 143  GLN C O   1 
ATOM   7477  C  CB  . GLN C  3 145 ? -13.931 -15.994 -37.936  1.00 226.48 ? 143  GLN C CB  1 
ATOM   7478  C  CG  . GLN C  3 145 ? -13.346 -15.086 -38.995  1.00 232.45 ? 143  GLN C CG  1 
ATOM   7479  C  CD  . GLN C  3 145 ? -13.129 -13.677 -38.486  1.00 237.86 ? 143  GLN C CD  1 
ATOM   7480  O  OE1 . GLN C  3 145 ? -13.668 -13.291 -37.448  1.00 243.33 ? 143  GLN C OE1 1 
ATOM   7481  N  NE2 . GLN C  3 145 ? -12.330 -12.901 -39.209  1.00 228.25 ? 143  GLN C NE2 1 
ATOM   7482  N  N   . LYS C  3 146 ? -12.043 -17.905 -39.681  1.00 226.14 ? 144  LYS C N   1 
ATOM   7483  C  CA  . LYS C  3 146 ? -10.738 -18.485 -39.990  1.00 227.49 ? 144  LYS C CA  1 
ATOM   7484  C  C   . LYS C  3 146 ? -9.619  -17.591 -39.466  1.00 237.58 ? 144  LYS C C   1 
ATOM   7485  O  O   . LYS C  3 146 ? -9.499  -16.429 -39.873  1.00 243.69 ? 144  LYS C O   1 
ATOM   7486  C  CB  . LYS C  3 146 ? -10.587 -18.691 -41.496  1.00 228.26 ? 144  LYS C CB  1 
ATOM   7487  C  CG  . LYS C  3 146 ? -9.260  -19.313 -41.920  1.00 231.23 ? 144  LYS C CG  1 
ATOM   7488  C  CD  . LYS C  3 146 ? -9.156  -19.394 -43.437  1.00 230.11 ? 144  LYS C CD  1 
ATOM   7489  C  CE  . LYS C  3 146 ? -7.834  -20.002 -43.875  1.00 231.93 ? 144  LYS C CE  1 
ATOM   7490  N  NZ  . LYS C  3 146 ? -7.623  -19.952 -45.348  1.00 230.80 ? 144  LYS C NZ  1 
ATOM   7491  N  N   . TYR C  3 147 ? -8.789  -18.140 -38.581  1.00 240.77 ? 145  TYR C N   1 
ATOM   7492  C  CA  . TYR C  3 147 ? -7.638  -17.435 -38.030  1.00 241.28 ? 145  TYR C CA  1 
ATOM   7493  C  C   . TYR C  3 147 ? -6.409  -18.323 -38.143  1.00 249.99 ? 145  TYR C C   1 
ATOM   7494  O  O   . TYR C  3 147 ? -6.474  -19.516 -37.830  1.00 251.80 ? 145  TYR C O   1 
ATOM   7495  C  CB  . TYR C  3 147 ? -7.877  -17.040 -36.569  1.00 228.86 ? 145  TYR C CB  1 
ATOM   7496  C  CG  . TYR C  3 147 ? -8.707  -15.791 -36.414  1.00 224.16 ? 145  TYR C CG  1 
ATOM   7497  C  CD1 . TYR C  3 147 ? -8.108  -14.540 -36.370  1.00 224.68 ? 145  TYR C CD1 1 
ATOM   7498  C  CD2 . TYR C  3 147 ? -10.090 -15.859 -36.324  1.00 223.85 ? 145  TYR C CD2 1 
ATOM   7499  C  CE1 . TYR C  3 147 ? -8.862  -13.392 -36.234  1.00 224.53 ? 145  TYR C CE1 1 
ATOM   7500  C  CE2 . TYR C  3 147 ? -10.853 -14.716 -36.186  1.00 229.05 ? 145  TYR C CE2 1 
ATOM   7501  C  CZ  . TYR C  3 147 ? -10.234 -13.484 -36.143  1.00 230.89 ? 145  TYR C CZ  1 
ATOM   7502  O  OH  . TYR C  3 147 ? -10.985 -12.339 -36.007  1.00 239.23 ? 145  TYR C OH  1 
ATOM   7503  N  N   . SER C  3 148 ? -5.295  -17.745 -38.599  1.00 252.10 ? 146  SER C N   1 
ATOM   7504  C  CA  . SER C  3 148 ? -4.024  -18.454 -38.754  1.00 253.99 ? 146  SER C CA  1 
ATOM   7505  C  C   . SER C  3 148 ? -4.148  -19.684 -39.648  1.00 264.96 ? 146  SER C C   1 
ATOM   7506  O  O   . SER C  3 148 ? -3.298  -20.581 -39.596  1.00 269.84 ? 146  SER C O   1 
ATOM   7507  C  CB  . SER C  3 148 ? -3.441  -18.852 -37.391  1.00 248.57 ? 146  SER C CB  1 
ATOM   7508  O  OG  . SER C  3 148 ? -2.176  -19.477 -37.532  1.00 244.26 ? 146  SER C OG  1 
ATOM   7509  N  N   . GLN C  3 149 ? -5.206  -19.746 -40.458  1.00 271.20 ? 147  GLN C N   1 
ATOM   7510  C  CA  . GLN C  3 149 ? -5.502  -20.848 -41.370  1.00 268.31 ? 147  GLN C CA  1 
ATOM   7511  C  C   . GLN C  3 149 ? -5.641  -22.193 -40.660  1.00 268.04 ? 147  GLN C C   1 
ATOM   7512  O  O   . GLN C  3 149 ? -5.664  -23.239 -41.324  1.00 266.98 ? 147  GLN C O   1 
ATOM   7513  C  CB  . GLN C  3 149 ? -4.452  -20.944 -42.487  1.00 264.21 ? 147  GLN C CB  1 
ATOM   7514  C  CG  . GLN C  3 149 ? -4.313  -19.670 -43.317  1.00 261.93 ? 147  GLN C CG  1 
ATOM   7515  C  CD  . GLN C  3 149 ? -3.309  -19.808 -44.447  1.00 274.48 ? 147  GLN C CD  1 
ATOM   7516  O  OE1 . GLN C  3 149 ? -2.931  -20.916 -44.827  1.00 281.12 ? 147  GLN C OE1 1 
ATOM   7517  N  NE2 . GLN C  3 149 ? -2.869  -18.677 -44.987  1.00 278.22 ? 147  GLN C NE2 1 
ATOM   7518  N  N   . ASN C  3 150 ? -5.750  -22.198 -39.329  1.00 262.06 ? 148  ASN C N   1 
ATOM   7519  C  CA  . ASN C  3 150 ? -5.871  -23.429 -38.557  1.00 257.25 ? 148  ASN C CA  1 
ATOM   7520  C  C   . ASN C  3 150 ? -6.791  -23.221 -37.359  1.00 243.42 ? 148  ASN C C   1 
ATOM   7521  O  O   . ASN C  3 150 ? -7.614  -24.086 -37.039  1.00 244.41 ? 148  ASN C O   1 
ATOM   7522  C  CB  . ASN C  3 150 ? -4.492  -23.909 -38.091  1.00 260.01 ? 148  ASN C CB  1 
ATOM   7523  C  CG  . ASN C  3 150 ? -4.565  -25.153 -37.218  1.00 257.96 ? 148  ASN C CG  1 
ATOM   7524  O  OD1 . ASN C  3 150 ? -5.473  -25.974 -37.357  1.00 262.60 ? 148  ASN C OD1 1 
ATOM   7525  N  ND2 . ASN C  3 150 ? -3.604  -25.297 -36.312  1.00 252.17 ? 148  ASN C ND2 1 
ATOM   7526  N  N   . SER C  3 151 ? -6.658  -22.079 -36.695  1.00 241.65 ? 149  SER C N   1 
ATOM   7527  C  CA  . SER C  3 151 ? -7.461  -21.768 -35.523  1.00 240.93 ? 149  SER C CA  1 
ATOM   7528  C  C   . SER C  3 151 ? -8.778  -21.122 -35.930  1.00 234.59 ? 149  SER C C   1 
ATOM   7529  O  O   . SER C  3 151 ? -8.863  -20.403 -36.929  1.00 232.89 ? 149  SER C O   1 
ATOM   7530  C  CB  . SER C  3 151 ? -6.702  -20.840 -34.573  1.00 246.05 ? 149  SER C CB  1 
ATOM   7531  O  OG  . SER C  3 151 ? -7.530  -20.423 -33.501  1.00 244.62 ? 149  SER C OG  1 
ATOM   7532  N  N   . TRP C  3 152 ? -9.814  -21.388 -35.142  1.00 228.46 ? 150  TRP C N   1 
ATOM   7533  C  CA  . TRP C  3 152 ? -11.143 -20.850 -35.386  1.00 225.27 ? 150  TRP C CA  1 
ATOM   7534  C  C   . TRP C  3 152 ? -11.603 -20.094 -34.152  1.00 217.88 ? 150  TRP C C   1 
ATOM   7535  O  O   . TRP C  3 152 ? -11.485 -20.596 -33.029  1.00 218.89 ? 150  TRP C O   1 
ATOM   7536  C  CB  . TRP C  3 152 ? -12.127 -21.964 -35.740  1.00 234.00 ? 150  TRP C CB  1 
ATOM   7537  C  CG  . TRP C  3 152 ? -11.624 -22.831 -36.847  1.00 242.60 ? 150  TRP C CG  1 
ATOM   7538  C  CD1 . TRP C  3 152 ? -10.944 -24.007 -36.721  1.00 244.31 ? 150  TRP C CD1 1 
ATOM   7539  C  CD2 . TRP C  3 152 ? -11.739 -22.581 -38.253  1.00 247.03 ? 150  TRP C CD2 1 
ATOM   7540  N  NE1 . TRP C  3 152 ? -10.636 -24.510 -37.961  1.00 249.91 ? 150  TRP C NE1 1 
ATOM   7541  C  CE2 . TRP C  3 152 ? -11.113 -23.654 -38.919  1.00 257.77 ? 150  TRP C CE2 1 
ATOM   7542  C  CE3 . TRP C  3 152 ? -12.313 -21.557 -39.013  1.00 243.03 ? 150  TRP C CE3 1 
ATOM   7543  C  CZ2 . TRP C  3 152 ? -11.047 -23.733 -40.310  1.00 266.08 ? 150  TRP C CZ2 1 
ATOM   7544  C  CZ3 . TRP C  3 152 ? -12.248 -21.638 -40.392  1.00 252.43 ? 150  TRP C CZ3 1 
ATOM   7545  C  CH2 . TRP C  3 152 ? -11.618 -22.717 -41.027  1.00 264.68 ? 150  TRP C CH2 1 
ATOM   7546  N  N   . ARG C  3 153 ? -12.112 -18.887 -34.359  1.00 204.07 ? 151  ARG C N   1 
ATOM   7547  C  CA  . ARG C  3 153 ? -12.600 -18.060 -33.270  1.00 203.03 ? 151  ARG C CA  1 
ATOM   7548  C  C   . ARG C  3 153 ? -14.107 -17.890 -33.387  1.00 205.23 ? 151  ARG C C   1 
ATOM   7549  O  O   . ARG C  3 153 ? -14.647 -17.748 -34.490  1.00 197.86 ? 151  ARG C O   1 
ATOM   7550  C  CB  . ARG C  3 153 ? -11.900 -16.701 -33.248  1.00 208.82 ? 151  ARG C CB  1 
ATOM   7551  C  CG  . ARG C  3 153 ? -10.401 -16.807 -33.002  1.00 216.11 ? 151  ARG C CG  1 
ATOM   7552  C  CD  . ARG C  3 153 ? -10.080 -17.746 -31.844  1.00 206.60 ? 151  ARG C CD  1 
ATOM   7553  N  NE  . ARG C  3 153 ? -10.402 -17.158 -30.549  1.00 198.86 ? 151  ARG C NE  1 
ATOM   7554  C  CZ  . ARG C  3 153 ? -10.136 -17.734 -29.381  1.00 198.48 ? 151  ARG C CZ  1 
ATOM   7555  N  NH1 . ARG C  3 153 ? -9.541  -18.918 -29.347  1.00 200.02 ? 151  ARG C NH1 1 
ATOM   7556  N  NH2 . ARG C  3 153 ? -10.465 -17.124 -28.250  1.00 196.83 ? 151  ARG C NH2 1 
ATOM   7557  N  N   . TYR C  3 154 ? -14.769 -17.918 -32.234  1.00 222.04 ? 152  TYR C N   1 
ATOM   7558  C  CA  . TYR C  3 154 ? -16.221 -17.894 -32.166  1.00 213.21 ? 152  TYR C CA  1 
ATOM   7559  C  C   . TYR C  3 154 ? -16.776 -16.615 -32.781  1.00 201.37 ? 152  TYR C C   1 
ATOM   7560  O  O   . TYR C  3 154 ? -16.134 -15.561 -32.774  1.00 198.98 ? 152  TYR C O   1 
ATOM   7561  C  CB  . TYR C  3 154 ? -16.660 -18.015 -30.708  1.00 217.74 ? 152  TYR C CB  1 
ATOM   7562  C  CG  . TYR C  3 154 ? -18.136 -18.233 -30.507  1.00 217.44 ? 152  TYR C CG  1 
ATOM   7563  C  CD1 . TYR C  3 154 ? -18.675 -19.510 -30.546  1.00 222.69 ? 152  TYR C CD1 1 
ATOM   7564  C  CD2 . TYR C  3 154 ? -18.988 -17.166 -30.258  1.00 208.65 ? 152  TYR C CD2 1 
ATOM   7565  C  CE1 . TYR C  3 154 ? -20.021 -19.718 -30.354  1.00 221.54 ? 152  TYR C CE1 1 
ATOM   7566  C  CE2 . TYR C  3 154 ? -20.336 -17.365 -30.063  1.00 203.91 ? 152  TYR C CE2 1 
ATOM   7567  C  CZ  . TYR C  3 154 ? -20.846 -18.645 -30.113  1.00 213.05 ? 152  TYR C CZ  1 
ATOM   7568  O  OH  . TYR C  3 154 ? -22.186 -18.859 -29.920  1.00 220.49 ? 152  TYR C OH  1 
ATOM   7569  N  N   . LEU C  3 155 ? -17.987 -16.721 -33.324  1.00 189.46 ? 153  LEU C N   1 
ATOM   7570  C  CA  . LEU C  3 155 ? -18.659 -15.579 -33.927  1.00 184.41 ? 153  LEU C CA  1 
ATOM   7571  C  C   . LEU C  3 155 ? -20.053 -15.415 -33.347  1.00 182.76 ? 153  LEU C C   1 
ATOM   7572  O  O   . LEU C  3 155 ? -20.237 -14.706 -32.353  1.00 180.40 ? 153  LEU C O   1 
ATOM   7573  C  CB  . LEU C  3 155 ? -18.737 -15.734 -35.445  1.00 184.36 ? 153  LEU C CB  1 
ATOM   7574  C  CG  . LEU C  3 155 ? -17.395 -15.688 -36.169  1.00 198.62 ? 153  LEU C CG  1 
ATOM   7575  C  CD1 . LEU C  3 155 ? -17.608 -15.771 -37.667  1.00 207.51 ? 153  LEU C CD1 1 
ATOM   7576  C  CD2 . LEU C  3 155 ? -16.643 -14.421 -35.798  1.00 199.50 ? 153  LEU C CD2 1 
ATOM   7577  N  N   . SER C  3 156 ? -21.039 -16.069 -33.955  1.00 186.03 ? 154  SER C N   1 
ATOM   7578  C  CA  . SER C  3 156 ? -22.426 -15.952 -33.536  1.00 185.08 ? 154  SER C CA  1 
ATOM   7579  C  C   . SER C  3 156 ? -23.037 -17.342 -33.386  1.00 192.84 ? 154  SER C C   1 
ATOM   7580  O  O   . SER C  3 156 ? -22.381 -18.366 -33.599  1.00 195.66 ? 154  SER C O   1 
ATOM   7581  C  CB  . SER C  3 156 ? -23.232 -15.104 -34.526  1.00 181.40 ? 154  SER C CB  1 
ATOM   7582  O  OG  . SER C  3 156 ? -23.280 -15.710 -35.802  1.00 182.69 ? 154  SER C OG  1 
ATOM   7583  N  N   . ASN C  3 157 ? -24.316 -17.369 -33.015  1.00 199.54 ? 155  ASN C N   1 
ATOM   7584  C  CA  . ASN C  3 157 ? -25.028 -18.603 -32.721  1.00 205.85 ? 155  ASN C CA  1 
ATOM   7585  C  C   . ASN C  3 157 ? -26.484 -18.446 -33.138  1.00 208.72 ? 155  ASN C C   1 
ATOM   7586  O  O   . ASN C  3 157 ? -27.025 -17.336 -33.141  1.00 205.90 ? 155  ASN C O   1 
ATOM   7587  C  CB  . ASN C  3 157 ? -24.927 -18.947 -31.228  1.00 222.92 ? 155  ASN C CB  1 
ATOM   7588  C  CG  . ASN C  3 157 ? -25.554 -20.279 -30.886  1.00 237.27 ? 155  ASN C CG  1 
ATOM   7589  O  OD1 . ASN C  3 157 ? -26.723 -20.346 -30.506  1.00 253.84 ? 155  ASN C OD1 1 
ATOM   7590  N  ND2 . ASN C  3 157 ? -24.776 -21.350 -31.007  1.00 233.94 ? 155  ASN C ND2 1 
ATOM   7591  N  N   . ARG C  3 158 ? -27.116 -19.564 -33.496  1.00 215.70 ? 156  ARG C N   1 
ATOM   7592  C  CA  . ARG C  3 158 ? -28.515 -19.525 -33.906  1.00 217.29 ? 156  ARG C CA  1 
ATOM   7593  C  C   . ARG C  3 158 ? -29.122 -20.917 -33.821  1.00 222.39 ? 156  ARG C C   1 
ATOM   7594  O  O   . ARG C  3 158 ? -28.555 -21.878 -34.350  1.00 220.24 ? 156  ARG C O   1 
ATOM   7595  C  CB  . ARG C  3 158 ? -28.652 -18.979 -35.325  1.00 209.43 ? 156  ARG C CB  1 
ATOM   7596  C  CG  . ARG C  3 158 ? -30.081 -18.759 -35.759  1.00 208.84 ? 156  ARG C CG  1 
ATOM   7597  C  CD  . ARG C  3 158 ? -30.109 -17.828 -36.939  1.00 207.81 ? 156  ARG C CD  1 
ATOM   7598  N  NE  . ARG C  3 158 ? -29.310 -16.637 -36.674  1.00 207.37 ? 156  ARG C NE  1 
ATOM   7599  C  CZ  . ARG C  3 158 ? -29.084 -15.681 -37.566  1.00 213.83 ? 156  ARG C CZ  1 
ATOM   7600  N  NH1 . ARG C  3 158 ? -29.600 -15.782 -38.783  1.00 214.94 ? 156  ARG C NH1 1 
ATOM   7601  N  NH2 . ARG C  3 158 ? -28.344 -14.627 -37.244  1.00 213.11 ? 156  ARG C NH2 1 
ATOM   7602  N  N   . LEU C  3 159 ? -30.272 -21.015 -33.163  1.00 217.03 ? 157  LEU C N   1 
ATOM   7603  C  CA  . LEU C  3 159 ? -31.034 -22.252 -33.117  1.00 214.52 ? 157  LEU C CA  1 
ATOM   7604  C  C   . LEU C  3 159 ? -31.932 -22.338 -34.346  1.00 214.90 ? 157  LEU C C   1 
ATOM   7605  O  O   . LEU C  3 159 ? -32.368 -21.321 -34.891  1.00 212.12 ? 157  LEU C O   1 
ATOM   7606  C  CB  . LEU C  3 159 ? -31.871 -22.332 -31.836  1.00 214.76 ? 157  LEU C CB  1 
ATOM   7607  C  CG  . LEU C  3 159 ? -31.161 -22.440 -30.478  1.00 216.31 ? 157  LEU C CG  1 
ATOM   7608  C  CD1 . LEU C  3 159 ? -30.650 -21.093 -29.977  1.00 214.07 ? 157  LEU C CD1 1 
ATOM   7609  C  CD2 . LEU C  3 159 ? -32.084 -23.074 -29.447  1.00 224.07 ? 157  LEU C CD2 1 
ATOM   7610  N  N   . LEU C  3 160 ? -32.202 -23.566 -34.783  1.00 220.24 ? 158  LEU C N   1 
ATOM   7611  C  CA  . LEU C  3 160 ? -32.938 -23.819 -36.015  1.00 217.94 ? 158  LEU C CA  1 
ATOM   7612  C  C   . LEU C  3 160 ? -34.235 -24.565 -35.719  1.00 232.35 ? 158  LEU C C   1 
ATOM   7613  O  O   . LEU C  3 160 ? -34.297 -25.388 -34.804  1.00 236.63 ? 158  LEU C O   1 
ATOM   7614  C  CB  . LEU C  3 160 ? -32.085 -24.626 -37.004  1.00 210.88 ? 158  LEU C CB  1 
ATOM   7615  C  CG  . LEU C  3 160 ? -30.980 -23.912 -37.789  1.00 207.74 ? 158  LEU C CG  1 
ATOM   7616  C  CD1 . LEU C  3 160 ? -29.844 -23.432 -36.897  1.00 209.02 ? 158  LEU C CD1 1 
ATOM   7617  C  CD2 . LEU C  3 160 ? -30.453 -24.832 -38.878  1.00 210.72 ? 158  LEU C CD2 1 
ATOM   7618  N  N   . ALA C  3 161 ? -35.277 -24.284 -36.516  1.00 242.92 ? 159  ALA C N   1 
ATOM   7619  C  CA  . ALA C  3 161 ? -36.595 -24.855 -36.267  1.00 241.99 ? 159  ALA C CA  1 
ATOM   7620  C  C   . ALA C  3 161 ? -36.992 -25.847 -37.360  1.00 249.17 ? 159  ALA C C   1 
ATOM   7621  O  O   . ALA C  3 161 ? -36.663 -25.655 -38.535  1.00 258.42 ? 159  ALA C O   1 
ATOM   7622  C  CB  . ALA C  3 161 ? -37.658 -23.753 -36.179  1.00 237.70 ? 159  ALA C CB  1 
ATOM   7623  N  N   . PRO C  3 162 ? -37.716 -26.921 -37.001  1.00 236.95 ? 160  PRO C N   1 
ATOM   7624  C  CA  . PRO C  3 162 ? -38.110 -27.923 -38.004  1.00 242.82 ? 160  PRO C CA  1 
ATOM   7625  C  C   . PRO C  3 162 ? -39.137 -27.407 -39.000  1.00 250.15 ? 160  PRO C C   1 
ATOM   7626  O  O   . PRO C  3 162 ? -40.343 -27.632 -38.840  1.00 255.54 ? 160  PRO C O   1 
ATOM   7627  C  CB  . PRO C  3 162 ? -38.679 -29.066 -37.151  1.00 244.88 ? 160  PRO C CB  1 
ATOM   7628  C  CG  . PRO C  3 162 ? -39.130 -28.407 -35.891  1.00 238.44 ? 160  PRO C CG  1 
ATOM   7629  C  CD  . PRO C  3 162 ? -38.150 -27.294 -35.643  1.00 231.73 ? 160  PRO C CD  1 
ATOM   7630  N  N   . SER C  3 163 ? -38.665 -26.714 -40.036  1.00 255.28 ? 161  SER C N   1 
ATOM   7631  C  CA  . SER C  3 163 ? -39.523 -26.229 -41.109  1.00 254.34 ? 161  SER C CA  1 
ATOM   7632  C  C   . SER C  3 163 ? -39.725 -27.331 -42.140  1.00 262.63 ? 161  SER C C   1 
ATOM   7633  O  O   . SER C  3 163 ? -38.754 -27.931 -42.611  1.00 257.76 ? 161  SER C O   1 
ATOM   7634  C  CB  . SER C  3 163 ? -38.913 -24.993 -41.770  1.00 245.57 ? 161  SER C CB  1 
ATOM   7635  O  OG  . SER C  3 163 ? -39.689 -24.560 -42.872  1.00 244.76 ? 161  SER C OG  1 
ATOM   7636  N  N   . ASP C  3 164 ? -40.986 -27.582 -42.499  1.00 271.32 ? 162  ASP C N   1 
ATOM   7637  C  CA  . ASP C  3 164 ? -41.305 -28.668 -43.420  1.00 275.98 ? 162  ASP C CA  1 
ATOM   7638  C  C   . ASP C  3 164 ? -40.755 -28.435 -44.823  1.00 269.14 ? 162  ASP C C   1 
ATOM   7639  O  O   . ASP C  3 164 ? -40.607 -29.398 -45.584  1.00 269.74 ? 162  ASP C O   1 
ATOM   7640  C  CB  . ASP C  3 164 ? -42.821 -28.869 -43.487  1.00 286.38 ? 162  ASP C CB  1 
ATOM   7641  C  CG  . ASP C  3 164 ? -43.438 -29.121 -42.125  1.00 286.46 ? 162  ASP C CG  1 
ATOM   7642  O  OD1 . ASP C  3 164 ? -43.230 -30.224 -41.575  1.00 301.59 ? 162  ASP C OD1 1 
ATOM   7643  O  OD2 . ASP C  3 164 ? -44.141 -28.223 -41.610  1.00 268.50 ? 162  ASP C OD2 1 
ATOM   7644  N  N   . SER C  3 165 ? -40.456 -27.196 -45.180  1.00 268.43 ? 163  SER C N   1 
ATOM   7645  C  CA  . SER C  3 165 ? -39.958 -26.839 -46.496  1.00 275.69 ? 163  SER C CA  1 
ATOM   7646  C  C   . SER C  3 165 ? -38.496 -26.417 -46.417  1.00 255.17 ? 163  SER C C   1 
ATOM   7647  O  O   . SER C  3 165 ? -37.993 -26.092 -45.336  1.00 245.05 ? 163  SER C O   1 
ATOM   7648  C  CB  . SER C  3 165 ? -40.800 -25.700 -47.094  1.00 285.63 ? 163  SER C CB  1 
ATOM   7649  O  OG  . SER C  3 165 ? -40.729 -24.531 -46.296  1.00 277.40 ? 163  SER C OG  1 
ATOM   7650  N  N   . PRO C  3 166 ? -37.773 -26.434 -47.538  1.00 265.26 ? 164  PRO C N   1 
ATOM   7651  C  CA  . PRO C  3 166 ? -36.401 -25.909 -47.530  1.00 251.05 ? 164  PRO C CA  1 
ATOM   7652  C  C   . PRO C  3 166 ? -36.386 -24.451 -47.100  1.00 243.66 ? 164  PRO C C   1 
ATOM   7653  O  O   . PRO C  3 166 ? -37.108 -23.614 -47.647  1.00 240.69 ? 164  PRO C O   1 
ATOM   7654  C  CB  . PRO C  3 166 ? -35.943 -26.080 -48.985  1.00 265.11 ? 164  PRO C CB  1 
ATOM   7655  C  CG  . PRO C  3 166 ? -37.206 -26.244 -49.778  1.00 279.53 ? 164  PRO C CG  1 
ATOM   7656  C  CD  . PRO C  3 166 ? -38.139 -26.971 -48.859  1.00 284.15 ? 164  PRO C CD  1 
ATOM   7657  N  N   . GLU C  3 167 ? -35.560 -24.155 -46.105  1.00 247.62 ? 165  GLU C N   1 
ATOM   7658  C  CA  . GLU C  3 167 ? -35.527 -22.844 -45.480  1.00 249.33 ? 165  GLU C CA  1 
ATOM   7659  C  C   . GLU C  3 167 ? -34.214 -22.142 -45.810  1.00 248.78 ? 165  GLU C C   1 
ATOM   7660  O  O   . GLU C  3 167 ? -33.183 -22.784 -46.027  1.00 251.12 ? 165  GLU C O   1 
ATOM   7661  C  CB  . GLU C  3 167 ? -35.705 -22.969 -43.964  1.00 250.06 ? 165  GLU C CB  1 
ATOM   7662  C  CG  . GLU C  3 167 ? -36.213 -21.720 -43.279  1.00 246.38 ? 165  GLU C CG  1 
ATOM   7663  C  CD  . GLU C  3 167 ? -36.565 -21.958 -41.824  1.00 254.79 ? 165  GLU C CD  1 
ATOM   7664  O  OE1 . GLU C  3 167 ? -36.472 -23.118 -41.373  1.00 258.65 ? 165  GLU C OE1 1 
ATOM   7665  O  OE2 . GLU C  3 167 ? -36.934 -20.986 -41.131  1.00 254.18 ? 165  GLU C OE2 1 
ATOM   7666  N  N   . TRP C  3 168 ? -34.262 -20.814 -45.856  1.00 241.67 ? 166  TRP C N   1 
ATOM   7667  C  CA  . TRP C  3 168 ? -33.112 -19.996 -46.224  1.00 247.09 ? 166  TRP C CA  1 
ATOM   7668  C  C   . TRP C  3 168 ? -32.762 -19.101 -45.041  1.00 240.88 ? 166  TRP C C   1 
ATOM   7669  O  O   . TRP C  3 168 ? -33.590 -18.296 -44.604  1.00 238.16 ? 166  TRP C O   1 
ATOM   7670  C  CB  . TRP C  3 168 ? -33.422 -19.171 -47.478  1.00 246.58 ? 166  TRP C CB  1 
ATOM   7671  C  CG  . TRP C  3 168 ? -32.224 -18.829 -48.334  1.00 237.39 ? 166  TRP C CG  1 
ATOM   7672  C  CD1 . TRP C  3 168 ? -31.204 -17.982 -48.014  1.00 244.30 ? 166  TRP C CD1 1 
ATOM   7673  C  CD2 . TRP C  3 168 ? -31.946 -19.306 -49.659  1.00 220.61 ? 166  TRP C CD2 1 
ATOM   7674  N  NE1 . TRP C  3 168 ? -30.302 -17.911 -49.048  1.00 227.11 ? 166  TRP C NE1 1 
ATOM   7675  C  CE2 . TRP C  3 168 ? -30.734 -18.713 -50.070  1.00 217.74 ? 166  TRP C CE2 1 
ATOM   7676  C  CE3 . TRP C  3 168 ? -32.599 -20.177 -50.533  1.00 225.64 ? 166  TRP C CE3 1 
ATOM   7677  C  CZ2 . TRP C  3 168 ? -30.163 -18.966 -51.312  1.00 218.85 ? 166  TRP C CZ2 1 
ATOM   7678  C  CZ3 . TRP C  3 168 ? -32.030 -20.427 -51.767  1.00 238.54 ? 166  TRP C CZ3 1 
ATOM   7679  C  CH2 . TRP C  3 168 ? -30.824 -19.823 -52.145  1.00 237.78 ? 166  TRP C CH2 1 
ATOM   7680  N  N   . LEU C  3 169 ? -31.545 -19.243 -44.518  1.00 235.07 ? 167  LEU C N   1 
ATOM   7681  C  CA  . LEU C  3 169 ? -31.098 -18.471 -43.364  1.00 234.23 ? 167  LEU C CA  1 
ATOM   7682  C  C   . LEU C  3 169 ? -30.008 -17.485 -43.773  1.00 236.50 ? 167  LEU C C   1 
ATOM   7683  O  O   . LEU C  3 169 ? -29.582 -17.434 -44.930  1.00 250.02 ? 167  LEU C O   1 
ATOM   7684  C  CB  . LEU C  3 169 ? -30.610 -19.395 -42.248  1.00 243.57 ? 167  LEU C CB  1 
ATOM   7685  C  CG  . LEU C  3 169 ? -31.639 -19.733 -41.166  1.00 260.87 ? 167  LEU C CG  1 
ATOM   7686  C  CD1 . LEU C  3 169 ? -32.746 -20.615 -41.726  1.00 269.35 ? 167  LEU C CD1 1 
ATOM   7687  C  CD2 . LEU C  3 169 ? -30.970 -20.387 -39.964  1.00 264.07 ? 167  LEU C CD2 1 
ATOM   7688  N  N   . SER C  3 170 ? -29.552 -16.694 -42.801  1.00 224.93 ? 168  SER C N   1 
ATOM   7689  C  CA  . SER C  3 170 ? -28.561 -15.659 -43.064  1.00 224.66 ? 168  SER C CA  1 
ATOM   7690  C  C   . SER C  3 170 ? -27.859 -15.289 -41.766  1.00 210.37 ? 168  SER C C   1 
ATOM   7691  O  O   . SER C  3 170 ? -28.491 -15.236 -40.709  1.00 211.90 ? 168  SER C O   1 
ATOM   7692  C  CB  . SER C  3 170 ? -29.208 -14.417 -43.687  1.00 234.93 ? 168  SER C CB  1 
ATOM   7693  O  OG  . SER C  3 170 ? -30.171 -13.858 -42.812  1.00 238.92 ? 168  SER C OG  1 
ATOM   7694  N  N   . PHE C  3 171 ? -26.556 -15.024 -41.857  1.00 203.61 ? 169  PHE C N   1 
ATOM   7695  C  CA  . PHE C  3 171 ? -25.750 -14.634 -40.704  1.00 202.75 ? 169  PHE C CA  1 
ATOM   7696  C  C   . PHE C  3 171 ? -25.008 -13.345 -41.020  1.00 201.30 ? 169  PHE C C   1 
ATOM   7697  O  O   . PHE C  3 171 ? -24.260 -13.279 -42.001  1.00 213.11 ? 169  PHE C O   1 
ATOM   7698  C  CB  . PHE C  3 171 ? -24.768 -15.741 -40.317  1.00 205.06 ? 169  PHE C CB  1 
ATOM   7699  C  CG  . PHE C  3 171 ? -25.402 -16.875 -39.564  1.00 215.19 ? 169  PHE C CG  1 
ATOM   7700  C  CD1 . PHE C  3 171 ? -25.522 -16.826 -38.185  1.00 233.35 ? 169  PHE C CD1 1 
ATOM   7701  C  CD2 . PHE C  3 171 ? -25.879 -17.989 -40.235  1.00 219.75 ? 169  PHE C CD2 1 
ATOM   7702  C  CE1 . PHE C  3 171 ? -26.103 -17.868 -37.488  1.00 237.61 ? 169  PHE C CE1 1 
ATOM   7703  C  CE2 . PHE C  3 171 ? -26.462 -19.035 -39.543  1.00 229.22 ? 169  PHE C CE2 1 
ATOM   7704  C  CZ  . PHE C  3 171 ? -26.574 -18.974 -38.168  1.00 234.75 ? 169  PHE C CZ  1 
ATOM   7705  N  N   . ASP C  3 172 ? -25.202 -12.333 -40.179  1.00 197.57 ? 170  ASP C N   1 
ATOM   7706  C  CA  . ASP C  3 172 ? -24.620 -11.009 -40.392  1.00 196.88 ? 170  ASP C CA  1 
ATOM   7707  C  C   . ASP C  3 172 ? -23.140 -11.030 -40.017  1.00 196.86 ? 170  ASP C C   1 
ATOM   7708  O  O   . ASP C  3 172 ? -22.781 -10.951 -38.840  1.00 196.30 ? 170  ASP C O   1 
ATOM   7709  C  CB  . ASP C  3 172 ? -25.381 -9.976  -39.570  1.00 222.49 ? 170  ASP C CB  1 
ATOM   7710  C  CG  . ASP C  3 172 ? -25.115 -8.553  -40.025  1.00 239.34 ? 170  ASP C CG  1 
ATOM   7711  O  OD1 . ASP C  3 172 ? -24.005 -8.278  -40.530  1.00 243.97 ? 170  ASP C OD1 1 
ATOM   7712  O  OD2 . ASP C  3 172 ? -26.023 -7.707  -39.874  1.00 245.97 ? 170  ASP C OD2 1 
ATOM   7713  N  N   . VAL C  3 173 ? -22.269 -11.110 -41.024  1.00 199.83 ? 171  VAL C N   1 
ATOM   7714  C  CA  . VAL C  3 173 ? -20.825 -11.130 -40.806  1.00 211.51 ? 171  VAL C CA  1 
ATOM   7715  C  C   . VAL C  3 173 ? -20.200 -9.857  -41.360  1.00 216.20 ? 171  VAL C C   1 
ATOM   7716  O  O   . VAL C  3 173 ? -19.089 -9.883  -41.902  1.00 216.77 ? 171  VAL C O   1 
ATOM   7717  C  CB  . VAL C  3 173 ? -20.180 -12.371 -41.448  1.00 226.81 ? 171  VAL C CB  1 
ATOM   7718  C  CG1 . VAL C  3 173 ? -20.561 -13.625 -40.685  1.00 239.08 ? 171  VAL C CG1 1 
ATOM   7719  C  CG2 . VAL C  3 173 ? -20.597 -12.486 -42.906  1.00 221.35 ? 171  VAL C CG2 1 
ATOM   7720  N  N   . THR C  3 174 ? -20.909 -8.735  -41.225  1.00 209.80 ? 172  THR C N   1 
ATOM   7721  C  CA  . THR C  3 174 ? -20.429 -7.476  -41.786  1.00 207.54 ? 172  THR C CA  1 
ATOM   7722  C  C   . THR C  3 174 ? -19.098 -7.068  -41.168  1.00 205.25 ? 172  THR C C   1 
ATOM   7723  O  O   . THR C  3 174 ? -18.155 -6.702  -41.880  1.00 209.45 ? 172  THR C O   1 
ATOM   7724  C  CB  . THR C  3 174 ? -21.476 -6.386  -41.580  1.00 214.95 ? 172  THR C CB  1 
ATOM   7725  O  OG1 . THR C  3 174 ? -22.664 -6.722  -42.307  1.00 220.52 ? 172  THR C OG1 1 
ATOM   7726  C  CG2 . THR C  3 174 ? -20.948 -5.044  -42.062  1.00 221.61 ? 172  THR C CG2 1 
ATOM   7727  N  N   . GLY C  3 175 ? -19.004 -7.130  -39.837  1.00 215.40 ? 173  GLY C N   1 
ATOM   7728  C  CA  . GLY C  3 175 ? -17.766 -6.765  -39.169  1.00 218.38 ? 173  GLY C CA  1 
ATOM   7729  C  C   . GLY C  3 175 ? -16.594 -7.633  -39.576  1.00 219.71 ? 173  GLY C C   1 
ATOM   7730  O  O   . GLY C  3 175 ? -15.440 -7.204  -39.488  1.00 224.11 ? 173  GLY C O   1 
ATOM   7731  N  N   . VAL C  3 176 ? -16.867 -8.856  -40.031  1.00 223.01 ? 174  VAL C N   1 
ATOM   7732  C  CA  . VAL C  3 176 ? -15.801 -9.738  -40.492  1.00 232.21 ? 174  VAL C CA  1 
ATOM   7733  C  C   . VAL C  3 176 ? -15.366 -9.360  -41.901  1.00 236.16 ? 174  VAL C C   1 
ATOM   7734  O  O   . VAL C  3 176 ? -14.168 -9.268  -42.194  1.00 242.53 ? 174  VAL C O   1 
ATOM   7735  C  CB  . VAL C  3 176 ? -16.253 -11.207 -40.417  1.00 231.18 ? 174  VAL C CB  1 
ATOM   7736  C  CG1 . VAL C  3 176 ? -15.180 -12.117 -40.990  1.00 240.65 ? 174  VAL C CG1 1 
ATOM   7737  C  CG2 . VAL C  3 176 ? -16.571 -11.592 -38.984  1.00 222.70 ? 174  VAL C CG2 1 
ATOM   7738  N  N   . VAL C  3 177 ? -16.335 -9.134  -42.790  1.00 229.81 ? 175  VAL C N   1 
ATOM   7739  C  CA  . VAL C  3 177 ? -16.017 -8.825  -44.182  1.00 233.30 ? 175  VAL C CA  1 
ATOM   7740  C  C   . VAL C  3 177 ? -15.269 -7.502  -44.279  1.00 240.43 ? 175  VAL C C   1 
ATOM   7741  O  O   . VAL C  3 177 ? -14.355 -7.347  -45.100  1.00 242.85 ? 175  VAL C O   1 
ATOM   7742  C  CB  . VAL C  3 177 ? -17.303 -8.817  -45.030  1.00 228.60 ? 175  VAL C CB  1 
ATOM   7743  C  CG1 . VAL C  3 177 ? -16.982 -8.498  -46.479  1.00 233.16 ? 175  VAL C CG1 1 
ATOM   7744  C  CG2 . VAL C  3 177 ? -18.017 -10.154 -44.924  1.00 220.77 ? 175  VAL C CG2 1 
ATOM   7745  N  N   . ARG C  3 178 ? -15.638 -6.531  -43.438  1.00 247.41 ? 176  ARG C N   1 
ATOM   7746  C  CA  . ARG C  3 178 ? -15.009 -5.214  -43.497  1.00 253.48 ? 176  ARG C CA  1 
ATOM   7747  C  C   . ARG C  3 178 ? -13.513 -5.299  -43.226  1.00 257.39 ? 176  ARG C C   1 
ATOM   7748  O  O   . ARG C  3 178 ? -12.715 -4.627  -43.891  1.00 261.36 ? 176  ARG C O   1 
ATOM   7749  C  CB  . ARG C  3 178 ? -15.678 -4.269  -42.500  1.00 250.57 ? 176  ARG C CB  1 
ATOM   7750  C  CG  . ARG C  3 178 ? -14.962 -2.936  -42.334  1.00 254.59 ? 176  ARG C CG  1 
ATOM   7751  C  CD  . ARG C  3 178 ? -15.746 -1.984  -41.444  1.00 257.61 ? 176  ARG C CD  1 
ATOM   7752  N  NE  . ARG C  3 178 ? -16.945 -1.481  -42.108  1.00 259.59 ? 176  ARG C NE  1 
ATOM   7753  C  CZ  . ARG C  3 178 ? -18.172 -1.947  -41.898  1.00 262.94 ? 176  ARG C CZ  1 
ATOM   7754  N  NH1 . ARG C  3 178 ? -18.375 -2.931  -41.031  1.00 265.09 ? 176  ARG C NH1 1 
ATOM   7755  N  NH2 . ARG C  3 178 ? -19.200 -1.424  -42.553  1.00 262.47 ? 176  ARG C NH2 1 
ATOM   7756  N  N   . GLN C  3 179 ? -13.110 -6.123  -42.255  1.00 261.16 ? 177  GLN C N   1 
ATOM   7757  C  CA  . GLN C  3 179 ? -11.691 -6.255  -41.943  1.00 263.34 ? 177  GLN C CA  1 
ATOM   7758  C  C   . GLN C  3 179 ? -10.952 -7.051  -43.010  1.00 263.85 ? 177  GLN C C   1 
ATOM   7759  O  O   . GLN C  3 179 ? -9.740  -6.881  -43.178  1.00 272.39 ? 177  GLN C O   1 
ATOM   7760  C  CB  . GLN C  3 179 ? -11.510 -6.912  -40.574  1.00 255.83 ? 177  GLN C CB  1 
ATOM   7761  C  CG  . GLN C  3 179 ? -12.163 -6.157  -39.425  1.00 254.90 ? 177  GLN C CG  1 
ATOM   7762  C  CD  . GLN C  3 179 ? -12.057 -6.899  -38.104  1.00 261.99 ? 177  GLN C CD  1 
ATOM   7763  O  OE1 . GLN C  3 179 ? -11.449 -7.967  -38.026  1.00 267.94 ? 177  GLN C OE1 1 
ATOM   7764  N  NE2 . GLN C  3 179 ? -12.652 -6.335  -37.058  1.00 258.95 ? 177  GLN C NE2 1 
ATOM   7765  N  N   . TRP C  3 180 ? -11.656 -7.917  -43.740  1.00 245.32 ? 178  TRP C N   1 
ATOM   7766  C  CA  . TRP C  3 180 ? -11.008 -8.737  -44.753  1.00 246.20 ? 178  TRP C CA  1 
ATOM   7767  C  C   . TRP C  3 180 ? -10.666 -7.961  -46.014  1.00 250.65 ? 178  TRP C C   1 
ATOM   7768  O  O   . TRP C  3 180 ? -9.750  -8.361  -46.742  1.00 257.60 ? 178  TRP C O   1 
ATOM   7769  C  CB  . TRP C  3 180 ? -11.896 -9.927  -45.113  1.00 240.26 ? 178  TRP C CB  1 
ATOM   7770  C  CG  . TRP C  3 180 ? -11.892 -10.993 -44.074  1.00 238.03 ? 178  TRP C CG  1 
ATOM   7771  C  CD1 . TRP C  3 180 ? -11.237 -10.971 -42.876  1.00 248.04 ? 178  TRP C CD1 1 
ATOM   7772  C  CD2 . TRP C  3 180 ? -12.569 -12.251 -44.138  1.00 231.94 ? 178  TRP C CD2 1 
ATOM   7773  N  NE1 . TRP C  3 180 ? -11.469 -12.138 -42.189  1.00 249.00 ? 178  TRP C NE1 1 
ATOM   7774  C  CE2 . TRP C  3 180 ? -12.283 -12.941 -42.943  1.00 244.63 ? 178  TRP C CE2 1 
ATOM   7775  C  CE3 . TRP C  3 180 ? -13.391 -12.862 -45.089  1.00 229.85 ? 178  TRP C CE3 1 
ATOM   7776  C  CZ2 . TRP C  3 180 ? -12.791 -14.211 -42.676  1.00 243.49 ? 178  TRP C CZ2 1 
ATOM   7777  C  CZ3 . TRP C  3 180 ? -13.893 -14.121 -44.822  1.00 228.60 ? 178  TRP C CZ3 1 
ATOM   7778  C  CH2 . TRP C  3 180 ? -13.592 -14.781 -43.626  1.00 234.41 ? 178  TRP C CH2 1 
ATOM   7779  N  N   . LEU C  3 181 ? -11.380 -6.871  -46.294  1.00 246.04 ? 179  LEU C N   1 
ATOM   7780  C  CA  . LEU C  3 181 ? -11.079 -6.065  -47.469  1.00 253.85 ? 179  LEU C CA  1 
ATOM   7781  C  C   . LEU C  3 181 ? -9.899  -5.133  -47.243  1.00 265.79 ? 179  LEU C C   1 
ATOM   7782  O  O   . LEU C  3 181 ? -9.318  -4.639  -48.218  1.00 272.83 ? 179  LEU C O   1 
ATOM   7783  C  CB  . LEU C  3 181 ? -12.314 -5.264  -47.888  1.00 247.80 ? 179  LEU C CB  1 
ATOM   7784  C  CG  . LEU C  3 181 ? -13.271 -5.903  -48.902  1.00 245.22 ? 179  LEU C CG  1 
ATOM   7785  C  CD1 . LEU C  3 181 ? -13.686 -7.307  -48.489  1.00 245.52 ? 179  LEU C CD1 1 
ATOM   7786  C  CD2 . LEU C  3 181 ? -14.497 -5.023  -49.088  1.00 240.63 ? 179  LEU C CD2 1 
ATOM   7787  N  N   . SER C  3 182 ? -9.530  -4.883  -45.984  1.00 271.47 ? 180  SER C N   1 
ATOM   7788  C  CA  . SER C  3 182 ? -8.337  -4.104  -45.684  1.00 271.75 ? 180  SER C CA  1 
ATOM   7789  C  C   . SER C  3 182 ? -7.066  -4.938  -45.757  1.00 281.21 ? 180  SER C C   1 
ATOM   7790  O  O   . SER C  3 182 ? -5.985  -4.379  -45.971  1.00 293.67 ? 180  SER C O   1 
ATOM   7791  C  CB  . SER C  3 182 ? -8.456  -3.467  -44.297  1.00 259.79 ? 180  SER C CB  1 
ATOM   7792  O  OG  . SER C  3 182 ? -8.504  -4.454  -43.279  1.00 257.53 ? 180  SER C OG  1 
ATOM   7793  N  N   . ARG C  3 183 ? -7.170  -6.253  -45.603  1.00 277.06 ? 181  ARG C N   1 
ATOM   7794  C  CA  . ARG C  3 183 ? -6.007  -7.125  -45.620  1.00 269.90 ? 181  ARG C CA  1 
ATOM   7795  C  C   . ARG C  3 183 ? -5.713  -7.603  -47.036  1.00 276.74 ? 181  ARG C C   1 
ATOM   7796  O  O   . ARG C  3 183 ? -6.614  -7.756  -47.866  1.00 280.00 ? 181  ARG C O   1 
ATOM   7797  C  CB  . ARG C  3 183 ? -6.220  -8.330  -44.702  1.00 255.14 ? 181  ARG C CB  1 
ATOM   7798  C  CG  . ARG C  3 183 ? -6.704  -7.952  -43.315  1.00 254.86 ? 181  ARG C CG  1 
ATOM   7799  C  CD  . ARG C  3 183 ? -7.056  -9.169  -42.480  1.00 267.98 ? 181  ARG C CD  1 
ATOM   7800  N  NE  . ARG C  3 183 ? -7.800  -8.793  -41.279  1.00 268.76 ? 181  ARG C NE  1 
ATOM   7801  C  CZ  . ARG C  3 183 ? -7.236  -8.426  -40.133  1.00 265.58 ? 181  ARG C CZ  1 
ATOM   7802  N  NH1 . ARG C  3 183 ? -5.915  -8.385  -40.024  1.00 267.27 ? 181  ARG C NH1 1 
ATOM   7803  N  NH2 . ARG C  3 183 ? -7.993  -8.099  -39.095  1.00 256.17 ? 181  ARG C NH2 1 
ATOM   7804  N  N   . GLY C  3 184 ? -4.436  -7.835  -47.307  1.00 276.77 ? 182  GLY C N   1 
ATOM   7805  C  CA  . GLY C  3 184 ? -4.029  -8.401  -48.572  1.00 284.34 ? 182  GLY C CA  1 
ATOM   7806  C  C   . GLY C  3 184 ? -4.099  -9.910  -48.635  1.00 291.17 ? 182  GLY C C   1 
ATOM   7807  O  O   . GLY C  3 184 ? -3.619  -10.500 -49.609  1.00 295.53 ? 182  GLY C O   1 
ATOM   7808  N  N   . GLY C  3 185 ? -4.674  -10.555 -47.621  1.00 289.17 ? 183  GLY C N   1 
ATOM   7809  C  CA  . GLY C  3 185 ? -4.794  -11.999 -47.613  1.00 284.70 ? 183  GLY C CA  1 
ATOM   7810  C  C   . GLY C  3 185 ? -5.746  -12.495 -48.680  1.00 275.57 ? 183  GLY C C   1 
ATOM   7811  O  O   . GLY C  3 185 ? -6.962  -12.330 -48.553  1.00 266.89 ? 183  GLY C O   1 
ATOM   7812  N  N   . GLU C  3 186 ? -5.208  -13.103 -49.737  1.00 268.18 ? 184  GLU C N   1 
ATOM   7813  C  CA  . GLU C  3 186 ? -6.010  -13.536 -50.874  1.00 258.04 ? 184  GLU C CA  1 
ATOM   7814  C  C   . GLU C  3 186 ? -6.752  -14.847 -50.625  1.00 254.53 ? 184  GLU C C   1 
ATOM   7815  O  O   . GLU C  3 186 ? -7.346  -15.388 -51.565  1.00 251.79 ? 184  GLU C O   1 
ATOM   7816  C  CB  . GLU C  3 186 ? -5.130  -13.667 -52.126  1.00 264.45 ? 184  GLU C CB  1 
ATOM   7817  C  CG  . GLU C  3 186 ? -4.527  -12.350 -52.617  1.00 261.33 ? 184  GLU C CG  1 
ATOM   7818  C  CD  . GLU C  3 186 ? -3.965  -12.439 -54.032  1.00 264.86 ? 184  GLU C CD  1 
ATOM   7819  O  OE1 . GLU C  3 186 ? -4.189  -13.467 -54.705  1.00 266.11 ? 184  GLU C OE1 1 
ATOM   7820  O  OE2 . GLU C  3 186 ? -3.302  -11.475 -54.473  1.00 259.95 ? 184  GLU C OE2 1 
ATOM   7821  N  N   . ILE C  3 187 ? -6.741  -15.369 -49.397  1.00 248.87 ? 185  ILE C N   1 
ATOM   7822  C  CA  . ILE C  3 187 ? -7.466  -16.593 -49.063  1.00 243.68 ? 185  ILE C CA  1 
ATOM   7823  C  C   . ILE C  3 187 ? -8.031  -16.457 -47.653  1.00 238.50 ? 185  ILE C C   1 
ATOM   7824  O  O   . ILE C  3 187 ? -7.281  -16.218 -46.699  1.00 239.06 ? 185  ILE C O   1 
ATOM   7825  C  CB  . ILE C  3 187 ? -6.582  -17.849 -49.176  1.00 242.30 ? 185  ILE C CB  1 
ATOM   7826  C  CG1 . ILE C  3 187 ? -7.330  -19.080 -48.657  1.00 237.79 ? 185  ILE C CG1 1 
ATOM   7827  C  CG2 . ILE C  3 187 ? -5.256  -17.660 -48.444  1.00 239.29 ? 185  ILE C CG2 1 
ATOM   7828  C  CD1 . ILE C  3 187 ? -8.575  -19.417 -49.448  1.00 236.01 ? 185  ILE C CD1 1 
ATOM   7829  N  N   . GLU C  3 188 ? -9.349  -16.595 -47.523  1.00 246.72 ? 186  GLU C N   1 
ATOM   7830  C  CA  . GLU C  3 188 ? -10.039 -16.547 -46.234  1.00 257.65 ? 186  GLU C CA  1 
ATOM   7831  C  C   . GLU C  3 188 ? -11.149 -17.596 -46.253  1.00 261.49 ? 186  GLU C C   1 
ATOM   7832  O  O   . GLU C  3 188 ? -11.269 -18.378 -47.201  1.00 271.35 ? 186  GLU C O   1 
ATOM   7833  C  CB  . GLU C  3 188 ? -10.583 -15.139 -45.952  1.00 260.56 ? 186  GLU C CB  1 
ATOM   7834  C  CG  . GLU C  3 188 ? -9.523  -14.053 -45.831  1.00 266.54 ? 186  GLU C CG  1 
ATOM   7835  C  CD  . GLU C  3 188 ? -8.707  -14.157 -44.554  1.00 272.32 ? 186  GLU C CD  1 
ATOM   7836  O  OE1 . GLU C  3 188 ? -9.068  -14.962 -43.668  1.00 280.70 ? 186  GLU C OE1 1 
ATOM   7837  O  OE2 . GLU C  3 188 ? -7.701  -13.426 -44.437  1.00 268.36 ? 186  GLU C OE2 1 
ATOM   7838  N  N   . GLY C  3 189 ? -11.972 -17.617 -45.210  1.00 255.75 ? 187  GLY C N   1 
ATOM   7839  C  CA  . GLY C  3 189 ? -13.064 -18.571 -45.160  1.00 254.86 ? 187  GLY C CA  1 
ATOM   7840  C  C   . GLY C  3 189 ? -13.760 -18.570 -43.814  1.00 254.21 ? 187  GLY C C   1 
ATOM   7841  O  O   . GLY C  3 189 ? -13.381 -17.851 -42.884  1.00 249.23 ? 187  GLY C O   1 
ATOM   7842  N  N   . PHE C  3 190 ? -14.799 -19.405 -43.730  1.00 249.00 ? 188  PHE C N   1 
ATOM   7843  C  CA  . PHE C  3 190 ? -15.597 -19.577 -42.524  1.00 229.65 ? 188  PHE C CA  1 
ATOM   7844  C  C   . PHE C  3 190 ? -15.687 -21.057 -42.170  1.00 228.85 ? 188  PHE C C   1 
ATOM   7845  O  O   . PHE C  3 190 ? -15.250 -21.933 -42.920  1.00 237.48 ? 188  PHE C O   1 
ATOM   7846  C  CB  . PHE C  3 190 ? -17.010 -18.999 -42.690  1.00 220.42 ? 188  PHE C CB  1 
ATOM   7847  C  CG  . PHE C  3 190 ? -17.045 -17.514 -42.909  1.00 216.84 ? 188  PHE C CG  1 
ATOM   7848  C  CD1 . PHE C  3 190 ? -17.116 -16.641 -41.837  1.00 211.72 ? 188  PHE C CD1 1 
ATOM   7849  C  CD2 . PHE C  3 190 ? -17.029 -16.991 -44.190  1.00 226.29 ? 188  PHE C CD2 1 
ATOM   7850  C  CE1 . PHE C  3 190 ? -17.160 -15.274 -42.038  1.00 209.19 ? 188  PHE C CE1 1 
ATOM   7851  C  CE2 . PHE C  3 190 ? -17.072 -15.626 -44.398  1.00 224.13 ? 188  PHE C CE2 1 
ATOM   7852  C  CZ  . PHE C  3 190 ? -17.137 -14.766 -43.321  1.00 215.33 ? 188  PHE C CZ  1 
ATOM   7853  N  N   . ARG C  3 191 ? -16.278 -21.332 -41.010  1.00 204.00 ? 189  ARG C N   1 
ATOM   7854  C  CA  . ARG C  3 191 ? -16.483 -22.697 -40.543  1.00 209.93 ? 189  ARG C CA  1 
ATOM   7855  C  C   . ARG C  3 191 ? -17.821 -22.773 -39.834  1.00 208.97 ? 189  ARG C C   1 
ATOM   7856  O  O   . ARG C  3 191 ? -18.152 -21.896 -39.031  1.00 212.75 ? 189  ARG C O   1 
ATOM   7857  C  CB  . ARG C  3 191 ? -15.369 -23.142 -39.591  1.00 224.24 ? 189  ARG C CB  1 
ATOM   7858  C  CG  . ARG C  3 191 ? -15.675 -24.431 -38.835  1.00 236.68 ? 189  ARG C CG  1 
ATOM   7859  C  CD  . ARG C  3 191 ? -14.808 -24.568 -37.585  1.00 244.30 ? 189  ARG C CD  1 
ATOM   7860  N  NE  . ARG C  3 191 ? -15.162 -25.745 -36.792  1.00 239.15 ? 189  ARG C NE  1 
ATOM   7861  C  CZ  . ARG C  3 191 ? -14.610 -26.056 -35.622  1.00 237.74 ? 189  ARG C CZ  1 
ATOM   7862  N  NH1 . ARG C  3 191 ? -13.675 -25.277 -35.096  1.00 233.07 ? 189  ARG C NH1 1 
ATOM   7863  N  NH2 . ARG C  3 191 ? -14.996 -27.148 -34.976  1.00 245.86 ? 189  ARG C NH2 1 
ATOM   7864  N  N   . LEU C  3 192 ? -18.583 -23.821 -40.119  1.00 221.69 ? 190  LEU C N   1 
ATOM   7865  C  CA  . LEU C  3 192 ? -19.873 -24.029 -39.472  1.00 222.59 ? 190  LEU C CA  1 
ATOM   7866  C  C   . LEU C  3 192 ? -19.872 -25.419 -38.845  1.00 242.36 ? 190  LEU C C   1 
ATOM   7867  O  O   . LEU C  3 192 ? -20.092 -26.419 -39.535  1.00 254.71 ? 190  LEU C O   1 
ATOM   7868  C  CB  . LEU C  3 192 ? -21.013 -23.861 -40.465  1.00 219.67 ? 190  LEU C CB  1 
ATOM   7869  C  CG  . LEU C  3 192 ? -22.407 -23.757 -39.852  1.00 217.16 ? 190  LEU C CG  1 
ATOM   7870  C  CD1 . LEU C  3 192 ? -23.236 -22.744 -40.617  1.00 218.67 ? 190  LEU C CD1 1 
ATOM   7871  C  CD2 . LEU C  3 192 ? -23.094 -25.110 -39.845  1.00 222.15 ? 190  LEU C CD2 1 
ATOM   7872  N  N   . SER C  3 193 ? -19.621 -25.481 -37.544  1.00 244.35 ? 191  SER C N   1 
ATOM   7873  C  CA  . SER C  3 193 ? -19.683 -26.729 -36.807  1.00 248.30 ? 191  SER C CA  1 
ATOM   7874  C  C   . SER C  3 193 ? -20.992 -26.781 -36.018  1.00 239.98 ? 191  SER C C   1 
ATOM   7875  O  O   . SER C  3 193 ? -21.954 -26.072 -36.334  1.00 230.67 ? 191  SER C O   1 
ATOM   7876  C  CB  . SER C  3 193 ? -18.447 -26.862 -35.912  1.00 256.94 ? 191  SER C CB  1 
ATOM   7877  O  OG  . SER C  3 193 ? -18.359 -25.784 -35.000  1.00 261.12 ? 191  SER C OG  1 
ATOM   7878  N  N   . ALA C  3 194 ? -21.038 -27.614 -34.988  1.00 243.94 ? 192  ALA C N   1 
ATOM   7879  C  CA  . ALA C  3 194 ? -22.236 -27.787 -34.183  1.00 245.84 ? 192  ALA C CA  1 
ATOM   7880  C  C   . ALA C  3 194 ? -21.947 -27.427 -32.728  1.00 250.93 ? 192  ALA C C   1 
ATOM   7881  O  O   . ALA C  3 194 ? -20.905 -26.858 -32.396  1.00 265.71 ? 192  ALA C O   1 
ATOM   7882  C  CB  . ALA C  3 194 ? -22.756 -29.217 -34.310  1.00 247.55 ? 192  ALA C CB  1 
ATOM   7883  N  N   . HIS C  3 195 ? -22.891 -27.767 -31.857  1.00 234.11 ? 193  HIS C N   1 
ATOM   7884  C  CA  . HIS C  3 195 ? -22.744 -27.464 -30.443  1.00 233.02 ? 193  HIS C CA  1 
ATOM   7885  C  C   . HIS C  3 195 ? -21.716 -28.389 -29.806  1.00 238.27 ? 193  HIS C C   1 
ATOM   7886  O  O   . HIS C  3 195 ? -21.630 -29.574 -30.142  1.00 244.27 ? 193  HIS C O   1 
ATOM   7887  C  CB  . HIS C  3 195 ? -24.088 -27.605 -29.735  1.00 238.09 ? 193  HIS C CB  1 
ATOM   7888  C  CG  . HIS C  3 195 ? -24.048 -27.238 -28.286  1.00 242.07 ? 193  HIS C CG  1 
ATOM   7889  N  ND1 . HIS C  3 195 ? -23.577 -26.022 -27.841  1.00 238.15 ? 193  HIS C ND1 1 
ATOM   7890  C  CD2 . HIS C  3 195 ? -24.421 -27.926 -27.181  1.00 247.39 ? 193  HIS C CD2 1 
ATOM   7891  C  CE1 . HIS C  3 195 ? -23.663 -25.975 -26.524  1.00 242.56 ? 193  HIS C CE1 1 
ATOM   7892  N  NE2 . HIS C  3 195 ? -24.172 -27.118 -26.098  1.00 248.05 ? 193  HIS C NE2 1 
ATOM   7893  N  N   . CYS C  3 196 ? -20.926 -27.839 -28.888  1.00 238.73 ? 194  CYS C N   1 
ATOM   7894  C  CA  . CYS C  3 196 ? -19.985 -28.613 -28.088  1.00 241.01 ? 194  CYS C CA  1 
ATOM   7895  C  C   . CYS C  3 196 ? -20.445 -28.567 -26.640  1.00 237.12 ? 194  CYS C C   1 
ATOM   7896  O  O   . CYS C  3 196 ? -20.479 -27.493 -26.031  1.00 223.88 ? 194  CYS C O   1 
ATOM   7897  C  CB  . CYS C  3 196 ? -18.558 -28.074 -28.204  1.00 246.71 ? 194  CYS C CB  1 
ATOM   7898  S  SG  . CYS C  3 196 ? -17.928 -27.722 -29.857  1.00 246.95 ? 194  CYS C SG  1 
ATOM   7899  N  N   . SER C  3 197 ? -20.798 -29.724 -26.094  1.00 246.79 ? 195  SER C N   1 
ATOM   7900  C  CA  . SER C  3 197 ? -21.285 -29.817 -24.722  1.00 239.87 ? 195  SER C CA  1 
ATOM   7901  C  C   . SER C  3 197 ? -20.119 -30.157 -23.799  1.00 238.97 ? 195  SER C C   1 
ATOM   7902  O  O   . SER C  3 197 ? -19.609 -31.282 -23.818  1.00 240.38 ? 195  SER C O   1 
ATOM   7903  C  CB  . SER C  3 197 ? -22.387 -30.865 -24.619  1.00 250.27 ? 195  SER C CB  1 
ATOM   7904  O  OG  . SER C  3 197 ? -21.899 -32.148 -24.975  1.00 258.73 ? 195  SER C OG  1 
ATOM   7905  N  N   . CYS C  3 198 ? -19.703 -29.189 -22.986  1.00 254.38 ? 196  CYS C N   1 
ATOM   7906  C  CA  . CYS C  3 198 ? -18.638 -29.415 -22.013  1.00 261.53 ? 196  CYS C CA  1 
ATOM   7907  C  C   . CYS C  3 198 ? -18.967 -28.746 -20.683  1.00 250.97 ? 196  CYS C C   1 
ATOM   7908  O  O   . CYS C  3 198 ? -20.082 -28.268 -20.479  1.00 244.46 ? 196  CYS C O   1 
ATOM   7909  C  CB  . CYS C  3 198 ? -17.298 -28.895 -22.539  1.00 267.80 ? 196  CYS C CB  1 
ATOM   7910  S  SG  . CYS C  3 198 ? -17.112 -27.096 -22.473  1.00 273.54 ? 196  CYS C SG  1 
ATOM   7911  N  N   . ILE C  3 209 ? -20.211 -35.121 -30.334  1.00 285.62 ? 207  ILE C N   1 
ATOM   7912  C  CA  . ILE C  3 209 ? -20.302 -34.146 -31.411  1.00 279.81 ? 207  ILE C CA  1 
ATOM   7913  C  C   . ILE C  3 209 ? -21.675 -34.253 -32.061  1.00 285.41 ? 207  ILE C C   1 
ATOM   7914  O  O   . ILE C  3 209 ? -22.054 -35.316 -32.562  1.00 284.92 ? 207  ILE C O   1 
ATOM   7915  C  CB  . ILE C  3 209 ? -19.177 -34.337 -32.440  1.00 279.72 ? 207  ILE C CB  1 
ATOM   7916  C  CG1 . ILE C  3 209 ? -18.364 -35.589 -32.101  1.00 283.01 ? 207  ILE C CG1 1 
ATOM   7917  C  CG2 . ILE C  3 209 ? -18.276 -33.108 -32.479  1.00 274.42 ? 207  ILE C CG2 1 
ATOM   7918  C  CD1 . ILE C  3 209 ? -17.498 -36.084 -33.235  1.00 285.78 ? 207  ILE C CD1 1 
ATOM   7919  N  N   . ASN C  3 210 ? -22.416 -33.148 -32.044  1.00 292.99 ? 208  ASN C N   1 
ATOM   7920  C  CA  . ASN C  3 210 ? -23.798 -33.105 -32.489  1.00 298.35 ? 208  ASN C CA  1 
ATOM   7921  C  C   . ASN C  3 210 ? -23.917 -32.442 -33.866  1.00 297.36 ? 208  ASN C C   1 
ATOM   7922  O  O   . ASN C  3 210 ? -22.955 -32.408 -34.639  1.00 297.62 ? 208  ASN C O   1 
ATOM   7923  C  CB  . ASN C  3 210 ? -24.628 -32.372 -31.428  1.00 288.98 ? 208  ASN C CB  1 
ATOM   7924  C  CG  . ASN C  3 210 ? -24.387 -32.909 -30.044  1.00 276.74 ? 208  ASN C CG  1 
ATOM   7925  O  OD1 . ASN C  3 210 ? -23.545 -32.397 -29.308  1.00 268.22 ? 208  ASN C OD1 1 
ATOM   7926  N  ND2 . ASN C  3 210 ? -25.122 -33.950 -29.677  1.00 281.15 ? 208  ASN C ND2 1 
ATOM   7927  N  N   . GLY C  3 211 ? -25.109 -31.927 -34.166  1.00 296.14 ? 209  GLY C N   1 
ATOM   7928  C  CA  . GLY C  3 211 ? -25.422 -31.118 -35.356  1.00 286.61 ? 209  GLY C CA  1 
ATOM   7929  C  C   . GLY C  3 211 ? -25.494 -31.752 -36.726  1.00 282.13 ? 209  GLY C C   1 
ATOM   7930  O  O   . GLY C  3 211 ? -26.361 -31.403 -37.531  1.00 277.21 ? 209  GLY C O   1 
ATOM   7931  N  N   . PHE C  3 212 ? -24.590 -32.675 -37.026  1.00 288.48 ? 210  PHE C N   1 
ATOM   7932  C  CA  . PHE C  3 212 ? -24.563 -33.327 -38.326  1.00 299.20 ? 210  PHE C CA  1 
ATOM   7933  C  C   . PHE C  3 212 ? -24.455 -34.824 -38.096  1.00 301.11 ? 210  PHE C C   1 
ATOM   7934  O  O   . PHE C  3 212 ? -23.570 -35.279 -37.364  1.00 299.54 ? 210  PHE C O   1 
ATOM   7935  C  CB  . PHE C  3 212 ? -23.392 -32.834 -39.187  1.00 303.73 ? 210  PHE C CB  1 
ATOM   7936  C  CG  . PHE C  3 212 ? -23.355 -31.340 -39.397  1.00 298.34 ? 210  PHE C CG  1 
ATOM   7937  C  CD1 . PHE C  3 212 ? -23.014 -30.485 -38.359  1.00 289.65 ? 210  PHE C CD1 1 
ATOM   7938  C  CD2 . PHE C  3 212 ? -23.613 -30.794 -40.645  1.00 299.06 ? 210  PHE C CD2 1 
ATOM   7939  C  CE1 . PHE C  3 212 ? -22.967 -29.122 -38.548  1.00 287.40 ? 210  PHE C CE1 1 
ATOM   7940  C  CE2 . PHE C  3 212 ? -23.558 -29.425 -40.842  1.00 293.36 ? 210  PHE C CE2 1 
ATOM   7941  C  CZ  . PHE C  3 212 ? -23.239 -28.590 -39.790  1.00 290.23 ? 210  PHE C CZ  1 
ATOM   7942  N  N   . THR C  3 213 ? -25.357 -35.587 -38.712  1.00 310.58 ? 211  THR C N   1 
ATOM   7943  C  CA  . THR C  3 213 ? -25.418 -37.025 -38.504  1.00 310.43 ? 211  THR C CA  1 
ATOM   7944  C  C   . THR C  3 213 ? -25.017 -37.832 -39.730  1.00 314.24 ? 211  THR C C   1 
ATOM   7945  O  O   . THR C  3 213 ? -24.866 -39.053 -39.623  1.00 313.97 ? 211  THR C O   1 
ATOM   7946  C  CB  . THR C  3 213 ? -26.832 -37.436 -38.064  1.00 306.02 ? 211  THR C CB  1 
ATOM   7947  O  OG1 . THR C  3 213 ? -27.755 -37.211 -39.138  1.00 301.59 ? 211  THR C OG1 1 
ATOM   7948  C  CG2 . THR C  3 213 ? -27.261 -36.619 -36.859  1.00 292.81 ? 211  THR C CG2 1 
ATOM   7949  N  N   . THR C  3 214 ? -24.839 -37.191 -40.881  1.00 327.45 ? 212  THR C N   1 
ATOM   7950  C  CA  . THR C  3 214 ? -24.414 -37.858 -42.101  1.00 334.91 ? 212  THR C CA  1 
ATOM   7951  C  C   . THR C  3 214 ? -22.981 -37.463 -42.442  1.00 338.13 ? 212  THR C C   1 
ATOM   7952  O  O   . THR C  3 214 ? -22.537 -36.350 -42.140  1.00 328.02 ? 212  THR C O   1 
ATOM   7953  C  CB  . THR C  3 214 ? -25.342 -37.504 -43.269  1.00 330.08 ? 212  THR C CB  1 
ATOM   7954  O  OG1 . THR C  3 214 ? -26.702 -37.503 -42.819  1.00 333.27 ? 212  THR C OG1 1 
ATOM   7955  C  CG2 . THR C  3 214 ? -25.198 -38.518 -44.401  1.00 325.69 ? 212  THR C CG2 1 
ATOM   7956  N  N   . GLY C  3 215 ? -22.263 -38.388 -43.085  1.00 343.16 ? 213  GLY C N   1 
ATOM   7957  C  CA  . GLY C  3 215 ? -20.897 -38.179 -43.515  1.00 332.20 ? 213  GLY C CA  1 
ATOM   7958  C  C   . GLY C  3 215 ? -20.701 -37.692 -44.934  1.00 329.17 ? 213  GLY C C   1 
ATOM   7959  O  O   . GLY C  3 215 ? -19.556 -37.463 -45.337  1.00 323.82 ? 213  GLY C O   1 
ATOM   7960  N  N   . ARG C  3 216 ? -21.776 -37.525 -45.712  1.00 326.59 ? 214  ARG C N   1 
ATOM   7961  C  CA  . ARG C  3 216 ? -21.634 -36.994 -47.063  1.00 322.45 ? 214  ARG C CA  1 
ATOM   7962  C  C   . ARG C  3 216 ? -21.405 -35.491 -47.066  1.00 320.87 ? 214  ARG C C   1 
ATOM   7963  O  O   . ARG C  3 216 ? -20.935 -34.951 -48.075  1.00 323.31 ? 214  ARG C O   1 
ATOM   7964  C  CB  . ARG C  3 216 ? -22.874 -37.319 -47.899  1.00 313.00 ? 214  ARG C CB  1 
ATOM   7965  C  CG  . ARG C  3 216 ? -23.262 -38.783 -47.899  1.00 307.24 ? 214  ARG C CG  1 
ATOM   7966  C  CD  . ARG C  3 216 ? -24.494 -39.018 -48.751  1.00 301.65 ? 214  ARG C CD  1 
ATOM   7967  N  NE  . ARG C  3 216 ? -24.751 -40.437 -48.957  1.00 299.06 ? 214  ARG C NE  1 
ATOM   7968  C  CZ  . ARG C  3 216 ? -25.697 -40.911 -49.760  1.00 305.64 ? 214  ARG C CZ  1 
ATOM   7969  N  NH1 . ARG C  3 216 ? -26.475 -40.075 -50.435  1.00 300.11 ? 214  ARG C NH1 1 
ATOM   7970  N  NH2 . ARG C  3 216 ? -25.863 -42.219 -49.891  1.00 323.08 ? 214  ARG C NH2 1 
ATOM   7971  N  N   . ARG C  3 217 ? -21.754 -34.810 -45.969  1.00 319.38 ? 215  ARG C N   1 
ATOM   7972  C  CA  . ARG C  3 217 ? -21.649 -33.362 -45.804  1.00 309.14 ? 215  ARG C CA  1 
ATOM   7973  C  C   . ARG C  3 217 ? -22.611 -32.617 -46.726  1.00 304.17 ? 215  ARG C C   1 
ATOM   7974  O  O   . ARG C  3 217 ? -22.856 -31.421 -46.537  1.00 299.55 ? 215  ARG C O   1 
ATOM   7975  C  CB  . ARG C  3 217 ? -20.210 -32.884 -46.034  1.00 307.45 ? 215  ARG C CB  1 
ATOM   7976  C  CG  . ARG C  3 217 ? -19.862 -31.595 -45.307  1.00 291.20 ? 215  ARG C CG  1 
ATOM   7977  C  CD  . ARG C  3 217 ? -18.875 -30.749 -46.099  1.00 286.83 ? 215  ARG C CD  1 
ATOM   7978  N  NE  . ARG C  3 217 ? -17.666 -31.485 -46.458  1.00 290.09 ? 215  ARG C NE  1 
ATOM   7979  C  CZ  . ARG C  3 217 ? -16.664 -30.972 -47.167  1.00 290.60 ? 215  ARG C CZ  1 
ATOM   7980  N  NH1 . ARG C  3 217 ? -16.723 -29.718 -47.592  1.00 280.17 ? 215  ARG C NH1 1 
ATOM   7981  N  NH2 . ARG C  3 217 ? -15.604 -31.712 -47.453  1.00 300.61 ? 215  ARG C NH2 1 
ATOM   7982  N  N   . GLY C  3 218 ? -23.175 -33.313 -47.712  1.00 291.72 ? 216  GLY C N   1 
ATOM   7983  C  CA  . GLY C  3 218 ? -24.106 -32.744 -48.660  1.00 280.82 ? 216  GLY C CA  1 
ATOM   7984  C  C   . GLY C  3 218 ? -25.560 -32.934 -48.319  1.00 276.82 ? 216  GLY C C   1 
ATOM   7985  O  O   . GLY C  3 218 ? -26.435 -32.497 -49.076  1.00 265.06 ? 216  GLY C O   1 
ATOM   7986  N  N   . ASP C  3 219 ? -25.849 -33.581 -47.190  1.00 286.74 ? 217  ASP C N   1 
ATOM   7987  C  CA  . ASP C  3 219 ? -27.224 -33.816 -46.777  1.00 285.94 ? 217  ASP C CA  1 
ATOM   7988  C  C   . ASP C  3 219 ? -27.817 -32.629 -46.026  1.00 279.36 ? 217  ASP C C   1 
ATOM   7989  O  O   . ASP C  3 219 ? -28.976 -32.272 -46.265  1.00 276.33 ? 217  ASP C O   1 
ATOM   7990  C  CB  . ASP C  3 219 ? -27.305 -35.085 -45.922  1.00 281.74 ? 217  ASP C CB  1 
ATOM   7991  C  CG  . ASP C  3 219 ? -26.966 -36.344 -46.712  1.00 280.30 ? 217  ASP C CG  1 
ATOM   7992  O  OD1 . ASP C  3 219 ? -26.105 -36.277 -47.615  1.00 277.32 ? 217  ASP C OD1 1 
ATOM   7993  O  OD2 . ASP C  3 219 ? -27.562 -37.407 -46.427  1.00 280.27 ? 217  ASP C OD2 1 
ATOM   7994  N  N   . LEU C  3 220 ? -27.054 -31.992 -45.132  1.00 268.79 ? 218  LEU C N   1 
ATOM   7995  C  CA  . LEU C  3 220 ? -27.622 -30.880 -44.377  1.00 262.85 ? 218  LEU C CA  1 
ATOM   7996  C  C   . LEU C  3 220 ? -27.562 -29.573 -45.158  1.00 252.79 ? 218  LEU C C   1 
ATOM   7997  O  O   . LEU C  3 220 ? -28.413 -28.693 -44.957  1.00 242.08 ? 218  LEU C O   1 
ATOM   7998  C  CB  . LEU C  3 220 ? -26.914 -30.721 -43.023  1.00 258.67 ? 218  LEU C CB  1 
ATOM   7999  C  CG  . LEU C  3 220 ? -27.608 -29.753 -42.054  1.00 252.72 ? 218  LEU C CG  1 
ATOM   8000  C  CD1 . LEU C  3 220 ? -29.037 -30.184 -41.847  1.00 251.28 ? 218  LEU C CD1 1 
ATOM   8001  C  CD2 . LEU C  3 220 ? -26.909 -29.648 -40.710  1.00 255.28 ? 218  LEU C CD2 1 
ATOM   8002  N  N   . ALA C  3 221 ? -26.579 -29.429 -46.047  1.00 262.24 ? 219  ALA C N   1 
ATOM   8003  C  CA  . ALA C  3 221 ? -26.428 -28.225 -46.844  1.00 259.55 ? 219  ALA C CA  1 
ATOM   8004  C  C   . ALA C  3 221 ? -26.083 -28.613 -48.268  1.00 262.04 ? 219  ALA C C   1 
ATOM   8005  O  O   . ALA C  3 221 ? -25.525 -29.682 -48.529  1.00 268.04 ? 219  ALA C O   1 
ATOM   8006  C  CB  . ALA C  3 221 ? -25.338 -27.296 -46.300  1.00 253.22 ? 219  ALA C CB  1 
ATOM   8007  N  N   . THR C  3 222 ? -26.398 -27.719 -49.191  1.00 252.98 ? 220  THR C N   1 
ATOM   8008  C  CA  . THR C  3 222 ? -26.069 -27.983 -50.584  1.00 258.24 ? 220  THR C CA  1 
ATOM   8009  C  C   . THR C  3 222 ? -24.558 -27.949 -50.793  1.00 267.70 ? 220  THR C C   1 
ATOM   8010  O  O   . THR C  3 222 ? -23.859 -27.040 -50.336  1.00 262.05 ? 220  THR C O   1 
ATOM   8011  C  CB  . THR C  3 222 ? -26.767 -26.996 -51.499  1.00 249.30 ? 220  THR C CB  1 
ATOM   8012  O  OG1 . THR C  3 222 ? -26.415 -27.279 -52.860  1.00 251.84 ? 220  THR C OG1 1 
ATOM   8013  C  CG2 . THR C  3 222 ? -26.386 -25.559 -51.145  1.00 238.99 ? 220  THR C CG2 1 
ATOM   8014  N  N   . ILE C  3 223 ? -24.057 -28.937 -51.529  1.00 290.86 ? 221  ILE C N   1 
ATOM   8015  C  CA  . ILE C  3 223 ? -22.625 -29.084 -51.784  1.00 292.27 ? 221  ILE C CA  1 
ATOM   8016  C  C   . ILE C  3 223 ? -22.446 -29.421 -53.260  1.00 297.89 ? 221  ILE C C   1 
ATOM   8017  O  O   . ILE C  3 223 ? -23.251 -30.165 -53.833  1.00 304.78 ? 221  ILE C O   1 
ATOM   8018  C  CB  . ILE C  3 223 ? -22.002 -30.173 -50.880  1.00 297.80 ? 221  ILE C CB  1 
ATOM   8019  C  CG1 . ILE C  3 223 ? -22.283 -29.899 -49.394  1.00 288.31 ? 221  ILE C CG1 1 
ATOM   8020  C  CG2 . ILE C  3 223 ? -20.499 -30.253 -51.113  1.00 294.48 ? 221  ILE C CG2 1 
ATOM   8021  C  CD1 . ILE C  3 223 ? -21.486 -28.730 -48.829  1.00 276.44 ? 221  ILE C CD1 1 
ATOM   8022  N  N   . HIS C  3 224 ? -21.366 -28.901 -53.861  1.00 307.30 ? 222  HIS C N   1 
ATOM   8023  C  CA  . HIS C  3 224 ? -21.068 -29.050 -55.293  1.00 325.43 ? 222  HIS C CA  1 
ATOM   8024  C  C   . HIS C  3 224 ? -22.329 -28.949 -56.152  1.00 324.24 ? 222  HIS C C   1 
ATOM   8025  O  O   . HIS C  3 224 ? -22.493 -29.680 -57.135  1.00 330.21 ? 222  HIS C O   1 
ATOM   8026  C  CB  . HIS C  3 224 ? -20.315 -30.360 -55.587  1.00 330.93 ? 222  HIS C CB  1 
ATOM   8027  C  CG  . HIS C  3 224 ? -21.143 -31.600 -55.421  1.00 328.72 ? 222  HIS C CG  1 
ATOM   8028  N  ND1 . HIS C  3 224 ? -21.439 -32.140 -54.187  1.00 316.23 ? 222  HIS C ND1 1 
ATOM   8029  C  CD2 . HIS C  3 224 ? -21.695 -32.434 -56.337  1.00 331.85 ? 222  HIS C CD2 1 
ATOM   8030  C  CE1 . HIS C  3 224 ? -22.160 -33.237 -54.348  1.00 317.79 ? 222  HIS C CE1 1 
ATOM   8031  N  NE2 . HIS C  3 224 ? -22.329 -33.438 -55.643  1.00 331.01 ? 222  HIS C NE2 1 
ATOM   8032  N  N   . GLY C  3 225 ? -23.223 -28.030 -55.789  1.00 287.48 ? 223  GLY C N   1 
ATOM   8033  C  CA  . GLY C  3 225 ? -24.444 -27.821 -56.537  1.00 272.36 ? 223  GLY C CA  1 
ATOM   8034  C  C   . GLY C  3 225 ? -24.733 -26.337 -56.656  1.00 252.40 ? 223  GLY C C   1 
ATOM   8035  O  O   . GLY C  3 225 ? -24.243 -25.515 -55.871  1.00 242.85 ? 223  GLY C O   1 
ATOM   8036  N  N   . MET C  3 226 ? -25.546 -26.005 -57.658  1.00 248.67 ? 224  MET C N   1 
ATOM   8037  C  CA  . MET C  3 226 ? -25.885 -24.613 -57.915  1.00 235.73 ? 224  MET C CA  1 
ATOM   8038  C  C   . MET C  3 226 ? -26.688 -24.050 -56.750  1.00 227.60 ? 224  MET C C   1 
ATOM   8039  O  O   . MET C  3 226 ? -27.305 -24.791 -55.980  1.00 219.09 ? 224  MET C O   1 
ATOM   8040  C  CB  . MET C  3 226 ? -26.670 -24.485 -59.221  1.00 239.53 ? 224  MET C CB  1 
ATOM   8041  C  CG  . MET C  3 226 ? -27.974 -25.254 -59.248  1.00 237.66 ? 224  MET C CG  1 
ATOM   8042  S  SD  . MET C  3 226 ? -28.548 -25.474 -60.937  1.00 234.79 ? 224  MET C SD  1 
ATOM   8043  C  CE  . MET C  3 226 ? -28.499 -23.779 -61.512  1.00 232.66 ? 224  MET C CE  1 
ATOM   8044  N  N   . ASN C  3 227 ? -26.657 -22.721 -56.618  1.00 244.91 ? 225  ASN C N   1 
ATOM   8045  C  CA  . ASN C  3 227 ? -27.256 -22.001 -55.495  1.00 248.85 ? 225  ASN C CA  1 
ATOM   8046  C  C   . ASN C  3 227 ? -26.540 -22.265 -54.181  1.00 239.37 ? 225  ASN C C   1 
ATOM   8047  O  O   . ASN C  3 227 ? -27.082 -21.984 -53.108  1.00 222.52 ? 225  ASN C O   1 
ATOM   8048  C  CB  . ASN C  3 227 ? -28.750 -22.334 -55.337  1.00 252.12 ? 225  ASN C CB  1 
ATOM   8049  C  CG  . ASN C  3 227 ? -29.544 -22.014 -56.578  1.00 252.59 ? 225  ASN C CG  1 
ATOM   8050  O  OD1 . ASN C  3 227 ? -28.983 -21.827 -57.655  1.00 251.12 ? 225  ASN C OD1 1 
ATOM   8051  N  ND2 . ASN C  3 227 ? -30.864 -21.949 -56.437  1.00 252.82 ? 225  ASN C ND2 1 
ATOM   8052  N  N   . ARG C  3 228 ? -25.328 -22.810 -54.249  1.00 238.15 ? 226  ARG C N   1 
ATOM   8053  C  CA  . ARG C  3 228 ? -24.566 -23.088 -53.050  1.00 222.02 ? 226  ARG C CA  1 
ATOM   8054  C  C   . ARG C  3 228 ? -24.283 -21.800 -52.281  1.00 219.63 ? 226  ARG C C   1 
ATOM   8055  O  O   . ARG C  3 228 ? -24.249 -20.715 -52.866  1.00 213.15 ? 226  ARG C O   1 
ATOM   8056  C  CB  . ARG C  3 228 ? -23.254 -23.766 -53.408  1.00 217.85 ? 226  ARG C CB  1 
ATOM   8057  C  CG  . ARG C  3 228 ? -22.380 -22.944 -54.299  1.00 213.62 ? 226  ARG C CG  1 
ATOM   8058  C  CD  . ARG C  3 228 ? -21.196 -23.762 -54.619  1.00 216.57 ? 226  ARG C CD  1 
ATOM   8059  N  NE  . ARG C  3 228 ? -20.120 -22.997 -55.214  1.00 219.37 ? 226  ARG C NE  1 
ATOM   8060  C  CZ  . ARG C  3 228 ? -18.955 -23.543 -55.511  1.00 227.53 ? 226  ARG C CZ  1 
ATOM   8061  N  NH1 . ARG C  3 228 ? -18.781 -24.825 -55.253  1.00 224.94 ? 226  ARG C NH1 1 
ATOM   8062  N  NH2 . ARG C  3 228 ? -17.989 -22.822 -56.059  1.00 239.20 ? 226  ARG C NH2 1 
ATOM   8063  N  N   . PRO C  3 229 ? -24.070 -21.908 -50.945  1.00 234.10 ? 227  PRO C N   1 
ATOM   8064  C  CA  . PRO C  3 229 ? -23.922 -20.720 -50.089  1.00 235.10 ? 227  PRO C CA  1 
ATOM   8065  C  C   . PRO C  3 229 ? -23.133 -19.569 -50.699  1.00 239.31 ? 227  PRO C C   1 
ATOM   8066  O  O   . PRO C  3 229 ? -22.036 -19.760 -51.237  1.00 242.34 ? 227  PRO C O   1 
ATOM   8067  C  CB  . PRO C  3 229 ? -23.211 -21.289 -48.858  1.00 235.86 ? 227  PRO C CB  1 
ATOM   8068  C  CG  . PRO C  3 229 ? -23.768 -22.680 -48.745  1.00 242.53 ? 227  PRO C CG  1 
ATOM   8069  C  CD  . PRO C  3 229 ? -24.010 -23.159 -50.161  1.00 242.51 ? 227  PRO C CD  1 
ATOM   8070  N  N   . PHE C  3 230 ? -23.702 -18.369 -50.629  1.00 236.96 ? 228  PHE C N   1 
ATOM   8071  C  CA  . PHE C  3 230 ? -23.110 -17.175 -51.209  1.00 235.76 ? 228  PHE C CA  1 
ATOM   8072  C  C   . PHE C  3 230 ? -23.145 -16.044 -50.188  1.00 218.77 ? 228  PHE C C   1 
ATOM   8073  O  O   . PHE C  3 230 ? -23.982 -16.022 -49.284  1.00 215.65 ? 228  PHE C O   1 
ATOM   8074  C  CB  . PHE C  3 230 ? -23.844 -16.750 -52.491  1.00 248.23 ? 228  PHE C CB  1 
ATOM   8075  C  CG  . PHE C  3 230 ? -25.233 -16.218 -52.254  1.00 244.12 ? 228  PHE C CG  1 
ATOM   8076  C  CD1 . PHE C  3 230 ? -26.304 -17.079 -52.069  1.00 240.02 ? 228  PHE C CD1 1 
ATOM   8077  C  CD2 . PHE C  3 230 ? -25.469 -14.852 -52.230  1.00 239.86 ? 228  PHE C CD2 1 
ATOM   8078  C  CE1 . PHE C  3 230 ? -27.580 -16.588 -51.856  1.00 230.26 ? 228  PHE C CE1 1 
ATOM   8079  C  CE2 . PHE C  3 230 ? -26.741 -14.356 -52.018  1.00 233.76 ? 228  PHE C CE2 1 
ATOM   8080  C  CZ  . PHE C  3 230 ? -27.797 -15.225 -51.831  1.00 229.42 ? 228  PHE C CZ  1 
ATOM   8081  N  N   . LEU C  3 231 ? -22.225 -15.094 -50.348  1.00 204.22 ? 229  LEU C N   1 
ATOM   8082  C  CA  . LEU C  3 231 ? -22.095 -13.954 -49.442  1.00 204.28 ? 229  LEU C CA  1 
ATOM   8083  C  C   . LEU C  3 231 ? -22.756 -12.736 -50.082  1.00 204.90 ? 229  LEU C C   1 
ATOM   8084  O  O   . LEU C  3 231 ? -22.209 -12.137 -51.010  1.00 215.50 ? 229  LEU C O   1 
ATOM   8085  C  CB  . LEU C  3 231 ? -20.629 -13.683 -49.126  1.00 206.36 ? 229  LEU C CB  1 
ATOM   8086  C  CG  . LEU C  3 231 ? -20.330 -12.522 -48.175  1.00 216.15 ? 229  LEU C CG  1 
ATOM   8087  C  CD1 . LEU C  3 231 ? -21.009 -12.742 -46.837  1.00 228.26 ? 229  LEU C CD1 1 
ATOM   8088  C  CD2 . LEU C  3 231 ? -18.834 -12.351 -47.985  1.00 215.28 ? 229  LEU C CD2 1 
ATOM   8089  N  N   . LEU C  3 232 ? -23.928 -12.359 -49.572  1.00 205.28 ? 230  LEU C N   1 
ATOM   8090  C  CA  . LEU C  3 232 ? -24.647 -11.201 -50.091  1.00 212.96 ? 230  LEU C CA  1 
ATOM   8091  C  C   . LEU C  3 232 ? -24.036 -9.918  -49.536  1.00 215.85 ? 230  LEU C C   1 
ATOM   8092  O  O   . LEU C  3 232 ? -23.882 -9.765  -48.320  1.00 218.83 ? 230  LEU C O   1 
ATOM   8093  C  CB  . LEU C  3 232 ? -26.130 -11.287 -49.731  1.00 216.37 ? 230  LEU C CB  1 
ATOM   8094  C  CG  . LEU C  3 232 ? -27.083 -10.300 -50.414  1.00 220.51 ? 230  LEU C CG  1 
ATOM   8095  C  CD1 . LEU C  3 232 ? -27.127 -10.536 -51.918  1.00 229.65 ? 230  LEU C CD1 1 
ATOM   8096  C  CD2 . LEU C  3 232 ? -28.477 -10.399 -49.814  1.00 213.89 ? 230  LEU C CD2 1 
ATOM   8097  N  N   . LEU C  3 233 ? -23.685 -8.997  -50.431  1.00 216.65 ? 231  LEU C N   1 
ATOM   8098  C  CA  . LEU C  3 233 ? -23.027 -7.751  -50.066  1.00 216.88 ? 231  LEU C CA  1 
ATOM   8099  C  C   . LEU C  3 233 ? -23.917 -6.568  -50.427  1.00 229.26 ? 231  LEU C C   1 
ATOM   8100  O  O   . LEU C  3 233 ? -24.611 -6.589  -51.448  1.00 241.32 ? 231  LEU C O   1 
ATOM   8101  C  CB  . LEU C  3 233 ? -21.672 -7.620  -50.773  1.00 216.04 ? 231  LEU C CB  1 
ATOM   8102  C  CG  . LEU C  3 233 ? -20.671 -8.765  -50.588  1.00 219.36 ? 231  LEU C CG  1 
ATOM   8103  C  CD1 . LEU C  3 233 ? -19.442 -8.564  -51.469  1.00 229.37 ? 231  LEU C CD1 1 
ATOM   8104  C  CD2 . LEU C  3 233 ? -20.270 -8.888  -49.130  1.00 219.45 ? 231  LEU C CD2 1 
ATOM   8105  N  N   . MET C  3 234 ? -23.899 -5.537  -49.584  1.00 218.60 ? 232  MET C N   1 
ATOM   8106  C  CA  . MET C  3 234 ? -24.655 -4.305  -49.817  1.00 214.33 ? 232  MET C CA  1 
ATOM   8107  C  C   . MET C  3 234 ? -23.726 -3.137  -49.501  1.00 220.99 ? 232  MET C C   1 
ATOM   8108  O  O   . MET C  3 234 ? -23.485 -2.830  -48.330  1.00 215.39 ? 232  MET C O   1 
ATOM   8109  C  CB  . MET C  3 234 ? -25.919 -4.260  -48.967  1.00 210.40 ? 232  MET C CB  1 
ATOM   8110  C  CG  . MET C  3 234 ? -26.837 -5.457  -49.156  1.00 214.75 ? 232  MET C CG  1 
ATOM   8111  S  SD  . MET C  3 234 ? -28.231 -5.449  -48.015  1.00 222.94 ? 232  MET C SD  1 
ATOM   8112  C  CE  . MET C  3 234 ? -29.069 -6.963  -48.478  1.00 219.00 ? 232  MET C CE  1 
ATOM   8113  N  N   . ALA C  3 235 ? -23.202 -2.492  -50.540  1.00 240.34 ? 233  ALA C N   1 
ATOM   8114  C  CA  . ALA C  3 235 ? -22.202 -1.448  -50.383  1.00 249.26 ? 233  ALA C CA  1 
ATOM   8115  C  C   . ALA C  3 235 ? -22.635 -0.192  -51.128  1.00 249.70 ? 233  ALA C C   1 
ATOM   8116  O  O   . ALA C  3 235 ? -23.591 -0.197  -51.907  1.00 240.88 ? 233  ALA C O   1 
ATOM   8117  C  CB  . ALA C  3 235 ? -20.827 -1.916  -50.882  1.00 253.69 ? 233  ALA C CB  1 
ATOM   8118  N  N   . THR C  3 236 ? -21.903 0.905   -50.879  1.00 261.73 ? 234  THR C N   1 
ATOM   8119  C  CA  . THR C  3 236 ? -22.167 2.204   -51.491  1.00 262.22 ? 234  THR C CA  1 
ATOM   8120  C  C   . THR C  3 236 ? -21.196 2.456   -52.633  1.00 269.53 ? 234  THR C C   1 
ATOM   8121  O  O   . THR C  3 236 ? -19.976 2.361   -52.429  1.00 273.24 ? 234  THR C O   1 
ATOM   8122  C  CB  . THR C  3 236 ? -22.046 3.318   -50.455  1.00 258.18 ? 234  THR C CB  1 
ATOM   8123  O  OG1 . THR C  3 236 ? -23.053 3.155   -49.450  1.00 263.08 ? 234  THR C OG1 1 
ATOM   8124  C  CG2 . THR C  3 236 ? -22.214 4.678   -51.107  1.00 249.42 ? 234  THR C CG2 1 
ATOM   8125  N  N   . PRO C  3 237 ? -21.688 2.778   -53.831  1.00 273.79 ? 235  PRO C N   1 
ATOM   8126  C  CA  . PRO C  3 237 ? -20.790 3.017   -54.969  1.00 277.39 ? 235  PRO C CA  1 
ATOM   8127  C  C   . PRO C  3 237 ? -19.853 4.193   -54.728  1.00 275.28 ? 235  PRO C C   1 
ATOM   8128  O  O   . PRO C  3 237 ? -20.119 5.081   -53.914  1.00 278.89 ? 235  PRO C O   1 
ATOM   8129  C  CB  . PRO C  3 237 ? -21.755 3.311   -56.126  1.00 274.35 ? 235  PRO C CB  1 
ATOM   8130  C  CG  . PRO C  3 237 ? -23.034 2.654   -55.726  1.00 267.32 ? 235  PRO C CG  1 
ATOM   8131  C  CD  . PRO C  3 237 ? -23.105 2.793   -54.232  1.00 261.24 ? 235  PRO C CD  1 
ATOM   8132  N  N   . LEU C  3 238 ? -18.733 4.190   -55.459  1.00 255.38 ? 236  LEU C N   1 
ATOM   8133  C  CA  . LEU C  3 238 ? -17.795 5.303   -55.366  1.00 254.52 ? 236  LEU C CA  1 
ATOM   8134  C  C   . LEU C  3 238 ? -18.390 6.576   -55.943  1.00 265.67 ? 236  LEU C C   1 
ATOM   8135  O  O   . LEU C  3 238 ? -17.955 7.678   -55.591  1.00 271.89 ? 236  LEU C O   1 
ATOM   8136  C  CB  . LEU C  3 238 ? -16.488 4.970   -56.090  1.00 255.20 ? 236  LEU C CB  1 
ATOM   8137  C  CG  . LEU C  3 238 ? -15.657 3.775   -55.613  1.00 248.18 ? 236  LEU C CG  1 
ATOM   8138  C  CD1 . LEU C  3 238 ? -16.144 2.463   -56.225  1.00 247.96 ? 236  LEU C CD1 1 
ATOM   8139  C  CD2 . LEU C  3 238 ? -14.190 4.011   -55.928  1.00 249.21 ? 236  LEU C CD2 1 
ATOM   8140  N  N   . GLU C  3 239 ? -19.374 6.440   -56.836  1.00 271.89 ? 237  GLU C N   1 
ATOM   8141  C  CA  . GLU C  3 239 ? -20.059 7.604   -57.382  1.00 276.81 ? 237  GLU C CA  1 
ATOM   8142  C  C   . GLU C  3 239 ? -20.798 8.377   -56.297  1.00 283.64 ? 237  GLU C C   1 
ATOM   8143  O  O   . GLU C  3 239 ? -20.975 9.596   -56.413  1.00 286.69 ? 237  GLU C O   1 
ATOM   8144  C  CB  . GLU C  3 239 ? -21.031 7.157   -58.476  1.00 269.83 ? 237  GLU C CB  1 
ATOM   8145  C  CG  . GLU C  3 239 ? -20.401 6.274   -59.543  1.00 264.63 ? 237  GLU C CG  1 
ATOM   8146  C  CD  . GLU C  3 239 ? -21.375 5.250   -60.095  1.00 257.73 ? 237  GLU C CD  1 
ATOM   8147  O  OE1 . GLU C  3 239 ? -22.495 5.146   -59.552  1.00 247.97 ? 237  GLU C OE1 1 
ATOM   8148  O  OE2 . GLU C  3 239 ? -21.021 4.548   -61.066  1.00 264.70 ? 237  GLU C OE2 1 
ATOM   8149  N  N   . ARG C  3 240 ? -21.225 7.690   -55.236  1.00 281.15 ? 238  ARG C N   1 
ATOM   8150  C  CA  . ARG C  3 240 ? -21.971 8.330   -54.158  1.00 269.73 ? 238  ARG C CA  1 
ATOM   8151  C  C   . ARG C  3 240 ? -21.035 9.007   -53.161  1.00 264.07 ? 238  ARG C C   1 
ATOM   8152  O  O   . ARG C  3 240 ? -21.156 10.208  -52.899  1.00 266.64 ? 238  ARG C O   1 
ATOM   8153  C  CB  . ARG C  3 240 ? -22.849 7.296   -53.447  1.00 261.29 ? 238  ARG C CB  1 
ATOM   8154  C  CG  . ARG C  3 240 ? -23.640 6.388   -54.374  1.00 255.19 ? 238  ARG C CG  1 
ATOM   8155  C  CD  . ARG C  3 240 ? -24.732 7.141   -55.108  1.00 254.23 ? 238  ARG C CD  1 
ATOM   8156  N  NE  . ARG C  3 240 ? -25.533 6.249   -55.938  1.00 254.13 ? 238  ARG C NE  1 
ATOM   8157  C  CZ  . ARG C  3 240 ? -25.324 6.050   -57.234  1.00 261.32 ? 238  ARG C CZ  1 
ATOM   8158  N  NH1 . ARG C  3 240 ? -24.341 6.687   -57.854  1.00 260.16 ? 238  ARG C NH1 1 
ATOM   8159  N  NH2 . ARG C  3 240 ? -26.100 5.216   -57.910  1.00 270.33 ? 238  ARG C NH2 1 
ATOM   8160  N  N   . ALA C  3 241 ? -20.093 8.244   -52.596  1.00 252.11 ? 239  ALA C N   1 
ATOM   8161  C  CA  . ALA C  3 241 ? -19.217 8.779   -51.556  1.00 254.15 ? 239  ALA C CA  1 
ATOM   8162  C  C   . ALA C  3 241 ? -18.385 9.945   -52.076  1.00 265.37 ? 239  ALA C C   1 
ATOM   8163  O  O   . ALA C  3 241 ? -18.265 10.981  -51.411  1.00 271.05 ? 239  ALA C O   1 
ATOM   8164  C  CB  . ALA C  3 241 ? -18.315 7.670   -51.015  1.00 251.64 ? 239  ALA C CB  1 
ATOM   8165  N  N   . GLN C  3 242 ? -17.805 9.797   -53.263  1.00 272.30 ? 240  GLN C N   1 
ATOM   8166  C  CA  . GLN C  3 242 ? -17.009 10.862  -53.868  1.00 273.08 ? 240  GLN C CA  1 
ATOM   8167  C  C   . GLN C  3 242 ? -17.893 12.002  -54.366  1.00 266.36 ? 240  GLN C C   1 
ATOM   8168  O  O   . GLN C  3 242 ? -17.622 13.174  -54.102  1.00 264.91 ? 240  GLN C O   1 
ATOM   8169  C  CB  . GLN C  3 242 ? -16.167 10.311  -55.019  1.00 271.65 ? 240  GLN C CB  1 
ATOM   8170  C  CG  . GLN C  3 242 ? -15.214 9.203   -54.610  1.00 264.06 ? 240  GLN C CG  1 
ATOM   8171  C  CD  . GLN C  3 242 ? -14.418 8.664   -55.779  1.00 265.10 ? 240  GLN C CD  1 
ATOM   8172  O  OE1 . GLN C  3 242 ? -14.527 9.160   -56.901  1.00 271.68 ? 240  GLN C OE1 1 
ATOM   8173  N  NE2 . GLN C  3 242 ? -13.610 7.642   -55.522  1.00 260.25 ? 240  GLN C NE2 1 
ATOM   8174  N  N   . ALA C  3 252 ? -28.389 10.789  -37.620  1.00 268.23 ? 250  ALA C N   1 
ATOM   8175  C  CA  . ALA C  3 252 ? -29.262 11.118  -36.498  1.00 270.72 ? 250  ALA C CA  1 
ATOM   8176  C  C   . ALA C  3 252 ? -28.498 11.096  -35.173  1.00 265.03 ? 250  ALA C C   1 
ATOM   8177  O  O   . ALA C  3 252 ? -28.465 10.076  -34.484  1.00 266.46 ? 250  ALA C O   1 
ATOM   8178  C  CB  . ALA C  3 252 ? -30.446 10.159  -36.449  1.00 270.62 ? 250  ALA C CB  1 
ATOM   8179  N  N   . LEU C  3 253 ? -27.871 12.220  -34.832  1.00 245.83 ? 251  LEU C N   1 
ATOM   8180  C  CA  . LEU C  3 253 ? -27.108 12.328  -33.598  1.00 232.21 ? 251  LEU C CA  1 
ATOM   8181  C  C   . LEU C  3 253 ? -28.035 12.606  -32.414  1.00 238.18 ? 251  LEU C C   1 
ATOM   8182  O  O   . LEU C  3 253 ? -29.133 13.154  -32.560  1.00 216.62 ? 251  LEU C O   1 
ATOM   8183  C  CB  . LEU C  3 253 ? -26.048 13.423  -33.721  1.00 221.58 ? 251  LEU C CB  1 
ATOM   8184  C  CG  . LEU C  3 253 ? -25.073 13.247  -34.888  1.00 225.52 ? 251  LEU C CG  1 
ATOM   8185  C  CD1 . LEU C  3 253 ? -24.070 14.387  -34.940  1.00 230.12 ? 251  LEU C CD1 1 
ATOM   8186  C  CD2 . LEU C  3 253 ? -24.363 11.904  -34.788  1.00 225.08 ? 251  LEU C CD2 1 
ATOM   8187  N  N   . ASP C  3 254 ? -27.572 12.218  -31.222  1.00 272.86 ? 252  ASP C N   1 
ATOM   8188  C  CA  . ASP C  3 254 ? -28.383 12.295  -30.010  1.00 267.72 ? 252  ASP C CA  1 
ATOM   8189  C  C   . ASP C  3 254 ? -28.002 13.476  -29.122  1.00 247.43 ? 252  ASP C C   1 
ATOM   8190  O  O   . ASP C  3 254 ? -27.790 14.592  -29.607  1.00 232.13 ? 252  ASP C O   1 
ATOM   8191  C  CB  . ASP C  3 254 ? -28.281 10.987  -29.212  1.00 276.43 ? 252  ASP C CB  1 
ATOM   8192  C  CG  . ASP C  3 254 ? -26.842 10.515  -29.014  1.00 270.08 ? 252  ASP C CG  1 
ATOM   8193  O  OD1 . ASP C  3 254 ? -25.902 11.297  -29.272  1.00 282.44 ? 252  ASP C OD1 1 
ATOM   8194  O  OD2 . ASP C  3 254 ? -26.652 9.357   -28.581  1.00 248.38 ? 252  ASP C OD2 1 
ATOM   8195  N  N   . THR C  3 255 ? -27.946 13.238  -27.809  1.00 242.16 ? 253  THR C N   1 
ATOM   8196  C  CA  . THR C  3 255 ? -27.632 14.294  -26.855  1.00 236.73 ? 253  THR C CA  1 
ATOM   8197  C  C   . THR C  3 255 ? -26.181 14.751  -26.948  1.00 250.99 ? 253  THR C C   1 
ATOM   8198  O  O   . THR C  3 255 ? -25.872 15.872  -26.530  1.00 256.47 ? 253  THR C O   1 
ATOM   8199  C  CB  . THR C  3 255 ? -27.932 13.816  -25.435  1.00 236.16 ? 253  THR C CB  1 
ATOM   8200  O  OG1 . THR C  3 255 ? -27.070 12.719  -25.111  1.00 255.87 ? 253  THR C OG1 1 
ATOM   8201  C  CG2 . THR C  3 255 ? -29.377 13.353  -25.329  1.00 222.01 ? 253  THR C CG2 1 
ATOM   8202  N  N   . ASN C  3 256 ? -25.290 13.917  -27.492  1.00 254.69 ? 254  ASN C N   1 
ATOM   8203  C  CA  . ASN C  3 256 ? -23.872 14.253  -27.583  1.00 254.89 ? 254  ASN C CA  1 
ATOM   8204  C  C   . ASN C  3 256 ? -23.586 15.327  -28.621  1.00 260.83 ? 254  ASN C C   1 
ATOM   8205  O  O   . ASN C  3 256 ? -22.443 15.785  -28.721  1.00 262.40 ? 254  ASN C O   1 
ATOM   8206  C  CB  . ASN C  3 256 ? -23.061 12.998  -27.909  1.00 252.24 ? 254  ASN C CB  1 
ATOM   8207  C  CG  . ASN C  3 256 ? -23.216 11.916  -26.861  1.00 258.28 ? 254  ASN C CG  1 
ATOM   8208  O  OD1 . ASN C  3 256 ? -23.393 12.204  -25.677  1.00 256.70 ? 254  ASN C OD1 1 
ATOM   8209  N  ND2 . ASN C  3 256 ? -23.160 10.662  -27.292  1.00 265.89 ? 254  ASN C ND2 1 
ATOM   8210  N  N   . TYR C  3 257 ? -24.590 15.729  -29.392  1.00 264.21 ? 255  TYR C N   1 
ATOM   8211  C  CA  . TYR C  3 257 ? -24.450 16.754  -30.414  1.00 262.23 ? 255  TYR C CA  1 
ATOM   8212  C  C   . TYR C  3 257 ? -25.539 17.793  -30.203  1.00 245.54 ? 255  TYR C C   1 
ATOM   8213  O  O   . TYR C  3 257 ? -25.358 18.975  -30.512  1.00 248.41 ? 255  TYR C O   1 
ATOM   8214  C  CB  . TYR C  3 257 ? -24.548 16.139  -31.809  1.00 274.49 ? 255  TYR C CB  1 
ATOM   8215  C  CG  . TYR C  3 257 ? -24.805 17.136  -32.916  1.00 273.66 ? 255  TYR C CG  1 
ATOM   8216  C  CD1 . TYR C  3 257 ? -23.775 17.902  -33.446  1.00 277.21 ? 255  TYR C CD1 1 
ATOM   8217  C  CD2 . TYR C  3 257 ? -26.086 17.317  -33.422  1.00 268.89 ? 255  TYR C CD2 1 
ATOM   8218  C  CE1 . TYR C  3 257 ? -24.013 18.814  -34.458  1.00 282.23 ? 255  TYR C CE1 1 
ATOM   8219  C  CE2 . TYR C  3 257 ? -26.334 18.228  -34.428  1.00 271.20 ? 255  TYR C CE2 1 
ATOM   8220  C  CZ  . TYR C  3 257 ? -25.295 18.973  -34.944  1.00 281.56 ? 255  TYR C CZ  1 
ATOM   8221  O  OH  . TYR C  3 257 ? -25.539 19.881  -35.948  1.00 294.09 ? 255  TYR C OH  1 
ATOM   8222  N  N   . CYS C  3 258 ? -26.678 17.348  -29.675  1.00 235.49 ? 256  CYS C N   1 
ATOM   8223  C  CA  . CYS C  3 258 ? -27.830 18.219  -29.516  1.00 241.30 ? 256  CYS C CA  1 
ATOM   8224  C  C   . CYS C  3 258 ? -27.733 19.121  -28.298  1.00 247.84 ? 256  CYS C C   1 
ATOM   8225  O  O   . CYS C  3 258 ? -28.481 20.100  -28.210  1.00 240.84 ? 256  CYS C O   1 
ATOM   8226  C  CB  . CYS C  3 258 ? -29.109 17.383  -29.426  1.00 242.79 ? 256  CYS C CB  1 
ATOM   8227  S  SG  . CYS C  3 258 ? -29.999 17.444  -30.965  1.00 248.68 ? 256  CYS C SG  1 
ATOM   8228  N  N   . PHE C  3 259 ? -26.838 18.817  -27.363  1.00 263.51 ? 257  PHE C N   1 
ATOM   8229  C  CA  . PHE C  3 259 ? -26.655 19.639  -26.177  1.00 271.69 ? 257  PHE C CA  1 
ATOM   8230  C  C   . PHE C  3 259 ? -25.431 20.536  -26.271  1.00 279.99 ? 257  PHE C C   1 
ATOM   8231  O  O   . PHE C  3 259 ? -25.362 21.544  -25.558  1.00 282.29 ? 257  PHE C O   1 
ATOM   8232  C  CB  . PHE C  3 259 ? -26.547 18.750  -24.930  1.00 267.90 ? 257  PHE C CB  1 
ATOM   8233  C  CG  . PHE C  3 259 ? -27.860 18.161  -24.481  1.00 259.35 ? 257  PHE C CG  1 
ATOM   8234  C  CD1 . PHE C  3 259 ? -28.611 17.365  -25.333  1.00 253.43 ? 257  PHE C CD1 1 
ATOM   8235  C  CD2 . PHE C  3 259 ? -28.326 18.381  -23.196  1.00 254.13 ? 257  PHE C CD2 1 
ATOM   8236  C  CE1 . PHE C  3 259 ? -29.812 16.820  -24.918  1.00 249.48 ? 257  PHE C CE1 1 
ATOM   8237  C  CE2 . PHE C  3 259 ? -29.520 17.831  -22.775  1.00 247.47 ? 257  PHE C CE2 1 
ATOM   8238  C  CZ  . PHE C  3 259 ? -30.265 17.052  -23.637  1.00 245.75 ? 257  PHE C CZ  1 
ATOM   8239  N  N   . SER C  3 260 ? -24.467 20.184  -27.120  1.00 281.71 ? 258  SER C N   1 
ATOM   8240  C  CA  . SER C  3 260 ? -23.257 20.967  -27.315  1.00 277.24 ? 258  SER C CA  1 
ATOM   8241  C  C   . SER C  3 260 ? -23.380 21.981  -28.444  1.00 282.00 ? 258  SER C C   1 
ATOM   8242  O  O   . SER C  3 260 ? -22.506 22.847  -28.574  1.00 279.84 ? 258  SER C O   1 
ATOM   8243  C  CB  . SER C  3 260 ? -22.063 20.042  -27.585  1.00 271.64 ? 258  SER C CB  1 
ATOM   8244  O  OG  . SER C  3 260 ? -22.283 19.236  -28.730  1.00 267.29 ? 258  SER C OG  1 
ATOM   8245  N  N   . SER C  3 261 ? -24.431 21.901  -29.257  1.00 283.14 ? 259  SER C N   1 
ATOM   8246  C  CA  . SER C  3 261 ? -24.619 22.808  -30.377  1.00 279.35 ? 259  SER C CA  1 
ATOM   8247  C  C   . SER C  3 261 ? -26.040 23.357  -30.375  1.00 267.77 ? 259  SER C C   1 
ATOM   8248  O  O   . SER C  3 261 ? -26.957 22.783  -29.780  1.00 258.40 ? 259  SER C O   1 
ATOM   8249  C  CB  . SER C  3 261 ? -24.327 22.116  -31.714  1.00 277.89 ? 259  SER C CB  1 
ATOM   8250  O  OG  . SER C  3 261 ? -25.191 21.010  -31.911  1.00 271.66 ? 259  SER C OG  1 
ATOM   8251  N  N   . THR C  3 262 ? -26.210 24.490  -31.058  1.00 268.20 ? 260  THR C N   1 
ATOM   8252  C  CA  . THR C  3 262 ? -27.504 25.162  -31.188  1.00 267.16 ? 260  THR C CA  1 
ATOM   8253  C  C   . THR C  3 262 ? -28.075 24.848  -32.566  1.00 257.06 ? 260  THR C C   1 
ATOM   8254  O  O   . THR C  3 262 ? -27.749 25.514  -33.552  1.00 263.27 ? 260  THR C O   1 
ATOM   8255  C  CB  . THR C  3 262 ? -27.354 26.665  -30.984  1.00 274.09 ? 260  THR C CB  1 
ATOM   8256  O  OG1 . THR C  3 262 ? -26.756 26.922  -29.708  1.00 277.12 ? 260  THR C OG1 1 
ATOM   8257  C  CG2 . THR C  3 262 ? -28.712 27.353  -31.058  1.00 267.48 ? 260  THR C CG2 1 
ATOM   8258  N  N   . GLU C  3 263 ? -28.935 23.837  -32.636  1.00 243.21 ? 261  GLU C N   1 
ATOM   8259  C  CA  . GLU C  3 263 ? -29.524 23.422  -33.900  1.00 238.29 ? 261  GLU C CA  1 
ATOM   8260  C  C   . GLU C  3 263 ? -30.787 24.225  -34.185  1.00 233.79 ? 261  GLU C C   1 
ATOM   8261  O  O   . GLU C  3 263 ? -31.560 24.538  -33.276  1.00 228.51 ? 261  GLU C O   1 
ATOM   8262  C  CB  . GLU C  3 263 ? -29.843 21.925  -33.877  1.00 240.67 ? 261  GLU C CB  1 
ATOM   8263  C  CG  . GLU C  3 263 ? -30.240 21.332  -35.223  1.00 240.57 ? 261  GLU C CG  1 
ATOM   8264  C  CD  . GLU C  3 263 ? -29.083 21.259  -36.202  1.00 231.03 ? 261  GLU C CD  1 
ATOM   8265  O  OE1 . GLU C  3 263 ? -27.928 21.126  -35.748  1.00 227.63 ? 261  GLU C OE1 1 
ATOM   8266  O  OE2 . GLU C  3 263 ? -29.329 21.337  -37.424  1.00 232.28 ? 261  GLU C OE2 1 
ATOM   8267  N  N   . LYS C  3 264 ? -30.977 24.573  -35.454  1.00 249.82 ? 262  LYS C N   1 
ATOM   8268  C  CA  . LYS C  3 264 ? -32.230 25.149  -35.918  1.00 248.35 ? 262  LYS C CA  1 
ATOM   8269  C  C   . LYS C  3 264 ? -33.197 24.084  -36.421  1.00 244.19 ? 262  LYS C C   1 
ATOM   8270  O  O   . LYS C  3 264 ? -34.386 24.373  -36.595  1.00 236.15 ? 262  LYS C O   1 
ATOM   8271  C  CB  . LYS C  3 264 ? -31.949 26.186  -37.019  1.00 255.23 ? 262  LYS C CB  1 
ATOM   8272  C  CG  . LYS C  3 264 ? -33.154 26.997  -37.472  1.00 256.43 ? 262  LYS C CG  1 
ATOM   8273  C  CD  . LYS C  3 264 ? -33.895 27.596  -36.287  1.00 257.80 ? 262  LYS C CD  1 
ATOM   8274  C  CE  . LYS C  3 264 ? -35.133 28.359  -36.738  1.00 258.25 ? 262  LYS C CE  1 
ATOM   8275  N  NZ  . LYS C  3 264 ? -35.931 28.878  -35.590  1.00 249.19 ? 262  LYS C NZ  1 
ATOM   8276  N  N   . ASN C  3 265 ? -32.717 22.860  -36.634  1.00 241.43 ? 263  ASN C N   1 
ATOM   8277  C  CA  . ASN C  3 265 ? -33.503 21.739  -37.119  1.00 233.10 ? 263  ASN C CA  1 
ATOM   8278  C  C   . ASN C  3 265 ? -33.983 20.854  -35.968  1.00 230.07 ? 263  ASN C C   1 
ATOM   8279  O  O   . ASN C  3 265 ? -33.916 21.217  -34.790  1.00 223.18 ? 263  ASN C O   1 
ATOM   8280  C  CB  . ASN C  3 265 ? -32.681 20.927  -38.119  1.00 242.39 ? 263  ASN C CB  1 
ATOM   8281  C  CG  . ASN C  3 265 ? -32.560 21.610  -39.457  1.00 252.38 ? 263  ASN C CG  1 
ATOM   8282  O  OD1 . ASN C  3 265 ? -33.552 22.075  -40.019  1.00 254.10 ? 263  ASN C OD1 1 
ATOM   8283  N  ND2 . ASN C  3 265 ? -31.343 21.677  -39.979  1.00 258.58 ? 263  ASN C ND2 1 
ATOM   8284  N  N   . CYS C  3 266 ? -34.458 19.659  -36.323  1.00 236.13 ? 264  CYS C N   1 
ATOM   8285  C  CA  . CYS C  3 266 ? -35.000 18.695  -35.375  1.00 235.52 ? 264  CYS C CA  1 
ATOM   8286  C  C   . CYS C  3 266 ? -33.935 18.193  -34.410  1.00 221.96 ? 264  CYS C C   1 
ATOM   8287  O  O   . CYS C  3 266 ? -33.243 17.207  -34.687  1.00 229.80 ? 264  CYS C O   1 
ATOM   8288  C  CB  . CYS C  3 266 ? -35.622 17.516  -36.117  1.00 245.86 ? 264  CYS C CB  1 
ATOM   8289  S  SG  . CYS C  3 266 ? -36.195 16.192  -35.041  1.00 249.36 ? 264  CYS C SG  1 
ATOM   8290  N  N   . CYS C  3 267 ? -33.788 18.881  -33.287  1.00 212.59 ? 265  CYS C N   1 
ATOM   8291  C  CA  . CYS C  3 267 ? -32.828 18.533  -32.254  1.00 213.00 ? 265  CYS C CA  1 
ATOM   8292  C  C   . CYS C  3 267 ? -33.570 18.232  -30.955  1.00 214.66 ? 265  CYS C C   1 
ATOM   8293  O  O   . CYS C  3 267 ? -34.630 18.806  -30.687  1.00 216.40 ? 265  CYS C O   1 
ATOM   8294  C  CB  . CYS C  3 267 ? -31.840 19.683  -32.063  1.00 241.02 ? 265  CYS C CB  1 
ATOM   8295  S  SG  . CYS C  3 267 ? -30.448 19.417  -30.968  1.00 286.51 ? 265  CYS C SG  1 
ATOM   8296  N  N   . VAL C  3 268 ? -33.015 17.335  -30.142  1.00 228.13 ? 266  VAL C N   1 
ATOM   8297  C  CA  . VAL C  3 268 ? -33.624 17.011  -28.853  1.00 228.86 ? 266  VAL C CA  1 
ATOM   8298  C  C   . VAL C  3 268 ? -33.242 18.086  -27.842  1.00 219.59 ? 266  VAL C C   1 
ATOM   8299  O  O   . VAL C  3 268 ? -32.058 18.322  -27.585  1.00 233.21 ? 266  VAL C O   1 
ATOM   8300  C  CB  . VAL C  3 268 ? -33.214 15.613  -28.364  1.00 227.27 ? 266  VAL C CB  1 
ATOM   8301  C  CG1 . VAL C  3 268 ? -31.738 15.354  -28.580  1.00 232.26 ? 266  VAL C CG1 1 
ATOM   8302  C  CG2 . VAL C  3 268 ? -33.585 15.439  -26.892  1.00 220.01 ? 266  VAL C CG2 1 
ATOM   8303  N  N   . ARG C  3 269 ? -34.246 18.747  -27.276  1.00 192.85 ? 267  ARG C N   1 
ATOM   8304  C  CA  . ARG C  3 269 ? -34.008 19.832  -26.340  1.00 199.39 ? 267  ARG C CA  1 
ATOM   8305  C  C   . ARG C  3 269 ? -34.022 19.308  -24.912  1.00 198.41 ? 267  ARG C C   1 
ATOM   8306  O  O   . ARG C  3 269 ? -34.703 18.330  -24.594  1.00 188.70 ? 267  ARG C O   1 
ATOM   8307  C  CB  . ARG C  3 269 ? -35.060 20.927  -26.502  1.00 201.48 ? 267  ARG C CB  1 
ATOM   8308  C  CG  . ARG C  3 269 ? -35.219 21.427  -27.925  1.00 204.13 ? 267  ARG C CG  1 
ATOM   8309  C  CD  . ARG C  3 269 ? -33.909 21.942  -28.485  1.00 211.72 ? 267  ARG C CD  1 
ATOM   8310  N  NE  . ARG C  3 269 ? -34.004 22.197  -29.920  1.00 221.07 ? 267  ARG C NE  1 
ATOM   8311  C  CZ  . ARG C  3 269 ? -32.987 22.591  -30.679  1.00 235.59 ? 267  ARG C CZ  1 
ATOM   8312  N  NH1 . ARG C  3 269 ? -31.789 22.774  -30.139  1.00 252.78 ? 267  ARG C NH1 1 
ATOM   8313  N  NH2 . ARG C  3 269 ? -33.162 22.798  -31.978  1.00 229.21 ? 267  ARG C NH2 1 
ATOM   8314  N  N   . GLN C  3 270 ? -33.257 19.974  -24.052  1.00 212.74 ? 268  GLN C N   1 
ATOM   8315  C  CA  . GLN C  3 270 ? -33.139 19.574  -22.657  1.00 218.06 ? 268  GLN C CA  1 
ATOM   8316  C  C   . GLN C  3 270 ? -34.369 19.999  -21.862  1.00 208.49 ? 268  GLN C C   1 
ATOM   8317  O  O   . GLN C  3 270 ? -34.897 21.101  -22.044  1.00 203.56 ? 268  GLN C O   1 
ATOM   8318  C  CB  . GLN C  3 270 ? -31.879 20.181  -22.043  1.00 229.98 ? 268  GLN C CB  1 
ATOM   8319  C  CG  . GLN C  3 270 ? -31.605 19.758  -20.615  1.00 234.97 ? 268  GLN C CG  1 
ATOM   8320  C  CD  . GLN C  3 270 ? -30.399 20.459  -20.033  1.00 247.73 ? 268  GLN C CD  1 
ATOM   8321  O  OE1 . GLN C  3 270 ? -29.732 21.239  -20.714  1.00 244.29 ? 268  GLN C OE1 1 
ATOM   8322  N  NE2 . GLN C  3 270 ? -30.116 20.192  -18.764  1.00 260.51 ? 268  GLN C NE2 1 
ATOM   8323  N  N   . LEU C  3 271 ? -34.827 19.111  -20.977  1.00 210.06 ? 269  LEU C N   1 
ATOM   8324  C  CA  . LEU C  3 271 ? -35.978 19.406  -20.122  1.00 210.42 ? 269  LEU C CA  1 
ATOM   8325  C  C   . LEU C  3 271 ? -35.908 18.525  -18.880  1.00 223.52 ? 269  LEU C C   1 
ATOM   8326  O  O   . LEU C  3 271 ? -36.080 17.306  -18.974  1.00 244.33 ? 269  LEU C O   1 
ATOM   8327  C  CB  . LEU C  3 271 ? -37.285 19.189  -20.872  1.00 198.05 ? 269  LEU C CB  1 
ATOM   8328  C  CG  . LEU C  3 271 ? -38.546 19.403  -20.030  1.00 194.11 ? 269  LEU C CG  1 
ATOM   8329  C  CD1 . LEU C  3 271 ? -38.589 20.821  -19.491  1.00 202.85 ? 269  LEU C CD1 1 
ATOM   8330  C  CD2 . LEU C  3 271 ? -39.789 19.092  -20.839  1.00 199.12 ? 269  LEU C CD2 1 
ATOM   8331  N  N   . TYR C  3 272 ? -35.658 19.141  -17.730  1.00 211.61 ? 270  TYR C N   1 
ATOM   8332  C  CA  . TYR C  3 272 ? -35.660 18.451  -16.447  1.00 205.95 ? 270  TYR C CA  1 
ATOM   8333  C  C   . TYR C  3 272 ? -37.028 18.627  -15.802  1.00 202.13 ? 270  TYR C C   1 
ATOM   8334  O  O   . TYR C  3 272 ? -37.467 19.758  -15.570  1.00 213.99 ? 270  TYR C O   1 
ATOM   8335  C  CB  . TYR C  3 272 ? -34.561 18.998  -15.538  1.00 221.67 ? 270  TYR C CB  1 
ATOM   8336  C  CG  . TYR C  3 272 ? -34.588 18.449  -14.135  1.00 230.36 ? 270  TYR C CG  1 
ATOM   8337  C  CD1 . TYR C  3 272 ? -34.090 17.185  -13.852  1.00 231.68 ? 270  TYR C CD1 1 
ATOM   8338  C  CD2 . TYR C  3 272 ? -35.109 19.199  -13.089  1.00 243.71 ? 270  TYR C CD2 1 
ATOM   8339  C  CE1 . TYR C  3 272 ? -34.109 16.684  -12.568  1.00 241.73 ? 270  TYR C CE1 1 
ATOM   8340  C  CE2 . TYR C  3 272 ? -35.134 18.707  -11.803  1.00 256.14 ? 270  TYR C CE2 1 
ATOM   8341  C  CZ  . TYR C  3 272 ? -34.633 17.449  -11.547  1.00 259.17 ? 270  TYR C CZ  1 
ATOM   8342  O  OH  . TYR C  3 272 ? -34.655 16.955  -10.264  1.00 277.95 ? 270  TYR C OH  1 
ATOM   8343  N  N   . ILE C  3 273 ? -37.694 17.515  -15.508  1.00 205.97 ? 271  ILE C N   1 
ATOM   8344  C  CA  . ILE C  3 273 ? -39.055 17.526  -14.986  1.00 214.45 ? 271  ILE C CA  1 
ATOM   8345  C  C   . ILE C  3 273 ? -39.004 17.190  -13.502  1.00 230.27 ? 271  ILE C C   1 
ATOM   8346  O  O   . ILE C  3 273 ? -38.584 16.091  -13.123  1.00 243.16 ? 271  ILE C O   1 
ATOM   8347  C  CB  . ILE C  3 273 ? -39.956 16.544  -15.746  1.00 204.14 ? 271  ILE C CB  1 
ATOM   8348  C  CG1 . ILE C  3 273 ? -40.069 16.962  -17.213  1.00 186.05 ? 271  ILE C CG1 1 
ATOM   8349  C  CG2 . ILE C  3 273 ? -41.331 16.467  -15.099  1.00 222.11 ? 271  ILE C CG2 1 
ATOM   8350  C  CD1 . ILE C  3 273 ? -41.023 16.108  -18.016  1.00 179.42 ? 271  ILE C CD1 1 
ATOM   8351  N  N   . ASP C  3 274 ? -39.432 18.134  -12.667  1.00 226.56 ? 272  ASP C N   1 
ATOM   8352  C  CA  . ASP C  3 274 ? -39.524 17.934  -11.228  1.00 222.74 ? 272  ASP C CA  1 
ATOM   8353  C  C   . ASP C  3 274 ? -40.955 17.577  -10.849  1.00 215.80 ? 272  ASP C C   1 
ATOM   8354  O  O   . ASP C  3 274 ? -41.911 18.100  -11.427  1.00 211.51 ? 272  ASP C O   1 
ATOM   8355  C  CB  . ASP C  3 274 ? -39.078 19.188  -10.470  1.00 234.36 ? 272  ASP C CB  1 
ATOM   8356  C  CG  . ASP C  3 274 ? -38.802 18.921  -8.996   1.00 246.95 ? 272  ASP C CG  1 
ATOM   8357  O  OD1 . ASP C  3 274 ? -39.496 18.079  -8.387   1.00 243.87 ? 272  ASP C OD1 1 
ATOM   8358  O  OD2 . ASP C  3 274 ? -37.890 19.566  -8.438   1.00 259.87 ? 272  ASP C OD2 1 
ATOM   8359  N  N   . PHE C  3 275 ? -41.093 16.682  -9.870   1.00 217.52 ? 273  PHE C N   1 
ATOM   8360  C  CA  . PHE C  3 275 ? -42.417 16.278  -9.418   1.00 216.60 ? 273  PHE C CA  1 
ATOM   8361  C  C   . PHE C  3 275 ? -43.016 17.315  -8.480   1.00 222.20 ? 273  PHE C C   1 
ATOM   8362  O  O   . PHE C  3 275 ? -44.215 17.605  -8.552   1.00 218.78 ? 273  PHE C O   1 
ATOM   8363  C  CB  . PHE C  3 275 ? -42.348 14.920  -8.723   1.00 210.34 ? 273  PHE C CB  1 
ATOM   8364  C  CG  . PHE C  3 275 ? -41.902 13.807  -9.618   1.00 197.63 ? 273  PHE C CG  1 
ATOM   8365  C  CD1 . PHE C  3 275 ? -42.815 13.098  -10.377  1.00 184.65 ? 273  PHE C CD1 1 
ATOM   8366  C  CD2 . PHE C  3 275 ? -40.564 13.474  -9.704   1.00 198.95 ? 273  PHE C CD2 1 
ATOM   8367  C  CE1 . PHE C  3 275 ? -42.398 12.072  -11.204  1.00 170.88 ? 273  PHE C CE1 1 
ATOM   8368  C  CE2 . PHE C  3 275 ? -40.143 12.453  -10.527  1.00 185.88 ? 273  PHE C CE2 1 
ATOM   8369  C  CZ  . PHE C  3 275 ? -41.061 11.751  -11.277  1.00 170.81 ? 273  PHE C CZ  1 
ATOM   8370  N  N   . ARG C  3 276 ? -42.197 17.876  -7.592   1.00 227.21 ? 274  ARG C N   1 
ATOM   8371  C  CA  . ARG C  3 276 ? -42.685 18.875  -6.652   1.00 234.34 ? 274  ARG C CA  1 
ATOM   8372  C  C   . ARG C  3 276 ? -42.842 20.242  -7.299   1.00 236.10 ? 274  ARG C C   1 
ATOM   8373  O  O   . ARG C  3 276 ? -43.726 21.010  -6.906   1.00 238.09 ? 274  ARG C O   1 
ATOM   8374  C  CB  . ARG C  3 276 ? -41.736 18.971  -5.455   1.00 247.99 ? 274  ARG C CB  1 
ATOM   8375  C  CG  . ARG C  3 276 ? -41.743 17.749  -4.551   1.00 253.83 ? 274  ARG C CG  1 
ATOM   8376  C  CD  . ARG C  3 276 ? -42.942 17.749  -3.609   1.00 270.65 ? 274  ARG C CD  1 
ATOM   8377  N  NE  . ARG C  3 276 ? -42.816 18.728  -2.529   1.00 283.37 ? 274  ARG C NE  1 
ATOM   8378  C  CZ  . ARG C  3 276 ? -43.403 19.923  -2.518   1.00 284.39 ? 274  ARG C CZ  1 
ATOM   8379  N  NH1 . ARG C  3 276 ? -44.169 20.300  -3.534   1.00 285.44 ? 274  ARG C NH1 1 
ATOM   8380  N  NH2 . ARG C  3 276 ? -43.228 20.741  -1.487   1.00 277.52 ? 274  ARG C NH2 1 
ATOM   8381  N  N   . LYS C  3 277 ? -42.017 20.555  -8.296   1.00 233.47 ? 275  LYS C N   1 
ATOM   8382  C  CA  . LYS C  3 277 ? -41.970 21.888  -8.884   1.00 239.70 ? 275  LYS C CA  1 
ATOM   8383  C  C   . LYS C  3 277 ? -42.824 22.025  -10.135  1.00 240.71 ? 275  LYS C C   1 
ATOM   8384  O  O   . LYS C  3 277 ? -43.529 23.027  -10.291  1.00 240.78 ? 275  LYS C O   1 
ATOM   8385  C  CB  . LYS C  3 277 ? -40.520 22.257  -9.214   1.00 248.26 ? 275  LYS C CB  1 
ATOM   8386  C  CG  . LYS C  3 277 ? -40.356 23.641  -9.802   1.00 257.02 ? 275  LYS C CG  1 
ATOM   8387  C  CD  . LYS C  3 277 ? -40.725 24.708  -8.790   1.00 271.04 ? 275  LYS C CD  1 
ATOM   8388  C  CE  . LYS C  3 277 ? -40.501 26.095  -9.363   1.00 282.65 ? 275  LYS C CE  1 
ATOM   8389  N  NZ  . LYS C  3 277 ? -41.303 26.316  -10.600  1.00 277.51 ? 275  LYS C NZ  1 
ATOM   8390  N  N   . ASP C  3 278 ? -42.780 21.045  -11.033  1.00 235.93 ? 276  ASP C N   1 
ATOM   8391  C  CA  . ASP C  3 278 ? -43.460 21.132  -12.315  1.00 234.59 ? 276  ASP C CA  1 
ATOM   8392  C  C   . ASP C  3 278 ? -44.718 20.275  -12.383  1.00 231.43 ? 276  ASP C C   1 
ATOM   8393  O  O   . ASP C  3 278 ? -45.414 20.297  -13.404  1.00 222.40 ? 276  ASP C O   1 
ATOM   8394  C  CB  . ASP C  3 278 ? -42.494 20.741  -13.440  1.00 223.63 ? 276  ASP C CB  1 
ATOM   8395  C  CG  . ASP C  3 278 ? -41.234 21.593  -13.443  1.00 225.77 ? 276  ASP C CG  1 
ATOM   8396  O  OD1 . ASP C  3 278 ? -41.307 22.778  -13.048  1.00 232.56 ? 276  ASP C OD1 1 
ATOM   8397  O  OD2 . ASP C  3 278 ? -40.167 21.077  -13.835  1.00 224.78 ? 276  ASP C OD2 1 
ATOM   8398  N  N   . LEU C  3 279 ? -45.019 19.512  -11.332  1.00 227.72 ? 277  LEU C N   1 
ATOM   8399  C  CA  . LEU C  3 279 ? -46.201 18.659  -11.312  1.00 217.76 ? 277  LEU C CA  1 
ATOM   8400  C  C   . LEU C  3 279 ? -46.934 18.774  -9.981   1.00 210.43 ? 277  LEU C C   1 
ATOM   8401  O  O   . LEU C  3 279 ? -48.159 18.617  -9.922   1.00 205.64 ? 277  LEU C O   1 
ATOM   8402  C  CB  . LEU C  3 279 ? -45.815 17.205  -11.586  1.00 211.37 ? 277  LEU C CB  1 
ATOM   8403  C  CG  . LEU C  3 279 ? -45.415 16.859  -13.025  1.00 195.42 ? 277  LEU C CG  1 
ATOM   8404  C  CD1 . LEU C  3 279 ? -44.999 15.399  -13.141  1.00 188.03 ? 277  LEU C CD1 1 
ATOM   8405  C  CD2 . LEU C  3 279 ? -46.548 17.168  -13.991  1.00 188.03 ? 277  LEU C CD2 1 
ATOM   8406  N  N   . GLY C  3 280 ? -46.195 19.033  -8.908   1.00 205.54 ? 278  GLY C N   1 
ATOM   8407  C  CA  . GLY C  3 280 ? -46.805 19.089  -7.594   1.00 212.41 ? 278  GLY C CA  1 
ATOM   8408  C  C   . GLY C  3 280 ? -47.172 17.717  -7.080   1.00 219.79 ? 278  GLY C C   1 
ATOM   8409  O  O   . GLY C  3 280 ? -48.265 17.538  -6.528   1.00 235.35 ? 278  GLY C O   1 
ATOM   8410  N  N   . TRP C  3 281 ? -46.292 16.736  -7.266   1.00 217.23 ? 279  TRP C N   1 
ATOM   8411  C  CA  . TRP C  3 281 ? -46.530 15.360  -6.841   1.00 212.98 ? 279  TRP C CA  1 
ATOM   8412  C  C   . TRP C  3 281 ? -45.515 14.983  -5.770   1.00 222.05 ? 279  TRP C C   1 
ATOM   8413  O  O   . TRP C  3 281 ? -44.329 14.799  -6.069   1.00 224.74 ? 279  TRP C O   1 
ATOM   8414  C  CB  . TRP C  3 281 ? -46.441 14.398  -8.020   1.00 201.15 ? 279  TRP C CB  1 
ATOM   8415  C  CG  . TRP C  3 281 ? -47.546 14.532  -9.002   1.00 193.99 ? 279  TRP C CG  1 
ATOM   8416  C  CD1 . TRP C  3 281 ? -48.587 15.416  -8.960   1.00 193.74 ? 279  TRP C CD1 1 
ATOM   8417  C  CD2 . TRP C  3 281 ? -47.724 13.755  -10.187  1.00 190.84 ? 279  TRP C CD2 1 
ATOM   8418  N  NE1 . TRP C  3 281 ? -49.403 15.233  -10.051  1.00 201.73 ? 279  TRP C NE1 1 
ATOM   8419  C  CE2 . TRP C  3 281 ? -48.894 14.219  -10.819  1.00 209.59 ? 279  TRP C CE2 1 
ATOM   8420  C  CE3 . TRP C  3 281 ? -47.005 12.709  -10.776  1.00 170.28 ? 279  TRP C CE3 1 
ATOM   8421  C  CZ2 . TRP C  3 281 ? -49.361 13.672  -12.012  1.00 211.33 ? 279  TRP C CZ2 1 
ATOM   8422  C  CZ3 . TRP C  3 281 ? -47.469 12.167  -11.959  1.00 162.53 ? 279  TRP C CZ3 1 
ATOM   8423  C  CH2 . TRP C  3 281 ? -48.636 12.649  -12.565  1.00 187.33 ? 279  TRP C CH2 1 
ATOM   8424  N  N   . LYS C  3 282 ? -45.980 14.855  -4.530   1.00 248.82 ? 280  LYS C N   1 
ATOM   8425  C  CA  . LYS C  3 282 ? -45.142 14.429  -3.417   1.00 253.66 ? 280  LYS C CA  1 
ATOM   8426  C  C   . LYS C  3 282 ? -45.380 12.968  -3.057   1.00 256.20 ? 280  LYS C C   1 
ATOM   8427  O  O   . LYS C  3 282 ? -44.893 12.499  -2.023   1.00 257.14 ? 280  LYS C O   1 
ATOM   8428  C  CB  . LYS C  3 282 ? -45.380 15.333  -2.200   1.00 257.43 ? 280  LYS C CB  1 
ATOM   8429  C  CG  . LYS C  3 282 ? -44.227 15.368  -1.193   1.00 255.76 ? 280  LYS C CG  1 
ATOM   8430  C  CD  . LYS C  3 282 ? -44.418 16.467  -0.156   1.00 254.67 ? 280  LYS C CD  1 
ATOM   8431  C  CE  . LYS C  3 282 ? -45.686 16.263  0.657    1.00 249.43 ? 280  LYS C CE  1 
ATOM   8432  N  NZ  . LYS C  3 282 ? -45.849 17.328  1.687    1.00 255.63 ? 280  LYS C NZ  1 
ATOM   8433  N  N   . TRP C  3 283 ? -46.118 12.241  -3.891   1.00 244.57 ? 281  TRP C N   1 
ATOM   8434  C  CA  . TRP C  3 283 ? -46.419 10.837  -3.659   1.00 238.46 ? 281  TRP C CA  1 
ATOM   8435  C  C   . TRP C  3 283 ? -45.427 9.897   -4.331   1.00 234.57 ? 281  TRP C C   1 
ATOM   8436  O  O   . TRP C  3 283 ? -45.547 8.677   -4.174   1.00 239.69 ? 281  TRP C O   1 
ATOM   8437  C  CB  . TRP C  3 283 ? -47.838 10.526  -4.143   1.00 232.63 ? 281  TRP C CB  1 
ATOM   8438  C  CG  . TRP C  3 283 ? -48.021 10.747  -5.610   1.00 222.20 ? 281  TRP C CG  1 
ATOM   8439  C  CD1 . TRP C  3 283 ? -48.266 11.934  -6.235   1.00 222.16 ? 281  TRP C CD1 1 
ATOM   8440  C  CD2 . TRP C  3 283 ? -47.985 9.751   -6.638   1.00 204.80 ? 281  TRP C CD2 1 
ATOM   8441  N  NE1 . TRP C  3 283 ? -48.378 11.739  -7.591   1.00 217.02 ? 281  TRP C NE1 1 
ATOM   8442  C  CE2 . TRP C  3 283 ? -48.210 10.407  -7.864   1.00 205.02 ? 281  TRP C CE2 1 
ATOM   8443  C  CE3 . TRP C  3 283 ? -47.782 8.367   -6.640   1.00 198.13 ? 281  TRP C CE3 1 
ATOM   8444  C  CZ2 . TRP C  3 283 ? -48.237 9.728   -9.080   1.00 192.74 ? 281  TRP C CZ2 1 
ATOM   8445  C  CZ3 . TRP C  3 283 ? -47.810 7.695   -7.847   1.00 198.31 ? 281  TRP C CZ3 1 
ATOM   8446  C  CH2 . TRP C  3 283 ? -48.037 8.376   -9.051   1.00 191.09 ? 281  TRP C CH2 1 
ATOM   8447  N  N   . ILE C  3 284 ? -44.450 10.427  -5.063   1.00 210.41 ? 282  ILE C N   1 
ATOM   8448  C  CA  . ILE C  3 284 ? -43.410 9.628   -5.702   1.00 195.35 ? 282  ILE C CA  1 
ATOM   8449  C  C   . ILE C  3 284 ? -42.113 9.903   -4.963   1.00 200.69 ? 282  ILE C C   1 
ATOM   8450  O  O   . ILE C  3 284 ? -41.569 11.013  -5.033   1.00 206.66 ? 282  ILE C O   1 
ATOM   8451  C  CB  . ILE C  3 284 ? -43.267 9.947   -7.193   1.00 183.92 ? 282  ILE C CB  1 
ATOM   8452  C  CG1 . ILE C  3 284 ? -44.560 9.612   -7.928   1.00 182.34 ? 282  ILE C CG1 1 
ATOM   8453  C  CG2 . ILE C  3 284 ? -42.093 9.183   -7.784   1.00 173.46 ? 282  ILE C CG2 1 
ATOM   8454  C  CD1 . ILE C  3 284 ? -44.486 9.872   -9.412   1.00 198.21 ? 282  ILE C CD1 1 
ATOM   8455  N  N   . HIS C  3 285 ? -41.604 8.887   -4.267   1.00 205.34 ? 283  HIS C N   1 
ATOM   8456  C  CA  . HIS C  3 285 ? -40.407 9.083   -3.460   1.00 220.44 ? 283  HIS C CA  1 
ATOM   8457  C  C   . HIS C  3 285 ? -39.173 9.191   -4.342   1.00 211.99 ? 283  HIS C C   1 
ATOM   8458  O  O   . HIS C  3 285 ? -38.416 10.164  -4.252   1.00 223.09 ? 283  HIS C O   1 
ATOM   8459  C  CB  . HIS C  3 285 ? -40.258 7.943   -2.454   1.00 239.58 ? 283  HIS C CB  1 
ATOM   8460  C  CG  . HIS C  3 285 ? -41.339 7.908   -1.419   1.00 245.60 ? 283  HIS C CG  1 
ATOM   8461  N  ND1 . HIS C  3 285 ? -42.675 7.823   -1.744   1.00 238.77 ? 283  HIS C ND1 1 
ATOM   8462  C  CD2 . HIS C  3 285 ? -41.281 7.952   -0.067   1.00 251.56 ? 283  HIS C CD2 1 
ATOM   8463  C  CE1 . HIS C  3 285 ? -43.395 7.816   -0.636   1.00 244.52 ? 283  HIS C CE1 1 
ATOM   8464  N  NE2 . HIS C  3 285 ? -42.573 7.892   0.396    1.00 255.84 ? 283  HIS C NE2 1 
ATOM   8465  N  N   . GLU C  3 286 ? -38.963 8.211   -5.211   1.00 204.07 ? 284  GLU C N   1 
ATOM   8466  C  CA  . GLU C  3 286 ? -37.810 8.228   -6.098   1.00 204.29 ? 284  GLU C CA  1 
ATOM   8467  C  C   . GLU C  3 286 ? -38.178 7.891   -7.529   1.00 198.22 ? 284  GLU C C   1 
ATOM   8468  O  O   . GLU C  3 286 ? -38.931 6.950   -7.778   1.00 207.21 ? 284  GLU C O   1 
ATOM   8469  C  CB  . GLU C  3 286 ? -36.728 7.267   -5.607   1.00 214.67 ? 284  GLU C CB  1 
ATOM   8470  C  CG  . GLU C  3 286 ? -36.130 7.654   -4.270   1.00 223.52 ? 284  GLU C CG  1 
ATOM   8471  C  CD  . GLU C  3 286 ? -35.353 8.956   -4.339   1.00 215.21 ? 284  GLU C CD  1 
ATOM   8472  O  OE1 . GLU C  3 286 ? -34.897 9.323   -5.446   1.00 203.86 ? 284  GLU C OE1 1 
ATOM   8473  O  OE2 . GLU C  3 286 ? -35.208 9.614   -3.286   1.00 221.60 ? 284  GLU C OE2 1 
ATOM   8474  N  N   . PRO C  3 287 ? -37.656 8.683   -8.475   1.00 193.32 ? 285  PRO C N   1 
ATOM   8475  C  CA  . PRO C  3 287 ? -36.837 9.858   -8.159   1.00 195.47 ? 285  PRO C CA  1 
ATOM   8476  C  C   . PRO C  3 287 ? -37.697 11.087  -7.892   1.00 210.74 ? 285  PRO C C   1 
ATOM   8477  O  O   . PRO C  3 287 ? -38.924 11.003  -7.956   1.00 224.42 ? 285  PRO C O   1 
ATOM   8478  C  CB  . PRO C  3 287 ? -35.996 10.042  -9.417   1.00 195.79 ? 285  PRO C CB  1 
ATOM   8479  C  CG  . PRO C  3 287 ? -36.890 9.559   -10.510  1.00 200.70 ? 285  PRO C CG  1 
ATOM   8480  C  CD  . PRO C  3 287 ? -37.703 8.424   -9.925   1.00 203.13 ? 285  PRO C CD  1 
ATOM   8481  N  N   . LYS C  3 288 ? -37.057 12.212  -7.579   1.00 211.60 ? 286  LYS C N   1 
ATOM   8482  C  CA  . LYS C  3 288 ? -37.751 13.476  -7.371   1.00 221.57 ? 286  LYS C CA  1 
ATOM   8483  C  C   . LYS C  3 288 ? -37.475 14.451  -8.511   1.00 238.71 ? 286  LYS C C   1 
ATOM   8484  O  O   . LYS C  3 288 ? -37.480 15.669  -8.314   1.00 247.06 ? 286  LYS C O   1 
ATOM   8485  C  CB  . LYS C  3 288 ? -37.363 14.091  -6.028   1.00 229.97 ? 286  LYS C CB  1 
ATOM   8486  C  CG  . LYS C  3 288 ? -37.722 13.225  -4.831   1.00 235.46 ? 286  LYS C CG  1 
ATOM   8487  C  CD  . LYS C  3 288 ? -37.123 13.755  -3.538   1.00 235.63 ? 286  LYS C CD  1 
ATOM   8488  C  CE  . LYS C  3 288 ? -37.401 12.805  -2.383   1.00 228.05 ? 286  LYS C CE  1 
ATOM   8489  N  NZ  . LYS C  3 288 ? -36.775 13.267  -1.114   1.00 233.95 ? 286  LYS C NZ  1 
ATOM   8490  N  N   . GLY C  3 289 ? -37.238 13.918  -9.707   1.00 240.24 ? 287  GLY C N   1 
ATOM   8491  C  CA  . GLY C  3 289 ? -36.922 14.714  -10.874  1.00 234.92 ? 287  GLY C CA  1 
ATOM   8492  C  C   . GLY C  3 289 ? -36.045 13.944  -11.839  1.00 225.65 ? 287  GLY C C   1 
ATOM   8493  O  O   . GLY C  3 289 ? -35.189 13.169  -11.404  1.00 229.20 ? 287  GLY C O   1 
ATOM   8494  N  N   . TYR C  3 290 ? -36.246 14.129  -13.143  1.00 228.53 ? 288  TYR C N   1 
ATOM   8495  C  CA  . TYR C  3 290 ? -35.467 13.396  -14.133  1.00 220.53 ? 288  TYR C CA  1 
ATOM   8496  C  C   . TYR C  3 290 ? -35.467 14.169  -15.448  1.00 218.36 ? 288  TYR C C   1 
ATOM   8497  O  O   . TYR C  3 290 ? -36.212 15.137  -15.626  1.00 215.19 ? 288  TYR C O   1 
ATOM   8498  C  CB  . TYR C  3 290 ? -36.016 11.980  -14.321  1.00 215.09 ? 288  TYR C CB  1 
ATOM   8499  C  CG  . TYR C  3 290 ? -37.287 11.926  -15.134  1.00 202.47 ? 288  TYR C CG  1 
ATOM   8500  C  CD1 . TYR C  3 290 ? -38.472 12.463  -14.644  1.00 198.79 ? 288  TYR C CD1 1 
ATOM   8501  C  CD2 . TYR C  3 290 ? -37.308 11.322  -16.383  1.00 190.00 ? 288  TYR C CD2 1 
ATOM   8502  C  CE1 . TYR C  3 290 ? -39.636 12.417  -15.382  1.00 184.48 ? 288  TYR C CE1 1 
ATOM   8503  C  CE2 . TYR C  3 290 ? -38.468 11.265  -17.125  1.00 190.93 ? 288  TYR C CE2 1 
ATOM   8504  C  CZ  . TYR C  3 290 ? -39.629 11.815  -16.620  1.00 195.10 ? 288  TYR C CZ  1 
ATOM   8505  O  OH  . TYR C  3 290 ? -40.788 11.765  -17.354  1.00 220.19 ? 288  TYR C OH  1 
ATOM   8506  N  N   . HIS C  3 291 ? -34.618 13.719  -16.376  1.00 204.42 ? 289  HIS C N   1 
ATOM   8507  C  CA  . HIS C  3 291 ? -34.451 14.357  -17.685  1.00 204.03 ? 289  HIS C CA  1 
ATOM   8508  C  C   . HIS C  3 291 ? -35.264 13.597  -18.732  1.00 207.39 ? 289  HIS C C   1 
ATOM   8509  O  O   . HIS C  3 291 ? -34.780 12.651  -19.352  1.00 208.70 ? 289  HIS C O   1 
ATOM   8510  C  CB  . HIS C  3 291 ? -32.977 14.418  -18.073  1.00 208.88 ? 289  HIS C CB  1 
ATOM   8511  C  CG  . HIS C  3 291 ? -32.173 15.376  -17.250  1.00 233.26 ? 289  HIS C CG  1 
ATOM   8512  N  ND1 . HIS C  3 291 ? -31.945 15.193  -15.902  1.00 251.41 ? 289  HIS C ND1 1 
ATOM   8513  C  CD2 . HIS C  3 291 ? -31.537 16.524  -17.585  1.00 241.64 ? 289  HIS C CD2 1 
ATOM   8514  C  CE1 . HIS C  3 291 ? -31.206 16.187  -15.442  1.00 255.12 ? 289  HIS C CE1 1 
ATOM   8515  N  NE2 . HIS C  3 291 ? -30.944 17.008  -16.443  1.00 254.77 ? 289  HIS C NE2 1 
ATOM   8516  N  N   . ALA C  3 292 ? -36.516 14.021  -18.932  1.00 206.54 ? 290  ALA C N   1 
ATOM   8517  C  CA  . ALA C  3 292 ? -37.346 13.415  -19.969  1.00 188.44 ? 290  ALA C CA  1 
ATOM   8518  C  C   . ALA C  3 292 ? -37.038 13.997  -21.343  1.00 188.58 ? 290  ALA C C   1 
ATOM   8519  O  O   . ALA C  3 292 ? -37.037 13.268  -22.341  1.00 200.10 ? 290  ALA C O   1 
ATOM   8520  C  CB  . ALA C  3 292 ? -38.826 13.596  -19.638  1.00 192.61 ? 290  ALA C CB  1 
ATOM   8521  N  N   . ASN C  3 293 ? -36.802 15.309  -21.413  1.00 193.20 ? 291  ASN C N   1 
ATOM   8522  C  CA  . ASN C  3 293 ? -36.503 16.014  -22.658  1.00 205.13 ? 291  ASN C CA  1 
ATOM   8523  C  C   . ASN C  3 293 ? -37.655 15.929  -23.652  1.00 196.31 ? 291  ASN C C   1 
ATOM   8524  O  O   . ASN C  3 293 ? -38.722 15.388  -23.338  1.00 182.85 ? 291  ASN C O   1 
ATOM   8525  C  CB  . ASN C  3 293 ? -35.216 15.480  -23.299  1.00 208.77 ? 291  ASN C CB  1 
ATOM   8526  C  CG  . ASN C  3 293 ? -34.000 15.678  -22.417  1.00 210.65 ? 291  ASN C CG  1 
ATOM   8527  O  OD1 . ASN C  3 293 ? -34.049 16.406  -21.426  1.00 214.08 ? 291  ASN C OD1 1 
ATOM   8528  N  ND2 . ASN C  3 293 ? -32.896 15.037  -22.779  1.00 211.61 ? 291  ASN C ND2 1 
ATOM   8529  N  N   . PHE C  3 294 ? -37.448 16.475  -24.850  1.00 195.15 ? 292  PHE C N   1 
ATOM   8530  C  CA  . PHE C  3 294 ? -38.456 16.459  -25.902  1.00 194.26 ? 292  PHE C CA  1 
ATOM   8531  C  C   . PHE C  3 294 ? -37.780 16.783  -27.229  1.00 193.10 ? 292  PHE C C   1 
ATOM   8532  O  O   . PHE C  3 294 ? -36.640 17.255  -27.269  1.00 190.06 ? 292  PHE C O   1 
ATOM   8533  C  CB  . PHE C  3 294 ? -39.583 17.450  -25.607  1.00 185.06 ? 292  PHE C CB  1 
ATOM   8534  C  CG  . PHE C  3 294 ? -39.117 18.869  -25.498  1.00 188.44 ? 292  PHE C CG  1 
ATOM   8535  C  CD1 . PHE C  3 294 ? -38.603 19.350  -24.305  1.00 194.11 ? 292  PHE C CD1 1 
ATOM   8536  C  CD2 . PHE C  3 294 ? -39.194 19.725  -26.584  1.00 198.40 ? 292  PHE C CD2 1 
ATOM   8537  C  CE1 . PHE C  3 294 ? -38.172 20.655  -24.195  1.00 207.60 ? 292  PHE C CE1 1 
ATOM   8538  C  CE2 . PHE C  3 294 ? -38.766 21.035  -26.482  1.00 212.96 ? 292  PHE C CE2 1 
ATOM   8539  C  CZ  . PHE C  3 294 ? -38.255 21.501  -25.283  1.00 217.60 ? 292  PHE C CZ  1 
ATOM   8540  N  N   . CYS C  3 295 ? -38.517 16.559  -28.319  1.00 187.31 ? 293  CYS C N   1 
ATOM   8541  C  CA  . CYS C  3 295 ? -38.044 16.836  -29.673  1.00 191.38 ? 293  CYS C CA  1 
ATOM   8542  C  C   . CYS C  3 295 ? -38.765 18.061  -30.212  1.00 211.10 ? 293  CYS C C   1 
ATOM   8543  O  O   . CYS C  3 295 ? -39.999 18.087  -30.260  1.00 225.73 ? 293  CYS C O   1 
ATOM   8544  C  CB  . CYS C  3 295 ? -38.278 15.653  -30.611  1.00 195.24 ? 293  CYS C CB  1 
ATOM   8545  S  SG  . CYS C  3 295 ? -37.545 14.094  -30.107  1.00 230.23 ? 293  CYS C SG  1 
ATOM   8546  N  N   . LEU C  3 296 ? -37.998 19.074  -30.602  1.00 228.14 ? 294  LEU C N   1 
ATOM   8547  C  CA  . LEU C  3 296 ? -38.538 20.288  -31.196  1.00 231.60 ? 294  LEU C CA  1 
ATOM   8548  C  C   . LEU C  3 296 ? -37.674 20.672  -32.388  1.00 227.53 ? 294  LEU C C   1 
ATOM   8549  O  O   . LEU C  3 296 ? -36.447 20.753  -32.267  1.00 226.60 ? 294  LEU C O   1 
ATOM   8550  C  CB  . LEU C  3 296 ? -38.589 21.422  -30.164  1.00 227.89 ? 294  LEU C CB  1 
ATOM   8551  C  CG  . LEU C  3 296 ? -39.592 22.563  -30.357  1.00 227.16 ? 294  LEU C CG  1 
ATOM   8552  C  CD1 . LEU C  3 296 ? -39.087 23.591  -31.361  1.00 239.50 ? 294  LEU C CD1 1 
ATOM   8553  C  CD2 . LEU C  3 296 ? -40.949 22.015  -30.779  1.00 221.91 ? 294  LEU C CD2 1 
ATOM   8554  N  N   . GLY C  3 297 ? -38.308 20.902  -33.535  1.00 219.42 ? 295  GLY C N   1 
ATOM   8555  C  CA  . GLY C  3 297 ? -37.582 21.289  -34.719  1.00 220.35 ? 295  GLY C CA  1 
ATOM   8556  C  C   . GLY C  3 297 ? -38.278 20.927  -36.014  1.00 227.18 ? 295  GLY C C   1 
ATOM   8557  O  O   . GLY C  3 297 ? -39.116 20.021  -36.069  1.00 233.34 ? 295  GLY C O   1 
ATOM   8558  N  N   . PRO C  3 298 ? -37.952 21.649  -37.082  1.00 236.95 ? 296  PRO C N   1 
ATOM   8559  C  CA  . PRO C  3 298 ? -38.527 21.359  -38.396  1.00 242.88 ? 296  PRO C CA  1 
ATOM   8560  C  C   . PRO C  3 298 ? -37.753 20.275  -39.132  1.00 235.10 ? 296  PRO C C   1 
ATOM   8561  O  O   . PRO C  3 298 ? -36.579 20.010  -38.861  1.00 235.13 ? 296  PRO C O   1 
ATOM   8562  C  CB  . PRO C  3 298 ? -38.401 22.705  -39.125  1.00 251.79 ? 296  PRO C CB  1 
ATOM   8563  C  CG  . PRO C  3 298 ? -37.173 23.317  -38.533  1.00 245.84 ? 296  PRO C CG  1 
ATOM   8564  C  CD  . PRO C  3 298 ? -37.135 22.874  -37.089  1.00 235.03 ? 296  PRO C CD  1 
ATOM   8565  N  N   . CYS C  3 299 ? -38.438 19.655  -40.094  1.00 238.68 ? 297  CYS C N   1 
ATOM   8566  C  CA  . CYS C  3 299 ? -37.845 18.596  -40.912  1.00 250.30 ? 297  CYS C CA  1 
ATOM   8567  C  C   . CYS C  3 299 ? -38.231 18.817  -42.370  1.00 270.04 ? 297  CYS C C   1 
ATOM   8568  O  O   . CYS C  3 299 ? -39.257 18.306  -42.840  1.00 277.57 ? 297  CYS C O   1 
ATOM   8569  C  CB  . CYS C  3 299 ? -38.291 17.209  -40.443  1.00 246.98 ? 297  CYS C CB  1 
ATOM   8570  S  SG  . CYS C  3 299 ? -37.922 16.820  -38.713  1.00 229.74 ? 297  CYS C SG  1 
ATOM   8571  N  N   . PRO C  3 300 ? -37.424 19.592  -43.128  1.00 291.28 ? 298  PRO C N   1 
ATOM   8572  C  CA  . PRO C  3 300 ? -37.738 19.821  -44.546  1.00 293.55 ? 298  PRO C CA  1 
ATOM   8573  C  C   . PRO C  3 300 ? -37.050 18.843  -45.486  1.00 292.55 ? 298  PRO C C   1 
ATOM   8574  O  O   . PRO C  3 300 ? -36.255 18.000  -45.050  1.00 293.22 ? 298  PRO C O   1 
ATOM   8575  C  CB  . PRO C  3 300 ? -37.260 21.263  -44.775  1.00 292.01 ? 298  PRO C CB  1 
ATOM   8576  C  CG  . PRO C  3 300 ? -36.204 21.513  -43.703  1.00 290.74 ? 298  PRO C CG  1 
ATOM   8577  C  CD  . PRO C  3 300 ? -36.228 20.351  -42.721  1.00 288.42 ? 298  PRO C CD  1 
ATOM   8578  N  N   . TYR C  3 301 ? -37.353 18.931  -46.779  1.00 290.51 ? 299  TYR C N   1 
ATOM   8579  C  CA  . TYR C  3 301 ? -36.760 18.029  -47.769  1.00 296.46 ? 299  TYR C CA  1 
ATOM   8580  C  C   . TYR C  3 301 ? -35.307 18.407  -48.061  1.00 300.64 ? 299  TYR C C   1 
ATOM   8581  O  O   . TYR C  3 301 ? -34.837 18.304  -49.196  1.00 305.94 ? 299  TYR C O   1 
ATOM   8582  C  CB  . TYR C  3 301 ? -37.579 18.028  -49.064  1.00 301.51 ? 299  TYR C CB  1 
ATOM   8583  C  CG  . TYR C  3 301 ? -39.062 17.846  -48.836  1.00 298.88 ? 299  TYR C CG  1 
ATOM   8584  C  CD1 . TYR C  3 301 ? -39.594 16.588  -48.583  1.00 293.82 ? 299  TYR C CD1 1 
ATOM   8585  C  CD2 . TYR C  3 301 ? -39.928 18.929  -48.869  1.00 303.33 ? 299  TYR C CD2 1 
ATOM   8586  C  CE1 . TYR C  3 301 ? -40.946 16.415  -48.364  1.00 298.42 ? 299  TYR C CE1 1 
ATOM   8587  C  CE2 . TYR C  3 301 ? -41.283 18.768  -48.653  1.00 311.08 ? 299  TYR C CE2 1 
ATOM   8588  C  CZ  . TYR C  3 301 ? -41.787 17.507  -48.400  1.00 308.09 ? 299  TYR C CZ  1 
ATOM   8589  O  OH  . TYR C  3 301 ? -43.135 17.330  -48.183  1.00 319.62 ? 299  TYR C OH  1 
ATOM   8590  N  N   . PRO C  3 321 ? -38.865 11.039  -45.719  1.00 242.12 ? 319  PRO C N   1 
ATOM   8591  C  CA  . PRO C  3 321 ? -39.696 12.030  -46.393  1.00 247.41 ? 319  PRO C CA  1 
ATOM   8592  C  C   . PRO C  3 321 ? -40.894 11.368  -47.065  1.00 248.93 ? 319  PRO C C   1 
ATOM   8593  O  O   . PRO C  3 321 ? -40.926 11.208  -48.285  1.00 250.61 ? 319  PRO C O   1 
ATOM   8594  C  CB  . PRO C  3 321 ? -38.876 12.807  -47.412  1.00 254.97 ? 319  PRO C CB  1 
ATOM   8595  N  N   . GLY C  3 322 ? -41.877 10.987  -46.262  1.00 259.12 ? 320  GLY C N   1 
ATOM   8596  C  CA  . GLY C  3 322 ? -43.061 10.346  -46.797  1.00 264.06 ? 320  GLY C CA  1 
ATOM   8597  C  C   . GLY C  3 322 ? -43.994 9.933   -45.681  1.00 266.42 ? 320  GLY C C   1 
ATOM   8598  O  O   . GLY C  3 322 ? -43.864 10.381  -44.538  1.00 260.25 ? 320  GLY C O   1 
ATOM   8599  N  N   . ALA C  3 323 ? -44.951 9.071   -46.042  1.00 271.67 ? 321  ALA C N   1 
ATOM   8600  C  CA  . ALA C  3 323 ? -45.929 8.503   -45.116  1.00 278.30 ? 321  ALA C CA  1 
ATOM   8601  C  C   . ALA C  3 323 ? -46.880 9.553   -44.549  1.00 280.00 ? 321  ALA C C   1 
ATOM   8602  O  O   . ALA C  3 323 ? -48.088 9.500   -44.806  1.00 290.14 ? 321  ALA C O   1 
ATOM   8603  C  CB  . ALA C  3 323 ? -45.229 7.768   -43.972  1.00 269.91 ? 321  ALA C CB  1 
ATOM   8604  N  N   . SER C  3 324 ? -46.360 10.494  -43.767  1.00 273.92 ? 322  SER C N   1 
ATOM   8605  C  CA  . SER C  3 324 ? -47.175 11.556  -43.195  1.00 272.10 ? 322  SER C CA  1 
ATOM   8606  C  C   . SER C  3 324 ? -47.232 12.762  -44.129  1.00 277.31 ? 322  SER C C   1 
ATOM   8607  O  O   . SER C  3 324 ? -46.314 13.009  -44.916  1.00 281.88 ? 322  SER C O   1 
ATOM   8608  C  CB  . SER C  3 324 ? -46.621 11.983  -41.835  1.00 251.49 ? 322  SER C CB  1 
ATOM   8609  O  OG  . SER C  3 324 ? -45.341 12.575  -41.980  1.00 246.03 ? 322  SER C OG  1 
ATOM   8610  N  N   . ALA C  3 325 ? -48.328 13.521  -44.029  1.00 265.73 ? 323  ALA C N   1 
ATOM   8611  C  CA  . ALA C  3 325 ? -48.482 14.727  -44.837  1.00 260.74 ? 323  ALA C CA  1 
ATOM   8612  C  C   . ALA C  3 325 ? -47.450 15.795  -44.496  1.00 257.02 ? 323  ALA C C   1 
ATOM   8613  O  O   . ALA C  3 325 ? -47.146 16.642  -45.343  1.00 259.12 ? 323  ALA C O   1 
ATOM   8614  C  CB  . ALA C  3 325 ? -49.889 15.298  -44.663  1.00 259.93 ? 323  ALA C CB  1 
ATOM   8615  N  N   . ALA C  3 326 ? -46.910 15.773  -43.284  1.00 262.67 ? 324  ALA C N   1 
ATOM   8616  C  CA  . ALA C  3 326 ? -45.927 16.746  -42.829  1.00 267.31 ? 324  ALA C CA  1 
ATOM   8617  C  C   . ALA C  3 326 ? -44.895 16.045  -41.953  1.00 258.45 ? 324  ALA C C   1 
ATOM   8618  O  O   . ALA C  3 326 ? -45.212 15.662  -40.818  1.00 250.49 ? 324  ALA C O   1 
ATOM   8619  C  CB  . ALA C  3 326 ? -46.604 17.886  -42.067  1.00 268.16 ? 324  ALA C CB  1 
ATOM   8620  N  N   . PRO C  3 327 ? -43.671 15.835  -42.441  1.00 251.24 ? 325  PRO C N   1 
ATOM   8621  C  CA  . PRO C  3 327 ? -42.656 15.138  -41.631  1.00 241.31 ? 325  PRO C CA  1 
ATOM   8622  C  C   . PRO C  3 327 ? -42.371 15.885  -40.336  1.00 236.90 ? 325  PRO C C   1 
ATOM   8623  O  O   . PRO C  3 327 ? -42.027 17.069  -40.338  1.00 233.96 ? 325  PRO C O   1 
ATOM   8624  C  CB  . PRO C  3 327 ? -41.432 15.099  -42.554  1.00 243.94 ? 325  PRO C CB  1 
ATOM   8625  C  CG  . PRO C  3 327 ? -41.986 15.257  -43.935  1.00 257.45 ? 325  PRO C CG  1 
ATOM   8626  C  CD  . PRO C  3 327 ? -43.164 16.177  -43.782  1.00 263.07 ? 325  PRO C CD  1 
ATOM   8627  N  N   . CYS C  3 328 ? -42.516 15.172  -39.222  1.00 228.63 ? 326  CYS C N   1 
ATOM   8628  C  CA  . CYS C  3 328 ? -42.395 15.729  -37.883  1.00 216.88 ? 326  CYS C CA  1 
ATOM   8629  C  C   . CYS C  3 328 ? -41.094 15.307  -37.215  1.00 213.64 ? 326  CYS C C   1 
ATOM   8630  O  O   . CYS C  3 328 ? -40.446 14.328  -37.603  1.00 216.87 ? 326  CYS C O   1 
ATOM   8631  C  CB  . CYS C  3 328 ? -43.571 15.299  -36.997  1.00 221.55 ? 326  CYS C CB  1 
ATOM   8632  S  SG  . CYS C  3 328 ? -45.193 15.952  -37.459  1.00 250.91 ? 326  CYS C SG  1 
ATOM   8633  N  N   . CYS C  3 329 ? -40.717 16.093  -36.207  1.00 218.03 ? 327  CYS C N   1 
ATOM   8634  C  CA  . CYS C  3 329 ? -39.557 15.858  -35.348  1.00 226.55 ? 327  CYS C CA  1 
ATOM   8635  C  C   . CYS C  3 329 ? -39.964 14.912  -34.221  1.00 222.64 ? 327  CYS C C   1 
ATOM   8636  O  O   . CYS C  3 329 ? -40.370 15.335  -33.136  1.00 223.39 ? 327  CYS C O   1 
ATOM   8637  C  CB  . CYS C  3 329 ? -39.039 17.181  -34.802  1.00 227.39 ? 327  CYS C CB  1 
ATOM   8638  S  SG  . CYS C  3 329 ? -37.533 17.104  -33.818  1.00 241.08 ? 327  CYS C SG  1 
ATOM   8639  N  N   . VAL C  3 330 ? -39.853 13.612  -34.475  1.00 227.17 ? 328  VAL C N   1 
ATOM   8640  C  CA  . VAL C  3 330 ? -40.276 12.606  -33.502  1.00 216.20 ? 328  VAL C CA  1 
ATOM   8641  C  C   . VAL C  3 330 ? -39.058 11.939  -32.873  1.00 195.68 ? 328  VAL C C   1 
ATOM   8642  O  O   . VAL C  3 330 ? -37.996 11.857  -33.506  1.00 200.97 ? 328  VAL C O   1 
ATOM   8643  C  CB  . VAL C  3 330 ? -41.206 11.568  -34.150  1.00 223.68 ? 328  VAL C CB  1 
ATOM   8644  C  CG1 . VAL C  3 330 ? -42.496 12.231  -34.605  1.00 232.56 ? 328  VAL C CG1 1 
ATOM   8645  C  CG2 . VAL C  3 330 ? -40.515 10.891  -35.321  1.00 231.11 ? 328  VAL C CG2 1 
ATOM   8646  N  N   . PRO C  3 331 ? -39.158 11.477  -31.629  1.00 190.44 ? 329  PRO C N   1 
ATOM   8647  C  CA  . PRO C  3 331 ? -38.027 10.781  -31.006  1.00 189.18 ? 329  PRO C CA  1 
ATOM   8648  C  C   . PRO C  3 331 ? -37.786 9.420   -31.634  1.00 195.89 ? 329  PRO C C   1 
ATOM   8649  O  O   . PRO C  3 331 ? -38.724 8.701   -31.984  1.00 196.73 ? 329  PRO C O   1 
ATOM   8650  C  CB  . PRO C  3 331 ? -38.459 10.647  -29.542  1.00 204.07 ? 329  PRO C CB  1 
ATOM   8651  C  CG  . PRO C  3 331 ? -39.950 10.695  -29.591  1.00 206.91 ? 329  PRO C CG  1 
ATOM   8652  C  CD  . PRO C  3 331 ? -40.282 11.651  -30.694  1.00 191.92 ? 329  PRO C CD  1 
ATOM   8653  N  N   . GLN C  3 332 ? -36.508 9.075   -31.776  1.00 197.78 ? 330  GLN C N   1 
ATOM   8654  C  CA  . GLN C  3 332 ? -36.097 7.781   -32.308  1.00 207.47 ? 330  GLN C CA  1 
ATOM   8655  C  C   . GLN C  3 332 ? -35.743 6.783   -31.216  1.00 198.64 ? 330  GLN C C   1 
ATOM   8656  O  O   . GLN C  3 332 ? -36.145 5.618   -31.294  1.00 212.33 ? 330  GLN C O   1 
ATOM   8657  C  CB  . GLN C  3 332 ? -34.903 7.952   -33.255  1.00 209.51 ? 330  GLN C CB  1 
ATOM   8658  C  CG  . GLN C  3 332 ? -34.436 6.659   -33.912  1.00 206.00 ? 330  GLN C CG  1 
ATOM   8659  C  CD  . GLN C  3 332 ? -33.334 6.884   -34.932  1.00 220.42 ? 330  GLN C CD  1 
ATOM   8660  O  OE1 . GLN C  3 332 ? -32.811 7.992   -35.064  1.00 225.13 ? 330  GLN C OE1 1 
ATOM   8661  N  NE2 . GLN C  3 332 ? -32.980 5.834   -35.664  1.00 226.37 ? 330  GLN C NE2 1 
ATOM   8662  N  N   . ALA C  3 333 ? -35.004 7.211   -30.198  1.00 191.37 ? 331  ALA C N   1 
ATOM   8663  C  CA  . ALA C  3 333 ? -34.616 6.353   -29.087  1.00 188.17 ? 331  ALA C CA  1 
ATOM   8664  C  C   . ALA C  3 333 ? -35.147 6.929   -27.781  1.00 193.88 ? 331  ALA C C   1 
ATOM   8665  O  O   . ALA C  3 333 ? -34.968 8.120   -27.503  1.00 200.15 ? 331  ALA C O   1 
ATOM   8666  C  CB  . ALA C  3 333 ? -33.094 6.193   -29.026  1.00 206.26 ? 331  ALA C CB  1 
ATOM   8667  N  N   . LEU C  3 334 ? -35.814 6.086   -26.992  1.00 188.03 ? 332  LEU C N   1 
ATOM   8668  C  CA  . LEU C  3 334 ? -36.341 6.471   -25.690  1.00 172.67 ? 332  LEU C CA  1 
ATOM   8669  C  C   . LEU C  3 334 ? -35.873 5.488   -24.625  1.00 170.35 ? 332  LEU C C   1 
ATOM   8670  O  O   . LEU C  3 334 ? -35.580 4.324   -24.908  1.00 171.45 ? 332  LEU C O   1 
ATOM   8671  C  CB  . LEU C  3 334 ? -37.871 6.538   -25.690  1.00 175.29 ? 332  LEU C CB  1 
ATOM   8672  C  CG  . LEU C  3 334 ? -38.514 7.688   -26.463  1.00 173.31 ? 332  LEU C CG  1 
ATOM   8673  C  CD1 . LEU C  3 334 ? -38.615 7.348   -27.944  1.00 191.75 ? 332  LEU C CD1 1 
ATOM   8674  C  CD2 . LEU C  3 334 ? -39.880 8.002   -25.881  1.00 167.35 ? 332  LEU C CD2 1 
ATOM   8675  N  N   . GLU C  3 335 ? -35.830 5.965   -23.380  1.00 180.87 ? 333  GLU C N   1 
ATOM   8676  C  CA  . GLU C  3 335 ? -35.316 5.168   -22.278  1.00 174.53 ? 333  GLU C CA  1 
ATOM   8677  C  C   . GLU C  3 335 ? -36.319 5.083   -21.132  1.00 170.50 ? 333  GLU C C   1 
ATOM   8678  O  O   . GLU C  3 335 ? -36.999 6.070   -20.820  1.00 168.90 ? 333  GLU C O   1 
ATOM   8679  C  CB  . GLU C  3 335 ? -33.979 5.741   -21.771  1.00 182.57 ? 333  GLU C CB  1 
ATOM   8680  C  CG  . GLU C  3 335 ? -32.858 5.739   -22.821  1.00 195.67 ? 333  GLU C CG  1 
ATOM   8681  C  CD  . GLU C  3 335 ? -31.531 6.272   -22.288  1.00 211.09 ? 333  GLU C CD  1 
ATOM   8682  O  OE1 . GLU C  3 335 ? -31.429 6.518   -21.068  1.00 220.14 ? 333  GLU C OE1 1 
ATOM   8683  O  OE2 . GLU C  3 335 ? -30.583 6.432   -23.088  1.00 227.49 ? 333  GLU C OE2 1 
ATOM   8684  N  N   . PRO C  3 336 ? -36.448 3.910   -20.507  1.00 161.44 ? 334  PRO C N   1 
ATOM   8685  C  CA  . PRO C  3 336 ? -37.402 3.747   -19.405  1.00 159.41 ? 334  PRO C CA  1 
ATOM   8686  C  C   . PRO C  3 336 ? -36.927 4.418   -18.126  1.00 159.25 ? 334  PRO C C   1 
ATOM   8687  O  O   . PRO C  3 336 ? -35.754 4.755   -17.957  1.00 161.35 ? 334  PRO C O   1 
ATOM   8688  C  CB  . PRO C  3 336 ? -37.478 2.228   -19.227  1.00 161.18 ? 334  PRO C CB  1 
ATOM   8689  C  CG  . PRO C  3 336 ? -36.167 1.747   -19.677  1.00 164.69 ? 334  PRO C CG  1 
ATOM   8690  C  CD  . PRO C  3 336 ? -35.762 2.647   -20.821  1.00 164.72 ? 334  PRO C CD  1 
ATOM   8691  N  N   . LEU C  3 337 ? -37.871 4.575   -17.199  1.00 169.90 ? 335  LEU C N   1 
ATOM   8692  C  CA  . LEU C  3 337 ? -37.630 5.253   -15.927  1.00 173.16 ? 335  LEU C CA  1 
ATOM   8693  C  C   . LEU C  3 337 ? -38.185 4.429   -14.771  1.00 170.88 ? 335  LEU C C   1 
ATOM   8694  O  O   . LEU C  3 337 ? -39.408 4.166   -14.731  1.00 155.51 ? 335  LEU C O   1 
ATOM   8695  C  CB  . LEU C  3 337 ? -38.256 6.652   -15.945  1.00 167.79 ? 335  LEU C CB  1 
ATOM   8696  C  CG  . LEU C  3 337 ? -38.240 7.414   -14.621  1.00 162.18 ? 335  LEU C CG  1 
ATOM   8697  C  CD1 . LEU C  3 337 ? -36.812 7.728   -14.216  1.00 197.24 ? 335  LEU C CD1 1 
ATOM   8698  C  CD2 . LEU C  3 337 ? -39.056 8.683   -14.725  1.00 156.67 ? 335  LEU C CD2 1 
ATOM   8699  N  N   . PRO C  3 338 ? -37.346 3.987   -13.828  1.00 184.35 ? 336  PRO C N   1 
ATOM   8700  C  CA  . PRO C  3 338 ? -37.860 3.323   -12.625  1.00 181.81 ? 336  PRO C CA  1 
ATOM   8701  C  C   . PRO C  3 338 ? -38.359 4.328   -11.595  1.00 167.04 ? 336  PRO C C   1 
ATOM   8702  O  O   . PRO C  3 338 ? -37.716 5.346   -11.323  1.00 160.52 ? 336  PRO C O   1 
ATOM   8703  C  CB  . PRO C  3 338 ? -36.638 2.553   -12.103  1.00 174.28 ? 336  PRO C CB  1 
ATOM   8704  C  CG  . PRO C  3 338 ? -35.472 3.354   -12.564  1.00 166.21 ? 336  PRO C CG  1 
ATOM   8705  C  CD  . PRO C  3 338 ? -35.872 3.940   -13.901  1.00 168.29 ? 336  PRO C CD  1 
ATOM   8706  N  N   . ILE C  3 339 ? -39.516 4.024   -11.002  1.00 157.82 ? 337  ILE C N   1 
ATOM   8707  C  CA  . ILE C  3 339 ? -40.137 4.891   -10.010  1.00 157.38 ? 337  ILE C CA  1 
ATOM   8708  C  C   . ILE C  3 339 ? -40.416 4.087   -8.750   1.00 171.89 ? 337  ILE C C   1 
ATOM   8709  O  O   . ILE C  3 339 ? -40.461 2.855   -8.765   1.00 173.01 ? 337  ILE C O   1 
ATOM   8710  C  CB  . ILE C  3 339 ? -41.442 5.534   -10.519  1.00 154.68 ? 337  ILE C CB  1 
ATOM   8711  C  CG1 . ILE C  3 339 ? -42.498 4.460   -10.788  1.00 153.42 ? 337  ILE C CG1 1 
ATOM   8712  C  CG2 . ILE C  3 339 ? -41.173 6.344   -11.765  1.00 154.82 ? 337  ILE C CG2 1 
ATOM   8713  C  CD1 . ILE C  3 339 ? -43.827 5.015   -11.230  1.00 151.79 ? 337  ILE C CD1 1 
ATOM   8714  N  N   . VAL C  3 340 ? -40.591 4.810   -7.646   1.00 168.75 ? 338  VAL C N   1 
ATOM   8715  C  CA  . VAL C  3 340 ? -40.923 4.214   -6.359   1.00 161.37 ? 338  VAL C CA  1 
ATOM   8716  C  C   . VAL C  3 340 ? -42.073 5.002   -5.755   1.00 163.42 ? 338  VAL C C   1 
ATOM   8717  O  O   . VAL C  3 340 ? -41.944 6.208   -5.516   1.00 167.85 ? 338  VAL C O   1 
ATOM   8718  C  CB  . VAL C  3 340 ? -39.727 4.183   -5.400   1.00 165.60 ? 338  VAL C CB  1 
ATOM   8719  C  CG1 . VAL C  3 340 ? -40.182 3.691   -4.044   1.00 167.52 ? 338  VAL C CG1 1 
ATOM   8720  C  CG2 . VAL C  3 340 ? -38.633 3.284   -5.952   1.00 173.45 ? 338  VAL C CG2 1 
ATOM   8721  N  N   . TYR C  3 341 ? -43.202 4.331   -5.542   1.00 172.03 ? 339  TYR C N   1 
ATOM   8722  C  CA  . TYR C  3 341 ? -44.357 4.942   -4.906   1.00 186.34 ? 339  TYR C CA  1 
ATOM   8723  C  C   . TYR C  3 341 ? -45.027 3.925   -3.994   1.00 203.38 ? 339  TYR C C   1 
ATOM   8724  O  O   . TYR C  3 341 ? -44.807 2.717   -4.107   1.00 211.28 ? 339  TYR C O   1 
ATOM   8725  C  CB  . TYR C  3 341 ? -45.357 5.467   -5.938   1.00 176.30 ? 339  TYR C CB  1 
ATOM   8726  C  CG  . TYR C  3 341 ? -46.061 4.385   -6.717   1.00 164.68 ? 339  TYR C CG  1 
ATOM   8727  C  CD1 . TYR C  3 341 ? -45.467 3.802   -7.824   1.00 159.18 ? 339  TYR C CD1 1 
ATOM   8728  C  CD2 . TYR C  3 341 ? -47.324 3.951   -6.343   1.00 170.96 ? 339  TYR C CD2 1 
ATOM   8729  C  CE1 . TYR C  3 341 ? -46.114 2.817   -8.538   1.00 155.96 ? 339  TYR C CE1 1 
ATOM   8730  C  CE2 . TYR C  3 341 ? -47.975 2.970   -7.047   1.00 172.10 ? 339  TYR C CE2 1 
ATOM   8731  C  CZ  . TYR C  3 341 ? -47.369 2.405   -8.143   1.00 160.10 ? 339  TYR C CZ  1 
ATOM   8732  O  OH  . TYR C  3 341 ? -48.026 1.423   -8.847   1.00 165.43 ? 339  TYR C OH  1 
ATOM   8733  N  N   . TYR C  3 342 ? -45.863 4.426   -3.093   1.00 211.31 ? 340  TYR C N   1 
ATOM   8734  C  CA  . TYR C  3 342 ? -46.578 3.587   -2.145   1.00 208.70 ? 340  TYR C CA  1 
ATOM   8735  C  C   . TYR C  3 342 ? -48.034 3.414   -2.564   1.00 204.38 ? 340  TYR C C   1 
ATOM   8736  O  O   . TYR C  3 342 ? -48.602 4.230   -3.295   1.00 188.30 ? 340  TYR C O   1 
ATOM   8737  C  CB  . TYR C  3 342 ? -46.509 4.182   -0.739   1.00 209.28 ? 340  TYR C CB  1 
ATOM   8738  C  CG  . TYR C  3 342 ? -45.210 3.921   -0.014   1.00 208.60 ? 340  TYR C CG  1 
ATOM   8739  C  CD1 . TYR C  3 342 ? -44.040 4.561   -0.398   1.00 205.20 ? 340  TYR C CD1 1 
ATOM   8740  C  CD2 . TYR C  3 342 ? -45.159 3.057   1.071    1.00 213.00 ? 340  TYR C CD2 1 
ATOM   8741  C  CE1 . TYR C  3 342 ? -42.851 4.337   0.268    1.00 209.84 ? 340  TYR C CE1 1 
ATOM   8742  C  CE2 . TYR C  3 342 ? -43.974 2.829   1.748    1.00 221.96 ? 340  TYR C CE2 1 
ATOM   8743  C  CZ  . TYR C  3 342 ? -42.822 3.471   1.339    1.00 215.36 ? 340  TYR C CZ  1 
ATOM   8744  O  OH  . TYR C  3 342 ? -41.633 3.251   1.999    1.00 206.68 ? 340  TYR C OH  1 
ATOM   8745  N  N   . VAL C  3 343 ? -48.636 2.331   -2.076   1.00 230.45 ? 341  VAL C N   1 
ATOM   8746  C  CA  . VAL C  3 343 ? -50.045 2.020   -2.307   1.00 236.65 ? 341  VAL C CA  1 
ATOM   8747  C  C   . VAL C  3 343 ? -50.655 1.731   -0.940   1.00 243.74 ? 341  VAL C C   1 
ATOM   8748  O  O   . VAL C  3 343 ? -50.546 0.611   -0.430   1.00 240.27 ? 341  VAL C O   1 
ATOM   8749  C  CB  . VAL C  3 343 ? -50.230 0.830   -3.256   1.00 223.51 ? 341  VAL C CB  1 
ATOM   8750  C  CG1 . VAL C  3 343 ? -51.708 0.541   -3.474   1.00 238.18 ? 341  VAL C CG1 1 
ATOM   8751  C  CG2 . VAL C  3 343 ? -49.527 1.083   -4.579   1.00 190.52 ? 341  VAL C CG2 1 
ATOM   8752  N  N   . GLY C  3 344 ? -51.301 2.732   -0.344   1.00 252.72 ? 342  GLY C N   1 
ATOM   8753  C  CA  . GLY C  3 344 ? -51.795 2.585   1.010    1.00 256.95 ? 342  GLY C CA  1 
ATOM   8754  C  C   . GLY C  3 344 ? -50.653 2.381   1.983    1.00 252.80 ? 342  GLY C C   1 
ATOM   8755  O  O   . GLY C  3 344 ? -50.051 3.347   2.461    1.00 247.56 ? 342  GLY C O   1 
ATOM   8756  N  N   . ARG C  3 345 ? -50.352 1.118   2.287    1.00 248.39 ? 343  ARG C N   1 
ATOM   8757  C  CA  . ARG C  3 345 ? -49.217 0.759   3.124    1.00 246.82 ? 343  ARG C CA  1 
ATOM   8758  C  C   . ARG C  3 345 ? -48.168 -0.049  2.371    1.00 248.52 ? 343  ARG C C   1 
ATOM   8759  O  O   . ARG C  3 345 ? -47.140 -0.401  2.961    1.00 248.49 ? 343  ARG C O   1 
ATOM   8760  C  CB  . ARG C  3 345 ? -49.679 -0.030  4.360    1.00 250.54 ? 343  ARG C CB  1 
ATOM   8761  C  CG  . ARG C  3 345 ? -50.901 0.543   5.065    1.00 251.32 ? 343  ARG C CG  1 
ATOM   8762  C  CD  . ARG C  3 345 ? -51.252 -0.257  6.316    1.00 249.55 ? 343  ARG C CD  1 
ATOM   8763  N  NE  . ARG C  3 345 ? -52.567 0.101   6.845    1.00 251.28 ? 343  ARG C NE  1 
ATOM   8764  C  CZ  . ARG C  3 345 ? -53.693 -0.549  6.562    1.00 249.42 ? 343  ARG C CZ  1 
ATOM   8765  N  NH1 . ARG C  3 345 ? -53.674 -1.601  5.754    1.00 241.98 ? 343  ARG C NH1 1 
ATOM   8766  N  NH2 . ARG C  3 345 ? -54.843 -0.148  7.090    1.00 250.57 ? 343  ARG C NH2 1 
ATOM   8767  N  N   . LYS C  3 346 ? -48.397 -0.354  1.091    1.00 237.68 ? 344  LYS C N   1 
ATOM   8768  C  CA  . LYS C  3 346 ? -47.517 -1.220  0.307    1.00 239.03 ? 344  LYS C CA  1 
ATOM   8769  C  C   . LYS C  3 346 ? -46.676 -0.417  -0.679   1.00 226.77 ? 344  LYS C C   1 
ATOM   8770  O  O   . LYS C  3 346 ? -47.231 0.173   -1.619   1.00 222.53 ? 344  LYS C O   1 
ATOM   8771  C  CB  . LYS C  3 346 ? -48.342 -2.276  -0.436   1.00 234.65 ? 344  LYS C CB  1 
ATOM   8772  C  CG  . LYS C  3 346 ? -49.356 -3.003  0.442    1.00 235.95 ? 344  LYS C CG  1 
ATOM   8773  C  CD  . LYS C  3 346 ? -50.091 -4.102  -0.314   1.00 226.24 ? 344  LYS C CD  1 
ATOM   8774  C  CE  . LYS C  3 346 ? -51.155 -4.756  0.562    1.00 227.09 ? 344  LYS C CE  1 
ATOM   8775  N  NZ  . LYS C  3 346 ? -50.555 -5.541  1.682    1.00 235.18 ? 344  LYS C NZ  1 
ATOM   8776  N  N   . PRO C  3 347 ? -45.350 -0.360  -0.507   1.00 223.84 ? 345  PRO C N   1 
ATOM   8777  C  CA  . PRO C  3 347 ? -44.487 0.323   -1.487   1.00 209.52 ? 345  PRO C CA  1 
ATOM   8778  C  C   . PRO C  3 347 ? -44.225 -0.557  -2.705   1.00 202.19 ? 345  PRO C C   1 
ATOM   8779  O  O   . PRO C  3 347 ? -43.859 -1.728  -2.573   1.00 200.89 ? 345  PRO C O   1 
ATOM   8780  C  CB  . PRO C  3 347 ? -43.196 0.582   -0.704   1.00 211.86 ? 345  PRO C CB  1 
ATOM   8781  C  CG  . PRO C  3 347 ? -43.146 -0.516  0.295    1.00 217.30 ? 345  PRO C CG  1 
ATOM   8782  C  CD  . PRO C  3 347 ? -44.580 -0.864  0.646    1.00 230.25 ? 345  PRO C CD  1 
ATOM   8783  N  N   . LYS C  3 348 ? -44.421 0.009   -3.895   1.00 194.56 ? 346  LYS C N   1 
ATOM   8784  C  CA  . LYS C  3 348 ? -44.233 -0.707  -5.153   1.00 196.02 ? 346  LYS C CA  1 
ATOM   8785  C  C   . LYS C  3 348 ? -43.155 -0.019  -5.981   1.00 188.23 ? 346  LYS C C   1 
ATOM   8786  O  O   . LYS C  3 348 ? -43.290 1.161   -6.321   1.00 191.53 ? 346  LYS C O   1 
ATOM   8787  C  CB  . LYS C  3 348 ? -45.550 -0.777  -5.931   1.00 192.21 ? 346  LYS C CB  1 
ATOM   8788  C  CG  . LYS C  3 348 ? -46.647 -1.537  -5.198   1.00 194.50 ? 346  LYS C CG  1 
ATOM   8789  C  CD  . LYS C  3 348 ? -47.901 -1.682  -6.043   1.00 191.08 ? 346  LYS C CD  1 
ATOM   8790  C  CE  . LYS C  3 348 ? -48.975 -2.467  -5.300   1.00 197.43 ? 346  LYS C CE  1 
ATOM   8791  N  NZ  . LYS C  3 348 ? -48.497 -3.833  -4.943   1.00 216.86 ? 346  LYS C NZ  1 
ATOM   8792  N  N   . VAL C  3 349 ? -42.088 -0.749  -6.301   1.00 171.07 ? 347  VAL C N   1 
ATOM   8793  C  CA  . VAL C  3 349 ? -41.035 -0.243  -7.177   1.00 162.78 ? 347  VAL C CA  1 
ATOM   8794  C  C   . VAL C  3 349 ? -41.369 -0.662  -8.601   1.00 160.99 ? 347  VAL C C   1 
ATOM   8795  O  O   . VAL C  3 349 ? -41.228 -1.833  -8.956   1.00 162.49 ? 347  VAL C O   1 
ATOM   8796  C  CB  . VAL C  3 349 ? -39.654 -0.756  -6.764   1.00 166.94 ? 347  VAL C CB  1 
ATOM   8797  C  CG1 . VAL C  3 349 ? -38.588 -0.144  -7.657   1.00 167.54 ? 347  VAL C CG1 1 
ATOM   8798  C  CG2 . VAL C  3 349 ? -39.391 -0.425  -5.317   1.00 169.55 ? 347  VAL C CG2 1 
ATOM   8799  N  N   . GLU C  3 350 ? -41.792 0.296   -9.423   1.00 158.41 ? 348  GLU C N   1 
ATOM   8800  C  CA  . GLU C  3 350 ? -42.205 0.018   -10.789  1.00 160.21 ? 348  GLU C CA  1 
ATOM   8801  C  C   . GLU C  3 350 ? -41.369 0.820   -11.779  1.00 167.20 ? 348  GLU C C   1 
ATOM   8802  O  O   . GLU C  3 350 ? -40.756 1.833   -11.430  1.00 168.50 ? 348  GLU C O   1 
ATOM   8803  C  CB  . GLU C  3 350 ? -43.694 0.321   -10.989  1.00 154.96 ? 348  GLU C CB  1 
ATOM   8804  C  CG  . GLU C  3 350 ? -44.599 -0.465  -10.053  1.00 157.75 ? 348  GLU C CG  1 
ATOM   8805  C  CD  . GLU C  3 350 ? -46.057 -0.410  -10.456  1.00 173.71 ? 348  GLU C CD  1 
ATOM   8806  O  OE1 . GLU C  3 350 ? -46.874 -1.113  -9.825   1.00 190.65 ? 348  GLU C OE1 1 
ATOM   8807  O  OE2 . GLU C  3 350 ? -46.382 0.324   -11.411  1.00 167.43 ? 348  GLU C OE2 1 
ATOM   8808  N  N   . GLN C  3 351 ? -41.367 0.361   -13.033  1.00 161.29 ? 349  GLN C N   1 
ATOM   8809  C  CA  . GLN C  3 351 ? -40.572 0.974   -14.092  1.00 157.06 ? 349  GLN C CA  1 
ATOM   8810  C  C   . GLN C  3 351 ? -41.460 1.283   -15.286  1.00 162.94 ? 349  GLN C C   1 
ATOM   8811  O  O   . GLN C  3 351 ? -42.029 0.369   -15.894  1.00 159.40 ? 349  GLN C O   1 
ATOM   8812  C  CB  . GLN C  3 351 ? -39.418 0.068   -14.519  1.00 160.13 ? 349  GLN C CB  1 
ATOM   8813  C  CG  . GLN C  3 351 ? -38.522 0.691   -15.566  1.00 160.75 ? 349  GLN C CG  1 
ATOM   8814  C  CD  . GLN C  3 351 ? -37.414 -0.243  -16.010  1.00 174.53 ? 349  GLN C CD  1 
ATOM   8815  O  OE1 . GLN C  3 351 ? -37.485 -1.453  -15.800  1.00 182.23 ? 349  GLN C OE1 1 
ATOM   8816  N  NE2 . GLN C  3 351 ? -36.377 0.318   -16.619  1.00 179.03 ? 349  GLN C NE2 1 
ATOM   8817  N  N   . LEU C  3 352 ? -41.539 2.564   -15.638  1.00 183.26 ? 350  LEU C N   1 
ATOM   8818  C  CA  . LEU C  3 352 ? -42.310 3.003   -16.790  1.00 159.97 ? 350  LEU C CA  1 
ATOM   8819  C  C   . LEU C  3 352 ? -41.500 2.807   -18.061  1.00 166.06 ? 350  LEU C C   1 
ATOM   8820  O  O   . LEU C  3 352 ? -40.276 2.953   -18.061  1.00 182.58 ? 350  LEU C O   1 
ATOM   8821  C  CB  . LEU C  3 352 ? -42.697 4.474   -16.648  1.00 154.76 ? 350  LEU C CB  1 
ATOM   8822  C  CG  . LEU C  3 352 ? -43.538 4.845   -15.432  1.00 176.28 ? 350  LEU C CG  1 
ATOM   8823  C  CD1 . LEU C  3 352 ? -43.826 6.335   -15.432  1.00 194.11 ? 350  LEU C CD1 1 
ATOM   8824  C  CD2 . LEU C  3 352 ? -44.828 4.046   -15.411  1.00 186.96 ? 350  LEU C CD2 1 
ATOM   8825  N  N   . SER C  3 353 ? -42.188 2.465   -19.144  1.00 175.49 ? 351  SER C N   1 
ATOM   8826  C  CA  . SER C  3 353 ? -41.537 2.199   -20.420  1.00 187.69 ? 351  SER C CA  1 
ATOM   8827  C  C   . SER C  3 353 ? -41.533 3.440   -21.310  1.00 190.91 ? 351  SER C C   1 
ATOM   8828  O  O   . SER C  3 353 ? -42.568 4.093   -21.483  1.00 207.06 ? 351  SER C O   1 
ATOM   8829  C  CB  . SER C  3 353 ? -42.231 1.031   -21.125  1.00 204.57 ? 351  SER C CB  1 
ATOM   8830  O  OG  . SER C  3 353 ? -43.620 1.274   -21.278  1.00 211.84 ? 351  SER C OG  1 
ATOM   8831  N  N   . ASN C  3 354 ? -40.360 3.756   -21.869  1.00 180.84 ? 352  ASN C N   1 
ATOM   8832  C  CA  . ASN C  3 354 ? -40.170 4.876   -22.788  1.00 193.85 ? 352  ASN C CA  1 
ATOM   8833  C  C   . ASN C  3 354 ? -40.580 6.214   -22.181  1.00 181.06 ? 352  ASN C C   1 
ATOM   8834  O  O   . ASN C  3 354 ? -41.716 6.666   -22.362  1.00 186.01 ? 352  ASN C O   1 
ATOM   8835  C  CB  . ASN C  3 354 ? -40.937 4.635   -24.095  1.00 206.02 ? 352  ASN C CB  1 
ATOM   8836  C  CG  . ASN C  3 354 ? -40.400 3.444   -24.882  1.00 192.97 ? 352  ASN C CG  1 
ATOM   8837  O  OD1 . ASN C  3 354 ? -39.486 3.587   -25.693  1.00 188.40 ? 352  ASN C OD1 1 
ATOM   8838  N  ND2 . ASN C  3 354 ? -40.973 2.268   -24.650  1.00 185.61 ? 352  ASN C ND2 1 
ATOM   8839  N  N   . MET C  3 355 ? -39.649 6.871   -21.487  1.00 159.20 ? 353  MET C N   1 
ATOM   8840  C  CA  . MET C  3 355 ? -39.917 8.168   -20.875  1.00 168.57 ? 353  MET C CA  1 
ATOM   8841  C  C   . MET C  3 355 ? -38.833 9.166   -21.261  1.00 169.80 ? 353  MET C C   1 
ATOM   8842  O  O   . MET C  3 355 ? -39.133 10.295  -21.665  1.00 174.06 ? 353  MET C O   1 
ATOM   8843  C  CB  . MET C  3 355 ? -40.004 8.056   -19.346  1.00 165.07 ? 353  MET C CB  1 
ATOM   8844  C  CG  . MET C  3 355 ? -41.157 7.217   -18.795  1.00 155.69 ? 353  MET C CG  1 
ATOM   8845  S  SD  . MET C  3 355 ? -42.790 7.856   -19.189  1.00 159.83 ? 353  MET C SD  1 
ATOM   8846  C  CE  . MET C  3 355 ? -42.734 9.463   -18.404  1.00 154.51 ? 353  MET C CE  1 
ATOM   8847  N  N   . ILE C  3 356 ? -37.572 8.762   -21.132  1.00 160.98 ? 354  ILE C N   1 
ATOM   8848  C  CA  . ILE C  3 356 ? -36.444 9.643   -21.422  1.00 164.23 ? 354  ILE C CA  1 
ATOM   8849  C  C   . ILE C  3 356 ? -36.190 9.654   -22.922  1.00 167.94 ? 354  ILE C C   1 
ATOM   8850  O  O   . ILE C  3 356 ? -35.869 8.620   -23.515  1.00 177.57 ? 354  ILE C O   1 
ATOM   8851  C  CB  . ILE C  3 356 ? -35.185 9.210   -20.657  1.00 178.60 ? 354  ILE C CB  1 
ATOM   8852  C  CG1 . ILE C  3 356 ? -35.355 9.434   -19.152  1.00 180.12 ? 354  ILE C CG1 1 
ATOM   8853  C  CG2 . ILE C  3 356 ? -33.967 9.959   -21.175  1.00 181.00 ? 354  ILE C CG2 1 
ATOM   8854  C  CD1 . ILE C  3 356 ? -35.931 8.249   -18.409  1.00 183.92 ? 354  ILE C CD1 1 
ATOM   8855  N  N   . VAL C  3 357 ? -36.319 10.826  -23.533  1.00 169.24 ? 355  VAL C N   1 
ATOM   8856  C  CA  . VAL C  3 357 ? -36.082 10.976  -24.964  1.00 169.96 ? 355  VAL C CA  1 
ATOM   8857  C  C   . VAL C  3 357 ? -34.594 11.187  -25.202  1.00 181.75 ? 355  VAL C C   1 
ATOM   8858  O  O   . VAL C  3 357 ? -34.016 12.180  -24.746  1.00 189.03 ? 355  VAL C O   1 
ATOM   8859  C  CB  . VAL C  3 357 ? -36.900 12.135  -25.540  1.00 170.79 ? 355  VAL C CB  1 
ATOM   8860  C  CG1 . VAL C  3 357 ? -36.477 12.401  -26.968  1.00 174.44 ? 355  VAL C CG1 1 
ATOM   8861  C  CG2 . VAL C  3 357 ? -38.382 11.807  -25.469  1.00 169.13 ? 355  VAL C CG2 1 
ATOM   8862  N  N   . ARG C  3 358 ? -33.972 10.248  -25.913  1.00 187.03 ? 356  ARG C N   1 
ATOM   8863  C  CA  . ARG C  3 358 ? -32.537 10.329  -26.216  1.00 197.18 ? 356  ARG C CA  1 
ATOM   8864  C  C   . ARG C  3 358 ? -32.316 10.991  -27.574  1.00 196.36 ? 356  ARG C C   1 
ATOM   8865  O  O   . ARG C  3 358 ? -31.797 12.108  -27.654  1.00 200.17 ? 356  ARG C O   1 
ATOM   8866  C  CB  . ARG C  3 358 ? -31.911 8.934   -26.158  1.00 222.07 ? 356  ARG C CB  1 
ATOM   8867  C  CG  . ARG C  3 358 ? -30.402 8.921   -26.327  1.00 236.43 ? 356  ARG C CG  1 
ATOM   8868  C  CD  . ARG C  3 358 ? -29.705 9.635   -25.173  1.00 227.11 ? 356  ARG C CD  1 
ATOM   8869  N  NE  . ARG C  3 358 ? -29.838 8.916   -23.907  1.00 224.61 ? 356  ARG C NE  1 
ATOM   8870  C  CZ  . ARG C  3 358 ? -29.258 9.292   -22.770  1.00 230.11 ? 356  ARG C CZ  1 
ATOM   8871  N  NH1 . ARG C  3 358 ? -28.501 10.380  -22.738  1.00 236.66 ? 356  ARG C NH1 1 
ATOM   8872  N  NH2 . ARG C  3 358 ? -29.429 8.580   -21.665  1.00 226.39 ? 356  ARG C NH2 1 
ATOM   8873  N  N   . SER C  3 359 ? -32.698 10.306  -28.648  1.00 191.11 ? 357  SER C N   1 
ATOM   8874  C  CA  . SER C  3 359 ? -32.515 10.789  -30.009  1.00 197.84 ? 357  SER C CA  1 
ATOM   8875  C  C   . SER C  3 359 ? -33.842 11.245  -30.595  1.00 198.36 ? 357  SER C C   1 
ATOM   8876  O  O   . SER C  3 359 ? -34.917 10.972  -30.057  1.00 192.85 ? 357  SER C O   1 
ATOM   8877  C  CB  . SER C  3 359 ? -31.908 9.703   -30.906  1.00 202.73 ? 357  SER C CB  1 
ATOM   8878  O  OG  . SER C  3 359 ? -30.692 9.217   -30.377  1.00 210.55 ? 357  SER C OG  1 
ATOM   8879  N  N   . CYS C  3 360 ? -33.747 11.933  -31.730  1.00 206.71 ? 358  CYS C N   1 
ATOM   8880  C  CA  . CYS C  3 360 ? -34.914 12.385  -32.471  1.00 215.76 ? 358  CYS C CA  1 
ATOM   8881  C  C   . CYS C  3 360 ? -34.660 12.185  -33.955  1.00 205.99 ? 358  CYS C C   1 
ATOM   8882  O  O   . CYS C  3 360 ? -33.548 12.412  -34.439  1.00 198.90 ? 358  CYS C O   1 
ATOM   8883  C  CB  . CYS C  3 360 ? -35.234 13.862  -32.202  1.00 226.06 ? 358  CYS C CB  1 
ATOM   8884  S  SG  . CYS C  3 360 ? -35.545 14.251  -30.461  1.00 256.79 ? 358  CYS C SG  1 
ATOM   8885  N  N   . LYS C  3 361 ? -35.692 11.740  -34.663  1.00 202.82 ? 359  LYS C N   1 
ATOM   8886  C  CA  . LYS C  3 361 ? -35.655 11.501  -36.098  1.00 202.70 ? 359  LYS C CA  1 
ATOM   8887  C  C   . LYS C  3 361 ? -36.770 12.293  -36.774  1.00 210.82 ? 359  LYS C C   1 
ATOM   8888  O  O   . LYS C  3 361 ? -37.590 12.943  -36.121  1.00 216.09 ? 359  LYS C O   1 
ATOM   8889  C  CB  . LYS C  3 361 ? -35.786 10.006  -36.416  1.00 205.43 ? 359  LYS C CB  1 
ATOM   8890  C  CG  . LYS C  3 361 ? -37.099 9.380   -35.952  1.00 205.40 ? 359  LYS C CG  1 
ATOM   8891  C  CD  . LYS C  3 361 ? -37.221 7.911   -36.358  1.00 205.01 ? 359  LYS C CD  1 
ATOM   8892  C  CE  . LYS C  3 361 ? -38.523 7.298   -35.841  1.00 200.37 ? 359  LYS C CE  1 
ATOM   8893  N  NZ  . LYS C  3 361 ? -38.695 5.860   -36.201  1.00 204.13 ? 359  LYS C NZ  1 
ATOM   8894  N  N   . CYS C  3 362 ? -36.790 12.241  -38.104  1.00 226.21 ? 360  CYS C N   1 
ATOM   8895  C  CA  . CYS C  3 362 ? -37.834 12.871  -38.905  1.00 230.57 ? 360  CYS C CA  1 
ATOM   8896  C  C   . CYS C  3 362 ? -38.461 11.827  -39.814  1.00 242.14 ? 360  CYS C C   1 
ATOM   8897  O  O   . CYS C  3 362 ? -37.788 11.281  -40.695  1.00 258.10 ? 360  CYS C O   1 
ATOM   8898  C  CB  . CYS C  3 362 ? -37.277 14.030  -39.729  1.00 234.35 ? 360  CYS C CB  1 
ATOM   8899  S  SG  . CYS C  3 362 ? -36.536 15.329  -38.740  1.00 240.96 ? 360  CYS C SG  1 
ATOM   8900  N  N   . SER C  3 363 ? -39.743 11.555  -39.609  1.00 242.61 ? 361  SER C N   1 
ATOM   8901  C  CA  . SER C  3 363 ? -40.438 10.580  -40.442  1.00 249.59 ? 361  SER C CA  1 
ATOM   8902  C  C   . SER C  3 363 ? -41.886 10.992  -40.654  1.00 269.40 ? 361  SER C C   1 
ATOM   8903  O  O   . SER C  3 363 ? -42.355 11.971  -40.072  1.00 278.13 ? 361  SER C O   1 
ATOM   8904  C  CB  . SER C  3 363 ? -40.368 9.183   -39.820  1.00 243.99 ? 361  SER C CB  1 
ATOM   8905  O  OG  . SER C  3 363 ? -40.890 9.184   -38.504  1.00 244.27 ? 361  SER C OG  1 
ATOM   8906  O  OXT . SER C  3 363 ? -42.615 10.359  -41.420  1.00 272.83 ? 361  SER C OXT 1 
ATOM   8907  N  N   . ILE D  3 9   ? -43.250 31.768  -34.079  1.00 214.79 ? 7    ILE D N   1 
ATOM   8908  C  CA  . ILE D  3 9   ? -42.568 32.349  -32.929  1.00 217.34 ? 7    ILE D CA  1 
ATOM   8909  C  C   . ILE D  3 9   ? -42.176 31.189  -32.002  1.00 217.14 ? 7    ILE D C   1 
ATOM   8910  O  O   . ILE D  3 9   ? -41.047 31.129  -31.510  1.00 217.25 ? 7    ILE D O   1 
ATOM   8911  C  CB  . ILE D  3 9   ? -43.420 33.413  -32.213  1.00 216.35 ? 7    ILE D CB  1 
ATOM   8912  C  CG1 . ILE D  3 9   ? -43.620 34.662  -33.084  1.00 222.67 ? 7    ILE D CG1 1 
ATOM   8913  C  CG2 . ILE D  3 9   ? -42.710 33.858  -30.979  1.00 221.10 ? 7    ILE D CG2 1 
ATOM   8914  C  CD1 . ILE D  3 9   ? -44.712 34.559  -34.128  1.00 226.91 ? 7    ILE D CD1 1 
ATOM   8915  N  N   . ASP D  3 10  ? -43.148 30.289  -31.793  1.00 221.84 ? 8    ASP D N   1 
ATOM   8916  C  CA  . ASP D  3 10  ? -43.044 29.018  -31.071  1.00 220.15 ? 8    ASP D CA  1 
ATOM   8917  C  C   . ASP D  3 10  ? -43.139 29.111  -29.566  1.00 216.99 ? 8    ASP D C   1 
ATOM   8918  O  O   . ASP D  3 10  ? -43.943 28.395  -28.968  1.00 215.92 ? 8    ASP D O   1 
ATOM   8919  C  CB  . ASP D  3 10  ? -41.749 28.312  -31.408  1.00 212.29 ? 8    ASP D CB  1 
ATOM   8920  C  CG  . ASP D  3 10  ? -41.714 27.868  -32.825  1.00 226.18 ? 8    ASP D CG  1 
ATOM   8921  O  OD1 . ASP D  3 10  ? -42.806 27.748  -33.426  1.00 238.84 ? 8    ASP D OD1 1 
ATOM   8922  O  OD2 . ASP D  3 10  ? -40.602 27.641  -33.339  1.00 229.18 ? 8    ASP D OD2 1 
ATOM   8923  N  N   . MET D  3 11  ? -42.234 29.852  -28.940  1.00 201.82 ? 9    MET D N   1 
ATOM   8924  C  CA  . MET D  3 11  ? -42.346 30.143  -27.511  1.00 200.66 ? 9    MET D CA  1 
ATOM   8925  C  C   . MET D  3 11  ? -41.761 29.030  -26.624  1.00 201.30 ? 9    MET D C   1 
ATOM   8926  O  O   . MET D  3 11  ? -41.365 27.996  -27.160  1.00 192.65 ? 9    MET D O   1 
ATOM   8927  C  CB  . MET D  3 11  ? -43.821 30.472  -27.267  1.00 207.32 ? 9    MET D CB  1 
ATOM   8928  C  CG  . MET D  3 11  ? -44.369 30.105  -26.069  1.00 214.49 ? 9    MET D CG  1 
ATOM   8929  S  SD  . MET D  3 11  ? -43.674 30.973  -24.679  1.00 206.45 ? 9    MET D SD  1 
ATOM   8930  C  CE  . MET D  3 11  ? -44.460 32.471  -25.057  1.00 227.63 ? 9    MET D CE  1 
ATOM   8931  N  N   . GLU D  3 12  ? -41.646 29.217  -25.289  1.00 209.84 ? 10   GLU D N   1 
ATOM   8932  C  CA  . GLU D  3 12  ? -41.096 28.194  -24.374  1.00 205.97 ? 10   GLU D CA  1 
ATOM   8933  C  C   . GLU D  3 12  ? -42.156 27.362  -23.674  1.00 197.64 ? 10   GLU D C   1 
ATOM   8934  O  O   . GLU D  3 12  ? -41.818 26.494  -22.856  1.00 189.36 ? 10   GLU D O   1 
ATOM   8935  C  CB  . GLU D  3 12  ? -40.185 28.825  -23.302  1.00 219.95 ? 10   GLU D CB  1 
ATOM   8936  C  CG  . GLU D  3 12  ? -39.163 27.924  -22.590  1.00 218.73 ? 10   GLU D CG  1 
ATOM   8937  C  CD  . GLU D  3 12  ? -38.544 28.614  -21.390  1.00 236.60 ? 10   GLU D CD  1 
ATOM   8938  O  OE1 . GLU D  3 12  ? -39.278 28.845  -20.406  1.00 251.86 ? 10   GLU D OE1 1 
ATOM   8939  O  OE2 . GLU D  3 12  ? -37.342 28.950  -21.441  1.00 235.71 ? 10   GLU D OE2 1 
ATOM   8940  N  N   . LEU D  3 13  ? -43.428 27.634  -23.941  1.00 198.75 ? 11   LEU D N   1 
ATOM   8941  C  CA  . LEU D  3 13  ? -44.490 26.834  -23.357  1.00 191.50 ? 11   LEU D CA  1 
ATOM   8942  C  C   . LEU D  3 13  ? -44.507 25.422  -23.903  1.00 181.93 ? 11   LEU D C   1 
ATOM   8943  O  O   . LEU D  3 13  ? -45.231 24.581  -23.361  1.00 178.84 ? 11   LEU D O   1 
ATOM   8944  C  CB  . LEU D  3 13  ? -45.861 27.489  -23.584  1.00 207.21 ? 11   LEU D CB  1 
ATOM   8945  C  CG  . LEU D  3 13  ? -46.514 27.628  -24.974  1.00 202.48 ? 11   LEU D CG  1 
ATOM   8946  C  CD1 . LEU D  3 13  ? -47.166 26.341  -25.524  1.00 189.72 ? 11   LEU D CD1 1 
ATOM   8947  C  CD2 . LEU D  3 13  ? -47.538 28.753  -24.967  1.00 215.10 ? 11   LEU D CD2 1 
ATOM   8948  N  N   . VAL D  3 14  ? -43.769 25.163  -24.982  1.00 190.16 ? 12   VAL D N   1 
ATOM   8949  C  CA  . VAL D  3 14  ? -43.667 23.810  -25.515  1.00 199.90 ? 12   VAL D CA  1 
ATOM   8950  C  C   . VAL D  3 14  ? -43.198 22.852  -24.428  1.00 198.22 ? 12   VAL D C   1 
ATOM   8951  O  O   . VAL D  3 14  ? -43.627 21.691  -24.371  1.00 188.89 ? 12   VAL D O   1 
ATOM   8952  C  CB  . VAL D  3 14  ? -42.731 23.801  -26.740  1.00 201.04 ? 12   VAL D CB  1 
ATOM   8953  C  CG1 . VAL D  3 14  ? -42.612 22.400  -27.337  1.00 188.19 ? 12   VAL D CG1 1 
ATOM   8954  C  CG2 . VAL D  3 14  ? -43.214 24.809  -27.789  1.00 212.82 ? 12   VAL D CG2 1 
ATOM   8955  N  N   . LYS D  3 15  ? -42.325 23.329  -23.537  1.00 199.85 ? 13   LYS D N   1 
ATOM   8956  C  CA  . LYS D  3 15  ? -41.869 22.500  -22.427  1.00 183.82 ? 13   LYS D CA  1 
ATOM   8957  C  C   . LYS D  3 15  ? -43.022 22.174  -21.491  1.00 174.29 ? 13   LYS D C   1 
ATOM   8958  O  O   . LYS D  3 15  ? -43.110 21.057  -20.970  1.00 168.95 ? 13   LYS D O   1 
ATOM   8959  C  CB  . LYS D  3 15  ? -40.746 23.212  -21.670  1.00 191.76 ? 13   LYS D CB  1 
ATOM   8960  C  CG  . LYS D  3 15  ? -39.555 23.611  -22.536  1.00 206.12 ? 13   LYS D CG  1 
ATOM   8961  C  CD  . LYS D  3 15  ? -38.493 24.347  -21.734  1.00 211.10 ? 13   LYS D CD  1 
ATOM   8962  C  CE  . LYS D  3 15  ? -37.305 24.718  -22.604  1.00 210.93 ? 13   LYS D CE  1 
ATOM   8963  N  NZ  . LYS D  3 15  ? -36.252 25.425  -21.828  1.00 216.12 ? 13   LYS D NZ  1 
ATOM   8964  N  N   . ARG D  3 16  ? -43.938 23.129  -21.299  1.00 182.67 ? 14   ARG D N   1 
ATOM   8965  C  CA  . ARG D  3 16  ? -45.100 22.897  -20.450  1.00 184.56 ? 14   ARG D CA  1 
ATOM   8966  C  C   . ARG D  3 16  ? -46.124 21.995  -21.119  1.00 183.31 ? 14   ARG D C   1 
ATOM   8967  O  O   . ARG D  3 16  ? -46.903 21.336  -20.420  1.00 173.57 ? 14   ARG D O   1 
ATOM   8968  C  CB  . ARG D  3 16  ? -45.741 24.233  -20.065  1.00 190.50 ? 14   ARG D CB  1 
ATOM   8969  C  CG  . ARG D  3 16  ? -44.934 25.034  -19.056  1.00 198.64 ? 14   ARG D CG  1 
ATOM   8970  C  CD  . ARG D  3 16  ? -44.755 24.242  -17.776  1.00 200.37 ? 14   ARG D CD  1 
ATOM   8971  N  NE  . ARG D  3 16  ? -46.030 23.731  -17.285  1.00 195.31 ? 14   ARG D NE  1 
ATOM   8972  C  CZ  . ARG D  3 16  ? -46.171 23.016  -16.173  1.00 195.93 ? 14   ARG D CZ  1 
ATOM   8973  N  NH1 . ARG D  3 16  ? -45.115 22.726  -15.427  1.00 207.89 ? 14   ARG D NH1 1 
ATOM   8974  N  NH2 . ARG D  3 16  ? -47.373 22.595  -15.806  1.00 191.09 ? 14   ARG D NH2 1 
ATOM   8975  N  N   . LYS D  3 17  ? -46.135 21.947  -22.453  1.00 177.55 ? 15   LYS D N   1 
ATOM   8976  C  CA  . LYS D  3 17  ? -47.003 21.008  -23.150  1.00 172.28 ? 15   LYS D CA  1 
ATOM   8977  C  C   . LYS D  3 17  ? -46.517 19.585  -22.939  1.00 168.14 ? 15   LYS D C   1 
ATOM   8978  O  O   . LYS D  3 17  ? -47.324 18.651  -22.896  1.00 167.61 ? 15   LYS D O   1 
ATOM   8979  C  CB  . LYS D  3 17  ? -47.054 21.343  -24.645  1.00 175.12 ? 15   LYS D CB  1 
ATOM   8980  C  CG  . LYS D  3 17  ? -47.982 22.501  -25.029  1.00 181.65 ? 15   LYS D CG  1 
ATOM   8981  C  CD  . LYS D  3 17  ? -47.967 22.732  -26.542  1.00 182.56 ? 15   LYS D CD  1 
ATOM   8982  C  CE  . LYS D  3 17  ? -48.955 23.805  -26.972  1.00 188.59 ? 15   LYS D CE  1 
ATOM   8983  N  NZ  . LYS D  3 17  ? -48.849 24.128  -28.423  1.00 191.66 ? 15   LYS D NZ  1 
ATOM   8984  N  N   . ARG D  3 18  ? -45.198 19.413  -22.824  1.00 177.10 ? 16   ARG D N   1 
ATOM   8985  C  CA  . ARG D  3 18  ? -44.618 18.113  -22.506  1.00 171.68 ? 16   ARG D CA  1 
ATOM   8986  C  C   . ARG D  3 18  ? -44.919 17.708  -21.066  1.00 171.84 ? 16   ARG D C   1 
ATOM   8987  O  O   . ARG D  3 18  ? -45.242 16.545  -20.799  1.00 166.73 ? 16   ARG D O   1 
ATOM   8988  C  CB  . ARG D  3 18  ? -43.109 18.152  -22.756  1.00 170.33 ? 16   ARG D CB  1 
ATOM   8989  C  CG  . ARG D  3 18  ? -42.320 16.946  -22.254  1.00 177.77 ? 16   ARG D CG  1 
ATOM   8990  C  CD  . ARG D  3 18  ? -42.376 15.772  -23.220  1.00 185.70 ? 16   ARG D CD  1 
ATOM   8991  N  NE  . ARG D  3 18  ? -41.726 14.582  -22.674  1.00 184.88 ? 16   ARG D NE  1 
ATOM   8992  C  CZ  . ARG D  3 18  ? -41.572 13.439  -23.337  1.00 186.51 ? 16   ARG D CZ  1 
ATOM   8993  N  NH1 . ARG D  3 18  ? -42.017 13.322  -24.582  1.00 199.47 ? 16   ARG D NH1 1 
ATOM   8994  N  NH2 . ARG D  3 18  ? -40.968 12.413  -22.756  1.00 171.70 ? 16   ARG D NH2 1 
ATOM   8995  N  N   . ILE D  3 19  ? -44.816 18.654  -20.126  1.00 175.75 ? 17   ILE D N   1 
ATOM   8996  C  CA  . ILE D  3 19  ? -45.042 18.346  -18.713  1.00 175.27 ? 17   ILE D CA  1 
ATOM   8997  C  C   . ILE D  3 19  ? -46.480 17.906  -18.481  1.00 176.09 ? 17   ILE D C   1 
ATOM   8998  O  O   . ILE D  3 19  ? -46.740 16.941  -17.752  1.00 166.50 ? 17   ILE D O   1 
ATOM   8999  C  CB  . ILE D  3 19  ? -44.678 19.557  -17.834  1.00 184.81 ? 17   ILE D CB  1 
ATOM   9000  C  CG1 . ILE D  3 19  ? -43.189 19.885  -17.958  1.00 194.15 ? 17   ILE D CG1 1 
ATOM   9001  C  CG2 . ILE D  3 19  ? -45.048 19.298  -16.388  1.00 186.12 ? 17   ILE D CG2 1 
ATOM   9002  C  CD1 . ILE D  3 19  ? -42.746 21.037  -17.081  1.00 200.50 ? 17   ILE D CD1 1 
ATOM   9003  N  N   . GLU D  3 20  ? -47.438 18.614  -19.081  1.00 181.50 ? 18   GLU D N   1 
ATOM   9004  C  CA  . GLU D  3 20  ? -48.835 18.233  -18.930  1.00 166.64 ? 18   GLU D CA  1 
ATOM   9005  C  C   . GLU D  3 20  ? -49.173 16.978  -19.719  1.00 165.21 ? 18   GLU D C   1 
ATOM   9006  O  O   . GLU D  3 20  ? -50.189 16.335  -19.431  1.00 165.88 ? 18   GLU D O   1 
ATOM   9007  C  CB  . GLU D  3 20  ? -49.737 19.391  -19.352  1.00 171.22 ? 18   GLU D CB  1 
ATOM   9008  C  CG  . GLU D  3 20  ? -49.726 20.547  -18.365  1.00 176.43 ? 18   GLU D CG  1 
ATOM   9009  C  CD  . GLU D  3 20  ? -50.205 20.137  -16.986  1.00 178.00 ? 18   GLU D CD  1 
ATOM   9010  O  OE1 . GLU D  3 20  ? -51.102 19.271  -16.899  1.00 186.49 ? 18   GLU D OE1 1 
ATOM   9011  O  OE2 . GLU D  3 20  ? -49.683 20.681  -15.991  1.00 174.78 ? 18   GLU D OE2 1 
ATOM   9012  N  N   . ALA D  3 21  ? -48.350 16.625  -20.710  1.00 187.07 ? 19   ALA D N   1 
ATOM   9013  C  CA  . ALA D  3 21  ? -48.497 15.348  -21.397  1.00 193.47 ? 19   ALA D CA  1 
ATOM   9014  C  C   . ALA D  3 21  ? -47.817 14.231  -20.622  1.00 188.97 ? 19   ALA D C   1 
ATOM   9015  O  O   . ALA D  3 21  ? -48.224 13.068  -20.726  1.00 189.47 ? 19   ALA D O   1 
ATOM   9016  C  CB  . ALA D  3 21  ? -47.933 15.434  -22.817  1.00 198.87 ? 19   ALA D CB  1 
ATOM   9017  N  N   . ILE D  3 22  ? -46.768 14.562  -19.865  1.00 184.09 ? 20   ILE D N   1 
ATOM   9018  C  CA  . ILE D  3 22  ? -46.168 13.592  -18.958  1.00 178.04 ? 20   ILE D CA  1 
ATOM   9019  C  C   . ILE D  3 22  ? -47.120 13.301  -17.805  1.00 167.62 ? 20   ILE D C   1 
ATOM   9020  O  O   . ILE D  3 22  ? -47.262 12.151  -17.370  1.00 167.92 ? 20   ILE D O   1 
ATOM   9021  C  CB  . ILE D  3 22  ? -44.806 14.103  -18.451  1.00 174.88 ? 20   ILE D CB  1 
ATOM   9022  C  CG1 . ILE D  3 22  ? -43.768 14.109  -19.572  1.00 163.05 ? 20   ILE D CG1 1 
ATOM   9023  C  CG2 . ILE D  3 22  ? -44.297 13.234  -17.317  1.00 187.57 ? 20   ILE D CG2 1 
ATOM   9024  C  CD1 . ILE D  3 22  ? -43.417 12.743  -20.063  1.00 159.98 ? 20   ILE D CD1 1 
ATOM   9025  N  N   . ARG D  3 23  ? -47.787 14.340  -17.296  1.00 159.97 ? 21   ARG D N   1 
ATOM   9026  C  CA  . ARG D  3 23  ? -48.725 14.175  -16.190  1.00 161.22 ? 21   ARG D CA  1 
ATOM   9027  C  C   . ARG D  3 23  ? -49.799 13.144  -16.517  1.00 159.59 ? 21   ARG D C   1 
ATOM   9028  O  O   . ARG D  3 23  ? -50.012 12.192  -15.760  1.00 158.67 ? 21   ARG D O   1 
ATOM   9029  C  CB  . ARG D  3 23  ? -49.353 15.527  -15.853  1.00 166.26 ? 21   ARG D CB  1 
ATOM   9030  C  CG  . ARG D  3 23  ? -50.493 15.460  -14.864  1.00 170.79 ? 21   ARG D CG  1 
ATOM   9031  C  CD  . ARG D  3 23  ? -51.145 16.817  -14.702  1.00 177.26 ? 21   ARG D CD  1 
ATOM   9032  N  NE  . ARG D  3 23  ? -50.236 17.799  -14.119  1.00 183.04 ? 21   ARG D NE  1 
ATOM   9033  C  CZ  . ARG D  3 23  ? -50.154 18.061  -12.818  1.00 190.55 ? 21   ARG D CZ  1 
ATOM   9034  N  NH1 . ARG D  3 23  ? -50.925 17.411  -11.957  1.00 190.79 ? 21   ARG D NH1 1 
ATOM   9035  N  NH2 . ARG D  3 23  ? -49.300 18.972  -12.377  1.00 198.72 ? 21   ARG D NH2 1 
ATOM   9036  N  N   . GLY D  3 24  ? -50.463 13.293  -17.664  1.00 165.83 ? 22   GLY D N   1 
ATOM   9037  C  CA  . GLY D  3 24  ? -51.476 12.323  -18.035  1.00 179.60 ? 22   GLY D CA  1 
ATOM   9038  C  C   . GLY D  3 24  ? -50.914 10.981  -18.450  1.00 187.53 ? 22   GLY D C   1 
ATOM   9039  O  O   . GLY D  3 24  ? -51.640 9.981   -18.423  1.00 196.20 ? 22   GLY D O   1 
ATOM   9040  N  N   . GLN D  3 25  ? -49.628 10.936  -18.809  1.00 190.20 ? 23   GLN D N   1 
ATOM   9041  C  CA  . GLN D  3 25  ? -48.995 9.696   -19.247  1.00 185.08 ? 23   GLN D CA  1 
ATOM   9042  C  C   . GLN D  3 25  ? -48.689 8.785   -18.065  1.00 164.36 ? 23   GLN D C   1 
ATOM   9043  O  O   . GLN D  3 25  ? -49.053 7.604   -18.073  1.00 160.57 ? 23   GLN D O   1 
ATOM   9044  C  CB  . GLN D  3 25  ? -47.711 10.004  -20.020  1.00 191.59 ? 23   GLN D CB  1 
ATOM   9045  C  CG  . GLN D  3 25  ? -47.053 8.792   -20.663  1.00 193.62 ? 23   GLN D CG  1 
ATOM   9046  C  CD  . GLN D  3 25  ? -45.662 9.104   -21.186  1.00 196.95 ? 23   GLN D CD  1 
ATOM   9047  O  OE1 . GLN D  3 25  ? -45.025 10.057  -20.742  1.00 202.70 ? 23   GLN D OE1 1 
ATOM   9048  N  NE2 . GLN D  3 25  ? -45.187 8.305   -22.136  1.00 197.02 ? 23   GLN D NE2 1 
ATOM   9049  N  N   . ILE D  3 26  ? -47.991 9.311   -17.056  1.00 160.96 ? 24   ILE D N   1 
ATOM   9050  C  CA  . ILE D  3 26  ? -47.644 8.507   -15.888  1.00 160.44 ? 24   ILE D CA  1 
ATOM   9051  C  C   . ILE D  3 26  ? -48.899 7.916   -15.260  1.00 172.84 ? 24   ILE D C   1 
ATOM   9052  O  O   . ILE D  3 26  ? -48.934 6.732   -14.905  1.00 192.56 ? 24   ILE D O   1 
ATOM   9053  C  CB  . ILE D  3 26  ? -46.854 9.352   -14.874  1.00 161.89 ? 24   ILE D CB  1 
ATOM   9054  C  CG1 . ILE D  3 26  ? -45.607 9.940   -15.529  1.00 161.71 ? 24   ILE D CG1 1 
ATOM   9055  C  CG2 . ILE D  3 26  ? -46.463 8.504   -13.670  1.00 162.47 ? 24   ILE D CG2 1 
ATOM   9056  C  CD1 . ILE D  3 26  ? -44.789 10.809  -14.596  1.00 165.16 ? 24   ILE D CD1 1 
ATOM   9057  N  N   . LEU D  3 27  ? -49.954 8.727   -15.128  1.00 166.95 ? 25   LEU D N   1 
ATOM   9058  C  CA  . LEU D  3 27  ? -51.190 8.248   -14.518  1.00 174.28 ? 25   LEU D CA  1 
ATOM   9059  C  C   . LEU D  3 27  ? -51.853 7.161   -15.352  1.00 183.90 ? 25   LEU D C   1 
ATOM   9060  O  O   . LEU D  3 27  ? -52.504 6.269   -14.797  1.00 200.79 ? 25   LEU D O   1 
ATOM   9061  C  CB  . LEU D  3 27  ? -52.154 9.411   -14.305  1.00 185.44 ? 25   LEU D CB  1 
ATOM   9062  C  CG  . LEU D  3 27  ? -51.654 10.466  -13.323  1.00 181.33 ? 25   LEU D CG  1 
ATOM   9063  C  CD1 . LEU D  3 27  ? -52.688 11.565  -13.151  1.00 196.00 ? 25   LEU D CD1 1 
ATOM   9064  C  CD2 . LEU D  3 27  ? -51.321 9.812   -11.997  1.00 171.87 ? 25   LEU D CD2 1 
ATOM   9065  N  N   . SER D  3 28  ? -51.717 7.220   -16.676  1.00 176.19 ? 26   SER D N   1 
ATOM   9066  C  CA  . SER D  3 28  ? -52.328 6.203   -17.521  1.00 178.51 ? 26   SER D CA  1 
ATOM   9067  C  C   . SER D  3 28  ? -51.525 4.906   -17.529  1.00 167.34 ? 26   SER D C   1 
ATOM   9068  O  O   . SER D  3 28  ? -52.111 3.818   -17.598  1.00 172.07 ? 26   SER D O   1 
ATOM   9069  C  CB  . SER D  3 28  ? -52.495 6.737   -18.943  1.00 202.41 ? 26   SER D CB  1 
ATOM   9070  O  OG  . SER D  3 28  ? -51.237 7.018   -19.533  1.00 205.10 ? 26   SER D OG  1 
ATOM   9071  N  N   . LYS D  3 29  ? -50.196 4.991   -17.442  1.00 171.34 ? 27   LYS D N   1 
ATOM   9072  C  CA  . LYS D  3 29  ? -49.396 3.774   -17.422  1.00 171.10 ? 27   LYS D CA  1 
ATOM   9073  C  C   . LYS D  3 29  ? -49.577 3.020   -16.116  1.00 171.42 ? 27   LYS D C   1 
ATOM   9074  O  O   . LYS D  3 29  ? -49.513 1.786   -16.097  1.00 183.58 ? 27   LYS D O   1 
ATOM   9075  C  CB  . LYS D  3 29  ? -47.923 4.110   -17.639  1.00 177.16 ? 27   LYS D CB  1 
ATOM   9076  C  CG  . LYS D  3 29  ? -47.617 4.635   -19.021  1.00 180.54 ? 27   LYS D CG  1 
ATOM   9077  C  CD  . LYS D  3 29  ? -46.145 4.940   -19.168  1.00 175.08 ? 27   LYS D CD  1 
ATOM   9078  C  CE  . LYS D  3 29  ? -45.815 5.286   -20.600  1.00 183.92 ? 27   LYS D CE  1 
ATOM   9079  N  NZ  . LYS D  3 29  ? -44.363 5.500   -20.803  1.00 193.85 ? 27   LYS D NZ  1 
ATOM   9080  N  N   . LEU D  3 30  ? -49.829 3.735   -15.029  1.00 171.59 ? 28   LEU D N   1 
ATOM   9081  C  CA  . LEU D  3 30  ? -50.120 3.120   -13.747  1.00 179.72 ? 28   LEU D CA  1 
ATOM   9082  C  C   . LEU D  3 30  ? -51.588 2.753   -13.619  1.00 183.78 ? 28   LEU D C   1 
ATOM   9083  O  O   . LEU D  3 30  ? -51.994 2.224   -12.577  1.00 178.87 ? 28   LEU D O   1 
ATOM   9084  C  CB  . LEU D  3 30  ? -49.719 4.067   -12.608  1.00 188.09 ? 28   LEU D CB  1 
ATOM   9085  C  CG  . LEU D  3 30  ? -48.249 4.487   -12.531  1.00 188.78 ? 28   LEU D CG  1 
ATOM   9086  C  CD1 . LEU D  3 30  ? -48.025 5.523   -11.439  1.00 191.95 ? 28   LEU D CD1 1 
ATOM   9087  C  CD2 . LEU D  3 30  ? -47.358 3.288   -12.307  1.00 190.44 ? 28   LEU D CD2 1 
ATOM   9088  N  N   . ARG D  3 31  ? -52.383 3.031   -14.657  1.00 185.59 ? 29   ARG D N   1 
ATOM   9089  C  CA  . ARG D  3 31  ? -53.827 2.794   -14.661  1.00 195.58 ? 29   ARG D CA  1 
ATOM   9090  C  C   . ARG D  3 31  ? -54.505 3.508   -13.492  1.00 200.29 ? 29   ARG D C   1 
ATOM   9091  O  O   . ARG D  3 31  ? -55.383 2.959   -12.821  1.00 199.74 ? 29   ARG D O   1 
ATOM   9092  C  CB  . ARG D  3 31  ? -54.141 1.296   -14.656  1.00 187.96 ? 29   ARG D CB  1 
ATOM   9093  C  CG  . ARG D  3 31  ? -55.514 0.941   -15.205  1.00 186.22 ? 29   ARG D CG  1 
ATOM   9094  C  CD  . ARG D  3 31  ? -55.803 -0.531  -14.992  1.00 191.30 ? 29   ARG D CD  1 
ATOM   9095  N  NE  . ARG D  3 31  ? -54.919 -1.374  -15.785  1.00 187.37 ? 29   ARG D NE  1 
ATOM   9096  C  CZ  . ARG D  3 31  ? -55.269 -1.945  -16.930  1.00 189.10 ? 29   ARG D CZ  1 
ATOM   9097  N  NH1 . ARG D  3 31  ? -56.493 -1.771  -17.408  1.00 196.46 ? 29   ARG D NH1 1 
ATOM   9098  N  NH2 . ARG D  3 31  ? -54.400 -2.697  -17.588  1.00 190.66 ? 29   ARG D NH2 1 
ATOM   9099  N  N   . LEU D  3 32  ? -54.092 4.746   -13.243  1.00 199.28 ? 30   LEU D N   1 
ATOM   9100  C  CA  . LEU D  3 32  ? -54.610 5.548   -12.147  1.00 183.28 ? 30   LEU D CA  1 
ATOM   9101  C  C   . LEU D  3 32  ? -55.304 6.787   -12.694  1.00 200.14 ? 30   LEU D C   1 
ATOM   9102  O  O   . LEU D  3 32  ? -54.909 7.335   -13.728  1.00 210.58 ? 30   LEU D O   1 
ATOM   9103  C  CB  . LEU D  3 32  ? -53.485 5.963   -11.197  1.00 187.83 ? 30   LEU D CB  1 
ATOM   9104  C  CG  . LEU D  3 32  ? -52.862 4.842   -10.362  1.00 206.49 ? 30   LEU D CG  1 
ATOM   9105  C  CD1 . LEU D  3 32  ? -51.748 5.379   -9.474   1.00 193.67 ? 30   LEU D CD1 1 
ATOM   9106  C  CD2 . LEU D  3 32  ? -53.922 4.137   -9.530   1.00 224.97 ? 30   LEU D CD2 1 
ATOM   9107  N  N   . ALA D  3 33  ? -56.358 7.218   -12.002  1.00 214.13 ? 31   ALA D N   1 
ATOM   9108  C  CA  . ALA D  3 33  ? -57.049 8.457   -12.338  1.00 215.91 ? 31   ALA D CA  1 
ATOM   9109  C  C   . ALA D  3 33  ? -56.576 9.643   -11.515  1.00 199.57 ? 31   ALA D C   1 
ATOM   9110  O  O   . ALA D  3 33  ? -56.553 10.770  -12.022  1.00 197.18 ? 31   ALA D O   1 
ATOM   9111  C  CB  . ALA D  3 33  ? -58.563 8.290   -12.158  1.00 221.00 ? 31   ALA D CB  1 
ATOM   9112  N  N   . SER D  3 34  ? -56.191 9.414   -10.263  1.00 195.37 ? 32   SER D N   1 
ATOM   9113  C  CA  . SER D  3 34  ? -55.722 10.463  -9.374   1.00 205.37 ? 32   SER D CA  1 
ATOM   9114  C  C   . SER D  3 34  ? -54.633 9.885   -8.485   1.00 201.86 ? 32   SER D C   1 
ATOM   9115  O  O   . SER D  3 34  ? -54.631 8.676   -8.220   1.00 195.09 ? 32   SER D O   1 
ATOM   9116  C  CB  . SER D  3 34  ? -56.869 11.030  -8.523   1.00 238.20 ? 32   SER D CB  1 
ATOM   9117  O  OG  . SER D  3 34  ? -57.461 10.024  -7.720   1.00 256.17 ? 32   SER D OG  1 
ATOM   9118  N  N   . PRO D  3 35  ? -53.694 10.708  -8.025   1.00 206.04 ? 33   PRO D N   1 
ATOM   9119  C  CA  . PRO D  3 35  ? -52.618 10.216  -7.145   1.00 214.30 ? 33   PRO D CA  1 
ATOM   9120  C  C   . PRO D  3 35  ? -53.174 9.595   -5.875   1.00 229.92 ? 33   PRO D C   1 
ATOM   9121  O  O   . PRO D  3 35  ? -54.180 10.073  -5.330   1.00 234.80 ? 33   PRO D O   1 
ATOM   9122  C  CB  . PRO D  3 35  ? -51.813 11.487  -6.836   1.00 206.36 ? 33   PRO D CB  1 
ATOM   9123  C  CG  . PRO D  3 35  ? -52.062 12.376  -8.009   1.00 201.06 ? 33   PRO D CG  1 
ATOM   9124  C  CD  . PRO D  3 35  ? -53.483 12.111  -8.423   1.00 204.07 ? 33   PRO D CD  1 
ATOM   9125  N  N   . PRO D  3 36  ? -52.553 8.522   -5.383   1.00 236.25 ? 34   PRO D N   1 
ATOM   9126  C  CA  . PRO D  3 36  ? -53.064 7.842   -4.186   1.00 232.06 ? 34   PRO D CA  1 
ATOM   9127  C  C   . PRO D  3 36  ? -52.838 8.666   -2.926   1.00 215.99 ? 34   PRO D C   1 
ATOM   9128  O  O   . PRO D  3 36  ? -52.197 9.719   -2.931   1.00 215.80 ? 34   PRO D O   1 
ATOM   9129  C  CB  . PRO D  3 36  ? -52.262 6.538   -4.148   1.00 230.58 ? 34   PRO D CB  1 
ATOM   9130  C  CG  . PRO D  3 36  ? -50.981 6.876   -4.832   1.00 230.23 ? 34   PRO D CG  1 
ATOM   9131  C  CD  . PRO D  3 36  ? -51.327 7.887   -5.899   1.00 232.07 ? 34   PRO D CD  1 
ATOM   9132  N  N   . SER D  3 37  ? -53.372 8.153   -1.822   1.00 208.20 ? 35   SER D N   1 
ATOM   9133  C  CA  . SER D  3 37  ? -53.286 8.841   -0.545   1.00 210.94 ? 35   SER D CA  1 
ATOM   9134  C  C   . SER D  3 37  ? -51.970 8.514   0.142    1.00 211.22 ? 35   SER D C   1 
ATOM   9135  O  O   . SER D  3 37  ? -51.527 7.363   0.161    1.00 209.38 ? 35   SER D O   1 
ATOM   9136  C  CB  . SER D  3 37  ? -54.453 8.456   0.366    1.00 217.21 ? 35   SER D CB  1 
ATOM   9137  O  OG  . SER D  3 37  ? -54.373 7.090   0.735    1.00 214.71 ? 35   SER D OG  1 
ATOM   9138  N  N   . GLN D  3 38  ? -51.367 9.540   0.731    1.00 231.00 ? 36   GLN D N   1 
ATOM   9139  C  CA  . GLN D  3 38  ? -50.066 9.428   1.375    1.00 247.11 ? 36   GLN D CA  1 
ATOM   9140  C  C   . GLN D  3 38  ? -50.172 9.725   2.871    1.00 250.50 ? 36   GLN D C   1 
ATOM   9141  O  O   . GLN D  3 38  ? -49.157 9.919   3.546    1.00 244.38 ? 36   GLN D O   1 
ATOM   9142  C  CB  . GLN D  3 38  ? -49.071 10.361  0.674    1.00 259.80 ? 36   GLN D CB  1 
ATOM   9143  C  CG  . GLN D  3 38  ? -47.589 10.081  0.911    1.00 264.90 ? 36   GLN D CG  1 
ATOM   9144  C  CD  . GLN D  3 38  ? -46.695 11.125  0.257    1.00 266.33 ? 36   GLN D CD  1 
ATOM   9145  O  OE1 . GLN D  3 38  ? -47.183 12.083  -0.343   1.00 268.65 ? 36   GLN D OE1 1 
ATOM   9146  N  NE2 . GLN D  3 38  ? -45.383 10.940  0.364    1.00 265.46 ? 36   GLN D NE2 1 
ATOM   9147  N  N   . GLY D  3 39  ? -51.392 9.743   3.402    1.00 241.77 ? 37   GLY D N   1 
ATOM   9148  C  CA  . GLY D  3 39  ? -51.623 9.921   4.817    1.00 243.59 ? 37   GLY D CA  1 
ATOM   9149  C  C   . GLY D  3 39  ? -51.766 8.563   5.458    1.00 243.84 ? 37   GLY D C   1 
ATOM   9150  O  O   . GLY D  3 39  ? -51.864 8.441   6.685    1.00 240.14 ? 37   GLY D O   1 
ATOM   9151  N  N   . GLU D  3 40  ? -51.797 7.533   4.615    1.00 249.09 ? 38   GLU D N   1 
ATOM   9152  C  CA  . GLU D  3 40  ? -51.771 6.138   5.030    1.00 241.28 ? 38   GLU D CA  1 
ATOM   9153  C  C   . GLU D  3 40  ? -50.376 5.551   4.801    1.00 240.53 ? 38   GLU D C   1 
ATOM   9154  O  O   . GLU D  3 40  ? -50.164 4.347   4.987    1.00 235.73 ? 38   GLU D O   1 
ATOM   9155  C  CB  . GLU D  3 40  ? -52.890 5.345   4.296    1.00 222.13 ? 38   GLU D CB  1 
ATOM   9156  C  CG  . GLU D  3 40  ? -54.431 5.824   4.634    1.00 206.38 ? 38   GLU D CG  1 
ATOM   9157  C  CD  . GLU D  3 40  ? -55.670 5.308   3.691    1.00 197.68 ? 38   GLU D CD  1 
ATOM   9158  O  OE1 . GLU D  3 40  ? -55.591 5.207   2.378    1.00 189.20 ? 38   GLU D OE1 1 
ATOM   9159  O  OE2 . GLU D  3 40  ? -56.758 5.070   4.342    1.00 201.16 ? 38   GLU D OE2 1 
ATOM   9160  N  N   . VAL D  3 41  ? -49.403 6.406   4.494    1.00 240.41 ? 39   VAL D N   1 
ATOM   9161  C  CA  . VAL D  3 41  ? -48.017 6.033   4.212    1.00 236.01 ? 39   VAL D CA  1 
ATOM   9162  C  C   . VAL D  3 41  ? -47.192 6.672   5.324    1.00 247.06 ? 39   VAL D C   1 
ATOM   9163  O  O   . VAL D  3 41  ? -47.458 7.826   5.691    1.00 247.19 ? 39   VAL D O   1 
ATOM   9164  C  CB  . VAL D  3 41  ? -47.574 6.525   2.821    1.00 235.00 ? 39   VAL D CB  1 
ATOM   9165  C  CG1 . VAL D  3 41  ? -46.121 6.155   2.513    1.00 248.86 ? 39   VAL D CG1 1 
ATOM   9166  C  CG2 . VAL D  3 41  ? -48.509 6.013   1.743    1.00 226.66 ? 39   VAL D CG2 1 
ATOM   9167  N  N   . PRO D  3 42  ? -46.194 5.998   5.888    1.00 262.74 ? 40   PRO D N   1 
ATOM   9168  C  CA  . PRO D  3 42  ? -45.434 6.617   6.973    1.00 280.63 ? 40   PRO D CA  1 
ATOM   9169  C  C   . PRO D  3 42  ? -44.266 7.413   6.423    1.00 282.90 ? 40   PRO D C   1 
ATOM   9170  O  O   . PRO D  3 42  ? -43.433 6.878   5.674    1.00 262.24 ? 40   PRO D O   1 
ATOM   9171  C  CB  . PRO D  3 42  ? -44.954 5.418   7.804    1.00 276.73 ? 40   PRO D CB  1 
ATOM   9172  C  CG  . PRO D  3 42  ? -45.009 4.225   6.865    1.00 259.68 ? 40   PRO D CG  1 
ATOM   9173  C  CD  . PRO D  3 42  ? -45.736 4.623   5.608    1.00 252.53 ? 40   PRO D CD  1 
ATOM   9174  N  N   . PRO D  3 43  ? -44.170 8.699   6.774    1.00 289.41 ? 41   PRO D N   1 
ATOM   9175  C  CA  . PRO D  3 43  ? -43.050 9.516   6.288    1.00 286.12 ? 41   PRO D CA  1 
ATOM   9176  C  C   . PRO D  3 43  ? -41.771 9.197   7.049    1.00 294.83 ? 41   PRO D C   1 
ATOM   9177  O  O   . PRO D  3 43  ? -41.758 9.170   8.282    1.00 291.69 ? 41   PRO D O   1 
ATOM   9178  C  CB  . PRO D  3 43  ? -43.515 10.955  6.556    1.00 283.44 ? 41   PRO D CB  1 
ATOM   9179  C  CG  . PRO D  3 43  ? -44.450 10.829  7.707    1.00 277.39 ? 41   PRO D CG  1 
ATOM   9180  C  CD  . PRO D  3 43  ? -45.145 9.496   7.542    1.00 276.89 ? 41   PRO D CD  1 
ATOM   9181  N  N   . GLY D  3 44  ? -40.695 8.956   6.305    1.00 247.32 ? 42   GLY D N   1 
ATOM   9182  C  CA  . GLY D  3 44  ? -39.395 8.778   6.904    1.00 255.87 ? 42   GLY D CA  1 
ATOM   9183  C  C   . GLY D  3 44  ? -38.707 7.474   6.550    1.00 240.29 ? 42   GLY D C   1 
ATOM   9184  O  O   . GLY D  3 44  ? -37.663 7.465   5.893    1.00 231.28 ? 42   GLY D O   1 
ATOM   9185  N  N   . PRO D  3 45  ? -39.287 6.343   6.961    1.00 233.29 ? 43   PRO D N   1 
ATOM   9186  C  CA  . PRO D  3 45  ? -38.618 5.049   6.752    1.00 235.12 ? 43   PRO D CA  1 
ATOM   9187  C  C   . PRO D  3 45  ? -38.578 4.683   5.277    1.00 245.45 ? 43   PRO D C   1 
ATOM   9188  O  O   . PRO D  3 45  ? -39.613 4.597   4.614    1.00 254.04 ? 43   PRO D O   1 
ATOM   9189  C  CB  . PRO D  3 45  ? -39.480 4.067   7.551    1.00 232.76 ? 43   PRO D CB  1 
ATOM   9190  C  CG  . PRO D  3 45  ? -40.814 4.717   7.638    1.00 225.58 ? 43   PRO D CG  1 
ATOM   9191  C  CD  . PRO D  3 45  ? -40.560 6.189   7.688    1.00 231.03 ? 43   PRO D CD  1 
ATOM   9192  N  N   . LEU D  3 46  ? -37.369 4.475   4.765    1.00 247.39 ? 44   LEU D N   1 
ATOM   9193  C  CA  . LEU D  3 46  ? -37.166 3.995   3.398    1.00 237.71 ? 44   LEU D CA  1 
ATOM   9194  C  C   . LEU D  3 46  ? -36.159 2.855   3.427    1.00 230.63 ? 44   LEU D C   1 
ATOM   9195  O  O   . LEU D  3 46  ? -34.951 3.096   3.596    1.00 244.56 ? 44   LEU D O   1 
ATOM   9196  C  CB  . LEU D  3 46  ? -36.708 5.101   2.458    1.00 234.53 ? 44   LEU D CB  1 
ATOM   9197  C  CG  . LEU D  3 46  ? -37.771 6.178   2.244    1.00 221.25 ? 44   LEU D CG  1 
ATOM   9198  C  CD1 . LEU D  3 46  ? -37.143 7.494   1.777    1.00 212.61 ? 44   LEU D CD1 1 
ATOM   9199  C  CD2 . LEU D  3 46  ? -38.887 5.691   1.311    1.00 198.11 ? 44   LEU D CD2 1 
ATOM   9200  N  N   . PRO D  3 47  ? -36.620 1.611   3.295    1.00 207.95 ? 45   PRO D N   1 
ATOM   9201  C  CA  . PRO D  3 47  ? -35.721 0.460   3.448    1.00 212.75 ? 45   PRO D CA  1 
ATOM   9202  C  C   . PRO D  3 47  ? -34.632 0.439   2.387    1.00 216.99 ? 45   PRO D C   1 
ATOM   9203  O  O   . PRO D  3 47  ? -34.849 0.828   1.237    1.00 229.79 ? 45   PRO D O   1 
ATOM   9204  C  CB  . PRO D  3 47  ? -36.661 -0.743  3.294    1.00 203.71 ? 45   PRO D CB  1 
ATOM   9205  C  CG  . PRO D  3 47  ? -37.800 -0.215  2.471    1.00 185.85 ? 45   PRO D CG  1 
ATOM   9206  C  CD  . PRO D  3 47  ? -37.984 1.206   2.915    1.00 179.91 ? 45   PRO D CD  1 
ATOM   9207  N  N   . GLU D  3 48  ? -33.442 -0.013  2.787    1.00 204.23 ? 46   GLU D N   1 
ATOM   9208  C  CA  . GLU D  3 48  ? -32.366 -0.195  1.825    1.00 195.10 ? 46   GLU D CA  1 
ATOM   9209  C  C   . GLU D  3 48  ? -32.577 -1.428  0.962    1.00 186.62 ? 46   GLU D C   1 
ATOM   9210  O  O   . GLU D  3 48  ? -31.759 -1.693  0.074    1.00 188.58 ? 46   GLU D O   1 
ATOM   9211  C  CB  . GLU D  3 48  ? -31.007 -0.282  2.541    1.00 186.11 ? 46   GLU D CB  1 
ATOM   9212  C  CG  . GLU D  3 48  ? -30.537 1.011   3.196    1.00 182.85 ? 46   GLU D CG  1 
ATOM   9213  C  CD  . GLU D  3 48  ? -29.079 0.949   3.601    1.00 182.50 ? 46   GLU D CD  1 
ATOM   9214  O  OE1 . GLU D  3 48  ? -28.515 -0.165  3.630    1.00 175.96 ? 46   GLU D OE1 1 
ATOM   9215  O  OE2 . GLU D  3 48  ? -28.496 2.017   3.882    1.00 190.23 ? 46   GLU D OE2 1 
ATOM   9216  N  N   . ALA D  3 49  ? -33.656 -2.181  1.202    1.00 176.07 ? 47   ALA D N   1 
ATOM   9217  C  CA  . ALA D  3 49  ? -34.004 -3.313  0.352    1.00 182.09 ? 47   ALA D CA  1 
ATOM   9218  C  C   . ALA D  3 49  ? -34.639 -2.838  -0.949   1.00 179.12 ? 47   ALA D C   1 
ATOM   9219  O  O   . ALA D  3 49  ? -34.416 -3.435  -2.009   1.00 185.38 ? 47   ALA D O   1 
ATOM   9220  C  CB  . ALA D  3 49  ? -34.938 -4.274  1.091    1.00 171.26 ? 47   ALA D CB  1 
ATOM   9221  N  N   . VAL D  3 50  ? -35.445 -1.775  -0.883   1.00 170.01 ? 48   VAL D N   1 
ATOM   9222  C  CA  . VAL D  3 50  ? -36.006 -1.203  -2.099   1.00 170.59 ? 48   VAL D CA  1 
ATOM   9223  C  C   . VAL D  3 50  ? -35.017 -0.259  -2.763   1.00 174.33 ? 48   VAL D C   1 
ATOM   9224  O  O   . VAL D  3 50  ? -35.160 0.045   -3.953   1.00 180.93 ? 48   VAL D O   1 
ATOM   9225  C  CB  . VAL D  3 50  ? -37.327 -0.475  -1.808   1.00 165.23 ? 48   VAL D CB  1 
ATOM   9226  C  CG1 . VAL D  3 50  ? -38.299 -1.407  -1.098   1.00 162.43 ? 48   VAL D CG1 1 
ATOM   9227  C  CG2 . VAL D  3 50  ? -37.082 0.772   -0.990   1.00 169.83 ? 48   VAL D CG2 1 
ATOM   9228  N  N   . LEU D  3 51  ? -34.015 0.213   -2.018   1.00 172.53 ? 49   LEU D N   1 
ATOM   9229  C  CA  . LEU D  3 51  ? -32.958 1.005   -2.628   1.00 172.42 ? 49   LEU D CA  1 
ATOM   9230  C  C   . LEU D  3 51  ? -32.024 0.129   -3.449   1.00 183.24 ? 49   LEU D C   1 
ATOM   9231  O  O   . LEU D  3 51  ? -31.439 0.601   -4.428   1.00 201.89 ? 49   LEU D O   1 
ATOM   9232  C  CB  . LEU D  3 51  ? -32.181 1.764   -1.551   1.00 174.23 ? 49   LEU D CB  1 
ATOM   9233  C  CG  . LEU D  3 51  ? -32.908 2.925   -0.862   1.00 183.72 ? 49   LEU D CG  1 
ATOM   9234  C  CD1 . LEU D  3 51  ? -31.974 3.653   0.095    1.00 208.41 ? 49   LEU D CD1 1 
ATOM   9235  C  CD2 . LEU D  3 51  ? -33.488 3.894   -1.877   1.00 181.98 ? 49   LEU D CD2 1 
ATOM   9236  N  N   . ALA D  3 52  ? -31.874 -1.143  -3.071   1.00 178.26 ? 50   ALA D N   1 
ATOM   9237  C  CA  . ALA D  3 52  ? -31.093 -2.067  -3.887   1.00 169.21 ? 50   ALA D CA  1 
ATOM   9238  C  C   . ALA D  3 52  ? -31.831 -2.448  -5.163   1.00 166.62 ? 50   ALA D C   1 
ATOM   9239  O  O   . ALA D  3 52  ? -31.194 -2.711  -6.189   1.00 168.00 ? 50   ALA D O   1 
ATOM   9240  C  CB  . ALA D  3 52  ? -30.736 -3.316  -3.080   1.00 167.83 ? 50   ALA D CB  1 
ATOM   9241  N  N   . LEU D  3 53  ? -33.166 -2.495  -5.115   1.00 154.56 ? 51   LEU D N   1 
ATOM   9242  C  CA  . LEU D  3 53  ? -33.953 -2.716  -6.325   1.00 154.96 ? 51   LEU D CA  1 
ATOM   9243  C  C   . LEU D  3 53  ? -33.806 -1.546  -7.285   1.00 156.74 ? 51   LEU D C   1 
ATOM   9244  O  O   . LEU D  3 53  ? -33.574 -1.734  -8.485   1.00 168.83 ? 51   LEU D O   1 
ATOM   9245  C  CB  . LEU D  3 53  ? -35.425 -2.920  -5.965   1.00 154.25 ? 51   LEU D CB  1 
ATOM   9246  C  CG  . LEU D  3 53  ? -35.940 -4.348  -5.823   1.00 153.75 ? 51   LEU D CG  1 
ATOM   9247  C  CD1 . LEU D  3 53  ? -37.321 -4.340  -5.192   1.00 166.15 ? 51   LEU D CD1 1 
ATOM   9248  C  CD2 . LEU D  3 53  ? -35.984 -5.003  -7.189   1.00 153.56 ? 51   LEU D CD2 1 
ATOM   9249  N  N   . TYR D  3 54  ? -33.950 -0.326  -6.769   1.00 155.40 ? 52   TYR D N   1 
ATOM   9250  C  CA  . TYR D  3 54  ? -33.854 0.860   -7.605   1.00 166.90 ? 52   TYR D CA  1 
ATOM   9251  C  C   . TYR D  3 54  ? -32.442 1.041   -8.155   1.00 189.67 ? 52   TYR D C   1 
ATOM   9252  O  O   . TYR D  3 54  ? -32.272 1.536   -9.275   1.00 209.35 ? 52   TYR D O   1 
ATOM   9253  C  CB  . TYR D  3 54  ? -34.299 2.077   -6.792   1.00 164.07 ? 52   TYR D CB  1 
ATOM   9254  C  CG  . TYR D  3 54  ? -34.420 3.370   -7.564   1.00 169.08 ? 52   TYR D CG  1 
ATOM   9255  C  CD1 . TYR D  3 54  ? -35.481 3.587   -8.436   1.00 166.25 ? 52   TYR D CD1 1 
ATOM   9256  C  CD2 . TYR D  3 54  ? -33.482 4.382   -7.409   1.00 176.30 ? 52   TYR D CD2 1 
ATOM   9257  C  CE1 . TYR D  3 54  ? -35.597 4.772   -9.136   1.00 172.58 ? 52   TYR D CE1 1 
ATOM   9258  C  CE2 . TYR D  3 54  ? -33.592 5.569   -8.105   1.00 181.73 ? 52   TYR D CE2 1 
ATOM   9259  C  CZ  . TYR D  3 54  ? -34.651 5.758   -8.967   1.00 181.84 ? 52   TYR D CZ  1 
ATOM   9260  O  OH  . TYR D  3 54  ? -34.768 6.939   -9.665   1.00 191.16 ? 52   TYR D OH  1 
ATOM   9261  N  N   . ASN D  3 55  ? -31.421 0.630   -7.394   1.00 190.00 ? 53   ASN D N   1 
ATOM   9262  C  CA  . ASN D  3 55  ? -30.039 0.765   -7.854   1.00 191.82 ? 53   ASN D CA  1 
ATOM   9263  C  C   . ASN D  3 55  ? -29.680 -0.269  -8.909   1.00 182.39 ? 53   ASN D C   1 
ATOM   9264  O  O   . ASN D  3 55  ? -28.806 -0.017  -9.745   1.00 170.21 ? 53   ASN D O   1 
ATOM   9265  C  CB  . ASN D  3 55  ? -29.078 0.629   -6.677   1.00 210.31 ? 53   ASN D CB  1 
ATOM   9266  C  CG  . ASN D  3 55  ? -29.073 1.840   -5.780   1.00 220.38 ? 53   ASN D CG  1 
ATOM   9267  O  OD1 . ASN D  3 55  ? -29.817 2.800   -6.000   1.00 194.67 ? 53   ASN D OD1 1 
ATOM   9268  N  ND2 . ASN D  3 55  ? -28.251 1.795   -4.744   1.00 278.20 ? 53   ASN D ND2 1 
ATOM   9269  N  N   . SER D  3 56  ? -30.350 -1.417  -8.911   1.00 181.28 ? 54   SER D N   1 
ATOM   9270  C  CA  . SER D  3 56  ? -30.030 -2.462  -9.870   1.00 172.81 ? 54   SER D CA  1 
ATOM   9271  C  C   . SER D  3 56  ? -30.713 -2.256  -11.212  1.00 186.61 ? 54   SER D C   1 
ATOM   9272  O  O   . SER D  3 56  ? -30.245 -2.801  -12.217  1.00 197.90 ? 54   SER D O   1 
ATOM   9273  C  CB  . SER D  3 56  ? -30.403 -3.830  -9.292   1.00 171.00 ? 54   SER D CB  1 
ATOM   9274  O  OG  . SER D  3 56  ? -31.767 -3.855  -8.914   1.00 192.32 ? 54   SER D OG  1 
ATOM   9275  N  N   . THR D  3 57  ? -31.783 -1.461  -11.261  1.00 182.71 ? 55   THR D N   1 
ATOM   9276  C  CA  . THR D  3 57  ? -32.446 -1.211  -12.534  1.00 181.71 ? 55   THR D CA  1 
ATOM   9277  C  C   . THR D  3 57  ? -31.708 -0.149  -13.333  1.00 183.78 ? 55   THR D C   1 
ATOM   9278  O  O   . THR D  3 57  ? -31.642 -0.225  -14.565  1.00 203.14 ? 55   THR D O   1 
ATOM   9279  C  CB  . THR D  3 57  ? -33.894 -0.776  -12.295  1.00 166.33 ? 55   THR D CB  1 
ATOM   9280  O  OG1 . THR D  3 57  ? -33.913 0.341   -11.395  1.00 166.05 ? 55   THR D OG1 1 
ATOM   9281  C  CG2 . THR D  3 57  ? -34.711 -1.915  -11.703  1.00 157.01 ? 55   THR D CG2 1 
ATOM   9282  N  N   . ARG D  3 58  ? -31.156 0.845   -12.643  1.00 158.54 ? 56   ARG D N   1 
ATOM   9283  C  CA  . ARG D  3 58  ? -30.343 1.889   -13.247  1.00 167.46 ? 56   ARG D CA  1 
ATOM   9284  C  C   . ARG D  3 58  ? -28.910 1.447   -13.509  1.00 168.49 ? 56   ARG D C   1 
ATOM   9285  O  O   . ARG D  3 58  ? -28.170 2.162   -14.194  1.00 177.40 ? 56   ARG D O   1 
ATOM   9286  C  CB  . ARG D  3 58  ? -30.366 3.129   -12.351  1.00 170.93 ? 56   ARG D CB  1 
ATOM   9287  C  CG  . ARG D  3 58  ? -31.762 3.715   -12.201  1.00 170.80 ? 56   ARG D CG  1 
ATOM   9288  C  CD  . ARG D  3 58  ? -31.724 5.153   -11.743  1.00 178.80 ? 56   ARG D CD  1 
ATOM   9289  N  NE  . ARG D  3 58  ? -31.131 5.264   -10.418  1.00 183.02 ? 56   ARG D NE  1 
ATOM   9290  C  CZ  . ARG D  3 58  ? -29.907 5.729   -10.190  1.00 190.17 ? 56   ARG D CZ  1 
ATOM   9291  N  NH1 . ARG D  3 58  ? -29.150 6.128   -11.203  1.00 193.60 ? 56   ARG D NH1 1 
ATOM   9292  N  NH2 . ARG D  3 58  ? -29.442 5.791   -8.951   1.00 199.83 ? 56   ARG D NH2 1 
ATOM   9293  N  N   . ASP D  3 59  ? -28.505 0.291   -12.987  1.00 179.83 ? 57   ASP D N   1 
ATOM   9294  C  CA  . ASP D  3 59  ? -27.109 -0.126  -13.033  1.00 185.01 ? 57   ASP D CA  1 
ATOM   9295  C  C   . ASP D  3 59  ? -26.683 -0.666  -14.398  1.00 186.40 ? 57   ASP D C   1 
ATOM   9296  O  O   . ASP D  3 59  ? -25.526 -0.478  -14.797  1.00 184.25 ? 57   ASP D O   1 
ATOM   9297  C  CB  . ASP D  3 59  ? -26.892 -1.186  -11.952  1.00 199.70 ? 57   ASP D CB  1 
ATOM   9298  C  CG  . ASP D  3 59  ? -25.433 -1.399  -11.613  1.00 227.59 ? 57   ASP D CG  1 
ATOM   9299  O  OD1 . ASP D  3 59  ? -24.550 -0.956  -12.375  1.00 249.65 ? 57   ASP D OD1 1 
ATOM   9300  O  OD2 . ASP D  3 59  ? -25.170 -2.015  -10.559  1.00 227.25 ? 57   ASP D OD2 1 
ATOM   9301  N  N   . ARG D  3 60  ? -27.583 -1.323  -15.131  1.00 201.63 ? 58   ARG D N   1 
ATOM   9302  C  CA  . ARG D  3 60  ? -27.203 -2.085  -16.319  1.00 210.98 ? 58   ARG D CA  1 
ATOM   9303  C  C   . ARG D  3 60  ? -26.593 -1.234  -17.431  1.00 223.22 ? 58   ARG D C   1 
ATOM   9304  O  O   . ARG D  3 60  ? -27.310 -0.694  -18.282  1.00 232.61 ? 58   ARG D O   1 
ATOM   9305  C  CB  . ARG D  3 60  ? -28.417 -2.849  -16.859  1.00 229.19 ? 58   ARG D CB  1 
ATOM   9306  C  CG  . ARG D  3 60  ? -29.694 -2.021  -16.984  1.00 231.27 ? 58   ARG D CG  1 
ATOM   9307  C  CD  . ARG D  3 60  ? -30.728 -2.723  -17.854  1.00 222.01 ? 58   ARG D CD  1 
ATOM   9308  N  NE  . ARG D  3 60  ? -31.946 -1.929  -17.995  1.00 211.07 ? 58   ARG D NE  1 
ATOM   9309  C  CZ  . ARG D  3 60  ? -33.105 -2.404  -18.439  1.00 200.64 ? 58   ARG D CZ  1 
ATOM   9310  N  NH1 . ARG D  3 60  ? -33.216 -3.680  -18.783  1.00 202.51 ? 58   ARG D NH1 1 
ATOM   9311  N  NH2 . ARG D  3 60  ? -34.158 -1.603  -18.531  1.00 187.97 ? 58   ARG D NH2 1 
ATOM   9312  N  N   . VAL D  3 61  ? -25.266 -1.110  -17.441  1.00 218.27 ? 59   VAL D N   1 
ATOM   9313  C  CA  . VAL D  3 61  ? -24.584 -0.602  -18.625  1.00 237.16 ? 59   VAL D CA  1 
ATOM   9314  C  C   . VAL D  3 61  ? -24.150 -1.751  -19.531  1.00 236.55 ? 59   VAL D C   1 
ATOM   9315  O  O   . VAL D  3 61  ? -23.906 -1.534  -20.728  1.00 244.50 ? 59   VAL D O   1 
ATOM   9316  C  CB  . VAL D  3 61  ? -23.381 0.283   -18.239  1.00 240.64 ? 59   VAL D CB  1 
ATOM   9317  C  CG1 . VAL D  3 61  ? -22.820 1.018   -19.460  1.00 243.54 ? 59   VAL D CG1 1 
ATOM   9318  C  CG2 . VAL D  3 61  ? -23.780 1.283   -17.167  1.00 229.93 ? 59   VAL D CG2 1 
ATOM   9319  N  N   . ALA D  3 62  ? -24.083 -2.971  -19.005  1.00 210.20 ? 60   ALA D N   1 
ATOM   9320  C  CA  . ALA D  3 62  ? -23.678 -4.137  -19.772  1.00 202.65 ? 60   ALA D CA  1 
ATOM   9321  C  C   . ALA D  3 62  ? -24.805 -5.158  -19.816  1.00 196.42 ? 60   ALA D C   1 
ATOM   9322  O  O   . ALA D  3 62  ? -25.628 -5.242  -18.899  1.00 192.05 ? 60   ALA D O   1 
ATOM   9323  C  CB  . ALA D  3 62  ? -22.423 -4.779  -19.184  1.00 202.07 ? 60   ALA D CB  1 
ATOM   9324  N  N   . GLY D  3 63  ? -24.832 -5.927  -20.902  1.00 184.59 ? 61   GLY D N   1 
ATOM   9325  C  CA  . GLY D  3 63  ? -25.849 -6.939  -21.097  1.00 182.05 ? 61   GLY D CA  1 
ATOM   9326  C  C   . GLY D  3 63  ? -26.725 -6.689  -22.306  1.00 192.17 ? 61   GLY D C   1 
ATOM   9327  O  O   . GLY D  3 63  ? -26.937 -5.539  -22.703  1.00 202.91 ? 61   GLY D O   1 
ATOM   9328  N  N   . GLU D  3 64  ? -27.242 -7.760  -22.897  1.00 188.42 ? 62   GLU D N   1 
ATOM   9329  C  CA  . GLU D  3 64  ? -28.126 -7.650  -24.047  1.00 185.97 ? 62   GLU D CA  1 
ATOM   9330  C  C   . GLU D  3 64  ? -29.331 -8.568  -23.889  1.00 181.16 ? 62   GLU D C   1 
ATOM   9331  O  O   . GLU D  3 64  ? -29.236 -9.625  -23.265  1.00 180.44 ? 62   GLU D O   1 
ATOM   9332  C  CB  . GLU D  3 64  ? -27.376 -7.981  -25.336  1.00 205.07 ? 62   GLU D CB  1 
ATOM   9333  C  CG  . GLU D  3 64  ? -26.295 -6.979  -25.704  1.00 222.81 ? 62   GLU D CG  1 
ATOM   9334  C  CD  . GLU D  3 64  ? -25.555 -7.366  -26.971  1.00 237.91 ? 62   GLU D CD  1 
ATOM   9335  O  OE1 . GLU D  3 64  ? -25.736 -8.510  -27.437  1.00 241.37 ? 62   GLU D OE1 1 
ATOM   9336  O  OE2 . GLU D  3 64  ? -24.796 -6.527  -27.501  1.00 240.07 ? 62   GLU D OE2 1 
ATOM   9337  N  N   . PRO D  3 72  ? -47.523 -4.243  -29.175  1.00 214.35 ? 70   PRO D N   1 
ATOM   9338  C  CA  . PRO D  3 72  ? -47.715 -4.796  -27.830  1.00 214.18 ? 70   PRO D CA  1 
ATOM   9339  C  C   . PRO D  3 72  ? -48.534 -3.874  -26.927  1.00 232.59 ? 70   PRO D C   1 
ATOM   9340  O  O   . PRO D  3 72  ? -48.016 -2.879  -26.414  1.00 224.60 ? 70   PRO D O   1 
ATOM   9341  C  CB  . PRO D  3 72  ? -46.284 -4.949  -27.309  1.00 198.07 ? 70   PRO D CB  1 
ATOM   9342  C  CG  . PRO D  3 72  ? -45.461 -5.121  -28.534  1.00 197.54 ? 70   PRO D CG  1 
ATOM   9343  C  CD  . PRO D  3 72  ? -46.107 -4.257  -29.580  1.00 208.82 ? 70   PRO D CD  1 
ATOM   9344  N  N   . GLU D  3 73  ? -49.812 -4.224  -26.744  1.00 249.65 ? 71   GLU D N   1 
ATOM   9345  C  CA  . GLU D  3 73  ? -50.723 -3.397  -25.956  1.00 246.67 ? 71   GLU D CA  1 
ATOM   9346  C  C   . GLU D  3 73  ? -50.371 -3.408  -24.474  1.00 234.93 ? 71   GLU D C   1 
ATOM   9347  O  O   . GLU D  3 73  ? -50.558 -2.398  -23.786  1.00 234.69 ? 71   GLU D O   1 
ATOM   9348  C  CB  . GLU D  3 73  ? -52.168 -3.869  -26.153  1.00 246.27 ? 71   GLU D CB  1 
ATOM   9349  C  CG  . GLU D  3 73  ? -52.366 -5.379  -25.989  1.00 235.35 ? 71   GLU D CG  1 
ATOM   9350  C  CD  . GLU D  3 73  ? -53.815 -5.773  -25.741  1.00 220.69 ? 71   GLU D CD  1 
ATOM   9351  O  OE1 . GLU D  3 73  ? -54.673 -4.871  -25.639  1.00 220.06 ? 71   GLU D OE1 1 
ATOM   9352  O  OE2 . GLU D  3 73  ? -54.093 -6.988  -25.641  1.00 216.75 ? 71   GLU D OE2 1 
ATOM   9353  N  N   . ALA D  3 74  ? -49.874 -4.536  -23.962  1.00 227.61 ? 72   ALA D N   1 
ATOM   9354  C  CA  . ALA D  3 74  ? -49.543 -4.669  -22.549  1.00 225.37 ? 72   ALA D CA  1 
ATOM   9355  C  C   . ALA D  3 74  ? -48.170 -4.112  -22.209  1.00 230.96 ? 72   ALA D C   1 
ATOM   9356  O  O   . ALA D  3 74  ? -47.859 -3.953  -21.023  1.00 230.52 ? 72   ALA D O   1 
ATOM   9357  C  CB  . ALA D  3 74  ? -49.625 -6.138  -22.123  1.00 216.10 ? 72   ALA D CB  1 
ATOM   9358  N  N   . ASP D  3 75  ? -47.354 -3.804  -23.213  1.00 235.40 ? 73   ASP D N   1 
ATOM   9359  C  CA  . ASP D  3 75  ? -45.990 -3.348  -23.001  1.00 237.05 ? 73   ASP D CA  1 
ATOM   9360  C  C   . ASP D  3 75  ? -45.901 -1.848  -22.754  1.00 228.08 ? 73   ASP D C   1 
ATOM   9361  O  O   . ASP D  3 75  ? -44.824 -1.353  -22.401  1.00 219.16 ? 73   ASP D O   1 
ATOM   9362  C  CB  . ASP D  3 75  ? -45.129 -3.733  -24.209  1.00 247.57 ? 73   ASP D CB  1 
ATOM   9363  C  CG  . ASP D  3 75  ? -43.652 -3.581  -23.943  1.00 251.45 ? 73   ASP D CG  1 
ATOM   9364  O  OD1 . ASP D  3 75  ? -43.238 -3.772  -22.779  1.00 247.27 ? 73   ASP D OD1 1 
ATOM   9365  O  OD2 . ASP D  3 75  ? -42.906 -3.276  -24.898  1.00 253.29 ? 73   ASP D OD2 1 
ATOM   9366  N  N   . TYR D  3 76  ? -47.005 -1.122  -22.897  1.00 231.41 ? 74   TYR D N   1 
ATOM   9367  C  CA  . TYR D  3 76  ? -47.009 0.313   -22.666  1.00 228.12 ? 74   TYR D CA  1 
ATOM   9368  C  C   . TYR D  3 76  ? -47.292 0.657   -21.214  1.00 205.63 ? 74   TYR D C   1 
ATOM   9369  O  O   . TYR D  3 76  ? -46.883 1.727   -20.750  1.00 204.72 ? 74   TYR D O   1 
ATOM   9370  C  CB  . TYR D  3 76  ? -48.046 0.983   -23.581  1.00 232.34 ? 74   TYR D CB  1 
ATOM   9371  C  CG  . TYR D  3 76  ? -48.530 2.352   -23.138  1.00 224.85 ? 74   TYR D CG  1 
ATOM   9372  C  CD1 . TYR D  3 76  ? -47.798 3.499   -23.424  1.00 215.22 ? 74   TYR D CD1 1 
ATOM   9373  C  CD2 . TYR D  3 76  ? -49.734 2.498   -22.454  1.00 219.89 ? 74   TYR D CD2 1 
ATOM   9374  C  CE1 . TYR D  3 76  ? -48.245 4.748   -23.032  1.00 208.12 ? 74   TYR D CE1 1 
ATOM   9375  C  CE2 . TYR D  3 76  ? -50.187 3.743   -22.057  1.00 215.54 ? 74   TYR D CE2 1 
ATOM   9376  C  CZ  . TYR D  3 76  ? -49.438 4.863   -22.348  1.00 206.49 ? 74   TYR D CZ  1 
ATOM   9377  O  OH  . TYR D  3 76  ? -49.885 6.103   -21.957  1.00 196.85 ? 74   TYR D OH  1 
ATOM   9378  N  N   . TYR D  3 77  ? -47.959 -0.230  -20.483  1.00 184.54 ? 75   TYR D N   1 
ATOM   9379  C  CA  . TYR D  3 77  ? -48.268 0.007   -19.085  1.00 185.77 ? 75   TYR D CA  1 
ATOM   9380  C  C   . TYR D  3 77  ? -47.037 -0.259  -18.216  1.00 175.28 ? 75   TYR D C   1 
ATOM   9381  O  O   . TYR D  3 77  ? -45.978 -0.680  -18.691  1.00 173.61 ? 75   TYR D O   1 
ATOM   9382  C  CB  . TYR D  3 77  ? -49.459 -0.848  -18.659  1.00 204.48 ? 75   TYR D CB  1 
ATOM   9383  C  CG  . TYR D  3 77  ? -50.773 -0.439  -19.300  1.00 208.77 ? 75   TYR D CG  1 
ATOM   9384  C  CD1 . TYR D  3 77  ? -51.595 0.519   -18.711  1.00 206.09 ? 75   TYR D CD1 1 
ATOM   9385  C  CD2 . TYR D  3 77  ? -51.185 -1.005  -20.500  1.00 206.38 ? 75   TYR D CD2 1 
ATOM   9386  C  CE1 . TYR D  3 77  ? -52.796 0.890   -19.299  1.00 214.36 ? 75   TYR D CE1 1 
ATOM   9387  C  CE2 . TYR D  3 77  ? -52.380 -0.639  -21.095  1.00 210.60 ? 75   TYR D CE2 1 
ATOM   9388  C  CZ  . TYR D  3 77  ? -53.181 0.308   -20.494  1.00 216.65 ? 75   TYR D CZ  1 
ATOM   9389  O  OH  . TYR D  3 77  ? -54.368 0.667   -21.094  1.00 212.74 ? 75   TYR D OH  1 
ATOM   9390  N  N   . ALA D  3 78  ? -47.181 0.008   -16.920  1.00 166.22 ? 76   ALA D N   1 
ATOM   9391  C  CA  . ALA D  3 78  ? -46.080 -0.115  -15.978  1.00 172.74 ? 76   ALA D CA  1 
ATOM   9392  C  C   . ALA D  3 78  ? -45.889 -1.560  -15.532  1.00 178.74 ? 76   ALA D C   1 
ATOM   9393  O  O   . ALA D  3 78  ? -46.828 -2.361  -15.517  1.00 183.13 ? 76   ALA D O   1 
ATOM   9394  C  CB  . ALA D  3 78  ? -46.323 0.770   -14.758  1.00 175.92 ? 76   ALA D CB  1 
ATOM   9395  N  N   . LYS D  3 79  ? -44.658 -1.874  -15.127  1.00 168.87 ? 77   LYS D N   1 
ATOM   9396  C  CA  . LYS D  3 79  ? -44.287 -3.208  -14.673  1.00 155.43 ? 77   LYS D CA  1 
ATOM   9397  C  C   . LYS D  3 79  ? -43.678 -3.109  -13.285  1.00 151.59 ? 77   LYS D C   1 
ATOM   9398  O  O   . LYS D  3 79  ? -42.726 -2.352  -13.076  1.00 148.84 ? 77   LYS D O   1 
ATOM   9399  C  CB  . LYS D  3 79  ? -43.293 -3.867  -15.634  1.00 153.00 ? 77   LYS D CB  1 
ATOM   9400  C  CG  . LYS D  3 79  ? -43.698 -3.782  -17.096  1.00 159.13 ? 77   LYS D CG  1 
ATOM   9401  C  CD  . LYS D  3 79  ? -44.984 -4.552  -17.354  1.00 168.06 ? 77   LYS D CD  1 
ATOM   9402  C  CE  . LYS D  3 79  ? -45.393 -4.495  -18.818  1.00 164.04 ? 77   LYS D CE  1 
ATOM   9403  N  NZ  . LYS D  3 79  ? -46.671 -5.224  -19.064  1.00 163.03 ? 77   LYS D NZ  1 
ATOM   9404  N  N   . GLU D  3 80  ? -44.215 -3.887  -12.347  1.00 166.61 ? 78   GLU D N   1 
ATOM   9405  C  CA  . GLU D  3 80  ? -43.726 -3.884  -10.975  1.00 171.23 ? 78   GLU D CA  1 
ATOM   9406  C  C   . GLU D  3 80  ? -42.421 -4.667  -10.900  1.00 163.57 ? 78   GLU D C   1 
ATOM   9407  O  O   . GLU D  3 80  ? -42.398 -5.880  -11.139  1.00 163.61 ? 78   GLU D O   1 
ATOM   9408  C  CB  . GLU D  3 80  ? -44.771 -4.472  -10.027  1.00 171.24 ? 78   GLU D CB  1 
ATOM   9409  C  CG  . GLU D  3 80  ? -44.326 -4.507  -8.573   1.00 172.01 ? 78   GLU D CG  1 
ATOM   9410  C  CD  . GLU D  3 80  ? -45.415 -4.996  -7.642   1.00 174.08 ? 78   GLU D CD  1 
ATOM   9411  O  OE1 . GLU D  3 80  ? -46.585 -5.049  -8.077   1.00 171.75 ? 78   GLU D OE1 1 
ATOM   9412  O  OE2 . GLU D  3 80  ? -45.101 -5.329  -6.479   1.00 178.98 ? 78   GLU D OE2 1 
ATOM   9413  N  N   . VAL D  3 81  ? -41.340 -3.974  -10.565  1.00 165.74 ? 79   VAL D N   1 
ATOM   9414  C  CA  . VAL D  3 81  ? -40.008 -4.566  -10.541  1.00 164.13 ? 79   VAL D CA  1 
ATOM   9415  C  C   . VAL D  3 81  ? -39.725 -5.106  -9.146   1.00 176.20 ? 79   VAL D C   1 
ATOM   9416  O  O   . VAL D  3 81  ? -39.751 -4.361  -8.160   1.00 186.00 ? 79   VAL D O   1 
ATOM   9417  C  CB  . VAL D  3 81  ? -38.944 -3.543  -10.958  1.00 172.87 ? 79   VAL D CB  1 
ATOM   9418  C  CG1 . VAL D  3 81  ? -37.559 -4.158  -10.866  1.00 178.08 ? 79   VAL D CG1 1 
ATOM   9419  C  CG2 . VAL D  3 81  ? -39.220 -3.045  -12.363  1.00 184.60 ? 79   VAL D CG2 1 
ATOM   9420  N  N   . THR D  3 82  ? -39.451 -6.404  -9.067   1.00 172.93 ? 80   THR D N   1 
ATOM   9421  C  CA  . THR D  3 82  ? -39.039 -7.057  -7.836   1.00 171.21 ? 80   THR D CA  1 
ATOM   9422  C  C   . THR D  3 82  ? -37.859 -7.969  -8.140   1.00 169.84 ? 80   THR D C   1 
ATOM   9423  O  O   . THR D  3 82  ? -37.672 -8.404  -9.277   1.00 176.41 ? 80   THR D O   1 
ATOM   9424  C  CB  . THR D  3 82  ? -40.195 -7.850  -7.207   1.00 167.05 ? 80   THR D CB  1 
ATOM   9425  O  OG1 . THR D  3 82  ? -40.800 -8.688  -8.200   1.00 164.52 ? 80   THR D OG1 1 
ATOM   9426  C  CG2 . THR D  3 82  ? -41.245 -6.906  -6.631   1.00 177.31 ? 80   THR D CG2 1 
ATOM   9427  N  N   . ARG D  3 83  ? -37.045 -8.237  -7.125   1.00 163.43 ? 81   ARG D N   1 
ATOM   9428  C  CA  . ARG D  3 83  ? -35.885 -9.096  -7.291   1.00 162.84 ? 81   ARG D CA  1 
ATOM   9429  C  C   . ARG D  3 83  ? -35.880 -10.167 -6.211   1.00 172.98 ? 81   ARG D C   1 
ATOM   9430  O  O   . ARG D  3 83  ? -36.558 -10.048 -5.187   1.00 180.64 ? 81   ARG D O   1 
ATOM   9431  C  CB  . ARG D  3 83  ? -34.582 -8.290  -7.246   1.00 158.33 ? 81   ARG D CB  1 
ATOM   9432  C  CG  . ARG D  3 83  ? -34.121 -7.945  -5.842   1.00 157.75 ? 81   ARG D CG  1 
ATOM   9433  C  CD  . ARG D  3 83  ? -32.743 -7.298  -5.846   1.00 162.76 ? 81   ARG D CD  1 
ATOM   9434  N  NE  . ARG D  3 83  ? -32.192 -7.179  -4.498   1.00 167.07 ? 81   ARG D NE  1 
ATOM   9435  C  CZ  . ARG D  3 83  ? -30.987 -6.689  -4.224   1.00 168.59 ? 81   ARG D CZ  1 
ATOM   9436  N  NH1 . ARG D  3 83  ? -30.203 -6.264  -5.206   1.00 164.03 ? 81   ARG D NH1 1 
ATOM   9437  N  NH2 . ARG D  3 83  ? -30.566 -6.622  -2.970   1.00 173.60 ? 81   ARG D NH2 1 
ATOM   9438  N  N   . VAL D  3 84  ? -35.111 -11.227 -6.458   1.00 173.89 ? 82   VAL D N   1 
ATOM   9439  C  CA  . VAL D  3 84  ? -34.939 -12.324 -5.508   1.00 171.45 ? 82   VAL D CA  1 
ATOM   9440  C  C   . VAL D  3 84  ? -33.484 -12.770 -5.546   1.00 171.09 ? 82   VAL D C   1 
ATOM   9441  O  O   . VAL D  3 84  ? -32.938 -13.044 -6.620   1.00 169.27 ? 82   VAL D O   1 
ATOM   9442  C  CB  . VAL D  3 84  ? -35.874 -13.516 -5.800   1.00 173.67 ? 82   VAL D CB  1 
ATOM   9443  C  CG1 . VAL D  3 84  ? -37.260 -13.268 -5.224   1.00 168.69 ? 82   VAL D CG1 1 
ATOM   9444  C  CG2 . VAL D  3 84  ? -35.960 -13.768 -7.287   1.00 183.18 ? 82   VAL D CG2 1 
ATOM   9445  N  N   . LEU D  3 85  ? -32.853 -12.824 -4.377   1.00 167.69 ? 83   LEU D N   1 
ATOM   9446  C  CA  . LEU D  3 85  ? -31.484 -13.297 -4.269   1.00 163.02 ? 83   LEU D CA  1 
ATOM   9447  C  C   . LEU D  3 85  ? -31.447 -14.817 -4.400   1.00 165.28 ? 83   LEU D C   1 
ATOM   9448  O  O   . LEU D  3 85  ? -32.478 -15.496 -4.375   1.00 167.05 ? 83   LEU D O   1 
ATOM   9449  C  CB  . LEU D  3 85  ? -30.871 -12.854 -2.944   1.00 158.76 ? 83   LEU D CB  1 
ATOM   9450  C  CG  . LEU D  3 85  ? -30.797 -11.340 -2.749   1.00 154.62 ? 83   LEU D CG  1 
ATOM   9451  C  CD1 . LEU D  3 85  ? -30.333 -11.014 -1.344   1.00 170.05 ? 83   LEU D CD1 1 
ATOM   9452  C  CD2 . LEU D  3 85  ? -29.883 -10.699 -3.776   1.00 152.84 ? 83   LEU D CD2 1 
ATOM   9453  N  N   . MET D  3 86  ? -30.240 -15.358 -4.539   1.00 172.76 ? 84   MET D N   1 
ATOM   9454  C  CA  . MET D  3 86  ? -30.091 -16.788 -4.746   1.00 177.95 ? 84   MET D CA  1 
ATOM   9455  C  C   . MET D  3 86  ? -29.893 -17.513 -3.418   1.00 181.52 ? 84   MET D C   1 
ATOM   9456  O  O   . MET D  3 86  ? -29.831 -16.913 -2.342   1.00 175.65 ? 84   MET D O   1 
ATOM   9457  C  CB  . MET D  3 86  ? -28.935 -17.089 -5.700   1.00 187.79 ? 84   MET D CB  1 
ATOM   9458  C  CG  . MET D  3 86  ? -27.549 -16.765 -5.170   1.00 186.84 ? 84   MET D CG  1 
ATOM   9459  S  SD  . MET D  3 86  ? -26.254 -17.529 -6.174   1.00 184.19 ? 84   MET D SD  1 
ATOM   9460  C  CE  . MET D  3 86  ? -24.797 -17.041 -5.257   1.00 187.42 ? 84   MET D CE  1 
ATOM   9461  N  N   . VAL D  3 87  ? -29.816 -18.833 -3.504   1.00 197.55 ? 85   VAL D N   1 
ATOM   9462  C  CA  . VAL D  3 87  ? -29.545 -19.687 -2.358   1.00 197.99 ? 85   VAL D CA  1 
ATOM   9463  C  C   . VAL D  3 87  ? -28.040 -19.818 -2.196   1.00 203.82 ? 85   VAL D C   1 
ATOM   9464  O  O   . VAL D  3 87  ? -27.305 -20.000 -3.173   1.00 206.99 ? 85   VAL D O   1 
ATOM   9465  C  CB  . VAL D  3 87  ? -30.212 -21.062 -2.535   1.00 201.15 ? 85   VAL D CB  1 
ATOM   9466  C  CG1 . VAL D  3 87  ? -30.043 -21.897 -1.280   1.00 213.00 ? 85   VAL D CG1 1 
ATOM   9467  C  CG2 . VAL D  3 87  ? -31.682 -20.885 -2.877   1.00 198.89 ? 85   VAL D CG2 1 
ATOM   9468  N  N   . GLU D  3 88  ? -27.579 -19.732 -0.956   1.00 213.26 ? 86   GLU D N   1 
ATOM   9469  C  CA  . GLU D  3 88  ? -26.157 -19.815 -0.676   1.00 223.51 ? 86   GLU D CA  1 
ATOM   9470  C  C   . GLU D  3 88  ? -25.643 -21.239 -0.887   1.00 236.55 ? 86   GLU D C   1 
ATOM   9471  O  O   . GLU D  3 88  ? -26.403 -22.191 -1.084   1.00 244.63 ? 86   GLU D O   1 
ATOM   9472  C  CB  . GLU D  3 88  ? -25.883 -19.352 0.747    1.00 235.02 ? 86   GLU D CB  1 
ATOM   9473  C  CG  . GLU D  3 88  ? -26.627 -18.088 1.107    1.00 233.07 ? 86   GLU D CG  1 
ATOM   9474  C  CD  . GLU D  3 88  ? -26.746 -17.899 2.601    1.00 245.18 ? 86   GLU D CD  1 
ATOM   9475  O  OE1 . GLU D  3 88  ? -26.179 -18.719 3.352    1.00 245.38 ? 86   GLU D OE1 1 
ATOM   9476  O  OE2 . GLU D  3 88  ? -27.427 -16.942 3.024    1.00 250.79 ? 86   GLU D OE2 1 
ATOM   9477  N  N   . THR D  3 89  ? -24.321 -21.378 -0.832   1.00 232.74 ? 87   THR D N   1 
ATOM   9478  C  CA  . THR D  3 89  ? -23.665 -22.676 -0.915   1.00 229.54 ? 87   THR D CA  1 
ATOM   9479  C  C   . THR D  3 89  ? -23.663 -23.424 0.407    1.00 230.58 ? 87   THR D C   1 
ATOM   9480  O  O   . THR D  3 89  ? -23.050 -24.493 0.497    1.00 232.50 ? 87   THR D O   1 
ATOM   9481  C  CB  . THR D  3 89  ? -22.223 -22.507 -1.398   1.00 229.31 ? 87   THR D CB  1 
ATOM   9482  O  OG1 . THR D  3 89  ? -21.618 -21.397 -0.721   1.00 225.52 ? 87   THR D OG1 1 
ATOM   9483  C  CG2 . THR D  3 89  ? -22.180 -22.288 -2.899   1.00 230.94 ? 87   THR D CG2 1 
ATOM   9484  N  N   . HIS D  3 90  ? -24.332 -22.896 1.423    1.00 245.01 ? 88   HIS D N   1 
ATOM   9485  C  CA  . HIS D  3 90  ? -24.342 -23.479 2.756    1.00 264.35 ? 88   HIS D CA  1 
ATOM   9486  C  C   . HIS D  3 90  ? -25.411 -24.545 2.947    1.00 265.72 ? 88   HIS D C   1 
ATOM   9487  O  O   . HIS D  3 90  ? -25.493 -25.123 4.036    1.00 273.78 ? 88   HIS D O   1 
ATOM   9488  C  CB  . HIS D  3 90  ? -24.510 -22.380 3.811    1.00 265.21 ? 88   HIS D CB  1 
ATOM   9489  C  CG  . HIS D  3 90  ? -23.512 -21.272 3.687    1.00 264.19 ? 88   HIS D CG  1 
ATOM   9490  N  ND1 . HIS D  3 90  ? -23.534 -20.363 2.651    1.00 251.44 ? 88   HIS D ND1 1 
ATOM   9491  C  CD2 . HIS D  3 90  ? -22.465 -20.923 4.472    1.00 270.11 ? 88   HIS D CD2 1 
ATOM   9492  C  CE1 . HIS D  3 90  ? -22.542 -19.504 2.800    1.00 253.04 ? 88   HIS D CE1 1 
ATOM   9493  N  NE2 . HIS D  3 90  ? -21.879 -19.821 3.897    1.00 267.94 ? 88   HIS D NE2 1 
ATOM   9494  N  N   . ASN D  3 91  ? -26.219 -24.839 1.927    1.00 252.37 ? 89   ASN D N   1 
ATOM   9495  C  CA  . ASN D  3 91  ? -27.294 -25.806 2.117    1.00 253.85 ? 89   ASN D CA  1 
ATOM   9496  C  C   . ASN D  3 91  ? -27.411 -26.856 1.015    1.00 237.75 ? 89   ASN D C   1 
ATOM   9497  O  O   . ASN D  3 91  ? -27.415 -28.058 1.305    1.00 233.61 ? 89   ASN D O   1 
ATOM   9498  C  CB  . ASN D  3 91  ? -28.629 -25.067 2.242    1.00 252.48 ? 89   ASN D CB  1 
ATOM   9499  C  CG  . ASN D  3 91  ? -28.756 -24.309 3.549    1.00 256.15 ? 89   ASN D CG  1 
ATOM   9500  O  OD1 . ASN D  3 91  ? -28.198 -24.710 4.571    1.00 272.86 ? 89   ASN D OD1 1 
ATOM   9501  N  ND2 . ASN D  3 91  ? -29.495 -23.206 3.522    1.00 240.19 ? 89   ASN D ND2 1 
ATOM   9502  N  N   . GLU D  3 92  ? -27.499 -26.433 -0.246   1.00 223.89 ? 90   GLU D N   1 
ATOM   9503  C  CA  . GLU D  3 92  ? -27.708 -27.375 -1.334   1.00 227.31 ? 90   GLU D CA  1 
ATOM   9504  C  C   . GLU D  3 92  ? -26.656 -27.350 -2.426   1.00 230.44 ? 90   GLU D C   1 
ATOM   9505  O  O   . GLU D  3 92  ? -26.559 -28.326 -3.177   1.00 234.07 ? 90   GLU D O   1 
ATOM   9506  C  CB  . GLU D  3 92  ? -29.073 -27.124 -1.991   1.00 230.75 ? 90   GLU D CB  1 
ATOM   9507  C  CG  . GLU D  3 92  ? -30.236 -27.273 -1.050   1.00 246.87 ? 90   GLU D CG  1 
ATOM   9508  C  CD  . GLU D  3 92  ? -31.536 -26.885 -1.702   1.00 252.55 ? 90   GLU D CD  1 
ATOM   9509  O  OE1 . GLU D  3 92  ? -31.494 -26.390 -2.847   1.00 246.92 ? 90   GLU D OE1 1 
ATOM   9510  O  OE2 . GLU D  3 92  ? -32.598 -27.075 -1.072   1.00 258.41 ? 90   GLU D OE2 1 
ATOM   9511  N  N   . ILE D  3 93  ? -25.861 -26.284 -2.540   1.00 243.83 ? 91   ILE D N   1 
ATOM   9512  C  CA  . ILE D  3 93  ? -24.964 -26.164 -3.688   1.00 255.15 ? 91   ILE D CA  1 
ATOM   9513  C  C   . ILE D  3 93  ? -23.683 -26.960 -3.507   1.00 254.52 ? 91   ILE D C   1 
ATOM   9514  O  O   . ILE D  3 93  ? -22.916 -27.117 -4.465   1.00 256.79 ? 91   ILE D O   1 
ATOM   9515  C  CB  . ILE D  3 93  ? -24.676 -24.675 -3.960   1.00 249.26 ? 91   ILE D CB  1 
ATOM   9516  C  CG1 . ILE D  3 93  ? -25.977 -23.868 -3.931   1.00 237.83 ? 91   ILE D CG1 1 
ATOM   9517  C  CG2 . ILE D  3 93  ? -24.022 -24.477 -5.321   1.00 238.35 ? 91   ILE D CG2 1 
ATOM   9518  C  CD1 . ILE D  3 93  ? -25.843 -22.476 -4.483   1.00 221.16 ? 91   ILE D CD1 1 
ATOM   9519  N  N   . TYR D  3 94  ? -23.457 -27.530 -2.324   1.00 261.59 ? 92   TYR D N   1 
ATOM   9520  C  CA  . TYR D  3 94  ? -22.266 -28.327 -2.084   1.00 275.10 ? 92   TYR D CA  1 
ATOM   9521  C  C   . TYR D  3 94  ? -22.564 -29.817 -2.007   1.00 283.19 ? 92   TYR D C   1 
ATOM   9522  O  O   . TYR D  3 94  ? -21.624 -30.620 -1.980   1.00 293.55 ? 92   TYR D O   1 
ATOM   9523  C  CB  . TYR D  3 94  ? -21.562 -27.873 -0.790   1.00 283.92 ? 92   TYR D CB  1 
ATOM   9524  C  CG  . TYR D  3 94  ? -22.278 -28.245 0.495    1.00 290.75 ? 92   TYR D CG  1 
ATOM   9525  C  CD1 . TYR D  3 94  ? -23.342 -27.490 0.966    1.00 284.36 ? 92   TYR D CD1 1 
ATOM   9526  C  CD2 . TYR D  3 94  ? -21.858 -29.333 1.258    1.00 294.07 ? 92   TYR D CD2 1 
ATOM   9527  C  CE1 . TYR D  3 94  ? -23.992 -27.822 2.142    1.00 286.53 ? 92   TYR D CE1 1 
ATOM   9528  C  CE2 . TYR D  3 94  ? -22.500 -29.672 2.438    1.00 292.62 ? 92   TYR D CE2 1 
ATOM   9529  C  CZ  . TYR D  3 94  ? -23.566 -28.912 2.874    1.00 291.10 ? 92   TYR D CZ  1 
ATOM   9530  O  OH  . TYR D  3 94  ? -24.208 -29.244 4.046    1.00 294.24 ? 92   TYR D OH  1 
ATOM   9531  N  N   . ASP D  3 95  ? -23.841 -30.204 -1.977   1.00 288.01 ? 93   ASP D N   1 
ATOM   9532  C  CA  . ASP D  3 95  ? -24.215 -31.593 -1.745   1.00 303.66 ? 93   ASP D CA  1 
ATOM   9533  C  C   . ASP D  3 95  ? -23.965 -32.489 -2.955   1.00 301.73 ? 93   ASP D C   1 
ATOM   9534  O  O   . ASP D  3 95  ? -23.878 -33.711 -2.791   1.00 310.90 ? 93   ASP D O   1 
ATOM   9535  C  CB  . ASP D  3 95  ? -25.691 -31.658 -1.331   1.00 299.16 ? 93   ASP D CB  1 
ATOM   9536  C  CG  . ASP D  3 95  ? -26.090 -33.011 -0.756   1.00 295.25 ? 93   ASP D CG  1 
ATOM   9537  O  OD1 . ASP D  3 95  ? -25.199 -33.797 -0.366   1.00 297.20 ? 93   ASP D OD1 1 
ATOM   9538  O  OD2 . ASP D  3 95  ? -27.310 -33.280 -0.681   1.00 282.59 ? 93   ASP D OD2 1 
ATOM   9539  N  N   . LYS D  3 96  ? -23.829 -31.928 -4.156   1.00 286.16 ? 94   LYS D N   1 
ATOM   9540  C  CA  . LYS D  3 96  ? -23.669 -32.744 -5.356   1.00 295.43 ? 94   LYS D CA  1 
ATOM   9541  C  C   . LYS D  3 96  ? -22.388 -32.467 -6.125   1.00 296.58 ? 94   LYS D C   1 
ATOM   9542  O  O   . LYS D  3 96  ? -21.710 -33.410 -6.547   1.00 310.42 ? 94   LYS D O   1 
ATOM   9543  C  CB  . LYS D  3 96  ? -24.872 -32.537 -6.295   1.00 293.64 ? 94   LYS D CB  1 
ATOM   9544  C  CG  . LYS D  3 96  ? -24.796 -33.338 -7.589   1.00 299.26 ? 94   LYS D CG  1 
ATOM   9545  C  CD  . LYS D  3 96  ? -26.021 -33.118 -8.470   1.00 290.37 ? 94   LYS D CD  1 
ATOM   9546  C  CE  . LYS D  3 96  ? -25.839 -33.750 -9.846   1.00 284.49 ? 94   LYS D CE  1 
ATOM   9547  N  NZ  . LYS D  3 96  ? -25.527 -35.204 -9.750   1.00 292.58 ? 94   LYS D NZ  1 
ATOM   9548  N  N   . PHE D  3 97  ? -22.038 -31.214 -6.318   1.00 276.40 ? 95   PHE D N   1 
ATOM   9549  C  CA  . PHE D  3 97  ? -20.926 -30.858 -7.191   1.00 273.90 ? 95   PHE D CA  1 
ATOM   9550  C  C   . PHE D  3 97  ? -19.949 -29.882 -6.559   1.00 271.29 ? 95   PHE D C   1 
ATOM   9551  O  O   . PHE D  3 97  ? -18.747 -29.979 -6.826   1.00 274.39 ? 95   PHE D O   1 
ATOM   9552  C  CB  . PHE D  3 97  ? -21.468 -30.268 -8.499   1.00 269.79 ? 95   PHE D CB  1 
ATOM   9553  C  CG  . PHE D  3 97  ? -22.828 -29.646 -8.360   1.00 266.27 ? 95   PHE D CG  1 
ATOM   9554  C  CD1 . PHE D  3 97  ? -22.998 -28.464 -7.659   1.00 258.63 ? 95   PHE D CD1 1 
ATOM   9555  C  CD2 . PHE D  3 97  ? -23.936 -30.238 -8.944   1.00 262.67 ? 95   PHE D CD2 1 
ATOM   9556  C  CE1 . PHE D  3 97  ? -24.249 -27.892 -7.531   1.00 251.71 ? 95   PHE D CE1 1 
ATOM   9557  C  CE2 . PHE D  3 97  ? -25.189 -29.668 -8.821   1.00 249.07 ? 95   PHE D CE2 1 
ATOM   9558  C  CZ  . PHE D  3 97  ? -25.345 -28.495 -8.114   1.00 246.76 ? 95   PHE D CZ  1 
ATOM   9559  N  N   . LYS D  3 98  ? -20.440 -28.932 -5.759   1.00 259.84 ? 96   LYS D N   1 
ATOM   9560  C  CA  . LYS D  3 98  ? -19.639 -27.842 -5.212   1.00 254.85 ? 96   LYS D CA  1 
ATOM   9561  C  C   . LYS D  3 98  ? -19.168 -26.951 -6.352   1.00 249.58 ? 96   LYS D C   1 
ATOM   9562  O  O   . LYS D  3 98  ? -19.880 -26.783 -7.347   1.00 238.08 ? 96   LYS D O   1 
ATOM   9563  C  CB  . LYS D  3 98  ? -18.455 -28.359 -4.385   1.00 251.82 ? 96   LYS D CB  1 
ATOM   9564  C  CG  . LYS D  3 98  ? -18.861 -29.121 -3.136   1.00 244.08 ? 96   LYS D CG  1 
ATOM   9565  C  CD  . LYS D  3 98  ? -17.696 -29.294 -2.176   1.00 237.84 ? 96   LYS D CD  1 
ATOM   9566  C  CE  . LYS D  3 98  ? -16.683 -30.298 -2.704   1.00 238.45 ? 96   LYS D CE  1 
ATOM   9567  N  NZ  . LYS D  3 98  ? -17.220 -31.689 -2.744   1.00 240.41 ? 96   LYS D NZ  1 
ATOM   9568  N  N   . GLN D  3 99  ? -17.982 -26.369 -6.214   1.00 253.17 ? 97   GLN D N   1 
ATOM   9569  C  CA  . GLN D  3 99  ? -17.440 -25.441 -7.195   1.00 249.07 ? 97   GLN D CA  1 
ATOM   9570  C  C   . GLN D  3 99  ? -16.159 -26.018 -7.777   1.00 258.85 ? 97   GLN D C   1 
ATOM   9571  O  O   . GLN D  3 99  ? -15.349 -26.607 -7.055   1.00 264.69 ? 97   GLN D O   1 
ATOM   9572  C  CB  . GLN D  3 99  ? -17.183 -24.063 -6.562   1.00 244.09 ? 97   GLN D CB  1 
ATOM   9573  C  CG  . GLN D  3 99  ? -16.672 -22.991 -7.519   1.00 234.63 ? 97   GLN D CG  1 
ATOM   9574  C  CD  . GLN D  3 99  ? -15.159 -22.912 -7.560   1.00 238.90 ? 97   GLN D CD  1 
ATOM   9575  O  OE1 . GLN D  3 99  ? -14.550 -22.968 -8.627   1.00 246.51 ? 97   GLN D OE1 1 
ATOM   9576  N  NE2 . GLN D  3 99  ? -14.543 -22.785 -6.389   1.00 236.00 ? 97   GLN D NE2 1 
ATOM   9577  N  N   . SER D  3 100 ? -15.984 -25.854 -9.087   1.00 261.79 ? 98   SER D N   1 
ATOM   9578  C  CA  . SER D  3 100 ? -14.787 -26.339 -9.756   1.00 261.38 ? 98   SER D CA  1 
ATOM   9579  C  C   . SER D  3 100 ? -14.452 -25.424 -10.926  1.00 256.22 ? 98   SER D C   1 
ATOM   9580  O  O   . SER D  3 100 ? -15.259 -24.593 -11.351  1.00 250.81 ? 98   SER D O   1 
ATOM   9581  C  CB  . SER D  3 100 ? -14.961 -27.785 -10.237  1.00 257.68 ? 98   SER D CB  1 
ATOM   9582  O  OG  . SER D  3 100 ? -15.162 -28.665 -9.144   1.00 257.61 ? 98   SER D OG  1 
ATOM   9583  N  N   . THR D  3 101 ? -13.232 -25.588 -11.444  1.00 257.90 ? 99   THR D N   1 
ATOM   9584  C  CA  . THR D  3 101 ? -12.756 -24.785 -12.564  1.00 254.28 ? 99   THR D CA  1 
ATOM   9585  C  C   . THR D  3 101 ? -13.546 -25.041 -13.838  1.00 253.02 ? 99   THR D C   1 
ATOM   9586  O  O   . THR D  3 101 ? -13.365 -24.313 -14.821  1.00 258.04 ? 99   THR D O   1 
ATOM   9587  C  CB  . THR D  3 101 ? -11.273 -25.070 -12.812  1.00 267.27 ? 99   THR D CB  1 
ATOM   9588  O  OG1 . THR D  3 101 ? -11.112 -26.427 -13.248  1.00 281.08 ? 99   THR D OG1 1 
ATOM   9589  C  CG2 . THR D  3 101 ? -10.473 -24.865 -11.532  1.00 268.62 ? 99   THR D CG2 1 
ATOM   9590  N  N   . HIS D  3 102 ? -14.415 -26.048 -13.838  1.00 253.35 ? 100  HIS D N   1 
ATOM   9591  C  CA  . HIS D  3 102 ? -15.159 -26.440 -15.024  1.00 261.39 ? 100  HIS D CA  1 
ATOM   9592  C  C   . HIS D  3 102 ? -16.518 -25.759 -15.106  1.00 266.64 ? 100  HIS D C   1 
ATOM   9593  O  O   . HIS D  3 102 ? -17.003 -25.498 -16.214  1.00 266.04 ? 100  HIS D O   1 
ATOM   9594  C  CB  . HIS D  3 102 ? -15.329 -27.965 -15.036  1.00 261.53 ? 100  HIS D CB  1 
ATOM   9595  C  CG  . HIS D  3 102 ? -15.908 -28.510 -16.306  1.00 263.01 ? 100  HIS D CG  1 
ATOM   9596  N  ND1 . HIS D  3 102 ? -16.374 -29.802 -16.409  1.00 262.03 ? 100  HIS D ND1 1 
ATOM   9597  C  CD2 . HIS D  3 102 ? -16.083 -27.948 -17.526  1.00 261.72 ? 100  HIS D CD2 1 
ATOM   9598  C  CE1 . HIS D  3 102 ? -16.822 -30.010 -17.634  1.00 260.72 ? 100  HIS D CE1 1 
ATOM   9599  N  NE2 . HIS D  3 102 ? -16.657 -28.900 -18.332  1.00 260.44 ? 100  HIS D NE2 1 
ATOM   9600  N  N   . SER D  3 103 ? -17.133 -25.440 -13.967  1.00 268.99 ? 101  SER D N   1 
ATOM   9601  C  CA  . SER D  3 103 ? -18.460 -24.837 -13.971  1.00 260.08 ? 101  SER D CA  1 
ATOM   9602  C  C   . SER D  3 103 ? -18.689 -24.068 -12.675  1.00 253.67 ? 101  SER D C   1 
ATOM   9603  O  O   . SER D  3 103 ? -17.965 -24.234 -11.690  1.00 250.20 ? 101  SER D O   1 
ATOM   9604  C  CB  . SER D  3 103 ? -19.548 -25.898 -14.168  1.00 266.36 ? 101  SER D CB  1 
ATOM   9605  O  OG  . SER D  3 103 ? -19.401 -26.961 -13.242  1.00 277.11 ? 101  SER D OG  1 
ATOM   9606  N  N   . ILE D  3 104 ? -19.713 -23.216 -12.698  1.00 257.74 ? 102  ILE D N   1 
ATOM   9607  C  CA  . ILE D  3 104 ? -20.152 -22.446 -11.539  1.00 253.28 ? 102  ILE D CA  1 
ATOM   9608  C  C   . ILE D  3 104 ? -21.672 -22.547 -11.449  1.00 245.15 ? 102  ILE D C   1 
ATOM   9609  O  O   . ILE D  3 104 ? -22.370 -22.295 -12.437  1.00 249.40 ? 102  ILE D O   1 
ATOM   9610  C  CB  . ILE D  3 104 ? -19.701 -20.976 -11.638  1.00 243.60 ? 102  ILE D CB  1 
ATOM   9611  C  CG1 . ILE D  3 104 ? -18.217 -20.853 -11.277  1.00 256.45 ? 102  ILE D CG1 1 
ATOM   9612  C  CG2 . ILE D  3 104 ? -20.563 -20.090 -10.754  1.00 229.86 ? 102  ILE D CG2 1 
ATOM   9613  C  CD1 . ILE D  3 104 ? -17.673 -19.445 -11.353  1.00 258.59 ? 102  ILE D CD1 1 
ATOM   9614  N  N   . TYR D  3 105 ? -22.184 -22.900 -10.270  1.00 231.52 ? 103  TYR D N   1 
ATOM   9615  C  CA  . TYR D  3 105 ? -23.605 -23.168 -10.084  1.00 229.37 ? 103  TYR D CA  1 
ATOM   9616  C  C   . TYR D  3 105 ? -24.266 -22.119 -9.197   1.00 239.29 ? 103  TYR D C   1 
ATOM   9617  O  O   . TYR D  3 105 ? -23.722 -21.731 -8.158   1.00 246.11 ? 103  TYR D O   1 
ATOM   9618  C  CB  . TYR D  3 105 ? -23.819 -24.561 -9.486   1.00 234.13 ? 103  TYR D CB  1 
ATOM   9619  C  CG  . TYR D  3 105 ? -23.170 -25.670 -10.284  1.00 242.36 ? 103  TYR D CG  1 
ATOM   9620  C  CD1 . TYR D  3 105 ? -23.827 -26.251 -11.363  1.00 242.08 ? 103  TYR D CD1 1 
ATOM   9621  C  CD2 . TYR D  3 105 ? -21.897 -26.130 -9.966   1.00 257.79 ? 103  TYR D CD2 1 
ATOM   9622  C  CE1 . TYR D  3 105 ? -23.238 -27.265 -12.097  1.00 255.04 ? 103  TYR D CE1 1 
ATOM   9623  C  CE2 . TYR D  3 105 ? -21.299 -27.143 -10.695  1.00 272.11 ? 103  TYR D CE2 1 
ATOM   9624  C  CZ  . TYR D  3 105 ? -21.974 -27.707 -11.758  1.00 270.76 ? 103  TYR D CZ  1 
ATOM   9625  O  OH  . TYR D  3 105 ? -21.376 -28.715 -12.482  1.00 279.87 ? 103  TYR D OH  1 
ATOM   9626  N  N   . MET D  3 106 ? -25.449 -21.666 -9.620   1.00 248.95 ? 104  MET D N   1 
ATOM   9627  C  CA  . MET D  3 106 ? -26.271 -20.717 -8.880   1.00 234.94 ? 104  MET D CA  1 
ATOM   9628  C  C   . MET D  3 106 ? -27.666 -21.300 -8.712   1.00 227.03 ? 104  MET D C   1 
ATOM   9629  O  O   . MET D  3 106 ? -28.247 -21.815 -9.671   1.00 228.94 ? 104  MET D O   1 
ATOM   9630  C  CB  . MET D  3 106 ? -26.351 -19.380 -9.613   1.00 227.53 ? 104  MET D CB  1 
ATOM   9631  C  CG  . MET D  3 106 ? -24.999 -18.800 -9.970   1.00 235.65 ? 104  MET D CG  1 
ATOM   9632  S  SD  . MET D  3 106 ? -25.145 -17.476 -11.176  1.00 238.27 ? 104  MET D SD  1 
ATOM   9633  C  CE  . MET D  3 106 ? -25.746 -18.390 -12.595  1.00 246.49 ? 104  MET D CE  1 
ATOM   9634  N  N   . PHE D  3 107 ? -28.218 -21.188 -7.504   1.00 213.66 ? 105  PHE D N   1 
ATOM   9635  C  CA  . PHE D  3 107 ? -29.493 -21.816 -7.183   1.00 216.32 ? 105  PHE D CA  1 
ATOM   9636  C  C   . PHE D  3 107 ? -30.468 -20.811 -6.589   1.00 211.41 ? 105  PHE D C   1 
ATOM   9637  O  O   . PHE D  3 107 ? -30.082 -19.901 -5.850   1.00 218.65 ? 105  PHE D O   1 
ATOM   9638  C  CB  . PHE D  3 107 ? -29.315 -22.983 -6.204   1.00 224.13 ? 105  PHE D CB  1 
ATOM   9639  C  CG  . PHE D  3 107 ? -28.944 -24.274 -6.867   1.00 234.95 ? 105  PHE D CG  1 
ATOM   9640  C  CD1 . PHE D  3 107 ? -27.650 -24.498 -7.304   1.00 246.70 ? 105  PHE D CD1 1 
ATOM   9641  C  CD2 . PHE D  3 107 ? -29.892 -25.265 -7.053   1.00 230.89 ? 105  PHE D CD2 1 
ATOM   9642  C  CE1 . PHE D  3 107 ? -27.309 -25.690 -7.918   1.00 254.49 ? 105  PHE D CE1 1 
ATOM   9643  C  CE2 . PHE D  3 107 ? -29.558 -26.458 -7.664   1.00 243.66 ? 105  PHE D CE2 1 
ATOM   9644  C  CZ  . PHE D  3 107 ? -28.265 -26.672 -8.097   1.00 253.94 ? 105  PHE D CZ  1 
ATOM   9645  N  N   . PHE D  3 108 ? -31.748 -21.008 -6.903   1.00 197.83 ? 106  PHE D N   1 
ATOM   9646  C  CA  . PHE D  3 108 ? -32.835 -20.168 -6.425   1.00 188.84 ? 106  PHE D CA  1 
ATOM   9647  C  C   . PHE D  3 108 ? -33.966 -21.055 -5.921   1.00 194.25 ? 106  PHE D C   1 
ATOM   9648  O  O   . PHE D  3 108 ? -33.996 -22.265 -6.170   1.00 208.81 ? 106  PHE D O   1 
ATOM   9649  C  CB  . PHE D  3 108 ? -33.353 -19.238 -7.529   1.00 191.45 ? 106  PHE D CB  1 
ATOM   9650  C  CG  . PHE D  3 108 ? -32.344 -18.237 -8.003   1.00 199.07 ? 106  PHE D CG  1 
ATOM   9651  C  CD1 . PHE D  3 108 ? -31.390 -18.588 -8.943   1.00 204.71 ? 106  PHE D CD1 1 
ATOM   9652  C  CD2 . PHE D  3 108 ? -32.363 -16.937 -7.526   1.00 202.71 ? 106  PHE D CD2 1 
ATOM   9653  C  CE1 . PHE D  3 108 ? -30.463 -17.668 -9.388   1.00 208.67 ? 106  PHE D CE1 1 
ATOM   9654  C  CE2 . PHE D  3 108 ? -31.441 -16.009 -7.969   1.00 209.60 ? 106  PHE D CE2 1 
ATOM   9655  C  CZ  . PHE D  3 108 ? -30.488 -16.375 -8.900   1.00 215.76 ? 106  PHE D CZ  1 
ATOM   9656  N  N   . GLN D  3 109 ? -34.915 -20.441 -5.224   1.00 188.28 ? 107  GLN D N   1 
ATOM   9657  C  CA  . GLN D  3 109 ? -36.085 -21.150 -4.737   1.00 188.07 ? 107  GLN D CA  1 
ATOM   9658  C  C   . GLN D  3 109 ? -37.237 -20.988 -5.730   1.00 188.62 ? 107  GLN D C   1 
ATOM   9659  O  O   . GLN D  3 109 ? -37.026 -20.687 -6.907   1.00 194.73 ? 107  GLN D O   1 
ATOM   9660  C  CB  . GLN D  3 109 ? -36.485 -20.633 -3.348   1.00 199.18 ? 107  GLN D CB  1 
ATOM   9661  C  CG  . GLN D  3 109 ? -35.480 -20.867 -2.244   1.00 205.15 ? 107  GLN D CG  1 
ATOM   9662  C  CD  . GLN D  3 109 ? -35.970 -20.347 -0.898   1.00 197.09 ? 107  GLN D CD  1 
ATOM   9663  O  OE1 . GLN D  3 109 ? -36.979 -19.643 -0.814   1.00 187.45 ? 107  GLN D OE1 1 
ATOM   9664  N  NE2 . GLN D  3 109 ? -35.263 -20.710 0.164    1.00 201.87 ? 107  GLN D NE2 1 
ATOM   9665  N  N   . THR D  3 110 ? -38.461 -21.218 -5.258   1.00 183.76 ? 108  THR D N   1 
ATOM   9666  C  CA  . THR D  3 110 ? -39.690 -20.992 -6.018   1.00 184.46 ? 108  THR D CA  1 
ATOM   9667  C  C   . THR D  3 110 ? -40.819 -20.477 -5.150   1.00 181.74 ? 108  THR D C   1 
ATOM   9668  O  O   . THR D  3 110 ? -41.768 -19.887 -5.679   1.00 181.83 ? 108  THR D O   1 
ATOM   9669  C  CB  . THR D  3 110 ? -40.158 -22.274 -6.718   1.00 188.48 ? 108  THR D CB  1 
ATOM   9670  O  OG1 . THR D  3 110 ? -39.028 -22.964 -7.271   1.00 191.71 ? 108  THR D OG1 1 
ATOM   9671  C  CG2 . THR D  3 110 ? -41.142 -21.945 -7.838   1.00 190.19 ? 108  THR D CG2 1 
ATOM   9672  N  N   . SER D  3 111 ? -40.749 -20.679 -3.836   1.00 193.81 ? 109  SER D N   1 
ATOM   9673  C  CA  . SER D  3 111 ? -41.745 -20.159 -2.917   1.00 207.47 ? 109  SER D CA  1 
ATOM   9674  C  C   . SER D  3 111 ? -41.727 -18.640 -2.853   1.00 213.67 ? 109  SER D C   1 
ATOM   9675  O  O   . SER D  3 111 ? -42.739 -18.041 -2.473   1.00 229.40 ? 109  SER D O   1 
ATOM   9676  C  CB  . SER D  3 111 ? -41.499 -20.738 -1.522   1.00 208.91 ? 109  SER D CB  1 
ATOM   9677  O  OG  . SER D  3 111 ? -41.492 -22.156 -1.537   1.00 223.19 ? 109  SER D OG  1 
ATOM   9678  N  N   . GLU D  3 112 ? -40.595 -18.013 -3.190   1.00 215.81 ? 110  GLU D N   1 
ATOM   9679  C  CA  . GLU D  3 112 ? -40.482 -16.565 -3.310   1.00 197.79 ? 110  GLU D CA  1 
ATOM   9680  C  C   . GLU D  3 112 ? -40.561 -16.098 -4.756   1.00 205.18 ? 110  GLU D C   1 
ATOM   9681  O  O   . GLU D  3 112 ? -40.880 -14.927 -5.006   1.00 207.26 ? 110  GLU D O   1 
ATOM   9682  C  CB  . GLU D  3 112 ? -39.176 -16.082 -2.662   1.00 203.73 ? 110  GLU D CB  1 
ATOM   9683  C  CG  . GLU D  3 112 ? -39.069 -16.361 -1.106   1.00 179.53 ? 110  GLU D CG  1 
ATOM   9684  C  CD  . GLU D  3 112 ? -37.685 -15.906 -0.470   1.00 175.04 ? 110  GLU D CD  1 
ATOM   9685  O  OE1 . GLU D  3 112 ? -36.738 -15.520 -1.250   1.00 182.51 ? 110  GLU D OE1 1 
ATOM   9686  O  OE2 . GLU D  3 112 ? -37.556 -15.928 0.802    1.00 174.82 ? 110  GLU D OE2 1 
ATOM   9687  N  N   . LEU D  3 113 ? -40.293 -16.987 -5.707   1.00 184.50 ? 111  LEU D N   1 
ATOM   9688  C  CA  . LEU D  3 113 ? -40.464 -16.637 -7.111   1.00 181.45 ? 111  LEU D CA  1 
ATOM   9689  C  C   . LEU D  3 113 ? -41.943 -16.565 -7.466   1.00 177.99 ? 111  LEU D C   1 
ATOM   9690  O  O   . LEU D  3 113 ? -42.404 -15.602 -8.091   1.00 178.88 ? 111  LEU D O   1 
ATOM   9691  C  CB  . LEU D  3 113 ? -39.730 -17.656 -7.987   1.00 186.88 ? 111  LEU D CB  1 
ATOM   9692  C  CG  . LEU D  3 113 ? -38.217 -17.458 -8.173   1.00 183.12 ? 111  LEU D CG  1 
ATOM   9693  C  CD1 . LEU D  3 113 ? -37.962 -16.230 -9.013   1.00 189.82 ? 111  LEU D CD1 1 
ATOM   9694  C  CD2 . LEU D  3 113 ? -37.450 -17.363 -6.846   1.00 177.47 ? 111  LEU D CD2 1 
ATOM   9695  N  N   . ARG D  3 114 ? -42.708 -17.568 -7.043   1.00 200.34 ? 112  ARG D N   1 
ATOM   9696  C  CA  . ARG D  3 114 ? -44.156 -17.557 -7.171   1.00 202.97 ? 112  ARG D CA  1 
ATOM   9697  C  C   . ARG D  3 114 ? -44.792 -16.678 -6.103   1.00 204.39 ? 112  ARG D C   1 
ATOM   9698  O  O   . ARG D  3 114 ? -46.030 -16.614 -6.038   1.00 207.74 ? 112  ARG D O   1 
ATOM   9699  C  CB  . ARG D  3 114 ? -44.692 -19.005 -7.067   1.00 211.10 ? 112  ARG D CB  1 
ATOM   9700  C  CG  . ARG D  3 114 ? -46.131 -19.379 -7.734   1.00 218.67 ? 112  ARG D CG  1 
ATOM   9701  C  CD  . ARG D  3 114 ? -46.767 -20.827 -7.282   1.00 223.46 ? 112  ARG D CD  1 
ATOM   9702  N  NE  . ARG D  3 114 ? -46.477 -21.303 -5.886   1.00 229.94 ? 112  ARG D NE  1 
ATOM   9703  C  CZ  . ARG D  3 114 ? -47.235 -21.130 -4.776   1.00 210.73 ? 112  ARG D CZ  1 
ATOM   9704  N  NH1 . ARG D  3 114 ? -48.418 -20.463 -4.805   1.00 197.03 ? 112  ARG D NH1 1 
ATOM   9705  N  NH2 . ARG D  3 114 ? -46.789 -21.648 -3.614   1.00 208.35 ? 112  ARG D NH2 1 
ATOM   9706  N  N   . GLU D  3 115 ? -44.002 -15.968 -5.292   1.00 196.55 ? 113  GLU D N   1 
ATOM   9707  C  CA  . GLU D  3 115 ? -44.524 -14.981 -4.353   1.00 198.02 ? 113  GLU D CA  1 
ATOM   9708  C  C   . GLU D  3 115 ? -44.367 -13.565 -4.889   1.00 191.71 ? 113  GLU D C   1 
ATOM   9709  O  O   . GLU D  3 115 ? -45.290 -12.757 -4.760   1.00 196.23 ? 113  GLU D O   1 
ATOM   9710  C  CB  . GLU D  3 115 ? -43.830 -15.129 -2.987   1.00 197.74 ? 113  GLU D CB  1 
ATOM   9711  C  CG  . GLU D  3 115 ? -44.571 -14.518 -1.819   1.00 195.99 ? 113  GLU D CG  1 
ATOM   9712  C  CD  . GLU D  3 115 ? -44.412 -13.025 -1.787   1.00 199.03 ? 113  GLU D CD  1 
ATOM   9713  O  OE1 . GLU D  3 115 ? -43.311 -12.559 -2.148   1.00 182.01 ? 113  GLU D OE1 1 
ATOM   9714  O  OE2 . GLU D  3 115 ? -45.366 -12.322 -1.390   1.00 217.66 ? 113  GLU D OE2 1 
ATOM   9715  N  N   . ALA D  3 116 ? -43.249 -13.272 -5.558   1.00 185.17 ? 114  ALA D N   1 
ATOM   9716  C  CA  . ALA D  3 116 ? -43.105 -11.979 -6.219   1.00 191.41 ? 114  ALA D CA  1 
ATOM   9717  C  C   . ALA D  3 116 ? -43.979 -11.895 -7.467   1.00 203.04 ? 114  ALA D C   1 
ATOM   9718  O  O   . ALA D  3 116 ? -44.567 -10.844 -7.756   1.00 214.29 ? 114  ALA D O   1 
ATOM   9719  C  CB  . ALA D  3 116 ? -41.637 -11.731 -6.571   1.00 181.42 ? 114  ALA D CB  1 
ATOM   9720  N  N   . VAL D  3 117 ? -44.085 -12.993 -8.210   1.00 192.94 ? 115  VAL D N   1 
ATOM   9721  C  CA  . VAL D  3 117 ? -44.975 -13.084 -9.365   1.00 186.21 ? 115  VAL D CA  1 
ATOM   9722  C  C   . VAL D  3 117 ? -45.887 -14.288 -9.164   1.00 191.21 ? 115  VAL D C   1 
ATOM   9723  O  O   . VAL D  3 117 ? -45.514 -15.413 -9.532   1.00 198.60 ? 115  VAL D O   1 
ATOM   9724  C  CB  . VAL D  3 117 ? -44.189 -13.193 -10.678  1.00 186.97 ? 115  VAL D CB  1 
ATOM   9725  C  CG1 . VAL D  3 117 ? -45.135 -13.150 -11.867  1.00 193.50 ? 115  VAL D CG1 1 
ATOM   9726  C  CG2 . VAL D  3 117 ? -43.157 -12.081 -10.777  1.00 186.97 ? 115  VAL D CG2 1 
ATOM   9727  N  N   . PRO D  3 118 ? -47.072 -14.106 -8.570   1.00 197.42 ? 116  PRO D N   1 
ATOM   9728  C  CA  . PRO D  3 118 ? -47.957 -15.245 -8.296   1.00 204.61 ? 116  PRO D CA  1 
ATOM   9729  C  C   . PRO D  3 118 ? -48.334 -16.032 -9.539   1.00 210.07 ? 116  PRO D C   1 
ATOM   9730  O  O   . PRO D  3 118 ? -48.135 -17.248 -9.593   1.00 229.34 ? 116  PRO D O   1 
ATOM   9731  C  CB  . PRO D  3 118 ? -49.189 -14.584 -7.663   1.00 204.86 ? 116  PRO D CB  1 
ATOM   9732  C  CG  . PRO D  3 118 ? -48.676 -13.306 -7.087   1.00 200.59 ? 116  PRO D CG  1 
ATOM   9733  C  CD  . PRO D  3 118 ? -47.625 -12.842 -8.056   1.00 195.10 ? 116  PRO D CD  1 
ATOM   9734  N  N   . GLU D  3 119 ? -48.891 -15.354 -10.537  1.00 203.54 ? 117  GLU D N   1 
ATOM   9735  C  CA  . GLU D  3 119 ? -49.333 -16.066 -11.729  1.00 216.77 ? 117  GLU D CA  1 
ATOM   9736  C  C   . GLU D  3 119 ? -48.266 -15.996 -12.815  1.00 214.25 ? 117  GLU D C   1 
ATOM   9737  O  O   . GLU D  3 119 ? -47.711 -14.912 -13.061  1.00 215.15 ? 117  GLU D O   1 
ATOM   9738  C  CB  . GLU D  3 119 ? -50.648 -15.481 -12.239  1.00 221.10 ? 117  GLU D CB  1 
ATOM   9739  C  CG  . GLU D  3 119 ? -51.336 -16.335 -13.290  1.00 233.71 ? 117  GLU D CG  1 
ATOM   9740  C  CD  . GLU D  3 119 ? -52.754 -15.888 -13.570  1.00 241.48 ? 117  GLU D CD  1 
ATOM   9741  O  OE1 . GLU D  3 119 ? -53.200 -14.899 -12.950  1.00 240.65 ? 117  GLU D OE1 1 
ATOM   9742  O  OE2 . GLU D  3 119 ? -53.422 -16.524 -14.412  1.00 248.24 ? 117  GLU D OE2 1 
ATOM   9743  N  N   . PRO D  3 120 ? -47.925 -17.123 -13.451  1.00 199.43 ? 118  PRO D N   1 
ATOM   9744  C  CA  . PRO D  3 120 ? -46.846 -17.113 -14.455  1.00 194.35 ? 118  PRO D CA  1 
ATOM   9745  C  C   . PRO D  3 120 ? -47.088 -16.169 -15.616  1.00 194.42 ? 118  PRO D C   1 
ATOM   9746  O  O   . PRO D  3 120 ? -46.126 -15.785 -16.294  1.00 193.02 ? 118  PRO D O   1 
ATOM   9747  C  CB  . PRO D  3 120 ? -46.804 -18.570 -14.938  1.00 201.70 ? 118  PRO D CB  1 
ATOM   9748  C  CG  . PRO D  3 120 ? -47.422 -19.356 -13.840  1.00 205.49 ? 118  PRO D CG  1 
ATOM   9749  C  CD  . PRO D  3 120 ? -48.480 -18.473 -13.254  1.00 202.86 ? 118  PRO D CD  1 
ATOM   9750  N  N   . VAL D  3 121 ? -48.337 -15.780 -15.872  1.00 189.35 ? 119  VAL D N   1 
ATOM   9751  C  CA  . VAL D  3 121 ? -48.619 -14.933 -17.025  1.00 186.96 ? 119  VAL D CA  1 
ATOM   9752  C  C   . VAL D  3 121 ? -48.196 -13.496 -16.764  1.00 182.70 ? 119  VAL D C   1 
ATOM   9753  O  O   . VAL D  3 121 ? -47.880 -12.757 -17.706  1.00 177.41 ? 119  VAL D O   1 
ATOM   9754  C  CB  . VAL D  3 121 ? -50.113 -15.019 -17.384  1.00 191.62 ? 119  VAL D CB  1 
ATOM   9755  C  CG1 . VAL D  3 121 ? -50.360 -14.440 -18.766  1.00 197.71 ? 119  VAL D CG1 1 
ATOM   9756  C  CG2 . VAL D  3 121 ? -50.610 -16.459 -17.298  1.00 198.96 ? 119  VAL D CG2 1 
ATOM   9757  N  N   . LEU D  3 122 ? -48.152 -13.083 -15.495  1.00 189.05 ? 120  LEU D N   1 
ATOM   9758  C  CA  . LEU D  3 122 ? -47.818 -11.708 -15.151  1.00 186.22 ? 120  LEU D CA  1 
ATOM   9759  C  C   . LEU D  3 122 ? -46.381 -11.371 -15.506  1.00 177.42 ? 120  LEU D C   1 
ATOM   9760  O  O   . LEU D  3 122 ? -46.066 -10.198 -15.732  1.00 171.70 ? 120  LEU D O   1 
ATOM   9761  C  CB  . LEU D  3 122 ? -48.050 -11.478 -13.654  1.00 195.66 ? 120  LEU D CB  1 
ATOM   9762  C  CG  . LEU D  3 122 ? -49.446 -11.779 -13.099  1.00 202.19 ? 120  LEU D CG  1 
ATOM   9763  C  CD1 . LEU D  3 122 ? -49.487 -11.622 -11.587  1.00 193.99 ? 120  LEU D CD1 1 
ATOM   9764  C  CD2 . LEU D  3 122 ? -50.486 -10.883 -13.751  1.00 208.84 ? 120  LEU D CD2 1 
ATOM   9765  N  N   . LEU D  3 123 ? -45.518 -12.379 -15.574  1.00 189.96 ? 121  LEU D N   1 
ATOM   9766  C  CA  . LEU D  3 123 ? -44.103 -12.162 -15.831  1.00 193.62 ? 121  LEU D CA  1 
ATOM   9767  C  C   . LEU D  3 123 ? -43.903 -11.586 -17.226  1.00 205.99 ? 121  LEU D C   1 
ATOM   9768  O  O   . LEU D  3 123 ? -44.414 -12.125 -18.213  1.00 216.81 ? 121  LEU D O   1 
ATOM   9769  C  CB  . LEU D  3 123 ? -43.345 -13.480 -15.679  1.00 197.34 ? 121  LEU D CB  1 
ATOM   9770  C  CG  . LEU D  3 123 ? -41.853 -13.430 -15.353  1.00 193.25 ? 121  LEU D CG  1 
ATOM   9771  C  CD1 . LEU D  3 123 ? -41.014 -13.203 -16.598  1.00 194.49 ? 121  LEU D CD1 1 
ATOM   9772  C  CD2 . LEU D  3 123 ? -41.590 -12.349 -14.318  1.00 189.62 ? 121  LEU D CD2 1 
ATOM   9773  N  N   . SER D  3 124 ? -43.173 -10.476 -17.303  1.00 199.30 ? 122  SER D N   1 
ATOM   9774  C  CA  . SER D  3 124 ? -42.876 -9.828  -18.571  1.00 193.04 ? 122  SER D CA  1 
ATOM   9775  C  C   . SER D  3 124 ? -41.414 -10.004 -18.966  1.00 199.79 ? 122  SER D C   1 
ATOM   9776  O  O   . SER D  3 124 ? -41.125 -10.556 -20.032  1.00 193.65 ? 122  SER D O   1 
ATOM   9777  C  CB  . SER D  3 124 ? -43.252 -8.341  -18.494  1.00 182.13 ? 122  SER D CB  1 
ATOM   9778  O  OG  . SER D  3 124 ? -43.007 -7.680  -19.721  1.00 179.30 ? 122  SER D OG  1 
ATOM   9779  N  N   . ARG D  3 125 ? -40.477 -9.544  -18.134  1.00 220.09 ? 123  ARG D N   1 
ATOM   9780  C  CA  . ARG D  3 125 ? -39.049 -9.703  -18.391  1.00 224.88 ? 123  ARG D CA  1 
ATOM   9781  C  C   . ARG D  3 125 ? -38.334 -10.119 -17.113  1.00 226.35 ? 123  ARG D C   1 
ATOM   9782  O  O   . ARG D  3 125 ? -38.514 -9.493  -16.063  1.00 233.01 ? 123  ARG D O   1 
ATOM   9783  C  CB  . ARG D  3 125 ? -38.428 -8.411  -18.938  1.00 223.84 ? 123  ARG D CB  1 
ATOM   9784  C  CG  . ARG D  3 125 ? -36.931 -8.515  -19.218  1.00 215.46 ? 123  ARG D CG  1 
ATOM   9785  C  CD  . ARG D  3 125 ? -36.404 -7.275  -19.936  1.00 216.92 ? 123  ARG D CD  1 
ATOM   9786  N  NE  . ARG D  3 125 ? -34.990 -7.394  -20.286  1.00 220.95 ? 123  ARG D NE  1 
ATOM   9787  C  CZ  . ARG D  3 125 ? -34.332 -6.530  -21.056  1.00 217.54 ? 123  ARG D CZ  1 
ATOM   9788  N  NH1 . ARG D  3 125 ? -34.959 -5.477  -21.568  1.00 215.06 ? 123  ARG D NH1 1 
ATOM   9789  N  NH2 . ARG D  3 125 ? -33.046 -6.722  -21.319  1.00 210.46 ? 123  ARG D NH2 1 
ATOM   9790  N  N   . ALA D  3 126 ? -37.518 -11.169 -17.207  1.00 216.06 ? 124  ALA D N   1 
ATOM   9791  C  CA  . ALA D  3 126 ? -36.785 -11.707 -16.061  1.00 216.44 ? 124  ALA D CA  1 
ATOM   9792  C  C   . ALA D  3 126 ? -35.324 -11.900 -16.457  1.00 200.71 ? 124  ALA D C   1 
ATOM   9793  O  O   . ALA D  3 126 ? -34.983 -12.875 -17.132  1.00 192.25 ? 124  ALA D O   1 
ATOM   9794  C  CB  . ALA D  3 126 ? -37.405 -13.014 -15.582  1.00 230.83 ? 124  ALA D CB  1 
ATOM   9795  N  N   . GLU D  3 127 ? -34.469 -10.965 -16.056  1.00 196.87 ? 125  GLU D N   1 
ATOM   9796  C  CA  . GLU D  3 127 ? -33.047 -11.015 -16.367  1.00 196.31 ? 125  GLU D CA  1 
ATOM   9797  C  C   . GLU D  3 127 ? -32.248 -11.370 -15.118  1.00 187.89 ? 125  GLU D C   1 
ATOM   9798  O  O   . GLU D  3 127 ? -32.442 -10.770 -14.056  1.00 191.96 ? 125  GLU D O   1 
ATOM   9799  C  CB  . GLU D  3 127 ? -32.575 -9.687  -16.965  1.00 199.72 ? 125  GLU D CB  1 
ATOM   9800  C  CG  . GLU D  3 127 ? -33.101 -8.453  -16.251  1.00 197.56 ? 125  GLU D CG  1 
ATOM   9801  C  CD  . GLU D  3 127 ? -32.754 -7.166  -16.977  1.00 198.48 ? 125  GLU D CD  1 
ATOM   9802  O  OE1 . GLU D  3 127 ? -31.900 -7.208  -17.887  1.00 194.13 ? 125  GLU D OE1 1 
ATOM   9803  O  OE2 . GLU D  3 127 ? -33.340 -6.114  -16.643  1.00 202.13 ? 125  GLU D OE2 1 
ATOM   9804  N  N   . LEU D  3 128 ? -31.366 -12.356 -15.251  1.00 181.00 ? 126  LEU D N   1 
ATOM   9805  C  CA  . LEU D  3 128 ? -30.485 -12.786 -14.172  1.00 182.28 ? 126  LEU D CA  1 
ATOM   9806  C  C   . LEU D  3 128 ? -29.209 -11.953 -14.207  1.00 178.42 ? 126  LEU D C   1 
ATOM   9807  O  O   . LEU D  3 128 ? -28.497 -11.947 -15.216  1.00 181.59 ? 126  LEU D O   1 
ATOM   9808  C  CB  . LEU D  3 128 ? -30.162 -14.271 -14.309  1.00 190.84 ? 126  LEU D CB  1 
ATOM   9809  C  CG  . LEU D  3 128 ? -29.150 -14.834 -13.311  1.00 204.74 ? 126  LEU D CG  1 
ATOM   9810  C  CD1 . LEU D  3 128 ? -29.669 -14.698 -11.889  1.00 213.56 ? 126  LEU D CD1 1 
ATOM   9811  C  CD2 . LEU D  3 128 ? -28.834 -16.284 -13.641  1.00 206.90 ? 126  LEU D CD2 1 
ATOM   9812  N  N   . ARG D  3 129 ? -28.922 -11.248 -13.117  1.00 181.69 ? 127  ARG D N   1 
ATOM   9813  C  CA  . ARG D  3 129 ? -27.793 -10.331 -13.060  1.00 183.63 ? 127  ARG D CA  1 
ATOM   9814  C  C   . ARG D  3 129 ? -26.710 -10.837 -12.115  1.00 202.90 ? 127  ARG D C   1 
ATOM   9815  O  O   . ARG D  3 129 ? -27.007 -11.373 -11.042  1.00 221.23 ? 127  ARG D O   1 
ATOM   9816  C  CB  . ARG D  3 129 ? -28.247 -8.940  -12.630  1.00 182.24 ? 127  ARG D CB  1 
ATOM   9817  C  CG  . ARG D  3 129 ? -29.348 -8.384  -13.496  1.00 173.73 ? 127  ARG D CG  1 
ATOM   9818  C  CD  . ARG D  3 129 ? -29.403 -6.884  -13.391  1.00 171.76 ? 127  ARG D CD  1 
ATOM   9819  N  NE  . ARG D  3 129 ? -30.377 -6.326  -14.315  1.00 173.30 ? 127  ARG D NE  1 
ATOM   9820  C  CZ  . ARG D  3 129 ? -30.525 -5.028  -14.543  1.00 176.73 ? 127  ARG D CZ  1 
ATOM   9821  N  NH1 . ARG D  3 129 ? -29.744 -4.153  -13.926  1.00 174.43 ? 127  ARG D NH1 1 
ATOM   9822  N  NH2 . ARG D  3 129 ? -31.446 -4.608  -15.397  1.00 188.28 ? 127  ARG D NH2 1 
ATOM   9823  N  N   . LEU D  3 130 ? -25.451 -10.662 -12.526  1.00 206.42 ? 128  LEU D N   1 
ATOM   9824  C  CA  . LEU D  3 130 ? -24.307 -11.107 -11.737  1.00 208.05 ? 128  LEU D CA  1 
ATOM   9825  C  C   . LEU D  3 130 ? -23.387 -9.943  -11.375  1.00 205.94 ? 128  LEU D C   1 
ATOM   9826  O  O   . LEU D  3 130 ? -23.774 -8.775  -11.484  1.00 200.53 ? 128  LEU D O   1 
ATOM   9827  C  CB  . LEU D  3 130 ? -23.517 -12.172 -12.501  1.00 206.24 ? 128  LEU D CB  1 
ATOM   9828  C  CG  . LEU D  3 130 ? -24.291 -13.309 -13.175  1.00 200.47 ? 128  LEU D CG  1 
ATOM   9829  C  CD1 . LEU D  3 130 ? -23.331 -14.351 -13.717  1.00 207.36 ? 128  LEU D CD1 1 
ATOM   9830  C  CD2 . LEU D  3 130 ? -25.277 -13.952 -12.221  1.00 201.38 ? 128  LEU D CD2 1 
ATOM   9831  N  N   . LEU D  3 131 ? -22.165 -10.256 -10.945  1.00 208.36 ? 129  LEU D N   1 
ATOM   9832  C  CA  . LEU D  3 131 ? -21.160 -9.250  -10.616  1.00 201.79 ? 129  LEU D CA  1 
ATOM   9833  C  C   . LEU D  3 131 ? -19.796 -9.740  -11.076  1.00 209.47 ? 129  LEU D C   1 
ATOM   9834  O  O   . LEU D  3 131 ? -19.282 -10.734 -10.553  1.00 217.29 ? 129  LEU D O   1 
ATOM   9835  C  CB  . LEU D  3 131 ? -21.140 -8.954  -9.115   1.00 198.15 ? 129  LEU D CB  1 
ATOM   9836  C  CG  . LEU D  3 131 ? -20.159 -7.860  -8.691   1.00 207.17 ? 129  LEU D CG  1 
ATOM   9837  C  CD1 . LEU D  3 131 ? -20.220 -6.669  -9.635   1.00 188.96 ? 129  LEU D CD1 1 
ATOM   9838  C  CD2 . LEU D  3 131 ? -20.432 -7.429  -7.260   1.00 228.15 ? 129  LEU D CD2 1 
ATOM   9839  N  N   . ARG D  3 132 ? -19.202 -9.028  -12.027  1.00 210.22 ? 130  ARG D N   1 
ATOM   9840  C  CA  . ARG D  3 132 ? -17.902 -9.387  -12.572  1.00 206.36 ? 130  ARG D CA  1 
ATOM   9841  C  C   . ARG D  3 132 ? -16.774 -8.814  -11.728  1.00 207.45 ? 130  ARG D C   1 
ATOM   9842  O  O   . ARG D  3 132 ? -16.940 -7.844  -10.986  1.00 212.77 ? 130  ARG D O   1 
ATOM   9843  C  CB  . ARG D  3 132 ? -17.748 -8.886  -14.010  1.00 210.19 ? 130  ARG D CB  1 
ATOM   9844  C  CG  . ARG D  3 132 ? -18.502 -9.683  -15.052  1.00 228.76 ? 130  ARG D CG  1 
ATOM   9845  C  CD  . ARG D  3 132 ? -18.115 -9.221  -16.459  1.00 247.53 ? 130  ARG D CD  1 
ATOM   9846  N  NE  . ARG D  3 132 ? -18.857 -9.924  -17.507  1.00 267.37 ? 130  ARG D NE  1 
ATOM   9847  C  CZ  . ARG D  3 132 ? -18.729 -9.690  -18.813  1.00 270.62 ? 130  ARG D CZ  1 
ATOM   9848  N  NH1 . ARG D  3 132 ? -17.881 -8.766  -19.247  1.00 271.51 ? 130  ARG D NH1 1 
ATOM   9849  N  NH2 . ARG D  3 132 ? -19.448 -10.384 -19.689  1.00 266.77 ? 130  ARG D NH2 1 
ATOM   9850  N  N   . LEU D  3 133 ? -15.622 -9.456  -11.830  1.00 200.02 ? 131  LEU D N   1 
ATOM   9851  C  CA  . LEU D  3 133 ? -14.367 -8.932  -11.325  1.00 202.96 ? 131  LEU D CA  1 
ATOM   9852  C  C   . LEU D  3 133 ? -13.459 -8.666  -12.514  1.00 210.88 ? 131  LEU D C   1 
ATOM   9853  O  O   . LEU D  3 133 ? -13.781 -9.020  -13.650  1.00 216.08 ? 131  LEU D O   1 
ATOM   9854  C  CB  . LEU D  3 133 ? -13.722 -9.910  -10.341  1.00 205.51 ? 131  LEU D CB  1 
ATOM   9855  C  CG  . LEU D  3 133 ? -14.469 -10.012 -9.013   1.00 204.74 ? 131  LEU D CG  1 
ATOM   9856  C  CD1 . LEU D  3 133 ? -13.768 -10.972 -8.070   1.00 226.59 ? 131  LEU D CD1 1 
ATOM   9857  C  CD2 . LEU D  3 133 ? -14.635 -8.641  -8.370   1.00 197.77 ? 131  LEU D CD2 1 
ATOM   9858  N  N   . LYS D  3 134 ? -12.322 -8.028  -12.255  1.00 216.56 ? 132  LYS D N   1 
ATOM   9859  C  CA  . LYS D  3 134 ? -11.404 -7.727  -13.346  1.00 233.45 ? 132  LYS D CA  1 
ATOM   9860  C  C   . LYS D  3 134 ? -10.957 -9.027  -14.007  1.00 240.08 ? 132  LYS D C   1 
ATOM   9861  O  O   . LYS D  3 134 ? -10.554 -9.977  -13.329  1.00 263.19 ? 132  LYS D O   1 
ATOM   9862  C  CB  . LYS D  3 134 ? -10.199 -6.927  -12.837  1.00 244.78 ? 132  LYS D CB  1 
ATOM   9863  C  CG  . LYS D  3 134 ? -9.350  -7.605  -11.758  1.00 240.93 ? 132  LYS D CG  1 
ATOM   9864  C  CD  . LYS D  3 134 ? -8.125  -6.754  -11.424  1.00 231.55 ? 132  LYS D CD  1 
ATOM   9865  C  CE  . LYS D  3 134 ? -7.242  -7.403  -10.368  1.00 223.75 ? 132  LYS D CE  1 
ATOM   9866  N  NZ  . LYS D  3 134 ? -6.027  -6.584  -10.085  1.00 221.50 ? 132  LYS D NZ  1 
ATOM   9867  N  N   . LEU D  3 135 ? -11.073 -9.090  -15.339  1.00 212.31 ? 133  LEU D N   1 
ATOM   9868  C  CA  . LEU D  3 135 ? -10.753 -10.309 -16.068  1.00 214.87 ? 133  LEU D CA  1 
ATOM   9869  C  C   . LEU D  3 135 ? -9.701  -10.119 -17.154  1.00 225.53 ? 133  LEU D C   1 
ATOM   9870  O  O   . LEU D  3 135 ? -9.232  -11.116 -17.717  1.00 235.25 ? 133  LEU D O   1 
ATOM   9871  C  CB  . LEU D  3 135 ? -12.025 -10.908 -16.689  1.00 213.80 ? 133  LEU D CB  1 
ATOM   9872  C  CG  . LEU D  3 135 ? -11.922 -12.403 -16.986  1.00 223.30 ? 133  LEU D CG  1 
ATOM   9873  C  CD1 . LEU D  3 135 ? -11.423 -13.122 -15.751  1.00 227.60 ? 133  LEU D CD1 1 
ATOM   9874  C  CD2 . LEU D  3 135 ? -13.251 -12.968 -17.412  1.00 225.82 ? 133  LEU D CD2 1 
ATOM   9875  N  N   . LYS D  3 136 ? -9.315  -8.887  -17.456  1.00 232.40 ? 134  LYS D N   1 
ATOM   9876  C  CA  . LYS D  3 136 ? -8.312  -8.574  -18.493  1.00 244.24 ? 134  LYS D CA  1 
ATOM   9877  C  C   . LYS D  3 136 ? -8.792  -9.149  -19.832  1.00 259.46 ? 134  LYS D C   1 
ATOM   9878  O  O   . LYS D  3 136 ? -10.002 -9.147  -20.110  1.00 264.81 ? 134  LYS D O   1 
ATOM   9879  C  CB  . LYS D  3 136 ? -6.935  -9.047  -18.065  1.00 243.39 ? 134  LYS D CB  1 
ATOM   9880  C  CG  . LYS D  3 136 ? -6.367  -8.381  -16.825  1.00 245.52 ? 134  LYS D CG  1 
ATOM   9881  C  CD  . LYS D  3 136 ? -5.001  -8.966  -16.484  1.00 251.73 ? 134  LYS D CD  1 
ATOM   9882  C  CE  . LYS D  3 136 ? -4.385  -8.317  -15.253  1.00 242.15 ? 134  LYS D CE  1 
ATOM   9883  N  NZ  . LYS D  3 136 ? -3.047  -8.910  -14.976  1.00 238.33 ? 134  LYS D NZ  1 
ATOM   9884  N  N   . VAL D  3 137 ? -7.888  -9.719  -20.628  1.00 267.57 ? 135  VAL D N   1 
ATOM   9885  C  CA  . VAL D  3 137 ? -8.037  -9.834  -22.079  1.00 276.65 ? 135  VAL D CA  1 
ATOM   9886  C  C   . VAL D  3 137 ? -9.345  -10.478 -22.535  1.00 275.02 ? 135  VAL D C   1 
ATOM   9887  O  O   . VAL D  3 137 ? -10.262 -9.779  -22.984  1.00 274.20 ? 135  VAL D O   1 
ATOM   9888  C  CB  . VAL D  3 137 ? -6.837  -10.586 -22.678  1.00 272.63 ? 135  VAL D CB  1 
ATOM   9889  C  CG1 . VAL D  3 137 ? -6.743  -10.315 -24.174  1.00 267.14 ? 135  VAL D CG1 1 
ATOM   9890  C  CG2 . VAL D  3 137 ? -5.555  -10.167 -21.980  1.00 269.49 ? 135  VAL D CG2 1 
ATOM   9891  N  N   . GLU D  3 138 ? -9.450  -11.804 -22.440  1.00 266.37 ? 136  GLU D N   1 
ATOM   9892  C  CA  . GLU D  3 138 ? -10.549 -12.487 -23.109  1.00 253.14 ? 136  GLU D CA  1 
ATOM   9893  C  C   . GLU D  3 138 ? -11.036 -13.681 -22.305  1.00 244.09 ? 136  GLU D C   1 
ATOM   9894  O  O   . GLU D  3 138 ? -10.247 -14.382 -21.666  1.00 253.23 ? 136  GLU D O   1 
ATOM   9895  C  CB  . GLU D  3 138 ? -10.129 -12.965 -24.507  1.00 255.48 ? 136  GLU D CB  1 
ATOM   9896  C  CG  . GLU D  3 138 ? -9.994  -11.873 -25.551  1.00 249.26 ? 136  GLU D CG  1 
ATOM   9897  C  CD  . GLU D  3 138 ? -9.385  -12.389 -26.839  1.00 255.72 ? 136  GLU D CD  1 
ATOM   9898  O  OE1 . GLU D  3 138 ? -9.001  -13.575 -26.889  1.00 259.78 ? 136  GLU D OE1 1 
ATOM   9899  O  OE2 . GLU D  3 138 ? -9.291  -11.606 -27.805  1.00 260.04 ? 136  GLU D OE2 1 
ATOM   9900  N  N   . GLN D  3 139 ? -12.353 -13.876 -22.318  1.00 230.73 ? 137  GLN D N   1 
ATOM   9901  C  CA  . GLN D  3 139 ? -12.967 -15.128 -21.905  1.00 232.77 ? 137  GLN D CA  1 
ATOM   9902  C  C   . GLN D  3 139 ? -14.307 -15.256 -22.621  1.00 236.81 ? 137  GLN D C   1 
ATOM   9903  O  O   . GLN D  3 139 ? -14.900 -14.262 -23.044  1.00 247.52 ? 137  GLN D O   1 
ATOM   9904  C  CB  . GLN D  3 139 ? -13.129 -15.211 -20.384  1.00 227.36 ? 137  GLN D CB  1 
ATOM   9905  C  CG  . GLN D  3 139 ? -13.253 -16.634 -19.854  1.00 232.59 ? 137  GLN D CG  1 
ATOM   9906  C  CD  . GLN D  3 139 ? -12.020 -17.482 -20.110  1.00 245.60 ? 137  GLN D CD  1 
ATOM   9907  O  OE1 . GLN D  3 139 ? -10.915 -16.964 -20.279  1.00 251.25 ? 137  GLN D OE1 1 
ATOM   9908  N  NE2 . GLN D  3 139 ? -12.205 -18.797 -20.130  1.00 246.58 ? 137  GLN D NE2 1 
ATOM   9909  N  N   . HIS D  3 140 ? -14.780 -16.495 -22.759  1.00 223.74 ? 138  HIS D N   1 
ATOM   9910  C  CA  . HIS D  3 140 ? -16.060 -16.786 -23.397  1.00 214.62 ? 138  HIS D CA  1 
ATOM   9911  C  C   . HIS D  3 140 ? -16.913 -17.638 -22.467  1.00 214.10 ? 138  HIS D C   1 
ATOM   9912  O  O   . HIS D  3 140 ? -16.421 -18.613 -21.891  1.00 217.31 ? 138  HIS D O   1 
ATOM   9913  C  CB  . HIS D  3 140 ? -15.856 -17.500 -24.734  1.00 226.69 ? 138  HIS D CB  1 
ATOM   9914  C  CG  . HIS D  3 140 ? -17.103 -17.620 -25.553  1.00 229.79 ? 138  HIS D CG  1 
ATOM   9915  N  ND1 . HIS D  3 140 ? -17.184 -18.425 -26.669  1.00 233.01 ? 138  HIS D ND1 1 
ATOM   9916  C  CD2 . HIS D  3 140 ? -18.316 -17.030 -25.426  1.00 226.63 ? 138  HIS D CD2 1 
ATOM   9917  C  CE1 . HIS D  3 140 ? -18.396 -18.335 -27.187  1.00 230.36 ? 138  HIS D CE1 1 
ATOM   9918  N  NE2 . HIS D  3 140 ? -19.101 -17.493 -26.454  1.00 221.05 ? 138  HIS D NE2 1 
ATOM   9919  N  N   . VAL D  3 141 ? -18.189 -17.275 -22.325  1.00 222.12 ? 139  VAL D N   1 
ATOM   9920  C  CA  . VAL D  3 141 ? -19.085 -17.889 -21.348  1.00 225.84 ? 139  VAL D CA  1 
ATOM   9921  C  C   . VAL D  3 141 ? -20.320 -18.440 -22.054  1.00 234.71 ? 139  VAL D C   1 
ATOM   9922  O  O   . VAL D  3 141 ? -20.917 -17.760 -22.898  1.00 233.12 ? 139  VAL D O   1 
ATOM   9923  C  CB  . VAL D  3 141 ? -19.490 -16.884 -20.257  1.00 210.58 ? 139  VAL D CB  1 
ATOM   9924  C  CG1 . VAL D  3 141 ? -20.455 -17.527 -19.278  1.00 210.53 ? 139  VAL D CG1 1 
ATOM   9925  C  CG2 . VAL D  3 141 ? -18.260 -16.367 -19.536  1.00 206.63 ? 139  VAL D CG2 1 
ATOM   9926  N  N   . GLU D  3 142 ? -20.694 -19.675 -21.711  1.00 243.98 ? 140  GLU D N   1 
ATOM   9927  C  CA  . GLU D  3 142 ? -21.943 -20.292 -22.139  1.00 239.19 ? 140  GLU D CA  1 
ATOM   9928  C  C   . GLU D  3 142 ? -22.820 -20.566 -20.923  1.00 235.35 ? 140  GLU D C   1 
ATOM   9929  O  O   . GLU D  3 142 ? -22.327 -21.006 -19.880  1.00 231.34 ? 140  GLU D O   1 
ATOM   9930  C  CB  . GLU D  3 142 ? -21.685 -21.598 -22.899  1.00 244.11 ? 140  GLU D CB  1 
ATOM   9931  C  CG  . GLU D  3 142 ? -20.819 -21.440 -24.139  1.00 251.93 ? 140  GLU D CG  1 
ATOM   9932  C  CD  . GLU D  3 142 ? -20.567 -22.760 -24.841  1.00 260.60 ? 140  GLU D CD  1 
ATOM   9933  O  OE1 . GLU D  3 142 ? -21.158 -23.776 -24.419  1.00 263.27 ? 140  GLU D OE1 1 
ATOM   9934  O  OE2 . GLU D  3 142 ? -19.778 -22.783 -25.810  1.00 264.77 ? 140  GLU D OE2 1 
ATOM   9935  N  N   . LEU D  3 143 ? -24.123 -20.334 -21.065  1.00 239.56 ? 141  LEU D N   1 
ATOM   9936  C  CA  . LEU D  3 143 ? -25.075 -20.482 -19.971  1.00 244.40 ? 141  LEU D CA  1 
ATOM   9937  C  C   . LEU D  3 143 ? -26.005 -21.662 -20.232  1.00 252.46 ? 141  LEU D C   1 
ATOM   9938  O  O   . LEU D  3 143 ? -26.359 -21.942 -21.382  1.00 271.96 ? 141  LEU D O   1 
ATOM   9939  C  CB  . LEU D  3 143 ? -25.892 -19.199 -19.779  1.00 240.79 ? 141  LEU D CB  1 
ATOM   9940  C  CG  . LEU D  3 143 ? -26.825 -19.123 -18.565  1.00 230.49 ? 141  LEU D CG  1 
ATOM   9941  C  CD1 . LEU D  3 143 ? -26.042 -19.240 -17.262  1.00 222.76 ? 141  LEU D CD1 1 
ATOM   9942  C  CD2 . LEU D  3 143 ? -27.638 -17.835 -18.588  1.00 230.72 ? 141  LEU D CD2 1 
ATOM   9943  N  N   . TYR D  3 144 ? -26.386 -22.361 -19.160  1.00 242.89 ? 142  TYR D N   1 
ATOM   9944  C  CA  . TYR D  3 144 ? -27.228 -23.546 -19.254  1.00 242.05 ? 142  TYR D CA  1 
ATOM   9945  C  C   . TYR D  3 144 ? -28.402 -23.451 -18.284  1.00 228.27 ? 142  TYR D C   1 
ATOM   9946  O  O   . TYR D  3 144 ? -28.427 -22.621 -17.371  1.00 218.71 ? 142  TYR D O   1 
ATOM   9947  C  CB  . TYR D  3 144 ? -26.413 -24.819 -18.988  1.00 247.14 ? 142  TYR D CB  1 
ATOM   9948  C  CG  . TYR D  3 144 ? -25.378 -25.093 -20.054  1.00 246.97 ? 142  TYR D CG  1 
ATOM   9949  C  CD1 . TYR D  3 144 ? -25.697 -25.840 -21.180  1.00 251.09 ? 142  TYR D CD1 1 
ATOM   9950  C  CD2 . TYR D  3 144 ? -24.086 -24.595 -19.943  1.00 242.22 ? 142  TYR D CD2 1 
ATOM   9951  C  CE1 . TYR D  3 144 ? -24.760 -26.091 -22.159  1.00 254.72 ? 142  TYR D CE1 1 
ATOM   9952  C  CE2 . TYR D  3 144 ? -23.142 -24.841 -20.920  1.00 250.63 ? 142  TYR D CE2 1 
ATOM   9953  C  CZ  . TYR D  3 144 ? -23.484 -25.590 -22.025  1.00 254.77 ? 142  TYR D CZ  1 
ATOM   9954  O  OH  . TYR D  3 144 ? -22.544 -25.839 -22.999  1.00 260.75 ? 142  TYR D OH  1 
ATOM   9955  N  N   . GLN D  3 145 ? -29.381 -24.331 -18.492  1.00 236.93 ? 143  GLN D N   1 
ATOM   9956  C  CA  . GLN D  3 145 ? -30.583 -24.415 -17.676  1.00 236.27 ? 143  GLN D CA  1 
ATOM   9957  C  C   . GLN D  3 145 ? -30.732 -25.831 -17.129  1.00 239.65 ? 143  GLN D C   1 
ATOM   9958  O  O   . GLN D  3 145 ? -30.304 -26.797 -17.763  1.00 248.31 ? 143  GLN D O   1 
ATOM   9959  C  CB  . GLN D  3 145 ? -31.821 -24.032 -18.500  1.00 244.50 ? 143  GLN D CB  1 
ATOM   9960  C  CG  . GLN D  3 145 ? -33.117 -23.939 -17.717  1.00 244.51 ? 143  GLN D CG  1 
ATOM   9961  C  CD  . GLN D  3 145 ? -34.323 -23.783 -18.623  1.00 244.60 ? 143  GLN D CD  1 
ATOM   9962  O  OE1 . GLN D  3 145 ? -34.186 -23.493 -19.814  1.00 247.29 ? 143  GLN D OE1 1 
ATOM   9963  N  NE2 . GLN D  3 145 ? -35.512 -23.982 -18.065  1.00 239.17 ? 143  GLN D NE2 1 
ATOM   9964  N  N   . LYS D  3 146 ? -31.349 -25.958 -15.953  1.00 230.96 ? 144  LYS D N   1 
ATOM   9965  C  CA  . LYS D  3 146 ? -31.535 -27.265 -15.323  1.00 230.09 ? 144  LYS D CA  1 
ATOM   9966  C  C   . LYS D  3 146 ? -32.792 -27.958 -15.848  1.00 235.62 ? 144  LYS D C   1 
ATOM   9967  O  O   . LYS D  3 146 ? -33.907 -27.465 -15.644  1.00 236.10 ? 144  LYS D O   1 
ATOM   9968  C  CB  . LYS D  3 146 ? -31.621 -27.111 -13.807  1.00 226.40 ? 144  LYS D CB  1 
ATOM   9969  C  CG  . LYS D  3 146 ? -31.704 -28.437 -13.072  1.00 226.43 ? 144  LYS D CG  1 
ATOM   9970  C  CD  . LYS D  3 146 ? -31.829 -28.229 -11.569  1.00 237.62 ? 144  LYS D CD  1 
ATOM   9971  C  CE  . LYS D  3 146 ? -33.078 -27.429 -11.217  1.00 254.18 ? 144  LYS D CE  1 
ATOM   9972  N  NZ  . LYS D  3 146 ? -34.346 -28.123 -11.591  1.00 259.89 ? 144  LYS D NZ  1 
ATOM   9973  N  N   . TYR D  3 147 ? -32.610 -29.112 -16.500  1.00 246.13 ? 145  TYR D N   1 
ATOM   9974  C  CA  . TYR D  3 147 ? -33.693 -29.921 -17.059  1.00 247.41 ? 145  TYR D CA  1 
ATOM   9975  C  C   . TYR D  3 147 ? -33.682 -31.323 -16.454  1.00 255.66 ? 145  TYR D C   1 
ATOM   9976  O  O   . TYR D  3 147 ? -32.622 -31.947 -16.351  1.00 263.75 ? 145  TYR D O   1 
ATOM   9977  C  CB  . TYR D  3 147 ? -33.577 -30.007 -18.589  1.00 248.50 ? 145  TYR D CB  1 
ATOM   9978  C  CG  . TYR D  3 147 ? -34.222 -28.833 -19.295  1.00 255.12 ? 145  TYR D CG  1 
ATOM   9979  C  CD1 . TYR D  3 147 ? -35.576 -28.839 -19.599  1.00 254.97 ? 145  TYR D CD1 1 
ATOM   9980  C  CD2 . TYR D  3 147 ? -33.477 -27.712 -19.652  1.00 263.49 ? 145  TYR D CD2 1 
ATOM   9981  C  CE1 . TYR D  3 147 ? -36.169 -27.760 -20.235  1.00 259.31 ? 145  TYR D CE1 1 
ATOM   9982  C  CE2 . TYR D  3 147 ? -34.060 -26.633 -20.291  1.00 263.59 ? 145  TYR D CE2 1 
ATOM   9983  C  CZ  . TYR D  3 147 ? -35.402 -26.659 -20.578  1.00 260.26 ? 145  TYR D CZ  1 
ATOM   9984  O  OH  . TYR D  3 147 ? -35.954 -25.568 -21.213  1.00 249.42 ? 145  TYR D OH  1 
ATOM   9985  N  N   . SER D  3 148 ? -34.856 -31.816 -16.045  1.00 249.24 ? 146  SER D N   1 
ATOM   9986  C  CA  . SER D  3 148 ? -34.998 -33.117 -15.385  1.00 243.27 ? 146  SER D CA  1 
ATOM   9987  C  C   . SER D  3 148 ? -34.151 -33.218 -14.126  1.00 245.87 ? 146  SER D C   1 
ATOM   9988  O  O   . SER D  3 148 ? -33.837 -34.327 -13.679  1.00 229.05 ? 146  SER D O   1 
ATOM   9989  C  CB  . SER D  3 148 ? -34.663 -34.276 -16.336  1.00 230.03 ? 146  SER D CB  1 
ATOM   9990  O  OG  . SER D  3 148 ? -35.529 -34.278 -17.456  1.00 229.49 ? 146  SER D OG  1 
ATOM   9991  N  N   . GLN D  3 149 ? -33.738 -32.066 -13.582  1.00 264.87 ? 147  GLN D N   1 
ATOM   9992  C  CA  . GLN D  3 149 ? -33.039 -31.954 -12.299  1.00 266.73 ? 147  GLN D CA  1 
ATOM   9993  C  C   . GLN D  3 149 ? -31.627 -32.538 -12.342  1.00 267.31 ? 147  GLN D C   1 
ATOM   9994  O  O   . GLN D  3 149 ? -30.980 -32.689 -11.298  1.00 264.62 ? 147  GLN D O   1 
ATOM   9995  C  CB  . GLN D  3 149 ? -33.886 -32.581 -11.178  1.00 266.58 ? 147  GLN D CB  1 
ATOM   9996  C  CG  . GLN D  3 149 ? -35.027 -31.676 -10.752  1.00 248.48 ? 147  GLN D CG  1 
ATOM   9997  C  CD  . GLN D  3 149 ? -35.724 -32.144 -9.494   1.00 247.91 ? 147  GLN D CD  1 
ATOM   9998  O  OE1 . GLN D  3 149 ? -35.145 -32.850 -8.667   1.00 261.88 ? 147  GLN D OE1 1 
ATOM   9999  N  NE2 . GLN D  3 149 ? -36.982 -31.751 -9.343   1.00 241.10 ? 147  GLN D NE2 1 
ATOM   10000 N  N   . ASN D  3 150 ? -31.137 -32.814 -13.548  1.00 248.83 ? 148  ASN D N   1 
ATOM   10001 C  CA  . ASN D  3 150 ? -29.889 -33.515 -13.797  1.00 230.66 ? 148  ASN D CA  1 
ATOM   10002 C  C   . ASN D  3 150 ? -29.343 -33.113 -15.178  1.00 228.78 ? 148  ASN D C   1 
ATOM   10003 O  O   . ASN D  3 150 ? -28.136 -32.918 -15.312  1.00 231.26 ? 148  ASN D O   1 
ATOM   10004 C  CB  . ASN D  3 150 ? -30.145 -35.027 -13.631  1.00 226.29 ? 148  ASN D CB  1 
ATOM   10005 C  CG  . ASN D  3 150 ? -30.480 -35.485 -12.094  1.00 211.65 ? 148  ASN D CG  1 
ATOM   10006 O  OD1 . ASN D  3 150 ? -29.850 -35.028 -11.088  1.00 208.90 ? 148  ASN D OD1 1 
ATOM   10007 N  ND2 . ASN D  3 150 ? -31.546 -36.348 -11.957  1.00 219.54 ? 148  ASN D ND2 1 
ATOM   10008 N  N   . SER D  3 151 ? -30.190 -32.950 -16.209  1.00 239.68 ? 149  SER D N   1 
ATOM   10009 C  CA  . SER D  3 151 ? -29.685 -32.599 -17.540  1.00 243.81 ? 149  SER D CA  1 
ATOM   10010 C  C   . SER D  3 151 ? -29.625 -31.076 -17.698  1.00 242.63 ? 149  SER D C   1 
ATOM   10011 O  O   . SER D  3 151 ? -30.398 -30.341 -17.082  1.00 244.91 ? 149  SER D O   1 
ATOM   10012 C  CB  . SER D  3 151 ? -30.561 -33.193 -18.645  1.00 245.02 ? 149  SER D CB  1 
ATOM   10013 O  OG  . SER D  3 151 ? -30.765 -34.581 -18.444  1.00 243.21 ? 149  SER D OG  1 
ATOM   10014 N  N   . TRP D  3 152 ? -28.689 -30.599 -18.522  1.00 254.37 ? 150  TRP D N   1 
ATOM   10015 C  CA  . TRP D  3 152 ? -28.488 -29.166 -18.723  1.00 246.84 ? 150  TRP D CA  1 
ATOM   10016 C  C   . TRP D  3 152 ? -28.670 -28.813 -20.194  1.00 248.87 ? 150  TRP D C   1 
ATOM   10017 O  O   . TRP D  3 152 ? -28.166 -29.522 -21.071  1.00 269.15 ? 150  TRP D O   1 
ATOM   10018 C  CB  . TRP D  3 152 ? -27.102 -28.744 -18.231  1.00 247.33 ? 150  TRP D CB  1 
ATOM   10019 C  CG  . TRP D  3 152 ? -26.813 -29.187 -16.817  1.00 246.24 ? 150  TRP D CG  1 
ATOM   10020 C  CD1 . TRP D  3 152 ? -26.200 -30.346 -16.424  1.00 252.03 ? 150  TRP D CD1 1 
ATOM   10021 C  CD2 . TRP D  3 152 ? -27.114 -28.468 -15.617  1.00 240.37 ? 150  TRP D CD2 1 
ATOM   10022 N  NE1 . TRP D  3 152 ? -26.109 -30.392 -15.052  1.00 245.70 ? 150  TRP D NE1 1 
ATOM   10023 C  CE2 . TRP D  3 152 ? -26.660 -29.250 -14.534  1.00 241.49 ? 150  TRP D CE2 1 
ATOM   10024 C  CE3 . TRP D  3 152 ? -27.725 -27.240 -15.352  1.00 233.65 ? 150  TRP D CE3 1 
ATOM   10025 C  CZ2 . TRP D  3 152 ? -26.799 -28.839 -13.209  1.00 238.90 ? 150  TRP D CZ2 1 
ATOM   10026 C  CZ3 . TRP D  3 152 ? -27.862 -26.836 -14.040  1.00 227.23 ? 150  TRP D CZ3 1 
ATOM   10027 C  CH2 . TRP D  3 152 ? -27.401 -27.631 -12.985  1.00 227.59 ? 150  TRP D CH2 1 
ATOM   10028 N  N   . ARG D  3 153 ? -29.399 -27.729 -20.465  1.00 233.14 ? 151  ARG D N   1 
ATOM   10029 C  CA  . ARG D  3 153 ? -29.677 -27.300 -21.829  1.00 234.36 ? 151  ARG D CA  1 
ATOM   10030 C  C   . ARG D  3 153 ? -29.120 -25.904 -22.075  1.00 236.02 ? 151  ARG D C   1 
ATOM   10031 O  O   . ARG D  3 153 ? -29.224 -25.020 -21.220  1.00 234.17 ? 151  ARG D O   1 
ATOM   10032 C  CB  . ARG D  3 153 ? -31.177 -27.321 -22.116  1.00 230.17 ? 151  ARG D CB  1 
ATOM   10033 C  CG  . ARG D  3 153 ? -31.532 -26.961 -23.543  1.00 242.33 ? 151  ARG D CG  1 
ATOM   10034 C  CD  . ARG D  3 153 ? -33.029 -26.801 -23.728  1.00 255.58 ? 151  ARG D CD  1 
ATOM   10035 N  NE  . ARG D  3 153 ? -33.354 -26.320 -25.069  1.00 269.23 ? 151  ARG D NE  1 
ATOM   10036 C  CZ  . ARG D  3 153 ? -33.497 -25.037 -25.390  1.00 270.31 ? 151  ARG D CZ  1 
ATOM   10037 N  NH1 . ARG D  3 153 ? -33.346 -24.100 -24.462  1.00 267.75 ? 151  ARG D NH1 1 
ATOM   10038 N  NH2 . ARG D  3 153 ? -33.792 -24.692 -26.637  1.00 265.94 ? 151  ARG D NH2 1 
ATOM   10039 N  N   . TYR D  3 154 ? -28.549 -25.720 -23.265  1.00 232.68 ? 152  TYR D N   1 
ATOM   10040 C  CA  . TYR D  3 154 ? -27.944 -24.457 -23.666  1.00 232.53 ? 152  TYR D CA  1 
ATOM   10041 C  C   . TYR D  3 154 ? -28.952 -23.313 -23.615  1.00 225.73 ? 152  TYR D C   1 
ATOM   10042 O  O   . TYR D  3 154 ? -30.161 -23.510 -23.764  1.00 221.32 ? 152  TYR D O   1 
ATOM   10043 C  CB  . TYR D  3 154 ? -27.376 -24.587 -25.080  1.00 255.89 ? 152  TYR D CB  1 
ATOM   10044 C  CG  . TYR D  3 154 ? -26.662 -23.360 -25.599  1.00 256.56 ? 152  TYR D CG  1 
ATOM   10045 C  CD1 . TYR D  3 154 ? -25.324 -23.133 -25.303  1.00 257.32 ? 152  TYR D CD1 1 
ATOM   10046 C  CD2 . TYR D  3 154 ? -27.321 -22.439 -26.402  1.00 249.67 ? 152  TYR D CD2 1 
ATOM   10047 C  CE1 . TYR D  3 154 ? -24.667 -22.016 -25.782  1.00 248.21 ? 152  TYR D CE1 1 
ATOM   10048 C  CE2 . TYR D  3 154 ? -26.674 -21.321 -26.886  1.00 240.47 ? 152  TYR D CE2 1 
ATOM   10049 C  CZ  . TYR D  3 154 ? -25.347 -21.115 -26.573  1.00 239.71 ? 152  TYR D CZ  1 
ATOM   10050 O  OH  . TYR D  3 154 ? -24.700 -20.004 -27.055  1.00 229.78 ? 152  TYR D OH  1 
ATOM   10051 N  N   . LEU D  3 155 ? -28.439 -22.106 -23.375  1.00 236.10 ? 153  LEU D N   1 
ATOM   10052 C  CA  . LEU D  3 155 ? -29.259 -20.900 -23.384  1.00 229.86 ? 153  LEU D CA  1 
ATOM   10053 C  C   . LEU D  3 155 ? -28.660 -19.841 -24.304  1.00 227.65 ? 153  LEU D C   1 
ATOM   10054 O  O   . LEU D  3 155 ? -29.037 -19.743 -25.478  1.00 225.99 ? 153  LEU D O   1 
ATOM   10055 C  CB  . LEU D  3 155 ? -29.420 -20.353 -21.966  1.00 224.28 ? 153  LEU D CB  1 
ATOM   10056 C  CG  . LEU D  3 155 ? -30.226 -21.246 -21.021  1.00 225.89 ? 153  LEU D CG  1 
ATOM   10057 C  CD1 . LEU D  3 155 ? -30.390 -20.581 -19.669  1.00 222.93 ? 153  LEU D CD1 1 
ATOM   10058 C  CD2 . LEU D  3 155 ? -31.584 -21.589 -21.615  1.00 222.04 ? 153  LEU D CD2 1 
ATOM   10059 N  N   . SER D  3 156 ? -27.733 -19.038 -23.782  1.00 225.53 ? 154  SER D N   1 
ATOM   10060 C  CA  . SER D  3 156 ? -27.095 -17.976 -24.547  1.00 223.65 ? 154  SER D CA  1 
ATOM   10061 C  C   . SER D  3 156 ? -25.583 -18.028 -24.344  1.00 226.31 ? 154  SER D C   1 
ATOM   10062 O  O   . SER D  3 156 ? -25.056 -18.845 -23.583  1.00 231.93 ? 154  SER D O   1 
ATOM   10063 C  CB  . SER D  3 156 ? -27.651 -16.601 -24.158  1.00 211.11 ? 154  SER D CB  1 
ATOM   10064 O  OG  . SER D  3 156 ? -27.363 -16.301 -22.805  1.00 206.19 ? 154  SER D OG  1 
ATOM   10065 N  N   . ASN D  3 157 ? -24.886 -17.145 -25.056  1.00 217.42 ? 155  ASN D N   1 
ATOM   10066 C  CA  . ASN D  3 157 ? -23.438 -17.017 -24.980  1.00 216.84 ? 155  ASN D CA  1 
ATOM   10067 C  C   . ASN D  3 157 ? -23.074 -15.542 -25.041  1.00 208.79 ? 155  ASN D C   1 
ATOM   10068 O  O   . ASN D  3 157 ? -23.845 -14.716 -25.535  1.00 208.59 ? 155  ASN D O   1 
ATOM   10069 C  CB  . ASN D  3 157 ? -22.743 -17.769 -26.116  1.00 232.06 ? 155  ASN D CB  1 
ATOM   10070 C  CG  . ASN D  3 157 ? -23.134 -17.235 -27.478  1.00 242.11 ? 155  ASN D CG  1 
ATOM   10071 O  OD1 . ASN D  3 157 ? -22.528 -16.292 -27.986  1.00 241.78 ? 155  ASN D OD1 1 
ATOM   10072 N  ND2 . ASN D  3 157 ? -24.161 -17.830 -28.072  1.00 244.14 ? 155  ASN D ND2 1 
ATOM   10073 N  N   . ARG D  3 158 ? -21.882 -15.214 -24.543  1.00 225.51 ? 156  ARG D N   1 
ATOM   10074 C  CA  . ARG D  3 158 ? -21.449 -13.822 -24.527  1.00 224.56 ? 156  ARG D CA  1 
ATOM   10075 C  C   . ARG D  3 158 ? -19.932 -13.748 -24.442  1.00 238.61 ? 156  ARG D C   1 
ATOM   10076 O  O   . ARG D  3 158 ? -19.320 -14.434 -23.616  1.00 247.36 ? 156  ARG D O   1 
ATOM   10077 C  CB  . ARG D  3 158 ? -22.088 -13.072 -23.353  1.00 211.83 ? 156  ARG D CB  1 
ATOM   10078 C  CG  . ARG D  3 158 ? -21.905 -11.566 -23.393  1.00 207.81 ? 156  ARG D CG  1 
ATOM   10079 C  CD  . ARG D  3 158 ? -22.937 -10.870 -22.512  1.00 202.04 ? 156  ARG D CD  1 
ATOM   10080 N  NE  . ARG D  3 158 ? -24.304 -11.250 -22.870  1.00 207.61 ? 156  ARG D NE  1 
ATOM   10081 C  CZ  . ARG D  3 158 ? -25.393 -10.849 -22.219  1.00 205.20 ? 156  ARG D CZ  1 
ATOM   10082 N  NH1 . ARG D  3 158 ? -25.285 -10.047 -21.170  1.00 192.31 ? 156  ARG D NH1 1 
ATOM   10083 N  NH2 . ARG D  3 158 ? -26.594 -11.249 -22.620  1.00 211.30 ? 156  ARG D NH2 1 
ATOM   10084 N  N   . LEU D  3 159 ? -19.334 -12.923 -25.298  1.00 242.67 ? 157  LEU D N   1 
ATOM   10085 C  CA  . LEU D  3 159 ? -17.905 -12.658 -25.230  1.00 243.82 ? 157  LEU D CA  1 
ATOM   10086 C  C   . LEU D  3 159 ? -17.642 -11.578 -24.186  1.00 249.94 ? 157  LEU D C   1 
ATOM   10087 O  O   . LEU D  3 159 ? -18.508 -10.748 -23.893  1.00 236.43 ? 157  LEU D O   1 
ATOM   10088 C  CB  . LEU D  3 159 ? -17.368 -12.229 -26.598  1.00 241.31 ? 157  LEU D CB  1 
ATOM   10089 C  CG  . LEU D  3 159 ? -15.855 -12.301 -26.838  1.00 246.44 ? 157  LEU D CG  1 
ATOM   10090 C  CD1 . LEU D  3 159 ? -15.358 -13.742 -26.802  1.00 250.98 ? 157  LEU D CD1 1 
ATOM   10091 C  CD2 . LEU D  3 159 ? -15.485 -11.638 -28.158  1.00 254.38 ? 157  LEU D CD2 1 
ATOM   10092 N  N   . LEU D  3 160 ? -16.450 -11.616 -23.595  1.00 269.01 ? 158  LEU D N   1 
ATOM   10093 C  CA  . LEU D  3 160 ? -16.102 -10.754 -22.473  1.00 251.63 ? 158  LEU D CA  1 
ATOM   10094 C  C   . LEU D  3 160 ? -15.010 -9.764  -22.865  1.00 252.65 ? 158  LEU D C   1 
ATOM   10095 O  O   . LEU D  3 160 ? -14.100 -10.095 -23.633  1.00 265.15 ? 158  LEU D O   1 
ATOM   10096 C  CB  . LEU D  3 160 ? -15.664 -11.591 -21.266  1.00 239.84 ? 158  LEU D CB  1 
ATOM   10097 C  CG  . LEU D  3 160 ? -16.809 -12.185 -20.429  1.00 229.82 ? 158  LEU D CG  1 
ATOM   10098 C  CD1 . LEU D  3 160 ? -17.608 -13.246 -21.175  1.00 229.91 ? 158  LEU D CD1 1 
ATOM   10099 C  CD2 . LEU D  3 160 ? -16.289 -12.757 -19.126  1.00 239.71 ? 158  LEU D CD2 1 
ATOM   10100 N  N   . ALA D  3 161 ? -15.103 -8.545  -22.313  1.00 244.75 ? 159  ALA D N   1 
ATOM   10101 C  CA  . ALA D  3 161 ? -14.225 -7.421  -22.595  1.00 251.18 ? 159  ALA D CA  1 
ATOM   10102 C  C   . ALA D  3 161 ? -13.311 -7.117  -21.409  1.00 250.28 ? 159  ALA D C   1 
ATOM   10103 O  O   . ALA D  3 161 ? -13.688 -7.329  -20.252  1.00 245.94 ? 159  ALA D O   1 
ATOM   10104 C  CB  . ALA D  3 161 ? -15.040 -6.168  -22.934  1.00 253.87 ? 159  ALA D CB  1 
ATOM   10105 N  N   . PRO D  3 162 ? -12.097 -6.612  -21.667  1.00 262.60 ? 160  PRO D N   1 
ATOM   10106 C  CA  . PRO D  3 162 ? -11.155 -6.351  -20.570  1.00 265.49 ? 160  PRO D CA  1 
ATOM   10107 C  C   . PRO D  3 162 ? -11.573 -5.208  -19.662  1.00 247.51 ? 160  PRO D C   1 
ATOM   10108 O  O   . PRO D  3 162 ? -11.060 -4.088  -19.773  1.00 241.17 ? 160  PRO D O   1 
ATOM   10109 C  CB  . PRO D  3 162 ? -9.844  -6.031  -21.304  1.00 278.99 ? 160  PRO D CB  1 
ATOM   10110 C  CG  . PRO D  3 162 ? -10.269 -5.558  -22.647  1.00 279.13 ? 160  PRO D CG  1 
ATOM   10111 C  CD  . PRO D  3 162 ? -11.493 -6.358  -22.986  1.00 271.70 ? 160  PRO D CD  1 
ATOM   10112 N  N   . SER D  3 163 ? -12.489 -5.488  -18.743  1.00 239.47 ? 161  SER D N   1 
ATOM   10113 C  CA  . SER D  3 163 ? -12.892 -4.512  -17.745  1.00 232.34 ? 161  SER D CA  1 
ATOM   10114 C  C   . SER D  3 163 ? -11.909 -4.586  -16.587  1.00 230.26 ? 161  SER D C   1 
ATOM   10115 O  O   . SER D  3 163 ? -11.739 -5.645  -15.972  1.00 226.40 ? 161  SER D O   1 
ATOM   10116 C  CB  . SER D  3 163 ? -14.318 -4.770  -17.262  1.00 223.58 ? 161  SER D CB  1 
ATOM   10117 O  OG  . SER D  3 163 ? -14.651 -3.924  -16.174  1.00 220.53 ? 161  SER D OG  1 
ATOM   10118 N  N   . ASP D  3 164 ? -11.258 -3.461  -16.300  1.00 245.36 ? 162  ASP D N   1 
ATOM   10119 C  CA  . ASP D  3 164 ? -10.340 -3.389  -15.176  1.00 249.24 ? 162  ASP D CA  1 
ATOM   10120 C  C   . ASP D  3 164 ? -11.085 -3.267  -13.854  1.00 245.12 ? 162  ASP D C   1 
ATOM   10121 O  O   . ASP D  3 164 ? -10.488 -3.479  -12.794  1.00 256.18 ? 162  ASP D O   1 
ATOM   10122 C  CB  . ASP D  3 164 ? -9.391  -2.197  -15.359  1.00 258.25 ? 162  ASP D CB  1 
ATOM   10123 C  CG  . ASP D  3 164 ? -8.658  -2.227  -16.698  1.00 261.19 ? 162  ASP D CG  1 
ATOM   10124 O  OD1 . ASP D  3 164 ? -7.756  -3.073  -16.882  1.00 259.78 ? 162  ASP D OD1 1 
ATOM   10125 O  OD2 . ASP D  3 164 ? -8.988  -1.395  -17.572  1.00 260.78 ? 162  ASP D OD2 1 
ATOM   10126 N  N   . SER D  3 165 ? -12.371 -2.943  -13.904  1.00 234.22 ? 163  SER D N   1 
ATOM   10127 C  CA  . SER D  3 165 ? -13.225 -2.696  -12.756  1.00 234.38 ? 163  SER D CA  1 
ATOM   10128 C  C   . SER D  3 165 ? -14.334 -3.740  -12.673  1.00 238.93 ? 163  SER D C   1 
ATOM   10129 O  O   . SER D  3 165 ? -14.641 -4.414  -13.664  1.00 236.66 ? 163  SER D O   1 
ATOM   10130 C  CB  . SER D  3 165 ? -13.844 -1.293  -12.852  1.00 227.16 ? 163  SER D CB  1 
ATOM   10131 O  OG  . SER D  3 165 ? -14.658 -1.181  -14.008  1.00 222.59 ? 163  SER D OG  1 
ATOM   10132 N  N   . PRO D  3 166 ? -14.942 -3.915  -11.498  1.00 232.98 ? 164  PRO D N   1 
ATOM   10133 C  CA  . PRO D  3 166 ? -16.086 -4.834  -11.389  1.00 228.12 ? 164  PRO D CA  1 
ATOM   10134 C  C   . PRO D  3 166 ? -17.244 -4.391  -12.274  1.00 225.76 ? 164  PRO D C   1 
ATOM   10135 O  O   . PRO D  3 166 ? -17.618 -3.216  -12.296  1.00 224.78 ? 164  PRO D O   1 
ATOM   10136 C  CB  . PRO D  3 166 ? -16.448 -4.777  -9.899   1.00 221.72 ? 164  PRO D CB  1 
ATOM   10137 C  CG  . PRO D  3 166 ? -15.812 -3.523  -9.381   1.00 220.17 ? 164  PRO D CG  1 
ATOM   10138 C  CD  . PRO D  3 166 ? -14.560 -3.361  -10.187  1.00 221.69 ? 164  PRO D CD  1 
ATOM   10139 N  N   . GLU D  3 167 ? -17.790 -5.340  -13.034  1.00 231.19 ? 165  GLU D N   1 
ATOM   10140 C  CA  . GLU D  3 167 ? -18.845 -5.080  -14.003  1.00 236.89 ? 165  GLU D CA  1 
ATOM   10141 C  C   . GLU D  3 167 ? -20.124 -5.831  -13.634  1.00 238.64 ? 165  GLU D C   1 
ATOM   10142 O  O   . GLU D  3 167 ? -20.080 -6.895  -13.009  1.00 244.52 ? 165  GLU D O   1 
ATOM   10143 C  CB  . GLU D  3 167 ? -18.377 -5.471  -15.409  1.00 244.29 ? 165  GLU D CB  1 
ATOM   10144 C  CG  . GLU D  3 167 ? -19.143 -4.825  -16.543  1.00 257.13 ? 165  GLU D CG  1 
ATOM   10145 C  CD  . GLU D  3 167 ? -18.531 -5.141  -17.890  1.00 267.91 ? 165  GLU D CD  1 
ATOM   10146 O  OE1 . GLU D  3 167 ? -17.464 -5.792  -17.911  1.00 268.27 ? 165  GLU D OE1 1 
ATOM   10147 O  OE2 . GLU D  3 167 ? -19.108 -4.737  -18.922  1.00 272.24 ? 165  GLU D OE2 1 
ATOM   10148 N  N   . TRP D  3 168 ? -21.270 -5.264  -14.018  1.00 221.73 ? 166  TRP D N   1 
ATOM   10149 C  CA  . TRP D  3 168 ? -22.584 -5.833  -13.723  1.00 210.04 ? 166  TRP D CA  1 
ATOM   10150 C  C   . TRP D  3 168 ? -23.289 -6.201  -15.024  1.00 205.28 ? 166  TRP D C   1 
ATOM   10151 O  O   . TRP D  3 168 ? -23.520 -5.334  -15.876  1.00 207.54 ? 166  TRP D O   1 
ATOM   10152 C  CB  . TRP D  3 168 ? -23.421 -4.847  -12.908  1.00 225.23 ? 166  TRP D CB  1 
ATOM   10153 C  CG  . TRP D  3 168 ? -24.519 -5.465  -12.104  1.00 228.14 ? 166  TRP D CG  1 
ATOM   10154 C  CD1 . TRP D  3 168 ? -25.738 -5.877  -12.555  1.00 244.55 ? 166  TRP D CD1 1 
ATOM   10155 C  CD2 . TRP D  3 168 ? -24.497 -5.739  -10.699  1.00 220.23 ? 166  TRP D CD2 1 
ATOM   10156 N  NE1 . TRP D  3 168 ? -26.479 -6.386  -11.514  1.00 245.01 ? 166  TRP D NE1 1 
ATOM   10157 C  CE2 . TRP D  3 168 ? -25.737 -6.314  -10.365  1.00 229.97 ? 166  TRP D CE2 1 
ATOM   10158 C  CE3 . TRP D  3 168 ? -23.547 -5.550  -9.692   1.00 206.14 ? 166  TRP D CE3 1 
ATOM   10159 C  CZ2 . TRP D  3 168 ? -26.051 -6.706  -9.065   1.00 211.59 ? 166  TRP D CZ2 1 
ATOM   10160 C  CZ3 . TRP D  3 168 ? -23.860 -5.939  -8.404   1.00 202.52 ? 166  TRP D CZ3 1 
ATOM   10161 C  CH2 . TRP D  3 168 ? -25.101 -6.510  -8.101   1.00 199.95 ? 166  TRP D CH2 1 
ATOM   10162 N  N   . LEU D  3 169 ? -23.631 -7.482  -15.174  1.00 204.51 ? 167  LEU D N   1 
ATOM   10163 C  CA  . LEU D  3 169 ? -24.246 -8.017  -16.386  1.00 224.31 ? 167  LEU D CA  1 
ATOM   10164 C  C   . LEU D  3 169 ? -25.703 -8.414  -16.147  1.00 229.60 ? 167  LEU D C   1 
ATOM   10165 O  O   . LEU D  3 169 ? -26.249 -8.270  -15.050  1.00 232.43 ? 167  LEU D O   1 
ATOM   10166 C  CB  . LEU D  3 169 ? -23.448 -9.209  -16.914  1.00 218.62 ? 167  LEU D CB  1 
ATOM   10167 C  CG  . LEU D  3 169 ? -22.438 -8.866  -18.010  1.00 229.79 ? 167  LEU D CG  1 
ATOM   10168 C  CD1 . LEU D  3 169 ? -23.154 -8.425  -19.279  1.00 216.00 ? 167  LEU D CD1 1 
ATOM   10169 C  CD2 . LEU D  3 169 ? -21.469 -7.793  -17.533  1.00 247.16 ? 167  LEU D CD2 1 
ATOM   10170 N  N   . SER D  3 170 ? -26.334 -8.922  -17.207  1.00 219.45 ? 168  SER D N   1 
ATOM   10171 C  CA  . SER D  3 170 ? -27.725 -9.354  -17.151  1.00 202.21 ? 168  SER D CA  1 
ATOM   10172 C  C   . SER D  3 170 ? -28.008 -10.279 -18.326  1.00 196.40 ? 168  SER D C   1 
ATOM   10173 O  O   . SER D  3 170 ? -27.566 -10.019 -19.448  1.00 195.27 ? 168  SER D O   1 
ATOM   10174 C  CB  . SER D  3 170 ? -28.685 -8.161  -17.174  1.00 198.21 ? 168  SER D CB  1 
ATOM   10175 O  OG  . SER D  3 170 ? -28.589 -7.463  -18.401  1.00 208.87 ? 168  SER D OG  1 
ATOM   10176 N  N   . PHE D  3 171 ? -28.746 -11.357 -18.058  1.00 204.48 ? 169  PHE D N   1 
ATOM   10177 C  CA  . PHE D  3 171 ? -29.111 -12.347 -19.067  1.00 207.93 ? 169  PHE D CA  1 
ATOM   10178 C  C   . PHE D  3 171 ? -30.620 -12.532 -19.085  1.00 204.52 ? 169  PHE D C   1 
ATOM   10179 O  O   . PHE D  3 171 ? -31.213 -12.927 -18.076  1.00 209.63 ? 169  PHE D O   1 
ATOM   10180 C  CB  . PHE D  3 171 ? -28.424 -13.686 -18.800  1.00 214.39 ? 169  PHE D CB  1 
ATOM   10181 C  CG  . PHE D  3 171 ? -26.996 -13.727 -19.235  1.00 219.81 ? 169  PHE D CG  1 
ATOM   10182 C  CD1 . PHE D  3 171 ? -26.669 -14.090 -20.530  1.00 222.38 ? 169  PHE D CD1 1 
ATOM   10183 C  CD2 . PHE D  3 171 ? -25.981 -13.399 -18.353  1.00 227.93 ? 169  PHE D CD2 1 
ATOM   10184 C  CE1 . PHE D  3 171 ? -25.356 -14.132 -20.940  1.00 232.91 ? 169  PHE D CE1 1 
ATOM   10185 C  CE2 . PHE D  3 171 ? -24.663 -13.436 -18.754  1.00 236.03 ? 169  PHE D CE2 1 
ATOM   10186 C  CZ  . PHE D  3 171 ? -24.349 -13.804 -20.052  1.00 242.55 ? 169  PHE D CZ  1 
ATOM   10187 N  N   . ASP D  3 172 ? -31.230 -12.270 -20.237  1.00 201.39 ? 170  ASP D N   1 
ATOM   10188 C  CA  . ASP D  3 172 ? -32.675 -12.408 -20.405  1.00 208.18 ? 170  ASP D CA  1 
ATOM   10189 C  C   . ASP D  3 172 ? -33.055 -13.883 -20.368  1.00 214.25 ? 170  ASP D C   1 
ATOM   10190 O  O   . ASP D  3 172 ? -32.977 -14.584 -21.379  1.00 226.59 ? 170  ASP D O   1 
ATOM   10191 C  CB  . ASP D  3 172 ? -33.117 -11.766 -21.714  1.00 206.44 ? 170  ASP D CB  1 
ATOM   10192 C  CG  . ASP D  3 172 ? -34.613 -11.536 -21.774  1.00 197.96 ? 170  ASP D CG  1 
ATOM   10193 O  OD1 . ASP D  3 172 ? -35.353 -12.487 -22.111  1.00 198.12 ? 170  ASP D OD1 1 
ATOM   10194 O  OD2 . ASP D  3 172 ? -35.047 -10.401 -21.489  1.00 192.09 ? 170  ASP D OD2 1 
ATOM   10195 N  N   . VAL D  3 173 ? -33.488 -14.359 -19.202  1.00 209.85 ? 171  VAL D N   1 
ATOM   10196 C  CA  . VAL D  3 173 ? -33.925 -15.742 -19.047  1.00 215.39 ? 171  VAL D CA  1 
ATOM   10197 C  C   . VAL D  3 173 ? -35.428 -15.753 -18.799  1.00 211.70 ? 171  VAL D C   1 
ATOM   10198 O  O   . VAL D  3 173 ? -35.940 -16.569 -18.024  1.00 212.16 ? 171  VAL D O   1 
ATOM   10199 C  CB  . VAL D  3 173 ? -33.160 -16.449 -17.912  1.00 219.27 ? 171  VAL D CB  1 
ATOM   10200 C  CG1 . VAL D  3 173 ? -31.718 -16.704 -18.325  1.00 214.81 ? 171  VAL D CG1 1 
ATOM   10201 C  CG2 . VAL D  3 173 ? -33.209 -15.619 -16.637  1.00 222.87 ? 171  VAL D CG2 1 
ATOM   10202 N  N   . THR D  3 174 ? -36.140 -14.840 -19.464  1.00 209.51 ? 172  THR D N   1 
ATOM   10203 C  CA  . THR D  3 174 ? -37.582 -14.721 -19.267  1.00 212.13 ? 172  THR D CA  1 
ATOM   10204 C  C   . THR D  3 174 ? -38.300 -16.019 -19.617  1.00 220.29 ? 172  THR D C   1 
ATOM   10205 O  O   . THR D  3 174 ? -39.164 -16.485 -18.864  1.00 224.10 ? 172  THR D O   1 
ATOM   10206 C  CB  . THR D  3 174 ? -38.122 -13.562 -20.100  1.00 212.20 ? 172  THR D CB  1 
ATOM   10207 O  OG1 . THR D  3 174 ? -37.515 -12.341 -19.661  1.00 193.97 ? 172  THR D OG1 1 
ATOM   10208 C  CG2 . THR D  3 174 ? -39.629 -13.458 -19.943  1.00 218.27 ? 172  THR D CG2 1 
ATOM   10209 N  N   . GLY D  3 175 ? -37.952 -16.619 -20.761  1.00 216.60 ? 173  GLY D N   1 
ATOM   10210 C  CA  . GLY D  3 175 ? -38.582 -17.869 -21.154  1.00 217.16 ? 173  GLY D CA  1 
ATOM   10211 C  C   . GLY D  3 175 ? -38.350 -18.989 -20.160  1.00 216.21 ? 173  GLY D C   1 
ATOM   10212 O  O   . GLY D  3 175 ? -39.161 -19.912 -20.057  1.00 224.45 ? 173  GLY D O   1 
ATOM   10213 N  N   . VAL D  3 176 ? -37.254 -18.915 -19.404  1.00 209.41 ? 174  VAL D N   1 
ATOM   10214 C  CA  . VAL D  3 176 ? -36.961 -19.932 -18.401  1.00 209.47 ? 174  VAL D CA  1 
ATOM   10215 C  C   . VAL D  3 176 ? -37.814 -19.721 -17.160  1.00 209.62 ? 174  VAL D C   1 
ATOM   10216 O  O   . VAL D  3 176 ? -38.432 -20.659 -16.647  1.00 215.43 ? 174  VAL D O   1 
ATOM   10217 C  CB  . VAL D  3 176 ? -35.461 -19.917 -18.054  1.00 210.40 ? 174  VAL D CB  1 
ATOM   10218 C  CG1 . VAL D  3 176 ? -35.177 -20.859 -16.898  1.00 212.60 ? 174  VAL D CG1 1 
ATOM   10219 C  CG2 . VAL D  3 176 ? -34.625 -20.288 -19.267  1.00 224.56 ? 174  VAL D CG2 1 
ATOM   10220 N  N   . VAL D  3 177 ? -37.857 -18.481 -16.666  1.00 194.80 ? 175  VAL D N   1 
ATOM   10221 C  CA  . VAL D  3 177 ? -38.568 -18.178 -15.426  1.00 184.94 ? 175  VAL D CA  1 
ATOM   10222 C  C   . VAL D  3 177 ? -40.064 -18.403 -15.590  1.00 185.26 ? 175  VAL D C   1 
ATOM   10223 O  O   . VAL D  3 177 ? -40.745 -18.846 -14.659  1.00 185.35 ? 175  VAL D O   1 
ATOM   10224 C  CB  . VAL D  3 177 ? -38.260 -16.738 -14.983  1.00 180.68 ? 175  VAL D CB  1 
ATOM   10225 C  CG1 . VAL D  3 177 ? -38.959 -16.434 -13.675  1.00 180.42 ? 175  VAL D CG1 1 
ATOM   10226 C  CG2 . VAL D  3 177 ? -36.761 -16.539 -14.862  1.00 180.48 ? 175  VAL D CG2 1 
ATOM   10227 N  N   . ARG D  3 178 ? -40.603 -18.073 -16.763  1.00 192.42 ? 176  ARG D N   1 
ATOM   10228 C  CA  . ARG D  3 178 ? -42.019 -18.315 -17.004  1.00 193.76 ? 176  ARG D CA  1 
ATOM   10229 C  C   . ARG D  3 178 ? -42.346 -19.799 -16.881  1.00 201.43 ? 176  ARG D C   1 
ATOM   10230 O  O   . ARG D  3 178 ? -43.369 -20.171 -16.293  1.00 201.29 ? 176  ARG D O   1 
ATOM   10231 C  CB  . ARG D  3 178 ? -42.409 -17.784 -18.381  1.00 196.55 ? 176  ARG D CB  1 
ATOM   10232 C  CG  . ARG D  3 178 ? -43.819 -18.139 -18.818  1.00 203.70 ? 176  ARG D CG  1 
ATOM   10233 C  CD  . ARG D  3 178 ? -44.192 -17.421 -20.104  1.00 210.54 ? 176  ARG D CD  1 
ATOM   10234 N  NE  . ARG D  3 178 ? -44.384 -15.988 -19.901  1.00 200.97 ? 176  ARG D NE  1 
ATOM   10235 C  CZ  . ARG D  3 178 ? -43.472 -15.064 -20.185  1.00 194.84 ? 176  ARG D CZ  1 
ATOM   10236 N  NH1 . ARG D  3 178 ? -42.297 -15.422 -20.687  1.00 194.88 ? 176  ARG D NH1 1 
ATOM   10237 N  NH2 . ARG D  3 178 ? -43.735 -13.783 -19.970  1.00 190.54 ? 176  ARG D NH2 1 
ATOM   10238 N  N   . GLN D  3 179 ? -41.472 -20.664 -17.407  1.00 219.41 ? 177  GLN D N   1 
ATOM   10239 C  CA  . GLN D  3 179 ? -41.700 -22.101 -17.299  1.00 224.90 ? 177  GLN D CA  1 
ATOM   10240 C  C   . GLN D  3 179 ? -41.552 -22.578 -15.865  1.00 215.70 ? 177  GLN D C   1 
ATOM   10241 O  O   . GLN D  3 179 ? -42.187 -23.561 -15.467  1.00 215.91 ? 177  GLN D O   1 
ATOM   10242 C  CB  . GLN D  3 179 ? -40.731 -22.868 -18.200  1.00 232.05 ? 177  GLN D CB  1 
ATOM   10243 C  CG  . GLN D  3 179 ? -40.886 -22.585 -19.682  1.00 242.02 ? 177  GLN D CG  1 
ATOM   10244 C  CD  . GLN D  3 179 ? -39.864 -23.324 -20.522  1.00 237.75 ? 177  GLN D CD  1 
ATOM   10245 O  OE1 . GLN D  3 179 ? -39.082 -24.125 -20.008  1.00 232.03 ? 177  GLN D OE1 1 
ATOM   10246 N  NE2 . GLN D  3 179 ? -39.864 -23.057 -21.823  1.00 233.47 ? 177  GLN D NE2 1 
ATOM   10247 N  N   . TRP D  3 180 ? -40.725 -21.896 -15.081  1.00 217.90 ? 178  TRP D N   1 
ATOM   10248 C  CA  . TRP D  3 180 ? -40.537 -22.272 -13.691  1.00 224.21 ? 178  TRP D CA  1 
ATOM   10249 C  C   . TRP D  3 180 ? -41.716 -21.872 -12.823  1.00 215.23 ? 178  TRP D C   1 
ATOM   10250 O  O   . TRP D  3 180 ? -41.944 -22.499 -11.783  1.00 217.88 ? 178  TRP D O   1 
ATOM   10251 C  CB  . TRP D  3 180 ? -39.250 -21.642 -13.154  1.00 229.70 ? 178  TRP D CB  1 
ATOM   10252 C  CG  . TRP D  3 180 ? -38.005 -22.318 -13.641  1.00 233.90 ? 178  TRP D CG  1 
ATOM   10253 C  CD1 . TRP D  3 180 ? -37.928 -23.391 -14.481  1.00 242.12 ? 178  TRP D CD1 1 
ATOM   10254 C  CD2 . TRP D  3 180 ? -36.656 -21.950 -13.333  1.00 226.09 ? 178  TRP D CD2 1 
ATOM   10255 N  NE1 . TRP D  3 180 ? -36.614 -23.723 -14.705  1.00 242.00 ? 178  TRP D NE1 1 
ATOM   10256 C  CE2 . TRP D  3 180 ? -35.813 -22.851 -14.013  1.00 235.54 ? 178  TRP D CE2 1 
ATOM   10257 C  CE3 . TRP D  3 180 ? -36.080 -20.949 -12.545  1.00 211.48 ? 178  TRP D CE3 1 
ATOM   10258 C  CZ2 . TRP D  3 180 ? -34.425 -22.781 -13.927  1.00 234.58 ? 178  TRP D CZ2 1 
ATOM   10259 C  CZ3 . TRP D  3 180 ? -34.704 -20.881 -12.462  1.00 210.59 ? 178  TRP D CZ3 1 
ATOM   10260 C  CH2 . TRP D  3 180 ? -33.891 -21.791 -13.148  1.00 225.50 ? 178  TRP D CH2 1 
ATOM   10261 N  N   . LEU D  3 181 ? -42.481 -20.859 -13.234  1.00 207.41 ? 179  LEU D N   1 
ATOM   10262 C  CA  . LEU D  3 181 ? -43.640 -20.436 -12.461  1.00 210.90 ? 179  LEU D CA  1 
ATOM   10263 C  C   . LEU D  3 181 ? -44.864 -21.292 -12.738  1.00 218.10 ? 179  LEU D C   1 
ATOM   10264 O  O   . LEU D  3 181 ? -45.776 -21.340 -11.903  1.00 214.55 ? 179  LEU D O   1 
ATOM   10265 C  CB  . LEU D  3 181 ? -43.964 -18.969 -12.756  1.00 203.48 ? 179  LEU D CB  1 
ATOM   10266 C  CG  . LEU D  3 181 ? -43.385 -17.904 -11.828  1.00 198.54 ? 179  LEU D CG  1 
ATOM   10267 C  CD1 . LEU D  3 181 ? -41.877 -18.031 -11.721  1.00 196.62 ? 179  LEU D CD1 1 
ATOM   10268 C  CD2 . LEU D  3 181 ? -43.771 -16.529 -12.339  1.00 199.96 ? 179  LEU D CD2 1 
ATOM   10269 N  N   . SER D  3 182 ? -44.887 -21.991 -13.875  1.00 234.60 ? 180  SER D N   1 
ATOM   10270 C  CA  . SER D  3 182 ? -46.015 -22.853 -14.201  1.00 250.90 ? 180  SER D CA  1 
ATOM   10271 C  C   . SER D  3 182 ? -45.910 -24.191 -13.492  1.00 259.42 ? 180  SER D C   1 
ATOM   10272 O  O   . SER D  3 182 ? -46.934 -24.783 -13.139  1.00 268.20 ? 180  SER D O   1 
ATOM   10273 C  CB  . SER D  3 182 ? -46.100 -23.077 -15.709  1.00 261.11 ? 180  SER D CB  1 
ATOM   10274 O  OG  . SER D  3 182 ? -47.063 -24.067 -16.032  1.00 273.44 ? 180  SER D OG  1 
ATOM   10275 N  N   . ARG D  3 183 ? -44.694 -24.677 -13.268  1.00 258.57 ? 181  ARG D N   1 
ATOM   10276 C  CA  . ARG D  3 183 ? -44.492 -25.897 -12.505  1.00 259.77 ? 181  ARG D CA  1 
ATOM   10277 C  C   . ARG D  3 183 ? -44.344 -25.569 -11.029  1.00 272.25 ? 181  ARG D C   1 
ATOM   10278 O  O   . ARG D  3 183 ? -43.846 -24.503 -10.666  1.00 260.72 ? 181  ARG D O   1 
ATOM   10279 C  CB  . ARG D  3 183 ? -43.259 -26.662 -12.993  1.00 238.33 ? 181  ARG D CB  1 
ATOM   10280 C  CG  . ARG D  3 183 ? -43.287 -27.021 -14.466  1.00 240.10 ? 181  ARG D CG  1 
ATOM   10281 C  CD  . ARG D  3 183 ? -42.061 -27.810 -14.840  1.00 251.22 ? 181  ARG D CD  1 
ATOM   10282 N  NE  . ARG D  3 183 ? -41.894 -27.883 -16.284  1.00 258.16 ? 181  ARG D NE  1 
ATOM   10283 C  CZ  . ARG D  3 183 ? -41.108 -27.067 -16.980  1.00 252.67 ? 181  ARG D CZ  1 
ATOM   10284 N  NH1 . ARG D  3 183 ? -40.413 -26.119 -16.362  1.00 240.96 ? 181  ARG D NH1 1 
ATOM   10285 N  NH2 . ARG D  3 183 ? -41.013 -27.200 -18.294  1.00 257.62 ? 181  ARG D NH2 1 
ATOM   10286 N  N   . GLY D  3 184 ? -44.788 -26.495 -10.183  1.00 295.99 ? 182  GLY D N   1 
ATOM   10287 C  CA  . GLY D  3 184 ? -44.618 -26.371 -8.745   1.00 299.61 ? 182  GLY D CA  1 
ATOM   10288 C  C   . GLY D  3 184 ? -43.281 -26.908 -8.269   1.00 296.90 ? 182  GLY D C   1 
ATOM   10289 O  O   . GLY D  3 184 ? -43.134 -27.301 -7.107   1.00 307.09 ? 182  GLY D O   1 
ATOM   10290 N  N   . GLY D  3 185 ? -42.289 -26.878 -9.160   1.00 270.42 ? 183  GLY D N   1 
ATOM   10291 C  CA  . GLY D  3 185 ? -40.951 -27.349 -8.854   1.00 251.62 ? 183  GLY D CA  1 
ATOM   10292 C  C   . GLY D  3 185 ? -40.335 -26.578 -7.708   1.00 246.12 ? 183  GLY D C   1 
ATOM   10293 O  O   . GLY D  3 185 ? -40.025 -25.386 -7.834   1.00 251.07 ? 183  GLY D O   1 
ATOM   10294 N  N   . GLU D  3 186 ? -40.138 -27.257 -6.577   1.00 238.43 ? 184  GLU D N   1 
ATOM   10295 C  CA  . GLU D  3 186 ? -39.742 -26.608 -5.331   1.00 235.98 ? 184  GLU D CA  1 
ATOM   10296 C  C   . GLU D  3 186 ? -38.293 -26.133 -5.337   1.00 221.47 ? 184  GLU D C   1 
ATOM   10297 O  O   . GLU D  3 186 ? -37.899 -25.390 -4.431   1.00 218.71 ? 184  GLU D O   1 
ATOM   10298 C  CB  . GLU D  3 186 ? -40.017 -27.588 -4.175   1.00 239.87 ? 184  GLU D CB  1 
ATOM   10299 C  CG  . GLU D  3 186 ? -39.759 -27.096 -2.747   1.00 244.98 ? 184  GLU D CG  1 
ATOM   10300 C  CD  . GLU D  3 186 ? -38.350 -27.392 -2.249   1.00 231.44 ? 184  GLU D CD  1 
ATOM   10301 O  OE1 . GLU D  3 186 ? -37.714 -28.331 -2.776   1.00 224.67 ? 184  GLU D OE1 1 
ATOM   10302 O  OE2 . GLU D  3 186 ? -37.887 -26.692 -1.319   1.00 231.47 ? 184  GLU D OE2 1 
ATOM   10303 N  N   . ILE D  3 187 ? -37.512 -26.470 -6.358   1.00 217.96 ? 185  ILE D N   1 
ATOM   10304 C  CA  . ILE D  3 187 ? -36.109 -26.066 -6.397   1.00 212.18 ? 185  ILE D CA  1 
ATOM   10305 C  C   . ILE D  3 187 ? -35.667 -25.905 -7.845   1.00 209.81 ? 185  ILE D C   1 
ATOM   10306 O  O   . ILE D  3 187 ? -35.940 -26.765 -8.689   1.00 217.37 ? 185  ILE D O   1 
ATOM   10307 C  CB  . ILE D  3 187 ? -35.203 -27.066 -5.651   1.00 222.11 ? 185  ILE D CB  1 
ATOM   10308 C  CG1 . ILE D  3 187 ? -33.734 -26.647 -5.770   1.00 215.27 ? 185  ILE D CG1 1 
ATOM   10309 C  CG2 . ILE D  3 187 ? -35.431 -28.490 -6.156   1.00 225.52 ? 185  ILE D CG2 1 
ATOM   10310 C  CD1 . ILE D  3 187 ? -33.424 -25.295 -5.163   1.00 203.81 ? 185  ILE D CD1 1 
ATOM   10311 N  N   . GLU D  3 188 ? -35.007 -24.787 -8.139   1.00 197.50 ? 186  GLU D N   1 
ATOM   10312 C  CA  . GLU D  3 188 ? -34.455 -24.521 -9.461   1.00 200.42 ? 186  GLU D CA  1 
ATOM   10313 C  C   . GLU D  3 188 ? -33.039 -23.976 -9.306   1.00 201.19 ? 186  GLU D C   1 
ATOM   10314 O  O   . GLU D  3 188 ? -32.517 -23.849 -8.194   1.00 199.11 ? 186  GLU D O   1 
ATOM   10315 C  CB  . GLU D  3 188 ? -35.341 -23.546 -10.247  1.00 213.27 ? 186  GLU D CB  1 
ATOM   10316 C  CG  . GLU D  3 188 ? -36.749 -24.064 -10.555  1.00 229.80 ? 186  GLU D CG  1 
ATOM   10317 C  CD  . GLU D  3 188 ? -36.779 -25.124 -11.650  1.00 217.34 ? 186  GLU D CD  1 
ATOM   10318 O  OE1 . GLU D  3 188 ? -35.730 -25.362 -12.285  1.00 209.49 ? 186  GLU D OE1 1 
ATOM   10319 O  OE2 . GLU D  3 188 ? -37.856 -25.720 -11.876  1.00 211.06 ? 186  GLU D OE2 1 
ATOM   10320 N  N   . GLY D  3 189 ? -32.417 -23.649 -10.432  1.00 205.47 ? 187  GLY D N   1 
ATOM   10321 C  CA  . GLY D  3 189 ? -31.069 -23.117 -10.416  1.00 206.74 ? 187  GLY D CA  1 
ATOM   10322 C  C   . GLY D  3 189 ? -30.496 -23.042 -11.815  1.00 211.02 ? 187  GLY D C   1 
ATOM   10323 O  O   . GLY D  3 189 ? -31.107 -23.491 -12.792  1.00 213.75 ? 187  GLY D O   1 
ATOM   10324 N  N   . PHE D  3 190 ? -29.295 -22.469 -11.893  1.00 207.88 ? 188  PHE D N   1 
ATOM   10325 C  CA  . PHE D  3 190 ? -28.587 -22.286 -13.154  1.00 212.62 ? 188  PHE D CA  1 
ATOM   10326 C  C   . PHE D  3 190 ? -27.191 -22.899 -13.066  1.00 237.20 ? 188  PHE D C   1 
ATOM   10327 O  O   . PHE D  3 190 ? -26.755 -23.373 -12.012  1.00 250.99 ? 188  PHE D O   1 
ATOM   10328 C  CB  . PHE D  3 190 ? -28.497 -20.801 -13.527  1.00 210.45 ? 188  PHE D CB  1 
ATOM   10329 C  CG  . PHE D  3 190 ? -29.826 -20.166 -13.820  1.00 223.04 ? 188  PHE D CG  1 
ATOM   10330 C  CD1 . PHE D  3 190 ? -30.351 -20.192 -15.103  1.00 236.77 ? 188  PHE D CD1 1 
ATOM   10331 C  CD2 . PHE D  3 190 ? -30.547 -19.535 -12.819  1.00 220.06 ? 188  PHE D CD2 1 
ATOM   10332 C  CE1 . PHE D  3 190 ? -31.573 -19.603 -15.383  1.00 232.24 ? 188  PHE D CE1 1 
ATOM   10333 C  CE2 . PHE D  3 190 ? -31.771 -18.944 -13.093  1.00 218.36 ? 188  PHE D CE2 1 
ATOM   10334 C  CZ  . PHE D  3 190 ? -32.283 -18.978 -14.376  1.00 219.70 ? 188  PHE D CZ  1 
ATOM   10335 N  N   . ARG D  3 191 ? -26.487 -22.885 -14.199  1.00 248.05 ? 189  ARG D N   1 
ATOM   10336 C  CA  . ARG D  3 191 ? -25.120 -23.379 -14.297  1.00 248.44 ? 189  ARG D CA  1 
ATOM   10337 C  C   . ARG D  3 191 ? -24.328 -22.485 -15.239  1.00 242.57 ? 189  ARG D C   1 
ATOM   10338 O  O   . ARG D  3 191 ? -24.819 -22.110 -16.307  1.00 243.00 ? 189  ARG D O   1 
ATOM   10339 C  CB  . ARG D  3 191 ? -25.077 -24.825 -14.801  1.00 253.60 ? 189  ARG D CB  1 
ATOM   10340 C  CG  . ARG D  3 191 ? -23.677 -25.311 -15.118  1.00 250.87 ? 189  ARG D CG  1 
ATOM   10341 C  CD  . ARG D  3 191 ? -23.697 -26.496 -16.057  1.00 260.69 ? 189  ARG D CD  1 
ATOM   10342 N  NE  . ARG D  3 191 ? -22.354 -26.830 -16.521  1.00 274.65 ? 189  ARG D NE  1 
ATOM   10343 C  CZ  . ARG D  3 191 ? -22.089 -27.764 -17.428  1.00 289.43 ? 189  ARG D CZ  1 
ATOM   10344 N  NH1 . ARG D  3 191 ? -23.078 -28.458 -17.973  1.00 291.83 ? 189  ARG D NH1 1 
ATOM   10345 N  NH2 . ARG D  3 191 ? -20.836 -28.001 -17.794  1.00 295.48 ? 189  ARG D NH2 1 
ATOM   10346 N  N   . LEU D  3 192 ? -23.099 -22.153 -14.847  1.00 241.16 ? 190  LEU D N   1 
ATOM   10347 C  CA  . LEU D  3 192 ? -22.225 -21.286 -15.635  1.00 243.73 ? 190  LEU D CA  1 
ATOM   10348 C  C   . LEU D  3 192 ? -20.895 -21.996 -15.896  1.00 257.01 ? 190  LEU D C   1 
ATOM   10349 O  O   . LEU D  3 192 ? -20.013 -22.019 -15.033  1.00 269.52 ? 190  LEU D O   1 
ATOM   10350 C  CB  . LEU D  3 192 ? -22.015 -19.953 -14.925  1.00 231.60 ? 190  LEU D CB  1 
ATOM   10351 C  CG  . LEU D  3 192 ? -21.403 -18.820 -15.746  1.00 227.13 ? 190  LEU D CG  1 
ATOM   10352 C  CD1 . LEU D  3 192 ? -22.030 -17.505 -15.333  1.00 222.98 ? 190  LEU D CD1 1 
ATOM   10353 C  CD2 . LEU D  3 192 ? -19.894 -18.774 -15.565  1.00 240.23 ? 190  LEU D CD2 1 
ATOM   10354 N  N   . SER D  3 193 ? -20.753 -22.573 -17.085  1.00 255.14 ? 191  SER D N   1 
ATOM   10355 C  CA  . SER D  3 193 ? -19.497 -23.123 -17.564  1.00 259.26 ? 191  SER D CA  1 
ATOM   10356 C  C   . SER D  3 193 ? -18.891 -22.160 -18.588  1.00 257.23 ? 191  SER D C   1 
ATOM   10357 O  O   . SER D  3 193 ? -19.304 -20.998 -18.680  1.00 258.83 ? 191  SER D O   1 
ATOM   10358 C  CB  . SER D  3 193 ? -19.730 -24.527 -18.130  1.00 269.17 ? 191  SER D CB  1 
ATOM   10359 O  OG  . SER D  3 193 ? -20.654 -24.493 -19.203  1.00 277.84 ? 191  SER D OG  1 
ATOM   10360 N  N   . ALA D  3 194 ? -17.917 -22.628 -19.363  1.00 251.28 ? 192  ALA D N   1 
ATOM   10361 C  CA  . ALA D  3 194 ? -17.252 -21.780 -20.344  1.00 245.90 ? 192  ALA D CA  1 
ATOM   10362 C  C   . ALA D  3 194 ? -17.451 -22.320 -21.765  1.00 241.94 ? 192  ALA D C   1 
ATOM   10363 O  O   . ALA D  3 194 ? -18.235 -23.242 -22.008  1.00 241.11 ? 192  ALA D O   1 
ATOM   10364 C  CB  . ALA D  3 194 ? -15.766 -21.648 -20.009  1.00 252.00 ? 192  ALA D CB  1 
ATOM   10365 N  N   . HIS D  3 195 ? -16.714 -21.729 -22.705  1.00 242.49 ? 193  HIS D N   1 
ATOM   10366 C  CA  . HIS D  3 195 ? -16.789 -22.116 -24.108  1.00 244.15 ? 193  HIS D CA  1 
ATOM   10367 C  C   . HIS D  3 195 ? -16.132 -23.471 -24.338  1.00 246.05 ? 193  HIS D C   1 
ATOM   10368 O  O   . HIS D  3 195 ? -15.190 -23.861 -23.641  1.00 245.80 ? 193  HIS D O   1 
ATOM   10369 C  CB  . HIS D  3 195 ? -16.118 -21.062 -24.986  1.00 247.58 ? 193  HIS D CB  1 
ATOM   10370 C  CG  . HIS D  3 195 ? -16.197 -21.354 -26.452  1.00 246.97 ? 193  HIS D CG  1 
ATOM   10371 N  ND1 . HIS D  3 195 ? -17.391 -21.578 -27.104  1.00 242.60 ? 193  HIS D ND1 1 
ATOM   10372 C  CD2 . HIS D  3 195 ? -15.229 -21.461 -27.394  1.00 252.44 ? 193  HIS D CD2 1 
ATOM   10373 C  CE1 . HIS D  3 195 ? -17.156 -21.810 -28.384  1.00 250.54 ? 193  HIS D CE1 1 
ATOM   10374 N  NE2 . HIS D  3 195 ? -15.852 -21.744 -28.586  1.00 255.39 ? 193  HIS D NE2 1 
ATOM   10375 N  N   . CYS D  3 196 ? -16.643 -24.199 -25.326  1.00 242.85 ? 194  CYS D N   1 
ATOM   10376 C  CA  . CYS D  3 196 ? -16.099 -25.502 -25.687  1.00 247.46 ? 194  CYS D CA  1 
ATOM   10377 C  C   . CYS D  3 196 ? -15.628 -25.437 -27.134  1.00 251.39 ? 194  CYS D C   1 
ATOM   10378 O  O   . CYS D  3 196 ? -16.449 -25.368 -28.055  1.00 252.62 ? 194  CYS D O   1 
ATOM   10379 C  CB  . CYS D  3 196 ? -17.146 -26.598 -25.502  1.00 251.10 ? 194  CYS D CB  1 
ATOM   10380 S  SG  . CYS D  3 196 ? -18.211 -26.433 -24.046  1.00 256.17 ? 194  CYS D SG  1 
ATOM   10381 N  N   . SER D  3 197 ? -14.311 -25.448 -27.333  1.00 259.78 ? 195  SER D N   1 
ATOM   10382 C  CA  . SER D  3 197 ? -13.721 -25.489 -28.666  1.00 260.63 ? 195  SER D CA  1 
ATOM   10383 C  C   . SER D  3 197 ? -13.480 -26.950 -29.028  1.00 260.67 ? 195  SER D C   1 
ATOM   10384 O  O   . SER D  3 197 ? -12.537 -27.573 -28.527  1.00 259.88 ? 195  SER D O   1 
ATOM   10385 C  CB  . SER D  3 197 ? -12.424 -24.685 -28.698  1.00 260.81 ? 195  SER D CB  1 
ATOM   10386 O  OG  . SER D  3 197 ? -11.870 -24.642 -29.999  1.00 263.53 ? 195  SER D OG  1 
ATOM   10387 N  N   . CYS D  3 198 ? -14.309 -27.488 -29.921  1.00 259.44 ? 196  CYS D N   1 
ATOM   10388 C  CA  . CYS D  3 198 ? -14.293 -28.910 -30.218  1.00 260.52 ? 196  CYS D CA  1 
ATOM   10389 C  C   . CYS D  3 198 ? -14.261 -29.136 -31.723  1.00 268.57 ? 196  CYS D C   1 
ATOM   10390 O  O   . CYS D  3 198 ? -14.552 -28.236 -32.516  1.00 264.83 ? 196  CYS D O   1 
ATOM   10391 C  CB  . CYS D  3 198 ? -15.508 -29.628 -29.597  1.00 254.11 ? 196  CYS D CB  1 
ATOM   10392 S  SG  . CYS D  3 198 ? -17.099 -29.474 -30.471  1.00 251.43 ? 196  CYS D SG  1 
ATOM   10393 N  N   . ASP D  3 199 ? -13.890 -30.356 -32.099  1.00 285.77 ? 197  ASP D N   1 
ATOM   10394 C  CA  . ASP D  3 199 ? -13.998 -30.832 -33.476  1.00 293.02 ? 197  ASP D CA  1 
ATOM   10395 C  C   . ASP D  3 199 ? -13.764 -32.336 -33.510  1.00 302.80 ? 197  ASP D C   1 
ATOM   10396 O  O   . ASP D  3 199 ? -14.300 -33.070 -32.681  1.00 299.74 ? 197  ASP D O   1 
ATOM   10397 C  CB  . ASP D  3 199 ? -13.006 -30.127 -34.401  1.00 298.27 ? 197  ASP D CB  1 
ATOM   10398 C  CG  . ASP D  3 199 ? -13.340 -30.336 -35.867  1.00 306.77 ? 197  ASP D CG  1 
ATOM   10399 O  OD1 . ASP D  3 199 ? -14.157 -29.556 -36.401  1.00 305.57 ? 197  ASP D OD1 1 
ATOM   10400 O  OD2 . ASP D  3 199 ? -12.798 -31.282 -36.479  1.00 308.60 ? 197  ASP D OD2 1 
ATOM   10401 N  N   . THR D  3 204 ? -11.349 -24.962 -20.060  1.00 217.90 ? 202  THR D N   1 
ATOM   10402 C  CA  . THR D  3 204 ? -11.798 -24.687 -18.703  1.00 211.64 ? 202  THR D CA  1 
ATOM   10403 C  C   . THR D  3 204 ? -12.469 -23.322 -18.615  1.00 211.83 ? 202  THR D C   1 
ATOM   10404 O  O   . THR D  3 204 ? -12.829 -22.734 -19.634  1.00 206.98 ? 202  THR D O   1 
ATOM   10405 C  CB  . THR D  3 204 ? -10.633 -24.752 -17.705  1.00 209.44 ? 202  THR D CB  1 
ATOM   10406 O  OG1 . THR D  3 204 ? -9.458  -24.190 -18.304  1.00 210.65 ? 202  THR D OG1 1 
ATOM   10407 C  CG2 . THR D  3 204 ? -10.366 -26.195 -17.308  1.00 212.94 ? 202  THR D CG2 1 
ATOM   10408 N  N   . LEU D  3 205 ? -12.609 -22.807 -17.396  1.00 234.00 ? 203  LEU D N   1 
ATOM   10409 C  CA  . LEU D  3 205 ? -13.242 -21.517 -17.153  1.00 232.39 ? 203  LEU D CA  1 
ATOM   10410 C  C   . LEU D  3 205 ? -12.304 -20.629 -16.351  1.00 236.90 ? 203  LEU D C   1 
ATOM   10411 O  O   . LEU D  3 205 ? -11.703 -21.080 -15.371  1.00 239.92 ? 203  LEU D O   1 
ATOM   10412 C  CB  . LEU D  3 205 ? -14.565 -21.694 -16.402  1.00 223.11 ? 203  LEU D CB  1 
ATOM   10413 C  CG  . LEU D  3 205 ? -15.230 -20.413 -15.898  1.00 210.04 ? 203  LEU D CG  1 
ATOM   10414 C  CD1 . LEU D  3 205 ? -15.616 -19.533 -17.066  1.00 210.06 ? 203  LEU D CD1 1 
ATOM   10415 C  CD2 . LEU D  3 205 ? -16.434 -20.723 -15.022  1.00 206.35 ? 203  LEU D CD2 1 
ATOM   10416 N  N   . GLN D  3 206 ? -12.183 -19.366 -16.763  1.00 235.85 ? 204  GLN D N   1 
ATOM   10417 C  CA  . GLN D  3 206 ? -11.307 -18.414 -16.090  1.00 233.41 ? 204  GLN D CA  1 
ATOM   10418 C  C   . GLN D  3 206 ? -12.045 -17.170 -15.614  1.00 223.11 ? 204  GLN D C   1 
ATOM   10419 O  O   . GLN D  3 206 ? -11.394 -16.178 -15.273  1.00 217.88 ? 204  GLN D O   1 
ATOM   10420 C  CB  . GLN D  3 206 ? -10.136 -17.995 -16.992  1.00 238.54 ? 204  GLN D CB  1 
ATOM   10421 C  CG  . GLN D  3 206 ? -9.374  -19.131 -17.658  1.00 252.27 ? 204  GLN D CG  1 
ATOM   10422 C  CD  . GLN D  3 206 ? -8.387  -18.632 -18.706  1.00 256.70 ? 204  GLN D CD  1 
ATOM   10423 O  OE1 . GLN D  3 206 ? -8.439  -17.475 -19.126  1.00 247.76 ? 204  GLN D OE1 1 
ATOM   10424 N  NE2 . GLN D  3 206 ? -7.480  -19.506 -19.129  1.00 269.89 ? 204  GLN D NE2 1 
ATOM   10425 N  N   . VAL D  3 207 ? -13.375 -17.185 -15.588  1.00 219.55 ? 205  VAL D N   1 
ATOM   10426 C  CA  . VAL D  3 207 ? -14.141 -15.992 -15.237  1.00 212.04 ? 205  VAL D CA  1 
ATOM   10427 C  C   . VAL D  3 207 ? -14.170 -15.824 -13.724  1.00 205.21 ? 205  VAL D C   1 
ATOM   10428 O  O   . VAL D  3 207 ? -14.405 -16.784 -12.981  1.00 204.12 ? 205  VAL D O   1 
ATOM   10429 C  CB  . VAL D  3 207 ? -15.563 -16.067 -15.809  1.00 206.64 ? 205  VAL D CB  1 
ATOM   10430 C  CG1 . VAL D  3 207 ? -16.389 -14.901 -15.308  1.00 193.69 ? 205  VAL D CG1 1 
ATOM   10431 C  CG2 . VAL D  3 207 ? -15.514 -16.029 -17.309  1.00 218.75 ? 205  VAL D CG2 1 
ATOM   10432 N  N   . ASP D  3 208 ? -13.936 -14.597 -13.265  1.00 200.89 ? 206  ASP D N   1 
ATOM   10433 C  CA  . ASP D  3 208 ? -14.019 -14.259 -11.847  1.00 196.31 ? 206  ASP D CA  1 
ATOM   10434 C  C   . ASP D  3 208 ? -15.336 -13.535 -11.603  1.00 190.06 ? 206  ASP D C   1 
ATOM   10435 O  O   . ASP D  3 208 ? -15.456 -12.336 -11.864  1.00 186.81 ? 206  ASP D O   1 
ATOM   10436 C  CB  . ASP D  3 208 ? -12.838 -13.396 -11.430  1.00 195.98 ? 206  ASP D CB  1 
ATOM   10437 C  CG  . ASP D  3 208 ? -11.517 -13.961 -11.890  1.00 224.26 ? 206  ASP D CG  1 
ATOM   10438 O  OD1 . ASP D  3 208 ? -11.504 -14.703 -12.893  1.00 239.49 ? 206  ASP D OD1 1 
ATOM   10439 O  OD2 . ASP D  3 208 ? -10.490 -13.659 -11.252  1.00 232.82 ? 206  ASP D OD2 1 
ATOM   10440 N  N   . ILE D  3 209 ? -16.324 -14.268 -11.103  1.00 201.64 ? 207  ILE D N   1 
ATOM   10441 C  CA  . ILE D  3 209 ? -17.598 -13.697 -10.687  1.00 202.81 ? 207  ILE D CA  1 
ATOM   10442 C  C   . ILE D  3 209 ? -17.643 -13.696 -9.168   1.00 214.77 ? 207  ILE D C   1 
ATOM   10443 O  O   . ILE D  3 209 ? -17.043 -14.555 -8.511   1.00 226.94 ? 207  ILE D O   1 
ATOM   10444 C  CB  . ILE D  3 209 ? -18.814 -14.451 -11.258  1.00 197.66 ? 207  ILE D CB  1 
ATOM   10445 C  CG1 . ILE D  3 209 ? -18.841 -15.894 -10.745  1.00 209.00 ? 207  ILE D CG1 1 
ATOM   10446 C  CG2 . ILE D  3 209 ? -18.790 -14.408 -12.770  1.00 204.07 ? 207  ILE D CG2 1 
ATOM   10447 C  CD1 . ILE D  3 209 ? -20.221 -16.492 -10.696  1.00 207.09 ? 207  ILE D CD1 1 
ATOM   10448 N  N   . ASN D  3 210 ? -18.318 -12.694 -8.612   1.00 211.90 ? 208  ASN D N   1 
ATOM   10449 C  CA  . ASN D  3 210 ? -18.533 -12.629 -7.171   1.00 213.69 ? 208  ASN D CA  1 
ATOM   10450 C  C   . ASN D  3 210 ? -19.114 -13.936 -6.653   1.00 231.01 ? 208  ASN D C   1 
ATOM   10451 O  O   . ASN D  3 210 ? -20.224 -14.325 -7.027   1.00 229.07 ? 208  ASN D O   1 
ATOM   10452 C  CB  . ASN D  3 210 ? -19.467 -11.467 -6.835   1.00 191.94 ? 208  ASN D CB  1 
ATOM   10453 C  CG  . ASN D  3 210 ? -19.241 -10.927 -5.434   1.00 190.39 ? 208  ASN D CG  1 
ATOM   10454 O  OD1 . ASN D  3 210 ? -18.140 -11.013 -4.892   1.00 200.01 ? 208  ASN D OD1 1 
ATOM   10455 N  ND2 . ASN D  3 210 ? -20.290 -10.377 -4.836   1.00 185.84 ? 208  ASN D ND2 1 
ATOM   10456 N  N   . GLY D  3 211 ? -18.359 -14.616 -5.794   1.00 242.72 ? 209  GLY D N   1 
ATOM   10457 C  CA  . GLY D  3 211 ? -18.827 -15.860 -5.219   1.00 229.83 ? 209  GLY D CA  1 
ATOM   10458 C  C   . GLY D  3 211 ? -18.743 -15.861 -3.711   1.00 226.72 ? 209  GLY D C   1 
ATOM   10459 O  O   . GLY D  3 211 ? -18.736 -14.801 -3.080   1.00 226.07 ? 209  GLY D O   1 
ATOM   10460 N  N   . PHE D  3 212 ? -18.656 -17.051 -3.121   1.00 241.53 ? 210  PHE D N   1 
ATOM   10461 C  CA  . PHE D  3 212 ? -18.577 -17.177 -1.674   1.00 256.95 ? 210  PHE D CA  1 
ATOM   10462 C  C   . PHE D  3 212 ? -17.150 -17.308 -1.178   1.00 260.55 ? 210  PHE D C   1 
ATOM   10463 O  O   . PHE D  3 212 ? -16.887 -17.006 -0.007   1.00 258.48 ? 210  PHE D O   1 
ATOM   10464 C  CB  . PHE D  3 212 ? -19.363 -18.405 -1.181   1.00 260.46 ? 210  PHE D CB  1 
ATOM   10465 C  CG  . PHE D  3 212 ? -20.793 -18.458 -1.649   1.00 267.96 ? 210  PHE D CG  1 
ATOM   10466 C  CD1 . PHE D  3 212 ? -21.096 -18.835 -2.948   1.00 274.08 ? 210  PHE D CD1 1 
ATOM   10467 C  CD2 . PHE D  3 212 ? -21.836 -18.168 -0.779   1.00 259.74 ? 210  PHE D CD2 1 
ATOM   10468 C  CE1 . PHE D  3 212 ? -22.402 -18.893 -3.381   1.00 271.95 ? 210  PHE D CE1 1 
ATOM   10469 C  CE2 . PHE D  3 212 ? -23.147 -18.228 -1.208   1.00 251.37 ? 210  PHE D CE2 1 
ATOM   10470 C  CZ  . PHE D  3 212 ? -23.430 -18.595 -2.509   1.00 261.08 ? 210  PHE D CZ  1 
ATOM   10471 N  N   . THR D  3 213 ? -16.240 -17.784 -2.031   1.00 265.34 ? 211  THR D N   1 
ATOM   10472 C  CA  . THR D  3 213 ? -14.841 -18.036 -1.694   1.00 265.01 ? 211  THR D CA  1 
ATOM   10473 C  C   . THR D  3 213 ? -14.711 -19.061 -0.569   1.00 271.60 ? 211  THR D C   1 
ATOM   10474 O  O   . THR D  3 213 ? -13.592 -19.440 -0.203   1.00 278.09 ? 211  THR D O   1 
ATOM   10475 C  CB  . THR D  3 213 ? -14.120 -16.731 -1.329   1.00 251.19 ? 211  THR D CB  1 
ATOM   10476 O  OG1 . THR D  3 213 ? -14.668 -16.196 -0.120   1.00 244.49 ? 211  THR D OG1 1 
ATOM   10477 C  CG2 . THR D  3 213 ? -14.283 -15.703 -2.446   1.00 236.64 ? 211  THR D CG2 1 
ATOM   10478 N  N   . THR D  3 214 ? -15.845 -19.482 0.006    1.00 266.54 ? 212  THR D N   1 
ATOM   10479 C  CA  . THR D  3 214 ? -15.944 -20.555 0.994    1.00 269.40 ? 212  THR D CA  1 
ATOM   10480 C  C   . THR D  3 214 ? -15.330 -20.204 2.346    1.00 270.10 ? 212  THR D C   1 
ATOM   10481 O  O   . THR D  3 214 ? -15.859 -20.608 3.387    1.00 284.73 ? 212  THR D O   1 
ATOM   10482 C  CB  . THR D  3 214 ? -15.310 -21.844 0.454    1.00 271.68 ? 212  THR D CB  1 
ATOM   10483 O  OG1 . THR D  3 214 ? -15.709 -22.044 -0.908   1.00 278.10 ? 212  THR D OG1 1 
ATOM   10484 C  CG2 . THR D  3 214 ? -15.738 -23.049 1.285    1.00 262.30 ? 212  THR D CG2 1 
ATOM   10485 N  N   . GLY D  3 215 ? -14.221 -19.467 2.360    1.00 252.74 ? 213  GLY D N   1 
ATOM   10486 C  CA  . GLY D  3 215 ? -13.463 -19.334 3.592    1.00 247.42 ? 213  GLY D CA  1 
ATOM   10487 C  C   . GLY D  3 215 ? -13.483 -18.016 4.343    1.00 243.44 ? 213  GLY D C   1 
ATOM   10488 O  O   . GLY D  3 215 ? -12.807 -17.900 5.370    1.00 247.80 ? 213  GLY D O   1 
ATOM   10489 N  N   . ARG D  3 216 ? -14.241 -17.024 3.884    1.00 223.78 ? 214  ARG D N   1 
ATOM   10490 C  CA  . ARG D  3 216 ? -14.282 -15.740 4.578    1.00 214.77 ? 214  ARG D CA  1 
ATOM   10491 C  C   . ARG D  3 216 ? -15.136 -15.860 5.836    1.00 208.11 ? 214  ARG D C   1 
ATOM   10492 O  O   . ARG D  3 216 ? -16.318 -16.212 5.764    1.00 202.61 ? 214  ARG D O   1 
ATOM   10493 C  CB  . ARG D  3 216 ? -14.820 -14.648 3.661    1.00 199.51 ? 214  ARG D CB  1 
ATOM   10494 C  CG  . ARG D  3 216 ? -14.097 -14.569 2.333    1.00 199.33 ? 214  ARG D CG  1 
ATOM   10495 C  CD  . ARG D  3 216 ? -12.604 -14.333 2.473    1.00 221.13 ? 214  ARG D CD  1 
ATOM   10496 N  NE  . ARG D  3 216 ? -11.962 -14.278 1.162    1.00 226.69 ? 214  ARG D NE  1 
ATOM   10497 C  CZ  . ARG D  3 216 ? -10.649 -14.224 0.970    1.00 230.99 ? 214  ARG D CZ  1 
ATOM   10498 N  NH1 . ARG D  3 216 ? -9.823  -14.222 2.010    1.00 225.93 ? 214  ARG D NH1 1 
ATOM   10499 N  NH2 . ARG D  3 216 ? -10.163 -14.178 -0.265   1.00 230.91 ? 214  ARG D NH2 1 
ATOM   10500 N  N   . ARG D  3 217 ? -14.534 -15.565 6.988    1.00 191.91 ? 215  ARG D N   1 
ATOM   10501 C  CA  . ARG D  3 217 ? -15.229 -15.687 8.262    1.00 193.81 ? 215  ARG D CA  1 
ATOM   10502 C  C   . ARG D  3 217 ? -15.254 -14.361 9.010    1.00 193.78 ? 215  ARG D C   1 
ATOM   10503 O  O   . ARG D  3 217 ? -15.072 -13.296 8.411    1.00 193.99 ? 215  ARG D O   1 
ATOM   10504 C  CB  . ARG D  3 217 ? -14.575 -16.758 9.135    1.00 201.67 ? 215  ARG D CB  1 
ATOM   10505 C  CG  . ARG D  3 217 ? -14.579 -18.140 8.526    1.00 202.80 ? 215  ARG D CG  1 
ATOM   10506 C  CD  . ARG D  3 217 ? -14.219 -19.177 9.567    1.00 210.68 ? 215  ARG D CD  1 
ATOM   10507 N  NE  . ARG D  3 217 ? -12.874 -18.973 10.088   1.00 217.47 ? 215  ARG D NE  1 
ATOM   10508 C  CZ  . ARG D  3 217 ? -11.799 -19.597 9.622    1.00 221.88 ? 215  ARG D CZ  1 
ATOM   10509 N  NH1 . ARG D  3 217 ? -11.918 -20.464 8.625    1.00 220.16 ? 215  ARG D NH1 1 
ATOM   10510 N  NH2 . ARG D  3 217 ? -10.607 -19.357 10.150   1.00 228.43 ? 215  ARG D NH2 1 
ATOM   10511 N  N   . GLY D  3 218 ? -15.493 -14.424 10.319   1.00 197.76 ? 216  GLY D N   1 
ATOM   10512 C  CA  . GLY D  3 218 ? -15.466 -13.251 11.170   1.00 199.12 ? 216  GLY D CA  1 
ATOM   10513 C  C   . GLY D  3 218 ? -16.771 -12.491 11.273   1.00 193.46 ? 216  GLY D C   1 
ATOM   10514 O  O   . GLY D  3 218 ? -17.853 -13.065 11.131   1.00 189.90 ? 216  GLY D O   1 
ATOM   10515 N  N   . ASP D  3 219 ? -16.674 -11.189 11.542   1.00 193.14 ? 217  ASP D N   1 
ATOM   10516 C  CA  . ASP D  3 219 ? -17.866 -10.355 11.619   1.00 188.19 ? 217  ASP D CA  1 
ATOM   10517 C  C   . ASP D  3 219 ? -18.330 -9.925  10.235   1.00 181.03 ? 217  ASP D C   1 
ATOM   10518 O  O   . ASP D  3 219 ? -19.537 -9.819  9.981    1.00 176.00 ? 217  ASP D O   1 
ATOM   10519 C  CB  . ASP D  3 219 ? -17.602 -9.138  12.504   1.00 191.48 ? 217  ASP D CB  1 
ATOM   10520 C  CG  . ASP D  3 219 ? -18.775 -8.195  12.542   1.00 186.79 ? 217  ASP D CG  1 
ATOM   10521 O  OD1 . ASP D  3 219 ? -19.915 -8.696  12.547   1.00 183.27 ? 217  ASP D OD1 1 
ATOM   10522 O  OD2 . ASP D  3 219 ? -18.567 -6.966  12.584   1.00 187.09 ? 217  ASP D OD2 1 
ATOM   10523 N  N   . LEU D  3 220 ? -17.384 -9.680  9.335    1.00 183.23 ? 218  LEU D N   1 
ATOM   10524 C  CA  . LEU D  3 220 ? -17.686 -9.209  7.993    1.00 174.98 ? 218  LEU D CA  1 
ATOM   10525 C  C   . LEU D  3 220 ? -18.191 -10.315 7.068    1.00 184.61 ? 218  LEU D C   1 
ATOM   10526 O  O   . LEU D  3 220 ? -18.652 -10.010 5.960    1.00 188.35 ? 218  LEU D O   1 
ATOM   10527 C  CB  . LEU D  3 220 ? -16.430 -8.558  7.404    1.00 177.01 ? 218  LEU D CB  1 
ATOM   10528 C  CG  . LEU D  3 220 ? -16.570 -7.639  6.192    1.00 187.60 ? 218  LEU D CG  1 
ATOM   10529 C  CD1 . LEU D  3 220 ? -17.638 -6.588  6.436    1.00 169.22 ? 218  LEU D CD1 1 
ATOM   10530 C  CD2 . LEU D  3 220 ? -15.232 -6.996  5.848    1.00 196.55 ? 218  LEU D CD2 1 
ATOM   10531 N  N   . ALA D  3 221 ? -18.127 -11.582 7.494    1.00 174.30 ? 219  ALA D N   1 
ATOM   10532 C  CA  . ALA D  3 221 ? -18.535 -12.689 6.631    1.00 171.96 ? 219  ALA D CA  1 
ATOM   10533 C  C   . ALA D  3 221 ? -20.001 -12.586 6.225    1.00 167.32 ? 219  ALA D C   1 
ATOM   10534 O  O   . ALA D  3 221 ? -20.367 -12.948 5.100    1.00 164.68 ? 219  ALA D O   1 
ATOM   10535 C  CB  . ALA D  3 221 ? -18.275 -14.023 7.329    1.00 178.01 ? 219  ALA D CB  1 
ATOM   10536 N  N   . THR D  3 222 ? -20.857 -12.106 7.131    1.00 172.13 ? 220  THR D N   1 
ATOM   10537 C  CA  . THR D  3 222 ? -22.285 -12.015 6.832    1.00 173.13 ? 220  THR D CA  1 
ATOM   10538 C  C   . THR D  3 222 ? -22.549 -11.111 5.637    1.00 158.37 ? 220  THR D C   1 
ATOM   10539 O  O   . THR D  3 222 ? -23.434 -11.392 4.821    1.00 155.49 ? 220  THR D O   1 
ATOM   10540 C  CB  . THR D  3 222 ? -23.044 -11.507 8.055    1.00 180.46 ? 220  THR D CB  1 
ATOM   10541 O  OG1 . THR D  3 222 ? -22.162 -10.714 8.860    1.00 188.18 ? 220  THR D OG1 1 
ATOM   10542 C  CG2 . THR D  3 222 ? -23.604 -12.664 8.874    1.00 170.33 ? 220  THR D CG2 1 
ATOM   10543 N  N   . ILE D  3 223 ? -21.795 -10.016 5.516    1.00 171.90 ? 221  ILE D N   1 
ATOM   10544 C  CA  . ILE D  3 223 ? -21.996 -9.122  4.382    1.00 187.25 ? 221  ILE D CA  1 
ATOM   10545 C  C   . ILE D  3 223 ? -21.347 -9.664  3.119    1.00 200.44 ? 221  ILE D C   1 
ATOM   10546 O  O   . ILE D  3 223 ? -21.662 -9.195  2.018    1.00 188.33 ? 221  ILE D O   1 
ATOM   10547 C  CB  . ILE D  3 223 ? -21.475 -7.711  4.715    1.00 197.87 ? 221  ILE D CB  1 
ATOM   10548 C  CG1 . ILE D  3 223 ? -21.882 -7.313  6.133    1.00 177.69 ? 221  ILE D CG1 1 
ATOM   10549 C  CG2 . ILE D  3 223 ? -22.028 -6.678  3.735    1.00 211.71 ? 221  ILE D CG2 1 
ATOM   10550 C  CD1 . ILE D  3 223 ? -21.695 -5.844  6.424    1.00 179.60 ? 221  ILE D CD1 1 
ATOM   10551 N  N   . HIS D  3 224 ? -20.499 -10.685 3.235    1.00 214.67 ? 222  HIS D N   1 
ATOM   10552 C  CA  . HIS D  3 224 ? -19.874 -11.282 2.064    1.00 214.99 ? 222  HIS D CA  1 
ATOM   10553 C  C   . HIS D  3 224 ? -20.834 -12.160 1.270    1.00 195.08 ? 222  HIS D C   1 
ATOM   10554 O  O   . HIS D  3 224 ? -20.416 -12.785 0.290    1.00 188.55 ? 222  HIS D O   1 
ATOM   10555 C  CB  . HIS D  3 224 ? -18.637 -12.089 2.478    1.00 231.12 ? 222  HIS D CB  1 
ATOM   10556 C  CG  . HIS D  3 224 ? -17.510 -12.022 1.491    1.00 239.04 ? 222  HIS D CG  1 
ATOM   10557 N  ND1 . HIS D  3 224 ? -17.709 -11.823 0.141    1.00 233.74 ? 222  HIS D ND1 1 
ATOM   10558 C  CD2 . HIS D  3 224 ? -16.170 -12.116 1.663    1.00 236.19 ? 222  HIS D CD2 1 
ATOM   10559 C  CE1 . HIS D  3 224 ? -16.542 -11.805 -0.477   1.00 236.86 ? 222  HIS D CE1 1 
ATOM   10560 N  NE2 . HIS D  3 224 ? -15.591 -11.983 0.423    1.00 250.84 ? 222  HIS D NE2 1 
ATOM   10561 N  N   . GLY D  3 225 ? -22.104 -12.203 1.651    1.00 180.52 ? 223  GLY D N   1 
ATOM   10562 C  CA  . GLY D  3 225 ? -23.092 -12.922 0.882    1.00 181.15 ? 223  GLY D CA  1 
ATOM   10563 C  C   . GLY D  3 225 ? -23.908 -11.945 0.069    1.00 178.37 ? 223  GLY D C   1 
ATOM   10564 O  O   . GLY D  3 225 ? -24.722 -12.345 -0.767   1.00 178.71 ? 223  GLY D O   1 
ATOM   10565 N  N   . MET D  3 226 ? -23.685 -10.653 0.298    1.00 179.74 ? 224  MET D N   1 
ATOM   10566 C  CA  . MET D  3 226 ? -24.339 -9.635  -0.502   1.00 174.95 ? 224  MET D CA  1 
ATOM   10567 C  C   . MET D  3 226 ? -23.765 -9.633  -1.910   1.00 174.84 ? 224  MET D C   1 
ATOM   10568 O  O   . MET D  3 226 ? -22.775 -10.305 -2.209   1.00 177.05 ? 224  MET D O   1 
ATOM   10569 C  CB  . MET D  3 226 ? -24.167 -8.248  0.115    1.00 173.62 ? 224  MET D CB  1 
ATOM   10570 C  CG  . MET D  3 226 ? -25.332 -7.778  0.956    1.00 182.77 ? 224  MET D CG  1 
ATOM   10571 S  SD  . MET D  3 226 ? -25.155 -6.041  1.404    1.00 185.42 ? 224  MET D SD  1 
ATOM   10572 C  CE  . MET D  3 226 ? -26.770 -5.716  2.109    1.00 189.07 ? 224  MET D CE  1 
ATOM   10573 N  N   . ASN D  3 227 ? -24.417 -8.871  -2.786   1.00 173.28 ? 225  ASN D N   1 
ATOM   10574 C  CA  . ASN D  3 227 ? -24.058 -8.754  -4.195   1.00 185.46 ? 225  ASN D CA  1 
ATOM   10575 C  C   . ASN D  3 227 ? -24.039 -10.102 -4.907   1.00 188.43 ? 225  ASN D C   1 
ATOM   10576 O  O   . ASN D  3 227 ? -23.510 -10.205 -6.021   1.00 196.58 ? 225  ASN D O   1 
ATOM   10577 C  CB  . ASN D  3 227 ? -22.705 -8.046  -4.375   1.00 191.88 ? 225  ASN D CB  1 
ATOM   10578 C  CG  . ASN D  3 227 ? -22.722 -6.606  -3.882   1.00 187.91 ? 225  ASN D CG  1 
ATOM   10579 O  OD1 . ASN D  3 227 ? -23.784 -6.000  -3.723   1.00 200.43 ? 225  ASN D OD1 1 
ATOM   10580 N  ND2 . ASN D  3 227 ? -21.538 -6.053  -3.636   1.00 175.24 ? 225  ASN D ND2 1 
ATOM   10581 N  N   . ARG D  3 228 ? -24.596 -11.141 -4.295   1.00 175.56 ? 226  ARG D N   1 
ATOM   10582 C  CA  . ARG D  3 228 ? -24.623 -12.436 -4.939   1.00 162.84 ? 226  ARG D CA  1 
ATOM   10583 C  C   . ARG D  3 228 ? -25.629 -12.415 -6.086   1.00 162.59 ? 226  ARG D C   1 
ATOM   10584 O  O   . ARG D  3 228 ? -26.562 -11.609 -6.087   1.00 172.76 ? 226  ARG D O   1 
ATOM   10585 C  CB  . ARG D  3 228 ? -24.979 -13.536 -3.938   1.00 176.08 ? 226  ARG D CB  1 
ATOM   10586 C  CG  . ARG D  3 228 ? -26.367 -13.436 -3.321   1.00 185.63 ? 226  ARG D CG  1 
ATOM   10587 C  CD  . ARG D  3 228 ? -26.613 -14.596 -2.363   1.00 184.19 ? 226  ARG D CD  1 
ATOM   10588 N  NE  . ARG D  3 228 ? -27.911 -14.519 -1.696   1.00 194.60 ? 226  ARG D NE  1 
ATOM   10589 C  CZ  . ARG D  3 228 ? -28.092 -14.066 -0.459   1.00 195.52 ? 226  ARG D CZ  1 
ATOM   10590 N  NH1 . ARG D  3 228 ? -27.054 -13.645 0.252    1.00 200.14 ? 226  ARG D NH1 1 
ATOM   10591 N  NH2 . ARG D  3 228 ? -29.308 -14.036 0.071    1.00 182.73 ? 226  ARG D NH2 1 
ATOM   10592 N  N   . PRO D  3 229 ? -25.423 -13.256 -7.099   1.00 157.64 ? 227  PRO D N   1 
ATOM   10593 C  CA  . PRO D  3 229 ? -26.380 -13.360 -8.210   1.00 158.65 ? 227  PRO D CA  1 
ATOM   10594 C  C   . PRO D  3 229 ? -27.844 -13.360 -7.799   1.00 158.02 ? 227  PRO D C   1 
ATOM   10595 O  O   . PRO D  3 229 ? -28.260 -14.138 -6.936   1.00 160.48 ? 227  PRO D O   1 
ATOM   10596 C  CB  . PRO D  3 229 ? -25.989 -14.691 -8.855   1.00 170.73 ? 227  PRO D CB  1 
ATOM   10597 C  CG  . PRO D  3 229 ? -24.509 -14.742 -8.662   1.00 176.68 ? 227  PRO D CG  1 
ATOM   10598 C  CD  . PRO D  3 229 ? -24.219 -14.070 -7.336   1.00 161.85 ? 227  PRO D CD  1 
ATOM   10599 N  N   . PHE D  3 230 ? -28.629 -12.472 -8.402   1.00 171.81 ? 228  PHE D N   1 
ATOM   10600 C  CA  . PHE D  3 230 ? -30.055 -12.377 -8.137   1.00 171.86 ? 228  PHE D CA  1 
ATOM   10601 C  C   . PHE D  3 230 ? -30.812 -12.306 -9.456   1.00 170.37 ? 228  PHE D C   1 
ATOM   10602 O  O   . PHE D  3 230 ? -30.278 -11.885 -10.484  1.00 170.56 ? 228  PHE D O   1 
ATOM   10603 C  CB  . PHE D  3 230 ? -30.395 -11.152 -7.284   1.00 166.62 ? 228  PHE D CB  1 
ATOM   10604 C  CG  . PHE D  3 230 ? -30.332 -9.857  -8.039   1.00 162.62 ? 228  PHE D CG  1 
ATOM   10605 C  CD1 . PHE D  3 230 ? -29.119 -9.234  -8.273   1.00 158.72 ? 228  PHE D CD1 1 
ATOM   10606 C  CD2 . PHE D  3 230 ? -31.487 -9.265  -8.519   1.00 169.37 ? 228  PHE D CD2 1 
ATOM   10607 C  CE1 . PHE D  3 230 ? -29.063 -8.044  -8.971   1.00 156.52 ? 228  PHE D CE1 1 
ATOM   10608 C  CE2 . PHE D  3 230 ? -31.436 -8.076  -9.216   1.00 174.23 ? 228  PHE D CE2 1 
ATOM   10609 C  CZ  . PHE D  3 230 ? -30.221 -7.463  -9.442   1.00 161.93 ? 228  PHE D CZ  1 
ATOM   10610 N  N   . LEU D  3 231 ? -32.078 -12.707 -9.409   1.00 167.26 ? 229  LEU D N   1 
ATOM   10611 C  CA  . LEU D  3 231 ? -32.948 -12.726 -10.577  1.00 180.93 ? 229  LEU D CA  1 
ATOM   10612 C  C   . LEU D  3 231 ? -33.895 -11.527 -10.515  1.00 183.33 ? 229  LEU D C   1 
ATOM   10613 O  O   . LEU D  3 231 ? -34.810 -11.489 -9.686   1.00 186.39 ? 229  LEU D O   1 
ATOM   10614 C  CB  . LEU D  3 231 ? -33.712 -14.045 -10.647  1.00 196.29 ? 229  LEU D CB  1 
ATOM   10615 C  CG  . LEU D  3 231 ? -34.629 -14.268 -11.848  1.00 202.98 ? 229  LEU D CG  1 
ATOM   10616 C  CD1 . LEU D  3 231 ? -33.855 -14.165 -13.155  1.00 201.04 ? 229  LEU D CD1 1 
ATOM   10617 C  CD2 . LEU D  3 231 ? -35.305 -15.619 -11.723  1.00 202.54 ? 229  LEU D CD2 1 
ATOM   10618 N  N   . LEU D  3 232 ? -33.649 -10.532 -11.366  1.00 171.41 ? 230  LEU D N   1 
ATOM   10619 C  CA  . LEU D  3 232 ? -34.495 -9.347  -11.433  1.00 164.41 ? 230  LEU D CA  1 
ATOM   10620 C  C   . LEU D  3 232 ? -35.780 -9.643  -12.205  1.00 165.73 ? 230  LEU D C   1 
ATOM   10621 O  O   . LEU D  3 232 ? -35.734 -10.125 -13.341  1.00 166.67 ? 230  LEU D O   1 
ATOM   10622 C  CB  . LEU D  3 232 ? -33.725 -8.202  -12.086  1.00 159.13 ? 230  LEU D CB  1 
ATOM   10623 C  CG  . LEU D  3 232 ? -34.352 -6.815  -12.002  1.00 156.48 ? 230  LEU D CG  1 
ATOM   10624 C  CD1 . LEU D  3 232 ? -34.488 -6.400  -10.545  1.00 163.38 ? 230  LEU D CD1 1 
ATOM   10625 C  CD2 . LEU D  3 232 ? -33.504 -5.821  -12.769  1.00 155.23 ? 230  LEU D CD2 1 
ATOM   10626 N  N   . LEU D  3 233 ? -36.926 -9.351  -11.589  1.00 166.24 ? 231  LEU D N   1 
ATOM   10627 C  CA  . LEU D  3 233 ? -38.233 -9.639  -12.168  1.00 168.91 ? 231  LEU D CA  1 
ATOM   10628 C  C   . LEU D  3 233 ? -39.005 -8.350  -12.433  1.00 164.29 ? 231  LEU D C   1 
ATOM   10629 O  O   . LEU D  3 233 ? -38.964 -7.414  -11.629  1.00 160.13 ? 231  LEU D O   1 
ATOM   10630 C  CB  . LEU D  3 233 ? -39.050 -10.543 -11.238  1.00 176.61 ? 231  LEU D CB  1 
ATOM   10631 C  CG  . LEU D  3 233 ? -38.380 -11.843 -10.791  1.00 175.01 ? 231  LEU D CG  1 
ATOM   10632 C  CD1 . LEU D  3 233 ? -39.239 -12.562 -9.757   1.00 173.63 ? 231  LEU D CD1 1 
ATOM   10633 C  CD2 . LEU D  3 233 ? -38.103 -12.735 -11.985  1.00 178.66 ? 231  LEU D CD2 1 
ATOM   10634 N  N   . MET D  3 234 ? -39.725 -8.312  -13.556  1.00 179.42 ? 232  MET D N   1 
ATOM   10635 C  CA  . MET D  3 234 ? -40.574 -7.177  -13.927  1.00 184.04 ? 232  MET D CA  1 
ATOM   10636 C  C   . MET D  3 234 ? -41.918 -7.726  -14.405  1.00 182.10 ? 232  MET D C   1 
ATOM   10637 O  O   . MET D  3 234 ? -42.026 -8.220  -15.531  1.00 179.25 ? 232  MET D O   1 
ATOM   10638 C  CB  . MET D  3 234 ? -39.912 -6.320  -15.003  1.00 189.18 ? 232  MET D CB  1 
ATOM   10639 C  CG  . MET D  3 234 ? -38.519 -5.815  -14.638  1.00 198.47 ? 232  MET D CG  1 
ATOM   10640 S  SD  . MET D  3 234 ? -37.711 -4.945  -15.999  1.00 226.99 ? 232  MET D SD  1 
ATOM   10641 C  CE  . MET D  3 234 ? -36.124 -4.547  -15.268  1.00 216.91 ? 232  MET D CE  1 
ATOM   10642 N  N   . ALA D  3 235 ? -42.946 -7.633  -13.561  1.00 177.21 ? 233  ALA D N   1 
ATOM   10643 C  CA  . ALA D  3 235 ? -44.244 -8.231  -13.840  1.00 175.30 ? 233  ALA D CA  1 
ATOM   10644 C  C   . ALA D  3 235 ? -45.343 -7.183  -13.722  1.00 179.46 ? 233  ALA D C   1 
ATOM   10645 O  O   . ALA D  3 235 ? -45.110 -6.045  -13.309  1.00 189.05 ? 233  ALA D O   1 
ATOM   10646 C  CB  . ALA D  3 235 ? -44.536 -9.406  -12.897  1.00 186.91 ? 233  ALA D CB  1 
ATOM   10647 N  N   . THR D  3 236 ? -46.574 -7.588  -14.103  1.00 177.08 ? 234  THR D N   1 
ATOM   10648 C  CA  . THR D  3 236 ? -47.752 -6.727  -14.037  1.00 177.81 ? 234  THR D CA  1 
ATOM   10649 C  C   . THR D  3 236 ? -48.565 -7.049  -12.793  1.00 180.32 ? 234  THR D C   1 
ATOM   10650 O  O   . THR D  3 236 ? -48.874 -8.227  -12.555  1.00 188.27 ? 234  THR D O   1 
ATOM   10651 C  CB  . THR D  3 236 ? -48.618 -6.908  -15.279  1.00 183.10 ? 234  THR D CB  1 
ATOM   10652 O  OG1 . THR D  3 236 ? -47.864 -6.556  -16.445  1.00 182.65 ? 234  THR D OG1 1 
ATOM   10653 C  CG2 . THR D  3 236 ? -49.854 -6.025  -15.199  1.00 191.40 ? 234  THR D CG2 1 
ATOM   10654 N  N   . PRO D  3 237 ? -48.907 -6.051  -11.975  1.00 188.42 ? 235  PRO D N   1 
ATOM   10655 C  CA  . PRO D  3 237 ? -49.637 -6.325  -10.730  1.00 191.92 ? 235  PRO D CA  1 
ATOM   10656 C  C   . PRO D  3 237 ? -50.970 -7.026  -10.958  1.00 198.54 ? 235  PRO D C   1 
ATOM   10657 O  O   . PRO D  3 237 ? -51.620 -6.867  -11.995  1.00 201.77 ? 235  PRO D O   1 
ATOM   10658 C  CB  . PRO D  3 237 ? -49.842 -4.930  -10.129  1.00 195.29 ? 235  PRO D CB  1 
ATOM   10659 C  CG  . PRO D  3 237 ? -48.727 -4.112  -10.694  1.00 191.80 ? 235  PRO D CG  1 
ATOM   10660 C  CD  . PRO D  3 237 ? -48.530 -4.632  -12.093  1.00 187.05 ? 235  PRO D CD  1 
ATOM   10661 N  N   . LEU D  3 238 ? -51.375 -7.805  -9.951   1.00 209.07 ? 236  LEU D N   1 
ATOM   10662 C  CA  . LEU D  3 238 ? -52.641 -8.527  -10.015  1.00 213.89 ? 236  LEU D CA  1 
ATOM   10663 C  C   . LEU D  3 238 ? -53.827 -7.583  -9.895   1.00 221.71 ? 236  LEU D C   1 
ATOM   10664 O  O   . LEU D  3 238 ? -54.914 -7.887  -10.402  1.00 219.53 ? 236  LEU D O   1 
ATOM   10665 C  CB  . LEU D  3 238 ? -52.708 -9.580  -8.905   1.00 215.08 ? 236  LEU D CB  1 
ATOM   10666 C  CG  . LEU D  3 238 ? -51.650 -10.685 -8.835   1.00 213.78 ? 236  LEU D CG  1 
ATOM   10667 C  CD1 . LEU D  3 238 ? -50.404 -10.213 -8.095   1.00 207.93 ? 236  LEU D CD1 1 
ATOM   10668 C  CD2 . LEU D  3 238 ? -52.224 -11.932 -8.180   1.00 224.44 ? 236  LEU D CD2 1 
ATOM   10669 N  N   . GLU D  3 239 ? -53.634 -6.434  -9.238   1.00 225.49 ? 237  GLU D N   1 
ATOM   10670 C  CA  . GLU D  3 239 ? -54.726 -5.484  -9.055   1.00 221.45 ? 237  GLU D CA  1 
ATOM   10671 C  C   . GLU D  3 239 ? -55.219 -4.957  -10.390  1.00 219.51 ? 237  GLU D C   1 
ATOM   10672 O  O   . GLU D  3 239 ? -56.393 -4.594  -10.522  1.00 232.51 ? 237  GLU D O   1 
ATOM   10673 C  CB  . GLU D  3 239 ? -54.284 -4.323  -8.160   1.00 212.55 ? 237  GLU D CB  1 
ATOM   10674 C  CG  . GLU D  3 239 ? -53.914 -4.715  -6.737   1.00 209.84 ? 237  GLU D CG  1 
ATOM   10675 C  CD  . GLU D  3 239 ? -52.552 -5.368  -6.644   1.00 216.64 ? 237  GLU D CD  1 
ATOM   10676 O  OE1 . GLU D  3 239 ? -51.811 -5.343  -7.649   1.00 225.24 ? 237  GLU D OE1 1 
ATOM   10677 O  OE2 . GLU D  3 239 ? -52.229 -5.917  -5.571   1.00 216.75 ? 237  GLU D OE2 1 
ATOM   10678 N  N   . ARG D  3 240 ? -54.340 -4.916  -11.390  1.00 205.77 ? 238  ARG D N   1 
ATOM   10679 C  CA  . ARG D  3 240 ? -54.730 -4.418  -12.699  1.00 208.23 ? 238  ARG D CA  1 
ATOM   10680 C  C   . ARG D  3 240 ? -55.498 -5.485  -13.466  1.00 215.95 ? 238  ARG D C   1 
ATOM   10681 O  O   . ARG D  3 240 ? -56.685 -5.315  -13.767  1.00 223.21 ? 238  ARG D O   1 
ATOM   10682 C  CB  . ARG D  3 240 ? -53.489 -3.972  -13.474  1.00 206.39 ? 238  ARG D CB  1 
ATOM   10683 C  CG  . ARG D  3 240 ? -52.541 -3.120  -12.647  1.00 204.68 ? 238  ARG D CG  1 
ATOM   10684 C  CD  . ARG D  3 240 ? -51.465 -2.475  -13.503  1.00 202.91 ? 238  ARG D CD  1 
ATOM   10685 N  NE  . ARG D  3 240 ? -50.369 -1.933  -12.702  1.00 198.64 ? 238  ARG D NE  1 
ATOM   10686 C  CZ  . ARG D  3 240 ? -50.417 -0.777  -12.045  1.00 196.53 ? 238  ARG D CZ  1 
ATOM   10687 N  NH1 . ARG D  3 240 ? -51.515 -0.032  -12.077  1.00 201.34 ? 238  ARG D NH1 1 
ATOM   10688 N  NH2 . ARG D  3 240 ? -49.365 -0.367  -11.347  1.00 187.52 ? 238  ARG D NH2 1 
ATOM   10689 N  N   . ALA D  3 241 ? -54.837 -6.606  -13.756  1.00 201.59 ? 239  ALA D N   1 
ATOM   10690 C  CA  . ALA D  3 241 ? -55.443 -7.717  -14.479  1.00 209.35 ? 239  ALA D CA  1 
ATOM   10691 C  C   . ALA D  3 241 ? -56.181 -7.242  -15.725  1.00 217.94 ? 239  ALA D C   1 
ATOM   10692 O  O   . ALA D  3 241 ? -55.754 -6.285  -16.381  1.00 212.26 ? 239  ALA D O   1 
ATOM   10693 C  CB  . ALA D  3 241 ? -56.395 -8.492  -13.563  1.00 215.48 ? 239  ALA D CB  1 
ATOM   10694 N  N   . GLN D  3 242 ? -57.296 -7.898  -16.041  1.00 224.77 ? 240  GLN D N   1 
ATOM   10695 C  CA  . GLN D  3 242 ? -58.131 -7.542  -17.185  1.00 224.47 ? 240  GLN D CA  1 
ATOM   10696 C  C   . GLN D  3 242 ? -57.319 -7.493  -18.479  1.00 231.42 ? 240  GLN D C   1 
ATOM   10697 O  O   . GLN D  3 242 ? -56.351 -8.237  -18.647  1.00 233.82 ? 240  GLN D O   1 
ATOM   10698 C  CB  . GLN D  3 242 ? -58.835 -6.203  -16.938  1.00 216.05 ? 240  GLN D CB  1 
ATOM   10699 C  CG  . GLN D  3 242 ? -59.753 -5.763  -18.066  1.00 218.16 ? 240  GLN D CG  1 
ATOM   10700 C  CD  . GLN D  3 242 ? -59.045 -4.902  -19.087  1.00 214.25 ? 240  GLN D CD  1 
ATOM   10701 O  OE1 . GLN D  3 242 ? -57.975 -4.356  -18.817  1.00 211.59 ? 240  GLN D OE1 1 
ATOM   10702 N  NE2 . GLN D  3 242 ? -59.630 -4.786  -20.275  1.00 213.04 ? 240  GLN D NE2 1 
ATOM   10703 N  N   . CYS D  3 258 ? -57.507 0.016   -35.068  1.00 251.38 ? 256  CYS D N   1 
ATOM   10704 C  CA  . CYS D  3 258 ? -58.769 0.178   -35.781  1.00 258.98 ? 256  CYS D CA  1 
ATOM   10705 C  C   . CYS D  3 258 ? -59.819 -0.749  -35.176  1.00 262.29 ? 256  CYS D C   1 
ATOM   10706 O  O   . CYS D  3 258 ? -61.002 -0.666  -35.506  1.00 261.75 ? 256  CYS D O   1 
ATOM   10707 C  CB  . CYS D  3 258 ? -58.572 -0.091  -37.272  1.00 269.72 ? 256  CYS D CB  1 
ATOM   10708 S  SG  . CYS D  3 258 ? -56.871 0.253   -37.796  1.00 291.82 ? 256  CYS D SG  1 
ATOM   10709 N  N   . PHE D  3 259 ? -59.374 -1.628  -34.278  1.00 280.20 ? 257  PHE D N   1 
ATOM   10710 C  CA  . PHE D  3 259 ? -60.296 -2.416  -33.472  1.00 288.83 ? 257  PHE D CA  1 
ATOM   10711 C  C   . PHE D  3 259 ? -60.592 -1.764  -32.134  1.00 293.27 ? 257  PHE D C   1 
ATOM   10712 O  O   . PHE D  3 259 ? -61.652 -2.018  -31.547  1.00 300.68 ? 257  PHE D O   1 
ATOM   10713 C  CB  . PHE D  3 259 ? -59.738 -3.827  -33.240  1.00 288.77 ? 257  PHE D CB  1 
ATOM   10714 C  CG  . PHE D  3 259 ? -58.509 -3.873  -32.376  1.00 295.86 ? 257  PHE D CG  1 
ATOM   10715 C  CD1 . PHE D  3 259 ? -57.246 -3.751  -32.933  1.00 301.60 ? 257  PHE D CD1 1 
ATOM   10716 C  CD2 . PHE D  3 259 ? -58.616 -4.074  -31.008  1.00 296.73 ? 257  PHE D CD2 1 
ATOM   10717 C  CE1 . PHE D  3 259 ? -56.115 -3.810  -32.136  1.00 301.23 ? 257  PHE D CE1 1 
ATOM   10718 C  CE2 . PHE D  3 259 ? -57.494 -4.132  -30.208  1.00 293.74 ? 257  PHE D CE2 1 
ATOM   10719 C  CZ  . PHE D  3 259 ? -56.241 -4.001  -30.771  1.00 295.99 ? 257  PHE D CZ  1 
ATOM   10720 N  N   . SER D  3 260 ? -59.677 -0.940  -31.639  1.00 291.76 ? 258  SER D N   1 
ATOM   10721 C  CA  . SER D  3 260 ? -59.919 -0.182  -30.426  1.00 288.99 ? 258  SER D CA  1 
ATOM   10722 C  C   . SER D  3 260 ? -60.735 1.074   -30.683  1.00 286.17 ? 258  SER D C   1 
ATOM   10723 O  O   . SER D  3 260 ? -61.164 1.726   -29.724  1.00 293.51 ? 258  SER D O   1 
ATOM   10724 C  CB  . SER D  3 260 ? -58.587 0.184   -29.773  1.00 280.65 ? 258  SER D CB  1 
ATOM   10725 O  OG  . SER D  3 260 ? -57.793 0.948   -30.662  1.00 277.64 ? 258  SER D OG  1 
ATOM   10726 N  N   . SER D  3 261 ? -60.974 1.418   -31.944  1.00 272.98 ? 259  SER D N   1 
ATOM   10727 C  CA  . SER D  3 261 ? -61.700 2.624   -32.300  1.00 271.47 ? 259  SER D CA  1 
ATOM   10728 C  C   . SER D  3 261 ? -62.815 2.286   -33.279  1.00 281.26 ? 259  SER D C   1 
ATOM   10729 O  O   . SER D  3 261 ? -62.657 1.428   -34.153  1.00 295.72 ? 259  SER D O   1 
ATOM   10730 C  CB  . SER D  3 261 ? -60.764 3.673   -32.917  1.00 265.52 ? 259  SER D CB  1 
ATOM   10731 O  OG  . SER D  3 261 ? -60.069 3.144   -34.034  1.00 268.61 ? 259  SER D OG  1 
ATOM   10732 N  N   . THR D  3 262 ? -63.957 2.957   -33.109  1.00 273.59 ? 260  THR D N   1 
ATOM   10733 C  CA  . THR D  3 262 ? -65.008 2.922   -34.115  1.00 279.02 ? 260  THR D CA  1 
ATOM   10734 C  C   . THR D  3 262 ? -64.761 3.932   -35.225  1.00 278.15 ? 260  THR D C   1 
ATOM   10735 O  O   . THR D  3 262 ? -65.286 3.765   -36.332  1.00 280.96 ? 260  THR D O   1 
ATOM   10736 C  CB  . THR D  3 262 ? -66.380 3.185   -33.477  1.00 272.09 ? 260  THR D CB  1 
ATOM   10737 O  OG1 . THR D  3 262 ? -66.409 4.501   -32.910  1.00 272.98 ? 260  THR D OG1 1 
ATOM   10738 C  CG2 . THR D  3 262 ? -66.667 2.159   -32.387  1.00 260.13 ? 260  THR D CG2 1 
ATOM   10739 N  N   . GLU D  3 263 ? -63.958 4.958   -34.957  1.00 263.18 ? 261  GLU D N   1 
ATOM   10740 C  CA  . GLU D  3 263 ? -63.603 5.942   -35.960  1.00 258.07 ? 261  GLU D CA  1 
ATOM   10741 C  C   . GLU D  3 263 ? -62.364 5.493   -36.724  1.00 251.59 ? 261  GLU D C   1 
ATOM   10742 O  O   . GLU D  3 263 ? -61.588 4.651   -36.267  1.00 241.63 ? 261  GLU D O   1 
ATOM   10743 C  CB  . GLU D  3 263 ? -63.344 7.304   -35.314  1.00 246.47 ? 261  GLU D CB  1 
ATOM   10744 C  CG  . GLU D  3 263 ? -64.522 7.856   -34.530  1.00 250.92 ? 261  GLU D CG  1 
ATOM   10745 C  CD  . GLU D  3 263 ? -65.750 8.093   -35.394  1.00 257.48 ? 261  GLU D CD  1 
ATOM   10746 O  OE1 . GLU D  3 263 ? -65.590 8.437   -36.584  1.00 260.64 ? 261  GLU D OE1 1 
ATOM   10747 O  OE2 . GLU D  3 263 ? -66.879 7.932   -34.883  1.00 251.67 ? 261  GLU D OE2 1 
ATOM   10748 N  N   . LYS D  3 264 ? -62.189 6.066   -37.916  1.00 267.07 ? 262  LYS D N   1 
ATOM   10749 C  CA  . LYS D  3 264 ? -60.963 5.829   -38.664  1.00 260.20 ? 262  LYS D CA  1 
ATOM   10750 C  C   . LYS D  3 264 ? -59.840 6.607   -37.984  1.00 270.25 ? 262  LYS D C   1 
ATOM   10751 O  O   . LYS D  3 264 ? -59.613 7.790   -38.259  1.00 271.66 ? 262  LYS D O   1 
ATOM   10752 C  CB  . LYS D  3 264 ? -61.133 6.178   -40.156  1.00 250.43 ? 262  LYS D CB  1 
ATOM   10753 C  CG  . LYS D  3 264 ? -61.399 7.636   -40.549  1.00 247.23 ? 262  LYS D CG  1 
ATOM   10754 C  CD  . LYS D  3 264 ? -62.778 8.126   -40.149  1.00 252.86 ? 262  LYS D CD  1 
ATOM   10755 C  CE  . LYS D  3 264 ? -62.676 9.100   -38.988  1.00 253.59 ? 262  LYS D CE  1 
ATOM   10756 N  NZ  . LYS D  3 264 ? -63.893 9.079   -38.136  1.00 257.28 ? 262  LYS D NZ  1 
ATOM   10757 N  N   . ASN D  3 265 ? -59.159 5.949   -37.055  1.00 280.66 ? 263  ASN D N   1 
ATOM   10758 C  CA  . ASN D  3 265 ? -58.103 6.581   -36.277  1.00 270.76 ? 263  ASN D CA  1 
ATOM   10759 C  C   . ASN D  3 265 ? -56.835 6.642   -37.124  1.00 269.66 ? 263  ASN D C   1 
ATOM   10760 O  O   . ASN D  3 265 ? -56.852 6.379   -38.330  1.00 275.48 ? 263  ASN D O   1 
ATOM   10761 C  CB  . ASN D  3 265 ? -57.881 5.823   -34.972  1.00 256.51 ? 263  ASN D CB  1 
ATOM   10762 C  CG  . ASN D  3 265 ? -57.285 6.694   -33.887  1.00 244.36 ? 263  ASN D CG  1 
ATOM   10763 O  OD1 . ASN D  3 265 ? -56.680 7.734   -34.160  1.00 240.68 ? 263  ASN D OD1 1 
ATOM   10764 N  ND2 . ASN D  3 265 ? -57.454 6.272   -32.643  1.00 241.17 ? 263  ASN D ND2 1 
ATOM   10765 N  N   . CYS D  3 266 ? -55.707 6.985   -36.503  1.00 262.41 ? 264  CYS D N   1 
ATOM   10766 C  CA  . CYS D  3 266 ? -54.417 6.941   -37.191  1.00 260.34 ? 264  CYS D CA  1 
ATOM   10767 C  C   . CYS D  3 266 ? -54.133 5.481   -37.534  1.00 260.52 ? 264  CYS D C   1 
ATOM   10768 O  O   . CYS D  3 266 ? -53.321 4.801   -36.904  1.00 254.82 ? 264  CYS D O   1 
ATOM   10769 C  CB  . CYS D  3 266 ? -53.328 7.565   -36.322  1.00 249.13 ? 264  CYS D CB  1 
ATOM   10770 S  SG  . CYS D  3 266 ? -51.570 7.394   -36.841  1.00 241.43 ? 264  CYS D SG  1 
ATOM   10771 N  N   . CYS D  3 267 ? -54.852 4.977   -38.535  1.00 261.71 ? 265  CYS D N   1 
ATOM   10772 C  CA  . CYS D  3 267 ? -54.644 3.632   -39.051  1.00 263.93 ? 265  CYS D CA  1 
ATOM   10773 C  C   . CYS D  3 267 ? -54.025 3.725   -40.439  1.00 261.56 ? 265  CYS D C   1 
ATOM   10774 O  O   . CYS D  3 267 ? -54.336 4.642   -41.209  1.00 273.02 ? 265  CYS D O   1 
ATOM   10775 C  CB  . CYS D  3 267 ? -55.962 2.839   -39.088  1.00 275.17 ? 265  CYS D CB  1 
ATOM   10776 S  SG  . CYS D  3 267 ? -56.537 2.235   -37.467  1.00 279.67 ? 265  CYS D SG  1 
ATOM   10777 N  N   . VAL D  3 268 ? -53.132 2.787   -40.745  1.00 241.95 ? 266  VAL D N   1 
ATOM   10778 C  CA  . VAL D  3 268 ? -52.406 2.837   -42.007  1.00 238.86 ? 266  VAL D CA  1 
ATOM   10779 C  C   . VAL D  3 268 ? -53.341 2.415   -43.134  1.00 243.68 ? 266  VAL D C   1 
ATOM   10780 O  O   . VAL D  3 268 ? -53.973 1.354   -43.076  1.00 243.68 ? 266  VAL D O   1 
ATOM   10781 C  CB  . VAL D  3 268 ? -51.146 1.965   -41.947  1.00 239.71 ? 266  VAL D CB  1 
ATOM   10782 C  CG1 . VAL D  3 268 ? -51.450 0.616   -41.308  1.00 243.16 ? 266  VAL D CG1 1 
ATOM   10783 C  CG2 . VAL D  3 268 ? -50.556 1.793   -43.334  1.00 245.15 ? 266  VAL D CG2 1 
ATOM   10784 N  N   . ARG D  3 269 ? -53.442 3.256   -44.159  1.00 257.27 ? 267  ARG D N   1 
ATOM   10785 C  CA  . ARG D  3 269 ? -54.385 3.059   -45.249  1.00 269.76 ? 267  ARG D CA  1 
ATOM   10786 C  C   . ARG D  3 269 ? -53.703 2.413   -46.451  1.00 266.83 ? 267  ARG D C   1 
ATOM   10787 O  O   . ARG D  3 269 ? -52.511 2.617   -46.702  1.00 259.39 ? 267  ARG D O   1 
ATOM   10788 C  CB  . ARG D  3 269 ? -55.022 4.391   -45.655  1.00 276.89 ? 267  ARG D CB  1 
ATOM   10789 C  CG  . ARG D  3 269 ? -55.802 5.069   -44.531  1.00 274.19 ? 267  ARG D CG  1 
ATOM   10790 C  CD  . ARG D  3 269 ? -56.873 4.142   -43.968  1.00 273.94 ? 267  ARG D CD  1 
ATOM   10791 N  NE  . ARG D  3 269 ? -57.366 4.588   -42.668  1.00 267.44 ? 267  ARG D NE  1 
ATOM   10792 C  CZ  . ARG D  3 269 ? -58.213 3.895   -41.914  1.00 259.13 ? 267  ARG D CZ  1 
ATOM   10793 N  NH1 . ARG D  3 269 ? -58.668 2.721   -42.329  1.00 259.42 ? 267  ARG D NH1 1 
ATOM   10794 N  NH2 . ARG D  3 269 ? -58.604 4.374   -40.743  1.00 252.81 ? 267  ARG D NH2 1 
ATOM   10795 N  N   . GLN D  3 270 ? -54.481 1.628   -47.193  1.00 270.08 ? 268  GLN D N   1 
ATOM   10796 C  CA  . GLN D  3 270 ? -53.968 0.885   -48.336  1.00 267.36 ? 268  GLN D CA  1 
ATOM   10797 C  C   . GLN D  3 270 ? -53.769 1.805   -49.536  1.00 270.60 ? 268  GLN D C   1 
ATOM   10798 O  O   . GLN D  3 270 ? -54.595 2.681   -49.810  1.00 278.76 ? 268  GLN D O   1 
ATOM   10799 C  CB  . GLN D  3 270 ? -54.928 -0.250  -48.695  1.00 272.50 ? 268  GLN D CB  1 
ATOM   10800 C  CG  . GLN D  3 270 ? -54.496 -1.109  -49.872  1.00 281.64 ? 268  GLN D CG  1 
ATOM   10801 C  CD  . GLN D  3 270 ? -55.546 -2.137  -50.257  1.00 290.04 ? 268  GLN D CD  1 
ATOM   10802 O  OE1 . GLN D  3 270 ? -56.590 -2.246  -49.614  1.00 291.67 ? 268  GLN D OE1 1 
ATOM   10803 N  NE2 . GLN D  3 270 ? -55.273 -2.896  -51.314  1.00 291.85 ? 268  GLN D NE2 1 
ATOM   10804 N  N   . LEU D  3 271 ? -52.664 1.598   -50.254  1.00 263.84 ? 269  LEU D N   1 
ATOM   10805 C  CA  . LEU D  3 271 ? -52.352 2.415   -51.428  1.00 265.91 ? 269  LEU D CA  1 
ATOM   10806 C  C   . LEU D  3 271 ? -51.391 1.634   -52.316  1.00 274.73 ? 269  LEU D C   1 
ATOM   10807 O  O   . LEU D  3 271 ? -50.230 1.437   -51.944  1.00 274.80 ? 269  LEU D O   1 
ATOM   10808 C  CB  . LEU D  3 271 ? -51.752 3.752   -51.011  1.00 260.70 ? 269  LEU D CB  1 
ATOM   10809 C  CG  . LEU D  3 271 ? -51.307 4.666   -52.151  1.00 261.00 ? 269  LEU D CG  1 
ATOM   10810 C  CD1 . LEU D  3 271 ? -52.480 4.982   -53.063  1.00 275.60 ? 269  LEU D CD1 1 
ATOM   10811 C  CD2 . LEU D  3 271 ? -50.688 5.940   -51.603  1.00 257.93 ? 269  LEU D CD2 1 
ATOM   10812 N  N   . TYR D  3 272 ? -51.867 1.204   -53.483  1.00 287.17 ? 270  TYR D N   1 
ATOM   10813 C  CA  . TYR D  3 272 ? -51.057 0.458   -54.441  1.00 291.32 ? 270  TYR D CA  1 
ATOM   10814 C  C   . TYR D  3 272 ? -50.524 1.414   -55.504  1.00 297.44 ? 270  TYR D C   1 
ATOM   10815 O  O   . TYR D  3 272 ? -51.305 2.089   -56.187  1.00 302.57 ? 270  TYR D O   1 
ATOM   10816 C  CB  . TYR D  3 272 ? -51.873 -0.666  -55.079  1.00 289.75 ? 270  TYR D CB  1 
ATOM   10817 C  CG  . TYR D  3 272 ? -51.158 -1.387  -56.200  1.00 288.39 ? 270  TYR D CG  1 
ATOM   10818 C  CD1 . TYR D  3 272 ? -50.163 -2.317  -55.929  1.00 283.33 ? 270  TYR D CD1 1 
ATOM   10819 C  CD2 . TYR D  3 272 ? -51.484 -1.142  -57.529  1.00 287.98 ? 270  TYR D CD2 1 
ATOM   10820 C  CE1 . TYR D  3 272 ? -49.509 -2.979  -56.949  1.00 280.81 ? 270  TYR D CE1 1 
ATOM   10821 C  CE2 . TYR D  3 272 ? -50.836 -1.799  -58.555  1.00 284.89 ? 270  TYR D CE2 1 
ATOM   10822 C  CZ  . TYR D  3 272 ? -49.850 -2.715  -58.260  1.00 282.78 ? 270  TYR D CZ  1 
ATOM   10823 O  OH  . TYR D  3 272 ? -49.205 -3.370  -59.283  1.00 287.27 ? 270  TYR D OH  1 
ATOM   10824 N  N   . ILE D  3 273 ? -49.201 1.458   -55.656  1.00 283.79 ? 271  ILE D N   1 
ATOM   10825 C  CA  . ILE D  3 273 ? -48.535 2.388   -56.563  1.00 271.34 ? 271  ILE D CA  1 
ATOM   10826 C  C   . ILE D  3 273 ? -47.898 1.600   -57.700  1.00 269.90 ? 271  ILE D C   1 
ATOM   10827 O  O   . ILE D  3 273 ? -47.025 0.753   -57.468  1.00 261.80 ? 271  ILE D O   1 
ATOM   10828 C  CB  . ILE D  3 273 ? -47.484 3.238   -55.834  1.00 260.52 ? 271  ILE D CB  1 
ATOM   10829 C  CG1 . ILE D  3 273 ? -48.165 4.156   -54.817  1.00 265.85 ? 271  ILE D CG1 1 
ATOM   10830 C  CG2 . ILE D  3 273 ? -46.668 4.042   -56.835  1.00 259.38 ? 271  ILE D CG2 1 
ATOM   10831 C  CD1 . ILE D  3 273 ? -47.223 5.124   -54.137  1.00 267.28 ? 271  ILE D CD1 1 
ATOM   10832 N  N   . ASP D  3 274 ? -48.322 1.895   -58.926  1.00 280.24 ? 272  ASP D N   1 
ATOM   10833 C  CA  . ASP D  3 274 ? -47.751 1.307   -60.130  1.00 282.76 ? 272  ASP D CA  1 
ATOM   10834 C  C   . ASP D  3 274 ? -46.790 2.303   -60.768  1.00 276.89 ? 272  ASP D C   1 
ATOM   10835 O  O   . ASP D  3 274 ? -47.024 3.514   -60.739  1.00 274.39 ? 272  ASP D O   1 
ATOM   10836 C  CB  . ASP D  3 274 ? -48.851 0.919   -61.125  1.00 280.62 ? 272  ASP D CB  1 
ATOM   10837 C  CG  . ASP D  3 274 ? -48.365 -0.042  -62.203  1.00 267.87 ? 272  ASP D CG  1 
ATOM   10838 O  OD1 . ASP D  3 274 ? -47.190 0.049   -62.615  1.00 260.21 ? 272  ASP D OD1 1 
ATOM   10839 O  OD2 . ASP D  3 274 ? -49.166 -0.895  -62.642  1.00 267.12 ? 272  ASP D OD2 1 
ATOM   10840 N  N   . PHE D  3 275 ? -45.704 1.786   -61.343  1.00 269.64 ? 273  PHE D N   1 
ATOM   10841 C  CA  . PHE D  3 275 ? -44.706 2.670   -61.934  1.00 265.89 ? 273  PHE D CA  1 
ATOM   10842 C  C   . PHE D  3 275 ? -45.151 3.188   -63.294  1.00 268.35 ? 273  PHE D C   1 
ATOM   10843 O  O   . PHE D  3 275 ? -44.977 4.373   -63.596  1.00 269.39 ? 273  PHE D O   1 
ATOM   10844 C  CB  . PHE D  3 275 ? -43.367 1.943   -62.050  1.00 270.51 ? 273  PHE D CB  1 
ATOM   10845 C  CG  . PHE D  3 275 ? -42.768 1.573   -60.725  1.00 268.38 ? 273  PHE D CG  1 
ATOM   10846 C  CD1 . PHE D  3 275 ? -41.957 2.466   -60.046  1.00 262.58 ? 273  PHE D CD1 1 
ATOM   10847 C  CD2 . PHE D  3 275 ? -43.019 0.335   -60.156  1.00 266.66 ? 273  PHE D CD2 1 
ATOM   10848 C  CE1 . PHE D  3 275 ? -41.406 2.130   -58.826  1.00 258.60 ? 273  PHE D CE1 1 
ATOM   10849 C  CE2 . PHE D  3 275 ? -42.469 -0.007  -58.935  1.00 259.45 ? 273  PHE D CE2 1 
ATOM   10850 C  CZ  . PHE D  3 275 ? -41.662 0.891   -58.271  1.00 257.37 ? 273  PHE D CZ  1 
ATOM   10851 N  N   . ARG D  3 276 ? -45.731 2.319   -64.122  1.00 275.09 ? 274  ARG D N   1 
ATOM   10852 C  CA  . ARG D  3 276 ? -46.194 2.747   -65.435  1.00 283.26 ? 274  ARG D CA  1 
ATOM   10853 C  C   . ARG D  3 276 ? -47.479 3.559   -65.347  1.00 293.50 ? 274  ARG D C   1 
ATOM   10854 O  O   . ARG D  3 276 ? -47.762 4.364   -66.242  1.00 306.04 ? 274  ARG D O   1 
ATOM   10855 C  CB  . ARG D  3 276 ? -46.400 1.529   -66.340  1.00 280.49 ? 274  ARG D CB  1 
ATOM   10856 C  CG  . ARG D  3 276 ? -45.117 0.776   -66.675  1.00 274.50 ? 274  ARG D CG  1 
ATOM   10857 C  CD  . ARG D  3 276 ? -44.315 1.461   -67.779  1.00 274.01 ? 274  ARG D CD  1 
ATOM   10858 N  NE  . ARG D  3 276 ? -44.948 1.331   -69.091  1.00 281.49 ? 274  ARG D NE  1 
ATOM   10859 C  CZ  . ARG D  3 276 ? -45.669 2.283   -69.675  1.00 275.91 ? 274  ARG D CZ  1 
ATOM   10860 N  NH1 . ARG D  3 276 ? -45.848 3.449   -69.068  1.00 274.44 ? 274  ARG D NH1 1 
ATOM   10861 N  NH2 . ARG D  3 276 ? -46.208 2.073   -70.869  1.00 274.27 ? 274  ARG D NH2 1 
ATOM   10862 N  N   . LYS D  3 277 ? -48.256 3.376   -64.281  1.00 296.07 ? 275  LYS D N   1 
ATOM   10863 C  CA  . LYS D  3 277 ? -49.552 4.030   -64.162  1.00 299.59 ? 275  LYS D CA  1 
ATOM   10864 C  C   . LYS D  3 277 ? -49.476 5.321   -63.354  1.00 299.92 ? 275  LYS D C   1 
ATOM   10865 O  O   . LYS D  3 277 ? -50.068 6.332   -63.747  1.00 302.25 ? 275  LYS D O   1 
ATOM   10866 C  CB  . LYS D  3 277 ? -50.559 3.068   -63.523  1.00 292.53 ? 275  LYS D CB  1 
ATOM   10867 C  CG  . LYS D  3 277 ? -51.951 3.645   -63.327  1.00 290.97 ? 275  LYS D CG  1 
ATOM   10868 C  CD  . LYS D  3 277 ? -52.633 3.918   -64.655  1.00 295.33 ? 275  LYS D CD  1 
ATOM   10869 C  CE  . LYS D  3 277 ? -54.067 4.378   -64.451  1.00 293.35 ? 275  LYS D CE  1 
ATOM   10870 N  NZ  . LYS D  3 277 ? -54.139 5.608   -63.617  1.00 288.18 ? 275  LYS D NZ  1 
ATOM   10871 N  N   . ASP D  3 278 ? -48.747 5.311   -62.240  1.00 287.00 ? 276  ASP D N   1 
ATOM   10872 C  CA  . ASP D  3 278 ? -48.692 6.451   -61.340  1.00 279.09 ? 276  ASP D CA  1 
ATOM   10873 C  C   . ASP D  3 278 ? -47.399 7.253   -61.454  1.00 275.41 ? 276  ASP D C   1 
ATOM   10874 O  O   . ASP D  3 278 ? -47.268 8.285   -60.790  1.00 276.88 ? 276  ASP D O   1 
ATOM   10875 C  CB  . ASP D  3 278 ? -48.891 5.982   -59.892  1.00 269.39 ? 276  ASP D CB  1 
ATOM   10876 C  CG  . ASP D  3 278 ? -50.219 5.254   -59.680  1.00 266.88 ? 276  ASP D CG  1 
ATOM   10877 O  OD1 . ASP D  3 278 ? -51.209 5.584   -60.368  1.00 271.51 ? 276  ASP D OD1 1 
ATOM   10878 O  OD2 . ASP D  3 278 ? -50.277 4.353   -58.817  1.00 265.82 ? 276  ASP D OD2 1 
ATOM   10879 N  N   . LEU D  3 279 ? -46.443 6.823   -62.277  1.00 267.95 ? 277  LEU D N   1 
ATOM   10880 C  CA  . LEU D  3 279 ? -45.179 7.546   -62.389  1.00 269.18 ? 277  LEU D CA  1 
ATOM   10881 C  C   . LEU D  3 279 ? -44.785 7.756   -63.845  1.00 270.96 ? 277  LEU D C   1 
ATOM   10882 O  O   . LEU D  3 279 ? -44.198 8.786   -64.193  1.00 271.45 ? 277  LEU D O   1 
ATOM   10883 C  CB  . LEU D  3 279 ? -44.061 6.802   -61.658  1.00 269.52 ? 277  LEU D CB  1 
ATOM   10884 C  CG  . LEU D  3 279 ? -44.073 6.879   -60.129  1.00 274.85 ? 277  LEU D CG  1 
ATOM   10885 C  CD1 . LEU D  3 279 ? -42.930 6.061   -59.544  1.00 272.62 ? 277  LEU D CD1 1 
ATOM   10886 C  CD2 . LEU D  3 279 ? -43.995 8.327   -59.670  1.00 276.49 ? 277  LEU D CD2 1 
ATOM   10887 N  N   . GLY D  3 280 ? -45.106 6.785   -64.694  1.00 270.25 ? 278  GLY D N   1 
ATOM   10888 C  CA  . GLY D  3 280 ? -44.717 6.849   -66.092  1.00 271.71 ? 278  GLY D CA  1 
ATOM   10889 C  C   . GLY D  3 280 ? -43.236 6.635   -66.309  1.00 269.77 ? 278  GLY D C   1 
ATOM   10890 O  O   . GLY D  3 280 ? -42.637 7.302   -67.163  1.00 270.10 ? 278  GLY D O   1 
ATOM   10891 N  N   . TRP D  3 281 ? -42.628 5.724   -65.552  1.00 271.28 ? 279  TRP D N   1 
ATOM   10892 C  CA  . TRP D  3 281 ? -41.193 5.464   -65.614  1.00 268.70 ? 279  TRP D CA  1 
ATOM   10893 C  C   . TRP D  3 281 ? -40.974 4.065   -66.177  1.00 258.58 ? 279  TRP D C   1 
ATOM   10894 O  O   . TRP D  3 281 ? -41.234 3.065   -65.498  1.00 257.63 ? 279  TRP D O   1 
ATOM   10895 C  CB  . TRP D  3 281 ? -40.551 5.614   -64.236  1.00 273.39 ? 279  TRP D CB  1 
ATOM   10896 C  CG  . TRP D  3 281 ? -40.495 7.035   -63.750  1.00 275.88 ? 279  TRP D CG  1 
ATOM   10897 C  CD1 . TRP D  3 281 ? -40.961 8.142   -64.401  1.00 273.23 ? 279  TRP D CD1 1 
ATOM   10898 C  CD2 . TRP D  3 281 ? -39.939 7.504   -62.514  1.00 273.06 ? 279  TRP D CD2 1 
ATOM   10899 N  NE1 . TRP D  3 281 ? -40.732 9.268   -63.648  1.00 268.46 ? 279  TRP D NE1 1 
ATOM   10900 C  CE2 . TRP D  3 281 ? -40.106 8.904   -62.485  1.00 270.92 ? 279  TRP D CE2 1 
ATOM   10901 C  CE3 . TRP D  3 281 ? -39.317 6.876   -61.428  1.00 264.66 ? 279  TRP D CE3 1 
ATOM   10902 C  CZ2 . TRP D  3 281 ? -39.674 9.686   -61.414  1.00 267.64 ? 279  TRP D CZ2 1 
ATOM   10903 C  CZ3 . TRP D  3 281 ? -38.889 7.656   -60.366  1.00 260.07 ? 279  TRP D CZ3 1 
ATOM   10904 C  CH2 . TRP D  3 281 ? -39.069 9.045   -60.368  1.00 261.45 ? 279  TRP D CH2 1 
ATOM   10905 N  N   . LYS D  3 282 ? -40.494 3.997   -67.415  1.00 252.63 ? 280  LYS D N   1 
ATOM   10906 C  CA  . LYS D  3 282 ? -40.223 2.734   -68.082  1.00 253.43 ? 280  LYS D CA  1 
ATOM   10907 C  C   . LYS D  3 282 ? -38.752 2.344   -68.010  1.00 259.45 ? 280  LYS D C   1 
ATOM   10908 O  O   . LYS D  3 282 ? -38.336 1.394   -68.680  1.00 268.94 ? 280  LYS D O   1 
ATOM   10909 C  CB  . LYS D  3 282 ? -40.690 2.804   -69.539  1.00 260.67 ? 280  LYS D CB  1 
ATOM   10910 C  CG  . LYS D  3 282 ? -41.095 1.464   -70.140  1.00 261.52 ? 280  LYS D CG  1 
ATOM   10911 C  CD  . LYS D  3 282 ? -41.735 1.648   -71.507  1.00 262.05 ? 280  LYS D CD  1 
ATOM   10912 C  CE  . LYS D  3 282 ? -40.816 2.409   -72.449  1.00 260.99 ? 280  LYS D CE  1 
ATOM   10913 N  NZ  . LYS D  3 282 ? -41.423 2.575   -73.799  1.00 265.94 ? 280  LYS D NZ  1 
ATOM   10914 N  N   . TRP D  3 283 ? -37.956 3.053   -67.212  1.00 256.08 ? 281  TRP D N   1 
ATOM   10915 C  CA  . TRP D  3 283 ? -36.536 2.763   -67.061  1.00 261.54 ? 281  TRP D CA  1 
ATOM   10916 C  C   . TRP D  3 283 ? -36.248 1.794   -65.923  1.00 266.66 ? 281  TRP D C   1 
ATOM   10917 O  O   . TRP D  3 283 ? -35.084 1.435   -65.711  1.00 264.05 ? 281  TRP D O   1 
ATOM   10918 C  CB  . TRP D  3 283 ? -35.757 4.062   -66.835  1.00 262.20 ? 281  TRP D CB  1 
ATOM   10919 C  CG  . TRP D  3 283 ? -36.131 4.748   -65.562  1.00 267.86 ? 281  TRP D CG  1 
ATOM   10920 C  CD1 . TRP D  3 283 ? -37.243 5.505   -65.338  1.00 268.72 ? 281  TRP D CD1 1 
ATOM   10921 C  CD2 . TRP D  3 283 ? -35.399 4.733   -64.330  1.00 269.22 ? 281  TRP D CD2 1 
ATOM   10922 N  NE1 . TRP D  3 283 ? -37.249 5.965   -64.043  1.00 270.35 ? 281  TRP D NE1 1 
ATOM   10923 C  CE2 . TRP D  3 283 ? -36.127 5.507   -63.404  1.00 268.98 ? 281  TRP D CE2 1 
ATOM   10924 C  CE3 . TRP D  3 283 ? -34.199 4.141   -63.920  1.00 265.45 ? 281  TRP D CE3 1 
ATOM   10925 C  CZ2 . TRP D  3 283 ? -35.693 5.708   -62.094  1.00 265.80 ? 281  TRP D CZ2 1 
ATOM   10926 C  CZ3 . TRP D  3 283 ? -33.771 4.341   -62.620  1.00 262.75 ? 281  TRP D CZ3 1 
ATOM   10927 C  CH2 . TRP D  3 283 ? -34.517 5.117   -61.723  1.00 262.48 ? 281  TRP D CH2 1 
ATOM   10928 N  N   . ILE D  3 284 ? -37.270 1.368   -65.185  1.00 273.59 ? 282  ILE D N   1 
ATOM   10929 C  CA  . ILE D  3 284 ? -37.123 0.421   -64.085  1.00 264.59 ? 282  ILE D CA  1 
ATOM   10930 C  C   . ILE D  3 284 ? -37.816 -0.869  -64.493  1.00 268.26 ? 282  ILE D C   1 
ATOM   10931 O  O   . ILE D  3 284 ? -39.044 -0.907  -64.641  1.00 274.36 ? 282  ILE D O   1 
ATOM   10932 C  CB  . ILE D  3 284 ? -37.705 0.966   -62.777  1.00 256.19 ? 282  ILE D CB  1 
ATOM   10933 C  CG1 . ILE D  3 284 ? -36.946 2.217   -62.334  1.00 261.33 ? 282  ILE D CG1 1 
ATOM   10934 C  CG2 . ILE D  3 284 ? -37.665 -0.105  -61.698  1.00 247.31 ? 282  ILE D CG2 1 
ATOM   10935 C  CD1 . ILE D  3 284 ? -37.481 2.831   -61.060  1.00 265.67 ? 282  ILE D CD1 1 
ATOM   10936 N  N   . HIS D  3 285 ? -37.035 -1.937  -64.658  1.00 271.83 ? 283  HIS D N   1 
ATOM   10937 C  CA  . HIS D  3 285 ? -37.593 -3.204  -65.114  1.00 270.37 ? 283  HIS D CA  1 
ATOM   10938 C  C   . HIS D  3 285 ? -38.270 -3.961  -63.977  1.00 263.15 ? 283  HIS D C   1 
ATOM   10939 O  O   . HIS D  3 285 ? -39.436 -4.358  -64.091  1.00 259.75 ? 283  HIS D O   1 
ATOM   10940 C  CB  . HIS D  3 285 ? -36.492 -4.057  -65.741  1.00 268.19 ? 283  HIS D CB  1 
ATOM   10941 C  CG  . HIS D  3 285 ? -35.899 -3.466  -66.981  1.00 268.45 ? 283  HIS D CG  1 
ATOM   10942 N  ND1 . HIS D  3 285 ? -36.071 -4.028  -68.228  1.00 282.15 ? 283  HIS D ND1 1 
ATOM   10943 C  CD2 . HIS D  3 285 ? -35.137 -2.363  -67.167  1.00 267.88 ? 283  HIS D CD2 1 
ATOM   10944 C  CE1 . HIS D  3 285 ? -35.439 -3.297  -69.129  1.00 287.18 ? 283  HIS D CE1 1 
ATOM   10945 N  NE2 . HIS D  3 285 ? -34.864 -2.280  -68.511  1.00 280.51 ? 283  HIS D NE2 1 
ATOM   10946 N  N   . GLU D  3 286 ? -37.551 -4.182  -62.881  1.00 251.62 ? 284  GLU D N   1 
ATOM   10947 C  CA  . GLU D  3 286 ? -38.086 -4.917  -61.742  1.00 246.08 ? 284  GLU D CA  1 
ATOM   10948 C  C   . GLU D  3 286 ? -37.822 -4.171  -60.436  1.00 244.20 ? 284  GLU D C   1 
ATOM   10949 O  O   . GLU D  3 286 ? -36.721 -3.669  -60.217  1.00 248.98 ? 284  GLU D O   1 
ATOM   10950 C  CB  . GLU D  3 286 ? -37.481 -6.322  -61.677  1.00 244.01 ? 284  GLU D CB  1 
ATOM   10951 C  CG  . GLU D  3 286 ? -37.792 -7.195  -62.884  1.00 243.94 ? 284  GLU D CG  1 
ATOM   10952 C  CD  . GLU D  3 286 ? -39.260 -7.568  -62.976  1.00 237.20 ? 284  GLU D CD  1 
ATOM   10953 O  OE1 . GLU D  3 286 ? -39.945 -7.562  -61.933  1.00 236.24 ? 284  GLU D OE1 1 
ATOM   10954 O  OE2 . GLU D  3 286 ? -39.728 -7.867  -64.095  1.00 238.55 ? 284  GLU D OE2 1 
ATOM   10955 N  N   . PRO D  3 287 ? -38.836 -4.096  -59.562  1.00 244.10 ? 285  PRO D N   1 
ATOM   10956 C  CA  . PRO D  3 287 ? -40.178 -4.645  -59.782  1.00 251.38 ? 285  PRO D CA  1 
ATOM   10957 C  C   . PRO D  3 287 ? -41.065 -3.714  -60.604  1.00 259.16 ? 285  PRO D C   1 
ATOM   10958 O  O   . PRO D  3 287 ? -40.618 -2.639  -61.007  1.00 257.58 ? 285  PRO D O   1 
ATOM   10959 C  CB  . PRO D  3 287 ? -40.720 -4.799  -58.363  1.00 246.47 ? 285  PRO D CB  1 
ATOM   10960 C  CG  . PRO D  3 287 ? -40.072 -3.688  -57.614  1.00 243.49 ? 285  PRO D CG  1 
ATOM   10961 C  CD  . PRO D  3 287 ? -38.695 -3.519  -58.214  1.00 244.03 ? 285  PRO D CD  1 
ATOM   10962 N  N   . LYS D  3 288 ? -42.310 -4.130  -60.843  1.00 263.78 ? 286  LYS D N   1 
ATOM   10963 C  CA  . LYS D  3 288 ? -43.273 -3.360  -61.621  1.00 257.22 ? 286  LYS D CA  1 
ATOM   10964 C  C   . LYS D  3 288 ? -44.438 -2.870  -60.764  1.00 251.84 ? 286  LYS D C   1 
ATOM   10965 O  O   . LYS D  3 288 ? -45.540 -2.644  -61.272  1.00 243.06 ? 286  LYS D O   1 
ATOM   10966 C  CB  . LYS D  3 288 ? -43.785 -4.188  -62.798  1.00 250.61 ? 286  LYS D CB  1 
ATOM   10967 C  CG  . LYS D  3 288 ? -42.685 -4.672  -63.727  1.00 240.73 ? 286  LYS D CG  1 
ATOM   10968 C  CD  . LYS D  3 288 ? -43.217 -5.650  -64.755  1.00 240.92 ? 286  LYS D CD  1 
ATOM   10969 C  CE  . LYS D  3 288 ? -42.094 -6.178  -65.633  1.00 240.28 ? 286  LYS D CE  1 
ATOM   10970 N  NZ  . LYS D  3 288 ? -42.569 -7.186  -66.622  1.00 248.53 ? 286  LYS D NZ  1 
ATOM   10971 N  N   . GLY D  3 289 ? -44.207 -2.706  -59.462  1.00 261.78 ? 287  GLY D N   1 
ATOM   10972 C  CA  . GLY D  3 289 ? -45.236 -2.224  -58.562  1.00 264.94 ? 287  GLY D CA  1 
ATOM   10973 C  C   . GLY D  3 289 ? -45.091 -2.728  -57.142  1.00 267.05 ? 287  GLY D C   1 
ATOM   10974 O  O   . GLY D  3 289 ? -44.680 -3.871  -56.918  1.00 269.36 ? 287  GLY D O   1 
ATOM   10975 N  N   . TYR D  3 290 ? -45.426 -1.883  -56.170  1.00 265.57 ? 288  TYR D N   1 
ATOM   10976 C  CA  . TYR D  3 290 ? -45.390 -2.282  -54.772  1.00 266.42 ? 288  TYR D CA  1 
ATOM   10977 C  C   . TYR D  3 290 ? -46.379 -1.428  -53.995  1.00 259.83 ? 288  TYR D C   1 
ATOM   10978 O  O   . TYR D  3 290 ? -46.929 -0.451  -54.508  1.00 260.97 ? 288  TYR D O   1 
ATOM   10979 C  CB  . TYR D  3 290 ? -43.981 -2.162  -54.190  1.00 269.42 ? 288  TYR D CB  1 
ATOM   10980 C  CG  . TYR D  3 290 ? -43.580 -0.750  -53.839  1.00 275.89 ? 288  TYR D CG  1 
ATOM   10981 C  CD1 . TYR D  3 290 ? -43.369 0.202   -54.827  1.00 277.28 ? 288  TYR D CD1 1 
ATOM   10982 C  CD2 . TYR D  3 290 ? -43.400 -0.373  -52.515  1.00 285.44 ? 288  TYR D CD2 1 
ATOM   10983 C  CE1 . TYR D  3 290 ? -42.995 1.494   -54.503  1.00 281.15 ? 288  TYR D CE1 1 
ATOM   10984 C  CE2 . TYR D  3 290 ? -43.024 0.913   -52.182  1.00 285.26 ? 288  TYR D CE2 1 
ATOM   10985 C  CZ  . TYR D  3 290 ? -42.824 1.843   -53.177  1.00 281.88 ? 288  TYR D CZ  1 
ATOM   10986 O  OH  . TYR D  3 290 ? -42.451 3.124   -52.838  1.00 281.49 ? 288  TYR D OH  1 
ATOM   10987 N  N   . HIS D  3 291 ? -46.591 -1.803  -52.736  1.00 263.59 ? 289  HIS D N   1 
ATOM   10988 C  CA  . HIS D  3 291 ? -47.612 -1.187  -51.888  1.00 270.34 ? 289  HIS D CA  1 
ATOM   10989 C  C   . HIS D  3 291 ? -46.949 -0.183  -50.945  1.00 268.93 ? 289  HIS D C   1 
ATOM   10990 O  O   . HIS D  3 291 ? -46.530 -0.524  -49.838  1.00 261.92 ? 289  HIS D O   1 
ATOM   10991 C  CB  . HIS D  3 291 ? -48.379 -2.257  -51.118  1.00 271.81 ? 289  HIS D CB  1 
ATOM   10992 C  CG  . HIS D  3 291 ? -49.244 -3.120  -51.982  1.00 277.79 ? 289  HIS D CG  1 
ATOM   10993 N  ND1 . HIS D  3 291 ? -50.580 -2.856  -52.194  1.00 287.97 ? 289  HIS D ND1 1 
ATOM   10994 C  CD2 . HIS D  3 291 ? -48.966 -4.243  -52.686  1.00 273.07 ? 289  HIS D CD2 1 
ATOM   10995 C  CE1 . HIS D  3 291 ? -51.088 -3.778  -52.992  1.00 287.40 ? 289  HIS D CE1 1 
ATOM   10996 N  NE2 . HIS D  3 291 ? -50.130 -4.631  -53.305  1.00 279.81 ? 289  HIS D NE2 1 
ATOM   10997 N  N   . ALA D  3 292 ? -46.875 1.075   -51.382  1.00 271.74 ? 290  ALA D N   1 
ATOM   10998 C  CA  . ALA D  3 292 ? -46.338 2.159   -50.556  1.00 268.62 ? 290  ALA D CA  1 
ATOM   10999 C  C   . ALA D  3 292 ? -47.498 2.842   -49.842  1.00 272.15 ? 290  ALA D C   1 
ATOM   11000 O  O   . ALA D  3 292 ? -48.160 3.728   -50.386  1.00 280.76 ? 290  ALA D O   1 
ATOM   11001 C  CB  . ALA D  3 292 ? -45.547 3.145   -51.405  1.00 274.91 ? 290  ALA D CB  1 
ATOM   11002 N  N   . ASN D  3 293 ? -47.741 2.438   -48.598  1.00 260.43 ? 291  ASN D N   1 
ATOM   11003 C  CA  . ASN D  3 293 ? -48.875 2.946   -47.837  1.00 260.28 ? 291  ASN D CA  1 
ATOM   11004 C  C   . ASN D  3 293 ? -48.557 4.334   -47.280  1.00 252.51 ? 291  ASN D C   1 
ATOM   11005 O  O   . ASN D  3 293 ? -47.544 4.954   -47.617  1.00 246.18 ? 291  ASN D O   1 
ATOM   11006 C  CB  . ASN D  3 293 ? -49.249 1.966   -46.730  1.00 263.47 ? 291  ASN D CB  1 
ATOM   11007 C  CG  . ASN D  3 293 ? -49.763 0.647   -47.271  1.00 268.48 ? 291  ASN D CG  1 
ATOM   11008 O  OD1 . ASN D  3 293 ? -50.126 0.543   -48.442  1.00 270.93 ? 291  ASN D OD1 1 
ATOM   11009 N  ND2 . ASN D  3 293 ? -49.805 -0.368  -46.417  1.00 273.48 ? 291  ASN D ND2 1 
ATOM   11010 N  N   . PHE D  3 294 ? -49.434 4.840   -46.415  1.00 250.57 ? 292  PHE D N   1 
ATOM   11011 C  CA  . PHE D  3 294 ? -49.244 6.152   -45.811  1.00 251.89 ? 292  PHE D CA  1 
ATOM   11012 C  C   . PHE D  3 294 ? -50.016 6.203   -44.498  1.00 252.06 ? 292  PHE D C   1 
ATOM   11013 O  O   . PHE D  3 294 ? -50.853 5.344   -44.212  1.00 244.53 ? 292  PHE D O   1 
ATOM   11014 C  CB  . PHE D  3 294 ? -49.689 7.271   -46.758  1.00 258.90 ? 292  PHE D CB  1 
ATOM   11015 C  CG  . PHE D  3 294 ? -51.151 7.233   -47.101  1.00 265.31 ? 292  PHE D CG  1 
ATOM   11016 C  CD1 . PHE D  3 294 ? -51.614 6.432   -48.131  1.00 272.94 ? 292  PHE D CD1 1 
ATOM   11017 C  CD2 . PHE D  3 294 ? -52.062 8.006   -46.399  1.00 263.82 ? 292  PHE D CD2 1 
ATOM   11018 C  CE1 . PHE D  3 294 ? -52.957 6.396   -48.450  1.00 277.80 ? 292  PHE D CE1 1 
ATOM   11019 C  CE2 . PHE D  3 294 ? -53.407 7.975   -46.712  1.00 269.14 ? 292  PHE D CE2 1 
ATOM   11020 C  CZ  . PHE D  3 294 ? -53.855 7.169   -47.740  1.00 276.37 ? 292  PHE D CZ  1 
ATOM   11021 N  N   . CYS D  3 295 ? -49.723 7.230   -43.703  1.00 256.80 ? 293  CYS D N   1 
ATOM   11022 C  CA  . CYS D  3 295 ? -50.347 7.429   -42.399  1.00 244.97 ? 293  CYS D CA  1 
ATOM   11023 C  C   . CYS D  3 295 ? -51.283 8.629   -42.466  1.00 242.60 ? 293  CYS D C   1 
ATOM   11024 O  O   . CYS D  3 295 ? -50.851 9.743   -42.783  1.00 240.00 ? 293  CYS D O   1 
ATOM   11025 C  CB  . CYS D  3 295 ? -49.295 7.637   -41.311  1.00 238.34 ? 293  CYS D CB  1 
ATOM   11026 S  SG  . CYS D  3 295 ? -48.089 6.300   -41.139  1.00 238.63 ? 293  CYS D SG  1 
ATOM   11027 N  N   . LEU D  3 296 ? -52.557 8.405   -42.155  1.00 236.43 ? 294  LEU D N   1 
ATOM   11028 C  CA  . LEU D  3 296 ? -53.563 9.458   -42.180  1.00 243.40 ? 294  LEU D CA  1 
ATOM   11029 C  C   . LEU D  3 296 ? -54.384 9.394   -40.902  1.00 241.58 ? 294  LEU D C   1 
ATOM   11030 O  O   . LEU D  3 296 ? -54.935 8.342   -40.565  1.00 243.47 ? 294  LEU D O   1 
ATOM   11031 C  CB  . LEU D  3 296 ? -54.471 9.327   -43.409  1.00 250.59 ? 294  LEU D CB  1 
ATOM   11032 C  CG  . LEU D  3 296 ? -55.234 10.572  -43.875  1.00 255.13 ? 294  LEU D CG  1 
ATOM   11033 C  CD1 . LEU D  3 296 ? -56.494 10.819  -43.054  1.00 250.83 ? 294  LEU D CD1 1 
ATOM   11034 C  CD2 . LEU D  3 296 ? -54.321 11.788  -43.837  1.00 256.54 ? 294  LEU D CD2 1 
ATOM   11035 N  N   . GLY D  3 297 ? -54.470 10.521  -40.203  1.00 235.75 ? 295  GLY D N   1 
ATOM   11036 C  CA  . GLY D  3 297 ? -55.221 10.595  -38.976  1.00 229.25 ? 295  GLY D CA  1 
ATOM   11037 C  C   . GLY D  3 297 ? -54.632 11.599  -38.008  1.00 225.21 ? 295  GLY D C   1 
ATOM   11038 O  O   . GLY D  3 297 ? -53.425 11.863  -38.008  1.00 231.21 ? 295  GLY D O   1 
ATOM   11039 N  N   . PRO D  3 298 ? -55.477 12.187  -37.169  1.00 210.74 ? 296  PRO D N   1 
ATOM   11040 C  CA  . PRO D  3 298 ? -54.996 13.141  -36.171  1.00 206.47 ? 296  PRO D CA  1 
ATOM   11041 C  C   . PRO D  3 298 ? -54.576 12.453  -34.879  1.00 207.75 ? 296  PRO D C   1 
ATOM   11042 O  O   . PRO D  3 298 ? -54.980 11.328  -34.573  1.00 207.14 ? 296  PRO D O   1 
ATOM   11043 C  CB  . PRO D  3 298 ? -56.222 14.033  -35.940  1.00 215.85 ? 296  PRO D CB  1 
ATOM   11044 C  CG  . PRO D  3 298 ? -57.366 13.089  -36.105  1.00 224.48 ? 296  PRO D CG  1 
ATOM   11045 C  CD  . PRO D  3 298 ? -56.946 12.085  -37.164  1.00 222.31 ? 296  PRO D CD  1 
ATOM   11046 N  N   . CYS D  3 299 ? -53.738 13.166  -34.124  1.00 226.79 ? 297  CYS D N   1 
ATOM   11047 C  CA  . CYS D  3 299 ? -53.248 12.715  -32.819  1.00 230.36 ? 297  CYS D CA  1 
ATOM   11048 C  C   . CYS D  3 299 ? -53.272 13.900  -31.861  1.00 226.06 ? 297  CYS D C   1 
ATOM   11049 O  O   . CYS D  3 299 ? -52.262 14.587  -31.671  1.00 231.70 ? 297  CYS D O   1 
ATOM   11050 C  CB  . CYS D  3 299 ? -51.825 12.145  -32.911  1.00 239.00 ? 297  CYS D CB  1 
ATOM   11051 S  SG  . CYS D  3 299 ? -51.440 10.823  -34.123  1.00 238.61 ? 297  CYS D SG  1 
ATOM   11052 N  N   . PRO D  3 300 ? -54.418 14.179  -31.241  1.00 213.91 ? 298  PRO D N   1 
ATOM   11053 C  CA  . PRO D  3 300 ? -54.470 15.294  -30.285  1.00 213.29 ? 298  PRO D CA  1 
ATOM   11054 C  C   . PRO D  3 300 ? -54.399 14.830  -28.838  1.00 196.97 ? 298  PRO D C   1 
ATOM   11055 O  O   . PRO D  3 300 ? -54.308 13.627  -28.570  1.00 195.50 ? 298  PRO D O   1 
ATOM   11056 C  CB  . PRO D  3 300 ? -55.818 15.952  -30.603  1.00 227.02 ? 298  PRO D CB  1 
ATOM   11057 C  CG  . PRO D  3 300 ? -56.654 14.842  -31.257  1.00 227.96 ? 298  PRO D CG  1 
ATOM   11058 C  CD  . PRO D  3 300 ? -55.760 13.647  -31.513  1.00 217.88 ? 298  PRO D CD  1 
ATOM   11059 N  N   . TYR D  3 301 ? -54.433 15.774  -27.897  1.00 198.63 ? 299  TYR D N   1 
ATOM   11060 C  CA  . TYR D  3 301 ? -54.390 15.415  -26.486  1.00 196.87 ? 299  TYR D CA  1 
ATOM   11061 C  C   . TYR D  3 301 ? -55.017 16.522  -25.652  1.00 200.78 ? 299  TYR D C   1 
ATOM   11062 O  O   . TYR D  3 301 ? -55.177 17.659  -26.106  1.00 199.42 ? 299  TYR D O   1 
ATOM   11063 C  CB  . TYR D  3 301 ? -52.956 15.125  -26.020  1.00 195.99 ? 299  TYR D CB  1 
ATOM   11064 C  CG  . TYR D  3 301 ? -52.082 16.336  -25.746  1.00 207.13 ? 299  TYR D CG  1 
ATOM   11065 C  CD1 . TYR D  3 301 ? -52.106 17.457  -26.571  1.00 206.77 ? 299  TYR D CD1 1 
ATOM   11066 C  CD2 . TYR D  3 301 ? -51.213 16.344  -24.662  1.00 212.76 ? 299  TYR D CD2 1 
ATOM   11067 C  CE1 . TYR D  3 301 ? -51.299 18.550  -26.311  1.00 210.00 ? 299  TYR D CE1 1 
ATOM   11068 C  CE2 . TYR D  3 301 ? -50.403 17.431  -24.397  1.00 207.05 ? 299  TYR D CE2 1 
ATOM   11069 C  CZ  . TYR D  3 301 ? -50.449 18.529  -25.223  1.00 205.84 ? 299  TYR D CZ  1 
ATOM   11070 O  OH  . TYR D  3 301 ? -49.642 19.609  -24.956  1.00 204.28 ? 299  TYR D OH  1 
ATOM   11071 N  N   . ILE D  3 302 ? -55.361 16.161  -24.413  1.00 219.04 ? 300  ILE D N   1 
ATOM   11072 C  CA  . ILE D  3 302 ? -56.005 17.048  -23.448  1.00 231.62 ? 300  ILE D CA  1 
ATOM   11073 C  C   . ILE D  3 302 ? -57.216 17.715  -24.093  1.00 241.54 ? 300  ILE D C   1 
ATOM   11074 O  O   . ILE D  3 302 ? -57.292 18.945  -24.189  1.00 232.01 ? 300  ILE D O   1 
ATOM   11075 C  CB  . ILE D  3 302 ? -55.012 18.085  -22.889  1.00 222.21 ? 300  ILE D CB  1 
ATOM   11076 C  CG1 . ILE D  3 302 ? -53.725 17.391  -22.456  1.00 207.29 ? 300  ILE D CG1 1 
ATOM   11077 C  CG2 . ILE D  3 302 ? -55.594 18.787  -21.670  1.00 237.37 ? 300  ILE D CG2 1 
ATOM   11078 C  CD1 . ILE D  3 302 ? -53.943 16.345  -21.384  1.00 202.11 ? 300  ILE D CD1 1 
ATOM   11079 N  N   . TRP D  3 303 ? -58.162 16.902  -24.552  1.00 259.85 ? 301  TRP D N   1 
ATOM   11080 C  CA  . TRP D  3 303 ? -59.413 17.393  -25.107  1.00 257.02 ? 301  TRP D CA  1 
ATOM   11081 C  C   . TRP D  3 303 ? -60.521 17.245  -24.070  1.00 253.76 ? 301  TRP D C   1 
ATOM   11082 O  O   . TRP D  3 303 ? -60.437 16.410  -23.165  1.00 254.77 ? 301  TRP D O   1 
ATOM   11083 C  CB  . TRP D  3 303 ? -59.776 16.642  -26.392  1.00 256.47 ? 301  TRP D CB  1 
ATOM   11084 C  CG  . TRP D  3 303 ? -60.480 17.511  -27.387  1.00 278.21 ? 301  TRP D CG  1 
ATOM   11085 C  CD1 . TRP D  3 303 ? -61.795 17.450  -27.749  1.00 285.51 ? 301  TRP D CD1 1 
ATOM   11086 C  CD2 . TRP D  3 303 ? -59.908 18.592  -28.132  1.00 279.59 ? 301  TRP D CD2 1 
ATOM   11087 N  NE1 . TRP D  3 303 ? -62.074 18.420  -28.682  1.00 282.91 ? 301  TRP D NE1 1 
ATOM   11088 C  CE2 . TRP D  3 303 ? -60.933 19.136  -28.933  1.00 278.27 ? 301  TRP D CE2 1 
ATOM   11089 C  CE3 . TRP D  3 303 ? -58.627 19.150  -28.203  1.00 271.08 ? 301  TRP D CE3 1 
ATOM   11090 C  CZ2 . TRP D  3 303 ? -60.717 20.210  -29.793  1.00 272.68 ? 301  TRP D CZ2 1 
ATOM   11091 C  CZ3 . TRP D  3 303 ? -58.415 20.215  -29.057  1.00 274.46 ? 301  TRP D CZ3 1 
ATOM   11092 C  CH2 . TRP D  3 303 ? -59.455 20.735  -29.841  1.00 275.46 ? 301  TRP D CH2 1 
ATOM   11093 N  N   . SER D  3 304 ? -61.558 18.073  -24.206  1.00 250.53 ? 302  SER D N   1 
ATOM   11094 C  CA  . SER D  3 304 ? -62.618 18.130  -23.206  1.00 251.51 ? 302  SER D CA  1 
ATOM   11095 C  C   . SER D  3 304 ? -63.269 16.764  -23.015  1.00 251.12 ? 302  SER D C   1 
ATOM   11096 O  O   . SER D  3 304 ? -63.322 15.939  -23.933  1.00 250.92 ? 302  SER D O   1 
ATOM   11097 C  CB  . SER D  3 304 ? -63.677 19.160  -23.605  1.00 256.37 ? 302  SER D CB  1 
ATOM   11098 O  OG  . SER D  3 304 ? -64.174 18.906  -24.906  1.00 256.68 ? 302  SER D OG  1 
ATOM   11099 N  N   . LEU D  3 305 ? -63.757 16.535  -21.795  1.00 249.46 ? 303  LEU D N   1 
ATOM   11100 C  CA  . LEU D  3 305 ? -64.412 15.288  -21.390  1.00 242.72 ? 303  LEU D CA  1 
ATOM   11101 C  C   . LEU D  3 305 ? -63.425 14.124  -21.374  1.00 223.60 ? 303  LEU D C   1 
ATOM   11102 O  O   . LEU D  3 305 ? -63.142 13.521  -22.406  1.00 224.52 ? 303  LEU D O   1 
ATOM   11103 C  CB  . LEU D  3 305 ? -65.606 14.972  -22.306  1.00 255.79 ? 303  LEU D CB  1 
ATOM   11104 C  CG  . LEU D  3 305 ? -66.698 16.044  -22.426  1.00 250.87 ? 303  LEU D CG  1 
ATOM   11105 C  CD1 . LEU D  3 305 ? -67.654 15.740  -23.575  1.00 233.10 ? 303  LEU D CD1 1 
ATOM   11106 C  CD2 . LEU D  3 305 ? -67.465 16.180  -21.119  1.00 244.30 ? 303  LEU D CD2 1 
ATOM   11107 N  N   . VAL D  3 312 ? -61.810 11.273  -20.128  1.00 227.84 ? 310  VAL D N   1 
ATOM   11108 C  CA  . VAL D  3 312 ? -61.373 10.944  -18.778  1.00 217.25 ? 310  VAL D CA  1 
ATOM   11109 C  C   . VAL D  3 312 ? -59.938 10.434  -18.796  1.00 208.20 ? 310  VAL D C   1 
ATOM   11110 O  O   . VAL D  3 312 ? -59.567 9.586   -17.987  1.00 201.18 ? 310  VAL D O   1 
ATOM   11111 C  CB  . VAL D  3 312 ? -62.310 9.914   -18.131  1.00 210.21 ? 310  VAL D CB  1 
ATOM   11112 C  CG1 . VAL D  3 312 ? -63.702 10.506  -17.963  1.00 211.73 ? 310  VAL D CG1 1 
ATOM   11113 C  CG2 . VAL D  3 312 ? -62.361 8.640   -18.968  1.00 204.27 ? 310  VAL D CG2 1 
ATOM   11114 N  N   . LEU D  3 313 ? -59.145 10.964  -19.730  1.00 222.16 ? 311  LEU D N   1 
ATOM   11115 C  CA  . LEU D  3 313 ? -57.750 10.580  -19.963  1.00 228.96 ? 311  LEU D CA  1 
ATOM   11116 C  C   . LEU D  3 313 ? -57.584 9.073   -20.161  1.00 228.69 ? 311  LEU D C   1 
ATOM   11117 O  O   . LEU D  3 313 ? -56.484 8.533   -19.988  1.00 219.79 ? 311  LEU D O   1 
ATOM   11118 C  CB  . LEU D  3 313 ? -56.826 11.090  -18.840  1.00 228.40 ? 311  LEU D CB  1 
ATOM   11119 C  CG  . LEU D  3 313 ? -56.583 10.339  -17.523  1.00 207.18 ? 311  LEU D CG  1 
ATOM   11120 C  CD1 . LEU D  3 313 ? -55.109 9.975   -17.371  1.00 194.62 ? 311  LEU D CD1 1 
ATOM   11121 C  CD2 . LEU D  3 313 ? -57.057 11.167  -16.344  1.00 197.40 ? 311  LEU D CD2 1 
ATOM   11122 N  N   . ALA D  3 314 ? -58.657 8.386   -20.563  1.00 225.19 ? 312  ALA D N   1 
ATOM   11123 C  CA  . ALA D  3 314 ? -58.620 6.932   -20.676  1.00 224.12 ? 312  ALA D CA  1 
ATOM   11124 C  C   . ALA D  3 314 ? -57.810 6.486   -21.894  1.00 230.58 ? 312  ALA D C   1 
ATOM   11125 O  O   . ALA D  3 314 ? -56.782 5.812   -21.758  1.00 214.60 ? 312  ALA D O   1 
ATOM   11126 C  CB  . ALA D  3 314 ? -60.048 6.383   -20.729  1.00 215.73 ? 312  ALA D CB  1 
ATOM   11127 N  N   . LEU D  3 315 ? -58.260 6.853   -23.099  1.00 247.71 ? 313  LEU D N   1 
ATOM   11128 C  CA  . LEU D  3 315 ? -57.596 6.458   -24.345  1.00 233.36 ? 313  LEU D CA  1 
ATOM   11129 C  C   . LEU D  3 315 ? -56.308 7.259   -24.505  1.00 227.96 ? 313  LEU D C   1 
ATOM   11130 O  O   . LEU D  3 315 ? -56.246 8.280   -25.192  1.00 231.64 ? 313  LEU D O   1 
ATOM   11131 C  CB  . LEU D  3 315 ? -58.512 6.667   -25.543  1.00 229.66 ? 313  LEU D CB  1 
ATOM   11132 C  CG  . LEU D  3 315 ? -59.764 5.793   -25.610  1.00 234.74 ? 313  LEU D CG  1 
ATOM   11133 C  CD1 . LEU D  3 315 ? -60.608 6.147   -26.825  1.00 240.67 ? 313  LEU D CD1 1 
ATOM   11134 C  CD2 . LEU D  3 315 ? -59.384 4.319   -25.621  1.00 227.32 ? 313  LEU D CD2 1 
ATOM   11135 N  N   . TYR D  3 316 ? -55.252 6.775   -23.853  1.00 217.28 ? 314  TYR D N   1 
ATOM   11136 C  CA  . TYR D  3 316 ? -53.950 7.418   -23.889  1.00 215.36 ? 314  TYR D CA  1 
ATOM   11137 C  C   . TYR D  3 316 ? -52.883 6.564   -24.557  1.00 208.39 ? 314  TYR D C   1 
ATOM   11138 O  O   . TYR D  3 316 ? -51.777 7.062   -24.798  1.00 206.38 ? 314  TYR D O   1 
ATOM   11139 C  CB  . TYR D  3 316 ? -53.499 7.772   -22.462  1.00 222.76 ? 314  TYR D CB  1 
ATOM   11140 C  CG  . TYR D  3 316 ? -52.788 9.104   -22.342  1.00 222.15 ? 314  TYR D CG  1 
ATOM   11141 C  CD1 . TYR D  3 316 ? -51.408 9.192   -22.483  1.00 215.64 ? 314  TYR D CD1 1 
ATOM   11142 C  CD2 . TYR D  3 316 ? -53.495 10.272  -22.077  1.00 214.61 ? 314  TYR D CD2 1 
ATOM   11143 C  CE1 . TYR D  3 316 ? -50.751 10.405  -22.372  1.00 199.22 ? 314  TYR D CE1 1 
ATOM   11144 C  CE2 . TYR D  3 316 ? -52.846 11.492  -21.964  1.00 204.14 ? 314  TYR D CE2 1 
ATOM   11145 C  CZ  . TYR D  3 316 ? -51.473 11.552  -22.113  1.00 191.64 ? 314  TYR D CZ  1 
ATOM   11146 O  OH  . TYR D  3 316 ? -50.817 12.757  -22.003  1.00 187.28 ? 314  TYR D OH  1 
ATOM   11147 N  N   . ASN D  3 317 ? -53.184 5.306   -24.872  1.00 200.39 ? 315  ASN D N   1 
ATOM   11148 C  CA  . ASN D  3 317 ? -52.195 4.402   -25.440  1.00 201.79 ? 315  ASN D CA  1 
ATOM   11149 C  C   . ASN D  3 317 ? -52.037 4.562   -26.947  1.00 213.27 ? 315  ASN D C   1 
ATOM   11150 O  O   . ASN D  3 317 ? -50.995 4.177   -27.490  1.00 209.15 ? 315  ASN D O   1 
ATOM   11151 C  CB  . ASN D  3 317 ? -52.572 2.960   -25.099  1.00 207.97 ? 315  ASN D CB  1 
ATOM   11152 C  CG  . ASN D  3 317 ? -54.073 2.746   -25.069  1.00 223.33 ? 315  ASN D CG  1 
ATOM   11153 O  OD1 . ASN D  3 317 ? -54.833 3.511   -25.662  1.00 235.96 ? 315  ASN D OD1 1 
ATOM   11154 N  ND2 . ASN D  3 317 ? -54.508 1.704   -24.369  1.00 224.92 ? 315  ASN D ND2 1 
ATOM   11155 N  N   . GLN D  3 318 ? -53.036 5.113   -27.635  1.00 228.54 ? 316  GLN D N   1 
ATOM   11156 C  CA  . GLN D  3 318 ? -52.940 5.379   -29.064  1.00 220.89 ? 316  GLN D CA  1 
ATOM   11157 C  C   . GLN D  3 318 ? -52.911 6.857   -29.406  1.00 217.35 ? 316  GLN D C   1 
ATOM   11158 O  O   . GLN D  3 318 ? -52.296 7.232   -30.406  1.00 211.90 ? 316  GLN D O   1 
ATOM   11159 C  CB  . GLN D  3 318 ? -54.113 4.732   -29.813  1.00 222.52 ? 316  GLN D CB  1 
ATOM   11160 C  CG  . GLN D  3 318 ? -54.114 3.218   -29.802  1.00 227.59 ? 316  GLN D CG  1 
ATOM   11161 C  CD  . GLN D  3 318 ? -55.123 2.640   -30.775  1.00 240.85 ? 316  GLN D CD  1 
ATOM   11162 O  OE1 . GLN D  3 318 ? -55.390 1.438   -30.770  1.00 249.16 ? 316  GLN D OE1 1 
ATOM   11163 N  NE2 . GLN D  3 318 ? -55.688 3.496   -31.620  1.00 243.12 ? 316  GLN D NE2 1 
ATOM   11164 N  N   . HIS D  3 319 ? -53.558 7.700   -28.597  1.00 231.19 ? 317  HIS D N   1 
ATOM   11165 C  CA  . HIS D  3 319 ? -53.634 9.125   -28.905  1.00 236.42 ? 317  HIS D CA  1 
ATOM   11166 C  C   . HIS D  3 319 ? -52.279 9.803   -28.732  1.00 227.67 ? 317  HIS D C   1 
ATOM   11167 O  O   . HIS D  3 319 ? -51.840 10.565  -29.601  1.00 226.36 ? 317  HIS D O   1 
ATOM   11168 C  CB  . HIS D  3 319 ? -54.690 9.795   -28.021  1.00 243.05 ? 317  HIS D CB  1 
ATOM   11169 C  CG  . HIS D  3 319 ? -56.089 9.325   -28.281  1.00 251.55 ? 317  HIS D CG  1 
ATOM   11170 N  ND1 . HIS D  3 319 ? -56.382 8.274   -29.123  1.00 258.42 ? 317  HIS D ND1 1 
ATOM   11171 C  CD2 . HIS D  3 319 ? -57.277 9.769   -27.808  1.00 251.81 ? 317  HIS D CD2 1 
ATOM   11172 C  CE1 . HIS D  3 319 ? -57.690 8.090   -29.158  1.00 256.14 ? 317  HIS D CE1 1 
ATOM   11173 N  NE2 . HIS D  3 319 ? -58.256 8.984   -28.368  1.00 253.03 ? 317  HIS D NE2 1 
ATOM   11174 N  N   . ASN D  3 320 ? -51.600 9.540   -27.614  1.00 224.70 ? 318  ASN D N   1 
ATOM   11175 C  CA  . ASN D  3 320 ? -50.303 10.152  -27.346  1.00 222.04 ? 318  ASN D CA  1 
ATOM   11176 C  C   . ASN D  3 320 ? -49.489 9.288   -26.385  1.00 212.83 ? 318  ASN D C   1 
ATOM   11177 O  O   . ASN D  3 320 ? -49.390 9.612   -25.194  1.00 208.10 ? 318  ASN D O   1 
ATOM   11178 C  CB  . ASN D  3 320 ? -50.493 11.563  -26.779  1.00 222.81 ? 318  ASN D CB  1 
ATOM   11179 C  CG  . ASN D  3 320 ? -49.186 12.332  -26.649  1.00 211.36 ? 318  ASN D CG  1 
ATOM   11180 O  OD1 . ASN D  3 320 ? -48.183 11.991  -27.274  1.00 207.26 ? 318  ASN D OD1 1 
ATOM   11181 N  ND2 . ASN D  3 320 ? -49.200 13.387  -25.840  1.00 210.55 ? 318  ASN D ND2 1 
ATOM   11182 N  N   . PRO D  3 321 ? -48.898 8.182   -26.853  1.00 220.35 ? 319  PRO D N   1 
ATOM   11183 C  CA  . PRO D  3 321 ? -48.061 7.359   -25.967  1.00 218.18 ? 319  PRO D CA  1 
ATOM   11184 C  C   . PRO D  3 321 ? -46.656 7.900   -25.771  1.00 217.35 ? 319  PRO D C   1 
ATOM   11185 O  O   . PRO D  3 321 ? -45.958 7.443   -24.854  1.00 225.94 ? 319  PRO D O   1 
ATOM   11186 C  CB  . PRO D  3 321 ? -48.036 6.003   -26.685  1.00 220.07 ? 319  PRO D CB  1 
ATOM   11187 C  CG  . PRO D  3 321 ? -48.135 6.365   -28.123  1.00 229.46 ? 319  PRO D CG  1 
ATOM   11188 C  CD  . PRO D  3 321 ? -49.041 7.576   -28.189  1.00 230.11 ? 319  PRO D CD  1 
ATOM   11189 N  N   . GLY D  3 322 ? -46.216 8.848   -26.602  1.00 198.80 ? 320  GLY D N   1 
ATOM   11190 C  CA  . GLY D  3 322 ? -44.953 9.530   -26.404  1.00 194.81 ? 320  GLY D CA  1 
ATOM   11191 C  C   . GLY D  3 322 ? -45.000 10.751  -25.507  1.00 203.48 ? 320  GLY D C   1 
ATOM   11192 O  O   . GLY D  3 322 ? -43.942 11.234  -25.089  1.00 200.02 ? 320  GLY D O   1 
ATOM   11193 N  N   . ALA D  3 323 ? -46.197 11.256  -25.195  1.00 198.73 ? 321  ALA D N   1 
ATOM   11194 C  CA  . ALA D  3 323 ? -46.372 12.445  -24.354  1.00 186.18 ? 321  ALA D CA  1 
ATOM   11195 C  C   . ALA D  3 323 ? -45.644 13.658  -24.929  1.00 187.50 ? 321  ALA D C   1 
ATOM   11196 O  O   . ALA D  3 323 ? -45.143 14.511  -24.194  1.00 191.50 ? 321  ALA D O   1 
ATOM   11197 C  CB  . ALA D  3 323 ? -45.923 12.184  -22.915  1.00 183.44 ? 321  ALA D CB  1 
ATOM   11198 N  N   . SER D  3 324 ? -45.602 13.749  -26.250  1.00 184.60 ? 322  SER D N   1 
ATOM   11199 C  CA  . SER D  3 324 ? -44.908 14.848  -26.893  1.00 195.10 ? 322  SER D CA  1 
ATOM   11200 C  C   . SER D  3 324 ? -45.811 16.074  -26.960  1.00 197.45 ? 322  SER D C   1 
ATOM   11201 O  O   . SER D  3 324 ? -47.034 15.989  -26.804  1.00 189.78 ? 322  SER D O   1 
ATOM   11202 C  CB  . SER D  3 324 ? -44.449 14.444  -28.292  1.00 207.18 ? 322  SER D CB  1 
ATOM   11203 O  OG  . SER D  3 324 ? -43.558 15.401  -28.832  1.00 218.13 ? 322  SER D OG  1 
ATOM   11204 N  N   . ALA D  3 325 ? -45.185 17.230  -27.189  1.00 205.67 ? 323  ALA D N   1 
ATOM   11205 C  CA  . ALA D  3 325 ? -45.936 18.479  -27.252  1.00 195.29 ? 323  ALA D CA  1 
ATOM   11206 C  C   . ALA D  3 325 ? -46.865 18.523  -28.452  1.00 194.21 ? 323  ALA D C   1 
ATOM   11207 O  O   . ALA D  3 325 ? -47.889 19.208  -28.432  1.00 187.27 ? 323  ALA D O   1 
ATOM   11208 C  CB  . ALA D  3 325 ? -44.972 19.665  -27.288  1.00 194.63 ? 323  ALA D CB  1 
ATOM   11209 N  N   . ALA D  3 326 ? -46.517 17.791  -29.526  1.00 206.60 ? 324  ALA D N   1 
ATOM   11210 C  CA  . ALA D  3 326 ? -47.341 17.737  -30.726  1.00 204.49 ? 324  ALA D CA  1 
ATOM   11211 C  C   . ALA D  3 326 ? -47.212 16.340  -31.309  1.00 198.95 ? 324  ALA D C   1 
ATOM   11212 O  O   . ALA D  3 326 ? -46.259 16.048  -32.049  1.00 198.49 ? 324  ALA D O   1 
ATOM   11213 C  CB  . ALA D  3 326 ? -46.933 18.795  -31.749  1.00 210.44 ? 324  ALA D CB  1 
ATOM   11214 N  N   . PRO D  3 327 ? -48.139 15.439  -30.987  1.00 196.44 ? 325  PRO D N   1 
ATOM   11215 C  CA  . PRO D  3 327 ? -48.072 14.078  -31.535  1.00 205.40 ? 325  PRO D CA  1 
ATOM   11216 C  C   . PRO D  3 327 ? -48.441 14.067  -33.011  1.00 214.82 ? 325  PRO D C   1 
ATOM   11217 O  O   . PRO D  3 327 ? -49.434 14.674  -33.421  1.00 232.21 ? 325  PRO D O   1 
ATOM   11218 C  CB  . PRO D  3 327 ? -49.097 13.306  -30.691  1.00 205.45 ? 325  PRO D CB  1 
ATOM   11219 C  CG  . PRO D  3 327 ? -49.324 14.154  -29.480  1.00 195.82 ? 325  PRO D CG  1 
ATOM   11220 C  CD  . PRO D  3 327 ? -49.184 15.562  -29.961  1.00 196.56 ? 325  PRO D CD  1 
ATOM   11221 N  N   . CYS D  3 328 ? -47.634 13.373  -33.806  1.00 203.24 ? 326  CYS D N   1 
ATOM   11222 C  CA  . CYS D  3 328 ? -47.862 13.237  -35.235  1.00 206.48 ? 326  CYS D CA  1 
ATOM   11223 C  C   . CYS D  3 328 ? -48.067 11.774  -35.604  1.00 210.71 ? 326  CYS D C   1 
ATOM   11224 O  O   . CYS D  3 328 ? -47.466 10.878  -35.008  1.00 217.75 ? 326  CYS D O   1 
ATOM   11225 C  CB  . CYS D  3 328 ? -46.689 13.788  -36.044  1.00 205.74 ? 326  CYS D CB  1 
ATOM   11226 S  SG  . CYS D  3 328 ? -46.359 15.540  -35.848  1.00 220.05 ? 326  CYS D SG  1 
ATOM   11227 N  N   . CYS D  3 329 ? -48.900 11.548  -36.622  1.00 219.55 ? 327  CYS D N   1 
ATOM   11228 C  CA  . CYS D  3 329 ? -49.193 10.207  -37.132  1.00 231.70 ? 327  CYS D CA  1 
ATOM   11229 C  C   . CYS D  3 329 ? -48.060 9.808   -38.078  1.00 233.22 ? 327  CYS D C   1 
ATOM   11230 O  O   . CYS D  3 329 ? -48.131 9.969   -39.298  1.00 243.08 ? 327  CYS D O   1 
ATOM   11231 C  CB  . CYS D  3 329 ? -50.562 10.198  -37.807  1.00 237.18 ? 327  CYS D CB  1 
ATOM   11232 S  SG  . CYS D  3 329 ? -51.243 8.624   -38.439  1.00 249.09 ? 327  CYS D SG  1 
ATOM   11233 N  N   . VAL D  3 330 ? -46.986 9.287   -37.487  1.00 220.83 ? 328  VAL D N   1 
ATOM   11234 C  CA  . VAL D  3 330 ? -45.758 8.970   -38.218  1.00 221.94 ? 328  VAL D CA  1 
ATOM   11235 C  C   . VAL D  3 330 ? -45.547 7.460   -38.290  1.00 220.27 ? 328  VAL D C   1 
ATOM   11236 O  O   . VAL D  3 330 ? -46.010 6.727   -37.404  1.00 219.32 ? 328  VAL D O   1 
ATOM   11237 C  CB  . VAL D  3 330 ? -44.544 9.654   -37.569  1.00 229.76 ? 328  VAL D CB  1 
ATOM   11238 C  CG1 . VAL D  3 330 ? -44.703 11.164  -37.617  1.00 231.01 ? 328  VAL D CG1 1 
ATOM   11239 C  CG2 . VAL D  3 330 ? -44.379 9.175   -36.135  1.00 228.25 ? 328  VAL D CG2 1 
ATOM   11240 N  N   . PRO D  3 331 ? -44.853 6.953   -39.311  1.00 207.74 ? 329  PRO D N   1 
ATOM   11241 C  CA  . PRO D  3 331 ? -44.586 5.513   -39.373  1.00 209.97 ? 329  PRO D CA  1 
ATOM   11242 C  C   . PRO D  3 331 ? -43.564 5.094   -38.333  1.00 205.02 ? 329  PRO D C   1 
ATOM   11243 O  O   . PRO D  3 331 ? -42.580 5.793   -38.080  1.00 202.93 ? 329  PRO D O   1 
ATOM   11244 C  CB  . PRO D  3 331 ? -44.040 5.315   -40.792  1.00 212.82 ? 329  PRO D CB  1 
ATOM   11245 C  CG  . PRO D  3 331 ? -43.418 6.622   -41.122  1.00 208.91 ? 329  PRO D CG  1 
ATOM   11246 C  CD  . PRO D  3 331 ? -44.310 7.658   -40.486  1.00 209.70 ? 329  PRO D CD  1 
ATOM   11247 N  N   . GLN D  3 332 ? -43.806 3.933   -37.730  1.00 221.87 ? 330  GLN D N   1 
ATOM   11248 C  CA  . GLN D  3 332 ? -42.888 3.368   -36.751  1.00 224.57 ? 330  GLN D CA  1 
ATOM   11249 C  C   . GLN D  3 332 ? -41.974 2.309   -37.345  1.00 231.85 ? 330  GLN D C   1 
ATOM   11250 O  O   . GLN D  3 332 ? -40.773 2.304   -37.060  1.00 243.04 ? 330  GLN D O   1 
ATOM   11251 C  CB  . GLN D  3 332 ? -43.669 2.765   -35.580  1.00 217.57 ? 330  GLN D CB  1 
ATOM   11252 C  CG  . GLN D  3 332 ? -42.787 2.236   -34.468  1.00 215.23 ? 330  GLN D CG  1 
ATOM   11253 C  CD  . GLN D  3 332 ? -43.583 1.765   -33.273  1.00 227.05 ? 330  GLN D CD  1 
ATOM   11254 O  OE1 . GLN D  3 332 ? -44.811 1.694   -33.320  1.00 235.82 ? 330  GLN D OE1 1 
ATOM   11255 N  NE2 . GLN D  3 332 ? -42.888 1.444   -32.187  1.00 226.83 ? 330  GLN D NE2 1 
ATOM   11256 N  N   . ALA D  3 333 ? -42.513 1.417   -38.171  1.00 220.17 ? 331  ALA D N   1 
ATOM   11257 C  CA  . ALA D  3 333 ? -41.751 0.335   -38.776  1.00 221.01 ? 331  ALA D CA  1 
ATOM   11258 C  C   . ALA D  3 333 ? -41.790 0.482   -40.289  1.00 233.24 ? 331  ALA D C   1 
ATOM   11259 O  O   . ALA D  3 333 ? -42.865 0.658   -40.872  1.00 242.73 ? 331  ALA D O   1 
ATOM   11260 C  CB  . ALA D  3 333 ? -42.305 -1.029  -38.358  1.00 216.93 ? 331  ALA D CB  1 
ATOM   11261 N  N   . LEU D  3 334 ? -40.618 0.412   -40.918  1.00 233.53 ? 332  LEU D N   1 
ATOM   11262 C  CA  . LEU D  3 334 ? -40.492 0.525   -42.363  1.00 230.32 ? 332  LEU D CA  1 
ATOM   11263 C  C   . LEU D  3 334 ? -39.668 -0.640  -42.898  1.00 229.75 ? 332  LEU D C   1 
ATOM   11264 O  O   . LEU D  3 334 ? -38.896 -1.268  -42.170  1.00 226.51 ? 332  LEU D O   1 
ATOM   11265 C  CB  . LEU D  3 334 ? -39.856 1.864   -42.771  1.00 225.45 ? 332  LEU D CB  1 
ATOM   11266 C  CG  . LEU D  3 334 ? -40.684 3.142   -42.572  1.00 220.01 ? 332  LEU D CG  1 
ATOM   11267 C  CD1 . LEU D  3 334 ? -40.638 3.647   -41.134  1.00 214.15 ? 332  LEU D CD1 1 
ATOM   11268 C  CD2 . LEU D  3 334 ? -40.232 4.228   -43.535  1.00 229.30 ? 332  LEU D CD2 1 
ATOM   11269 N  N   . GLU D  3 335 ? -39.842 -0.924  -44.191  1.00 239.80 ? 333  GLU D N   1 
ATOM   11270 C  CA  . GLU D  3 335 ? -39.190 -2.057  -44.832  1.00 246.57 ? 333  GLU D CA  1 
ATOM   11271 C  C   . GLU D  3 335 ? -38.468 -1.619  -46.100  1.00 238.52 ? 333  GLU D C   1 
ATOM   11272 O  O   . GLU D  3 335 ? -38.999 -0.815  -46.877  1.00 239.23 ? 333  GLU D O   1 
ATOM   11273 C  CB  . GLU D  3 335 ? -40.212 -3.156  -45.167  1.00 250.88 ? 333  GLU D CB  1 
ATOM   11274 C  CG  . GLU D  3 335 ? -40.904 -3.744  -43.942  1.00 259.81 ? 333  GLU D CG  1 
ATOM   11275 C  CD  . GLU D  3 335 ? -41.853 -4.877  -44.285  1.00 265.62 ? 333  GLU D CD  1 
ATOM   11276 O  OE1 . GLU D  3 335 ? -41.862 -5.312  -45.455  1.00 264.91 ? 333  GLU D OE1 1 
ATOM   11277 O  OE2 . GLU D  3 335 ? -42.591 -5.334  -43.385  1.00 271.02 ? 333  GLU D OE2 1 
ATOM   11278 N  N   . PRO D  3 336 ? -37.262 -2.131  -46.337  1.00 230.57 ? 334  PRO D N   1 
ATOM   11279 C  CA  . PRO D  3 336 ? -36.505 -1.735  -47.529  1.00 232.30 ? 334  PRO D CA  1 
ATOM   11280 C  C   . PRO D  3 336 ? -37.088 -2.364  -48.785  1.00 241.65 ? 334  PRO D C   1 
ATOM   11281 O  O   . PRO D  3 336 ? -37.924 -3.269  -48.739  1.00 244.75 ? 334  PRO D O   1 
ATOM   11282 C  CB  . PRO D  3 336 ? -35.097 -2.259  -47.241  1.00 235.88 ? 334  PRO D CB  1 
ATOM   11283 C  CG  . PRO D  3 336 ? -35.323 -3.442  -46.360  1.00 236.25 ? 334  PRO D CG  1 
ATOM   11284 C  CD  . PRO D  3 336 ? -36.528 -3.108  -45.514  1.00 236.46 ? 334  PRO D CD  1 
ATOM   11285 N  N   . LEU D  3 337 ? -36.622 -1.866  -49.929  1.00 247.31 ? 335  LEU D N   1 
ATOM   11286 C  CA  . LEU D  3 337 ? -37.121 -2.304  -51.229  1.00 245.10 ? 335  LEU D CA  1 
ATOM   11287 C  C   . LEU D  3 337 ? -35.956 -2.528  -52.184  1.00 238.81 ? 335  LEU D C   1 
ATOM   11288 O  O   . LEU D  3 337 ? -35.195 -1.578  -52.464  1.00 238.99 ? 335  LEU D O   1 
ATOM   11289 C  CB  . LEU D  3 337 ? -38.098 -1.280  -51.808  1.00 247.55 ? 335  LEU D CB  1 
ATOM   11290 C  CG  . LEU D  3 337 ? -38.577 -1.606  -53.223  1.00 253.12 ? 335  LEU D CG  1 
ATOM   11291 C  CD1 . LEU D  3 337 ? -39.341 -2.922  -53.234  1.00 255.35 ? 335  LEU D CD1 1 
ATOM   11292 C  CD2 . LEU D  3 337 ? -39.428 -0.480  -53.784  1.00 257.93 ? 335  LEU D CD2 1 
ATOM   11293 N  N   . PRO D  3 338 ? -35.772 -3.740  -52.704  1.00 227.73 ? 336  PRO D N   1 
ATOM   11294 C  CA  . PRO D  3 338 ? -34.755 -3.957  -53.740  1.00 233.16 ? 336  PRO D CA  1 
ATOM   11295 C  C   . PRO D  3 338 ? -35.269 -3.562  -55.119  1.00 245.66 ? 336  PRO D C   1 
ATOM   11296 O  O   . PRO D  3 338 ? -36.443 -3.753  -55.446  1.00 254.92 ? 336  PRO D O   1 
ATOM   11297 C  CB  . PRO D  3 338 ? -34.489 -5.464  -53.653  1.00 233.16 ? 336  PRO D CB  1 
ATOM   11298 C  CG  . PRO D  3 338 ? -35.779 -6.038  -53.149  1.00 225.18 ? 336  PRO D CG  1 
ATOM   11299 C  CD  . PRO D  3 338 ? -36.375 -5.000  -52.235  1.00 220.38 ? 336  PRO D CD  1 
ATOM   11300 N  N   . ILE D  3 339 ? -34.369 -3.003  -55.936  1.00 243.86 ? 337  ILE D N   1 
ATOM   11301 C  CA  . ILE D  3 339 ? -34.712 -2.515  -57.267  1.00 243.39 ? 337  ILE D CA  1 
ATOM   11302 C  C   . ILE D  3 339 ? -33.690 -3.018  -58.282  1.00 257.23 ? 337  ILE D C   1 
ATOM   11303 O  O   . ILE D  3 339 ? -32.574 -3.411  -57.936  1.00 253.61 ? 337  ILE D O   1 
ATOM   11304 C  CB  . ILE D  3 339 ? -34.797 -0.974  -57.320  1.00 233.95 ? 337  ILE D CB  1 
ATOM   11305 C  CG1 . ILE D  3 339 ? -33.441 -0.353  -56.977  1.00 234.38 ? 337  ILE D CG1 1 
ATOM   11306 C  CG2 . ILE D  3 339 ? -35.871 -0.464  -56.372  1.00 233.40 ? 337  ILE D CG2 1 
ATOM   11307 C  CD1 . ILE D  3 339 ? -33.423 1.157   -57.067  1.00 235.11 ? 337  ILE D CD1 1 
ATOM   11308 N  N   . VAL D  3 340 ? -34.089 -2.992  -59.555  1.00 273.63 ? 338  VAL D N   1 
ATOM   11309 C  CA  . VAL D  3 340 ? -33.238 -3.409  -60.668  1.00 261.09 ? 338  VAL D CA  1 
ATOM   11310 C  C   . VAL D  3 340 ? -33.392 -2.395  -61.795  1.00 258.25 ? 338  VAL D C   1 
ATOM   11311 O  O   . VAL D  3 340 ? -34.493 -2.218  -62.329  1.00 250.94 ? 338  VAL D O   1 
ATOM   11312 C  CB  . VAL D  3 340 ? -33.583 -4.823  -61.170  1.00 253.39 ? 338  VAL D CB  1 
ATOM   11313 C  CG1 . VAL D  3 340 ? -32.803 -5.143  -62.437  1.00 252.68 ? 338  VAL D CG1 1 
ATOM   11314 C  CG2 . VAL D  3 340 ? -33.306 -5.861  -60.088  1.00 249.84 ? 338  VAL D CG2 1 
ATOM   11315 N  N   . TYR D  3 341 ? -32.295 -1.735  -62.164  1.00 261.32 ? 339  TYR D N   1 
ATOM   11316 C  CA  . TYR D  3 341 ? -32.312 -0.735  -63.223  1.00 274.78 ? 339  TYR D CA  1 
ATOM   11317 C  C   . TYR D  3 341 ? -31.039 -0.858  -64.050  1.00 292.79 ? 339  TYR D C   1 
ATOM   11318 O  O   . TYR D  3 341 ? -30.030 -1.405  -63.598  1.00 292.19 ? 339  TYR D O   1 
ATOM   11319 C  CB  . TYR D  3 341 ? -32.436 0.689   -62.663  1.00 269.46 ? 339  TYR D CB  1 
ATOM   11320 C  CG  . TYR D  3 341 ? -31.204 1.158   -61.917  1.00 268.94 ? 339  TYR D CG  1 
ATOM   11321 C  CD1 . TYR D  3 341 ? -30.948 0.732   -60.620  1.00 265.36 ? 339  TYR D CD1 1 
ATOM   11322 C  CD2 . TYR D  3 341 ? -30.296 2.030   -62.508  1.00 268.86 ? 339  TYR D CD2 1 
ATOM   11323 C  CE1 . TYR D  3 341 ? -29.826 1.156   -59.934  1.00 260.15 ? 339  TYR D CE1 1 
ATOM   11324 C  CE2 . TYR D  3 341 ? -29.171 2.461   -61.826  1.00 263.59 ? 339  TYR D CE2 1 
ATOM   11325 C  CZ  . TYR D  3 341 ? -28.940 2.020   -60.541  1.00 260.71 ? 339  TYR D CZ  1 
ATOM   11326 O  OH  . TYR D  3 341 ? -27.821 2.446   -59.861  1.00 263.35 ? 339  TYR D OH  1 
ATOM   11327 N  N   . TYR D  3 342 ? -31.092 -0.330  -65.269  1.00 300.56 ? 340  TYR D N   1 
ATOM   11328 C  CA  . TYR D  3 342 ? -29.963 -0.369  -66.186  1.00 294.03 ? 340  TYR D CA  1 
ATOM   11329 C  C   . TYR D  3 342 ? -29.348 1.017   -66.339  1.00 287.45 ? 340  TYR D C   1 
ATOM   11330 O  O   . TYR D  3 342 ? -30.023 2.040   -66.184  1.00 281.58 ? 340  TYR D O   1 
ATOM   11331 C  CB  . TYR D  3 342 ? -30.381 -0.890  -67.565  1.00 287.54 ? 340  TYR D CB  1 
ATOM   11332 C  CG  . TYR D  3 342 ? -30.482 -2.397  -67.687  1.00 278.18 ? 340  TYR D CG  1 
ATOM   11333 C  CD1 . TYR D  3 342 ? -29.362 -3.169  -67.972  1.00 265.91 ? 340  TYR D CD1 1 
ATOM   11334 C  CD2 . TYR D  3 342 ? -31.703 -3.045  -67.544  1.00 277.24 ? 340  TYR D CD2 1 
ATOM   11335 C  CE1 . TYR D  3 342 ? -29.453 -4.542  -68.097  1.00 261.58 ? 340  TYR D CE1 1 
ATOM   11336 C  CE2 . TYR D  3 342 ? -31.803 -4.418  -67.667  1.00 267.56 ? 340  TYR D CE2 1 
ATOM   11337 C  CZ  . TYR D  3 342 ? -30.676 -5.160  -67.943  1.00 261.83 ? 340  TYR D CZ  1 
ATOM   11338 O  OH  . TYR D  3 342 ? -30.771 -6.526  -68.067  1.00 262.66 ? 340  TYR D OH  1 
ATOM   11339 N  N   . VAL D  3 343 ? -28.052 1.037   -66.639  1.00 289.03 ? 341  VAL D N   1 
ATOM   11340 C  CA  . VAL D  3 343 ? -27.355 2.269   -66.985  1.00 288.30 ? 341  VAL D CA  1 
ATOM   11341 C  C   . VAL D  3 343 ? -26.484 2.026   -68.212  1.00 291.37 ? 341  VAL D C   1 
ATOM   11342 O  O   . VAL D  3 343 ? -26.237 0.880   -68.591  1.00 288.72 ? 341  VAL D O   1 
ATOM   11343 C  CB  . VAL D  3 343 ? -26.505 2.801   -65.818  1.00 282.26 ? 341  VAL D CB  1 
ATOM   11344 C  CG1 . VAL D  3 343 ? -25.727 4.028   -66.259  1.00 286.42 ? 341  VAL D CG1 1 
ATOM   11345 C  CG2 . VAL D  3 343 ? -27.380 3.137   -64.630  1.00 273.08 ? 341  VAL D CG2 1 
ATOM   11346 N  N   . ARG D  3 345 ? -24.281 0.025   -69.694  1.00 272.59 ? 343  ARG D N   1 
ATOM   11347 C  CA  . ARG D  3 345 ? -23.975 -1.355  -70.053  1.00 272.09 ? 343  ARG D CA  1 
ATOM   11348 C  C   . ARG D  3 345 ? -23.813 -2.221  -68.812  1.00 265.91 ? 343  ARG D C   1 
ATOM   11349 O  O   . ARG D  3 345 ? -23.617 -3.433  -68.907  1.00 262.85 ? 343  ARG D O   1 
ATOM   11350 C  CB  . ARG D  3 345 ? -22.706 -1.419  -70.909  1.00 282.67 ? 343  ARG D CB  1 
ATOM   11351 C  CG  . ARG D  3 345 ? -21.524 -0.634  -70.353  1.00 287.39 ? 343  ARG D CG  1 
ATOM   11352 C  CD  . ARG D  3 345 ? -20.355 -0.644  -71.332  1.00 298.19 ? 343  ARG D CD  1 
ATOM   11353 N  NE  . ARG D  3 345 ? -19.656 0.638   -71.370  1.00 299.29 ? 343  ARG D NE  1 
ATOM   11354 C  CZ  . ARG D  3 345 ? -18.492 0.880   -70.775  1.00 294.20 ? 343  ARG D CZ  1 
ATOM   11355 N  NH1 . ARG D  3 345 ? -17.878 -0.077  -70.092  1.00 289.21 ? 343  ARG D NH1 1 
ATOM   11356 N  NH2 . ARG D  3 345 ? -17.939 2.082   -70.869  1.00 295.69 ? 343  ARG D NH2 1 
ATOM   11357 N  N   . LYS D  3 346 ? -23.900 -1.590  -67.647  1.00 262.87 ? 344  LYS D N   1 
ATOM   11358 C  CA  . LYS D  3 346 ? -23.708 -2.284  -66.380  1.00 278.71 ? 344  LYS D CA  1 
ATOM   11359 C  C   . LYS D  3 346 ? -25.032 -2.371  -65.634  1.00 282.15 ? 344  LYS D C   1 
ATOM   11360 O  O   . LYS D  3 346 ? -25.533 -1.341  -65.155  1.00 273.45 ? 344  LYS D O   1 
ATOM   11361 C  CB  . LYS D  3 346 ? -22.658 -1.565  -65.528  1.00 273.29 ? 344  LYS D CB  1 
ATOM   11362 C  CG  . LYS D  3 346 ? -21.351 -1.258  -66.261  1.00 268.10 ? 344  LYS D CG  1 
ATOM   11363 C  CD  . LYS D  3 346 ? -20.347 -0.569  -65.344  1.00 256.37 ? 344  LYS D CD  1 
ATOM   11364 C  CE  . LYS D  3 346 ? -19.122 -0.079  -66.110  1.00 252.79 ? 344  LYS D CE  1 
ATOM   11365 N  NZ  . LYS D  3 346 ? -18.329 -1.182  -66.719  1.00 251.33 ? 344  LYS D NZ  1 
ATOM   11366 N  N   . PRO D  3 347 ? -25.643 -3.553  -65.516  1.00 294.23 ? 345  PRO D N   1 
ATOM   11367 C  CA  . PRO D  3 347 ? -26.863 -3.673  -64.704  1.00 288.18 ? 345  PRO D CA  1 
ATOM   11368 C  C   . PRO D  3 347 ? -26.519 -3.678  -63.219  1.00 279.83 ? 345  PRO D C   1 
ATOM   11369 O  O   . PRO D  3 347 ? -25.681 -4.461  -62.765  1.00 293.46 ? 345  PRO D O   1 
ATOM   11370 C  CB  . PRO D  3 347 ? -27.459 -5.014  -65.151  1.00 280.36 ? 345  PRO D CB  1 
ATOM   11371 C  CG  . PRO D  3 347 ? -26.283 -5.807  -65.617  1.00 279.50 ? 345  PRO D CG  1 
ATOM   11372 C  CD  . PRO D  3 347 ? -25.307 -4.813  -66.205  1.00 285.44 ? 345  PRO D CD  1 
ATOM   11373 N  N   . LYS D  3 348 ? -27.170 -2.799  -62.462  1.00 237.25 ? 346  LYS D N   1 
ATOM   11374 C  CA  . LYS D  3 348 ? -26.868 -2.612  -61.049  1.00 229.75 ? 346  LYS D CA  1 
ATOM   11375 C  C   . LYS D  3 348 ? -28.093 -2.951  -60.216  1.00 228.76 ? 346  LYS D C   1 
ATOM   11376 O  O   . LYS D  3 348 ? -29.169 -2.382  -60.425  1.00 232.60 ? 346  LYS D O   1 
ATOM   11377 C  CB  . LYS D  3 348 ? -26.403 -1.183  -60.773  1.00 230.71 ? 346  LYS D CB  1 
ATOM   11378 C  CG  . LYS D  3 348 ? -25.094 -0.836  -61.456  1.00 232.55 ? 346  LYS D CG  1 
ATOM   11379 C  CD  . LYS D  3 348 ? -24.579 0.523   -61.026  1.00 234.24 ? 346  LYS D CD  1 
ATOM   11380 C  CE  . LYS D  3 348 ? -23.253 0.836   -61.699  1.00 239.86 ? 346  LYS D CE  1 
ATOM   11381 N  NZ  . LYS D  3 348 ? -22.218 -0.198  -61.410  1.00 239.89 ? 346  LYS D NZ  1 
ATOM   11382 N  N   . VAL D  3 349 ? -27.922 -3.872  -59.274  1.00 236.13 ? 347  VAL D N   1 
ATOM   11383 C  CA  . VAL D  3 349 ? -28.972 -4.268  -58.346  1.00 241.72 ? 347  VAL D CA  1 
ATOM   11384 C  C   . VAL D  3 349 ? -28.729 -3.519  -57.040  1.00 235.33 ? 347  VAL D C   1 
ATOM   11385 O  O   . VAL D  3 349 ? -27.719 -3.743  -56.364  1.00 226.26 ? 347  VAL D O   1 
ATOM   11386 C  CB  . VAL D  3 349 ? -28.987 -5.787  -58.131  1.00 245.94 ? 347  VAL D CB  1 
ATOM   11387 C  CG1 . VAL D  3 349 ? -30.133 -6.185  -57.221  1.00 248.04 ? 347  VAL D CG1 1 
ATOM   11388 C  CG2 . VAL D  3 349 ? -29.085 -6.506  -59.467  1.00 245.95 ? 347  VAL D CG2 1 
ATOM   11389 N  N   . GLU D  3 350 ? -29.651 -2.629  -56.680  1.00 238.88 ? 348  GLU D N   1 
ATOM   11390 C  CA  . GLU D  3 350 ? -29.536 -1.811  -55.483  1.00 237.48 ? 348  GLU D CA  1 
ATOM   11391 C  C   . GLU D  3 350 ? -30.777 -1.977  -54.612  1.00 234.84 ? 348  GLU D C   1 
ATOM   11392 O  O   . GLU D  3 350 ? -31.829 -2.430  -55.070  1.00 243.32 ? 348  GLU D O   1 
ATOM   11393 C  CB  . GLU D  3 350 ? -29.338 -0.328  -55.834  1.00 239.81 ? 348  GLU D CB  1 
ATOM   11394 C  CG  . GLU D  3 350 ? -28.131 -0.049  -56.720  1.00 249.05 ? 348  GLU D CG  1 
ATOM   11395 C  CD  . GLU D  3 350 ? -27.804 1.430   -56.818  1.00 258.39 ? 348  GLU D CD  1 
ATOM   11396 O  OE1 . GLU D  3 350 ? -26.770 1.774   -57.428  1.00 271.90 ? 348  GLU D OE1 1 
ATOM   11397 O  OE2 . GLU D  3 350 ? -28.577 2.248   -56.279  1.00 252.54 ? 348  GLU D OE2 1 
ATOM   11398 N  N   . GLN D  3 351 ? -30.646 -1.602  -53.339  1.00 214.64 ? 349  GLN D N   1 
ATOM   11399 C  CA  . GLN D  3 351 ? -31.730 -1.731  -52.373  1.00 209.01 ? 349  GLN D CA  1 
ATOM   11400 C  C   . GLN D  3 351 ? -31.902 -0.411  -51.638  1.00 206.96 ? 349  GLN D C   1 
ATOM   11401 O  O   . GLN D  3 351 ? -30.941 0.110   -51.062  1.00 202.69 ? 349  GLN D O   1 
ATOM   11402 C  CB  . GLN D  3 351 ? -31.456 -2.869  -51.386  1.00 203.89 ? 349  GLN D CB  1 
ATOM   11403 C  CG  . GLN D  3 351 ? -32.591 -3.137  -50.411  1.00 204.11 ? 349  GLN D CG  1 
ATOM   11404 C  CD  . GLN D  3 351 ? -32.266 -4.242  -49.423  1.00 209.12 ? 349  GLN D CD  1 
ATOM   11405 O  OE1 . GLN D  3 351 ? -31.108 -4.622  -49.261  1.00 218.15 ? 349  GLN D OE1 1 
ATOM   11406 N  NE2 . GLN D  3 351 ? -33.290 -4.765  -48.759  1.00 206.48 ? 349  GLN D NE2 1 
ATOM   11407 N  N   . LEU D  3 352 ? -33.122 0.122   -51.660  1.00 216.04 ? 350  LEU D N   1 
ATOM   11408 C  CA  . LEU D  3 352 ? -33.427 1.380   -50.994  1.00 218.39 ? 350  LEU D CA  1 
ATOM   11409 C  C   . LEU D  3 352 ? -33.792 1.144   -49.535  1.00 216.79 ? 350  LEU D C   1 
ATOM   11410 O  O   . LEU D  3 352 ? -34.419 0.142   -49.181  1.00 210.04 ? 350  LEU D O   1 
ATOM   11411 C  CB  . LEU D  3 352 ? -34.584 2.093   -51.691  1.00 219.89 ? 350  LEU D CB  1 
ATOM   11412 C  CG  . LEU D  3 352 ? -34.359 2.484   -53.150  1.00 232.09 ? 350  LEU D CG  1 
ATOM   11413 C  CD1 . LEU D  3 352 ? -35.599 3.155   -53.712  1.00 244.33 ? 350  LEU D CD1 1 
ATOM   11414 C  CD2 . LEU D  3 352 ? -33.149 3.392   -53.278  1.00 233.06 ? 350  LEU D CD2 1 
ATOM   11415 N  N   . SER D  3 353 ? -33.409 2.092   -48.687  1.00 229.80 ? 351  SER D N   1 
ATOM   11416 C  CA  . SER D  3 353 ? -33.646 2.007   -47.254  1.00 228.08 ? 351  SER D CA  1 
ATOM   11417 C  C   . SER D  3 353 ? -34.892 2.802   -46.887  1.00 228.24 ? 351  SER D C   1 
ATOM   11418 O  O   . SER D  3 353 ? -35.037 3.959   -47.295  1.00 229.91 ? 351  SER D O   1 
ATOM   11419 C  CB  . SER D  3 353 ? -32.438 2.527   -46.475  1.00 228.49 ? 351  SER D CB  1 
ATOM   11420 O  OG  . SER D  3 353 ? -32.136 3.863   -46.838  1.00 225.10 ? 351  SER D OG  1 
ATOM   11421 N  N   . ASN D  3 354 ? -35.787 2.171   -46.123  1.00 234.17 ? 352  ASN D N   1 
ATOM   11422 C  CA  . ASN D  3 354 ? -36.998 2.808   -45.613  1.00 242.09 ? 352  ASN D CA  1 
ATOM   11423 C  C   . ASN D  3 354 ? -37.905 3.292   -46.742  1.00 243.85 ? 352  ASN D C   1 
ATOM   11424 O  O   . ASN D  3 354 ? -37.797 4.441   -47.184  1.00 251.79 ? 352  ASN D O   1 
ATOM   11425 C  CB  . ASN D  3 354 ? -36.640 3.974   -44.683  1.00 244.22 ? 352  ASN D CB  1 
ATOM   11426 C  CG  . ASN D  3 354 ? -35.893 3.525   -43.436  1.00 242.18 ? 352  ASN D CG  1 
ATOM   11427 O  OD1 . ASN D  3 354 ? -36.504 3.172   -42.426  1.00 240.86 ? 352  ASN D OD1 1 
ATOM   11428 N  ND2 . ASN D  3 354 ? -34.566 3.545   -43.498  1.00 241.61 ? 352  ASN D ND2 1 
ATOM   11429 N  N   . MET D  3 355 ? -38.810 2.428   -47.210  1.00 236.17 ? 353  MET D N   1 
ATOM   11430 C  CA  . MET D  3 355 ? -39.734 2.795   -48.280  1.00 236.00 ? 353  MET D CA  1 
ATOM   11431 C  C   . MET D  3 355 ? -41.160 2.354   -47.971  1.00 234.48 ? 353  MET D C   1 
ATOM   11432 O  O   . MET D  3 355 ? -42.106 3.137   -48.117  1.00 234.46 ? 353  MET D O   1 
ATOM   11433 C  CB  . MET D  3 355 ? -39.278 2.189   -49.610  1.00 243.66 ? 353  MET D CB  1 
ATOM   11434 C  CG  . MET D  3 355 ? -37.959 2.738   -50.130  1.00 244.00 ? 353  MET D CG  1 
ATOM   11435 S  SD  . MET D  3 355 ? -38.020 4.516   -50.429  1.00 248.28 ? 353  MET D SD  1 
ATOM   11436 C  CE  . MET D  3 355 ? -39.302 4.607   -51.677  1.00 237.95 ? 353  MET D CE  1 
ATOM   11437 N  N   . ILE D  3 356 ? -41.323 1.102   -47.553  1.00 233.35 ? 354  ILE D N   1 
ATOM   11438 C  CA  . ILE D  3 356 ? -42.636 0.522   -47.286  1.00 237.28 ? 354  ILE D CA  1 
ATOM   11439 C  C   . ILE D  3 356 ? -43.040 0.850   -45.855  1.00 243.96 ? 354  ILE D C   1 
ATOM   11440 O  O   . ILE D  3 356 ? -42.352 0.470   -44.901  1.00 248.17 ? 354  ILE D O   1 
ATOM   11441 C  CB  . ILE D  3 356 ? -42.633 -0.997  -47.516  1.00 242.33 ? 354  ILE D CB  1 
ATOM   11442 C  CG1 . ILE D  3 356 ? -42.445 -1.326  -48.998  1.00 257.17 ? 354  ILE D CG1 1 
ATOM   11443 C  CG2 . ILE D  3 356 ? -43.919 -1.622  -46.986  1.00 242.72 ? 354  ILE D CG2 1 
ATOM   11444 C  CD1 . ILE D  3 356 ? -40.999 -1.512  -49.409  1.00 263.02 ? 354  ILE D CD1 1 
ATOM   11445 N  N   . VAL D  3 357 ? -44.168 1.535   -45.704  1.00 246.72 ? 355  VAL D N   1 
ATOM   11446 C  CA  . VAL D  3 357 ? -44.684 1.916   -44.395  1.00 237.64 ? 355  VAL D CA  1 
ATOM   11447 C  C   . VAL D  3 357 ? -45.608 0.812   -43.898  1.00 237.13 ? 355  VAL D C   1 
ATOM   11448 O  O   . VAL D  3 357 ? -46.601 0.477   -44.553  1.00 246.29 ? 355  VAL D O   1 
ATOM   11449 C  CB  . VAL D  3 357 ? -45.416 3.263   -44.463  1.00 244.96 ? 355  VAL D CB  1 
ATOM   11450 C  CG1 . VAL D  3 357 ? -46.110 3.560   -43.143  1.00 246.91 ? 355  VAL D CG1 1 
ATOM   11451 C  CG2 . VAL D  3 357 ? -44.439 4.368   -44.829  1.00 247.95 ? 355  VAL D CG2 1 
ATOM   11452 N  N   . ARG D  3 358 ? -45.287 0.248   -42.737  1.00 235.82 ? 356  ARG D N   1 
ATOM   11453 C  CA  . ARG D  3 358 ? -46.081 -0.846  -42.165  1.00 238.14 ? 356  ARG D CA  1 
ATOM   11454 C  C   . ARG D  3 358 ? -47.104 -0.298  -41.174  1.00 233.64 ? 356  ARG D C   1 
ATOM   11455 O  O   . ARG D  3 358 ? -48.311 -0.320  -41.433  1.00 234.39 ? 356  ARG D O   1 
ATOM   11456 C  CB  . ARG D  3 358 ? -45.161 -1.871  -41.503  1.00 242.35 ? 356  ARG D CB  1 
ATOM   11457 C  CG  . ARG D  3 358 ? -45.885 -3.076  -40.940  1.00 244.96 ? 356  ARG D CG  1 
ATOM   11458 C  CD  . ARG D  3 358 ? -46.510 -3.902  -42.049  1.00 249.04 ? 356  ARG D CD  1 
ATOM   11459 N  NE  . ARG D  3 358 ? -45.506 -4.526  -42.905  1.00 240.77 ? 356  ARG D NE  1 
ATOM   11460 C  CZ  . ARG D  3 358 ? -45.789 -5.374  -43.889  1.00 240.48 ? 356  ARG D CZ  1 
ATOM   11461 N  NH1 . ARG D  3 358 ? -47.049 -5.700  -44.141  1.00 239.93 ? 356  ARG D NH1 1 
ATOM   11462 N  NH2 . ARG D  3 358 ? -44.815 -5.897  -44.620  1.00 242.50 ? 356  ARG D NH2 1 
ATOM   11463 N  N   . SER D  3 359 ? -46.630 0.196   -40.036  1.00 227.98 ? 357  SER D N   1 
ATOM   11464 C  CA  . SER D  3 359 ? -47.485 0.715   -38.981  1.00 226.50 ? 357  SER D CA  1 
ATOM   11465 C  C   . SER D  3 359 ? -47.337 2.228   -38.867  1.00 226.72 ? 357  SER D C   1 
ATOM   11466 O  O   . SER D  3 359 ? -46.453 2.842   -39.471  1.00 230.42 ? 357  SER D O   1 
ATOM   11467 C  CB  . SER D  3 359 ? -47.154 0.048   -37.643  1.00 232.49 ? 357  SER D CB  1 
ATOM   11468 O  OG  . SER D  3 359 ? -48.010 0.519   -36.619  1.00 236.90 ? 357  SER D OG  1 
ATOM   11469 N  N   . CYS D  3 360 ? -48.224 2.829   -38.074  1.00 227.61 ? 358  CYS D N   1 
ATOM   11470 C  CA  . CYS D  3 360 ? -48.195 4.261   -37.811  1.00 226.91 ? 358  CYS D CA  1 
ATOM   11471 C  C   . CYS D  3 360 ? -48.417 4.506   -36.325  1.00 232.08 ? 358  CYS D C   1 
ATOM   11472 O  O   . CYS D  3 360 ? -49.267 3.863   -35.704  1.00 236.94 ? 358  CYS D O   1 
ATOM   11473 C  CB  . CYS D  3 360 ? -49.258 5.004   -38.631  1.00 234.42 ? 358  CYS D CB  1 
ATOM   11474 S  SG  . CYS D  3 360 ? -49.166 4.731   -40.422  1.00 233.57 ? 358  CYS D SG  1 
ATOM   11475 N  N   . LYS D  3 361 ? -47.652 5.441   -35.762  1.00 239.16 ? 359  LYS D N   1 
ATOM   11476 C  CA  . LYS D  3 361 ? -47.728 5.785   -34.347  1.00 237.03 ? 359  LYS D CA  1 
ATOM   11477 C  C   . LYS D  3 361 ? -47.928 7.288   -34.188  1.00 227.35 ? 359  LYS D C   1 
ATOM   11478 O  O   . LYS D  3 361 ? -47.849 8.053   -35.152  1.00 227.27 ? 359  LYS D O   1 
ATOM   11479 C  CB  . LYS D  3 361 ? -46.462 5.355   -33.594  1.00 240.36 ? 359  LYS D CB  1 
ATOM   11480 C  CG  . LYS D  3 361 ? -45.189 6.035   -34.095  1.00 243.48 ? 359  LYS D CG  1 
ATOM   11481 C  CD  . LYS D  3 361 ? -43.968 5.643   -33.271  1.00 237.16 ? 359  LYS D CD  1 
ATOM   11482 C  CE  . LYS D  3 361 ? -42.698 6.300   -33.806  1.00 224.32 ? 359  LYS D CE  1 
ATOM   11483 N  NZ  . LYS D  3 361 ? -41.483 5.925   -33.023  1.00 221.71 ? 359  LYS D NZ  1 
ATOM   11484 N  N   . CYS D  3 362 ? -48.184 7.706   -32.945  1.00 213.03 ? 360  CYS D N   1 
ATOM   11485 C  CA  . CYS D  3 362 ? -48.235 9.118   -32.569  1.00 216.97 ? 360  CYS D CA  1 
ATOM   11486 C  C   . CYS D  3 362 ? -47.127 9.394   -31.558  1.00 217.59 ? 360  CYS D C   1 
ATOM   11487 O  O   . CYS D  3 362 ? -47.174 8.897   -30.427  1.00 218.29 ? 360  CYS D O   1 
ATOM   11488 C  CB  . CYS D  3 362 ? -49.597 9.501   -31.991  1.00 227.77 ? 360  CYS D CB  1 
ATOM   11489 S  SG  . CYS D  3 362 ? -51.070 9.146   -33.016  1.00 256.07 ? 360  CYS D SG  1 
ATOM   11490 N  N   . SER D  3 363 ? -46.141 10.196  -31.952  1.00 223.99 ? 361  SER D N   1 
ATOM   11491 C  CA  . SER D  3 363 ? -45.039 10.529  -31.055  1.00 224.81 ? 361  SER D CA  1 
ATOM   11492 C  C   . SER D  3 363 ? -44.504 11.941  -31.299  1.00 215.52 ? 361  SER D C   1 
ATOM   11493 O  O   . SER D  3 363 ? -44.946 12.656  -32.203  1.00 204.73 ? 361  SER D O   1 
ATOM   11494 C  CB  . SER D  3 363 ? -43.909 9.504   -31.196  1.00 227.52 ? 361  SER D CB  1 
ATOM   11495 O  OG  . SER D  3 363 ? -43.420 9.449   -32.525  1.00 225.96 ? 361  SER D OG  1 
ATOM   11496 O  OXT . SER D  3 363 ? -43.618 12.404  -30.580  1.00 213.40 ? 361  SER D OXT 1 
ATOM   11497 N  N   . PHE E  1 1   ? -11.046 -58.645 -50.678  1.00 192.00 ? 1    PHE E N   1 
ATOM   11498 C  CA  . PHE E  1 1   ? -11.089 -57.784 -51.854  1.00 202.75 ? 1    PHE E CA  1 
ATOM   11499 C  C   . PHE E  1 1   ? -12.404 -57.025 -51.904  1.00 209.19 ? 1    PHE E C   1 
ATOM   11500 O  O   . PHE E  1 1   ? -12.521 -55.993 -52.565  1.00 215.36 ? 1    PHE E O   1 
ATOM   11501 C  CB  . PHE E  1 1   ? -10.896 -58.600 -53.142  1.00 216.90 ? 1    PHE E CB  1 
ATOM   11502 C  CG  . PHE E  1 1   ? -11.975 -59.630 -53.396  1.00 223.21 ? 1    PHE E CG  1 
ATOM   11503 C  CD1 . PHE E  1 1   ? -11.900 -60.887 -52.819  1.00 221.94 ? 1    PHE E CD1 1 
ATOM   11504 C  CD2 . PHE E  1 1   ? -13.043 -59.353 -54.240  1.00 224.97 ? 1    PHE E CD2 1 
ATOM   11505 C  CE1 . PHE E  1 1   ? -12.880 -61.841 -53.060  1.00 218.91 ? 1    PHE E CE1 1 
ATOM   11506 C  CE2 . PHE E  1 1   ? -14.027 -60.306 -54.484  1.00 217.20 ? 1    PHE E CE2 1 
ATOM   11507 C  CZ  . PHE E  1 1   ? -13.942 -61.550 -53.893  1.00 209.15 ? 1    PHE E CZ  1 
ATOM   11508 N  N   . ASN E  1 2   ? -13.390 -57.547 -51.183  1.00 203.45 ? 2    ASN E N   1 
ATOM   11509 C  CA  . ASN E  1 2   ? -14.755 -57.050 -51.243  1.00 218.41 ? 2    ASN E CA  1 
ATOM   11510 C  C   . ASN E  1 2   ? -15.095 -56.066 -50.130  1.00 216.33 ? 2    ASN E C   1 
ATOM   11511 O  O   . ASN E  1 2   ? -16.274 -55.751 -49.940  1.00 225.27 ? 2    ASN E O   1 
ATOM   11512 C  CB  . ASN E  1 2   ? -15.720 -58.232 -51.213  1.00 232.19 ? 2    ASN E CB  1 
ATOM   11513 C  CG  . ASN E  1 2   ? -15.457 -59.165 -50.045  1.00 226.82 ? 2    ASN E CG  1 
ATOM   11514 O  OD1 . ASN E  1 2   ? -14.305 -59.401 -49.666  1.00 199.48 ? 2    ASN E OD1 1 
ATOM   11515 N  ND2 . ASN E  1 2   ? -16.525 -59.707 -49.471  1.00 247.78 ? 2    ASN E ND2 1 
ATOM   11516 N  N   . LEU E  1 3   ? -14.103 -55.561 -49.401  1.00 210.56 ? 3    LEU E N   1 
ATOM   11517 C  CA  . LEU E  1 3   ? -14.369 -54.550 -48.385  1.00 214.49 ? 3    LEU E CA  1 
ATOM   11518 C  C   . LEU E  1 3   ? -14.637 -53.206 -49.046  1.00 218.90 ? 3    LEU E C   1 
ATOM   11519 O  O   . LEU E  1 3   ? -13.876 -52.765 -49.913  1.00 224.20 ? 3    LEU E O   1 
ATOM   11520 C  CB  . LEU E  1 3   ? -13.199 -54.437 -47.410  1.00 201.18 ? 3    LEU E CB  1 
ATOM   11521 C  CG  . LEU E  1 3   ? -13.130 -55.547 -46.368  1.00 196.14 ? 3    LEU E CG  1 
ATOM   11522 C  CD1 . LEU E  1 3   ? -11.873 -55.416 -45.520  1.00 194.23 ? 3    LEU E CD1 1 
ATOM   11523 C  CD2 . LEU E  1 3   ? -14.382 -55.521 -45.508  1.00 198.00 ? 3    LEU E CD2 1 
ATOM   11524 N  N   . ASP E  1 4   ? -15.715 -52.551 -48.627  1.00 225.36 ? 4    ASP E N   1 
ATOM   11525 C  CA  . ASP E  1 4   ? -16.118 -51.282 -49.219  1.00 234.40 ? 4    ASP E CA  1 
ATOM   11526 C  C   . ASP E  1 4   ? -15.255 -50.161 -48.654  1.00 221.17 ? 4    ASP E C   1 
ATOM   11527 O  O   . ASP E  1 4   ? -15.385 -49.795 -47.479  1.00 219.84 ? 4    ASP E O   1 
ATOM   11528 C  CB  . ASP E  1 4   ? -17.595 -51.014 -48.957  1.00 256.45 ? 4    ASP E CB  1 
ATOM   11529 C  CG  . ASP E  1 4   ? -18.056 -49.697 -49.542  1.00 272.50 ? 4    ASP E CG  1 
ATOM   11530 O  OD1 . ASP E  1 4   ? -18.126 -49.588 -50.784  1.00 274.83 ? 4    ASP E OD1 1 
ATOM   11531 O  OD2 . ASP E  1 4   ? -18.347 -48.773 -48.757  1.00 280.17 ? 4    ASP E OD2 1 
ATOM   11532 N  N   . VAL E  1 5   ? -14.385 -49.606 -49.502  1.00 218.53 ? 5    VAL E N   1 
ATOM   11533 C  CA  . VAL E  1 5   ? -13.556 -48.471 -49.131  1.00 221.74 ? 5    VAL E CA  1 
ATOM   11534 C  C   . VAL E  1 5   ? -14.120 -47.176 -49.678  1.00 225.15 ? 5    VAL E C   1 
ATOM   11535 O  O   . VAL E  1 5   ? -13.575 -46.097 -49.409  1.00 226.69 ? 5    VAL E O   1 
ATOM   11536 C  CB  . VAL E  1 5   ? -12.096 -48.665 -49.595  1.00 224.74 ? 5    VAL E CB  1 
ATOM   11537 C  CG1 . VAL E  1 5   ? -11.126 -47.945 -48.656  1.00 223.00 ? 5    VAL E CG1 1 
ATOM   11538 C  CG2 . VAL E  1 5   ? -11.748 -50.142 -49.677  1.00 213.79 ? 5    VAL E CG2 1 
ATOM   11539 N  N   . ASP E  1 6   ? -15.201 -47.256 -50.457  1.00 237.21 ? 6    ASP E N   1 
ATOM   11540 C  CA  . ASP E  1 6   ? -15.806 -46.051 -51.009  1.00 251.03 ? 6    ASP E CA  1 
ATOM   11541 C  C   . ASP E  1 6   ? -16.572 -45.281 -49.940  1.00 249.62 ? 6    ASP E C   1 
ATOM   11542 O  O   . ASP E  1 6   ? -16.425 -44.059 -49.831  1.00 255.38 ? 6    ASP E O   1 
ATOM   11543 C  CB  . ASP E  1 6   ? -16.726 -46.412 -52.178  1.00 272.92 ? 6    ASP E CB  1 
ATOM   11544 C  CG  . ASP E  1 6   ? -15.981 -47.046 -53.342  1.00 276.86 ? 6    ASP E CG  1 
ATOM   11545 O  OD1 . ASP E  1 6   ? -14.736 -46.934 -53.387  1.00 286.15 ? 6    ASP E OD1 1 
ATOM   11546 O  OD2 . ASP E  1 6   ? -16.641 -47.650 -54.215  1.00 265.79 ? 6    ASP E OD2 1 
ATOM   11547 N  N   . SER E  1 7   ? -17.372 -45.971 -49.122  1.00 255.73 ? 7    SER E N   1 
ATOM   11548 C  CA  . SER E  1 7   ? -18.206 -45.324 -48.103  1.00 258.28 ? 7    SER E CA  1 
ATOM   11549 C  C   . SER E  1 7   ? -18.138 -46.093 -46.787  1.00 249.66 ? 7    SER E C   1 
ATOM   11550 O  O   . SER E  1 7   ? -19.091 -46.775 -46.394  1.00 257.73 ? 7    SER E O   1 
ATOM   11551 C  CB  . SER E  1 7   ? -19.655 -45.195 -48.585  1.00 265.53 ? 7    SER E CB  1 
ATOM   11552 O  OG  . SER E  1 7   ? -20.196 -46.446 -48.979  1.00 261.99 ? 7    SER E OG  1 
ATOM   11553 N  N   . PRO E  1 8   ? -17.018 -46.002 -46.075  1.00 236.47 ? 8    PRO E N   1 
ATOM   11554 C  CA  . PRO E  1 8   ? -16.926 -46.629 -44.754  1.00 230.70 ? 8    PRO E CA  1 
ATOM   11555 C  C   . PRO E  1 8   ? -17.461 -45.733 -43.647  1.00 237.52 ? 8    PRO E C   1 
ATOM   11556 O  O   . PRO E  1 8   ? -17.458 -44.505 -43.742  1.00 255.96 ? 8    PRO E O   1 
ATOM   11557 C  CB  . PRO E  1 8   ? -15.417 -46.857 -44.596  1.00 223.31 ? 8    PRO E CB  1 
ATOM   11558 C  CG  . PRO E  1 8   ? -14.814 -45.717 -45.335  1.00 227.04 ? 8    PRO E CG  1 
ATOM   11559 C  CD  . PRO E  1 8   ? -15.729 -45.421 -46.496  1.00 234.47 ? 8    PRO E CD  1 
ATOM   11560 N  N   . ALA E  1 9   ? -17.923 -46.376 -42.573  1.00 235.19 ? 9    ALA E N   1 
ATOM   11561 C  CA  . ALA E  1 9   ? -18.457 -45.660 -41.417  1.00 250.35 ? 9    ALA E CA  1 
ATOM   11562 C  C   . ALA E  1 9   ? -17.317 -45.178 -40.522  1.00 247.67 ? 9    ALA E C   1 
ATOM   11563 O  O   . ALA E  1 9   ? -16.468 -45.973 -40.101  1.00 223.15 ? 9    ALA E O   1 
ATOM   11564 C  CB  . ALA E  1 9   ? -19.420 -46.554 -40.640  1.00 253.31 ? 9    ALA E CB  1 
ATOM   11565 N  N   . GLU E  1 10  ? -17.289 -43.874 -40.235  1.00 265.13 ? 10   GLU E N   1 
ATOM   11566 C  CA  . GLU E  1 10  ? -16.241 -43.255 -39.424  1.00 259.52 ? 10   GLU E CA  1 
ATOM   11567 C  C   . GLU E  1 10  ? -16.796 -42.920 -38.041  1.00 262.94 ? 10   GLU E C   1 
ATOM   11568 O  O   . GLU E  1 10  ? -17.642 -42.028 -37.903  1.00 261.93 ? 10   GLU E O   1 
ATOM   11569 C  CB  . GLU E  1 10  ? -15.688 -42.007 -40.110  1.00 261.06 ? 10   GLU E CB  1 
ATOM   11570 C  CG  . GLU E  1 10  ? -14.649 -41.254 -39.288  1.00 251.29 ? 10   GLU E CG  1 
ATOM   11571 C  CD  . GLU E  1 10  ? -14.004 -40.114 -40.055  1.00 243.29 ? 10   GLU E CD  1 
ATOM   11572 O  OE1 . GLU E  1 10  ? -14.161 -40.060 -41.292  1.00 243.96 ? 10   GLU E OE1 1 
ATOM   11573 O  OE2 . GLU E  1 10  ? -13.334 -39.273 -39.421  1.00 242.18 ? 10   GLU E OE2 1 
ATOM   11574 N  N   . TYR E  1 11  ? -16.324 -43.641 -37.025  1.00 261.41 ? 11   TYR E N   1 
ATOM   11575 C  CA  . TYR E  1 11  ? -16.681 -43.382 -35.635  1.00 260.69 ? 11   TYR E CA  1 
ATOM   11576 C  C   . TYR E  1 11  ? -15.522 -42.704 -34.912  1.00 261.55 ? 11   TYR E C   1 
ATOM   11577 O  O   . TYR E  1 11  ? -14.355 -43.032 -35.146  1.00 268.25 ? 11   TYR E O   1 
ATOM   11578 C  CB  . TYR E  1 11  ? -17.068 -44.676 -34.914  1.00 244.01 ? 11   TYR E CB  1 
ATOM   11579 C  CG  . TYR E  1 11  ? -18.302 -45.339 -35.485  1.00 253.60 ? 11   TYR E CG  1 
ATOM   11580 C  CD1 . TYR E  1 11  ? -18.220 -46.185 -36.585  1.00 242.69 ? 11   TYR E CD1 1 
ATOM   11581 C  CD2 . TYR E  1 11  ? -19.556 -45.098 -34.937  1.00 277.78 ? 11   TYR E CD2 1 
ATOM   11582 C  CE1 . TYR E  1 11  ? -19.350 -46.784 -37.113  1.00 256.75 ? 11   TYR E CE1 1 
ATOM   11583 C  CE2 . TYR E  1 11  ? -20.692 -45.689 -35.458  1.00 287.59 ? 11   TYR E CE2 1 
ATOM   11584 C  CZ  . TYR E  1 11  ? -20.583 -46.530 -36.545  1.00 280.21 ? 11   TYR E CZ  1 
ATOM   11585 O  OH  . TYR E  1 11  ? -21.715 -47.116 -37.061  1.00 286.92 ? 11   TYR E OH  1 
ATOM   11586 N  N   . SER E  1 12  ? -15.850 -41.764 -34.022  1.00 252.39 ? 12   SER E N   1 
ATOM   11587 C  CA  . SER E  1 12  ? -14.835 -40.999 -33.311  1.00 231.20 ? 12   SER E CA  1 
ATOM   11588 C  C   . SER E  1 12  ? -15.185 -40.874 -31.835  1.00 231.38 ? 12   SER E C   1 
ATOM   11589 O  O   . SER E  1 12  ? -16.357 -40.888 -31.447  1.00 235.68 ? 12   SER E O   1 
ATOM   11590 C  CB  . SER E  1 12  ? -14.665 -39.597 -33.911  1.00 238.30 ? 12   SER E CB  1 
ATOM   11591 O  OG  . SER E  1 12  ? -15.872 -38.857 -33.833  1.00 260.78 ? 12   SER E OG  1 
ATOM   11592 N  N   . GLY E  1 13  ? -14.142 -40.738 -31.018  1.00 223.78 ? 13   GLY E N   1 
ATOM   11593 C  CA  . GLY E  1 13  ? -14.283 -40.533 -29.596  1.00 227.47 ? 13   GLY E CA  1 
ATOM   11594 C  C   . GLY E  1 13  ? -13.508 -39.307 -29.159  1.00 233.83 ? 13   GLY E C   1 
ATOM   11595 O  O   . GLY E  1 13  ? -12.972 -38.565 -29.989  1.00 233.97 ? 13   GLY E O   1 
ATOM   11596 N  N   . PRO E  1 14  ? -13.433 -39.067 -27.848  1.00 230.48 ? 14   PRO E N   1 
ATOM   11597 C  CA  . PRO E  1 14  ? -12.695 -37.896 -27.355  1.00 230.47 ? 14   PRO E CA  1 
ATOM   11598 C  C   . PRO E  1 14  ? -11.249 -37.898 -27.830  1.00 222.30 ? 14   PRO E C   1 
ATOM   11599 O  O   . PRO E  1 14  ? -10.590 -38.938 -27.879  1.00 214.70 ? 14   PRO E O   1 
ATOM   11600 C  CB  . PRO E  1 14  ? -12.786 -38.037 -25.831  1.00 225.41 ? 14   PRO E CB  1 
ATOM   11601 C  CG  . PRO E  1 14  ? -14.016 -38.863 -25.603  1.00 225.44 ? 14   PRO E CG  1 
ATOM   11602 C  CD  . PRO E  1 14  ? -14.077 -39.820 -26.757  1.00 224.60 ? 14   PRO E CD  1 
ATOM   11603 N  N   . GLU E  1 15  ? -10.767 -36.714 -28.193  1.00 225.55 ? 15   GLU E N   1 
ATOM   11604 C  CA  . GLU E  1 15  ? -9.402  -36.562 -28.674  1.00 222.29 ? 15   GLU E CA  1 
ATOM   11605 C  C   . GLU E  1 15  ? -8.396  -36.746 -27.543  1.00 217.13 ? 15   GLU E C   1 
ATOM   11606 O  O   . GLU E  1 15  ? -8.647  -36.398 -26.385  1.00 218.94 ? 15   GLU E O   1 
ATOM   11607 C  CB  . GLU E  1 15  ? -9.233  -35.201 -29.346  1.00 230.04 ? 15   GLU E CB  1 
ATOM   11608 C  CG  . GLU E  1 15  ? -8.981  -34.052 -28.394  1.00 237.32 ? 15   GLU E CG  1 
ATOM   11609 C  CD  . GLU E  1 15  ? -8.585  -32.783 -29.114  1.00 252.16 ? 15   GLU E CD  1 
ATOM   11610 O  OE1 . GLU E  1 15  ? -8.698  -32.741 -30.359  1.00 250.68 ? 15   GLU E OE1 1 
ATOM   11611 O  OE2 . GLU E  1 15  ? -8.192  -31.816 -28.426  1.00 265.97 ? 15   GLU E OE2 1 
ATOM   11612 N  N   . GLY E  1 16  ? -7.236  -37.296 -27.900  1.00 218.96 ? 16   GLY E N   1 
ATOM   11613 C  CA  . GLY E  1 16  ? -6.187  -37.591 -26.949  1.00 225.27 ? 16   GLY E CA  1 
ATOM   11614 C  C   . GLY E  1 16  ? -6.453  -38.782 -26.058  1.00 222.96 ? 16   GLY E C   1 
ATOM   11615 O  O   . GLY E  1 16  ? -5.621  -39.089 -25.197  1.00 223.40 ? 16   GLY E O   1 
ATOM   11616 N  N   . SER E  1 17  ? -7.572  -39.475 -26.251  1.00 218.83 ? 17   SER E N   1 
ATOM   11617 C  CA  . SER E  1 17  ? -8.006  -40.556 -25.378  1.00 214.36 ? 17   SER E CA  1 
ATOM   11618 C  C   . SER E  1 17  ? -7.579  -41.937 -25.850  1.00 205.96 ? 17   SER E C   1 
ATOM   11619 O  O   . SER E  1 17  ? -7.937  -42.925 -25.199  1.00 195.93 ? 17   SER E O   1 
ATOM   11620 C  CB  . SER E  1 17  ? -9.528  -40.527 -25.238  1.00 226.36 ? 17   SER E CB  1 
ATOM   11621 O  OG  . SER E  1 17  ? -10.155 -40.750 -26.490  1.00 229.69 ? 17   SER E OG  1 
ATOM   11622 N  N   . TYR E  1 18  ? -6.837  -42.034 -26.956  1.00 211.61 ? 18   TYR E N   1 
ATOM   11623 C  CA  . TYR E  1 18  ? -6.483  -43.320 -27.563  1.00 205.24 ? 18   TYR E CA  1 
ATOM   11624 C  C   . TYR E  1 18  ? -7.739  -44.107 -27.926  1.00 201.31 ? 18   TYR E C   1 
ATOM   11625 O  O   . TYR E  1 18  ? -7.774  -45.337 -27.839  1.00 192.83 ? 18   TYR E O   1 
ATOM   11626 C  CB  . TYR E  1 18  ? -5.568  -44.146 -26.654  1.00 203.26 ? 18   TYR E CB  1 
ATOM   11627 C  CG  . TYR E  1 18  ? -4.155  -43.620 -26.537  1.00 202.39 ? 18   TYR E CG  1 
ATOM   11628 C  CD1 . TYR E  1 18  ? -3.784  -42.422 -27.135  1.00 206.09 ? 18   TYR E CD1 1 
ATOM   11629 C  CD2 . TYR E  1 18  ? -3.194  -44.319 -25.820  1.00 198.25 ? 18   TYR E CD2 1 
ATOM   11630 C  CE1 . TYR E  1 18  ? -2.498  -41.938 -27.025  1.00 207.49 ? 18   TYR E CE1 1 
ATOM   11631 C  CE2 . TYR E  1 18  ? -1.905  -43.840 -25.703  1.00 203.48 ? 18   TYR E CE2 1 
ATOM   11632 C  CZ  . TYR E  1 18  ? -1.561  -42.651 -26.309  1.00 213.86 ? 18   TYR E CZ  1 
ATOM   11633 O  OH  . TYR E  1 18  ? -0.275  -42.176 -26.194  1.00 225.38 ? 18   TYR E OH  1 
ATOM   11634 N  N   . PHE E  1 19  ? -8.778  -43.378 -28.335  1.00 215.50 ? 19   PHE E N   1 
ATOM   11635 C  CA  . PHE E  1 19  ? -10.010 -43.986 -28.819  1.00 207.24 ? 19   PHE E CA  1 
ATOM   11636 C  C   . PHE E  1 19  ? -9.707  -44.932 -29.970  1.00 195.00 ? 19   PHE E C   1 
ATOM   11637 O  O   . PHE E  1 19  ? -9.203  -44.512 -31.014  1.00 191.62 ? 19   PHE E O   1 
ATOM   11638 C  CB  . PHE E  1 19  ? -10.987 -42.895 -29.263  1.00 200.64 ? 19   PHE E CB  1 
ATOM   11639 C  CG  . PHE E  1 19  ? -12.279 -43.425 -29.802  1.00 203.22 ? 19   PHE E CG  1 
ATOM   11640 C  CD1 . PHE E  1 19  ? -13.321 -43.745 -28.950  1.00 204.75 ? 19   PHE E CD1 1 
ATOM   11641 C  CD2 . PHE E  1 19  ? -12.445 -43.615 -31.161  1.00 204.35 ? 19   PHE E CD2 1 
ATOM   11642 C  CE1 . PHE E  1 19  ? -14.509 -44.235 -29.446  1.00 208.54 ? 19   PHE E CE1 1 
ATOM   11643 C  CE2 . PHE E  1 19  ? -13.624 -44.110 -31.662  1.00 207.00 ? 19   PHE E CE2 1 
ATOM   11644 C  CZ  . PHE E  1 19  ? -14.661 -44.419 -30.805  1.00 213.28 ? 19   PHE E CZ  1 
ATOM   11645 N  N   . GLY E  1 20  ? -10.009 -46.211 -29.778  1.00 196.00 ? 20   GLY E N   1 
ATOM   11646 C  CA  . GLY E  1 20  ? -9.714  -47.226 -30.765  1.00 198.76 ? 20   GLY E CA  1 
ATOM   11647 C  C   . GLY E  1 20  ? -8.568  -48.133 -30.403  1.00 187.86 ? 20   GLY E C   1 
ATOM   11648 O  O   . GLY E  1 20  ? -8.143  -48.937 -31.243  1.00 184.42 ? 20   GLY E O   1 
ATOM   11649 N  N   . PHE E  1 21  ? -8.047  -48.019 -29.183  1.00 193.25 ? 21   PHE E N   1 
ATOM   11650 C  CA  . PHE E  1 21  ? -6.963  -48.885 -28.746  1.00 194.35 ? 21   PHE E CA  1 
ATOM   11651 C  C   . PHE E  1 21  ? -7.405  -50.343 -28.675  1.00 201.87 ? 21   PHE E C   1 
ATOM   11652 O  O   . PHE E  1 21  ? -6.583  -51.250 -28.853  1.00 192.66 ? 21   PHE E O   1 
ATOM   11653 C  CB  . PHE E  1 21  ? -6.450  -48.400 -27.395  1.00 190.04 ? 21   PHE E CB  1 
ATOM   11654 C  CG  . PHE E  1 21  ? -5.203  -49.075 -26.953  1.00 200.49 ? 21   PHE E CG  1 
ATOM   11655 C  CD1 . PHE E  1 21  ? -3.970  -48.566 -27.316  1.00 209.44 ? 21   PHE E CD1 1 
ATOM   11656 C  CD2 . PHE E  1 21  ? -5.257  -50.228 -26.193  1.00 216.13 ? 21   PHE E CD2 1 
ATOM   11657 C  CE1 . PHE E  1 21  ? -2.811  -49.188 -26.917  1.00 208.71 ? 21   PHE E CE1 1 
ATOM   11658 C  CE2 . PHE E  1 21  ? -4.101  -50.857 -25.792  1.00 211.86 ? 21   PHE E CE2 1 
ATOM   11659 C  CZ  . PHE E  1 21  ? -2.876  -50.334 -26.154  1.00 212.44 ? 21   PHE E CZ  1 
ATOM   11660 N  N   . ALA E  1 22  ? -8.681  -50.587 -28.382  1.00 212.43 ? 22   ALA E N   1 
ATOM   11661 C  CA  . ALA E  1 22  ? -9.263  -51.924 -28.411  1.00 213.11 ? 22   ALA E CA  1 
ATOM   11662 C  C   . ALA E  1 22  ? -10.660 -51.839 -29.007  1.00 215.23 ? 22   ALA E C   1 
ATOM   11663 O  O   . ALA E  1 22  ? -11.429 -50.937 -28.661  1.00 214.00 ? 22   ALA E O   1 
ATOM   11664 C  CB  . ALA E  1 22  ? -9.316  -52.545 -27.010  1.00 211.61 ? 22   ALA E CB  1 
ATOM   11665 N  N   . VAL E  1 23  ? -10.983 -52.762 -29.913  1.00 205.12 ? 23   VAL E N   1 
ATOM   11666 C  CA  . VAL E  1 23  ? -12.276 -52.770 -30.584  1.00 202.42 ? 23   VAL E CA  1 
ATOM   11667 C  C   . VAL E  1 23  ? -12.882 -54.167 -30.525  1.00 192.64 ? 23   VAL E C   1 
ATOM   11668 O  O   . VAL E  1 23  ? -12.172 -55.168 -30.387  1.00 181.47 ? 23   VAL E O   1 
ATOM   11669 C  CB  . VAL E  1 23  ? -12.147 -52.289 -32.043  1.00 194.15 ? 23   VAL E CB  1 
ATOM   11670 C  CG1 . VAL E  1 23  ? -11.603 -50.867 -32.084  1.00 195.40 ? 23   VAL E CG1 1 
ATOM   11671 C  CG2 . VAL E  1 23  ? -11.246 -53.217 -32.816  1.00 186.29 ? 23   VAL E CG2 1 
ATOM   11672 N  N   . ASP E  1 24  ? -14.211 -54.226 -30.615  1.00 210.31 ? 24   ASP E N   1 
ATOM   11673 C  CA  . ASP E  1 24  ? -14.950 -55.490 -30.654  1.00 211.50 ? 24   ASP E CA  1 
ATOM   11674 C  C   . ASP E  1 24  ? -16.384 -55.198 -31.108  1.00 207.81 ? 24   ASP E C   1 
ATOM   11675 O  O   . ASP E  1 24  ? -16.773 -54.042 -31.305  1.00 188.64 ? 24   ASP E O   1 
ATOM   11676 C  CB  . ASP E  1 24  ? -14.924 -56.196 -29.295  1.00 219.84 ? 24   ASP E CB  1 
ATOM   11677 C  CG  . ASP E  1 24  ? -15.157 -57.694 -29.409  1.00 218.06 ? 24   ASP E CG  1 
ATOM   11678 O  OD1 . ASP E  1 24  ? -14.175 -58.441 -29.604  1.00 207.47 ? 24   ASP E OD1 1 
ATOM   11679 O  OD2 . ASP E  1 24  ? -16.327 -58.121 -29.317  1.00 228.66 ? 24   ASP E OD2 1 
ATOM   11680 N  N   . PHE E  1 25  ? -17.170 -56.264 -31.256  1.00 207.72 ? 25   PHE E N   1 
ATOM   11681 C  CA  . PHE E  1 25  ? -18.579 -56.189 -31.621  1.00 210.03 ? 25   PHE E CA  1 
ATOM   11682 C  C   . PHE E  1 25  ? -19.479 -56.396 -30.403  1.00 217.63 ? 25   PHE E C   1 
ATOM   11683 O  O   . PHE E  1 25  ? -19.026 -56.712 -29.302  1.00 217.00 ? 25   PHE E O   1 
ATOM   11684 C  CB  . PHE E  1 25  ? -18.915 -57.233 -32.691  1.00 215.92 ? 25   PHE E CB  1 
ATOM   11685 C  CG  . PHE E  1 25  ? -18.252 -56.990 -34.016  1.00 216.91 ? 25   PHE E CG  1 
ATOM   11686 C  CD1 . PHE E  1 25  ? -16.983 -57.482 -34.272  1.00 223.08 ? 25   PHE E CD1 1 
ATOM   11687 C  CD2 . PHE E  1 25  ? -18.911 -56.290 -35.015  1.00 219.11 ? 25   PHE E CD2 1 
ATOM   11688 C  CE1 . PHE E  1 25  ? -16.373 -57.264 -35.494  1.00 234.32 ? 25   PHE E CE1 1 
ATOM   11689 C  CE2 . PHE E  1 25  ? -18.312 -56.072 -36.240  1.00 226.01 ? 25   PHE E CE2 1 
ATOM   11690 C  CZ  . PHE E  1 25  ? -17.040 -56.559 -36.481  1.00 241.68 ? 25   PHE E CZ  1 
ATOM   11691 N  N   . PHE E  1 26  ? -20.782 -56.196 -30.617  1.00 229.56 ? 26   PHE E N   1 
ATOM   11692 C  CA  . PHE E  1 26  ? -21.790 -56.413 -29.584  1.00 235.35 ? 26   PHE E CA  1 
ATOM   11693 C  C   . PHE E  1 26  ? -23.056 -56.978 -30.216  1.00 252.61 ? 26   PHE E C   1 
ATOM   11694 O  O   . PHE E  1 26  ? -23.691 -56.308 -31.036  1.00 258.12 ? 26   PHE E O   1 
ATOM   11695 C  CB  . PHE E  1 26  ? -22.099 -55.115 -28.841  1.00 235.95 ? 26   PHE E CB  1 
ATOM   11696 C  CG  . PHE E  1 26  ? -22.961 -55.304 -27.637  1.00 236.34 ? 26   PHE E CG  1 
ATOM   11697 C  CD1 . PHE E  1 26  ? -22.919 -56.489 -26.919  1.00 236.50 ? 26   PHE E CD1 1 
ATOM   11698 C  CD2 . PHE E  1 26  ? -23.823 -54.305 -27.225  1.00 248.45 ? 26   PHE E CD2 1 
ATOM   11699 C  CE1 . PHE E  1 26  ? -23.717 -56.667 -25.803  1.00 252.43 ? 26   PHE E CE1 1 
ATOM   11700 C  CE2 . PHE E  1 26  ? -24.624 -54.475 -26.111  1.00 260.65 ? 26   PHE E CE2 1 
ATOM   11701 C  CZ  . PHE E  1 26  ? -24.572 -55.658 -25.399  1.00 261.28 ? 26   PHE E CZ  1 
ATOM   11702 N  N   . VAL E  1 27  ? -23.426 -58.196 -29.828  1.00 265.04 ? 27   VAL E N   1 
ATOM   11703 C  CA  . VAL E  1 27  ? -24.645 -58.840 -30.321  1.00 280.85 ? 27   VAL E CA  1 
ATOM   11704 C  C   . VAL E  1 27  ? -25.460 -59.342 -29.131  1.00 280.63 ? 27   VAL E C   1 
ATOM   11705 O  O   . VAL E  1 27  ? -25.247 -60.467 -28.652  1.00 284.02 ? 27   VAL E O   1 
ATOM   11706 C  CB  . VAL E  1 27  ? -24.308 -59.954 -31.327  1.00 271.24 ? 27   VAL E CB  1 
ATOM   11707 C  CG1 . VAL E  1 27  ? -23.153 -60.831 -30.827  1.00 249.31 ? 27   VAL E CG1 1 
ATOM   11708 C  CG2 . VAL E  1 27  ? -25.543 -60.790 -31.672  1.00 283.95 ? 27   VAL E CG2 1 
ATOM   11709 N  N   . PRO E  1 28  ? -26.389 -58.533 -28.602  1.00 266.40 ? 28   PRO E N   1 
ATOM   11710 C  CA  . PRO E  1 28  ? -27.158 -58.950 -27.421  1.00 271.09 ? 28   PRO E CA  1 
ATOM   11711 C  C   . PRO E  1 28  ? -28.305 -59.903 -27.710  1.00 282.15 ? 28   PRO E C   1 
ATOM   11712 O  O   . PRO E  1 28  ? -28.367 -60.552 -28.760  1.00 281.61 ? 28   PRO E O   1 
ATOM   11713 C  CB  . PRO E  1 28  ? -27.680 -57.620 -26.867  1.00 276.22 ? 28   PRO E CB  1 
ATOM   11714 C  CG  . PRO E  1 28  ? -27.814 -56.764 -28.072  1.00 275.09 ? 28   PRO E CG  1 
ATOM   11715 C  CD  . PRO E  1 28  ? -26.673 -57.139 -28.978  1.00 261.73 ? 28   PRO E CD  1 
ATOM   11716 N  N   . SER E  1 29  ? -29.224 -59.977 -26.746  1.00 282.59 ? 29   SER E N   1 
ATOM   11717 C  CA  . SER E  1 29  ? -30.289 -60.979 -26.758  1.00 281.17 ? 29   SER E CA  1 
ATOM   11718 C  C   . SER E  1 29  ? -31.171 -60.877 -27.994  1.00 291.21 ? 29   SER E C   1 
ATOM   11719 O  O   . SER E  1 29  ? -31.477 -59.781 -28.474  1.00 283.28 ? 29   SER E O   1 
ATOM   11720 C  CB  . SER E  1 29  ? -31.157 -60.837 -25.512  1.00 272.02 ? 29   SER E CB  1 
ATOM   11721 O  OG  . SER E  1 29  ? -30.367 -60.914 -24.343  1.00 266.08 ? 29   SER E OG  1 
ATOM   11722 N  N   . ALA E  1 30  ? -31.588 -62.039 -28.487  1.00 324.02 ? 30   ALA E N   1 
ATOM   11723 C  CA  . ALA E  1 30  ? -32.523 -62.243 -29.603  1.00 332.87 ? 30   ALA E CA  1 
ATOM   11724 C  C   . ALA E  1 30  ? -32.022 -61.519 -30.857  1.00 336.31 ? 30   ALA E C   1 
ATOM   11725 O  O   . ALA E  1 30  ? -30.815 -61.298 -31.031  1.00 317.98 ? 30   ALA E O   1 
ATOM   11726 C  CB  . ALA E  1 30  ? -33.913 -61.838 -29.161  1.00 321.06 ? 30   ALA E CB  1 
ATOM   11727 N  N   . SER E  1 31  ? -32.946 -61.168 -31.762  1.00 338.63 ? 31   SER E N   1 
ATOM   11728 C  CA  . SER E  1 31  ? -32.610 -60.476 -33.011  1.00 320.48 ? 31   SER E CA  1 
ATOM   11729 C  C   . SER E  1 31  ? -32.777 -58.971 -32.811  1.00 321.65 ? 31   SER E C   1 
ATOM   11730 O  O   . SER E  1 31  ? -33.755 -58.351 -33.241  1.00 324.11 ? 31   SER E O   1 
ATOM   11731 C  CB  . SER E  1 31  ? -33.472 -60.994 -34.148  1.00 315.08 ? 31   SER E CB  1 
ATOM   11732 O  OG  . SER E  1 31  ? -34.846 -60.898 -33.819  1.00 317.49 ? 31   SER E OG  1 
ATOM   11733 N  N   . SER E  1 32  ? -31.791 -58.376 -32.149  1.00 308.42 ? 32   SER E N   1 
ATOM   11734 C  CA  . SER E  1 32  ? -31.802 -56.958 -31.842  1.00 286.41 ? 32   SER E CA  1 
ATOM   11735 C  C   . SER E  1 32  ? -30.860 -56.213 -32.791  1.00 265.97 ? 32   SER E C   1 
ATOM   11736 O  O   . SER E  1 32  ? -30.446 -56.744 -33.829  1.00 261.63 ? 32   SER E O   1 
ATOM   11737 C  CB  . SER E  1 32  ? -31.426 -56.758 -30.365  1.00 276.96 ? 32   SER E CB  1 
ATOM   11738 O  OG  . SER E  1 32  ? -32.287 -57.483 -29.500  1.00 270.35 ? 32   SER E OG  1 
ATOM   11739 N  N   . ARG E  1 33  ? -30.525 -54.976 -32.445  1.00 249.23 ? 33   ARG E N   1 
ATOM   11740 C  CA  . ARG E  1 33  ? -29.549 -54.208 -33.194  1.00 249.74 ? 33   ARG E CA  1 
ATOM   11741 C  C   . ARG E  1 33  ? -28.136 -54.628 -32.791  1.00 255.57 ? 33   ARG E C   1 
ATOM   11742 O  O   . ARG E  1 33  ? -27.928 -55.352 -31.812  1.00 264.01 ? 33   ARG E O   1 
ATOM   11743 C  CB  . ARG E  1 33  ? -29.776 -52.712 -32.972  1.00 251.98 ? 33   ARG E CB  1 
ATOM   11744 C  CG  . ARG E  1 33  ? -31.065 -52.190 -33.609  1.00 270.94 ? 33   ARG E CG  1 
ATOM   11745 C  CD  . ARG E  1 33  ? -31.429 -50.778 -33.149  1.00 279.50 ? 33   ARG E CD  1 
ATOM   11746 N  NE  . ARG E  1 33  ? -31.583 -50.689 -31.699  1.00 280.97 ? 33   ARG E NE  1 
ATOM   11747 C  CZ  . ARG E  1 33  ? -30.736 -50.059 -30.892  1.00 278.49 ? 33   ARG E CZ  1 
ATOM   11748 N  NH1 . ARG E  1 33  ? -29.674 -49.441 -31.390  1.00 269.73 ? 33   ARG E NH1 1 
ATOM   11749 N  NH2 . ARG E  1 33  ? -30.959 -50.034 -29.585  1.00 282.70 ? 33   ARG E NH2 1 
ATOM   11750 N  N   . MET E  1 34  ? -27.157 -54.173 -33.567  1.00 236.79 ? 34   MET E N   1 
ATOM   11751 C  CA  . MET E  1 34  ? -25.759 -54.503 -33.344  1.00 221.90 ? 34   MET E CA  1 
ATOM   11752 C  C   . MET E  1 34  ? -24.973 -53.225 -33.067  1.00 221.11 ? 34   MET E C   1 
ATOM   11753 O  O   . MET E  1 34  ? -25.354 -52.135 -33.502  1.00 226.73 ? 34   MET E O   1 
ATOM   11754 C  CB  . MET E  1 34  ? -25.172 -55.236 -34.554  1.00 228.08 ? 34   MET E CB  1 
ATOM   11755 C  CG  . MET E  1 34  ? -25.823 -56.578 -34.877  1.00 250.23 ? 34   MET E CG  1 
ATOM   11756 S  SD  . MET E  1 34  ? -24.811 -58.006 -34.438  1.00 260.69 ? 34   MET E SD  1 
ATOM   11757 C  CE  . MET E  1 34  ? -25.790 -59.343 -35.122  1.00 242.06 ? 34   MET E CE  1 
ATOM   11758 N  N   . PHE E  1 35  ? -23.854 -53.365 -32.353  1.00 227.14 ? 35   PHE E N   1 
ATOM   11759 C  CA  . PHE E  1 35  ? -23.093 -52.206 -31.900  1.00 224.97 ? 35   PHE E CA  1 
ATOM   11760 C  C   . PHE E  1 35  ? -21.596 -52.441 -32.066  1.00 229.02 ? 35   PHE E C   1 
ATOM   11761 O  O   . PHE E  1 35  ? -21.135 -53.573 -32.230  1.00 217.17 ? 35   PHE E O   1 
ATOM   11762 C  CB  . PHE E  1 35  ? -23.396 -51.877 -30.433  1.00 226.70 ? 35   PHE E CB  1 
ATOM   11763 C  CG  . PHE E  1 35  ? -24.839 -51.569 -30.170  1.00 248.39 ? 35   PHE E CG  1 
ATOM   11764 C  CD1 . PHE E  1 35  ? -25.330 -50.286 -30.346  1.00 256.97 ? 35   PHE E CD1 1 
ATOM   11765 C  CD2 . PHE E  1 35  ? -25.707 -52.562 -29.749  1.00 251.65 ? 35   PHE E CD2 1 
ATOM   11766 C  CE1 . PHE E  1 35  ? -26.661 -49.998 -30.104  1.00 254.20 ? 35   PHE E CE1 1 
ATOM   11767 C  CE2 . PHE E  1 35  ? -27.040 -52.282 -29.506  1.00 251.96 ? 35   PHE E CE2 1 
ATOM   11768 C  CZ  . PHE E  1 35  ? -27.516 -50.998 -29.683  1.00 250.41 ? 35   PHE E CZ  1 
ATOM   11769 N  N   . LEU E  1 36  ? -20.843 -51.341 -32.027  1.00 240.57 ? 36   LEU E N   1 
ATOM   11770 C  CA  . LEU E  1 36  ? -19.384 -51.363 -31.990  1.00 228.11 ? 36   LEU E CA  1 
ATOM   11771 C  C   . LEU E  1 36  ? -18.899 -51.032 -30.583  1.00 222.73 ? 36   LEU E C   1 
ATOM   11772 O  O   . LEU E  1 36  ? -19.344 -50.049 -29.980  1.00 230.00 ? 36   LEU E O   1 
ATOM   11773 C  CB  . LEU E  1 36  ? -18.786 -50.365 -32.984  1.00 232.88 ? 36   LEU E CB  1 
ATOM   11774 C  CG  . LEU E  1 36  ? -19.023 -50.540 -34.484  1.00 239.45 ? 36   LEU E CG  1 
ATOM   11775 C  CD1 . LEU E  1 36  ? -20.356 -49.935 -34.898  1.00 272.93 ? 36   LEU E CD1 1 
ATOM   11776 C  CD2 . LEU E  1 36  ? -17.886 -49.894 -35.249  1.00 236.34 ? 36   LEU E CD2 1 
ATOM   11777 N  N   . LEU E  1 37  ? -17.986 -51.847 -30.069  1.00 197.60 ? 37   LEU E N   1 
ATOM   11778 C  CA  . LEU E  1 37  ? -17.343 -51.594 -28.787  1.00 194.89 ? 37   LEU E CA  1 
ATOM   11779 C  C   . LEU E  1 37  ? -15.942 -51.048 -29.046  1.00 192.62 ? 37   LEU E C   1 
ATOM   11780 O  O   . LEU E  1 37  ? -15.131 -51.708 -29.703  1.00 188.24 ? 37   LEU E O   1 
ATOM   11781 C  CB  . LEU E  1 37  ? -17.285 -52.873 -27.954  1.00 193.00 ? 37   LEU E CB  1 
ATOM   11782 C  CG  . LEU E  1 37  ? -18.634 -53.454 -27.525  1.00 196.90 ? 37   LEU E CG  1 
ATOM   11783 C  CD1 . LEU E  1 37  ? -18.433 -54.693 -26.669  1.00 199.28 ? 37   LEU E CD1 1 
ATOM   11784 C  CD2 . LEU E  1 37  ? -19.462 -52.415 -26.789  1.00 207.17 ? 37   LEU E CD2 1 
ATOM   11785 N  N   . VAL E  1 38  ? -15.667 -49.838 -28.562  1.00 216.79 ? 38   VAL E N   1 
ATOM   11786 C  CA  . VAL E  1 38  ? -14.380 -49.182 -28.773  1.00 218.94 ? 38   VAL E CA  1 
ATOM   11787 C  C   . VAL E  1 38  ? -13.781 -48.806 -27.422  1.00 214.27 ? 38   VAL E C   1 
ATOM   11788 O  O   . VAL E  1 38  ? -14.481 -48.274 -26.553  1.00 209.01 ? 38   VAL E O   1 
ATOM   11789 C  CB  . VAL E  1 38  ? -14.511 -47.942 -29.672  1.00 236.42 ? 38   VAL E CB  1 
ATOM   11790 C  CG1 . VAL E  1 38  ? -13.137 -47.381 -29.970  1.00 227.51 ? 38   VAL E CG1 1 
ATOM   11791 C  CG2 . VAL E  1 38  ? -15.246 -48.288 -30.958  1.00 241.02 ? 38   VAL E CG2 1 
ATOM   11792 N  N   . GLY E  1 39  ? -12.493 -49.093 -27.248  1.00 207.60 ? 39   GLY E N   1 
ATOM   11793 C  CA  . GLY E  1 39  ? -11.781 -48.724 -26.032  1.00 208.12 ? 39   GLY E CA  1 
ATOM   11794 C  C   . GLY E  1 39  ? -11.048 -47.395 -26.155  1.00 200.34 ? 39   GLY E C   1 
ATOM   11795 O  O   . GLY E  1 39  ? -10.421 -47.103 -27.172  1.00 195.49 ? 39   GLY E O   1 
ATOM   11796 N  N   . ALA E  1 40  ? -11.145 -46.587 -25.096  1.00 192.03 ? 40   ALA E N   1 
ATOM   11797 C  CA  . ALA E  1 40  ? -10.394 -45.339 -24.965  1.00 192.73 ? 40   ALA E CA  1 
ATOM   11798 C  C   . ALA E  1 40  ? -9.753  -45.328 -23.584  1.00 196.62 ? 40   ALA E C   1 
ATOM   11799 O  O   . ALA E  1 40  ? -10.305 -44.757 -22.632  1.00 193.80 ? 40   ALA E O   1 
ATOM   11800 C  CB  . ALA E  1 40  ? -11.289 -44.118 -25.178  1.00 198.10 ? 40   ALA E CB  1 
ATOM   11801 N  N   . PRO E  1 41  ? -8.585  -45.961 -23.435  1.00 209.28 ? 41   PRO E N   1 
ATOM   11802 C  CA  . PRO E  1 41  ? -8.018  -46.153 -22.089  1.00 209.52 ? 41   PRO E CA  1 
ATOM   11803 C  C   . PRO E  1 41  ? -7.487  -44.882 -21.437  1.00 207.49 ? 41   PRO E C   1 
ATOM   11804 O  O   . PRO E  1 41  ? -7.363  -44.850 -20.206  1.00 207.97 ? 41   PRO E O   1 
ATOM   11805 C  CB  . PRO E  1 41  ? -6.895  -47.172 -22.328  1.00 197.23 ? 41   PRO E CB  1 
ATOM   11806 C  CG  . PRO E  1 41  ? -6.513  -46.977 -23.758  1.00 197.01 ? 41   PRO E CG  1 
ATOM   11807 C  CD  . PRO E  1 41  ? -7.780  -46.618 -24.480  1.00 204.36 ? 41   PRO E CD  1 
ATOM   11808 N  N   . LYS E  1 42  ? -7.183  -43.832 -22.199  1.00 212.34 ? 42   LYS E N   1 
ATOM   11809 C  CA  . LYS E  1 42  ? -6.688  -42.589 -21.623  1.00 205.64 ? 42   LYS E CA  1 
ATOM   11810 C  C   . LYS E  1 42  ? -7.775  -41.530 -21.510  1.00 212.25 ? 42   LYS E C   1 
ATOM   11811 O  O   . LYS E  1 42  ? -7.463  -40.346 -21.349  1.00 223.79 ? 42   LYS E O   1 
ATOM   11812 C  CB  . LYS E  1 42  ? -5.510  -42.046 -22.433  1.00 193.18 ? 42   LYS E CB  1 
ATOM   11813 C  CG  . LYS E  1 42  ? -4.184  -42.683 -22.084  1.00 189.31 ? 42   LYS E CG  1 
ATOM   11814 C  CD  . LYS E  1 42  ? -3.023  -41.887 -22.647  1.00 190.11 ? 42   LYS E CD  1 
ATOM   11815 C  CE  . LYS E  1 42  ? -1.708  -42.358 -22.052  1.00 189.58 ? 42   LYS E CE  1 
ATOM   11816 N  NZ  . LYS E  1 42  ? -0.543  -41.592 -22.561  1.00 212.25 ? 42   LYS E NZ  1 
ATOM   11817 N  N   . ALA E  1 43  ? -9.039  -41.930 -21.590  1.00 203.05 ? 43   ALA E N   1 
ATOM   11818 C  CA  . ALA E  1 43  ? -10.139 -40.978 -21.596  1.00 210.29 ? 43   ALA E CA  1 
ATOM   11819 C  C   . ALA E  1 43  ? -10.454 -40.506 -20.184  1.00 214.62 ? 43   ALA E C   1 
ATOM   11820 O  O   . ALA E  1 43  ? -10.566 -41.314 -19.257  1.00 219.45 ? 43   ALA E O   1 
ATOM   11821 C  CB  . ALA E  1 43  ? -11.380 -41.609 -22.224  1.00 215.46 ? 43   ALA E CB  1 
ATOM   11822 N  N   . ASN E  1 44  ? -10.590 -39.194 -20.021  1.00 207.42 ? 44   ASN E N   1 
ATOM   11823 C  CA  . ASN E  1 44  ? -11.086 -38.647 -18.769  1.00 211.55 ? 44   ASN E CA  1 
ATOM   11824 C  C   . ASN E  1 44  ? -12.548 -39.039 -18.573  1.00 214.48 ? 44   ASN E C   1 
ATOM   11825 O  O   . ASN E  1 44  ? -13.339 -39.029 -19.520  1.00 217.49 ? 44   ASN E O   1 
ATOM   11826 C  CB  . ASN E  1 44  ? -10.936 -37.128 -18.758  1.00 218.96 ? 44   ASN E CB  1 
ATOM   11827 C  CG  . ASN E  1 44  ? -9.544  -36.675 -18.353  1.00 226.96 ? 44   ASN E CG  1 
ATOM   11828 O  OD1 . ASN E  1 44  ? -8.975  -37.177 -17.383  1.00 212.72 ? 44   ASN E OD1 1 
ATOM   11829 N  ND2 . ASN E  1 44  ? -8.991  -35.710 -19.090  1.00 307.06 ? 44   ASN E ND2 1 
ATOM   11830 N  N   . THR E  1 45  ? -12.897 -39.430 -17.349  1.00 222.11 ? 45   THR E N   1 
ATOM   11831 C  CA  . THR E  1 45  ? -14.269 -39.787 -17.003  1.00 228.37 ? 45   THR E CA  1 
ATOM   11832 C  C   . THR E  1 45  ? -14.801 -38.862 -15.915  1.00 229.51 ? 45   THR E C   1 
ATOM   11833 O  O   . THR E  1 45  ? -14.116 -37.955 -15.437  1.00 231.69 ? 45   THR E O   1 
ATOM   11834 C  CB  . THR E  1 45  ? -14.369 -41.242 -16.539  1.00 227.07 ? 45   THR E CB  1 
ATOM   11835 O  OG1 . THR E  1 45  ? -13.687 -41.395 -15.289  1.00 215.74 ? 45   THR E OG1 1 
ATOM   11836 C  CG2 . THR E  1 45  ? -13.760 -42.168 -17.570  1.00 225.37 ? 45   THR E CG2 1 
ATOM   11837 N  N   . THR E  1 46  ? -16.044 -39.120 -15.517  1.00 226.70 ? 46   THR E N   1 
ATOM   11838 C  CA  . THR E  1 46  ? -16.723 -38.347 -14.486  1.00 246.13 ? 46   THR E CA  1 
ATOM   11839 C  C   . THR E  1 46  ? -16.490 -38.908 -13.092  1.00 241.07 ? 46   THR E C   1 
ATOM   11840 O  O   . THR E  1 46  ? -17.054 -38.387 -12.123  1.00 252.03 ? 46   THR E O   1 
ATOM   11841 C  CB  . THR E  1 46  ? -18.226 -38.297 -14.776  1.00 257.07 ? 46   THR E CB  1 
ATOM   11842 O  OG1 . THR E  1 46  ? -18.746 -39.630 -14.797  1.00 250.93 ? 46   THR E OG1 1 
ATOM   11843 C  CG2 . THR E  1 46  ? -18.489 -37.641 -16.124  1.00 244.51 ? 46   THR E CG2 1 
ATOM   11844 N  N   . GLN E  1 47  ? -15.682 -39.954 -12.978  1.00 226.13 ? 47   GLN E N   1 
ATOM   11845 C  CA  . GLN E  1 47  ? -15.412 -40.574 -11.690  1.00 222.53 ? 47   GLN E CA  1 
ATOM   11846 C  C   . GLN E  1 47  ? -14.765 -39.576 -10.735  1.00 225.32 ? 47   GLN E C   1 
ATOM   11847 O  O   . GLN E  1 47  ? -13.804 -38.892 -11.116  1.00 225.10 ? 47   GLN E O   1 
ATOM   11848 C  CB  . GLN E  1 47  ? -14.509 -41.784 -11.881  1.00 213.85 ? 47   GLN E CB  1 
ATOM   11849 C  CG  . GLN E  1 47  ? -15.183 -42.937 -12.589  1.00 212.03 ? 47   GLN E CG  1 
ATOM   11850 C  CD  . GLN E  1 47  ? -14.188 -43.932 -13.134  1.00 212.80 ? 47   GLN E CD  1 
ATOM   11851 O  OE1 . GLN E  1 47  ? -12.992 -43.653 -13.195  1.00 209.89 ? 47   GLN E OE1 1 
ATOM   11852 N  NE2 . GLN E  1 47  ? -14.672 -45.103 -13.524  1.00 213.57 ? 47   GLN E NE2 1 
ATOM   11853 N  N   . PRO E  1 48  ? -15.257 -39.461 -9.501   1.00 240.81 ? 48   PRO E N   1 
ATOM   11854 C  CA  . PRO E  1 48  ? -14.734 -38.451 -8.567   1.00 258.02 ? 48   PRO E CA  1 
ATOM   11855 C  C   . PRO E  1 48  ? -13.259 -38.667 -8.264   1.00 242.64 ? 48   PRO E C   1 
ATOM   11856 O  O   . PRO E  1 48  ? -12.850 -39.728 -7.785   1.00 220.99 ? 48   PRO E O   1 
ATOM   11857 C  CB  . PRO E  1 48  ? -15.606 -38.640 -7.319   1.00 263.00 ? 48   PRO E CB  1 
ATOM   11858 C  CG  . PRO E  1 48  ? -16.840 -39.338 -7.804   1.00 249.77 ? 48   PRO E CG  1 
ATOM   11859 C  CD  . PRO E  1 48  ? -16.373 -40.226 -8.919   1.00 238.38 ? 48   PRO E CD  1 
ATOM   11860 N  N   . GLY E  1 49  ? -12.454 -37.652 -8.576   1.00 252.27 ? 49   GLY E N   1 
ATOM   11861 C  CA  . GLY E  1 49  ? -11.042 -37.662 -8.262   1.00 231.49 ? 49   GLY E CA  1 
ATOM   11862 C  C   . GLY E  1 49  ? -10.200 -38.539 -9.152   1.00 214.17 ? 49   GLY E C   1 
ATOM   11863 O  O   . GLY E  1 49  ? -8.983  -38.623 -8.940   1.00 212.04 ? 49   GLY E O   1 
ATOM   11864 N  N   . ILE E  1 50  ? -10.802 -39.202 -10.131  1.00 220.25 ? 50   ILE E N   1 
ATOM   11865 C  CA  . ILE E  1 50  ? -10.105 -40.133 -11.007  1.00 228.20 ? 50   ILE E CA  1 
ATOM   11866 C  C   . ILE E  1 50  ? -9.752  -39.402 -12.296  1.00 234.10 ? 50   ILE E C   1 
ATOM   11867 O  O   . ILE E  1 50  ? -10.637 -39.025 -13.073  1.00 235.95 ? 50   ILE E O   1 
ATOM   11868 C  CB  . ILE E  1 50  ? -10.956 -41.376 -11.281  1.00 222.67 ? 50   ILE E CB  1 
ATOM   11869 C  CG1 . ILE E  1 50  ? -11.328 -42.049 -9.959   1.00 229.26 ? 50   ILE E CG1 1 
ATOM   11870 C  CG2 . ILE E  1 50  ? -10.203 -42.333 -12.187  1.00 206.91 ? 50   ILE E CG2 1 
ATOM   11871 C  CD1 . ILE E  1 50  ? -11.977 -43.398 -10.119  1.00 219.98 ? 50   ILE E CD1 1 
ATOM   11872 N  N   . VAL E  1 51  ? -8.459  -39.206 -12.532  1.00 242.13 ? 51   VAL E N   1 
ATOM   11873 C  CA  . VAL E  1 51  ? -7.976  -38.554 -13.744  1.00 245.06 ? 51   VAL E CA  1 
ATOM   11874 C  C   . VAL E  1 51  ? -7.619  -39.623 -14.773  1.00 223.62 ? 51   VAL E C   1 
ATOM   11875 O  O   . VAL E  1 51  ? -6.818  -40.524 -14.497  1.00 204.18 ? 51   VAL E O   1 
ATOM   11876 C  CB  . VAL E  1 51  ? -6.780  -37.637 -13.448  1.00 256.79 ? 51   VAL E CB  1 
ATOM   11877 C  CG1 . VAL E  1 51  ? -5.809  -38.296 -12.481  1.00 258.42 ? 51   VAL E CG1 1 
ATOM   11878 C  CG2 . VAL E  1 51  ? -6.074  -37.243 -14.741  1.00 255.07 ? 51   VAL E CG2 1 
ATOM   11879 N  N   . GLU E  1 52  ? -8.237  -39.532 -15.954  1.00 220.35 ? 52   GLU E N   1 
ATOM   11880 C  CA  . GLU E  1 52  ? -7.980  -40.442 -17.075  1.00 209.35 ? 52   GLU E CA  1 
ATOM   11881 C  C   . GLU E  1 52  ? -8.173  -41.904 -16.680  1.00 203.18 ? 52   GLU E C   1 
ATOM   11882 O  O   . GLU E  1 52  ? -7.312  -42.755 -16.917  1.00 195.26 ? 52   GLU E O   1 
ATOM   11883 C  CB  . GLU E  1 52  ? -6.581  -40.229 -17.655  1.00 209.10 ? 52   GLU E CB  1 
ATOM   11884 C  CG  . GLU E  1 52  ? -6.396  -38.913 -18.374  1.00 227.28 ? 52   GLU E CG  1 
ATOM   11885 C  CD  . GLU E  1 52  ? -5.074  -38.841 -19.112  1.00 235.29 ? 52   GLU E CD  1 
ATOM   11886 O  OE1 . GLU E  1 52  ? -4.901  -37.908 -19.925  1.00 248.74 ? 52   GLU E OE1 1 
ATOM   11887 O  OE2 . GLU E  1 52  ? -4.209  -39.713 -18.880  1.00 225.63 ? 52   GLU E OE2 1 
ATOM   11888 N  N   . GLY E  1 53  ? -9.324  -42.196 -16.074  1.00 218.26 ? 53   GLY E N   1 
ATOM   11889 C  CA  . GLY E  1 53  ? -9.640  -43.572 -15.742  1.00 221.86 ? 53   GLY E CA  1 
ATOM   11890 C  C   . GLY E  1 53  ? -9.841  -44.444 -16.964  1.00 217.21 ? 53   GLY E C   1 
ATOM   11891 O  O   . GLY E  1 53  ? -9.597  -45.652 -16.915  1.00 214.82 ? 53   GLY E O   1 
ATOM   11892 N  N   . GLY E  1 54  ? -10.289 -43.857 -18.066  1.00 214.00 ? 54   GLY E N   1 
ATOM   11893 C  CA  . GLY E  1 54  ? -10.585 -44.607 -19.265  1.00 195.93 ? 54   GLY E CA  1 
ATOM   11894 C  C   . GLY E  1 54  ? -12.011 -45.131 -19.265  1.00 198.03 ? 54   GLY E C   1 
ATOM   11895 O  O   . GLY E  1 54  ? -12.635 -45.331 -18.225  1.00 214.03 ? 54   GLY E O   1 
ATOM   11896 N  N   . GLN E  1 55  ? -12.527 -45.375 -20.465  1.00 189.24 ? 55   GLN E N   1 
ATOM   11897 C  CA  . GLN E  1 55  ? -13.888 -45.874 -20.589  1.00 199.02 ? 55   GLN E CA  1 
ATOM   11898 C  C   . GLN E  1 55  ? -14.026 -46.694 -21.861  1.00 213.27 ? 55   GLN E C   1 
ATOM   11899 O  O   . GLN E  1 55  ? -13.175 -46.648 -22.755  1.00 209.17 ? 55   GLN E O   1 
ATOM   11900 C  CB  . GLN E  1 55  ? -14.914 -44.731 -20.583  1.00 197.55 ? 55   GLN E CB  1 
ATOM   11901 C  CG  . GLN E  1 55  ? -14.680 -43.662 -21.648  1.00 201.47 ? 55   GLN E CG  1 
ATOM   11902 C  CD  . GLN E  1 55  ? -15.605 -42.464 -21.492  1.00 210.11 ? 55   GLN E CD  1 
ATOM   11903 O  OE1 . GLN E  1 55  ? -16.381 -42.384 -20.541  1.00 213.14 ? 55   GLN E OE1 1 
ATOM   11904 N  NE2 . GLN E  1 55  ? -15.528 -41.529 -22.434  1.00 220.69 ? 55   GLN E NE2 1 
ATOM   11905 N  N   . VAL E  1 56  ? -15.117 -47.452 -21.925  1.00 228.00 ? 56   VAL E N   1 
ATOM   11906 C  CA  . VAL E  1 56  ? -15.495 -48.217 -23.106  1.00 219.70 ? 56   VAL E CA  1 
ATOM   11907 C  C   . VAL E  1 56  ? -16.817 -47.667 -23.617  1.00 220.37 ? 56   VAL E C   1 
ATOM   11908 O  O   . VAL E  1 56  ? -17.797 -47.600 -22.867  1.00 217.99 ? 56   VAL E O   1 
ATOM   11909 C  CB  . VAL E  1 56  ? -15.604 -49.720 -22.795  1.00 211.87 ? 56   VAL E CB  1 
ATOM   11910 C  CG1 . VAL E  1 56  ? -16.113 -50.475 -24.008  1.00 218.02 ? 56   VAL E CG1 1 
ATOM   11911 C  CG2 . VAL E  1 56  ? -14.253 -50.256 -22.363  1.00 201.86 ? 56   VAL E CG2 1 
ATOM   11912 N  N   . LEU E  1 57  ? -16.847 -47.289 -24.890  1.00 230.49 ? 57   LEU E N   1 
ATOM   11913 C  CA  . LEU E  1 57  ? -18.004 -46.619 -25.465  1.00 241.07 ? 57   LEU E CA  1 
ATOM   11914 C  C   . LEU E  1 57  ? -18.819 -47.578 -26.320  1.00 235.36 ? 57   LEU E C   1 
ATOM   11915 O  O   . LEU E  1 57  ? -18.268 -48.414 -27.043  1.00 225.16 ? 57   LEU E O   1 
ATOM   11916 C  CB  . LEU E  1 57  ? -17.585 -45.411 -26.306  1.00 244.37 ? 57   LEU E CB  1 
ATOM   11917 C  CG  . LEU E  1 57  ? -17.036 -44.189 -25.568  1.00 248.38 ? 57   LEU E CG  1 
ATOM   11918 C  CD1 . LEU E  1 57  ? -15.529 -44.299 -25.366  1.00 240.72 ? 57   LEU E CD1 1 
ATOM   11919 C  CD2 . LEU E  1 57  ? -17.392 -42.908 -26.309  1.00 253.22 ? 57   LEU E CD2 1 
ATOM   11920 N  N   . LYS E  1 58  ? -20.137 -47.440 -26.230  1.00 239.09 ? 58   LYS E N   1 
ATOM   11921 C  CA  . LYS E  1 58  ? -21.080 -48.186 -27.053  1.00 245.06 ? 58   LYS E CA  1 
ATOM   11922 C  C   . LYS E  1 58  ? -21.534 -47.257 -28.173  1.00 268.35 ? 58   LYS E C   1 
ATOM   11923 O  O   . LYS E  1 58  ? -22.252 -46.281 -27.925  1.00 288.62 ? 58   LYS E O   1 
ATOM   11924 C  CB  . LYS E  1 58  ? -22.259 -48.674 -26.211  1.00 249.53 ? 58   LYS E CB  1 
ATOM   11925 C  CG  . LYS E  1 58  ? -23.258 -49.561 -26.943  1.00 249.73 ? 58   LYS E CG  1 
ATOM   11926 C  CD  . LYS E  1 58  ? -24.557 -49.708 -26.143  1.00 247.14 ? 58   LYS E CD  1 
ATOM   11927 C  CE  . LYS E  1 58  ? -25.257 -48.361 -25.949  1.00 250.48 ? 58   LYS E CE  1 
ATOM   11928 N  NZ  . LYS E  1 58  ? -26.574 -48.473 -25.255  1.00 251.57 ? 58   LYS E NZ  1 
ATOM   11929 N  N   . CYS E  1 59  ? -21.110 -47.552 -29.398  1.00 263.23 ? 59   CYS E N   1 
ATOM   11930 C  CA  . CYS E  1 59  ? -21.470 -46.756 -30.562  1.00 263.06 ? 59   CYS E CA  1 
ATOM   11931 C  C   . CYS E  1 59  ? -22.523 -47.510 -31.362  1.00 254.20 ? 59   CYS E C   1 
ATOM   11932 O  O   . CYS E  1 59  ? -22.437 -48.733 -31.516  1.00 237.89 ? 59   CYS E O   1 
ATOM   11933 C  CB  . CYS E  1 59  ? -20.243 -46.466 -31.439  1.00 247.82 ? 59   CYS E CB  1 
ATOM   11934 S  SG  . CYS E  1 59  ? -18.884 -45.570 -30.621  1.00 249.97 ? 59   CYS E SG  1 
ATOM   11935 N  N   . ASP E  1 60  ? -23.507 -46.784 -31.885  1.00 267.34 ? 60   ASP E N   1 
ATOM   11936 C  CA  . ASP E  1 60  ? -24.617 -47.407 -32.591  1.00 261.76 ? 60   ASP E CA  1 
ATOM   11937 C  C   . ASP E  1 60  ? -24.374 -47.317 -34.091  1.00 239.85 ? 60   ASP E C   1 
ATOM   11938 O  O   . ASP E  1 60  ? -23.978 -46.265 -34.605  1.00 242.80 ? 60   ASP E O   1 
ATOM   11939 C  CB  . ASP E  1 60  ? -25.952 -46.759 -32.217  1.00 260.48 ? 60   ASP E CB  1 
ATOM   11940 C  CG  . ASP E  1 60  ? -27.119 -47.330 -33.006  1.00 257.81 ? 60   ASP E CG  1 
ATOM   11941 O  OD1 . ASP E  1 60  ? -27.189 -48.572 -33.130  1.00 264.29 ? 60   ASP E OD1 1 
ATOM   11942 O  OD2 . ASP E  1 60  ? -27.964 -46.546 -33.494  1.00 260.71 ? 60   ASP E OD2 1 
ATOM   11943 N  N   . TRP E  1 61  ? -24.609 -48.431 -34.782  1.00 245.42 ? 61   TRP E N   1 
ATOM   11944 C  CA  . TRP E  1 61  ? -24.509 -48.513 -36.232  1.00 246.76 ? 61   TRP E CA  1 
ATOM   11945 C  C   . TRP E  1 61  ? -25.805 -48.140 -36.944  1.00 265.37 ? 61   TRP E C   1 
ATOM   11946 O  O   . TRP E  1 61  ? -25.759 -47.457 -37.975  1.00 262.38 ? 61   TRP E O   1 
ATOM   11947 C  CB  . TRP E  1 61  ? -24.071 -49.922 -36.632  1.00 240.20 ? 61   TRP E CB  1 
ATOM   11948 C  CG  . TRP E  1 61  ? -24.383 -50.274 -38.050  1.00 245.12 ? 61   TRP E CG  1 
ATOM   11949 C  CD1 . TRP E  1 61  ? -25.176 -51.298 -38.481  1.00 252.60 ? 61   TRP E CD1 1 
ATOM   11950 C  CD2 . TRP E  1 61  ? -23.946 -49.583 -39.228  1.00 264.63 ? 61   TRP E CD2 1 
ATOM   11951 N  NE1 . TRP E  1 61  ? -25.244 -51.299 -39.853  1.00 271.53 ? 61   TRP E NE1 1 
ATOM   11952 C  CE2 . TRP E  1 61  ? -24.501 -50.255 -40.335  1.00 277.24 ? 61   TRP E CE2 1 
ATOM   11953 C  CE3 . TRP E  1 61  ? -23.135 -48.465 -39.454  1.00 269.40 ? 61   TRP E CE3 1 
ATOM   11954 C  CZ2 . TRP E  1 61  ? -24.271 -49.847 -41.649  1.00 283.44 ? 61   TRP E CZ2 1 
ATOM   11955 C  CZ3 . TRP E  1 61  ? -22.908 -48.061 -40.761  1.00 274.95 ? 61   TRP E CZ3 1 
ATOM   11956 C  CH2 . TRP E  1 61  ? -23.474 -48.752 -41.840  1.00 279.36 ? 61   TRP E CH2 1 
ATOM   11957 N  N   . SER E  1 62  ? -26.954 -48.575 -36.405  1.00 260.33 ? 62   SER E N   1 
ATOM   11958 C  CA  . SER E  1 62  ? -28.271 -48.450 -37.032  1.00 259.66 ? 62   SER E CA  1 
ATOM   11959 C  C   . SER E  1 62  ? -28.413 -47.166 -37.837  1.00 266.79 ? 62   SER E C   1 
ATOM   11960 O  O   . SER E  1 62  ? -28.873 -47.193 -38.982  1.00 271.23 ? 62   SER E O   1 
ATOM   11961 C  CB  . SER E  1 62  ? -29.375 -48.526 -35.970  1.00 263.77 ? 62   SER E CB  1 
ATOM   11962 O  OG  . SER E  1 62  ? -29.412 -47.367 -35.151  1.00 267.20 ? 62   SER E OG  1 
ATOM   11963 N  N   . SER E  1 63  ? -27.996 -46.048 -37.251  1.00 268.10 ? 63   SER E N   1 
ATOM   11964 C  CA  . SER E  1 63  ? -27.963 -44.759 -37.928  1.00 274.64 ? 63   SER E CA  1 
ATOM   11965 C  C   . SER E  1 63  ? -27.279 -43.768 -36.998  1.00 273.82 ? 63   SER E C   1 
ATOM   11966 O  O   . SER E  1 63  ? -26.973 -44.083 -35.845  1.00 269.31 ? 63   SER E O   1 
ATOM   11967 C  CB  . SER E  1 63  ? -29.367 -44.277 -38.303  1.00 285.32 ? 63   SER E CB  1 
ATOM   11968 O  OG  . SER E  1 63  ? -29.304 -43.149 -39.155  1.00 291.77 ? 63   SER E OG  1 
ATOM   11969 N  N   . THR E  1 64  ? -27.017 -42.570 -37.530  1.00 278.95 ? 64   THR E N   1 
ATOM   11970 C  CA  . THR E  1 64  ? -26.646 -41.388 -36.752  1.00 281.45 ? 64   THR E CA  1 
ATOM   11971 C  C   . THR E  1 64  ? -25.204 -41.413 -36.243  1.00 272.87 ? 64   THR E C   1 
ATOM   11972 O  O   . THR E  1 64  ? -24.634 -40.354 -35.953  1.00 274.84 ? 64   THR E O   1 
ATOM   11973 C  CB  . THR E  1 64  ? -27.617 -41.202 -35.578  1.00 285.75 ? 64   THR E CB  1 
ATOM   11974 O  OG1 . THR E  1 64  ? -28.949 -41.529 -35.996  1.00 292.19 ? 64   THR E OG1 1 
ATOM   11975 C  CG2 . THR E  1 64  ? -27.601 -39.767 -35.091  1.00 292.34 ? 64   THR E CG2 1 
ATOM   11976 N  N   . ARG E  1 65  ? -24.610 -42.606 -36.121  1.00 263.81 ? 65   ARG E N   1 
ATOM   11977 C  CA  . ARG E  1 65  ? -23.186 -42.779 -35.794  1.00 255.36 ? 65   ARG E CA  1 
ATOM   11978 C  C   . ARG E  1 65  ? -22.825 -42.243 -34.406  1.00 254.08 ? 65   ARG E C   1 
ATOM   11979 O  O   . ARG E  1 65  ? -21.669 -41.889 -34.156  1.00 249.88 ? 65   ARG E O   1 
ATOM   11980 C  CB  . ARG E  1 65  ? -22.287 -42.120 -36.842  1.00 255.77 ? 65   ARG E CB  1 
ATOM   11981 C  CG  . ARG E  1 65  ? -22.695 -42.368 -38.280  1.00 258.95 ? 65   ARG E CG  1 
ATOM   11982 C  CD  . ARG E  1 65  ? -22.137 -43.664 -38.804  1.00 251.10 ? 65   ARG E CD  1 
ATOM   11983 N  NE  . ARG E  1 65  ? -22.523 -43.882 -40.193  1.00 254.47 ? 65   ARG E NE  1 
ATOM   11984 C  CZ  . ARG E  1 65  ? -21.815 -43.470 -41.239  1.00 254.91 ? 65   ARG E CZ  1 
ATOM   11985 N  NH1 . ARG E  1 65  ? -20.675 -42.816 -41.062  1.00 252.22 ? 65   ARG E NH1 1 
ATOM   11986 N  NH2 . ARG E  1 65  ? -22.250 -43.717 -42.465  1.00 258.29 ? 65   ARG E NH2 1 
ATOM   11987 N  N   . ARG E  1 66  ? -23.786 -42.184 -33.483  1.00 269.69 ? 66   ARG E N   1 
ATOM   11988 C  CA  . ARG E  1 66  ? -23.559 -41.584 -32.171  1.00 265.04 ? 66   ARG E CA  1 
ATOM   11989 C  C   . ARG E  1 66  ? -23.083 -42.622 -31.159  1.00 255.19 ? 66   ARG E C   1 
ATOM   11990 O  O   . ARG E  1 66  ? -23.619 -43.732 -31.089  1.00 251.96 ? 66   ARG E O   1 
ATOM   11991 C  CB  . ARG E  1 66  ? -24.834 -40.913 -31.660  1.00 266.90 ? 66   ARG E CB  1 
ATOM   11992 C  CG  . ARG E  1 66  ? -25.170 -39.612 -32.354  1.00 276.22 ? 66   ARG E CG  1 
ATOM   11993 C  CD  . ARG E  1 66  ? -26.435 -39.020 -31.776  1.00 286.68 ? 66   ARG E CD  1 
ATOM   11994 N  NE  . ARG E  1 66  ? -26.760 -37.734 -32.380  1.00 305.20 ? 66   ARG E NE  1 
ATOM   11995 C  CZ  . ARG E  1 66  ? -27.875 -37.056 -32.131  1.00 313.31 ? 66   ARG E CZ  1 
ATOM   11996 N  NH1 . ARG E  1 66  ? -28.776 -37.547 -31.290  1.00 305.64 ? 66   ARG E NH1 1 
ATOM   11997 N  NH2 . ARG E  1 66  ? -28.092 -35.890 -32.724  1.00 321.68 ? 66   ARG E NH2 1 
ATOM   11998 N  N   . CYS E  1 67  ? -22.085 -42.242 -30.360  1.00 264.46 ? 67   CYS E N   1 
ATOM   11999 C  CA  . CYS E  1 67  ? -21.502 -43.108 -29.343  1.00 250.55 ? 67   CYS E CA  1 
ATOM   12000 C  C   . CYS E  1 67  ? -22.000 -42.737 -27.949  1.00 253.20 ? 67   CYS E C   1 
ATOM   12001 O  O   . CYS E  1 67  ? -22.213 -41.560 -27.639  1.00 266.53 ? 67   CYS E O   1 
ATOM   12002 C  CB  . CYS E  1 67  ? -19.975 -43.044 -29.385  1.00 260.23 ? 67   CYS E CB  1 
ATOM   12003 S  SG  . CYS E  1 67  ? -19.234 -43.591 -30.956  1.00 270.42 ? 67   CYS E SG  1 
ATOM   12004 N  N   . GLN E  1 68  ? -22.172 -43.754 -27.106  1.00 250.36 ? 68   GLN E N   1 
ATOM   12005 C  CA  . GLN E  1 68  ? -22.663 -43.576 -25.750  1.00 259.39 ? 68   GLN E CA  1 
ATOM   12006 C  C   . GLN E  1 68  ? -21.728 -44.290 -24.779  1.00 255.41 ? 68   GLN E C   1 
ATOM   12007 O  O   . GLN E  1 68  ? -21.387 -45.466 -25.001  1.00 253.61 ? 68   GLN E O   1 
ATOM   12008 C  CB  . GLN E  1 68  ? -24.095 -44.116 -25.627  1.00 256.74 ? 68   GLN E CB  1 
ATOM   12009 C  CG  . GLN E  1 68  ? -25.194 -43.083 -25.876  1.00 273.43 ? 68   GLN E CG  1 
ATOM   12010 C  CD  . GLN E  1 68  ? -25.134 -41.908 -24.912  1.00 277.59 ? 68   GLN E CD  1 
ATOM   12011 O  OE1 . GLN E  1 68  ? -24.665 -42.039 -23.781  1.00 267.71 ? 68   GLN E OE1 1 
ATOM   12012 N  NE2 . GLN E  1 68  ? -25.611 -40.751 -25.360  1.00 281.98 ? 68   GLN E NE2 1 
ATOM   12013 N  N   . PRO E  1 69  ? -21.268 -43.620 -23.720  1.00 247.66 ? 69   PRO E N   1 
ATOM   12014 C  CA  . PRO E  1 69  ? -20.400 -44.284 -22.738  1.00 238.65 ? 69   PRO E CA  1 
ATOM   12015 C  C   . PRO E  1 69  ? -21.113 -45.411 -21.999  1.00 242.12 ? 69   PRO E C   1 
ATOM   12016 O  O   . PRO E  1 69  ? -22.297 -45.313 -21.670  1.00 256.66 ? 69   PRO E O   1 
ATOM   12017 C  CB  . PRO E  1 69  ? -20.013 -43.148 -21.782  1.00 234.07 ? 69   PRO E CB  1 
ATOM   12018 C  CG  . PRO E  1 69  ? -20.238 -41.893 -22.555  1.00 235.66 ? 69   PRO E CG  1 
ATOM   12019 C  CD  . PRO E  1 69  ? -21.420 -42.183 -23.436  1.00 251.46 ? 69   PRO E CD  1 
ATOM   12020 N  N   . ILE E  1 70  ? -20.387 -46.501 -21.766  1.00 231.40 ? 70   ILE E N   1 
ATOM   12021 C  CA  . ILE E  1 70  ? -20.880 -47.611 -20.953  1.00 233.80 ? 70   ILE E CA  1 
ATOM   12022 C  C   . ILE E  1 70  ? -20.428 -47.408 -19.511  1.00 236.07 ? 70   ILE E C   1 
ATOM   12023 O  O   . ILE E  1 70  ? -19.224 -47.374 -19.231  1.00 218.92 ? 70   ILE E O   1 
ATOM   12024 C  CB  . ILE E  1 70  ? -20.383 -48.960 -21.489  1.00 215.08 ? 70   ILE E CB  1 
ATOM   12025 C  CG1 . ILE E  1 70  ? -20.786 -49.130 -22.949  1.00 216.32 ? 70   ILE E CG1 1 
ATOM   12026 C  CG2 . ILE E  1 70  ? -20.959 -50.089 -20.661  1.00 215.52 ? 70   ILE E CG2 1 
ATOM   12027 C  CD1 . ILE E  1 70  ? -20.310 -50.420 -23.564  1.00 221.45 ? 70   ILE E CD1 1 
ATOM   12028 N  N   . GLU E  1 71  ? -21.390 -47.285 -18.593  1.00 256.80 ? 71   GLU E N   1 
ATOM   12029 C  CA  . GLU E  1 71  ? -21.099 -47.076 -17.172  1.00 241.91 ? 71   GLU E CA  1 
ATOM   12030 C  C   . GLU E  1 71  ? -20.680 -48.395 -16.533  1.00 249.03 ? 71   GLU E C   1 
ATOM   12031 O  O   . GLU E  1 71  ? -21.512 -49.189 -16.090  1.00 266.43 ? 71   GLU E O   1 
ATOM   12032 C  CB  . GLU E  1 71  ? -22.301 -46.493 -16.444  1.00 229.75 ? 71   GLU E CB  1 
ATOM   12033 C  CG  . GLU E  1 71  ? -22.000 -46.117 -14.999  1.00 230.12 ? 71   GLU E CG  1 
ATOM   12034 C  CD  . GLU E  1 71  ? -23.211 -45.576 -14.268  1.00 267.13 ? 71   GLU E CD  1 
ATOM   12035 O  OE1 . GLU E  1 71  ? -24.309 -45.553 -14.865  1.00 289.56 ? 71   GLU E OE1 1 
ATOM   12036 O  OE2 . GLU E  1 71  ? -23.069 -45.189 -13.089  1.00 291.93 ? 71   GLU E OE2 1 
ATOM   12037 N  N   . PHE E  1 72  ? -19.368 -48.638 -16.485  1.00 220.98 ? 72   PHE E N   1 
ATOM   12038 C  CA  . PHE E  1 72  ? -18.839 -49.792 -15.769  1.00 208.39 ? 72   PHE E CA  1 
ATOM   12039 C  C   . PHE E  1 72  ? -18.635 -49.491 -14.291  1.00 226.67 ? 72   PHE E C   1 
ATOM   12040 O  O   . PHE E  1 72  ? -18.884 -50.351 -13.439  1.00 223.43 ? 72   PHE E O   1 
ATOM   12041 C  CB  . PHE E  1 72  ? -17.518 -50.246 -16.393  1.00 204.51 ? 72   PHE E CB  1 
ATOM   12042 C  CG  . PHE E  1 72  ? -17.681 -50.987 -17.692  1.00 226.23 ? 72   PHE E CG  1 
ATOM   12043 C  CD1 . PHE E  1 72  ? -17.925 -52.352 -17.702  1.00 230.31 ? 72   PHE E CD1 1 
ATOM   12044 C  CD2 . PHE E  1 72  ? -17.579 -50.322 -18.902  1.00 235.87 ? 72   PHE E CD2 1 
ATOM   12045 C  CE1 . PHE E  1 72  ? -18.071 -53.039 -18.895  1.00 217.91 ? 72   PHE E CE1 1 
ATOM   12046 C  CE2 . PHE E  1 72  ? -17.719 -51.006 -20.098  1.00 231.63 ? 72   PHE E CE2 1 
ATOM   12047 C  CZ  . PHE E  1 72  ? -17.970 -52.365 -20.093  1.00 215.79 ? 72   PHE E CZ  1 
ATOM   12048 N  N   . ASP E  1 73  ? -18.177 -48.282 -13.973  1.00 256.69 ? 73   ASP E N   1 
ATOM   12049 C  CA  . ASP E  1 73  ? -17.920 -47.900 -12.587  1.00 257.12 ? 73   ASP E CA  1 
ATOM   12050 C  C   . ASP E  1 73  ? -17.971 -46.385 -12.486  1.00 245.16 ? 73   ASP E C   1 
ATOM   12051 O  O   . ASP E  1 73  ? -17.238 -45.692 -13.199  1.00 260.77 ? 73   ASP E O   1 
ATOM   12052 C  CB  . ASP E  1 73  ? -16.564 -48.434 -12.120  1.00 241.40 ? 73   ASP E CB  1 
ATOM   12053 C  CG  . ASP E  1 73  ? -16.174 -47.913 -10.749  1.00 229.94 ? 73   ASP E CG  1 
ATOM   12054 O  OD1 . ASP E  1 73  ? -17.051 -47.847 -9.863   1.00 221.44 ? 73   ASP E OD1 1 
ATOM   12055 O  OD2 . ASP E  1 73  ? -14.988 -47.570 -10.558  1.00 228.46 ? 73   ASP E OD2 1 
ATOM   12056 N  N   . ALA E  1 74  ? -18.832 -45.870 -11.610  1.00 230.39 ? 74   ALA E N   1 
ATOM   12057 C  CA  . ALA E  1 74  ? -18.951 -44.435 -11.405  1.00 241.05 ? 74   ALA E CA  1 
ATOM   12058 C  C   . ALA E  1 74  ? -18.234 -43.953 -10.153  1.00 259.26 ? 74   ALA E C   1 
ATOM   12059 O  O   . ALA E  1 74  ? -18.110 -42.739 -9.956   1.00 272.32 ? 74   ALA E O   1 
ATOM   12060 C  CB  . ALA E  1 74  ? -20.430 -44.032 -11.335  1.00 251.90 ? 74   ALA E CB  1 
ATOM   12061 N  N   . THR E  1 75  ? -17.767 -44.866 -9.308   1.00 269.62 ? 75   THR E N   1 
ATOM   12062 C  CA  . THR E  1 75  ? -17.168 -44.518 -8.029   1.00 275.87 ? 75   THR E CA  1 
ATOM   12063 C  C   . THR E  1 75  ? -15.700 -44.122 -8.183   1.00 261.75 ? 75   THR E C   1 
ATOM   12064 O  O   . THR E  1 75  ? -15.044 -44.410 -9.188   1.00 247.43 ? 75   THR E O   1 
ATOM   12065 C  CB  . THR E  1 75  ? -17.289 -45.681 -7.045   1.00 273.39 ? 75   THR E CB  1 
ATOM   12066 O  OG1 . THR E  1 75  ? -16.413 -46.747 -7.443   1.00 270.44 ? 75   THR E OG1 1 
ATOM   12067 C  CG2 . THR E  1 75  ? -18.723 -46.194 -7.004   1.00 276.71 ? 75   THR E CG2 1 
ATOM   12068 N  N   . GLY E  1 76  ? -15.193 -43.442 -7.160   1.00 251.01 ? 76   GLY E N   1 
ATOM   12069 C  CA  . GLY E  1 76  ? -13.795 -43.071 -7.072   1.00 241.92 ? 76   GLY E CA  1 
ATOM   12070 C  C   . GLY E  1 76  ? -12.949 -44.136 -6.407   1.00 237.22 ? 76   GLY E C   1 
ATOM   12071 O  O   . GLY E  1 76  ? -13.236 -45.335 -6.485   1.00 228.40 ? 76   GLY E O   1 
ATOM   12072 N  N   . ASN E  1 77  ? -11.884 -43.691 -5.742   1.00 236.15 ? 77   ASN E N   1 
ATOM   12073 C  CA  . ASN E  1 77  ? -10.973 -44.594 -5.045   1.00 231.05 ? 77   ASN E CA  1 
ATOM   12074 C  C   . ASN E  1 77  ? -11.539 -44.978 -3.683   1.00 235.33 ? 77   ASN E C   1 
ATOM   12075 O  O   . ASN E  1 77  ? -11.762 -44.111 -2.830   1.00 247.17 ? 77   ASN E O   1 
ATOM   12076 C  CB  . ASN E  1 77  ? -9.605  -43.941 -4.880   1.00 238.71 ? 77   ASN E CB  1 
ATOM   12077 C  CG  . ASN E  1 77  ? -8.919  -43.700 -6.200   1.00 245.51 ? 77   ASN E CG  1 
ATOM   12078 O  OD1 . ASN E  1 77  ? -9.553  -43.732 -7.254   1.00 249.72 ? 77   ASN E OD1 1 
ATOM   12079 N  ND2 . ASN E  1 77  ? -7.615  -43.457 -6.155   1.00 247.57 ? 77   ASN E ND2 1 
ATOM   12080 N  N   . ARG E  1 78  ? -11.765 -46.272 -3.477   1.00 225.86 ? 78   ARG E N   1 
ATOM   12081 C  CA  . ARG E  1 78  ? -12.159 -46.756 -2.163   1.00 233.42 ? 78   ARG E CA  1 
ATOM   12082 C  C   . ARG E  1 78  ? -11.033 -46.548 -1.156   1.00 228.36 ? 78   ARG E C   1 
ATOM   12083 O  O   . ARG E  1 78  ? -9.848  -46.601 -1.494   1.00 221.27 ? 78   ARG E O   1 
ATOM   12084 C  CB  . ARG E  1 78  ? -12.541 -48.235 -2.227   1.00 230.73 ? 78   ARG E CB  1 
ATOM   12085 C  CG  . ARG E  1 78  ? -13.923 -48.493 -2.813   1.00 241.83 ? 78   ARG E CG  1 
ATOM   12086 C  CD  . ARG E  1 78  ? -14.168 -49.977 -3.053   1.00 244.99 ? 78   ARG E CD  1 
ATOM   12087 N  NE  . ARG E  1 78  ? -13.233 -50.544 -4.022   1.00 242.27 ? 78   ARG E NE  1 
ATOM   12088 C  CZ  . ARG E  1 78  ? -13.313 -51.779 -4.510   1.00 232.16 ? 78   ARG E CZ  1 
ATOM   12089 N  NH1 . ARG E  1 78  ? -14.288 -52.590 -4.123   1.00 232.29 ? 78   ARG E NH1 1 
ATOM   12090 N  NH2 . ARG E  1 78  ? -12.416 -52.207 -5.387   1.00 223.91 ? 78   ARG E NH2 1 
ATOM   12091 N  N   . ASP E  1 79  ? -11.419 -46.297 0.092    1.00 231.64 ? 79   ASP E N   1 
ATOM   12092 C  CA  . ASP E  1 79  ? -10.480 -46.140 1.196    1.00 232.68 ? 79   ASP E CA  1 
ATOM   12093 C  C   . ASP E  1 79  ? -10.352 -47.451 1.961    1.00 240.87 ? 79   ASP E C   1 
ATOM   12094 O  O   . ASP E  1 79  ? -11.363 -48.080 2.294    1.00 254.27 ? 79   ASP E O   1 
ATOM   12095 C  CB  . ASP E  1 79  ? -10.931 -45.029 2.148    1.00 226.68 ? 79   ASP E CB  1 
ATOM   12096 C  CG  . ASP E  1 79  ? -10.501 -43.649 1.692    1.00 227.19 ? 79   ASP E CG  1 
ATOM   12097 O  OD1 . ASP E  1 79  ? -9.327  -43.481 1.295    1.00 225.71 ? 79   ASP E OD1 1 
ATOM   12098 O  OD2 . ASP E  1 79  ? -11.340 -42.727 1.734    1.00 238.89 ? 79   ASP E OD2 1 
ATOM   12099 N  N   . TYR E  1 80  ? -9.110  -47.871 2.217    1.00 226.54 ? 80   TYR E N   1 
ATOM   12100 C  CA  . TYR E  1 80  ? -8.880  -48.931 3.194    1.00 219.78 ? 80   TYR E CA  1 
ATOM   12101 C  C   . TYR E  1 80  ? -9.097  -48.407 4.611    1.00 236.06 ? 80   TYR E C   1 
ATOM   12102 O  O   . TYR E  1 80  ? -9.726  -49.075 5.441    1.00 247.17 ? 80   TYR E O   1 
ATOM   12103 C  CB  . TYR E  1 80  ? -7.472  -49.509 3.023    1.00 206.96 ? 80   TYR E CB  1 
ATOM   12104 C  CG  . TYR E  1 80  ? -7.039  -50.479 4.105    1.00 208.04 ? 80   TYR E CG  1 
ATOM   12105 C  CD1 . TYR E  1 80  ? -7.315  -51.839 4.004    1.00 208.41 ? 80   TYR E CD1 1 
ATOM   12106 C  CD2 . TYR E  1 80  ? -6.347  -50.034 5.225    1.00 220.75 ? 80   TYR E CD2 1 
ATOM   12107 C  CE1 . TYR E  1 80  ? -6.915  -52.726 4.991    1.00 209.65 ? 80   TYR E CE1 1 
ATOM   12108 C  CE2 . TYR E  1 80  ? -5.947  -50.911 6.216    1.00 222.48 ? 80   TYR E CE2 1 
ATOM   12109 C  CZ  . TYR E  1 80  ? -6.231  -52.255 6.095    1.00 210.55 ? 80   TYR E CZ  1 
ATOM   12110 O  OH  . TYR E  1 80  ? -5.829  -53.125 7.084    1.00 211.53 ? 80   TYR E OH  1 
ATOM   12111 N  N   . ALA E  1 81  ? -8.594  -47.209 4.899    1.00 233.69 ? 81   ALA E N   1 
ATOM   12112 C  CA  . ALA E  1 81  ? -8.831  -46.544 6.170    1.00 223.92 ? 81   ALA E CA  1 
ATOM   12113 C  C   . ALA E  1 81  ? -8.809  -45.038 5.930    1.00 224.50 ? 81   ALA E C   1 
ATOM   12114 O  O   . ALA E  1 81  ? -8.616  -44.572 4.802    1.00 218.00 ? 81   ALA E O   1 
ATOM   12115 C  CB  . ALA E  1 81  ? -7.800  -46.972 7.218    1.00 220.81 ? 81   ALA E CB  1 
ATOM   12116 N  N   . LYS E  1 82  ? -9.027  -44.277 7.002    1.00 230.42 ? 82   LYS E N   1 
ATOM   12117 C  CA  . LYS E  1 82  ? -9.008  -42.820 6.909    1.00 226.79 ? 82   LYS E CA  1 
ATOM   12118 C  C   . LYS E  1 82  ? -7.636  -42.333 6.447    1.00 221.72 ? 82   LYS E C   1 
ATOM   12119 O  O   . LYS E  1 82  ? -6.607  -42.707 7.019    1.00 219.85 ? 82   LYS E O   1 
ATOM   12120 C  CB  . LYS E  1 82  ? -9.371  -42.202 8.260    1.00 215.55 ? 82   LYS E CB  1 
ATOM   12121 C  CG  . LYS E  1 82  ? -9.413  -40.684 8.252    1.00 220.78 ? 82   LYS E CG  1 
ATOM   12122 C  CD  . LYS E  1 82  ? -9.642  -40.117 9.642    1.00 226.68 ? 82   LYS E CD  1 
ATOM   12123 C  CE  . LYS E  1 82  ? -9.588  -38.597 9.621    1.00 233.54 ? 82   LYS E CE  1 
ATOM   12124 N  NZ  . LYS E  1 82  ? -9.689  -38.010 10.982   1.00 239.45 ? 82   LYS E NZ  1 
ATOM   12125 N  N   . ASP E  1 83  ? -7.632  -41.511 5.393    1.00 232.03 ? 83   ASP E N   1 
ATOM   12126 C  CA  . ASP E  1 83  ? -6.408  -40.990 4.773    1.00 230.82 ? 83   ASP E CA  1 
ATOM   12127 C  C   . ASP E  1 83  ? -5.522  -42.108 4.231    1.00 234.99 ? 83   ASP E C   1 
ATOM   12128 O  O   . ASP E  1 83  ? -4.304  -41.946 4.110    1.00 236.77 ? 83   ASP E O   1 
ATOM   12129 C  CB  . ASP E  1 83  ? -5.608  -40.109 5.739    1.00 234.05 ? 83   ASP E CB  1 
ATOM   12130 C  CG  . ASP E  1 83  ? -6.411  -38.936 6.261    1.00 248.11 ? 83   ASP E CG  1 
ATOM   12131 O  OD1 . ASP E  1 83  ? -6.566  -37.945 5.520    1.00 251.24 ? 83   ASP E OD1 1 
ATOM   12132 O  OD2 . ASP E  1 83  ? -6.872  -38.996 7.419    1.00 256.57 ? 83   ASP E OD2 1 
ATOM   12133 N  N   . ASP E  1 84  ? -6.123  -43.249 3.903    1.00 230.82 ? 84   ASP E N   1 
ATOM   12134 C  CA  . ASP E  1 84  ? -5.389  -44.419 3.419    1.00 236.86 ? 84   ASP E CA  1 
ATOM   12135 C  C   . ASP E  1 84  ? -6.135  -45.008 2.231    1.00 252.12 ? 84   ASP E C   1 
ATOM   12136 O  O   . ASP E  1 84  ? -6.949  -45.928 2.380    1.00 264.00 ? 84   ASP E O   1 
ATOM   12137 C  CB  . ASP E  1 84  ? -5.210  -45.449 4.537    1.00 226.59 ? 84   ASP E CB  1 
ATOM   12138 C  CG  . ASP E  1 84  ? -4.071  -46.412 4.272    1.00 224.03 ? 84   ASP E CG  1 
ATOM   12139 O  OD1 . ASP E  1 84  ? -3.119  -46.041 3.554    1.00 233.59 ? 84   ASP E OD1 1 
ATOM   12140 O  OD2 . ASP E  1 84  ? -4.125  -47.541 4.798    1.00 217.16 ? 84   ASP E OD2 1 
ATOM   12141 N  N   . PRO E  1 85  ? -5.914  -44.466 1.030    1.00 247.11 ? 85   PRO E N   1 
ATOM   12142 C  CA  . PRO E  1 85  ? -6.635  -44.956 -0.155   1.00 234.58 ? 85   PRO E CA  1 
ATOM   12143 C  C   . PRO E  1 85  ? -6.290  -46.405 -0.478   1.00 221.26 ? 85   PRO E C   1 
ATOM   12144 O  O   . PRO E  1 85  ? -5.125  -46.806 -0.452   1.00 218.85 ? 85   PRO E O   1 
ATOM   12145 C  CB  . PRO E  1 85  ? -6.172  -44.007 -1.269   1.00 220.58 ? 85   PRO E CB  1 
ATOM   12146 C  CG  . PRO E  1 85  ? -5.654  -42.794 -0.553   1.00 226.31 ? 85   PRO E CG  1 
ATOM   12147 C  CD  . PRO E  1 85  ? -5.052  -43.315 0.714    1.00 233.97 ? 85   PRO E CD  1 
ATOM   12148 N  N   . LEU E  1 86  ? -7.324  -47.190 -0.808   1.00 233.43 ? 86   LEU E N   1 
ATOM   12149 C  CA  . LEU E  1 86  ? -7.139  -48.611 -1.091   1.00 235.35 ? 86   LEU E CA  1 
ATOM   12150 C  C   . LEU E  1 86  ? -6.681  -48.882 -2.519   1.00 232.85 ? 86   LEU E C   1 
ATOM   12151 O  O   . LEU E  1 86  ? -5.921  -49.829 -2.752   1.00 224.57 ? 86   LEU E O   1 
ATOM   12152 C  CB  . LEU E  1 86  ? -8.439  -49.372 -0.827   1.00 237.11 ? 86   LEU E CB  1 
ATOM   12153 C  CG  . LEU E  1 86  ? -8.407  -50.850 -1.215   1.00 232.51 ? 86   LEU E CG  1 
ATOM   12154 C  CD1 . LEU E  1 86  ? -7.658  -51.661 -0.170   1.00 238.73 ? 86   LEU E CD1 1 
ATOM   12155 C  CD2 . LEU E  1 86  ? -9.809  -51.391 -1.432   1.00 236.50 ? 86   LEU E CD2 1 
ATOM   12156 N  N   . GLU E  1 87  ? -7.129  -48.084 -3.483   1.00 232.42 ? 87   GLU E N   1 
ATOM   12157 C  CA  . GLU E  1 87  ? -6.850  -48.351 -4.886   1.00 216.65 ? 87   GLU E CA  1 
ATOM   12158 C  C   . GLU E  1 87  ? -6.538  -47.048 -5.605   1.00 213.25 ? 87   GLU E C   1 
ATOM   12159 O  O   . GLU E  1 87  ? -6.769  -45.953 -5.088   1.00 229.03 ? 87   GLU E O   1 
ATOM   12160 C  CB  . GLU E  1 87  ? -8.028  -49.064 -5.553   1.00 216.86 ? 87   GLU E CB  1 
ATOM   12161 C  CG  . GLU E  1 87  ? -9.347  -48.341 -5.353   1.00 233.89 ? 87   GLU E CG  1 
ATOM   12162 C  CD  . GLU E  1 87  ? -10.543 -49.206 -5.683   1.00 245.75 ? 87   GLU E CD  1 
ATOM   12163 O  OE1 . GLU E  1 87  ? -10.341 -50.368 -6.095   1.00 247.64 ? 87   GLU E OE1 1 
ATOM   12164 O  OE2 . GLU E  1 87  ? -11.686 -48.726 -5.516   1.00 252.87 ? 87   GLU E OE2 1 
ATOM   12165 N  N   . PHE E  1 88  ? -6.012  -47.181 -6.823   1.00 201.85 ? 88   PHE E N   1 
ATOM   12166 C  CA  . PHE E  1 88  ? -5.647  -46.028 -7.649   1.00 204.63 ? 88   PHE E CA  1 
ATOM   12167 C  C   . PHE E  1 88  ? -6.148  -46.293 -9.064   1.00 207.17 ? 88   PHE E C   1 
ATOM   12168 O  O   . PHE E  1 88  ? -5.495  -46.997 -9.842   1.00 192.34 ? 88   PHE E O   1 
ATOM   12169 C  CB  . PHE E  1 88  ? -4.145  -45.778 -7.631   1.00 220.32 ? 88   PHE E CB  1 
ATOM   12170 C  CG  . PHE E  1 88  ? -3.561  -45.689 -6.251   1.00 230.19 ? 88   PHE E CG  1 
ATOM   12171 C  CD1 . PHE E  1 88  ? -3.486  -44.470 -5.598   1.00 227.69 ? 88   PHE E CD1 1 
ATOM   12172 C  CD2 . PHE E  1 88  ? -3.084  -46.820 -5.608   1.00 224.92 ? 88   PHE E CD2 1 
ATOM   12173 C  CE1 . PHE E  1 88  ? -2.948  -44.380 -4.328   1.00 223.03 ? 88   PHE E CE1 1 
ATOM   12174 C  CE2 . PHE E  1 88  ? -2.544  -46.737 -4.335   1.00 215.75 ? 88   PHE E CE2 1 
ATOM   12175 C  CZ  . PHE E  1 88  ? -2.476  -45.515 -3.696   1.00 220.75 ? 88   PHE E CZ  1 
ATOM   12176 N  N   . LYS E  1 89  ? -7.301  -45.715 -9.392   1.00 226.32 ? 89   LYS E N   1 
ATOM   12177 C  CA  . LYS E  1 89  ? -7.931  -45.902 -10.690  1.00 231.82 ? 89   LYS E CA  1 
ATOM   12178 C  C   . LYS E  1 89  ? -7.511  -44.840 -11.688  1.00 227.34 ? 89   LYS E C   1 
ATOM   12179 O  O   . LYS E  1 89  ? -7.861  -44.942 -12.867  1.00 236.65 ? 89   LYS E O   1 
ATOM   12180 C  CB  . LYS E  1 89  ? -9.460  -45.896 -10.546  1.00 236.53 ? 89   LYS E CB  1 
ATOM   12181 C  CG  . LYS E  1 89  ? -10.038 -47.119 -9.841   1.00 233.51 ? 89   LYS E CG  1 
ATOM   12182 C  CD  . LYS E  1 89  ? -11.528 -46.949 -9.584   1.00 237.00 ? 89   LYS E CD  1 
ATOM   12183 C  CE  . LYS E  1 89  ? -12.094 -48.123 -8.809   1.00 232.57 ? 89   LYS E CE  1 
ATOM   12184 N  NZ  . LYS E  1 89  ? -13.532 -47.920 -8.479   1.00 240.31 ? 89   LYS E NZ  1 
ATOM   12185 N  N   . SER E  1 90  ? -6.797  -43.815 -11.239  1.00 207.19 ? 90   SER E N   1 
ATOM   12186 C  CA  . SER E  1 90  ? -6.262  -42.821 -12.155  1.00 196.31 ? 90   SER E CA  1 
ATOM   12187 C  C   . SER E  1 90  ? -5.215  -43.465 -13.049  1.00 201.68 ? 90   SER E C   1 
ATOM   12188 O  O   . SER E  1 90  ? -4.363  -44.222 -12.575  1.00 200.32 ? 90   SER E O   1 
ATOM   12189 C  CB  . SER E  1 90  ? -5.652  -41.658 -11.378  1.00 200.05 ? 90   SER E CB  1 
ATOM   12190 O  OG  . SER E  1 90  ? -6.652  -40.926 -10.697  1.00 203.30 ? 90   SER E OG  1 
ATOM   12191 N  N   . HIS E  1 91  ? -5.290  -43.174 -14.349  1.00 212.55 ? 91   HIS E N   1 
ATOM   12192 C  CA  . HIS E  1 91  ? -4.349  -43.708 -15.337  1.00 216.39 ? 91   HIS E CA  1 
ATOM   12193 C  C   . HIS E  1 91  ? -4.321  -45.236 -15.333  1.00 206.76 ? 91   HIS E C   1 
ATOM   12194 O  O   . HIS E  1 91  ? -3.282  -45.852 -15.586  1.00 190.88 ? 91   HIS E O   1 
ATOM   12195 C  CB  . HIS E  1 91  ? -2.939  -43.155 -15.112  1.00 225.76 ? 91   HIS E CB  1 
ATOM   12196 C  CG  . HIS E  1 91  ? -2.884  -41.666 -14.970  1.00 231.41 ? 91   HIS E CG  1 
ATOM   12197 N  ND1 . HIS E  1 91  ? -3.158  -40.805 -16.010  1.00 226.55 ? 91   HIS E ND1 1 
ATOM   12198 C  CD2 . HIS E  1 91  ? -2.580  -40.885 -13.906  1.00 232.32 ? 91   HIS E CD2 1 
ATOM   12199 C  CE1 . HIS E  1 91  ? -3.027  -39.558 -15.594  1.00 219.06 ? 91   HIS E CE1 1 
ATOM   12200 N  NE2 . HIS E  1 91  ? -2.677  -39.579 -14.320  1.00 223.51 ? 91   HIS E NE2 1 
ATOM   12201 N  N   . GLN E  1 92  ? -5.468  -45.860 -15.067  1.00 207.63 ? 92   GLN E N   1 
ATOM   12202 C  CA  . GLN E  1 92  ? -5.545  -47.311 -14.997  1.00 203.85 ? 92   GLN E CA  1 
ATOM   12203 C  C   . GLN E  1 92  ? -5.714  -47.956 -16.363  1.00 199.13 ? 92   GLN E C   1 
ATOM   12204 O  O   . GLN E  1 92  ? -5.658  -49.187 -16.457  1.00 194.84 ? 92   GLN E O   1 
ATOM   12205 C  CB  . GLN E  1 92  ? -6.699  -47.743 -14.087  1.00 206.35 ? 92   GLN E CB  1 
ATOM   12206 C  CG  . GLN E  1 92  ? -8.088  -47.522 -14.675  1.00 211.75 ? 92   GLN E CG  1 
ATOM   12207 C  CD  . GLN E  1 92  ? -9.196  -47.854 -13.691  1.00 226.53 ? 92   GLN E CD  1 
ATOM   12208 O  OE1 . GLN E  1 92  ? -8.969  -48.538 -12.693  1.00 231.30 ? 92   GLN E OE1 1 
ATOM   12209 N  NE2 . GLN E  1 92  ? -10.402 -47.374 -13.969  1.00 234.01 ? 92   GLN E NE2 1 
ATOM   12210 N  N   . TRP E  1 93  ? -5.947  -47.160 -17.405  1.00 199.46 ? 93   TRP E N   1 
ATOM   12211 C  CA  . TRP E  1 93  ? -6.056  -47.664 -18.772  1.00 203.73 ? 93   TRP E CA  1 
ATOM   12212 C  C   . TRP E  1 93  ? -7.207  -48.661 -18.919  1.00 205.05 ? 93   TRP E C   1 
ATOM   12213 O  O   . TRP E  1 93  ? -7.078  -49.697 -19.575  1.00 204.07 ? 93   TRP E O   1 
ATOM   12214 C  CB  . TRP E  1 93  ? -4.732  -48.278 -19.230  1.00 196.44 ? 93   TRP E CB  1 
ATOM   12215 C  CG  . TRP E  1 93  ? -3.739  -47.264 -19.727  1.00 190.00 ? 93   TRP E CG  1 
ATOM   12216 C  CD1 . TRP E  1 93  ? -3.142  -46.263 -19.005  1.00 180.30 ? 93   TRP E CD1 1 
ATOM   12217 C  CD2 . TRP E  1 93  ? -3.221  -47.163 -21.058  1.00 198.46 ? 93   TRP E CD2 1 
ATOM   12218 N  NE1 . TRP E  1 93  ? -2.289  -45.544 -19.812  1.00 180.65 ? 93   TRP E NE1 1 
ATOM   12219 C  CE2 . TRP E  1 93  ? -2.320  -46.077 -21.076  1.00 195.25 ? 93   TRP E CE2 1 
ATOM   12220 C  CE3 . TRP E  1 93  ? -3.432  -47.885 -22.239  1.00 175.86 ? 93   TRP E CE3 1 
ATOM   12221 C  CZ2 . TRP E  1 93  ? -1.633  -45.700 -22.230  1.00 207.30 ? 93   TRP E CZ2 1 
ATOM   12222 C  CZ3 . TRP E  1 93  ? -2.751  -47.506 -23.381  1.00 174.88 ? 93   TRP E CZ3 1 
ATOM   12223 C  CH2 . TRP E  1 93  ? -1.863  -46.424 -23.369  1.00 184.01 ? 93   TRP E CH2 1 
ATOM   12224 N  N   . PHE E  1 94  ? -8.345  -48.343 -18.302  1.00 206.40 ? 94   PHE E N   1 
ATOM   12225 C  CA  . PHE E  1 94  ? -9.539  -49.159 -18.466  1.00 196.09 ? 94   PHE E CA  1 
ATOM   12226 C  C   . PHE E  1 94  ? -10.044 -49.034 -19.896  1.00 204.32 ? 94   PHE E C   1 
ATOM   12227 O  O   . PHE E  1 94  ? -10.269 -47.926 -20.395  1.00 197.52 ? 94   PHE E O   1 
ATOM   12228 C  CB  . PHE E  1 94  ? -10.622 -48.731 -17.477  1.00 196.78 ? 94   PHE E CB  1 
ATOM   12229 C  CG  . PHE E  1 94  ? -11.932 -49.453 -17.650  1.00 194.59 ? 94   PHE E CG  1 
ATOM   12230 C  CD1 . PHE E  1 94  ? -12.065 -50.779 -17.269  1.00 196.35 ? 94   PHE E CD1 1 
ATOM   12231 C  CD2 . PHE E  1 94  ? -13.035 -48.800 -18.178  1.00 203.89 ? 94   PHE E CD2 1 
ATOM   12232 C  CE1 . PHE E  1 94  ? -13.268 -51.444 -17.421  1.00 199.60 ? 94   PHE E CE1 1 
ATOM   12233 C  CE2 . PHE E  1 94  ? -14.240 -49.460 -18.331  1.00 210.92 ? 94   PHE E CE2 1 
ATOM   12234 C  CZ  . PHE E  1 94  ? -14.354 -50.785 -17.952  1.00 206.76 ? 94   PHE E CZ  1 
ATOM   12235 N  N   . GLY E  1 95  ? -10.227 -50.171 -20.554  1.00 209.10 ? 95   GLY E N   1 
ATOM   12236 C  CA  . GLY E  1 95  ? -10.539 -50.192 -21.962  1.00 204.49 ? 95   GLY E CA  1 
ATOM   12237 C  C   . GLY E  1 95  ? -9.356  -50.460 -22.858  1.00 181.63 ? 95   GLY E C   1 
ATOM   12238 O  O   . GLY E  1 95  ? -9.455  -50.233 -24.068  1.00 179.30 ? 95   GLY E O   1 
ATOM   12239 N  N   . ALA E  1 96  ? -8.230  -50.909 -22.300  1.00 179.99 ? 96   ALA E N   1 
ATOM   12240 C  CA  . ALA E  1 96  ? -7.087  -51.262 -23.130  1.00 194.73 ? 96   ALA E CA  1 
ATOM   12241 C  C   . ALA E  1 96  ? -7.330  -52.556 -23.895  1.00 204.21 ? 96   ALA E C   1 
ATOM   12242 O  O   . ALA E  1 96  ? -6.738  -52.765 -24.960  1.00 223.84 ? 96   ALA E O   1 
ATOM   12243 C  CB  . ALA E  1 96  ? -5.828  -51.374 -22.272  1.00 195.33 ? 96   ALA E CB  1 
ATOM   12244 N  N   . SER E  1 97  ? -8.183  -53.436 -23.371  1.00 182.81 ? 97   SER E N   1 
ATOM   12245 C  CA  . SER E  1 97  ? -8.582  -54.652 -24.070  1.00 173.44 ? 97   SER E CA  1 
ATOM   12246 C  C   . SER E  1 97  ? -10.068 -54.875 -23.845  1.00 175.58 ? 97   SER E C   1 
ATOM   12247 O  O   . SER E  1 97  ? -10.510 -54.969 -22.697  1.00 175.91 ? 97   SER E O   1 
ATOM   12248 C  CB  . SER E  1 97  ? -7.781  -55.851 -23.565  1.00 165.74 ? 97   SER E CB  1 
ATOM   12249 O  OG  . SER E  1 97  ? -8.134  -56.138 -22.225  1.00 168.60 ? 97   SER E OG  1 
ATOM   12250 N  N   . VAL E  1 98  ? -10.834 -54.986 -24.929  1.00 169.90 ? 98   VAL E N   1 
ATOM   12251 C  CA  . VAL E  1 98  ? -12.278 -55.192 -24.860  1.00 174.95 ? 98   VAL E CA  1 
ATOM   12252 C  C   . VAL E  1 98  ? -12.628 -56.466 -25.611  1.00 179.12 ? 98   VAL E C   1 
ATOM   12253 O  O   . VAL E  1 98  ? -12.219 -56.645 -26.764  1.00 195.94 ? 98   VAL E O   1 
ATOM   12254 C  CB  . VAL E  1 98  ? -13.061 -54.001 -25.439  1.00 175.55 ? 98   VAL E CB  1 
ATOM   12255 C  CG1 . VAL E  1 98  ? -14.554 -54.187 -25.196  1.00 180.54 ? 98   VAL E CG1 1 
ATOM   12256 C  CG2 . VAL E  1 98  ? -12.578 -52.692 -24.835  1.00 183.14 ? 98   VAL E CG2 1 
ATOM   12257 N  N   . ARG E  1 99  ? -13.388 -57.343 -24.960  1.00 180.74 ? 99   ARG E N   1 
ATOM   12258 C  CA  . ARG E  1 99  ? -13.814 -58.604 -25.550  1.00 185.64 ? 99   ARG E CA  1 
ATOM   12259 C  C   . ARG E  1 99  ? -15.271 -58.842 -25.189  1.00 191.75 ? 99   ARG E C   1 
ATOM   12260 O  O   . ARG E  1 99  ? -15.665 -58.649 -24.036  1.00 193.09 ? 99   ARG E O   1 
ATOM   12261 C  CB  . ARG E  1 99  ? -12.941 -59.769 -25.069  1.00 198.20 ? 99   ARG E CB  1 
ATOM   12262 C  CG  . ARG E  1 99  ? -11.584 -59.864 -25.759  1.00 201.92 ? 99   ARG E CG  1 
ATOM   12263 C  CD  . ARG E  1 99  ? -11.711 -59.937 -27.277  1.00 199.28 ? 99   ARG E CD  1 
ATOM   12264 N  NE  . ARG E  1 99  ? -11.439 -58.654 -27.918  1.00 204.30 ? 99   ARG E NE  1 
ATOM   12265 C  CZ  . ARG E  1 99  ? -10.238 -58.267 -28.338  1.00 194.58 ? 99   ARG E CZ  1 
ATOM   12266 N  NH1 . ARG E  1 99  ? -9.188  -59.061 -28.175  1.00 195.20 ? 99   ARG E NH1 1 
ATOM   12267 N  NH2 . ARG E  1 99  ? -10.083 -57.082 -28.914  1.00 184.09 ? 99   ARG E NH2 1 
ATOM   12268 N  N   . SER E  1 100 ? -16.064 -59.259 -26.175  1.00 200.29 ? 100  SER E N   1 
ATOM   12269 C  CA  . SER E  1 100 ? -17.504 -59.410 -26.016  1.00 211.17 ? 100  SER E CA  1 
ATOM   12270 C  C   . SER E  1 100 ? -17.956 -60.782 -26.495  1.00 229.01 ? 100  SER E C   1 
ATOM   12271 O  O   . SER E  1 100 ? -17.465 -61.293 -27.508  1.00 231.42 ? 100  SER E O   1 
ATOM   12272 C  CB  . SER E  1 100 ? -18.259 -58.320 -26.783  1.00 196.69 ? 100  SER E CB  1 
ATOM   12273 O  OG  . SER E  1 100 ? -19.638 -58.318 -26.464  1.00 201.24 ? 100  SER E OG  1 
ATOM   12274 N  N   . LYS E  1 101 ? -18.893 -61.376 -25.755  1.00 244.54 ? 101  LYS E N   1 
ATOM   12275 C  CA  . LYS E  1 101 ? -19.486 -62.666 -26.105  1.00 243.56 ? 101  LYS E CA  1 
ATOM   12276 C  C   . LYS E  1 101 ? -20.989 -62.581 -25.876  1.00 240.56 ? 101  LYS E C   1 
ATOM   12277 O  O   . LYS E  1 101 ? -21.443 -62.587 -24.728  1.00 230.56 ? 101  LYS E O   1 
ATOM   12278 C  CB  . LYS E  1 101 ? -18.873 -63.795 -25.278  1.00 241.15 ? 101  LYS E CB  1 
ATOM   12279 C  CG  . LYS E  1 101 ? -19.460 -65.168 -25.557  1.00 245.75 ? 101  LYS E CG  1 
ATOM   12280 C  CD  . LYS E  1 101 ? -18.872 -66.214 -24.623  1.00 243.95 ? 101  LYS E CD  1 
ATOM   12281 C  CE  . LYS E  1 101 ? -19.398 -67.606 -24.940  1.00 251.56 ? 101  LYS E CE  1 
ATOM   12282 N  NZ  . LYS E  1 101 ? -20.875 -67.701 -24.778  1.00 265.08 ? 101  LYS E NZ  1 
ATOM   12283 N  N   . GLN E  1 102 ? -21.757 -62.524 -26.964  1.00 243.69 ? 102  GLN E N   1 
ATOM   12284 C  CA  . GLN E  1 102 ? -23.222 -62.420 -26.926  1.00 253.23 ? 102  GLN E CA  1 
ATOM   12285 C  C   . GLN E  1 102 ? -23.599 -61.132 -26.205  1.00 261.57 ? 102  GLN E C   1 
ATOM   12286 O  O   . GLN E  1 102 ? -23.189 -60.048 -26.656  1.00 266.18 ? 102  GLN E O   1 
ATOM   12287 C  CB  . GLN E  1 102 ? -23.810 -63.677 -26.288  1.00 258.46 ? 102  GLN E CB  1 
ATOM   12288 C  CG  . GLN E  1 102 ? -23.431 -64.997 -26.896  1.00 261.14 ? 102  GLN E CG  1 
ATOM   12289 C  CD  . GLN E  1 102 ? -23.734 -66.136 -25.944  1.00 264.25 ? 102  GLN E CD  1 
ATOM   12290 O  OE1 . GLN E  1 102 ? -24.317 -65.927 -24.880  1.00 258.93 ? 102  GLN E OE1 1 
ATOM   12291 N  NE2 . GLN E  1 102 ? -23.363 -67.347 -26.329  1.00 268.01 ? 102  GLN E NE2 1 
ATOM   12292 N  N   . ASP E  1 103 ? -24.346 -61.195 -25.102  1.00 259.17 ? 103  ASP E N   1 
ATOM   12293 C  CA  . ASP E  1 103 ? -24.754 -60.036 -24.325  1.00 250.14 ? 103  ASP E CA  1 
ATOM   12294 C  C   . ASP E  1 103 ? -23.779 -59.732 -23.201  1.00 237.71 ? 103  ASP E C   1 
ATOM   12295 O  O   . ASP E  1 103 ? -24.122 -58.992 -22.272  1.00 234.48 ? 103  ASP E O   1 
ATOM   12296 C  CB  . ASP E  1 103 ? -26.162 -60.247 -23.762  1.00 248.23 ? 103  ASP E CB  1 
ATOM   12297 C  CG  . ASP E  1 103 ? -26.217 -61.360 -22.733  1.00 247.65 ? 103  ASP E CG  1 
ATOM   12298 O  OD1 . ASP E  1 103 ? -25.426 -62.320 -22.858  1.00 252.92 ? 103  ASP E OD1 1 
ATOM   12299 O  OD2 . ASP E  1 103 ? -27.053 -61.281 -21.806  1.00 242.76 ? 103  ASP E OD2 1 
ATOM   12300 N  N   . LYS E  1 104 ? -22.579 -60.301 -23.259  1.00 233.24 ? 104  LYS E N   1 
ATOM   12301 C  CA  . LYS E  1 104 ? -21.543 -60.098 -22.258  1.00 230.80 ? 104  LYS E CA  1 
ATOM   12302 C  C   . LYS E  1 104 ? -20.472 -59.177 -22.828  1.00 222.11 ? 104  LYS E C   1 
ATOM   12303 O  O   . LYS E  1 104 ? -20.020 -59.370 -23.962  1.00 218.64 ? 104  LYS E O   1 
ATOM   12304 C  CB  . LYS E  1 104 ? -20.928 -61.438 -21.850  1.00 232.46 ? 104  LYS E CB  1 
ATOM   12305 C  CG  . LYS E  1 104 ? -21.953 -62.476 -21.417  1.00 243.87 ? 104  LYS E CG  1 
ATOM   12306 C  CD  . LYS E  1 104 ? -21.305 -63.832 -21.191  1.00 246.19 ? 104  LYS E CD  1 
ATOM   12307 C  CE  . LYS E  1 104 ? -22.328 -64.870 -20.764  1.00 256.68 ? 104  LYS E CE  1 
ATOM   12308 N  NZ  . LYS E  1 104 ? -22.949 -64.524 -19.457  1.00 266.30 ? 104  LYS E NZ  1 
ATOM   12309 N  N   . ILE E  1 105 ? -20.066 -58.184 -22.043  1.00 222.97 ? 105  ILE E N   1 
ATOM   12310 C  CA  . ILE E  1 105 ? -18.991 -57.274 -22.420  1.00 217.94 ? 105  ILE E CA  1 
ATOM   12311 C  C   . ILE E  1 105 ? -17.961 -57.280 -21.304  1.00 220.61 ? 105  ILE E C   1 
ATOM   12312 O  O   . ILE E  1 105 ? -18.287 -56.965 -20.152  1.00 215.09 ? 105  ILE E O   1 
ATOM   12313 C  CB  . ILE E  1 105 ? -19.500 -55.849 -22.682  1.00 220.61 ? 105  ILE E CB  1 
ATOM   12314 C  CG1 . ILE E  1 105 ? -20.538 -55.856 -23.804  1.00 234.84 ? 105  ILE E CG1 1 
ATOM   12315 C  CG2 . ILE E  1 105 ? -18.341 -54.930 -23.023  1.00 211.24 ? 105  ILE E CG2 1 
ATOM   12316 C  CD1 . ILE E  1 105 ? -21.080 -54.490 -24.134  1.00 251.54 ? 105  ILE E CD1 1 
ATOM   12317 N  N   . LEU E  1 106 ? -16.725 -57.641 -21.641  1.00 221.69 ? 106  LEU E N   1 
ATOM   12318 C  CA  . LEU E  1 106 ? -15.627 -57.699 -20.686  1.00 213.42 ? 106  LEU E CA  1 
ATOM   12319 C  C   . LEU E  1 106 ? -14.587 -56.644 -21.043  1.00 219.49 ? 106  LEU E C   1 
ATOM   12320 O  O   . LEU E  1 106 ? -14.024 -56.665 -22.144  1.00 212.96 ? 106  LEU E O   1 
ATOM   12321 C  CB  . LEU E  1 106 ? -15.000 -59.093 -20.663  1.00 200.07 ? 106  LEU E CB  1 
ATOM   12322 C  CG  . LEU E  1 106 ? -13.795 -59.262 -19.737  1.00 195.56 ? 106  LEU E CG  1 
ATOM   12323 C  CD1 . LEU E  1 106 ? -14.210 -59.111 -18.282  1.00 195.30 ? 106  LEU E CD1 1 
ATOM   12324 C  CD2 . LEU E  1 106 ? -13.109 -60.600 -19.973  1.00 196.22 ? 106  LEU E CD2 1 
ATOM   12325 N  N   . ALA E  1 107 ? -14.343 -55.721 -20.114  1.00 216.69 ? 107  ALA E N   1 
ATOM   12326 C  CA  . ALA E  1 107 ? -13.319 -54.700 -20.270  1.00 201.65 ? 107  ALA E CA  1 
ATOM   12327 C  C   . ALA E  1 107 ? -12.395 -54.717 -19.062  1.00 196.24 ? 107  ALA E C   1 
ATOM   12328 O  O   . ALA E  1 107 ? -12.809 -55.058 -17.950  1.00 198.40 ? 107  ALA E O   1 
ATOM   12329 C  CB  . ALA E  1 107 ? -13.936 -53.311 -20.438  1.00 199.05 ? 107  ALA E CB  1 
ATOM   12330 N  N   . CYS E  1 108 ? -11.137 -54.337 -19.287  1.00 196.84 ? 108  CYS E N   1 
ATOM   12331 C  CA  . CYS E  1 108 ? -10.114 -54.456 -18.259  1.00 208.63 ? 108  CYS E CA  1 
ATOM   12332 C  C   . CYS E  1 108 ? -9.248  -53.204 -18.205  1.00 202.51 ? 108  CYS E C   1 
ATOM   12333 O  O   . CYS E  1 108 ? -9.158  -52.432 -19.165  1.00 187.15 ? 108  CYS E O   1 
ATOM   12334 C  CB  . CYS E  1 108 ? -9.243  -55.691 -18.489  1.00 210.65 ? 108  CYS E CB  1 
ATOM   12335 S  SG  . CYS E  1 108 ? -10.141 -57.259 -18.373  1.00 226.78 ? 108  CYS E SG  1 
ATOM   12336 N  N   . ALA E  1 109 ? -8.592  -53.030 -17.054  1.00 207.44 ? 109  ALA E N   1 
ATOM   12337 C  CA  . ALA E  1 109 ? -7.702  -51.904 -16.770  1.00 201.57 ? 109  ALA E CA  1 
ATOM   12338 C  C   . ALA E  1 109 ? -6.328  -52.447 -16.397  1.00 207.14 ? 109  ALA E C   1 
ATOM   12339 O  O   . ALA E  1 109 ? -6.060  -52.726 -15.215  1.00 214.19 ? 109  ALA E O   1 
ATOM   12340 C  CB  . ALA E  1 109 ? -8.270  -51.027 -15.657  1.00 198.67 ? 109  ALA E CB  1 
ATOM   12341 N  N   . PRO E  1 110 ? -5.434  -52.639 -17.375  1.00 209.23 ? 110  PRO E N   1 
ATOM   12342 C  CA  . PRO E  1 110 ? -4.126  -53.249 -17.076  1.00 195.81 ? 110  PRO E CA  1 
ATOM   12343 C  C   . PRO E  1 110 ? -3.239  -52.419 -16.161  1.00 203.11 ? 110  PRO E C   1 
ATOM   12344 O  O   . PRO E  1 110 ? -2.425  -52.992 -15.428  1.00 202.11 ? 110  PRO E O   1 
ATOM   12345 C  CB  . PRO E  1 110 ? -3.495  -53.416 -18.468  1.00 187.12 ? 110  PRO E CB  1 
ATOM   12346 C  CG  . PRO E  1 110 ? -4.659  -53.454 -19.407  1.00 193.62 ? 110  PRO E CG  1 
ATOM   12347 C  CD  . PRO E  1 110 ? -5.663  -52.504 -18.822  1.00 215.59 ? 110  PRO E CD  1 
ATOM   12348 N  N   . LEU E  1 111 ? -3.368  -51.092 -16.167  1.00 214.87 ? 111  LEU E N   1 
ATOM   12349 C  CA  . LEU E  1 111 ? -2.540  -50.236 -15.328  1.00 212.85 ? 111  LEU E CA  1 
ATOM   12350 C  C   . LEU E  1 111 ? -3.246  -49.820 -14.042  1.00 223.08 ? 111  LEU E C   1 
ATOM   12351 O  O   . LEU E  1 111 ? -2.860  -48.823 -13.419  1.00 233.71 ? 111  LEU E O   1 
ATOM   12352 C  CB  . LEU E  1 111 ? -2.080  -49.006 -16.111  1.00 212.95 ? 111  LEU E CB  1 
ATOM   12353 C  CG  . LEU E  1 111 ? -0.837  -49.264 -16.962  1.00 200.95 ? 111  LEU E CG  1 
ATOM   12354 C  CD1 . LEU E  1 111 ? -0.470  -48.036 -17.773  1.00 223.85 ? 111  LEU E CD1 1 
ATOM   12355 C  CD2 . LEU E  1 111 ? 0.323   -49.696 -16.084  1.00 175.81 ? 111  LEU E CD2 1 
ATOM   12356 N  N   . TYR E  1 112 ? -4.283  -50.555 -13.649  1.00 218.98 ? 112  TYR E N   1 
ATOM   12357 C  CA  . TYR E  1 112 ? -4.900  -50.377 -12.342  1.00 200.91 ? 112  TYR E CA  1 
ATOM   12358 C  C   . TYR E  1 112 ? -3.937  -50.812 -11.249  1.00 197.44 ? 112  TYR E C   1 
ATOM   12359 O  O   . TYR E  1 112 ? -3.434  -51.939 -11.261  1.00 199.21 ? 112  TYR E O   1 
ATOM   12360 C  CB  . TYR E  1 112 ? -6.199  -51.184 -12.269  1.00 188.67 ? 112  TYR E CB  1 
ATOM   12361 C  CG  . TYR E  1 112 ? -6.734  -51.434 -10.873  1.00 198.34 ? 112  TYR E CG  1 
ATOM   12362 C  CD1 . TYR E  1 112 ? -7.564  -50.513 -10.243  1.00 215.43 ? 112  TYR E CD1 1 
ATOM   12363 C  CD2 . TYR E  1 112 ? -6.434  -52.613 -10.197  1.00 201.29 ? 112  TYR E CD2 1 
ATOM   12364 C  CE1 . TYR E  1 112 ? -8.064  -50.753 -8.967   1.00 218.97 ? 112  TYR E CE1 1 
ATOM   12365 C  CE2 . TYR E  1 112 ? -6.927  -52.859 -8.926   1.00 206.93 ? 112  TYR E CE2 1 
ATOM   12366 C  CZ  . TYR E  1 112 ? -7.741  -51.928 -8.317   1.00 214.50 ? 112  TYR E CZ  1 
ATOM   12367 O  OH  . TYR E  1 112 ? -8.231  -52.177 -7.055   1.00 217.08 ? 112  TYR E OH  1 
ATOM   12368 N  N   . HIS E  1 113 ? -3.695  -49.922 -10.294  1.00 196.67 ? 113  HIS E N   1 
ATOM   12369 C  CA  . HIS E  1 113 ? -2.844  -50.216 -9.155   1.00 196.57 ? 113  HIS E CA  1 
ATOM   12370 C  C   . HIS E  1 113 ? -3.716  -50.452 -7.933   1.00 207.57 ? 113  HIS E C   1 
ATOM   12371 O  O   . HIS E  1 113 ? -4.801  -49.878 -7.803   1.00 217.46 ? 113  HIS E O   1 
ATOM   12372 C  CB  . HIS E  1 113 ? -1.855  -49.079 -8.869   1.00 195.11 ? 113  HIS E CB  1 
ATOM   12373 C  CG  . HIS E  1 113 ? -0.891  -48.817 -9.983   1.00 206.93 ? 113  HIS E CG  1 
ATOM   12374 N  ND1 . HIS E  1 113 ? -1.279  -48.264 -11.184  1.00 221.53 ? 113  HIS E ND1 1 
ATOM   12375 C  CD2 . HIS E  1 113 ? 0.443   -49.030 -10.080  1.00 210.75 ? 113  HIS E CD2 1 
ATOM   12376 C  CE1 . HIS E  1 113 ? -0.226  -48.151 -11.974  1.00 226.43 ? 113  HIS E CE1 1 
ATOM   12377 N  NE2 . HIS E  1 113 ? 0.831   -48.609 -11.328  1.00 222.31 ? 113  HIS E NE2 1 
ATOM   12378 N  N   . TRP E  1 114 ? -3.228  -51.291 -7.027   1.00 207.46 ? 114  TRP E N   1 
ATOM   12379 C  CA  . TRP E  1 114 ? -3.978  -51.596 -5.821   1.00 209.42 ? 114  TRP E CA  1 
ATOM   12380 C  C   . TRP E  1 114 ? -3.029  -51.690 -4.636   1.00 202.65 ? 114  TRP E C   1 
ATOM   12381 O  O   . TRP E  1 114 ? -1.954  -52.293 -4.726   1.00 198.13 ? 114  TRP E O   1 
ATOM   12382 C  CB  . TRP E  1 114 ? -4.782  -52.889 -5.988   1.00 216.62 ? 114  TRP E CB  1 
ATOM   12383 C  CG  . TRP E  1 114 ? -4.989  -53.662 -4.719   1.00 222.78 ? 114  TRP E CG  1 
ATOM   12384 C  CD1 . TRP E  1 114 ? -6.001  -53.497 -3.818   1.00 227.19 ? 114  TRP E CD1 1 
ATOM   12385 C  CD2 . TRP E  1 114 ? -4.192  -54.752 -4.228   1.00 217.32 ? 114  TRP E CD2 1 
ATOM   12386 N  NE1 . TRP E  1 114 ? -5.873  -54.397 -2.789   1.00 221.85 ? 114  TRP E NE1 1 
ATOM   12387 C  CE2 . TRP E  1 114 ? -4.773  -55.181 -3.018   1.00 221.15 ? 114  TRP E CE2 1 
ATOM   12388 C  CE3 . TRP E  1 114 ? -3.040  -55.398 -4.688   1.00 209.81 ? 114  TRP E CE3 1 
ATOM   12389 C  CZ2 . TRP E  1 114 ? -4.242  -56.224 -2.263   1.00 219.87 ? 114  TRP E CZ2 1 
ATOM   12390 C  CZ3 . TRP E  1 114 ? -2.516  -56.435 -3.938   1.00 206.66 ? 114  TRP E CZ3 1 
ATOM   12391 C  CH2 . TRP E  1 114 ? -3.116  -56.837 -2.739   1.00 212.05 ? 114  TRP E CH2 1 
ATOM   12392 N  N   . ARG E  1 115 ? -3.437  -51.070 -3.531   1.00 219.27 ? 115  ARG E N   1 
ATOM   12393 C  CA  . ARG E  1 115 ? -2.615  -50.998 -2.333   1.00 216.51 ? 115  ARG E CA  1 
ATOM   12394 C  C   . ARG E  1 115 ? -2.785  -52.276 -1.531   1.00 218.90 ? 115  ARG E C   1 
ATOM   12395 O  O   . ARG E  1 115 ? -3.889  -52.826 -1.449   1.00 228.06 ? 115  ARG E O   1 
ATOM   12396 C  CB  . ARG E  1 115 ? -3.016  -49.790 -1.481   1.00 217.53 ? 115  ARG E CB  1 
ATOM   12397 C  CG  . ARG E  1 115 ? -2.418  -49.783 -0.083   1.00 221.40 ? 115  ARG E CG  1 
ATOM   12398 C  CD  . ARG E  1 115 ? -3.229  -48.878 0.837    1.00 219.60 ? 115  ARG E CD  1 
ATOM   12399 N  NE  . ARG E  1 115 ? -2.712  -48.858 2.202    1.00 216.33 ? 115  ARG E NE  1 
ATOM   12400 C  CZ  . ARG E  1 115 ? -2.993  -49.775 3.121    1.00 220.64 ? 115  ARG E CZ  1 
ATOM   12401 N  NH1 . ARG E  1 115 ? -3.792  -50.788 2.827    1.00 232.38 ? 115  ARG E NH1 1 
ATOM   12402 N  NH2 . ARG E  1 115 ? -2.474  -49.682 4.337    1.00 219.48 ? 115  ARG E NH2 1 
ATOM   12403 N  N   . THR E  1 116 ? -1.687  -52.763 -0.962   1.00 209.25 ? 116  THR E N   1 
ATOM   12404 C  CA  . THR E  1 116 ? -1.732  -54.057 -0.306   1.00 210.83 ? 116  THR E CA  1 
ATOM   12405 C  C   . THR E  1 116 ? -2.630  -53.960 0.923    1.00 224.60 ? 116  THR E C   1 
ATOM   12406 O  O   . THR E  1 116 ? -2.809  -52.885 1.498    1.00 237.79 ? 116  THR E O   1 
ATOM   12407 C  CB  . THR E  1 116 ? -0.314  -54.485 0.101    1.00 212.53 ? 116  THR E CB  1 
ATOM   12408 O  OG1 . THR E  1 116 ? 0.534   -54.465 -1.056   1.00 210.46 ? 116  THR E OG1 1 
ATOM   12409 C  CG2 . THR E  1 116 ? -0.293  -55.887 0.681    1.00 215.16 ? 116  THR E CG2 1 
ATOM   12410 N  N   . GLU E  1 117 ? -3.172  -55.095 1.349    1.00 227.04 ? 117  GLU E N   1 
ATOM   12411 C  CA  . GLU E  1 117 ? -4.056  -55.125 2.505    1.00 227.60 ? 117  GLU E CA  1 
ATOM   12412 C  C   . GLU E  1 117 ? -3.277  -55.431 3.770    1.00 220.95 ? 117  GLU E C   1 
ATOM   12413 O  O   . GLU E  1 117 ? -3.853  -55.492 4.862    1.00 222.82 ? 117  GLU E O   1 
ATOM   12414 C  CB  . GLU E  1 117 ? -5.174  -56.157 2.285    1.00 228.63 ? 117  GLU E CB  1 
ATOM   12415 C  CG  . GLU E  1 117 ? -6.419  -55.921 3.130    1.00 235.59 ? 117  GLU E CG  1 
ATOM   12416 C  CD  . GLU E  1 117 ? -7.556  -56.872 2.798    1.00 232.61 ? 117  GLU E CD  1 
ATOM   12417 O  OE1 . GLU E  1 117 ? -7.358  -57.786 1.967    1.00 221.42 ? 117  GLU E OE1 1 
ATOM   12418 O  OE2 . GLU E  1 117 ? -8.661  -56.675 3.346    1.00 245.71 ? 117  GLU E OE2 1 
ATOM   12419 N  N   . MET E  1 118 ? -1.973  -55.613 3.628    1.00 226.78 ? 118  MET E N   1 
ATOM   12420 C  CA  . MET E  1 118 ? -1.035  -55.834 4.713    1.00 235.74 ? 118  MET E CA  1 
ATOM   12421 C  C   . MET E  1 118 ? -0.239  -54.581 5.039    1.00 234.03 ? 118  MET E C   1 
ATOM   12422 O  O   . MET E  1 118 ? -0.017  -54.284 6.218    1.00 242.82 ? 118  MET E O   1 
ATOM   12423 C  CB  . MET E  1 118 ? -0.082  -56.974 4.338    1.00 245.06 ? 118  MET E CB  1 
ATOM   12424 C  CG  . MET E  1 118 ? -0.749  -58.347 4.288    1.00 255.39 ? 118  MET E CG  1 
ATOM   12425 S  SD  . MET E  1 118 ? 0.172   -59.545 3.293    1.00 281.20 ? 118  MET E SD  1 
ATOM   12426 C  CE  . MET E  1 118 ? -0.979  -60.918 3.248    1.00 264.57 ? 118  MET E CE  1 
ATOM   12427 N  N   . LYS E  1 119 ? 0.155   -53.818 4.016    1.00 231.50 ? 119  LYS E N   1 
ATOM   12428 C  CA  . LYS E  1 119 ? 0.912   -52.580 4.175    1.00 227.74 ? 119  LYS E CA  1 
ATOM   12429 C  C   . LYS E  1 119 ? 0.555   -51.641 3.024    1.00 217.43 ? 119  LYS E C   1 
ATOM   12430 O  O   . LYS E  1 119 ? -0.254  -51.970 2.152    1.00 226.94 ? 119  LYS E O   1 
ATOM   12431 C  CB  . LYS E  1 119 ? 2.422   -52.849 4.230    1.00 228.79 ? 119  LYS E CB  1 
ATOM   12432 C  CG  . LYS E  1 119 ? 2.880   -53.569 5.495    1.00 236.39 ? 119  LYS E CG  1 
ATOM   12433 C  CD  . LYS E  1 119 ? 4.389   -53.718 5.600    1.00 235.12 ? 119  LYS E CD  1 
ATOM   12434 C  CE  . LYS E  1 119 ? 4.755   -54.355 6.939    1.00 241.62 ? 119  LYS E CE  1 
ATOM   12435 N  NZ  . LYS E  1 119 ? 6.221   -54.530 7.127    1.00 246.57 ? 119  LYS E NZ  1 
ATOM   12436 N  N   . GLN E  1 120 ? 1.168   -50.455 3.026    1.00 198.91 ? 120  GLN E N   1 
ATOM   12437 C  CA  . GLN E  1 120 ? 0.846   -49.391 2.066    1.00 197.76 ? 120  GLN E CA  1 
ATOM   12438 C  C   . GLN E  1 120 ? 1.728   -49.493 0.824    1.00 196.67 ? 120  GLN E C   1 
ATOM   12439 O  O   . GLN E  1 120 ? 2.803   -48.899 0.752    1.00 196.71 ? 120  GLN E O   1 
ATOM   12440 C  CB  . GLN E  1 120 ? 0.992   -48.025 2.718    1.00 198.13 ? 120  GLN E CB  1 
ATOM   12441 C  CG  . GLN E  1 120 ? -0.086  -47.690 3.740    1.00 215.71 ? 120  GLN E CG  1 
ATOM   12442 C  CD  . GLN E  1 120 ? 0.214   -46.412 4.492    1.00 228.26 ? 120  GLN E CD  1 
ATOM   12443 O  OE1 . GLN E  1 120 ? 1.039   -45.610 4.057    1.00 229.60 ? 120  GLN E OE1 1 
ATOM   12444 N  NE2 . GLN E  1 120 ? -0.466  -46.204 5.617    1.00 236.50 ? 120  GLN E NE2 1 
ATOM   12445 N  N   . GLU E  1 121 ? 1.273   -50.257 -0.171   1.00 210.68 ? 121  GLU E N   1 
ATOM   12446 C  CA  . GLU E  1 121 ? 1.932   -50.338 -1.468   1.00 217.80 ? 121  GLU E CA  1 
ATOM   12447 C  C   . GLU E  1 121 ? 1.050   -49.745 -2.569   1.00 209.65 ? 121  GLU E C   1 
ATOM   12448 O  O   . GLU E  1 121 ? -0.027  -49.194 -2.311   1.00 205.49 ? 121  GLU E O   1 
ATOM   12449 C  CB  . GLU E  1 121 ? 2.325   -51.783 -1.787   1.00 219.93 ? 121  GLU E CB  1 
ATOM   12450 C  CG  . GLU E  1 121 ? 3.339   -52.400 -0.831   1.00 217.86 ? 121  GLU E CG  1 
ATOM   12451 C  CD  . GLU E  1 121 ? 4.722   -51.772 -0.967   1.00 218.77 ? 121  GLU E CD  1 
ATOM   12452 O  OE1 . GLU E  1 121 ? 5.532   -51.899 -0.025   1.00 231.60 ? 121  GLU E OE1 1 
ATOM   12453 O  OE2 . GLU E  1 121 ? 5.001   -51.152 -2.016   1.00 211.18 ? 121  GLU E OE2 1 
ATOM   12454 N  N   . ARG E  1 122 ? 1.529   -49.845 -3.817   1.00 215.02 ? 122  ARG E N   1 
ATOM   12455 C  CA  . ARG E  1 122 ? 0.816   -49.394 -5.014   1.00 216.03 ? 122  ARG E CA  1 
ATOM   12456 C  C   . ARG E  1 122 ? 1.192   -50.375 -6.129   1.00 212.22 ? 122  ARG E C   1 
ATOM   12457 O  O   . ARG E  1 122 ? 2.054   -50.116 -6.973   1.00 205.55 ? 122  ARG E O   1 
ATOM   12458 C  CB  . ARG E  1 122 ? 1.166   -47.954 -5.390   1.00 220.67 ? 122  ARG E CB  1 
ATOM   12459 C  CG  . ARG E  1 122 ? 0.286   -47.363 -6.484   1.00 221.75 ? 122  ARG E CG  1 
ATOM   12460 C  CD  . ARG E  1 122 ? 0.455   -45.851 -6.597   1.00 218.73 ? 122  ARG E CD  1 
ATOM   12461 N  NE  . ARG E  1 122 ? -0.576  -45.248 -7.439   1.00 216.38 ? 122  ARG E NE  1 
ATOM   12462 C  CZ  . ARG E  1 122 ? -0.468  -45.087 -8.753   1.00 203.73 ? 122  ARG E CZ  1 
ATOM   12463 N  NH1 . ARG E  1 122 ? 0.627   -45.484 -9.385   1.00 199.15 ? 122  ARG E NH1 1 
ATOM   12464 N  NH2 . ARG E  1 122 ? -1.458  -44.530 -9.438   1.00 202.27 ? 122  ARG E NH2 1 
ATOM   12465 N  N   . GLU E  1 123 ? 0.524   -51.523 -6.128   1.00 211.30 ? 123  GLU E N   1 
ATOM   12466 C  CA  . GLU E  1 123 ? 0.926   -52.627 -6.977   1.00 202.01 ? 123  GLU E CA  1 
ATOM   12467 C  C   . GLU E  1 123 ? -0.075  -52.835 -8.098   1.00 195.61 ? 123  GLU E C   1 
ATOM   12468 O  O   . GLU E  1 123 ? -1.268  -53.039 -7.834   1.00 201.12 ? 123  GLU E O   1 
ATOM   12469 C  CB  . GLU E  1 123 ? 1.054   -53.904 -6.146   1.00 209.77 ? 123  GLU E CB  1 
ATOM   12470 C  CG  . GLU E  1 123 ? 2.082   -53.792 -5.039   1.00 223.58 ? 123  GLU E CG  1 
ATOM   12471 C  CD  . GLU E  1 123 ? 2.265   -55.085 -4.278   1.00 226.01 ? 123  GLU E CD  1 
ATOM   12472 O  OE1 . GLU E  1 123 ? 3.218   -55.167 -3.473   1.00 241.79 ? 123  GLU E OE1 1 
ATOM   12473 O  OE2 . GLU E  1 123 ? 1.466   -56.022 -4.495   1.00 211.46 ? 123  GLU E OE2 1 
ATOM   12474 N  N   . PRO E  1 124 ? 0.350   -52.813 -9.284   1.00 186.65 ? 124  PRO E N   1 
ATOM   12475 C  CA  . PRO E  1 124 ? -0.555  -52.928 -10.450  1.00 182.59 ? 124  PRO E CA  1 
ATOM   12476 C  C   . PRO E  1 124 ? -1.063  -54.343 -10.716  1.00 182.26 ? 124  PRO E C   1 
ATOM   12477 O  O   . PRO E  1 124 ? -0.585  -55.073 -11.579  1.00 191.36 ? 124  PRO E O   1 
ATOM   12478 C  CB  . PRO E  1 124 ? 0.315   -52.412 -11.598  1.00 177.83 ? 124  PRO E CB  1 
ATOM   12479 C  CG  . PRO E  1 124 ? 1.703   -52.727 -11.184  1.00 179.99 ? 124  PRO E CG  1 
ATOM   12480 C  CD  . PRO E  1 124 ? 1.748   -52.581 -9.689   1.00 186.37 ? 124  PRO E CD  1 
ATOM   12481 N  N   . VAL E  1 125 ? -2.068  -54.756 -9.941   1.00 190.04 ? 125  VAL E N   1 
ATOM   12482 C  CA  . VAL E  1 125 ? -2.615  -56.101 -10.097  1.00 194.58 ? 125  VAL E CA  1 
ATOM   12483 C  C   . VAL E  1 125 ? -3.626  -56.195 -11.231  1.00 190.60 ? 125  VAL E C   1 
ATOM   12484 O  O   . VAL E  1 125 ? -3.971  -57.308 -11.649  1.00 193.02 ? 125  VAL E O   1 
ATOM   12485 C  CB  . VAL E  1 125 ? -3.268  -56.587 -8.794   1.00 202.53 ? 125  VAL E CB  1 
ATOM   12486 C  CG1 . VAL E  1 125 ? -2.214  -56.765 -7.721   1.00 197.45 ? 125  VAL E CG1 1 
ATOM   12487 C  CG2 . VAL E  1 125 ? -4.345  -55.614 -8.347   1.00 203.40 ? 125  VAL E CG2 1 
ATOM   12488 N  N   . GLY E  1 126 ? -4.134  -55.070 -11.723  1.00 194.56 ? 126  GLY E N   1 
ATOM   12489 C  CA  . GLY E  1 126 ? -5.132  -55.091 -12.773  1.00 190.30 ? 126  GLY E CA  1 
ATOM   12490 C  C   . GLY E  1 126 ? -6.505  -55.532 -12.312  1.00 193.82 ? 126  GLY E C   1 
ATOM   12491 O  O   . GLY E  1 126 ? -6.637  -56.343 -11.390  1.00 200.27 ? 126  GLY E O   1 
ATOM   12492 N  N   . THR E  1 127 ? -7.542  -55.003 -12.956  1.00 185.36 ? 127  THR E N   1 
ATOM   12493 C  CA  . THR E  1 127 ? -8.912  -55.357 -12.627  1.00 189.48 ? 127  THR E CA  1 
ATOM   12494 C  C   . THR E  1 127 ? -9.771  -55.288 -13.880  1.00 199.41 ? 127  THR E C   1 
ATOM   12495 O  O   . THR E  1 127 ? -9.450  -54.569 -14.830  1.00 201.13 ? 127  THR E O   1 
ATOM   12496 C  CB  . THR E  1 127 ? -9.484  -54.437 -11.549  1.00 204.54 ? 127  THR E CB  1 
ATOM   12497 O  OG1 . THR E  1 127 ? -10.761 -54.932 -11.129  1.00 211.88 ? 127  THR E OG1 1 
ATOM   12498 C  CG2 . THR E  1 127 ? -9.638  -53.020 -12.085  1.00 214.37 ? 127  THR E CG2 1 
ATOM   12499 N  N   . CYS E  1 128 ? -10.859 -56.053 -13.880  1.00 213.31 ? 128  CYS E N   1 
ATOM   12500 C  CA  . CYS E  1 128 ? -11.808 -56.055 -14.983  1.00 216.04 ? 128  CYS E CA  1 
ATOM   12501 C  C   . CYS E  1 128 ? -13.225 -55.829 -14.471  1.00 210.54 ? 128  CYS E C   1 
ATOM   12502 O  O   . CYS E  1 128 ? -13.550 -56.156 -13.326  1.00 212.34 ? 128  CYS E O   1 
ATOM   12503 C  CB  . CYS E  1 128 ? -11.745 -57.363 -15.764  1.00 205.16 ? 128  CYS E CB  1 
ATOM   12504 S  SG  . CYS E  1 128 ? -10.094 -57.721 -16.392  1.00 203.02 ? 128  CYS E SG  1 
ATOM   12505 N  N   . PHE E  1 129 ? -14.059 -55.244 -15.326  1.00 195.74 ? 129  PHE E N   1 
ATOM   12506 C  CA  . PHE E  1 129 ? -15.488 -55.123 -15.076  1.00 205.96 ? 129  PHE E CA  1 
ATOM   12507 C  C   . PHE E  1 129 ? -16.274 -55.918 -16.116  1.00 210.10 ? 129  PHE E C   1 
ATOM   12508 O  O   . PHE E  1 129 ? -16.039 -55.777 -17.322  1.00 199.85 ? 129  PHE E O   1 
ATOM   12509 C  CB  . PHE E  1 129 ? -15.910 -53.656 -15.074  1.00 218.50 ? 129  PHE E CB  1 
ATOM   12510 C  CG  . PHE E  1 129 ? -15.430 -52.899 -13.868  1.00 224.40 ? 129  PHE E CG  1 
ATOM   12511 C  CD1 . PHE E  1 129 ? -16.170 -52.898 -12.697  1.00 227.65 ? 129  PHE E CD1 1 
ATOM   12512 C  CD2 . PHE E  1 129 ? -14.231 -52.205 -13.897  1.00 216.83 ? 129  PHE E CD2 1 
ATOM   12513 C  CE1 . PHE E  1 129 ? -15.735 -52.207 -11.586  1.00 221.91 ? 129  PHE E CE1 1 
ATOM   12514 C  CE2 . PHE E  1 129 ? -13.790 -51.510 -12.785  1.00 211.64 ? 129  PHE E CE2 1 
ATOM   12515 C  CZ  . PHE E  1 129 ? -14.543 -51.513 -11.629  1.00 212.57 ? 129  PHE E CZ  1 
ATOM   12516 N  N   . LEU E  1 130 ? -17.202 -56.748 -15.643  1.00 232.31 ? 130  LEU E N   1 
ATOM   12517 C  CA  . LEU E  1 130 ? -18.044 -57.592 -16.485  1.00 230.85 ? 130  LEU E CA  1 
ATOM   12518 C  C   . LEU E  1 130 ? -19.495 -57.131 -16.403  1.00 240.83 ? 130  LEU E C   1 
ATOM   12519 O  O   . LEU E  1 130 ? -20.025 -56.929 -15.305  1.00 234.46 ? 130  LEU E O   1 
ATOM   12520 C  CB  . LEU E  1 130 ? -17.938 -59.058 -16.064  1.00 227.33 ? 130  LEU E CB  1 
ATOM   12521 C  CG  . LEU E  1 130 ? -18.858 -60.028 -16.807  1.00 232.05 ? 130  LEU E CG  1 
ATOM   12522 C  CD1 . LEU E  1 130 ? -18.574 -60.004 -18.297  1.00 224.20 ? 130  LEU E CD1 1 
ATOM   12523 C  CD2 . LEU E  1 130 ? -18.720 -61.433 -16.249  1.00 239.78 ? 130  LEU E CD2 1 
ATOM   12524 N  N   . GLN E  1 131 ? -20.136 -56.975 -17.564  1.00 246.63 ? 131  GLN E N   1 
ATOM   12525 C  CA  . GLN E  1 131 ? -21.519 -56.510 -17.661  1.00 250.43 ? 131  GLN E CA  1 
ATOM   12526 C  C   . GLN E  1 131 ? -22.385 -57.550 -18.362  1.00 249.01 ? 131  GLN E C   1 
ATOM   12527 O  O   . GLN E  1 131 ? -22.254 -57.765 -19.573  1.00 265.19 ? 131  GLN E O   1 
ATOM   12528 C  CB  . GLN E  1 131 ? -21.603 -55.175 -18.394  1.00 242.52 ? 131  GLN E CB  1 
ATOM   12529 C  CG  . GLN E  1 131 ? -23.008 -54.600 -18.435  1.00 228.48 ? 131  GLN E CG  1 
ATOM   12530 C  CD  . GLN E  1 131 ? -23.027 -53.148 -18.838  1.00 228.50 ? 131  GLN E CD  1 
ATOM   12531 O  OE1 . GLN E  1 131 ? -21.981 -52.512 -18.948  1.00 217.14 ? 131  GLN E OE1 1 
ATOM   12532 N  NE2 . GLN E  1 131 ? -24.218 -52.617 -19.084  1.00 245.35 ? 131  GLN E NE2 1 
ATOM   12533 N  N   . ASP E  1 132 ? -23.257 -58.207 -17.606  1.00 245.91 ? 132  ASP E N   1 
ATOM   12534 C  CA  . ASP E  1 132 ? -24.234 -59.128 -18.186  1.00 248.09 ? 132  ASP E CA  1 
ATOM   12535 C  C   . ASP E  1 132 ? -25.621 -58.489 -18.187  1.00 251.75 ? 132  ASP E C   1 
ATOM   12536 O  O   . ASP E  1 132 ? -26.574 -58.998 -17.598  1.00 261.69 ? 132  ASP E O   1 
ATOM   12537 C  CB  . ASP E  1 132 ? -24.233 -60.453 -17.430  1.00 257.47 ? 132  ASP E CB  1 
ATOM   12538 C  CG  . ASP E  1 132 ? -25.036 -61.529 -18.146  1.00 264.06 ? 132  ASP E CG  1 
ATOM   12539 O  OD1 . ASP E  1 132 ? -24.520 -62.132 -19.116  1.00 269.69 ? 132  ASP E OD1 1 
ATOM   12540 O  OD2 . ASP E  1 132 ? -26.184 -61.775 -17.723  1.00 260.19 ? 132  ASP E OD2 1 
ATOM   12541 N  N   . GLY E  1 133 ? -25.709 -57.337 -18.846  1.00 248.59 ? 133  GLY E N   1 
ATOM   12542 C  CA  . GLY E  1 133 ? -26.958 -56.614 -18.926  1.00 266.66 ? 133  GLY E CA  1 
ATOM   12543 C  C   . GLY E  1 133 ? -26.980 -55.433 -17.982  1.00 267.86 ? 133  GLY E C   1 
ATOM   12544 O  O   . GLY E  1 133 ? -26.457 -54.355 -18.289  1.00 268.70 ? 133  GLY E O   1 
ATOM   12545 N  N   . THR E  1 134 ? -27.591 -55.634 -16.816  1.00 259.18 ? 134  THR E N   1 
ATOM   12546 C  CA  . THR E  1 134 ? -27.696 -54.601 -15.796  1.00 257.43 ? 134  THR E CA  1 
ATOM   12547 C  C   . THR E  1 134 ? -26.611 -54.735 -14.740  1.00 239.63 ? 134  THR E C   1 
ATOM   12548 O  O   . THR E  1 134 ? -25.930 -53.758 -14.417  1.00 234.84 ? 134  THR E O   1 
ATOM   12549 C  CB  . THR E  1 134 ? -29.070 -54.655 -15.111  1.00 277.75 ? 134  THR E CB  1 
ATOM   12550 O  OG1 . THR E  1 134 ? -29.145 -55.823 -14.280  1.00 275.75 ? 134  THR E OG1 1 
ATOM   12551 C  CG2 . THR E  1 134 ? -30.193 -54.695 -16.135  1.00 283.57 ? 134  THR E CG2 1 
ATOM   12552 N  N   . LYS E  1 135 ? -26.430 -55.940 -14.213  1.00 236.36 ? 135  LYS E N   1 
ATOM   12553 C  CA  . LYS E  1 135 ? -25.476 -56.157 -13.138  1.00 239.25 ? 135  LYS E CA  1 
ATOM   12554 C  C   . LYS E  1 135 ? -24.057 -55.961 -13.651  1.00 236.74 ? 135  LYS E C   1 
ATOM   12555 O  O   . LYS E  1 135 ? -23.689 -56.476 -14.712  1.00 231.99 ? 135  LYS E O   1 
ATOM   12556 C  CB  . LYS E  1 135 ? -25.657 -57.559 -12.563  1.00 244.69 ? 135  LYS E CB  1 
ATOM   12557 C  CG  . LYS E  1 135 ? -27.086 -57.851 -12.111  1.00 257.22 ? 135  LYS E CG  1 
ATOM   12558 C  CD  . LYS E  1 135 ? -27.490 -57.000 -10.914  1.00 257.02 ? 135  LYS E CD  1 
ATOM   12559 C  CE  . LYS E  1 135 ? -28.963 -57.193 -10.562  1.00 255.83 ? 135  LYS E CE  1 
ATOM   12560 N  NZ  . LYS E  1 135 ? -29.344 -58.625 -10.407  1.00 252.99 ? 135  LYS E NZ  1 
ATOM   12561 N  N   . THR E  1 136 ? -23.272 -55.179 -12.914  1.00 245.06 ? 136  THR E N   1 
ATOM   12562 C  CA  . THR E  1 136 ? -21.862 -54.959 -13.212  1.00 241.41 ? 136  THR E CA  1 
ATOM   12563 C  C   . THR E  1 136 ? -21.023 -55.468 -12.046  1.00 252.01 ? 136  THR E C   1 
ATOM   12564 O  O   . THR E  1 136 ? -21.213 -55.031 -10.905  1.00 271.56 ? 136  THR E O   1 
ATOM   12565 C  CB  . THR E  1 136 ? -21.591 -53.477 -13.469  1.00 229.15 ? 136  THR E CB  1 
ATOM   12566 O  OG1 . THR E  1 136 ? -22.355 -53.042 -14.602  1.00 222.46 ? 136  THR E OG1 1 
ATOM   12567 C  CG2 . THR E  1 136 ? -20.116 -53.254 -13.740  1.00 210.39 ? 136  THR E CG2 1 
ATOM   12568 N  N   . VAL E  1 137 ? -20.089 -56.379 -12.330  1.00 226.21 ? 137  VAL E N   1 
ATOM   12569 C  CA  . VAL E  1 137 ? -19.245 -56.974 -11.301  1.00 217.56 ? 137  VAL E CA  1 
ATOM   12570 C  C   . VAL E  1 137 ? -17.789 -56.653 -11.606  1.00 214.98 ? 137  VAL E C   1 
ATOM   12571 O  O   . VAL E  1 137 ? -17.413 -56.351 -12.740  1.00 215.19 ? 137  VAL E O   1 
ATOM   12572 C  CB  . VAL E  1 137 ? -19.439 -58.500 -11.177  1.00 219.92 ? 137  VAL E CB  1 
ATOM   12573 C  CG1 . VAL E  1 137 ? -20.896 -58.842 -10.946  1.00 231.05 ? 137  VAL E CG1 1 
ATOM   12574 C  CG2 . VAL E  1 137 ? -18.913 -59.207 -12.414  1.00 218.82 ? 137  VAL E CG2 1 
ATOM   12575 N  N   . GLU E  1 138 ? -16.966 -56.728 -10.566  1.00 213.14 ? 138  GLU E N   1 
ATOM   12576 C  CA  . GLU E  1 138 ? -15.526 -56.548 -10.667  1.00 204.45 ? 138  GLU E CA  1 
ATOM   12577 C  C   . GLU E  1 138 ? -14.827 -57.903 -10.702  1.00 204.80 ? 138  GLU E C   1 
ATOM   12578 O  O   . GLU E  1 138 ? -15.304 -58.884 -10.122  1.00 209.40 ? 138  GLU E O   1 
ATOM   12579 C  CB  . GLU E  1 138 ? -15.009 -55.712 -9.496   1.00 210.27 ? 138  GLU E CB  1 
ATOM   12580 C  CG  . GLU E  1 138 ? -13.602 -55.168 -9.660   1.00 202.41 ? 138  GLU E CG  1 
ATOM   12581 C  CD  . GLU E  1 138 ? -13.155 -54.354 -8.458   1.00 205.50 ? 138  GLU E CD  1 
ATOM   12582 O  OE1 . GLU E  1 138 ? -13.806 -54.457 -7.396   1.00 203.05 ? 138  GLU E OE1 1 
ATOM   12583 O  OE2 . GLU E  1 138 ? -12.148 -53.623 -8.568   1.00 204.82 ? 138  GLU E OE2 1 
ATOM   12584 N  N   . TYR E  1 139 ? -13.687 -57.952 -11.393  1.00 215.50 ? 139  TYR E N   1 
ATOM   12585 C  CA  . TYR E  1 139 ? -12.915 -59.190 -11.541  1.00 225.34 ? 139  TYR E CA  1 
ATOM   12586 C  C   . TYR E  1 139 ? -11.425 -58.864 -11.487  1.00 223.10 ? 139  TYR E C   1 
ATOM   12587 O  O   . TYR E  1 139 ? -10.863 -58.332 -12.450  1.00 215.29 ? 139  TYR E O   1 
ATOM   12588 C  CB  . TYR E  1 139 ? -13.271 -59.906 -12.835  1.00 229.12 ? 139  TYR E CB  1 
ATOM   12589 C  CG  . TYR E  1 139 ? -12.480 -61.171 -13.055  1.00 223.08 ? 139  TYR E CG  1 
ATOM   12590 C  CD1 . TYR E  1 139 ? -12.542 -62.220 -12.147  1.00 235.64 ? 139  TYR E CD1 1 
ATOM   12591 C  CD2 . TYR E  1 139 ? -11.663 -61.312 -14.165  1.00 217.49 ? 139  TYR E CD2 1 
ATOM   12592 C  CE1 . TYR E  1 139 ? -11.817 -63.379 -12.346  1.00 240.85 ? 139  TYR E CE1 1 
ATOM   12593 C  CE2 . TYR E  1 139 ? -10.935 -62.466 -14.373  1.00 219.64 ? 139  TYR E CE2 1 
ATOM   12594 C  CZ  . TYR E  1 139 ? -11.014 -63.496 -13.462  1.00 228.34 ? 139  TYR E CZ  1 
ATOM   12595 O  OH  . TYR E  1 139 ? -10.286 -64.644 -13.671  1.00 223.55 ? 139  TYR E OH  1 
ATOM   12596 N  N   . ALA E  1 140 ? -10.789 -59.190 -10.361  1.00 230.42 ? 140  ALA E N   1 
ATOM   12597 C  CA  . ALA E  1 140 ? -9.357  -58.965 -10.155  1.00 235.76 ? 140  ALA E CA  1 
ATOM   12598 C  C   . ALA E  1 140 ? -8.727  -60.229 -9.582   1.00 234.16 ? 140  ALA E C   1 
ATOM   12599 O  O   . ALA E  1 140 ? -8.508  -60.332 -8.365   1.00 224.56 ? 140  ALA E O   1 
ATOM   12600 C  CB  . ALA E  1 140 ? -9.114  -57.764 -9.241   1.00 233.39 ? 140  ALA E CB  1 
ATOM   12601 N  N   . PRO E  1 141 ? -8.416  -61.215 -10.433  1.00 230.47 ? 141  PRO E N   1 
ATOM   12602 C  CA  . PRO E  1 141 ? -7.852  -62.480 -9.931   1.00 231.47 ? 141  PRO E CA  1 
ATOM   12603 C  C   . PRO E  1 141 ? -6.421  -62.362 -9.443   1.00 224.69 ? 141  PRO E C   1 
ATOM   12604 O  O   . PRO E  1 141 ? -5.930  -63.291 -8.786   1.00 230.91 ? 141  PRO E O   1 
ATOM   12605 C  CB  . PRO E  1 141 ? -7.943  -63.410 -11.149  1.00 215.23 ? 141  PRO E CB  1 
ATOM   12606 C  CG  . PRO E  1 141 ? -7.851  -62.488 -12.310  1.00 204.85 ? 141  PRO E CG  1 
ATOM   12607 C  CD  . PRO E  1 141 ? -8.572  -61.226 -11.898  1.00 214.37 ? 141  PRO E CD  1 
ATOM   12608 N  N   . CYS E  1 142 ? -5.733  -61.268 -9.765   1.00 203.35 ? 142  CYS E N   1 
ATOM   12609 C  CA  . CYS E  1 142 ? -4.375  -61.019 -9.311   1.00 193.74 ? 142  CYS E CA  1 
ATOM   12610 C  C   . CYS E  1 142 ? -4.332  -60.143 -8.069   1.00 198.10 ? 142  CYS E C   1 
ATOM   12611 O  O   . CYS E  1 142 ? -3.264  -59.989 -7.464   1.00 202.91 ? 142  CYS E O   1 
ATOM   12612 C  CB  . CYS E  1 142 ? -3.573  -60.378 -10.445  1.00 186.44 ? 142  CYS E CB  1 
ATOM   12613 S  SG  . CYS E  1 142 ? -3.132  -61.602 -11.703  1.00 183.93 ? 142  CYS E SG  1 
ATOM   12614 N  N   . ARG E  1 143 ? -5.460  -59.538 -7.706   1.00 198.23 ? 143  ARG E N   1 
ATOM   12615 C  CA  . ARG E  1 143 ? -5.612  -58.804 -6.454   1.00 209.35 ? 143  ARG E CA  1 
ATOM   12616 C  C   . ARG E  1 143 ? -5.816  -59.825 -5.338   1.00 224.18 ? 143  ARG E C   1 
ATOM   12617 O  O   . ARG E  1 143 ? -6.936  -60.099 -4.899   1.00 237.08 ? 143  ARG E O   1 
ATOM   12618 C  CB  . ARG E  1 143 ? -6.788  -57.843 -6.551   1.00 212.56 ? 143  ARG E CB  1 
ATOM   12619 C  CG  . ARG E  1 143 ? -6.879  -56.822 -5.441   1.00 219.37 ? 143  ARG E CG  1 
ATOM   12620 C  CD  . ARG E  1 143 ? -8.050  -55.881 -5.682   1.00 220.15 ? 143  ARG E CD  1 
ATOM   12621 N  NE  . ARG E  1 143 ? -9.334  -56.574 -5.603   1.00 217.54 ? 143  ARG E NE  1 
ATOM   12622 C  CZ  . ARG E  1 143 ? -10.469 -56.100 -6.104   1.00 216.77 ? 143  ARG E CZ  1 
ATOM   12623 N  NH1 . ARG E  1 143 ? -10.480 -54.928 -6.722   1.00 209.15 ? 143  ARG E NH1 1 
ATOM   12624 N  NH2 . ARG E  1 143 ? -11.594 -56.793 -5.982   1.00 223.60 ? 143  ARG E NH2 1 
ATOM   12625 N  N   . SER E  1 144 ? -4.712  -60.416 -4.887   1.00 220.45 ? 144  SER E N   1 
ATOM   12626 C  CA  . SER E  1 144 ? -4.751  -61.498 -3.910   1.00 228.22 ? 144  SER E CA  1 
ATOM   12627 C  C   . SER E  1 144 ? -3.881  -61.154 -2.699   1.00 246.78 ? 144  SER E C   1 
ATOM   12628 O  O   . SER E  1 144 ? -3.414  -60.022 -2.537   1.00 254.17 ? 144  SER E O   1 
ATOM   12629 C  CB  . SER E  1 144 ? -4.301  -62.812 -4.556   1.00 217.30 ? 144  SER E CB  1 
ATOM   12630 O  OG  . SER E  1 144 ? -4.500  -63.921 -3.692   1.00 221.23 ? 144  SER E OG  1 
ATOM   12631 N  N   . GLN E  1 145 ? -3.650  -62.162 -1.853   1.00 265.26 ? 145  GLN E N   1 
ATOM   12632 C  CA  . GLN E  1 145 ? -2.720  -62.051 -0.736   1.00 262.17 ? 145  GLN E CA  1 
ATOM   12633 C  C   . GLN E  1 145 ? -1.301  -62.403 -1.154   1.00 249.41 ? 145  GLN E C   1 
ATOM   12634 O  O   . GLN E  1 145 ? -0.363  -62.201 -0.374   1.00 252.58 ? 145  GLN E O   1 
ATOM   12635 C  CB  . GLN E  1 145 ? -3.157  -62.968 0.421    1.00 256.79 ? 145  GLN E CB  1 
ATOM   12636 C  CG  . GLN E  1 145 ? -4.616  -62.829 0.877    1.00 248.60 ? 145  GLN E CG  1 
ATOM   12637 C  CD  . GLN E  1 145 ? -5.024  -61.401 1.196    1.00 240.73 ? 145  GLN E CD  1 
ATOM   12638 O  OE1 . GLN E  1 145 ? -6.063  -60.926 0.737    1.00 239.34 ? 145  GLN E OE1 1 
ATOM   12639 N  NE2 . GLN E  1 145 ? -4.222  -60.720 2.007    1.00 234.86 ? 145  GLN E NE2 1 
ATOM   12640 N  N   . ASP E  1 146 ? -1.136  -62.925 -2.370   1.00 217.40 ? 146  ASP E N   1 
ATOM   12641 C  CA  . ASP E  1 146 ? 0.171   -63.179 -2.969   1.00 205.73 ? 146  ASP E CA  1 
ATOM   12642 C  C   . ASP E  1 146 ? 0.687   -61.846 -3.496   1.00 201.06 ? 146  ASP E C   1 
ATOM   12643 O  O   . ASP E  1 146 ? 0.533   -61.492 -4.667   1.00 200.06 ? 146  ASP E O   1 
ATOM   12644 C  CB  . ASP E  1 146 ? 0.063   -64.226 -4.069   1.00 208.54 ? 146  ASP E CB  1 
ATOM   12645 C  CG  . ASP E  1 146 ? 1.418   -64.658 -4.599   1.00 218.33 ? 146  ASP E CG  1 
ATOM   12646 O  OD1 . ASP E  1 146 ? 2.426   -64.518 -3.874   1.00 210.45 ? 146  ASP E OD1 1 
ATOM   12647 O  OD2 . ASP E  1 146 ? 1.470   -65.141 -5.750   1.00 226.71 ? 146  ASP E OD2 1 
ATOM   12648 N  N   . ILE E  1 147 ? 1.277   -61.076 -2.587   1.00 201.26 ? 147  ILE E N   1 
ATOM   12649 C  CA  . ILE E  1 147 ? 1.642   -59.694 -2.874   1.00 207.64 ? 147  ILE E CA  1 
ATOM   12650 C  C   . ILE E  1 147 ? 3.081   -59.602 -3.366   1.00 205.71 ? 147  ILE E C   1 
ATOM   12651 O  O   . ILE E  1 147 ? 3.779   -60.616 -3.489   1.00 200.34 ? 147  ILE E O   1 
ATOM   12652 C  CB  . ILE E  1 147 ? 1.437   -58.806 -1.634   1.00 216.61 ? 147  ILE E CB  1 
ATOM   12653 C  CG1 . ILE E  1 147 ? 2.447   -59.180 -0.546   1.00 211.40 ? 147  ILE E CG1 1 
ATOM   12654 C  CG2 . ILE E  1 147 ? 0.009   -58.937 -1.127   1.00 214.14 ? 147  ILE E CG2 1 
ATOM   12655 C  CD1 . ILE E  1 147 ? 2.294   -58.400 0.734    1.00 205.99 ? 147  ILE E CD1 1 
ATOM   12656 N  N   . ASP E  1 148 ? 3.516   -58.373 -3.658   1.00 208.20 ? 148  ASP E N   1 
ATOM   12657 C  CA  . ASP E  1 148 ? 4.870   -58.041 -4.090   1.00 200.08 ? 148  ASP E CA  1 
ATOM   12658 C  C   . ASP E  1 148 ? 5.201   -58.622 -5.460   1.00 202.51 ? 148  ASP E C   1 
ATOM   12659 O  O   . ASP E  1 148 ? 4.419   -59.394 -6.026   1.00 209.87 ? 148  ASP E O   1 
ATOM   12660 C  CB  . ASP E  1 148 ? 5.903   -58.510 -3.064   1.00 200.67 ? 148  ASP E CB  1 
ATOM   12661 C  CG  . ASP E  1 148 ? 7.102   -57.593 -2.994   1.00 201.31 ? 148  ASP E CG  1 
ATOM   12662 O  OD1 . ASP E  1 148 ? 7.412   -56.941 -4.012   1.00 198.87 ? 148  ASP E OD1 1 
ATOM   12663 O  OD2 . ASP E  1 148 ? 7.735   -57.523 -1.922   1.00 209.71 ? 148  ASP E OD2 1 
ATOM   12664 N  N   . ALA E  1 149 ? 6.355   -58.229 -6.010   1.00 207.86 ? 149  ALA E N   1 
ATOM   12665 C  CA  . ALA E  1 149 ? 6.744   -58.693 -7.338   1.00 207.73 ? 149  ALA E CA  1 
ATOM   12666 C  C   . ALA E  1 149 ? 6.856   -60.211 -7.380   1.00 205.57 ? 149  ALA E C   1 
ATOM   12667 O  O   . ALA E  1 149 ? 6.536   -60.833 -8.400   1.00 196.88 ? 149  ALA E O   1 
ATOM   12668 C  CB  . ALA E  1 149 ? 8.064   -58.044 -7.757   1.00 209.03 ? 149  ALA E CB  1 
ATOM   12669 N  N   . ASP E  1 150 ? 7.312   -60.826 -6.282   1.00 210.72 ? 150  ASP E N   1 
ATOM   12670 C  CA  . ASP E  1 150 ? 7.401   -62.282 -6.229   1.00 207.02 ? 150  ASP E CA  1 
ATOM   12671 C  C   . ASP E  1 150 ? 6.044   -62.931 -6.452   1.00 203.13 ? 150  ASP E C   1 
ATOM   12672 O  O   . ASP E  1 150 ? 5.971   -64.074 -6.918   1.00 199.94 ? 150  ASP E O   1 
ATOM   12673 C  CB  . ASP E  1 150 ? 7.987   -62.734 -4.891   1.00 212.53 ? 150  ASP E CB  1 
ATOM   12674 C  CG  . ASP E  1 150 ? 9.225   -61.957 -4.508   1.00 227.88 ? 150  ASP E CG  1 
ATOM   12675 O  OD1 . ASP E  1 150 ? 10.322  -62.312 -4.989   1.00 244.47 ? 150  ASP E OD1 1 
ATOM   12676 O  OD2 . ASP E  1 150 ? 9.101   -61.000 -3.715   1.00 218.11 ? 150  ASP E OD2 1 
ATOM   12677 N  N   . GLY E  1 151 ? 4.965   -62.230 -6.118   1.00 205.20 ? 151  GLY E N   1 
ATOM   12678 C  CA  . GLY E  1 151 ? 3.634   -62.756 -6.322   1.00 215.33 ? 151  GLY E CA  1 
ATOM   12679 C  C   . GLY E  1 151 ? 2.913   -62.132 -7.500   1.00 211.44 ? 151  GLY E C   1 
ATOM   12680 O  O   . GLY E  1 151 ? 3.465   -62.030 -8.600   1.00 203.55 ? 151  GLY E O   1 
ATOM   12681 N  N   . GLN E  1 152 ? 1.679   -61.684 -7.267   1.00 200.33 ? 152  GLN E N   1 
ATOM   12682 C  CA  . GLN E  1 152 ? 0.820   -61.140 -8.309   1.00 189.69 ? 152  GLN E CA  1 
ATOM   12683 C  C   . GLN E  1 152 ? 0.675   -59.628 -8.201   1.00 187.59 ? 152  GLN E C   1 
ATOM   12684 O  O   . GLN E  1 152 ? -0.257  -59.057 -8.775   1.00 184.49 ? 152  GLN E O   1 
ATOM   12685 C  CB  . GLN E  1 152 ? -0.554  -61.810 -8.250   1.00 191.51 ? 152  GLN E CB  1 
ATOM   12686 C  CG  . GLN E  1 152 ? -0.519  -63.310 -8.506   1.00 195.29 ? 152  GLN E CG  1 
ATOM   12687 C  CD  . GLN E  1 152 ? -1.859  -63.985 -8.268   1.00 201.04 ? 152  GLN E CD  1 
ATOM   12688 O  OE1 . GLN E  1 152 ? -2.807  -63.364 -7.790   1.00 212.05 ? 152  GLN E OE1 1 
ATOM   12689 N  NE2 . GLN E  1 152 ? -1.940  -65.268 -8.596   1.00 198.65 ? 152  GLN E NE2 1 
ATOM   12690 N  N   . GLY E  1 153 ? 1.575   -58.974 -7.463   1.00 201.98 ? 153  GLY E N   1 
ATOM   12691 C  CA  . GLY E  1 153 ? 1.475   -57.537 -7.271   1.00 213.96 ? 153  GLY E CA  1 
ATOM   12692 C  C   . GLY E  1 153 ? 1.586   -56.751 -8.560   1.00 206.80 ? 153  GLY E C   1 
ATOM   12693 O  O   . GLY E  1 153 ? 0.933   -55.715 -8.721   1.00 214.42 ? 153  GLY E O   1 
ATOM   12694 N  N   . PHE E  1 154 ? 2.404   -57.227 -9.493   1.00 190.80 ? 154  PHE E N   1 
ATOM   12695 C  CA  . PHE E  1 154 ? 2.613   -56.560 -10.770  1.00 187.48 ? 154  PHE E CA  1 
ATOM   12696 C  C   . PHE E  1 154 ? 2.071   -57.404 -11.914  1.00 189.11 ? 154  PHE E C   1 
ATOM   12697 O  O   . PHE E  1 154 ? 2.522   -57.294 -13.057  1.00 179.24 ? 154  PHE E O   1 
ATOM   12698 C  CB  . PHE E  1 154 ? 4.089   -56.228 -10.962  1.00 185.29 ? 154  PHE E CB  1 
ATOM   12699 C  CG  . PHE E  1 154 ? 4.562   -55.092 -10.099  1.00 190.00 ? 154  PHE E CG  1 
ATOM   12700 C  CD1 . PHE E  1 154 ? 4.685   -55.248 -8.729   1.00 196.80 ? 154  PHE E CD1 1 
ATOM   12701 C  CD2 . PHE E  1 154 ? 4.883   -53.869 -10.659  1.00 188.94 ? 154  PHE E CD2 1 
ATOM   12702 C  CE1 . PHE E  1 154 ? 5.112   -54.203 -7.938   1.00 204.30 ? 154  PHE E CE1 1 
ATOM   12703 C  CE2 . PHE E  1 154 ? 5.311   -52.821 -9.871   1.00 194.21 ? 154  PHE E CE2 1 
ATOM   12704 C  CZ  . PHE E  1 154 ? 5.427   -52.988 -8.511   1.00 200.46 ? 154  PHE E CZ  1 
ATOM   12705 N  N   . CYS E  1 155 ? 1.064   -58.223 -11.597  1.00 194.37 ? 155  CYS E N   1 
ATOM   12706 C  CA  . CYS E  1 155 ? 0.451   -59.126 -12.564  1.00 196.96 ? 155  CYS E CA  1 
ATOM   12707 C  C   . CYS E  1 155 ? -0.128  -58.381 -13.756  1.00 198.85 ? 155  CYS E C   1 
ATOM   12708 O  O   . CYS E  1 155 ? -0.017  -58.845 -14.898  1.00 193.62 ? 155  CYS E O   1 
ATOM   12709 C  CB  . CYS E  1 155 ? -0.644  -59.932 -11.870  1.00 193.97 ? 155  CYS E CB  1 
ATOM   12710 S  SG  . CYS E  1 155 ? -1.867  -60.648 -12.974  1.00 194.94 ? 155  CYS E SG  1 
ATOM   12711 N  N   . GLN E  1 156 ? -0.771  -57.239 -13.510  1.00 218.34 ? 156  GLN E N   1 
ATOM   12712 C  CA  . GLN E  1 156 ? -1.477  -56.488 -14.549  1.00 216.48 ? 156  GLN E CA  1 
ATOM   12713 C  C   . GLN E  1 156 ? -2.493  -57.385 -15.258  1.00 205.17 ? 156  GLN E C   1 
ATOM   12714 O  O   . GLN E  1 156 ? -2.513  -57.506 -16.487  1.00 194.20 ? 156  GLN E O   1 
ATOM   12715 C  CB  . GLN E  1 156 ? -0.496  -55.850 -15.538  1.00 205.63 ? 156  GLN E CB  1 
ATOM   12716 C  CG  . GLN E  1 156 ? 0.513   -54.911 -14.878  1.00 197.10 ? 156  GLN E CG  1 
ATOM   12717 C  CD  . GLN E  1 156 ? 1.356   -54.135 -15.877  1.00 185.27 ? 156  GLN E CD  1 
ATOM   12718 O  OE1 . GLN E  1 156 ? 2.547   -54.403 -16.041  1.00 177.31 ? 156  GLN E OE1 1 
ATOM   12719 N  NE2 . GLN E  1 156 ? 0.744   -53.155 -16.537  1.00 190.91 ? 156  GLN E NE2 1 
ATOM   12720 N  N   . GLY E  1 157 ? -3.328  -58.040 -14.453  1.00 204.23 ? 157  GLY E N   1 
ATOM   12721 C  CA  . GLY E  1 157 ? -4.350  -58.909 -15.009  1.00 203.99 ? 157  GLY E CA  1 
ATOM   12722 C  C   . GLY E  1 157 ? -5.307  -58.134 -15.898  1.00 221.90 ? 157  GLY E C   1 
ATOM   12723 O  O   . GLY E  1 157 ? -5.695  -57.002 -15.594  1.00 235.61 ? 157  GLY E O   1 
ATOM   12724 N  N   . GLY E  1 158 ? -5.686  -58.754 -17.011  1.00 218.32 ? 158  GLY E N   1 
ATOM   12725 C  CA  . GLY E  1 158 ? -6.544  -58.124 -17.991  1.00 217.42 ? 158  GLY E CA  1 
ATOM   12726 C  C   . GLY E  1 158 ? -5.806  -57.425 -19.104  1.00 207.47 ? 158  GLY E C   1 
ATOM   12727 O  O   . GLY E  1 158 ? -6.437  -56.713 -19.897  1.00 209.07 ? 158  GLY E O   1 
ATOM   12728 N  N   . PHE E  1 159 ? -4.486  -57.603 -19.183  1.00 190.55 ? 159  PHE E N   1 
ATOM   12729 C  CA  . PHE E  1 159 ? -3.714  -57.029 -20.276  1.00 199.30 ? 159  PHE E CA  1 
ATOM   12730 C  C   . PHE E  1 159 ? -4.191  -57.571 -21.615  1.00 197.63 ? 159  PHE E C   1 
ATOM   12731 O  O   . PHE E  1 159 ? -4.217  -56.846 -22.616  1.00 212.70 ? 159  PHE E O   1 
ATOM   12732 C  CB  . PHE E  1 159 ? -2.231  -57.323 -20.059  1.00 202.04 ? 159  PHE E CB  1 
ATOM   12733 C  CG  . PHE E  1 159 ? -1.314  -56.571 -20.977  1.00 217.24 ? 159  PHE E CG  1 
ATOM   12734 C  CD1 . PHE E  1 159 ? -1.077  -55.218 -20.780  1.00 225.32 ? 159  PHE E CD1 1 
ATOM   12735 C  CD2 . PHE E  1 159 ? -0.658  -57.216 -22.014  1.00 203.76 ? 159  PHE E CD2 1 
ATOM   12736 C  CE1 . PHE E  1 159 ? -0.221  -54.515 -21.613  1.00 216.39 ? 159  PHE E CE1 1 
ATOM   12737 C  CE2 . PHE E  1 159 ? 0.204   -56.518 -22.849  1.00 197.61 ? 159  PHE E CE2 1 
ATOM   12738 C  CZ  . PHE E  1 159 ? 0.422   -55.166 -22.646  1.00 203.09 ? 159  PHE E CZ  1 
ATOM   12739 N  N   . SER E  1 160 ? -4.569  -58.845 -21.650  1.00 163.77 ? 160  SER E N   1 
ATOM   12740 C  CA  . SER E  1 160 ? -5.218  -59.443 -22.805  1.00 163.52 ? 160  SER E CA  1 
ATOM   12741 C  C   . SER E  1 160 ? -6.303  -60.396 -22.326  1.00 166.71 ? 160  SER E C   1 
ATOM   12742 O  O   . SER E  1 160 ? -6.144  -61.063 -21.300  1.00 168.83 ? 160  SER E O   1 
ATOM   12743 C  CB  . SER E  1 160 ? -4.204  -60.176 -23.682  1.00 181.43 ? 160  SER E CB  1 
ATOM   12744 O  OG  . SER E  1 160 ? -3.597  -61.226 -22.953  1.00 188.79 ? 160  SER E OG  1 
ATOM   12745 N  N   . ILE E  1 161 ? -7.408  -60.453 -23.069  1.00 159.61 ? 161  ILE E N   1 
ATOM   12746 C  CA  . ILE E  1 161 ? -8.556  -61.270 -22.704  1.00 167.22 ? 161  ILE E CA  1 
ATOM   12747 C  C   . ILE E  1 161 ? -9.160  -61.905 -23.951  1.00 191.34 ? 161  ILE E C   1 
ATOM   12748 O  O   . ILE E  1 161 ? -8.892  -61.497 -25.084  1.00 206.49 ? 161  ILE E O   1 
ATOM   12749 C  CB  . ILE E  1 161 ? -9.623  -60.454 -21.950  1.00 170.10 ? 161  ILE E CB  1 
ATOM   12750 C  CG1 . ILE E  1 161 ? -9.863  -59.119 -22.661  1.00 185.55 ? 161  ILE E CG1 1 
ATOM   12751 C  CG2 . ILE E  1 161 ? -9.202  -60.244 -20.504  1.00 169.90 ? 161  ILE E CG2 1 
ATOM   12752 C  CD1 . ILE E  1 161 ? -10.950 -58.276 -22.032  1.00 203.48 ? 161  ILE E CD1 1 
ATOM   12753 N  N   . ASP E  1 162 ? -10.001 -62.912 -23.718  1.00 197.45 ? 162  ASP E N   1 
ATOM   12754 C  CA  . ASP E  1 162 ? -10.739 -63.622 -24.756  1.00 199.67 ? 162  ASP E CA  1 
ATOM   12755 C  C   . ASP E  1 162 ? -11.787 -64.493 -24.079  1.00 199.54 ? 162  ASP E C   1 
ATOM   12756 O  O   . ASP E  1 162 ? -11.710 -64.760 -22.876  1.00 193.50 ? 162  ASP E O   1 
ATOM   12757 C  CB  . ASP E  1 162 ? -9.815  -64.470 -25.635  1.00 199.55 ? 162  ASP E CB  1 
ATOM   12758 C  CG  . ASP E  1 162 ? -10.328 -64.615 -27.054  1.00 196.37 ? 162  ASP E CG  1 
ATOM   12759 O  OD1 . ASP E  1 162 ? -11.537 -64.389 -27.277  1.00 198.26 ? 162  ASP E OD1 1 
ATOM   12760 O  OD2 . ASP E  1 162 ? -9.521  -64.956 -27.944  1.00 195.62 ? 162  ASP E OD2 1 
ATOM   12761 N  N   . PHE E  1 163 ? -12.782 -64.909 -24.858  1.00 216.81 ? 163  PHE E N   1 
ATOM   12762 C  CA  . PHE E  1 163 ? -13.813 -65.830 -24.401  1.00 222.28 ? 163  PHE E CA  1 
ATOM   12763 C  C   . PHE E  1 163 ? -13.695 -67.180 -25.105  1.00 219.85 ? 163  PHE E C   1 
ATOM   12764 O  O   . PHE E  1 163 ? -13.331 -67.259 -26.283  1.00 214.52 ? 163  PHE E O   1 
ATOM   12765 C  CB  . PHE E  1 163 ? -15.213 -65.252 -24.643  1.00 230.18 ? 163  PHE E CB  1 
ATOM   12766 C  CG  . PHE E  1 163 ? -15.629 -64.192 -23.652  1.00 220.52 ? 163  PHE E CG  1 
ATOM   12767 C  CD1 . PHE E  1 163 ? -16.077 -64.541 -22.389  1.00 213.17 ? 163  PHE E CD1 1 
ATOM   12768 C  CD2 . PHE E  1 163 ? -15.602 -62.849 -23.996  1.00 213.53 ? 163  PHE E CD2 1 
ATOM   12769 C  CE1 . PHE E  1 163 ? -16.477 -63.570 -21.488  1.00 207.92 ? 163  PHE E CE1 1 
ATOM   12770 C  CE2 . PHE E  1 163 ? -15.999 -61.873 -23.095  1.00 203.93 ? 163  PHE E CE2 1 
ATOM   12771 C  CZ  . PHE E  1 163 ? -16.437 -62.236 -21.841  1.00 204.34 ? 163  PHE E CZ  1 
ATOM   12772 N  N   . THR E  1 164 ? -14.015 -68.245 -24.371  1.00 213.05 ? 164  THR E N   1 
ATOM   12773 C  CA  . THR E  1 164 ? -14.153 -69.575 -24.947  1.00 210.70 ? 164  THR E CA  1 
ATOM   12774 C  C   . THR E  1 164 ? -15.609 -69.823 -25.334  1.00 218.08 ? 164  THR E C   1 
ATOM   12775 O  O   . THR E  1 164 ? -16.496 -69.007 -25.079  1.00 220.79 ? 164  THR E O   1 
ATOM   12776 C  CB  . THR E  1 164 ? -13.680 -70.653 -23.971  1.00 208.83 ? 164  THR E CB  1 
ATOM   12777 O  OG1 . THR E  1 164 ? -14.601 -70.747 -22.879  1.00 212.06 ? 164  THR E OG1 1 
ATOM   12778 C  CG2 . THR E  1 164 ? -12.303 -70.313 -23.433  1.00 203.37 ? 164  THR E CG2 1 
ATOM   12779 N  N   . LYS E  1 165 ? -15.851 -70.972 -25.963  1.00 219.09 ? 165  LYS E N   1 
ATOM   12780 C  CA  . LYS E  1 165 ? -17.207 -71.318 -26.367  1.00 234.28 ? 165  LYS E CA  1 
ATOM   12781 C  C   . LYS E  1 165 ? -18.015 -71.939 -25.233  1.00 254.81 ? 165  LYS E C   1 
ATOM   12782 O  O   . LYS E  1 165 ? -19.233 -72.097 -25.371  1.00 269.53 ? 165  LYS E O   1 
ATOM   12783 C  CB  . LYS E  1 165 ? -17.163 -72.269 -27.574  1.00 229.56 ? 165  LYS E CB  1 
ATOM   12784 C  CG  . LYS E  1 165 ? -18.512 -72.530 -28.240  1.00 231.45 ? 165  LYS E CG  1 
ATOM   12785 C  CD  . LYS E  1 165 ? -18.354 -73.142 -29.619  1.00 230.56 ? 165  LYS E CD  1 
ATOM   12786 C  CE  . LYS E  1 165 ? -19.707 -73.537 -30.186  1.00 233.91 ? 165  LYS E CE  1 
ATOM   12787 N  NZ  . LYS E  1 165 ? -19.599 -74.226 -31.499  1.00 235.47 ? 165  LYS E NZ  1 
ATOM   12788 N  N   . ALA E  1 166 ? -17.386 -72.243 -24.097  1.00 252.79 ? 166  ALA E N   1 
ATOM   12789 C  CA  . ALA E  1 166 ? -18.063 -72.863 -22.964  1.00 246.24 ? 166  ALA E CA  1 
ATOM   12790 C  C   . ALA E  1 166 ? -18.161 -71.922 -21.767  1.00 234.40 ? 166  ALA E C   1 
ATOM   12791 O  O   . ALA E  1 166 ? -18.151 -72.367 -20.615  1.00 227.96 ? 166  ALA E O   1 
ATOM   12792 C  CB  . ALA E  1 166 ? -17.360 -74.158 -22.561  1.00 240.30 ? 166  ALA E CB  1 
ATOM   12793 N  N   . ASP E  1 167 ? -18.254 -70.617 -22.033  1.00 231.94 ? 167  ASP E N   1 
ATOM   12794 C  CA  . ASP E  1 167 ? -18.460 -69.598 -21.004  1.00 230.34 ? 167  ASP E CA  1 
ATOM   12795 C  C   . ASP E  1 167 ? -17.339 -69.617 -19.964  1.00 226.15 ? 167  ASP E C   1 
ATOM   12796 O  O   . ASP E  1 167 ? -17.578 -69.562 -18.755  1.00 222.97 ? 167  ASP E O   1 
ATOM   12797 C  CB  . ASP E  1 167 ? -19.834 -69.747 -20.341  1.00 236.89 ? 167  ASP E CB  1 
ATOM   12798 C  CG  . ASP E  1 167 ? -20.983 -69.592 -21.325  1.00 240.70 ? 167  ASP E CG  1 
ATOM   12799 O  OD1 . ASP E  1 167 ? -20.777 -69.846 -22.529  1.00 247.95 ? 167  ASP E OD1 1 
ATOM   12800 O  OD2 . ASP E  1 167 ? -22.092 -69.203 -20.896  1.00 233.97 ? 167  ASP E OD2 1 
ATOM   12801 N  N   . ARG E  1 168 ? -16.103 -69.698 -20.449  1.00 229.91 ? 168  ARG E N   1 
ATOM   12802 C  CA  . ARG E  1 168 ? -14.916 -69.499 -19.631  1.00 224.78 ? 168  ARG E CA  1 
ATOM   12803 C  C   . ARG E  1 168 ? -14.185 -68.249 -20.109  1.00 211.30 ? 168  ARG E C   1 
ATOM   12804 O  O   . ARG E  1 168 ? -14.086 -68.000 -21.315  1.00 206.78 ? 168  ARG E O   1 
ATOM   12805 C  CB  . ARG E  1 168 ? -13.987 -70.720 -19.695  1.00 226.15 ? 168  ARG E CB  1 
ATOM   12806 C  CG  . ARG E  1 168 ? -14.588 -71.997 -19.097  1.00 226.76 ? 168  ARG E CG  1 
ATOM   12807 C  CD  . ARG E  1 168 ? -13.552 -73.098 -18.857  1.00 221.28 ? 168  ARG E CD  1 
ATOM   12808 N  NE  . ARG E  1 168 ? -12.668 -72.818 -17.728  1.00 217.77 ? 168  ARG E NE  1 
ATOM   12809 C  CZ  . ARG E  1 168 ? -12.635 -73.543 -16.613  1.00 223.90 ? 168  ARG E CZ  1 
ATOM   12810 N  NH1 . ARG E  1 168 ? -13.440 -74.590 -16.481  1.00 226.32 ? 168  ARG E NH1 1 
ATOM   12811 N  NH2 . ARG E  1 168 ? -11.800 -73.225 -15.631  1.00 229.71 ? 168  ARG E NH2 1 
ATOM   12812 N  N   . VAL E  1 169 ? -13.684 -67.459 -19.167  1.00 211.30 ? 169  VAL E N   1 
ATOM   12813 C  CA  . VAL E  1 169 ? -12.887 -66.278 -19.484  1.00 203.92 ? 169  VAL E CA  1 
ATOM   12814 C  C   . VAL E  1 169 ? -11.409 -66.648 -19.482  1.00 214.60 ? 169  VAL E C   1 
ATOM   12815 O  O   . VAL E  1 169 ? -10.940 -67.389 -18.609  1.00 211.72 ? 169  VAL E O   1 
ATOM   12816 C  CB  . VAL E  1 169 ? -13.188 -65.144 -18.487  1.00 207.29 ? 169  VAL E CB  1 
ATOM   12817 C  CG1 . VAL E  1 169 ? -12.171 -64.028 -18.616  1.00 208.23 ? 169  VAL E CG1 1 
ATOM   12818 C  CG2 . VAL E  1 169 ? -14.593 -64.622 -18.706  1.00 220.21 ? 169  VAL E CG2 1 
ATOM   12819 N  N   . LEU E  1 170 ? -10.667 -66.134 -20.462  1.00 217.17 ? 170  LEU E N   1 
ATOM   12820 C  CA  . LEU E  1 170 ? -9.219  -66.303 -20.533  1.00 196.35 ? 170  LEU E CA  1 
ATOM   12821 C  C   . LEU E  1 170 ? -8.539  -64.953 -20.326  1.00 193.94 ? 170  LEU E C   1 
ATOM   12822 O  O   . LEU E  1 170 ? -8.720  -64.031 -21.130  1.00 194.34 ? 170  LEU E O   1 
ATOM   12823 C  CB  . LEU E  1 170 ? -8.807  -66.915 -21.870  1.00 185.62 ? 170  LEU E CB  1 
ATOM   12824 C  CG  . LEU E  1 170 ? -7.304  -66.967 -22.126  1.00 177.32 ? 170  LEU E CG  1 
ATOM   12825 C  CD1 . LEU E  1 170 ? -6.618  -67.767 -21.035  1.00 177.50 ? 170  LEU E CD1 1 
ATOM   12826 C  CD2 . LEU E  1 170 ? -7.023  -67.564 -23.488  1.00 178.17 ? 170  LEU E CD2 1 
ATOM   12827 N  N   . LEU E  1 171 ? -7.744  -64.850 -19.263  1.00 201.03 ? 171  LEU E N   1 
ATOM   12828 C  CA  . LEU E  1 171 ? -7.063  -63.618 -18.889  1.00 200.06 ? 171  LEU E CA  1 
ATOM   12829 C  C   . LEU E  1 171 ? -5.554  -63.817 -18.897  1.00 202.40 ? 171  LEU E C   1 
ATOM   12830 O  O   . LEU E  1 171 ? -5.050  -64.846 -18.435  1.00 218.57 ? 171  LEU E O   1 
ATOM   12831 C  CB  . LEU E  1 171 ? -7.512  -63.144 -17.504  1.00 200.62 ? 171  LEU E CB  1 
ATOM   12832 C  CG  . LEU E  1 171 ? -6.841  -61.904 -16.910  1.00 206.13 ? 171  LEU E CG  1 
ATOM   12833 C  CD1 . LEU E  1 171 ? -7.863  -61.102 -16.134  1.00 222.63 ? 171  LEU E CD1 1 
ATOM   12834 C  CD2 . LEU E  1 171 ? -5.678  -62.276 -15.997  1.00 195.03 ? 171  LEU E CD2 1 
ATOM   12835 N  N   . GLY E  1 172 ? -4.838  -62.821 -19.415  1.00 184.53 ? 172  GLY E N   1 
ATOM   12836 C  CA  . GLY E  1 172 ? -3.385  -62.827 -19.446  1.00 176.41 ? 172  GLY E CA  1 
ATOM   12837 C  C   . GLY E  1 172 ? -2.817  -61.812 -18.465  1.00 170.76 ? 172  GLY E C   1 
ATOM   12838 O  O   . GLY E  1 172 ? -3.274  -60.669 -18.408  1.00 170.61 ? 172  GLY E O   1 
ATOM   12839 N  N   . GLY E  1 173 ? -1.817  -62.252 -17.698  1.00 163.84 ? 173  GLY E N   1 
ATOM   12840 C  CA  . GLY E  1 173 ? -1.140  -61.408 -16.739  1.00 162.42 ? 173  GLY E CA  1 
ATOM   12841 C  C   . GLY E  1 173 ? 0.369   -61.506 -16.849  1.00 162.12 ? 173  GLY E C   1 
ATOM   12842 O  O   . GLY E  1 173 ? 1.002   -62.385 -16.254  1.00 183.02 ? 173  GLY E O   1 
ATOM   12843 N  N   . PRO E  1 174 ? 0.977   -60.590 -17.608  1.00 155.36 ? 174  PRO E N   1 
ATOM   12844 C  CA  . PRO E  1 174 ? 2.408   -60.725 -17.936  1.00 152.16 ? 174  PRO E CA  1 
ATOM   12845 C  C   . PRO E  1 174 ? 3.351   -60.535 -16.762  1.00 155.44 ? 174  PRO E C   1 
ATOM   12846 O  O   . PRO E  1 174 ? 4.519   -60.936 -16.855  1.00 154.56 ? 174  PRO E O   1 
ATOM   12847 C  CB  . PRO E  1 174 ? 2.631   -59.628 -18.987  1.00 149.10 ? 174  PRO E CB  1 
ATOM   12848 C  CG  . PRO E  1 174 ? 1.264   -59.268 -19.474  1.00 149.28 ? 174  PRO E CG  1 
ATOM   12849 C  CD  . PRO E  1 174 ? 0.359   -59.455 -18.306  1.00 153.59 ? 174  PRO E CD  1 
ATOM   12850 N  N   . GLY E  1 175 ? 2.899   -59.944 -15.666  1.00 158.84 ? 175  GLY E N   1 
ATOM   12851 C  CA  . GLY E  1 175 ? 3.821   -59.596 -14.605  1.00 163.40 ? 175  GLY E CA  1 
ATOM   12852 C  C   . GLY E  1 175 ? 3.891   -60.561 -13.440  1.00 186.47 ? 175  GLY E C   1 
ATOM   12853 O  O   . GLY E  1 175 ? 4.727   -60.388 -12.550  1.00 203.66 ? 175  GLY E O   1 
ATOM   12854 N  N   . SER E  1 176 ? 3.009   -61.560 -13.416  1.00 191.39 ? 176  SER E N   1 
ATOM   12855 C  CA  . SER E  1 176 ? 2.956   -62.495 -12.299  1.00 185.15 ? 176  SER E CA  1 
ATOM   12856 C  C   . SER E  1 176 ? 4.293   -63.203 -12.091  1.00 202.49 ? 176  SER E C   1 
ATOM   12857 O  O   . SER E  1 176 ? 5.016   -63.497 -13.047  1.00 223.38 ? 176  SER E O   1 
ATOM   12858 C  CB  . SER E  1 176 ? 1.853   -63.526 -12.533  1.00 176.81 ? 176  SER E CB  1 
ATOM   12859 O  OG  . SER E  1 176 ? 0.571   -62.944 -12.391  1.00 178.20 ? 176  SER E OG  1 
ATOM   12860 N  N   . PHE E  1 177 ? 4.619   -63.465 -10.821  1.00 204.93 ? 177  PHE E N   1 
ATOM   12861 C  CA  . PHE E  1 177 ? 5.783   -64.264 -10.418  1.00 207.35 ? 177  PHE E CA  1 
ATOM   12862 C  C   . PHE E  1 177 ? 7.089   -63.687 -10.973  1.00 210.80 ? 177  PHE E C   1 
ATOM   12863 O  O   . PHE E  1 177 ? 7.852   -64.363 -11.668  1.00 215.42 ? 177  PHE E O   1 
ATOM   12864 C  CB  . PHE E  1 177 ? 5.623   -65.731 -10.844  1.00 208.77 ? 177  PHE E CB  1 
ATOM   12865 C  CG  . PHE E  1 177 ? 4.278   -66.328 -10.526  1.00 216.08 ? 177  PHE E CG  1 
ATOM   12866 C  CD1 . PHE E  1 177 ? 3.667   -66.104 -9.304   1.00 229.75 ? 177  PHE E CD1 1 
ATOM   12867 C  CD2 . PHE E  1 177 ? 3.636   -67.137 -11.452  1.00 210.95 ? 177  PHE E CD2 1 
ATOM   12868 C  CE1 . PHE E  1 177 ? 2.433   -66.662 -9.017   1.00 231.49 ? 177  PHE E CE1 1 
ATOM   12869 C  CE2 . PHE E  1 177 ? 2.405   -67.698 -11.171  1.00 216.84 ? 177  PHE E CE2 1 
ATOM   12870 C  CZ  . PHE E  1 177 ? 1.803   -67.460 -9.952   1.00 226.10 ? 177  PHE E CZ  1 
ATOM   12871 N  N   . TYR E  1 178 ? 7.356   -62.429 -10.617  1.00 202.87 ? 178  TYR E N   1 
ATOM   12872 C  CA  . TYR E  1 178 ? 8.517   -61.687 -11.119  1.00 198.54 ? 178  TYR E CA  1 
ATOM   12873 C  C   . TYR E  1 178 ? 8.557   -61.699 -12.647  1.00 182.87 ? 178  TYR E C   1 
ATOM   12874 O  O   . TYR E  1 178 ? 9.588   -61.960 -13.270  1.00 170.86 ? 178  TYR E O   1 
ATOM   12875 C  CB  . TYR E  1 178 ? 9.821   -62.227 -10.527  1.00 203.45 ? 178  TYR E CB  1 
ATOM   12876 C  CG  . TYR E  1 178 ? 10.516  -61.238 -9.621   1.00 213.65 ? 178  TYR E CG  1 
ATOM   12877 C  CD1 . TYR E  1 178 ? 11.124  -60.103 -10.141  1.00 228.56 ? 178  TYR E CD1 1 
ATOM   12878 C  CD2 . TYR E  1 178 ? 10.560  -61.433 -8.247   1.00 207.85 ? 178  TYR E CD2 1 
ATOM   12879 C  CE1 . TYR E  1 178 ? 11.755  -59.191 -9.318   1.00 234.09 ? 178  TYR E CE1 1 
ATOM   12880 C  CE2 . TYR E  1 178 ? 11.191  -60.526 -7.417   1.00 210.66 ? 178  TYR E CE2 1 
ATOM   12881 C  CZ  . TYR E  1 178 ? 11.785  -59.407 -7.956   1.00 222.38 ? 178  TYR E CZ  1 
ATOM   12882 O  OH  . TYR E  1 178 ? 12.415  -58.504 -7.130   1.00 225.82 ? 178  TYR E OH  1 
ATOM   12883 N  N   . TRP E  1 179 ? 7.399   -61.409 -13.247  1.00 187.16 ? 179  TRP E N   1 
ATOM   12884 C  CA  . TRP E  1 179 ? 7.234   -61.289 -14.698  1.00 176.36 ? 179  TRP E CA  1 
ATOM   12885 C  C   . TRP E  1 179 ? 7.484   -62.602 -15.430  1.00 171.31 ? 179  TRP E C   1 
ATOM   12886 O  O   . TRP E  1 179 ? 7.843   -62.604 -16.609  1.00 163.05 ? 179  TRP E O   1 
ATOM   12887 C  CB  . TRP E  1 179 ? 8.119   -60.190 -15.289  1.00 179.17 ? 179  TRP E CB  1 
ATOM   12888 C  CG  . TRP E  1 179 ? 7.703   -58.822 -14.890  1.00 182.29 ? 179  TRP E CG  1 
ATOM   12889 C  CD1 . TRP E  1 179 ? 6.779   -58.036 -15.511  1.00 170.59 ? 179  TRP E CD1 1 
ATOM   12890 C  CD2 . TRP E  1 179 ? 8.222   -58.051 -13.804  1.00 184.96 ? 179  TRP E CD2 1 
ATOM   12891 N  NE1 . TRP E  1 179 ? 6.670   -56.833 -14.863  1.00 174.61 ? 179  TRP E NE1 1 
ATOM   12892 C  CE2 . TRP E  1 179 ? 7.549   -56.815 -13.813  1.00 181.21 ? 179  TRP E CE2 1 
ATOM   12893 C  CE3 . TRP E  1 179 ? 9.183   -58.290 -12.818  1.00 192.45 ? 179  TRP E CE3 1 
ATOM   12894 C  CZ2 . TRP E  1 179 ? 7.806   -55.821 -12.878  1.00 188.03 ? 179  TRP E CZ2 1 
ATOM   12895 C  CZ3 . TRP E  1 179 ? 9.435   -57.301 -11.891  1.00 196.00 ? 179  TRP E CZ3 1 
ATOM   12896 C  CH2 . TRP E  1 179 ? 8.750   -56.082 -11.927  1.00 194.53 ? 179  TRP E CH2 1 
ATOM   12897 N  N   . GLN E  1 180 ? 7.297   -63.736 -14.752  1.00 194.49 ? 180  GLN E N   1 
ATOM   12898 C  CA  . GLN E  1 180 ? 7.165   -64.994 -15.480  1.00 201.25 ? 180  GLN E CA  1 
ATOM   12899 C  C   . GLN E  1 180 ? 5.892   -65.026 -16.320  1.00 195.63 ? 180  GLN E C   1 
ATOM   12900 O  O   . GLN E  1 180 ? 5.858   -65.686 -17.365  1.00 200.45 ? 180  GLN E O   1 
ATOM   12901 C  CB  . GLN E  1 180 ? 7.176   -66.183 -14.516  1.00 197.93 ? 180  GLN E CB  1 
ATOM   12902 C  CG  . GLN E  1 180 ? 8.509   -66.468 -13.859  1.00 184.97 ? 180  GLN E CG  1 
ATOM   12903 C  CD  . GLN E  1 180 ? 8.481   -67.716 -12.995  1.00 195.69 ? 180  GLN E CD  1 
ATOM   12904 O  OE1 . GLN E  1 180 ? 7.600   -68.567 -13.135  1.00 199.63 ? 180  GLN E OE1 1 
ATOM   12905 N  NE2 . GLN E  1 180 ? 9.440   -67.824 -12.085  1.00 206.88 ? 180  GLN E NE2 1 
ATOM   12906 N  N   . GLY E  1 181 ? 4.854   -64.318 -15.887  1.00 183.76 ? 181  GLY E N   1 
ATOM   12907 C  CA  . GLY E  1 181 ? 3.549   -64.349 -16.514  1.00 183.55 ? 181  GLY E CA  1 
ATOM   12908 C  C   . GLY E  1 181 ? 2.659   -65.458 -15.972  1.00 196.54 ? 181  GLY E C   1 
ATOM   12909 O  O   . GLY E  1 181 ? 3.111   -66.418 -15.348  1.00 208.95 ? 181  GLY E O   1 
ATOM   12910 N  N   . GLN E  1 182 ? 1.359   -65.316 -16.231  1.00 193.72 ? 182  GLN E N   1 
ATOM   12911 C  CA  . GLN E  1 182 ? 0.385   -66.274 -15.731  1.00 189.09 ? 182  GLN E CA  1 
ATOM   12912 C  C   . GLN E  1 182 ? -0.884  -66.178 -16.564  1.00 191.73 ? 182  GLN E C   1 
ATOM   12913 O  O   . GLN E  1 182 ? -1.267  -65.094 -17.009  1.00 194.86 ? 182  GLN E O   1 
ATOM   12914 C  CB  . GLN E  1 182 ? 0.076   -66.030 -14.247  1.00 189.90 ? 182  GLN E CB  1 
ATOM   12915 C  CG  . GLN E  1 182 ? -0.763  -67.110 -13.588  1.00 200.36 ? 182  GLN E CG  1 
ATOM   12916 C  CD  . GLN E  1 182 ? -1.028  -66.834 -12.118  1.00 213.15 ? 182  GLN E CD  1 
ATOM   12917 O  OE1 . GLN E  1 182 ? -0.923  -65.697 -11.657  1.00 212.87 ? 182  GLN E OE1 1 
ATOM   12918 N  NE2 . GLN E  1 182 ? -1.367  -67.879 -11.373  1.00 220.29 ? 182  GLN E NE2 1 
ATOM   12919 N  N   . LEU E  1 183 ? -1.527  -67.325 -16.771  1.00 194.94 ? 183  LEU E N   1 
ATOM   12920 C  CA  . LEU E  1 183 ? -2.846  -67.403 -17.384  1.00 195.10 ? 183  LEU E CA  1 
ATOM   12921 C  C   . LEU E  1 183 ? -3.865  -67.850 -16.343  1.00 195.68 ? 183  LEU E C   1 
ATOM   12922 O  O   . LEU E  1 183 ? -3.653  -68.855 -15.659  1.00 196.82 ? 183  LEU E O   1 
ATOM   12923 C  CB  . LEU E  1 183 ? -2.840  -68.370 -18.567  1.00 190.63 ? 183  LEU E CB  1 
ATOM   12924 C  CG  . LEU E  1 183 ? -1.858  -68.052 -19.694  1.00 183.49 ? 183  LEU E CG  1 
ATOM   12925 C  CD1 . LEU E  1 183 ? -2.065  -69.027 -20.835  1.00 200.20 ? 183  LEU E CD1 1 
ATOM   12926 C  CD2 . LEU E  1 183 ? -2.024  -66.620 -20.174  1.00 172.47 ? 183  LEU E CD2 1 
ATOM   12927 N  N   . ILE E  1 184 ? -4.971  -67.116 -16.236  1.00 203.92 ? 184  ILE E N   1 
ATOM   12928 C  CA  . ILE E  1 184 ? -6.047  -67.436 -15.305  1.00 209.74 ? 184  ILE E CA  1 
ATOM   12929 C  C   . ILE E  1 184 ? -7.338  -67.626 -16.094  1.00 206.84 ? 184  ILE E C   1 
ATOM   12930 O  O   . ILE E  1 184 ? -7.667  -66.811 -16.964  1.00 196.44 ? 184  ILE E O   1 
ATOM   12931 C  CB  . ILE E  1 184 ? -6.207  -66.347 -14.226  1.00 219.08 ? 184  ILE E CB  1 
ATOM   12932 C  CG1 . ILE E  1 184 ? -4.931  -66.231 -13.379  1.00 217.31 ? 184  ILE E CG1 1 
ATOM   12933 C  CG2 . ILE E  1 184 ? -7.402  -66.637 -13.334  1.00 233.86 ? 184  ILE E CG2 1 
ATOM   12934 C  CD1 . ILE E  1 184 ? -5.049  -65.277 -12.192  1.00 207.60 ? 184  ILE E CD1 1 
ATOM   12935 N  N   . SER E  1 185 ? -8.057  -68.711 -15.797  1.00 213.12 ? 185  SER E N   1 
ATOM   12936 C  CA  . SER E  1 185 ? -9.331  -69.027 -16.435  1.00 219.20 ? 185  SER E CA  1 
ATOM   12937 C  C   . SER E  1 185 ? -10.376 -69.337 -15.373  1.00 233.33 ? 185  SER E C   1 
ATOM   12938 O  O   . SER E  1 185 ? -10.179 -70.237 -14.549  1.00 234.52 ? 185  SER E O   1 
ATOM   12939 C  CB  . SER E  1 185 ? -9.186  -70.210 -17.394  1.00 208.97 ? 185  SER E CB  1 
ATOM   12940 O  OG  . SER E  1 185 ? -10.392 -70.436 -18.103  1.00 207.51 ? 185  SER E OG  1 
ATOM   12941 N  N   . ASP E  1 186 ? -11.494 -68.609 -15.404  1.00 235.82 ? 186  ASP E N   1 
ATOM   12942 C  CA  . ASP E  1 186 ? -12.602 -68.835 -14.484  1.00 233.89 ? 186  ASP E CA  1 
ATOM   12943 C  C   . ASP E  1 186 ? -13.917 -68.961 -15.242  1.00 237.17 ? 186  ASP E C   1 
ATOM   12944 O  O   . ASP E  1 186 ? -14.133 -68.312 -16.269  1.00 240.90 ? 186  ASP E O   1 
ATOM   12945 C  CB  . ASP E  1 186 ? -12.714 -67.711 -13.443  1.00 230.48 ? 186  ASP E CB  1 
ATOM   12946 C  CG  . ASP E  1 186 ? -11.685 -67.838 -12.338  1.00 232.49 ? 186  ASP E CG  1 
ATOM   12947 O  OD1 . ASP E  1 186 ? -11.814 -68.774 -11.522  1.00 233.27 ? 186  ASP E OD1 1 
ATOM   12948 O  OD2 . ASP E  1 186 ? -10.752 -67.010 -12.282  1.00 234.46 ? 186  ASP E OD2 1 
ATOM   12949 N  N   . GLN E  1 187 ? -14.801 -69.802 -14.708  1.00 234.87 ? 187  GLN E N   1 
ATOM   12950 C  CA  . GLN E  1 187 ? -16.147 -69.955 -15.248  1.00 233.61 ? 187  GLN E CA  1 
ATOM   12951 C  C   . GLN E  1 187 ? -16.987 -68.713 -14.962  1.00 229.19 ? 187  GLN E C   1 
ATOM   12952 O  O   . GLN E  1 187 ? -16.962 -68.182 -13.846  1.00 227.60 ? 187  GLN E O   1 
ATOM   12953 C  CB  . GLN E  1 187 ? -16.802 -71.197 -14.652  1.00 233.83 ? 187  GLN E CB  1 
ATOM   12954 C  CG  . GLN E  1 187 ? -16.107 -72.489 -15.038  1.00 228.14 ? 187  GLN E CG  1 
ATOM   12955 C  CD  . GLN E  1 187 ? -16.634 -73.683 -14.276  1.00 232.03 ? 187  GLN E CD  1 
ATOM   12956 O  OE1 . GLN E  1 187 ? -17.407 -73.537 -13.329  1.00 238.90 ? 187  GLN E OE1 1 
ATOM   12957 N  NE2 . GLN E  1 187 ? -16.216 -74.876 -14.683  1.00 233.66 ? 187  GLN E NE2 1 
ATOM   12958 N  N   . VAL E  1 188 ? -17.698 -68.224 -15.988  1.00 222.51 ? 188  VAL E N   1 
ATOM   12959 C  CA  . VAL E  1 188 ? -18.495 -67.003 -15.844  1.00 222.04 ? 188  VAL E CA  1 
ATOM   12960 C  C   . VAL E  1 188 ? -19.566 -67.166 -14.773  1.00 234.40 ? 188  VAL E C   1 
ATOM   12961 O  O   . VAL E  1 188 ? -19.995 -66.182 -14.157  1.00 239.25 ? 188  VAL E O   1 
ATOM   12962 C  CB  . VAL E  1 188 ? -19.107 -66.595 -17.201  1.00 216.70 ? 188  VAL E CB  1 
ATOM   12963 C  CG1 . VAL E  1 188 ? -18.006 -66.429 -18.249  1.00 213.04 ? 188  VAL E CG1 1 
ATOM   12964 C  CG2 . VAL E  1 188 ? -20.158 -67.595 -17.648  1.00 222.00 ? 188  VAL E CG2 1 
ATOM   12965 N  N   . ALA E  1 189 ? -20.019 -68.400 -14.530  1.00 232.51 ? 189  ALA E N   1 
ATOM   12966 C  CA  . ALA E  1 189 ? -21.010 -68.616 -13.484  1.00 232.87 ? 189  ALA E CA  1 
ATOM   12967 C  C   . ALA E  1 189 ? -20.418 -68.352 -12.111  1.00 229.59 ? 189  ALA E C   1 
ATOM   12968 O  O   . ALA E  1 189 ? -21.126 -67.901 -11.205  1.00 230.48 ? 189  ALA E O   1 
ATOM   12969 C  CB  . ALA E  1 189 ? -21.569 -70.037 -13.559  1.00 235.09 ? 189  ALA E CB  1 
ATOM   12970 N  N   . GLU E  1 190 ? -19.128 -68.631 -11.948  1.00 232.68 ? 190  GLU E N   1 
ATOM   12971 C  CA  . GLU E  1 190 ? -18.428 -68.387 -10.695  1.00 239.22 ? 190  GLU E CA  1 
ATOM   12972 C  C   . GLU E  1 190 ? -17.999 -66.932 -10.523  1.00 229.11 ? 190  GLU E C   1 
ATOM   12973 O  O   . GLU E  1 190 ? -17.921 -66.448 -9.389   1.00 230.86 ? 190  GLU E O   1 
ATOM   12974 C  CB  . GLU E  1 190 ? -17.213 -69.307 -10.623  1.00 246.94 ? 190  GLU E CB  1 
ATOM   12975 C  CG  . GLU E  1 190 ? -16.586 -69.455 -9.262   1.00 254.43 ? 190  GLU E CG  1 
ATOM   12976 C  CD  . GLU E  1 190 ? -15.375 -70.360 -9.316   1.00 252.84 ? 190  GLU E CD  1 
ATOM   12977 O  OE1 . GLU E  1 190 ? -14.924 -70.838 -8.255   1.00 262.14 ? 190  GLU E OE1 1 
ATOM   12978 O  OE2 . GLU E  1 190 ? -14.883 -70.610 -10.436  1.00 244.21 ? 190  GLU E OE2 1 
ATOM   12979 N  N   . ILE E  1 191 ? -17.713 -66.224 -11.619  1.00 229.58 ? 191  ILE E N   1 
ATOM   12980 C  CA  . ILE E  1 191 ? -17.231 -64.846 -11.523  1.00 228.69 ? 191  ILE E CA  1 
ATOM   12981 C  C   . ILE E  1 191 ? -18.302 -63.948 -10.914  1.00 231.89 ? 191  ILE E C   1 
ATOM   12982 O  O   . ILE E  1 191 ? -18.034 -63.163 -9.997   1.00 242.63 ? 191  ILE E O   1 
ATOM   12983 C  CB  . ILE E  1 191 ? -16.790 -64.337 -12.910  1.00 236.47 ? 191  ILE E CB  1 
ATOM   12984 C  CG1 . ILE E  1 191 ? -15.613 -65.159 -13.443  1.00 228.96 ? 191  ILE E CG1 1 
ATOM   12985 C  CG2 . ILE E  1 191 ? -16.437 -62.859 -12.853  1.00 233.49 ? 191  ILE E CG2 1 
ATOM   12986 C  CD1 . ILE E  1 191 ? -15.158 -64.734 -14.823  1.00 220.23 ? 191  ILE E CD1 1 
ATOM   12987 N  N   . VAL E  1 192 ? -19.533 -64.054 -11.415  1.00 226.99 ? 192  VAL E N   1 
ATOM   12988 C  CA  . VAL E  1 192 ? -20.606 -63.195 -10.929  1.00 239.99 ? 192  VAL E CA  1 
ATOM   12989 C  C   . VAL E  1 192 ? -21.129 -63.688 -9.583   1.00 244.46 ? 192  VAL E C   1 
ATOM   12990 O  O   . VAL E  1 192 ? -21.466 -62.887 -8.703   1.00 237.14 ? 192  VAL E O   1 
ATOM   12991 C  CB  . VAL E  1 192 ? -21.722 -63.105 -11.988  1.00 242.78 ? 192  VAL E CB  1 
ATOM   12992 C  CG1 . VAL E  1 192 ? -22.153 -64.495 -12.445  1.00 239.36 ? 192  VAL E CG1 1 
ATOM   12993 C  CG2 . VAL E  1 192 ? -22.905 -62.308 -11.460  1.00 248.07 ? 192  VAL E CG2 1 
ATOM   12994 N  N   . SER E  1 193 ? -21.183 -65.008 -9.391   1.00 243.00 ? 193  SER E N   1 
ATOM   12995 C  CA  . SER E  1 193 ? -21.764 -65.557 -8.171   1.00 245.34 ? 193  SER E CA  1 
ATOM   12996 C  C   . SER E  1 193 ? -20.883 -65.282 -6.958   1.00 240.75 ? 193  SER E C   1 
ATOM   12997 O  O   . SER E  1 193 ? -21.388 -64.950 -5.879   1.00 236.29 ? 193  SER E O   1 
ATOM   12998 C  CB  . SER E  1 193 ? -22.000 -67.058 -8.341   1.00 243.65 ? 193  SER E CB  1 
ATOM   12999 O  OG  . SER E  1 193 ? -20.776 -67.778 -8.333   1.00 234.95 ? 193  SER E OG  1 
ATOM   13000 N  N   . LYS E  1 194 ? -19.567 -65.385 -7.118   1.00 248.56 ? 194  LYS E N   1 
ATOM   13001 C  CA  . LYS E  1 194 ? -18.640 -65.197 -6.011   1.00 241.34 ? 194  LYS E CA  1 
ATOM   13002 C  C   . LYS E  1 194 ? -18.218 -63.747 -5.845   1.00 227.58 ? 194  LYS E C   1 
ATOM   13003 O  O   . LYS E  1 194 ? -17.375 -63.453 -4.992   1.00 226.03 ? 194  LYS E O   1 
ATOM   13004 C  CB  . LYS E  1 194 ? -17.397 -66.071 -6.213   1.00 245.33 ? 194  LYS E CB  1 
ATOM   13005 C  CG  . LYS E  1 194 ? -17.652 -67.565 -6.109   1.00 239.46 ? 194  LYS E CG  1 
ATOM   13006 C  CD  . LYS E  1 194 ? -18.292 -67.921 -4.784   1.00 244.61 ? 194  LYS E CD  1 
ATOM   13007 C  CE  . LYS E  1 194 ? -18.527 -69.416 -4.682   1.00 242.92 ? 194  LYS E CE  1 
ATOM   13008 N  NZ  . LYS E  1 194 ? -19.320 -69.925 -5.834   1.00 242.28 ? 194  LYS E NZ  1 
ATOM   13009 N  N   . TYR E  1 195 ? -18.786 -62.841 -6.634   1.00 224.27 ? 195  TYR E N   1 
ATOM   13010 C  CA  . TYR E  1 195 ? -18.449 -61.430 -6.533   1.00 221.03 ? 195  TYR E CA  1 
ATOM   13011 C  C   . TYR E  1 195 ? -18.990 -60.848 -5.233   1.00 240.54 ? 195  TYR E C   1 
ATOM   13012 O  O   . TYR E  1 195 ? -20.138 -61.102 -4.857   1.00 256.81 ? 195  TYR E O   1 
ATOM   13013 C  CB  . TYR E  1 195 ? -19.017 -60.670 -7.731   1.00 219.72 ? 195  TYR E CB  1 
ATOM   13014 C  CG  . TYR E  1 195 ? -18.900 -59.169 -7.616   1.00 222.60 ? 195  TYR E CG  1 
ATOM   13015 C  CD1 . TYR E  1 195 ? -17.661 -58.546 -7.627   1.00 227.90 ? 195  TYR E CD1 1 
ATOM   13016 C  CD2 . TYR E  1 195 ? -20.033 -58.375 -7.488   1.00 225.10 ? 195  TYR E CD2 1 
ATOM   13017 C  CE1 . TYR E  1 195 ? -17.553 -57.171 -7.517   1.00 229.62 ? 195  TYR E CE1 1 
ATOM   13018 C  CE2 . TYR E  1 195 ? -19.933 -56.999 -7.380   1.00 224.04 ? 195  TYR E CE2 1 
ATOM   13019 C  CZ  . TYR E  1 195 ? -18.691 -56.404 -7.397   1.00 219.59 ? 195  TYR E CZ  1 
ATOM   13020 O  OH  . TYR E  1 195 ? -18.577 -55.039 -7.290   1.00 214.28 ? 195  TYR E OH  1 
ATOM   13021 N  N   . ASP E  1 196 ? -18.156 -60.069 -4.544   1.00 236.60 ? 196  ASP E N   1 
ATOM   13022 C  CA  . ASP E  1 196 ? -18.534 -59.398 -3.305   1.00 229.40 ? 196  ASP E CA  1 
ATOM   13023 C  C   . ASP E  1 196 ? -17.819 -58.057 -3.210   1.00 224.24 ? 196  ASP E C   1 
ATOM   13024 O  O   . ASP E  1 196 ? -16.586 -58.020 -3.101   1.00 221.95 ? 196  ASP E O   1 
ATOM   13025 C  CB  . ASP E  1 196 ? -18.205 -60.263 -2.087   1.00 226.22 ? 196  ASP E CB  1 
ATOM   13026 C  CG  . ASP E  1 196 ? -19.298 -61.264 -1.768   1.00 229.48 ? 196  ASP E CG  1 
ATOM   13027 O  OD1 . ASP E  1 196 ? -20.469 -60.995 -2.105   1.00 230.61 ? 196  ASP E OD1 1 
ATOM   13028 O  OD2 . ASP E  1 196 ? -18.985 -62.323 -1.185   1.00 231.88 ? 196  ASP E OD2 1 
ATOM   13029 N  N   . PRO E  1 197 ? -18.552 -56.940 -3.249   1.00 228.59 ? 197  PRO E N   1 
ATOM   13030 C  CA  . PRO E  1 197 ? -17.893 -55.623 -3.237   1.00 224.70 ? 197  PRO E CA  1 
ATOM   13031 C  C   . PRO E  1 197 ? -17.127 -55.333 -1.959   1.00 228.59 ? 197  PRO E C   1 
ATOM   13032 O  O   . PRO E  1 197 ? -16.384 -54.345 -1.915   1.00 232.58 ? 197  PRO E O   1 
ATOM   13033 C  CB  . PRO E  1 197 ? -19.061 -54.643 -3.423   1.00 233.30 ? 197  PRO E CB  1 
ATOM   13034 C  CG  . PRO E  1 197 ? -20.248 -55.382 -2.909   1.00 243.43 ? 197  PRO E CG  1 
ATOM   13035 C  CD  . PRO E  1 197 ? -20.018 -56.819 -3.290   1.00 239.69 ? 197  PRO E CD  1 
ATOM   13036 N  N   . ASN E  1 198 ? -17.288 -56.149 -0.921   1.00 233.41 ? 198  ASN E N   1 
ATOM   13037 C  CA  . ASN E  1 198 ? -16.576 -55.984 0.336    1.00 242.00 ? 198  ASN E CA  1 
ATOM   13038 C  C   . ASN E  1 198 ? -15.403 -56.942 0.477    1.00 250.71 ? 198  ASN E C   1 
ATOM   13039 O  O   . ASN E  1 198 ? -14.707 -56.905 1.497    1.00 251.65 ? 198  ASN E O   1 
ATOM   13040 C  CB  . ASN E  1 198 ? -17.541 -56.180 1.506    1.00 248.73 ? 198  ASN E CB  1 
ATOM   13041 C  CG  . ASN E  1 198 ? -18.258 -57.512 1.442    1.00 249.91 ? 198  ASN E CG  1 
ATOM   13042 O  OD1 . ASN E  1 198 ? -18.555 -58.016 0.358    1.00 241.45 ? 198  ASN E OD1 1 
ATOM   13043 N  ND2 . ASN E  1 198 ? -18.547 -58.088 2.603    1.00 260.74 ? 198  ASN E ND2 1 
ATOM   13044 N  N   . VAL E  1 199 ? -15.170 -57.795 -0.518   1.00 248.60 ? 199  VAL E N   1 
ATOM   13045 C  CA  . VAL E  1 199 ? -14.056 -58.738 -0.526   1.00 239.69 ? 199  VAL E CA  1 
ATOM   13046 C  C   . VAL E  1 199 ? -13.103 -58.328 -1.639   1.00 233.43 ? 199  VAL E C   1 
ATOM   13047 O  O   . VAL E  1 199 ? -13.489 -58.282 -2.814   1.00 227.96 ? 199  VAL E O   1 
ATOM   13048 C  CB  . VAL E  1 199 ? -14.535 -60.184 -0.718   1.00 239.58 ? 199  VAL E CB  1 
ATOM   13049 C  CG1 . VAL E  1 199 ? -13.349 -61.144 -0.681   1.00 242.72 ? 199  VAL E CG1 1 
ATOM   13050 C  CG2 . VAL E  1 199 ? -15.557 -60.551 0.347    1.00 239.46 ? 199  VAL E CG2 1 
ATOM   13051 N  N   . TYR E  1 200 ? -11.856 -58.041 -1.273   1.00 233.53 ? 200  TYR E N   1 
ATOM   13052 C  CA  . TYR E  1 200 ? -10.887 -57.550 -2.238   1.00 231.42 ? 200  TYR E CA  1 
ATOM   13053 C  C   . TYR E  1 200 ? -10.053 -58.663 -2.849   1.00 226.73 ? 200  TYR E C   1 
ATOM   13054 O  O   . TYR E  1 200 ? -9.449  -58.458 -3.908   1.00 223.98 ? 200  TYR E O   1 
ATOM   13055 C  CB  . TYR E  1 200 ? -9.952  -56.530 -1.581   1.00 229.69 ? 200  TYR E CB  1 
ATOM   13056 C  CG  . TYR E  1 200 ? -10.661 -55.481 -0.757   1.00 237.33 ? 200  TYR E CG  1 
ATOM   13057 C  CD1 . TYR E  1 200 ? -11.821 -54.871 -1.217   1.00 239.39 ? 200  TYR E CD1 1 
ATOM   13058 C  CD2 . TYR E  1 200 ? -10.174 -55.109 0.490    1.00 257.32 ? 200  TYR E CD2 1 
ATOM   13059 C  CE1 . TYR E  1 200 ? -12.473 -53.910 -0.458   1.00 258.08 ? 200  TYR E CE1 1 
ATOM   13060 C  CE2 . TYR E  1 200 ? -10.819 -54.150 1.257    1.00 272.13 ? 200  TYR E CE2 1 
ATOM   13061 C  CZ  . TYR E  1 200 ? -11.968 -53.554 0.779    1.00 269.86 ? 200  TYR E CZ  1 
ATOM   13062 O  OH  . TYR E  1 200 ? -12.611 -52.601 1.538    1.00 263.85 ? 200  TYR E OH  1 
ATOM   13063 N  N   . SER E  1 201 ? -10.019 -59.837 -2.224   1.00 214.46 ? 201  SER E N   1 
ATOM   13064 C  CA  . SER E  1 201 ? -9.272  -60.987 -2.729   1.00 214.51 ? 201  SER E CA  1 
ATOM   13065 C  C   . SER E  1 201 ? -10.208 -62.190 -2.712   1.00 219.96 ? 201  SER E C   1 
ATOM   13066 O  O   . SER E  1 201 ? -10.319 -62.888 -1.701   1.00 222.12 ? 201  SER E O   1 
ATOM   13067 C  CB  . SER E  1 201 ? -8.022  -61.233 -1.901   1.00 216.01 ? 201  SER E CB  1 
ATOM   13068 O  OG  . SER E  1 201 ? -7.120  -60.149 -2.014   1.00 214.22 ? 201  SER E OG  1 
ATOM   13069 N  N   . ILE E  1 202 ? -10.888 -62.421 -3.827   1.00 227.36 ? 202  ILE E N   1 
ATOM   13070 C  CA  . ILE E  1 202 ? -11.833 -63.522 -3.942   1.00 227.57 ? 202  ILE E CA  1 
ATOM   13071 C  C   . ILE E  1 202 ? -11.108 -64.731 -4.513   1.00 222.89 ? 202  ILE E C   1 
ATOM   13072 O  O   . ILE E  1 202 ? -10.467 -64.645 -5.569   1.00 214.44 ? 202  ILE E O   1 
ATOM   13073 C  CB  . ILE E  1 202 ? -13.032 -63.131 -4.820   1.00 235.11 ? 202  ILE E CB  1 
ATOM   13074 C  CG1 . ILE E  1 202 ? -13.700 -61.866 -4.278   1.00 242.36 ? 202  ILE E CG1 1 
ATOM   13075 C  CG2 . ILE E  1 202 ? -14.034 -64.269 -4.884   1.00 237.63 ? 202  ILE E CG2 1 
ATOM   13076 C  CD1 . ILE E  1 202 ? -14.874 -61.393 -5.109   1.00 242.48 ? 202  ILE E CD1 1 
ATOM   13077 N  N   . LYS E  1 203 ? -11.204 -65.857 -3.813   1.00 226.33 ? 203  LYS E N   1 
ATOM   13078 C  CA  . LYS E  1 203 ? -10.614 -67.114 -4.254   1.00 233.36 ? 203  LYS E CA  1 
ATOM   13079 C  C   . LYS E  1 203 ? -11.672 -67.939 -4.972   1.00 235.07 ? 203  LYS E C   1 
ATOM   13080 O  O   . LYS E  1 203 ? -12.756 -68.179 -4.428   1.00 227.63 ? 203  LYS E O   1 
ATOM   13081 C  CB  . LYS E  1 203 ? -10.042 -67.900 -3.074   1.00 236.91 ? 203  LYS E CB  1 
ATOM   13082 C  CG  . LYS E  1 203 ? -9.093  -69.013 -3.489   1.00 230.51 ? 203  LYS E CG  1 
ATOM   13083 C  CD  . LYS E  1 203 ? -8.056  -68.491 -4.469   1.00 222.54 ? 203  LYS E CD  1 
ATOM   13084 C  CE  . LYS E  1 203 ? -7.168  -69.603 -4.990   1.00 221.98 ? 203  LYS E CE  1 
ATOM   13085 N  NZ  . LYS E  1 203 ? -6.204  -69.088 -6.000   1.00 216.00 ? 203  LYS E NZ  1 
ATOM   13086 N  N   . TYR E  1 204 ? -11.353 -68.372 -6.187   1.00 246.38 ? 204  TYR E N   1 
ATOM   13087 C  CA  . TYR E  1 204 ? -12.250 -69.176 -7.003   1.00 261.21 ? 204  TYR E CA  1 
ATOM   13088 C  C   . TYR E  1 204 ? -11.752 -70.616 -7.057   1.00 269.06 ? 204  TYR E C   1 
ATOM   13089 O  O   . TYR E  1 204 ? -10.559 -70.857 -7.272   1.00 269.70 ? 204  TYR E O   1 
ATOM   13090 C  CB  . TYR E  1 204 ? -12.371 -68.582 -8.407   1.00 254.69 ? 204  TYR E CB  1 
ATOM   13091 C  CG  . TYR E  1 204 ? -12.705 -67.100 -8.419   1.00 244.97 ? 204  TYR E CG  1 
ATOM   13092 C  CD1 . TYR E  1 204 ? -14.018 -66.666 -8.291   1.00 238.38 ? 204  TYR E CD1 1 
ATOM   13093 C  CD2 . TYR E  1 204 ? -11.706 -66.138 -8.548   1.00 238.34 ? 204  TYR E CD2 1 
ATOM   13094 C  CE1 . TYR E  1 204 ? -14.330 -65.320 -8.303   1.00 232.42 ? 204  TYR E CE1 1 
ATOM   13095 C  CE2 . TYR E  1 204 ? -12.011 -64.786 -8.559   1.00 228.74 ? 204  TYR E CE2 1 
ATOM   13096 C  CZ  . TYR E  1 204 ? -13.324 -64.385 -8.436   1.00 223.34 ? 204  TYR E CZ  1 
ATOM   13097 O  OH  . TYR E  1 204 ? -13.640 -63.046 -8.445   1.00 220.35 ? 204  TYR E OH  1 
ATOM   13098 N  N   . ASN E  1 205 ? -12.669 -71.568 -6.835   1.00 271.54 ? 205  ASN E N   1 
ATOM   13099 C  CA  . ASN E  1 205 ? -12.296 -72.979 -6.748   1.00 263.12 ? 205  ASN E CA  1 
ATOM   13100 C  C   . ASN E  1 205 ? -11.991 -73.576 -8.120   1.00 260.34 ? 205  ASN E C   1 
ATOM   13101 O  O   . ASN E  1 205 ? -11.062 -74.381 -8.257   1.00 265.91 ? 205  ASN E O   1 
ATOM   13102 C  CB  . ASN E  1 205 ? -13.396 -73.777 -6.048   1.00 262.11 ? 205  ASN E CB  1 
ATOM   13103 C  CG  . ASN E  1 205 ? -14.783 -73.396 -6.517   1.00 264.16 ? 205  ASN E CG  1 
ATOM   13104 O  OD1 . ASN E  1 205 ? -15.398 -72.476 -5.979   1.00 269.99 ? 205  ASN E OD1 1 
ATOM   13105 N  ND2 . ASN E  1 205 ? -15.284 -74.103 -7.522   1.00 258.23 ? 205  ASN E ND2 1 
ATOM   13106 N  N   . ASN E  1 206 ? -12.763 -73.214 -9.145   1.00 247.51 ? 206  ASN E N   1 
ATOM   13107 C  CA  . ASN E  1 206 ? -12.544 -73.724 -10.491  1.00 237.46 ? 206  ASN E CA  1 
ATOM   13108 C  C   . ASN E  1 206 ? -11.544 -72.882 -11.275  1.00 234.72 ? 206  ASN E C   1 
ATOM   13109 O  O   . ASN E  1 206 ? -11.577 -72.882 -12.512  1.00 228.54 ? 206  ASN E O   1 
ATOM   13110 C  CB  . ASN E  1 206 ? -13.871 -73.813 -11.246  1.00 236.97 ? 206  ASN E CB  1 
ATOM   13111 C  CG  . ASN E  1 206 ? -14.873 -74.719 -10.557  1.00 239.26 ? 206  ASN E CG  1 
ATOM   13112 O  OD1 . ASN E  1 206 ? -14.503 -75.741 -9.977   1.00 241.80 ? 206  ASN E OD1 1 
ATOM   13113 N  ND2 . ASN E  1 206 ? -16.147 -74.343 -10.606  1.00 241.12 ? 206  ASN E ND2 1 
ATOM   13114 N  N   . GLN E  1 207 ? -10.664 -72.166 -10.577  1.00 240.69 ? 207  GLN E N   1 
ATOM   13115 C  CA  . GLN E  1 207 ? -9.659  -71.334 -11.224  1.00 229.87 ? 207  GLN E CA  1 
ATOM   13116 C  C   . GLN E  1 207 ? -8.550  -72.206 -11.797  1.00 218.26 ? 207  GLN E C   1 
ATOM   13117 O  O   . GLN E  1 207 ? -8.023  -73.091 -11.116  1.00 223.17 ? 207  GLN E O   1 
ATOM   13118 C  CB  . GLN E  1 207 ? -9.087  -70.329 -10.215  1.00 224.30 ? 207  GLN E CB  1 
ATOM   13119 C  CG  . GLN E  1 207 ? -8.153  -69.263 -10.787  1.00 208.22 ? 207  GLN E CG  1 
ATOM   13120 C  CD  . GLN E  1 207 ? -7.733  -68.232 -9.741   1.00 206.26 ? 207  GLN E CD  1 
ATOM   13121 O  OE1 . GLN E  1 207 ? -8.395  -68.065 -8.715   1.00 210.09 ? 207  GLN E OE1 1 
ATOM   13122 N  NE2 . GLN E  1 207 ? -6.633  -67.535 -10.001  1.00 200.27 ? 207  GLN E NE2 1 
ATOM   13123 N  N   . LEU E  1 208 ? -8.192  -71.947 -13.047  1.00 202.55 ? 208  LEU E N   1 
ATOM   13124 C  CA  . LEU E  1 208 ? -7.061  -72.592 -13.695  1.00 201.07 ? 208  LEU E CA  1 
ATOM   13125 C  C   . LEU E  1 208 ? -5.956  -71.559 -13.854  1.00 209.44 ? 208  LEU E C   1 
ATOM   13126 O  O   . LEU E  1 208 ? -6.182  -70.493 -14.436  1.00 213.59 ? 208  LEU E O   1 
ATOM   13127 C  CB  . LEU E  1 208 ? -7.474  -73.165 -15.054  1.00 198.33 ? 208  LEU E CB  1 
ATOM   13128 C  CG  . LEU E  1 208 ? -8.493  -74.303 -15.018  1.00 206.07 ? 208  LEU E CG  1 
ATOM   13129 C  CD1 . LEU E  1 208 ? -8.813  -74.787 -16.419  1.00 205.57 ? 208  LEU E CD1 1 
ATOM   13130 C  CD2 . LEU E  1 208 ? -7.964  -75.441 -14.167  1.00 209.36 ? 208  LEU E CD2 1 
ATOM   13131 N  N   . ALA E  1 209 ? -4.760  -71.874 -13.356  1.00 217.03 ? 209  ALA E N   1 
ATOM   13132 C  CA  . ALA E  1 209 ? -3.683  -70.896 -13.379  1.00 210.68 ? 209  ALA E CA  1 
ATOM   13133 C  C   . ALA E  1 209 ? -2.335  -71.580 -13.562  1.00 205.85 ? 209  ALA E C   1 
ATOM   13134 O  O   . ALA E  1 209 ? -2.101  -72.666 -13.023  1.00 204.60 ? 209  ALA E O   1 
ATOM   13135 C  CB  . ALA E  1 209 ? -3.678  -70.064 -12.091  1.00 205.94 ? 209  ALA E CB  1 
ATOM   13136 N  N   . THR E  1 210 ? -1.457  -70.933 -14.332  1.00 207.13 ? 210  THR E N   1 
ATOM   13137 C  CA  . THR E  1 210 ? -0.076  -71.385 -14.504  1.00 212.01 ? 210  THR E CA  1 
ATOM   13138 C  C   . THR E  1 210 ? 0.727   -71.004 -13.268  1.00 202.54 ? 210  THR E C   1 
ATOM   13139 O  O   . THR E  1 210 ? 1.014   -69.825 -13.038  1.00 193.79 ? 210  THR E O   1 
ATOM   13140 C  CB  . THR E  1 210 ? 0.546   -70.785 -15.760  1.00 212.48 ? 210  THR E CB  1 
ATOM   13141 O  OG1 . THR E  1 210 ? 0.375   -69.365 -15.745  1.00 212.43 ? 210  THR E OG1 1 
ATOM   13142 C  CG2 . THR E  1 210 ? -0.118  -71.353 -17.005  1.00 218.58 ? 210  THR E CG2 1 
ATOM   13143 N  N   . ARG E  1 211 ? 1.081   -72.003 -12.471  1.00 209.17 ? 211  ARG E N   1 
ATOM   13144 C  CA  . ARG E  1 211 ? 1.787   -71.777 -11.225  1.00 209.52 ? 211  ARG E CA  1 
ATOM   13145 C  C   . ARG E  1 211 ? 3.248   -71.387 -11.490  1.00 217.43 ? 211  ARG E C   1 
ATOM   13146 O  O   . ARG E  1 211 ? 3.777   -71.539 -12.594  1.00 220.97 ? 211  ARG E O   1 
ATOM   13147 C  CB  . ARG E  1 211 ? 1.653   -73.021 -10.348  1.00 213.99 ? 211  ARG E CB  1 
ATOM   13148 C  CG  . ARG E  1 211 ? 0.192   -73.254 -9.959   1.00 225.55 ? 211  ARG E CG  1 
ATOM   13149 C  CD  . ARG E  1 211 ? -0.053  -74.540 -9.194   1.00 242.78 ? 211  ARG E CD  1 
ATOM   13150 N  NE  . ARG E  1 211 ? -1.455  -74.648 -8.798   1.00 252.57 ? 211  ARG E NE  1 
ATOM   13151 C  CZ  . ARG E  1 211 ? -2.414  -75.174 -9.555   1.00 247.24 ? 211  ARG E CZ  1 
ATOM   13152 N  NH1 . ARG E  1 211 ? -2.138  -75.646 -10.764  1.00 240.94 ? 211  ARG E NH1 1 
ATOM   13153 N  NH2 . ARG E  1 211 ? -3.658  -75.223 -9.103   1.00 247.67 ? 211  ARG E NH2 1 
ATOM   13154 N  N   . THR E  1 212 ? 3.897   -70.870 -10.446  1.00 212.05 ? 212  THR E N   1 
ATOM   13155 C  CA  . THR E  1 212 ? 5.261   -70.355 -10.549  1.00 206.29 ? 212  THR E CA  1 
ATOM   13156 C  C   . THR E  1 212 ? 6.288   -71.454 -10.829  1.00 211.32 ? 212  THR E C   1 
ATOM   13157 O  O   . THR E  1 212 ? 6.175   -72.582 -10.343  1.00 216.77 ? 212  THR E O   1 
ATOM   13158 C  CB  . THR E  1 212 ? 5.632   -69.607 -9.266   1.00 205.75 ? 212  THR E CB  1 
ATOM   13159 O  OG1 . THR E  1 212 ? 7.023   -69.266 -9.285   1.00 203.03 ? 212  THR E OG1 1 
ATOM   13160 C  CG2 . THR E  1 212 ? 5.328   -70.450 -8.028   1.00 216.54 ? 212  THR E CG2 1 
ATOM   13161 N  N   . ALA E  1 213 ? 7.290   -71.117 -11.635  1.00 206.89 ? 213  ALA E N   1 
ATOM   13162 C  CA  . ALA E  1 213 ? 8.357   -72.029 -12.026  1.00 205.57 ? 213  ALA E CA  1 
ATOM   13163 C  C   . ALA E  1 213 ? 9.708   -71.508 -11.522  1.00 203.37 ? 213  ALA E C   1 
ATOM   13164 O  O   . ALA E  1 213 ? 9.781   -70.631 -10.656  1.00 206.92 ? 213  ALA E O   1 
ATOM   13165 C  CB  . ALA E  1 213 ? 8.352   -72.231 -13.542  1.00 200.22 ? 213  ALA E CB  1 
ATOM   13166 N  N   . GLN E  1 214 ? 10.783  -72.095 -12.048  1.00 196.08 ? 214  GLN E N   1 
ATOM   13167 C  CA  . GLN E  1 214 ? 12.139  -71.739 -11.654  1.00 191.45 ? 214  GLN E CA  1 
ATOM   13168 C  C   . GLN E  1 214 ? 12.483  -70.307 -12.058  1.00 189.02 ? 214  GLN E C   1 
ATOM   13169 O  O   . GLN E  1 214 ? 11.881  -69.719 -12.958  1.00 190.75 ? 214  GLN E O   1 
ATOM   13170 C  CB  . GLN E  1 214 ? 13.156  -72.698 -12.266  1.00 192.42 ? 214  GLN E CB  1 
ATOM   13171 C  CG  . GLN E  1 214 ? 13.005  -74.141 -11.831  1.00 196.32 ? 214  GLN E CG  1 
ATOM   13172 C  CD  . GLN E  1 214 ? 12.011  -74.910 -12.671  1.00 187.45 ? 214  GLN E CD  1 
ATOM   13173 O  OE1 . GLN E  1 214 ? 11.085  -74.337 -13.244  1.00 185.48 ? 214  GLN E OE1 1 
ATOM   13174 N  NE2 . GLN E  1 214 ? 12.201  -76.219 -12.750  1.00 188.78 ? 214  GLN E NE2 1 
ATOM   13175 N  N   . ALA E  1 215 ? 13.494  -69.758 -11.376  1.00 164.55 ? 215  ALA E N   1 
ATOM   13176 C  CA  . ALA E  1 215 ? 13.887  -68.363 -11.557  1.00 177.62 ? 215  ALA E CA  1 
ATOM   13177 C  C   . ALA E  1 215 ? 14.419  -68.053 -12.955  1.00 186.90 ? 215  ALA E C   1 
ATOM   13178 O  O   . ALA E  1 215 ? 14.461  -66.876 -13.331  1.00 189.94 ? 215  ALA E O   1 
ATOM   13179 C  CB  . ALA E  1 215 ? 14.928  -67.978 -10.506  1.00 185.78 ? 215  ALA E CB  1 
ATOM   13180 N  N   . ILE E  1 216 ? 14.854  -69.058 -13.725  1.00 199.55 ? 216  ILE E N   1 
ATOM   13181 C  CA  . ILE E  1 216 ? 15.367  -68.783 -15.067  1.00 188.79 ? 216  ILE E CA  1 
ATOM   13182 C  C   . ILE E  1 216 ? 14.265  -68.270 -15.987  1.00 172.49 ? 216  ILE E C   1 
ATOM   13183 O  O   . ILE E  1 216 ? 14.554  -67.582 -16.977  1.00 158.60 ? 216  ILE E O   1 
ATOM   13184 C  CB  . ILE E  1 216 ? 16.040  -70.032 -15.678  1.00 170.13 ? 216  ILE E CB  1 
ATOM   13185 C  CG1 . ILE E  1 216 ? 16.813  -69.667 -16.955  1.00 160.67 ? 216  ILE E CG1 1 
ATOM   13186 C  CG2 . ILE E  1 216 ? 15.009  -71.114 -15.958  1.00 173.73 ? 216  ILE E CG2 1 
ATOM   13187 C  CD1 . ILE E  1 216 ? 17.421  -70.852 -17.688  1.00 154.67 ? 216  ILE E CD1 1 
ATOM   13188 N  N   . PHE E  1 217 ? 13.006  -68.567 -15.675  1.00 181.23 ? 217  PHE E N   1 
ATOM   13189 C  CA  . PHE E  1 217 ? 11.878  -68.165 -16.502  1.00 184.47 ? 217  PHE E CA  1 
ATOM   13190 C  C   . PHE E  1 217 ? 11.330  -66.790 -16.139  1.00 200.57 ? 217  PHE E C   1 
ATOM   13191 O  O   . PHE E  1 217 ? 10.350  -66.355 -16.753  1.00 201.55 ? 217  PHE E O   1 
ATOM   13192 C  CB  . PHE E  1 217 ? 10.757  -69.207 -16.408  1.00 171.78 ? 217  PHE E CB  1 
ATOM   13193 C  CG  . PHE E  1 217 ? 11.144  -70.562 -16.925  1.00 173.25 ? 217  PHE E CG  1 
ATOM   13194 C  CD1 . PHE E  1 217 ? 11.228  -70.802 -18.289  1.00 189.40 ? 217  PHE E CD1 1 
ATOM   13195 C  CD2 . PHE E  1 217 ? 11.412  -71.599 -16.048  1.00 180.89 ? 217  PHE E CD2 1 
ATOM   13196 C  CE1 . PHE E  1 217 ? 11.581  -72.050 -18.769  1.00 194.68 ? 217  PHE E CE1 1 
ATOM   13197 C  CE2 . PHE E  1 217 ? 11.765  -72.850 -16.519  1.00 200.36 ? 217  PHE E CE2 1 
ATOM   13198 C  CZ  . PHE E  1 217 ? 11.849  -73.077 -17.882  1.00 203.68 ? 217  PHE E CZ  1 
ATOM   13199 N  N   . ASP E  1 218 ? 11.926  -66.102 -15.163  1.00 206.35 ? 218  ASP E N   1 
ATOM   13200 C  CA  . ASP E  1 218 ? 11.536  -64.727 -14.885  1.00 195.48 ? 218  ASP E CA  1 
ATOM   13201 C  C   . ASP E  1 218 ? 11.764  -63.864 -16.119  1.00 179.67 ? 218  ASP E C   1 
ATOM   13202 O  O   . ASP E  1 218 ? 12.592  -64.179 -16.981  1.00 163.58 ? 218  ASP E O   1 
ATOM   13203 C  CB  . ASP E  1 218 ? 12.327  -64.147 -13.703  1.00 196.03 ? 218  ASP E CB  1 
ATOM   13204 C  CG  . ASP E  1 218 ? 12.014  -64.830 -12.378  1.00 189.08 ? 218  ASP E CG  1 
ATOM   13205 O  OD1 . ASP E  1 218 ? 11.099  -65.675 -12.338  1.00 190.52 ? 218  ASP E OD1 1 
ATOM   13206 O  OD2 . ASP E  1 218 ? 12.680  -64.504 -11.368  1.00 185.68 ? 218  ASP E OD2 1 
ATOM   13207 N  N   . ASP E  1 219 ? 11.012  -62.766 -16.198  1.00 189.94 ? 219  ASP E N   1 
ATOM   13208 C  CA  . ASP E  1 219 ? 11.129  -61.815 -17.301  1.00 190.30 ? 219  ASP E CA  1 
ATOM   13209 C  C   . ASP E  1 219 ? 10.815  -62.500 -18.633  1.00 182.09 ? 219  ASP E C   1 
ATOM   13210 O  O   . ASP E  1 219 ? 11.579  -62.433 -19.596  1.00 181.75 ? 219  ASP E O   1 
ATOM   13211 C  CB  . ASP E  1 219 ? 12.519  -61.166 -17.307  1.00 205.81 ? 219  ASP E CB  1 
ATOM   13212 C  CG  . ASP E  1 219 ? 12.644  -60.045 -18.318  1.00 234.83 ? 219  ASP E CG  1 
ATOM   13213 O  OD1 . ASP E  1 219 ? 11.711  -59.221 -18.414  1.00 237.13 ? 219  ASP E OD1 1 
ATOM   13214 O  OD2 . ASP E  1 219 ? 13.681  -59.988 -19.011  1.00 254.56 ? 219  ASP E OD2 1 
ATOM   13215 N  N   . SER E  1 220 ? 9.672   -63.181 -18.679  1.00 181.80 ? 220  SER E N   1 
ATOM   13216 C  CA  . SER E  1 220 ? 9.243   -63.894 -19.875  1.00 181.04 ? 220  SER E CA  1 
ATOM   13217 C  C   . SER E  1 220 ? 8.000   -63.303 -20.520  1.00 188.66 ? 220  SER E C   1 
ATOM   13218 O  O   . SER E  1 220 ? 7.819   -63.452 -21.731  1.00 195.81 ? 220  SER E O   1 
ATOM   13219 C  CB  . SER E  1 220 ? 8.979   -65.372 -19.553  1.00 170.48 ? 220  SER E CB  1 
ATOM   13220 O  OG  . SER E  1 220 ? 10.186  -66.068 -19.300  1.00 165.45 ? 220  SER E OG  1 
ATOM   13221 N  N   . TYR E  1 221 ? 7.142   -62.649 -19.735  1.00 182.39 ? 221  TYR E N   1 
ATOM   13222 C  CA  . TYR E  1 221 ? 5.936   -61.990 -20.238  1.00 169.13 ? 221  TYR E CA  1 
ATOM   13223 C  C   . TYR E  1 221 ? 4.945   -62.997 -20.831  1.00 165.97 ? 221  TYR E C   1 
ATOM   13224 O  O   . TYR E  1 221 ? 4.377   -62.775 -21.902  1.00 160.74 ? 221  TYR E O   1 
ATOM   13225 C  CB  . TYR E  1 221 ? 6.279   -60.899 -21.262  1.00 165.18 ? 221  TYR E CB  1 
ATOM   13226 C  CG  . TYR E  1 221 ? 7.015   -59.682 -20.713  1.00 171.83 ? 221  TYR E CG  1 
ATOM   13227 C  CD1 . TYR E  1 221 ? 7.402   -59.607 -19.379  1.00 206.19 ? 221  TYR E CD1 1 
ATOM   13228 C  CD2 . TYR E  1 221 ? 7.323   -58.606 -21.540  1.00 168.47 ? 221  TYR E CD2 1 
ATOM   13229 C  CE1 . TYR E  1 221 ? 8.074   -58.495 -18.887  1.00 209.58 ? 221  TYR E CE1 1 
ATOM   13230 C  CE2 . TYR E  1 221 ? 7.992   -57.493 -21.057  1.00 171.50 ? 221  TYR E CE2 1 
ATOM   13231 C  CZ  . TYR E  1 221 ? 8.366   -57.443 -19.730  1.00 185.39 ? 221  TYR E CZ  1 
ATOM   13232 O  OH  . TYR E  1 221 ? 9.032   -56.343 -19.239  1.00 180.41 ? 221  TYR E OH  1 
ATOM   13233 N  N   . LEU E  1 222 ? 4.762   -64.130 -20.149  1.00 173.42 ? 222  LEU E N   1 
ATOM   13234 C  CA  . LEU E  1 222 ? 3.685   -65.048 -20.505  1.00 185.16 ? 222  LEU E CA  1 
ATOM   13235 C  C   . LEU E  1 222 ? 2.334   -64.387 -20.265  1.00 172.73 ? 222  LEU E C   1 
ATOM   13236 O  O   . LEU E  1 222 ? 2.074   -63.853 -19.185  1.00 171.52 ? 222  LEU E O   1 
ATOM   13237 C  CB  . LEU E  1 222 ? 3.788   -66.345 -19.700  1.00 200.54 ? 222  LEU E CB  1 
ATOM   13238 C  CG  . LEU E  1 222 ? 2.541   -67.234 -19.734  1.00 191.48 ? 222  LEU E CG  1 
ATOM   13239 C  CD1 . LEU E  1 222 ? 2.278   -67.742 -21.143  1.00 188.93 ? 222  LEU E CD1 1 
ATOM   13240 C  CD2 . LEU E  1 222 ? 2.662   -68.391 -18.757  1.00 189.96 ? 222  LEU E CD2 1 
ATOM   13241 N  N   . GLY E  1 223 ? 1.463   -64.442 -21.267  1.00 178.31 ? 223  GLY E N   1 
ATOM   13242 C  CA  . GLY E  1 223 ? 0.181   -63.773 -21.199  1.00 183.98 ? 223  GLY E CA  1 
ATOM   13243 C  C   . GLY E  1 223 ? 0.131   -62.445 -21.914  1.00 182.58 ? 223  GLY E C   1 
ATOM   13244 O  O   . GLY E  1 223 ? -0.863  -61.720 -21.774  1.00 177.70 ? 223  GLY E O   1 
ATOM   13245 N  N   . TYR E  1 224 ? 1.179   -62.103 -22.669  1.00 182.47 ? 224  TYR E N   1 
ATOM   13246 C  CA  . TYR E  1 224 ? 1.222   -60.834 -23.386  1.00 167.38 ? 224  TYR E CA  1 
ATOM   13247 C  C   . TYR E  1 224 ? 0.091   -60.733 -24.401  1.00 168.43 ? 224  TYR E C   1 
ATOM   13248 O  O   . TYR E  1 224 ? -0.475  -59.654 -24.605  1.00 167.63 ? 224  TYR E O   1 
ATOM   13249 C  CB  . TYR E  1 224 ? 2.580   -60.681 -24.069  1.00 169.99 ? 224  TYR E CB  1 
ATOM   13250 C  CG  . TYR E  1 224 ? 2.888   -59.284 -24.555  1.00 184.31 ? 224  TYR E CG  1 
ATOM   13251 C  CD1 . TYR E  1 224 ? 3.492   -58.355 -23.716  1.00 199.66 ? 224  TYR E CD1 1 
ATOM   13252 C  CD2 . TYR E  1 224 ? 2.592   -58.898 -25.855  1.00 180.60 ? 224  TYR E CD2 1 
ATOM   13253 C  CE1 . TYR E  1 224 ? 3.784   -57.077 -24.154  1.00 192.87 ? 224  TYR E CE1 1 
ATOM   13254 C  CE2 . TYR E  1 224 ? 2.879   -57.622 -26.301  1.00 176.23 ? 224  TYR E CE2 1 
ATOM   13255 C  CZ  . TYR E  1 224 ? 3.476   -56.717 -25.446  1.00 182.52 ? 224  TYR E CZ  1 
ATOM   13256 O  OH  . TYR E  1 224 ? 3.765   -55.446 -25.887  1.00 185.13 ? 224  TYR E OH  1 
ATOM   13257 N  N   . SER E  1 225 ? -0.250  -61.847 -25.046  1.00 174.79 ? 225  SER E N   1 
ATOM   13258 C  CA  . SER E  1 225 ? -1.381  -61.918 -25.961  1.00 180.70 ? 225  SER E CA  1 
ATOM   13259 C  C   . SER E  1 225 ? -2.050  -63.278 -25.807  1.00 187.90 ? 225  SER E C   1 
ATOM   13260 O  O   . SER E  1 225 ? -1.418  -64.250 -25.388  1.00 193.12 ? 225  SER E O   1 
ATOM   13261 C  CB  . SER E  1 225 ? -0.937  -61.685 -27.411  1.00 180.63 ? 225  SER E CB  1 
ATOM   13262 O  OG  . SER E  1 225 ? -0.023  -62.686 -27.828  1.00 181.35 ? 225  SER E OG  1 
ATOM   13263 N  N   . VAL E  1 226 ? -3.346  -63.343 -26.143  1.00 176.64 ? 226  VAL E N   1 
ATOM   13264 C  CA  . VAL E  1 226 ? -4.120  -64.569 -25.983  1.00 178.30 ? 226  VAL E CA  1 
ATOM   13265 C  C   . VAL E  1 226 ? -5.074  -64.778 -27.154  1.00 167.65 ? 226  VAL E C   1 
ATOM   13266 O  O   . VAL E  1 226 ? -5.465  -63.842 -27.854  1.00 162.35 ? 226  VAL E O   1 
ATOM   13267 C  CB  . VAL E  1 226 ? -4.925  -64.589 -24.663  1.00 181.15 ? 226  VAL E CB  1 
ATOM   13268 C  CG1 . VAL E  1 226 ? -3.993  -64.685 -23.460  1.00 168.56 ? 226  VAL E CG1 1 
ATOM   13269 C  CG2 . VAL E  1 226 ? -5.821  -63.367 -24.574  1.00 183.96 ? 226  VAL E CG2 1 
ATOM   13270 N  N   . ALA E  1 227 ? -5.468  -66.040 -27.322  1.00 166.07 ? 227  ALA E N   1 
ATOM   13271 C  CA  . ALA E  1 227 ? -6.425  -66.491 -28.324  1.00 173.79 ? 227  ALA E CA  1 
ATOM   13272 C  C   . ALA E  1 227 ? -6.920  -67.863 -27.891  1.00 181.56 ? 227  ALA E C   1 
ATOM   13273 O  O   . ALA E  1 227 ? -6.287  -68.530 -27.071  1.00 179.85 ? 227  ALA E O   1 
ATOM   13274 C  CB  . ALA E  1 227 ? -5.800  -66.547 -29.721  1.00 181.74 ? 227  ALA E CB  1 
ATOM   13275 N  N   . VAL E  1 228 ? -8.058  -68.282 -28.444  1.00 180.08 ? 228  VAL E N   1 
ATOM   13276 C  CA  . VAL E  1 228 ? -8.682  -69.538 -28.042  1.00 190.63 ? 228  VAL E CA  1 
ATOM   13277 C  C   . VAL E  1 228 ? -8.976  -70.406 -29.260  1.00 203.44 ? 228  VAL E C   1 
ATOM   13278 O  O   . VAL E  1 228 ? -9.157  -69.909 -30.376  1.00 207.89 ? 228  VAL E O   1 
ATOM   13279 C  CB  . VAL E  1 228 ? -9.972  -69.297 -27.228  1.00 195.95 ? 228  VAL E CB  1 
ATOM   13280 C  CG1 . VAL E  1 228 ? -9.659  -68.532 -25.952  1.00 196.36 ? 228  VAL E CG1 1 
ATOM   13281 C  CG2 . VAL E  1 228 ? -10.986 -68.543 -28.065  1.00 200.96 ? 228  VAL E CG2 1 
ATOM   13282 N  N   . GLY E  1 229 ? -9.025  -71.720 -29.029  1.00 207.58 ? 229  GLY E N   1 
ATOM   13283 C  CA  . GLY E  1 229 ? -9.291  -72.702 -30.067  1.00 210.21 ? 229  GLY E CA  1 
ATOM   13284 C  C   . GLY E  1 229 ? -9.014  -74.122 -29.609  1.00 211.13 ? 229  GLY E C   1 
ATOM   13285 O  O   . GLY E  1 229 ? -8.251  -74.331 -28.661  1.00 210.56 ? 229  GLY E O   1 
ATOM   13286 N  N   . ASP E  1 230 ? -9.647  -75.103 -30.253  1.00 214.85 ? 230  ASP E N   1 
ATOM   13287 C  CA  . ASP E  1 230 ? -9.465  -76.515 -29.928  1.00 226.09 ? 230  ASP E CA  1 
ATOM   13288 C  C   . ASP E  1 230 ? -8.274  -77.089 -30.690  1.00 234.19 ? 230  ASP E C   1 
ATOM   13289 O  O   . ASP E  1 230 ? -8.137  -76.873 -31.897  1.00 244.49 ? 230  ASP E O   1 
ATOM   13290 C  CB  . ASP E  1 230 ? -10.728 -77.309 -30.263  1.00 238.55 ? 230  ASP E CB  1 
ATOM   13291 C  CG  . ASP E  1 230 ? -10.689 -78.720 -29.719  1.00 242.22 ? 230  ASP E CG  1 
ATOM   13292 O  OD1 . ASP E  1 230 ? -9.863  -78.995 -28.824  1.00 237.30 ? 230  ASP E OD1 1 
ATOM   13293 O  OD2 . ASP E  1 230 ? -11.477 -79.559 -30.203  1.00 248.03 ? 230  ASP E OD2 1 
ATOM   13294 N  N   . PHE E  1 231 ? -7.423  -77.830 -29.989  1.00 227.01 ? 231  PHE E N   1 
ATOM   13295 C  CA  . PHE E  1 231 ? -6.202  -78.321 -30.614  1.00 217.60 ? 231  PHE E CA  1 
ATOM   13296 C  C   . PHE E  1 231 ? -5.933  -79.784 -30.304  1.00 215.40 ? 231  PHE E C   1 
ATOM   13297 O  O   . PHE E  1 231 ? -5.395  -80.518 -31.133  1.00 212.11 ? 231  PHE E O   1 
ATOM   13298 C  CB  . PHE E  1 231 ? -5.012  -77.479 -30.171  1.00 211.91 ? 231  PHE E CB  1 
ATOM   13299 C  CG  . PHE E  1 231 ? -5.020  -76.090 -30.727  1.00 207.66 ? 231  PHE E CG  1 
ATOM   13300 C  CD1 . PHE E  1 231 ? -4.597  -75.855 -32.022  1.00 203.34 ? 231  PHE E CD1 1 
ATOM   13301 C  CD2 . PHE E  1 231 ? -5.466  -75.020 -29.968  1.00 207.65 ? 231  PHE E CD2 1 
ATOM   13302 C  CE1 . PHE E  1 231 ? -4.602  -74.582 -32.548  1.00 201.21 ? 231  PHE E CE1 1 
ATOM   13303 C  CE2 . PHE E  1 231 ? -5.477  -73.735 -30.494  1.00 205.90 ? 231  PHE E CE2 1 
ATOM   13304 C  CZ  . PHE E  1 231 ? -5.043  -73.519 -31.784  1.00 203.91 ? 231  PHE E CZ  1 
ATOM   13305 N  N   . ASN E  1 232 ? -6.299  -80.214 -29.104  1.00 216.71 ? 232  ASN E N   1 
ATOM   13306 C  CA  . ASN E  1 232 ? -6.135  -81.604 -28.723  1.00 216.82 ? 232  ASN E CA  1 
ATOM   13307 C  C   . ASN E  1 232 ? -7.319  -82.473 -29.135  1.00 216.87 ? 232  ASN E C   1 
ATOM   13308 O  O   . ASN E  1 232 ? -7.408  -83.627 -28.703  1.00 217.99 ? 232  ASN E O   1 
ATOM   13309 C  CB  . ASN E  1 232 ? -5.908  -81.694 -27.218  1.00 210.32 ? 232  ASN E CB  1 
ATOM   13310 C  CG  . ASN E  1 232 ? -6.960  -80.954 -26.421  1.00 213.60 ? 232  ASN E CG  1 
ATOM   13311 O  OD1 . ASN E  1 232 ? -7.683  -80.109 -26.944  1.00 216.22 ? 232  ASN E OD1 1 
ATOM   13312 N  ND2 . ASN E  1 232 ? -7.051  -81.276 -25.139  1.00 214.66 ? 232  ASN E ND2 1 
ATOM   13313 N  N   . GLY E  1 233 ? -8.214  -81.954 -29.974  1.00 221.64 ? 233  GLY E N   1 
ATOM   13314 C  CA  . GLY E  1 233 ? -9.297  -82.741 -30.531  1.00 225.60 ? 233  GLY E CA  1 
ATOM   13315 C  C   . GLY E  1 233 ? -10.239 -83.328 -29.500  1.00 238.53 ? 233  GLY E C   1 
ATOM   13316 O  O   . GLY E  1 233 ? -10.543 -84.525 -29.545  1.00 243.27 ? 233  GLY E O   1 
ATOM   13317 N  N   . ASP E  1 234 ? -10.708 -82.503 -28.564  1.00 241.68 ? 234  ASP E N   1 
ATOM   13318 C  CA  . ASP E  1 234 ? -11.640 -82.961 -27.538  1.00 243.96 ? 234  ASP E CA  1 
ATOM   13319 C  C   . ASP E  1 234 ? -12.933 -82.162 -27.484  1.00 240.93 ? 234  ASP E C   1 
ATOM   13320 O  O   . ASP E  1 234 ? -13.996 -82.740 -27.236  1.00 241.19 ? 234  ASP E O   1 
ATOM   13321 C  CB  . ASP E  1 234 ? -10.966 -82.944 -26.151  1.00 242.87 ? 234  ASP E CB  1 
ATOM   13322 C  CG  . ASP E  1 234 ? -10.811 -81.542 -25.581  1.00 247.04 ? 234  ASP E CG  1 
ATOM   13323 O  OD1 . ASP E  1 234 ? -10.603 -80.593 -26.364  1.00 252.15 ? 234  ASP E OD1 1 
ATOM   13324 O  OD2 . ASP E  1 234 ? -10.912 -81.388 -24.345  1.00 245.16 ? 234  ASP E OD2 1 
ATOM   13325 N  N   . GLY E  1 235 ? -12.882 -80.852 -27.709  1.00 242.28 ? 235  GLY E N   1 
ATOM   13326 C  CA  . GLY E  1 235 ? -14.088 -80.046 -27.729  1.00 245.77 ? 235  GLY E CA  1 
ATOM   13327 C  C   . GLY E  1 235 ? -14.025 -78.873 -26.775  1.00 239.90 ? 235  GLY E C   1 
ATOM   13328 O  O   . GLY E  1 235 ? -14.869 -77.973 -26.826  1.00 241.82 ? 235  GLY E O   1 
ATOM   13329 N  N   . ILE E  1 236 ? -13.034 -78.879 -25.889  1.00 242.42 ? 236  ILE E N   1 
ATOM   13330 C  CA  . ILE E  1 236 ? -12.839 -77.801 -24.929  1.00 240.29 ? 236  ILE E CA  1 
ATOM   13331 C  C   . ILE E  1 236 ? -11.834 -76.819 -25.515  1.00 237.57 ? 236  ILE E C   1 
ATOM   13332 O  O   . ILE E  1 236 ? -10.716 -77.205 -25.874  1.00 232.08 ? 236  ILE E O   1 
ATOM   13333 C  CB  . ILE E  1 236 ? -12.363 -78.337 -23.572  1.00 235.84 ? 236  ILE E CB  1 
ATOM   13334 C  CG1 . ILE E  1 236 ? -13.356 -79.365 -23.027  1.00 239.20 ? 236  ILE E CG1 1 
ATOM   13335 C  CG2 . ILE E  1 236 ? -12.173 -77.193 -22.582  1.00 233.56 ? 236  ILE E CG2 1 
ATOM   13336 C  CD1 . ILE E  1 236 ? -14.751 -78.817 -22.825  1.00 241.80 ? 236  ILE E CD1 1 
ATOM   13337 N  N   . ASP E  1 237 ? -12.237 -75.554 -25.624  1.00 242.24 ? 237  ASP E N   1 
ATOM   13338 C  CA  . ASP E  1 237 ? -11.344 -74.523 -26.133  1.00 234.21 ? 237  ASP E CA  1 
ATOM   13339 C  C   . ASP E  1 237 ? -10.094 -74.432 -25.270  1.00 225.13 ? 237  ASP E C   1 
ATOM   13340 O  O   . ASP E  1 237 ? -10.177 -74.301 -24.046  1.00 227.19 ? 237  ASP E O   1 
ATOM   13341 C  CB  . ASP E  1 237 ? -12.062 -73.174 -26.170  1.00 235.13 ? 237  ASP E CB  1 
ATOM   13342 C  CG  . ASP E  1 237 ? -12.905 -72.997 -27.417  1.00 240.22 ? 237  ASP E CG  1 
ATOM   13343 O  OD1 . ASP E  1 237 ? -13.147 -74.002 -28.119  1.00 250.89 ? 237  ASP E OD1 1 
ATOM   13344 O  OD2 . ASP E  1 237 ? -13.332 -71.855 -27.690  1.00 235.53 ? 237  ASP E OD2 1 
ATOM   13345 N  N   . ASP E  1 238 ? -8.935  -74.512 -25.914  1.00 212.33 ? 238  ASP E N   1 
ATOM   13346 C  CA  . ASP E  1 238 ? -7.652  -74.483 -25.231  1.00 212.28 ? 238  ASP E CA  1 
ATOM   13347 C  C   . ASP E  1 238 ? -7.012  -73.100 -25.329  1.00 221.66 ? 238  ASP E C   1 
ATOM   13348 O  O   . ASP E  1 238 ? -7.385  -72.274 -26.166  1.00 224.93 ? 238  ASP E O   1 
ATOM   13349 C  CB  . ASP E  1 238 ? -6.729  -75.561 -25.802  1.00 214.07 ? 238  ASP E CB  1 
ATOM   13350 C  CG  . ASP E  1 238 ? -7.326  -76.953 -25.674  1.00 222.86 ? 238  ASP E CG  1 
ATOM   13351 O  OD1 . ASP E  1 238 ? -7.827  -77.272 -24.574  1.00 222.80 ? 238  ASP E OD1 1 
ATOM   13352 O  OD2 . ASP E  1 238 ? -7.304  -77.725 -26.657  1.00 227.02 ? 238  ASP E OD2 1 
ATOM   13353 N  N   . PHE E  1 239 ? -6.031  -72.860 -24.456  1.00 224.13 ? 239  PHE E N   1 
ATOM   13354 C  CA  . PHE E  1 239 ? -5.453  -71.534 -24.245  1.00 215.22 ? 239  PHE E CA  1 
ATOM   13355 C  C   . PHE E  1 239 ? -4.117  -71.389 -24.975  1.00 196.72 ? 239  PHE E C   1 
ATOM   13356 O  O   . PHE E  1 239 ? -3.168  -72.134 -24.703  1.00 171.86 ? 239  PHE E O   1 
ATOM   13357 C  CB  . PHE E  1 239 ? -5.279  -71.261 -22.749  1.00 211.65 ? 239  PHE E CB  1 
ATOM   13358 C  CG  . PHE E  1 239 ? -6.541  -71.452 -21.940  1.00 215.71 ? 239  PHE E CG  1 
ATOM   13359 C  CD1 . PHE E  1 239 ? -7.780  -71.078 -22.446  1.00 214.38 ? 239  PHE E CD1 1 
ATOM   13360 C  CD2 . PHE E  1 239 ? -6.486  -72.011 -20.673  1.00 222.00 ? 239  PHE E CD2 1 
ATOM   13361 C  CE1 . PHE E  1 239 ? -8.935  -71.259 -21.700  1.00 214.60 ? 239  PHE E CE1 1 
ATOM   13362 C  CE2 . PHE E  1 239 ? -7.635  -72.192 -19.925  1.00 230.37 ? 239  PHE E CE2 1 
ATOM   13363 C  CZ  . PHE E  1 239 ? -8.860  -71.818 -20.440  1.00 223.38 ? 239  PHE E CZ  1 
ATOM   13364 N  N   . VAL E  1 240 ? -4.054  -70.428 -25.900  1.00 193.25 ? 240  VAL E N   1 
ATOM   13365 C  CA  . VAL E  1 240 ? -2.839  -70.075 -26.630  1.00 175.93 ? 240  VAL E CA  1 
ATOM   13366 C  C   . VAL E  1 240 ? -2.375  -68.696 -26.179  1.00 174.43 ? 240  VAL E C   1 
ATOM   13367 O  O   . VAL E  1 240 ? -3.180  -67.761 -26.089  1.00 184.29 ? 240  VAL E O   1 
ATOM   13368 C  CB  . VAL E  1 240 ? -3.080  -70.093 -28.151  1.00 176.77 ? 240  VAL E CB  1 
ATOM   13369 C  CG1 . VAL E  1 240 ? -1.783  -69.835 -28.895  1.00 176.69 ? 240  VAL E CG1 1 
ATOM   13370 C  CG2 . VAL E  1 240 ? -3.706  -71.413 -28.575  1.00 186.50 ? 240  VAL E CG2 1 
ATOM   13371 N  N   . SER E  1 241 ? -1.072  -68.557 -25.929  1.00 175.52 ? 241  SER E N   1 
ATOM   13372 C  CA  . SER E  1 241 ? -0.538  -67.295 -25.432  1.00 171.22 ? 241  SER E CA  1 
ATOM   13373 C  C   . SER E  1 241 ? 0.892   -67.080 -25.906  1.00 178.25 ? 241  SER E C   1 
ATOM   13374 O  O   . SER E  1 241 ? 1.708   -68.008 -25.900  1.00 200.85 ? 241  SER E O   1 
ATOM   13375 C  CB  . SER E  1 241 ? -0.577  -67.233 -23.902  1.00 163.85 ? 241  SER E CB  1 
ATOM   13376 O  OG  . SER E  1 241 ? -0.178  -65.954 -23.442  1.00 161.63 ? 241  SER E OG  1 
ATOM   13377 N  N   . GLY E  1 242 ? 1.185   -65.841 -26.300  1.00 159.20 ? 242  GLY E N   1 
ATOM   13378 C  CA  . GLY E  1 242 ? 2.538   -65.476 -26.681  1.00 162.46 ? 242  GLY E CA  1 
ATOM   13379 C  C   . GLY E  1 242 ? 3.413   -65.204 -25.465  1.00 152.02 ? 242  GLY E C   1 
ATOM   13380 O  O   . GLY E  1 242 ? 2.980   -64.621 -24.469  1.00 149.85 ? 242  GLY E O   1 
ATOM   13381 N  N   . VAL E  1 243 ? 4.657   -65.665 -25.552  1.00 161.10 ? 243  VAL E N   1 
ATOM   13382 C  CA  . VAL E  1 243 ? 5.668   -65.457 -24.517  1.00 160.87 ? 243  VAL E CA  1 
ATOM   13383 C  C   . VAL E  1 243 ? 6.866   -64.788 -25.182  1.00 161.20 ? 243  VAL E C   1 
ATOM   13384 O  O   . VAL E  1 243 ? 7.883   -65.453 -25.432  1.00 154.24 ? 243  VAL E O   1 
ATOM   13385 C  CB  . VAL E  1 243 ? 6.055   -66.781 -23.844  1.00 165.97 ? 243  VAL E CB  1 
ATOM   13386 C  CG1 . VAL E  1 243 ? 6.705   -66.521 -22.496  1.00 182.53 ? 243  VAL E CG1 1 
ATOM   13387 C  CG2 . VAL E  1 243 ? 4.832   -67.667 -23.693  1.00 154.74 ? 243  VAL E CG2 1 
ATOM   13388 N  N   . PRO E  1 244 ? 6.785   -63.486 -25.488  1.00 160.40 ? 244  PRO E N   1 
ATOM   13389 C  CA  . PRO E  1 244 ? 7.727   -62.886 -26.452  1.00 159.02 ? 244  PRO E CA  1 
ATOM   13390 C  C   . PRO E  1 244 ? 9.161   -62.775 -25.962  1.00 162.36 ? 244  PRO E C   1 
ATOM   13391 O  O   . PRO E  1 244 ? 10.064  -62.646 -26.796  1.00 172.67 ? 244  PRO E O   1 
ATOM   13392 C  CB  . PRO E  1 244 ? 7.125   -61.498 -26.714  1.00 154.61 ? 244  PRO E CB  1 
ATOM   13393 C  CG  . PRO E  1 244 ? 6.336   -61.197 -25.498  1.00 154.52 ? 244  PRO E CG  1 
ATOM   13394 C  CD  . PRO E  1 244 ? 5.786   -62.514 -25.018  1.00 157.51 ? 244  PRO E CD  1 
ATOM   13395 N  N   . ARG E  1 245 ? 9.413   -62.785 -24.658  1.00 166.66 ? 245  ARG E N   1 
ATOM   13396 C  CA  . ARG E  1 245 ? 10.779  -62.667 -24.171  1.00 175.09 ? 245  ARG E CA  1 
ATOM   13397 C  C   . ARG E  1 245 ? 11.392  -64.001 -23.772  1.00 187.51 ? 245  ARG E C   1 
ATOM   13398 O  O   . ARG E  1 245 ? 12.555  -64.033 -23.356  1.00 199.87 ? 245  ARG E O   1 
ATOM   13399 C  CB  . ARG E  1 245 ? 10.842  -61.685 -22.999  1.00 176.97 ? 245  ARG E CB  1 
ATOM   13400 C  CG  . ARG E  1 245 ? 10.721  -60.234 -23.431  1.00 178.99 ? 245  ARG E CG  1 
ATOM   13401 C  CD  . ARG E  1 245 ? 11.084  -59.293 -22.302  1.00 179.82 ? 245  ARG E CD  1 
ATOM   13402 N  NE  . ARG E  1 245 ? 12.474  -59.452 -21.884  1.00 185.19 ? 245  ARG E NE  1 
ATOM   13403 C  CZ  . ARG E  1 245 ? 13.496  -58.783 -22.407  1.00 202.25 ? 245  ARG E CZ  1 
ATOM   13404 N  NH1 . ARG E  1 245 ? 13.291  -57.895 -23.368  1.00 200.21 ? 245  ARG E NH1 1 
ATOM   13405 N  NH2 . ARG E  1 245 ? 14.726  -58.992 -21.958  1.00 227.29 ? 245  ARG E NH2 1 
ATOM   13406 N  N   . ALA E  1 246 ? 10.649  -65.099 -23.891  1.00 180.01 ? 246  ALA E N   1 
ATOM   13407 C  CA  . ALA E  1 246 ? 11.197  -66.408 -23.578  1.00 176.67 ? 246  ALA E CA  1 
ATOM   13408 C  C   . ALA E  1 246 ? 12.321  -66.769 -24.551  1.00 179.46 ? 246  ALA E C   1 
ATOM   13409 O  O   . ALA E  1 246 ? 12.500  -66.156 -25.606  1.00 174.83 ? 246  ALA E O   1 
ATOM   13410 C  CB  . ALA E  1 246 ? 10.099  -67.470 -23.622  1.00 175.48 ? 246  ALA E CB  1 
ATOM   13411 N  N   . ALA E  1 247 ? 13.079  -67.799 -24.175  1.00 195.56 ? 247  ALA E N   1 
ATOM   13412 C  CA  . ALA E  1 247 ? 14.192  -68.299 -24.983  1.00 196.79 ? 247  ALA E CA  1 
ATOM   13413 C  C   . ALA E  1 247 ? 15.180  -67.188 -25.321  1.00 187.94 ? 247  ALA E C   1 
ATOM   13414 O  O   . ALA E  1 247 ? 15.652  -67.077 -26.454  1.00 174.04 ? 247  ALA E O   1 
ATOM   13415 C  CB  . ALA E  1 247 ? 13.687  -68.976 -26.259  1.00 184.74 ? 247  ALA E CB  1 
ATOM   13416 N  N   . ARG E  1 248 ? 15.497  -66.359 -24.324  1.00 197.79 ? 248  ARG E N   1 
ATOM   13417 C  CA  . ARG E  1 248 ? 16.475  -65.281 -24.476  1.00 199.43 ? 248  ARG E CA  1 
ATOM   13418 C  C   . ARG E  1 248 ? 16.069  -64.329 -25.601  1.00 205.10 ? 248  ARG E C   1 
ATOM   13419 O  O   . ARG E  1 248 ? 16.821  -64.092 -26.549  1.00 215.05 ? 248  ARG E O   1 
ATOM   13420 C  CB  . ARG E  1 248 ? 17.883  -65.847 -24.707  1.00 204.10 ? 248  ARG E CB  1 
ATOM   13421 C  CG  . ARG E  1 248 ? 18.637  -66.226 -23.435  1.00 203.55 ? 248  ARG E CG  1 
ATOM   13422 C  CD  . ARG E  1 248 ? 17.989  -67.380 -22.677  1.00 208.33 ? 248  ARG E CD  1 
ATOM   13423 N  NE  . ARG E  1 248 ? 18.538  -68.673 -23.076  1.00 212.74 ? 248  ARG E NE  1 
ATOM   13424 C  CZ  . ARG E  1 248 ? 19.678  -69.172 -22.610  1.00 224.63 ? 248  ARG E CZ  1 
ATOM   13425 N  NH1 . ARG E  1 248 ? 20.395  -68.487 -21.729  1.00 239.39 ? 248  ARG E NH1 1 
ATOM   13426 N  NH2 . ARG E  1 248 ? 20.107  -70.353 -23.027  1.00 223.13 ? 248  ARG E NH2 1 
ATOM   13427 N  N   . THR E  1 249 ? 14.854  -63.789 -25.491  1.00 182.48 ? 249  THR E N   1 
ATOM   13428 C  CA  . THR E  1 249 ? 14.244  -62.862 -26.444  1.00 178.64 ? 249  THR E CA  1 
ATOM   13429 C  C   . THR E  1 249 ? 13.991  -63.483 -27.811  1.00 168.52 ? 249  THR E C   1 
ATOM   13430 O  O   . THR E  1 249 ? 13.650  -62.761 -28.756  1.00 169.81 ? 249  THR E O   1 
ATOM   13431 C  CB  . THR E  1 249 ? 15.076  -61.588 -26.628  1.00 181.33 ? 249  THR E CB  1 
ATOM   13432 O  OG1 . THR E  1 249 ? 16.289  -61.902 -27.323  1.00 180.02 ? 249  THR E OG1 1 
ATOM   13433 C  CG2 . THR E  1 249 ? 15.412  -60.977 -25.275  1.00 184.86 ? 249  THR E CG2 1 
ATOM   13434 N  N   . LEU E  1 250 ? 14.106  -64.804 -27.943  1.00 160.54 ? 250  LEU E N   1 
ATOM   13435 C  CA  . LEU E  1 250 ? 13.693  -65.448 -29.183  1.00 159.34 ? 250  LEU E CA  1 
ATOM   13436 C  C   . LEU E  1 250 ? 12.184  -65.412 -29.343  1.00 156.64 ? 250  LEU E C   1 
ATOM   13437 O  O   . LEU E  1 250 ? 11.677  -65.390 -30.468  1.00 157.59 ? 250  LEU E O   1 
ATOM   13438 C  CB  . LEU E  1 250 ? 14.180  -66.894 -29.212  1.00 161.65 ? 250  LEU E CB  1 
ATOM   13439 C  CG  . LEU E  1 250 ? 14.765  -67.442 -30.511  1.00 189.28 ? 250  LEU E CG  1 
ATOM   13440 C  CD1 . LEU E  1 250 ? 15.693  -66.434 -31.169  1.00 200.52 ? 250  LEU E CD1 1 
ATOM   13441 C  CD2 . LEU E  1 250 ? 15.491  -68.748 -30.237  1.00 204.77 ? 250  LEU E CD2 1 
ATOM   13442 N  N   . GLY E  1 251 ? 11.460  -65.406 -28.233  1.00 147.79 ? 251  GLY E N   1 
ATOM   13443 C  CA  . GLY E  1 251 ? 10.017  -65.413 -28.255  1.00 147.56 ? 251  GLY E CA  1 
ATOM   13444 C  C   . GLY E  1 251 ? 9.477   -66.816 -28.409  1.00 147.10 ? 251  GLY E C   1 
ATOM   13445 O  O   . GLY E  1 251 ? 9.986   -67.601 -29.214  1.00 146.70 ? 251  GLY E O   1 
ATOM   13446 N  N   . MET E  1 252 ? 8.425   -67.133 -27.662  1.00 157.05 ? 252  MET E N   1 
ATOM   13447 C  CA  . MET E  1 252 ? 7.794   -68.437 -27.733  1.00 157.78 ? 252  MET E CA  1 
ATOM   13448 C  C   . MET E  1 252 ? 6.289   -68.258 -27.640  1.00 153.78 ? 252  MET E C   1 
ATOM   13449 O  O   . MET E  1 252 ? 5.784   -67.180 -27.319  1.00 152.06 ? 252  MET E O   1 
ATOM   13450 C  CB  . MET E  1 252 ? 8.282   -69.379 -26.625  1.00 152.21 ? 252  MET E CB  1 
ATOM   13451 C  CG  . MET E  1 252 ? 9.733   -69.788 -26.731  1.00 161.06 ? 252  MET E CG  1 
ATOM   13452 S  SD  . MET E  1 252 ? 10.152  -71.006 -25.476  1.00 164.92 ? 252  MET E SD  1 
ATOM   13453 C  CE  . MET E  1 252 ? 9.272   -72.432 -26.107  1.00 165.16 ? 252  MET E CE  1 
ATOM   13454 N  N   . VAL E  1 253 ? 5.572   -69.338 -27.930  1.00 155.40 ? 253  VAL E N   1 
ATOM   13455 C  CA  . VAL E  1 253 ? 4.127   -69.396 -27.762  1.00 153.58 ? 253  VAL E CA  1 
ATOM   13456 C  C   . VAL E  1 253 ? 3.800   -70.686 -27.024  1.00 176.17 ? 253  VAL E C   1 
ATOM   13457 O  O   . VAL E  1 253 ? 4.135   -71.778 -27.498  1.00 186.81 ? 253  VAL E O   1 
ATOM   13458 C  CB  . VAL E  1 253 ? 3.392   -69.325 -29.110  1.00 150.48 ? 253  VAL E CB  1 
ATOM   13459 C  CG1 . VAL E  1 253 ? 1.944   -69.755 -28.958  1.00 156.41 ? 253  VAL E CG1 1 
ATOM   13460 C  CG2 . VAL E  1 253 ? 3.470   -67.916 -29.670  1.00 148.67 ? 253  VAL E CG2 1 
ATOM   13461 N  N   . TYR E  1 254 ? 3.161   -70.562 -25.862  1.00 180.38 ? 254  TYR E N   1 
ATOM   13462 C  CA  . TYR E  1 254 ? 2.772   -71.710 -25.058  1.00 171.13 ? 254  TYR E CA  1 
ATOM   13463 C  C   . TYR E  1 254 ? 1.314   -72.051 -25.319  1.00 168.41 ? 254  TYR E C   1 
ATOM   13464 O  O   . TYR E  1 254 ? 0.459   -71.164 -25.381  1.00 162.87 ? 254  TYR E O   1 
ATOM   13465 C  CB  . TYR E  1 254 ? 2.969   -71.431 -23.567  1.00 158.99 ? 254  TYR E CB  1 
ATOM   13466 C  CG  . TYR E  1 254 ? 4.402   -71.194 -23.137  1.00 166.88 ? 254  TYR E CG  1 
ATOM   13467 C  CD1 . TYR E  1 254 ? 5.473   -71.582 -23.937  1.00 177.62 ? 254  TYR E CD1 1 
ATOM   13468 C  CD2 . TYR E  1 254 ? 4.682   -70.559 -21.932  1.00 167.63 ? 254  TYR E CD2 1 
ATOM   13469 C  CE1 . TYR E  1 254 ? 6.785   -71.354 -23.539  1.00 183.82 ? 254  TYR E CE1 1 
ATOM   13470 C  CE2 . TYR E  1 254 ? 5.985   -70.322 -21.530  1.00 172.78 ? 254  TYR E CE2 1 
ATOM   13471 C  CZ  . TYR E  1 254 ? 7.032   -70.722 -22.334  1.00 181.05 ? 254  TYR E CZ  1 
ATOM   13472 O  OH  . TYR E  1 254 ? 8.327   -70.484 -21.924  1.00 173.32 ? 254  TYR E OH  1 
ATOM   13473 N  N   . ILE E  1 255 ? 1.030   -73.343 -25.433  1.00 178.15 ? 255  ILE E N   1 
ATOM   13474 C  CA  . ILE E  1 255 ? -0.334  -73.838 -25.541  1.00 181.94 ? 255  ILE E CA  1 
ATOM   13475 C  C   . ILE E  1 255 ? -0.628  -74.680 -24.313  1.00 175.94 ? 255  ILE E C   1 
ATOM   13476 O  O   . ILE E  1 255 ? 0.114   -75.619 -24.004  1.00 177.68 ? 255  ILE E O   1 
ATOM   13477 C  CB  . ILE E  1 255 ? -0.552  -74.647 -26.830  1.00 193.86 ? 255  ILE E CB  1 
ATOM   13478 C  CG1 . ILE E  1 255 ? -0.411  -73.745 -28.058  1.00 191.42 ? 255  ILE E CG1 1 
ATOM   13479 C  CG2 . ILE E  1 255 ? -1.921  -75.305 -26.812  1.00 193.49 ? 255  ILE E CG2 1 
ATOM   13480 C  CD1 . ILE E  1 255 ? -0.886  -74.392 -29.340  1.00 192.13 ? 255  ILE E CD1 1 
ATOM   13481 N  N   . TYR E  1 256 ? -1.701  -74.333 -23.611  1.00 175.53 ? 256  TYR E N   1 
ATOM   13482 C  CA  . TYR E  1 256 ? -2.138  -75.056 -22.429  1.00 197.22 ? 256  TYR E CA  1 
ATOM   13483 C  C   . TYR E  1 256 ? -3.521  -75.656 -22.651  1.00 204.77 ? 256  TYR E C   1 
ATOM   13484 O  O   . TYR E  1 256 ? -4.364  -75.080 -23.343  1.00 209.77 ? 256  TYR E O   1 
ATOM   13485 C  CB  . TYR E  1 256 ? -2.156  -74.147 -21.199  1.00 198.50 ? 256  TYR E CB  1 
ATOM   13486 C  CG  . TYR E  1 256 ? -0.790  -73.657 -20.770  1.00 186.68 ? 256  TYR E CG  1 
ATOM   13487 C  CD1 . TYR E  1 256 ? -0.021  -74.392 -19.875  1.00 185.48 ? 256  TYR E CD1 1 
ATOM   13488 C  CD2 . TYR E  1 256 ? -0.274  -72.457 -21.247  1.00 170.37 ? 256  TYR E CD2 1 
ATOM   13489 C  CE1 . TYR E  1 256 ? 1.223   -73.952 -19.470  1.00 182.90 ? 256  TYR E CE1 1 
ATOM   13490 C  CE2 . TYR E  1 256 ? 0.969   -72.008 -20.844  1.00 171.15 ? 256  TYR E CE2 1 
ATOM   13491 C  CZ  . TYR E  1 256 ? 1.714   -72.761 -19.957  1.00 180.18 ? 256  TYR E CZ  1 
ATOM   13492 O  OH  . TYR E  1 256 ? 2.953   -72.324 -19.552  1.00 178.18 ? 256  TYR E OH  1 
ATOM   13493 N  N   . ASP E  1 257 ? -3.745  -76.824 -22.051  1.00 203.69 ? 257  ASP E N   1 
ATOM   13494 C  CA  . ASP E  1 257 ? -5.061  -77.448 -22.088  1.00 206.90 ? 257  ASP E CA  1 
ATOM   13495 C  C   . ASP E  1 257 ? -6.080  -76.607 -21.326  1.00 205.40 ? 257  ASP E C   1 
ATOM   13496 O  O   . ASP E  1 257 ? -5.801  -76.093 -20.239  1.00 206.85 ? 257  ASP E O   1 
ATOM   13497 C  CB  . ASP E  1 257 ? -4.993  -78.857 -21.502  1.00 220.04 ? 257  ASP E CB  1 
ATOM   13498 C  CG  . ASP E  1 257 ? -6.321  -79.580 -21.572  1.00 233.87 ? 257  ASP E CG  1 
ATOM   13499 O  OD1 . ASP E  1 257 ? -7.069  -79.358 -22.548  1.00 230.25 ? 257  ASP E OD1 1 
ATOM   13500 O  OD2 . ASP E  1 257 ? -6.616  -80.366 -20.649  1.00 246.37 ? 257  ASP E OD2 1 
ATOM   13501 N  N   . GLY E  1 258 ? -7.272  -76.474 -21.906  1.00 206.43 ? 258  GLY E N   1 
ATOM   13502 C  CA  . GLY E  1 258 ? -8.316  -75.646 -21.333  1.00 212.65 ? 258  GLY E CA  1 
ATOM   13503 C  C   . GLY E  1 258 ? -9.154  -76.331 -20.274  1.00 212.48 ? 258  GLY E C   1 
ATOM   13504 O  O   . GLY E  1 258 ? -10.267 -75.888 -19.969  1.00 216.51 ? 258  GLY E O   1 
ATOM   13505 N  N   . LYS E  1 259 ? -8.638  -77.413 -19.709  1.00 202.38 ? 259  LYS E N   1 
ATOM   13506 C  CA  . LYS E  1 259 ? -9.341  -78.149 -18.669  1.00 208.18 ? 259  LYS E CA  1 
ATOM   13507 C  C   . LYS E  1 259 ? -8.566  -78.243 -17.365  1.00 210.75 ? 259  LYS E C   1 
ATOM   13508 O  O   . LYS E  1 259 ? -9.158  -78.079 -16.295  1.00 218.93 ? 259  LYS E O   1 
ATOM   13509 C  CB  . LYS E  1 259 ? -9.678  -79.561 -19.166  1.00 210.97 ? 259  LYS E CB  1 
ATOM   13510 C  CG  . LYS E  1 259 ? -10.631 -80.329 -18.267  1.00 220.60 ? 259  LYS E CG  1 
ATOM   13511 C  CD  . LYS E  1 259 ? -10.812 -81.755 -18.758  1.00 233.75 ? 259  LYS E CD  1 
ATOM   13512 C  CE  . LYS E  1 259 ? -9.539  -82.566 -18.570  1.00 237.08 ? 259  LYS E CE  1 
ATOM   13513 N  NZ  . LYS E  1 259 ? -9.707  -83.991 -18.970  1.00 242.75 ? 259  LYS E NZ  1 
ATOM   13514 N  N   . ASN E  1 260 ? -7.253  -78.496 -17.414  1.00 211.47 ? 260  ASN E N   1 
ATOM   13515 C  CA  . ASN E  1 260 ? -6.467  -78.638 -16.194  1.00 216.36 ? 260  ASN E CA  1 
ATOM   13516 C  C   . ASN E  1 260 ? -5.157  -77.861 -16.228  1.00 211.56 ? 260  ASN E C   1 
ATOM   13517 O  O   . ASN E  1 260 ? -4.295  -78.091 -15.370  1.00 219.09 ? 260  ASN E O   1 
ATOM   13518 C  CB  . ASN E  1 260 ? -6.174  -80.115 -15.889  1.00 225.60 ? 260  ASN E CB  1 
ATOM   13519 C  CG  . ASN E  1 260 ? -5.503  -80.846 -17.044  1.00 228.36 ? 260  ASN E CG  1 
ATOM   13520 O  OD1 . ASN E  1 260 ? -4.849  -80.239 -17.892  1.00 203.04 ? 260  ASN E OD1 1 
ATOM   13521 N  ND2 . ASN E  1 260 ? -5.663  -82.166 -17.074  1.00 292.56 ? 260  ASN E ND2 1 
ATOM   13522 N  N   . MET E  1 261 ? -4.973  -76.968 -17.199  1.00 205.91 ? 261  MET E N   1 
ATOM   13523 C  CA  . MET E  1 261 ? -3.800  -76.100 -17.273  1.00 199.08 ? 261  MET E CA  1 
ATOM   13524 C  C   . MET E  1 261 ? -2.514  -76.931 -17.360  1.00 201.75 ? 261  MET E C   1 
ATOM   13525 O  O   . MET E  1 261 ? -1.699  -76.987 -16.435  1.00 206.07 ? 261  MET E O   1 
ATOM   13526 C  CB  . MET E  1 261 ? -3.768  -75.140 -16.076  1.00 199.54 ? 261  MET E CB  1 
ATOM   13527 C  CG  . MET E  1 261 ? -2.940  -73.902 -16.318  1.00 193.37 ? 261  MET E CG  1 
ATOM   13528 S  SD  . MET E  1 261 ? -3.542  -73.007 -17.759  1.00 184.42 ? 261  MET E SD  1 
ATOM   13529 C  CE  . MET E  1 261 ? -4.784  -71.947 -17.037  1.00 189.49 ? 261  MET E CE  1 
ATOM   13530 N  N   . SER E  1 262 ? -2.358  -77.583 -18.512  1.00 191.27 ? 262  SER E N   1 
ATOM   13531 C  CA  . SER E  1 262 ? -1.167  -78.358 -18.827  1.00 185.12 ? 262  SER E CA  1 
ATOM   13532 C  C   . SER E  1 262 ? -0.662  -77.964 -20.209  1.00 178.90 ? 262  SER E C   1 
ATOM   13533 O  O   . SER E  1 262 ? -1.452  -77.739 -21.126  1.00 181.93 ? 262  SER E O   1 
ATOM   13534 C  CB  . SER E  1 262 ? -1.460  -79.862 -18.780  1.00 196.78 ? 262  SER E CB  1 
ATOM   13535 O  OG  . SER E  1 262 ? -0.299  -80.622 -19.058  1.00 204.68 ? 262  SER E OG  1 
ATOM   13536 N  N   . SER E  1 263 ? 0.661   -77.942 -20.369  1.00 183.98 ? 263  SER E N   1 
ATOM   13537 C  CA  . SER E  1 263 ? 1.257   -77.516 -21.631  1.00 185.20 ? 263  SER E CA  1 
ATOM   13538 C  C   . SER E  1 263 ? 1.027   -78.559 -22.719  1.00 198.31 ? 263  SER E C   1 
ATOM   13539 O  O   . SER E  1 263 ? 1.257   -79.755 -22.511  1.00 217.78 ? 263  SER E O   1 
ATOM   13540 C  CB  . SER E  1 263 ? 2.753   -77.264 -21.454  1.00 170.21 ? 263  SER E CB  1 
ATOM   13541 O  OG  . SER E  1 263 ? 3.320   -76.706 -22.629  1.00 165.31 ? 263  SER E OG  1 
ATOM   13542 N  N   . LEU E  1 264 ? 0.565   -78.105 -23.884  1.00 191.13 ? 264  LEU E N   1 
ATOM   13543 C  CA  . LEU E  1 264 ? 0.262   -78.991 -25.002  1.00 186.43 ? 264  LEU E CA  1 
ATOM   13544 C  C   . LEU E  1 264 ? 1.289   -78.878 -26.120  1.00 176.66 ? 264  LEU E C   1 
ATOM   13545 O  O   . LEU E  1 264 ? 1.881   -79.883 -26.523  1.00 176.01 ? 264  LEU E O   1 
ATOM   13546 C  CB  . LEU E  1 264 ? -1.141  -78.701 -25.550  1.00 197.29 ? 264  LEU E CB  1 
ATOM   13547 C  CG  . LEU E  1 264 ? -2.343  -79.017 -24.660  1.00 215.96 ? 264  LEU E CG  1 
ATOM   13548 C  CD1 . LEU E  1 264 ? -3.639  -78.731 -25.402  1.00 220.93 ? 264  LEU E CD1 1 
ATOM   13549 C  CD2 . LEU E  1 264 ? -2.306  -80.463 -24.188  1.00 218.67 ? 264  LEU E CD2 1 
ATOM   13550 N  N   . TYR E  1 265 ? 1.516   -77.674 -26.634  1.00 176.75 ? 265  TYR E N   1 
ATOM   13551 C  CA  . TYR E  1 265 ? 2.404   -77.478 -27.767  1.00 190.20 ? 265  TYR E CA  1 
ATOM   13552 C  C   . TYR E  1 265 ? 3.187   -76.189 -27.562  1.00 177.63 ? 265  TYR E C   1 
ATOM   13553 O  O   . TYR E  1 265 ? 2.781   -75.302 -26.806  1.00 164.96 ? 265  TYR E O   1 
ATOM   13554 C  CB  . TYR E  1 265 ? 1.633   -77.440 -29.096  1.00 208.86 ? 265  TYR E CB  1 
ATOM   13555 C  CG  . TYR E  1 265 ? 0.935   -78.739 -29.465  1.00 233.14 ? 265  TYR E CG  1 
ATOM   13556 C  CD1 . TYR E  1 265 ? 1.623   -79.774 -30.093  1.00 241.94 ? 265  TYR E CD1 1 
ATOM   13557 C  CD2 . TYR E  1 265 ? -0.415  -78.927 -29.191  1.00 235.55 ? 265  TYR E CD2 1 
ATOM   13558 C  CE1 . TYR E  1 265 ? 0.984   -80.959 -30.434  1.00 243.51 ? 265  TYR E CE1 1 
ATOM   13559 C  CE2 . TYR E  1 265 ? -1.060  -80.106 -29.527  1.00 235.14 ? 265  TYR E CE2 1 
ATOM   13560 C  CZ  . TYR E  1 265 ? -0.358  -81.117 -30.148  1.00 232.54 ? 265  TYR E CZ  1 
ATOM   13561 O  OH  . TYR E  1 265 ? -1.003  -82.286 -30.482  1.00 214.29 ? 265  TYR E OH  1 
ATOM   13562 N  N   . ASN E  1 266 ? 4.342   -76.117 -28.221  1.00 194.95 ? 266  ASN E N   1 
ATOM   13563 C  CA  . ASN E  1 266 ? 5.201   -74.943 -28.186  1.00 189.93 ? 266  ASN E CA  1 
ATOM   13564 C  C   . ASN E  1 266 ? 5.589   -74.478 -29.582  1.00 185.35 ? 266  ASN E C   1 
ATOM   13565 O  O   . ASN E  1 266 ? 5.798   -75.288 -30.492  1.00 194.92 ? 266  ASN E O   1 
ATOM   13566 C  CB  . ASN E  1 266 ? 6.472   -75.210 -27.398  1.00 192.81 ? 266  ASN E CB  1 
ATOM   13567 C  CG  . ASN E  1 266 ? 6.273   -75.073 -25.915  1.00 173.86 ? 266  ASN E CG  1 
ATOM   13568 O  OD1 . ASN E  1 266 ? 5.350   -74.398 -25.451  1.00 137.07 ? 266  ASN E OD1 1 
ATOM   13569 N  ND2 . ASN E  1 266 ? 7.145   -75.703 -25.153  1.00 225.08 ? 266  ASN E ND2 1 
ATOM   13570 N  N   . PHE E  1 267 ? 5.690   -73.162 -29.730  1.00 165.35 ? 267  PHE E N   1 
ATOM   13571 C  CA  . PHE E  1 267 ? 6.305   -72.529 -30.883  1.00 163.58 ? 267  PHE E CA  1 
ATOM   13572 C  C   . PHE E  1 267 ? 7.455   -71.660 -30.393  1.00 146.90 ? 267  PHE E C   1 
ATOM   13573 O  O   . PHE E  1 267 ? 7.433   -71.156 -29.267  1.00 143.94 ? 267  PHE E O   1 
ATOM   13574 C  CB  . PHE E  1 267 ? 5.295   -71.693 -31.671  1.00 183.81 ? 267  PHE E CB  1 
ATOM   13575 C  CG  . PHE E  1 267 ? 4.121   -72.482 -32.170  1.00 193.88 ? 267  PHE E CG  1 
ATOM   13576 C  CD1 . PHE E  1 267 ? 4.158   -73.111 -33.406  1.00 192.23 ? 267  PHE E CD1 1 
ATOM   13577 C  CD2 . PHE E  1 267 ? 2.984   -72.612 -31.391  1.00 193.35 ? 267  PHE E CD2 1 
ATOM   13578 C  CE1 . PHE E  1 267 ? 3.073   -73.843 -33.858  1.00 195.40 ? 267  PHE E CE1 1 
ATOM   13579 C  CE2 . PHE E  1 267 ? 1.899   -73.340 -31.833  1.00 196.01 ? 267  PHE E CE2 1 
ATOM   13580 C  CZ  . PHE E  1 267 ? 1.941   -73.958 -33.068  1.00 199.91 ? 267  PHE E CZ  1 
ATOM   13581 N  N   . THR E  1 268 ? 8.484   -71.523 -31.225  1.00 154.99 ? 268  THR E N   1 
ATOM   13582 C  CA  . THR E  1 268 ? 9.663   -70.739 -30.881  1.00 153.90 ? 268  THR E CA  1 
ATOM   13583 C  C   . THR E  1 268 ? 10.012  -69.802 -32.028  1.00 160.57 ? 268  THR E C   1 
ATOM   13584 O  O   . THR E  1 268 ? 10.031  -70.220 -33.190  1.00 177.53 ? 268  THR E O   1 
ATOM   13585 C  CB  . THR E  1 268 ? 10.852  -71.648 -30.558  1.00 156.42 ? 268  THR E CB  1 
ATOM   13586 O  OG1 . THR E  1 268 ? 10.445  -72.650 -29.618  1.00 151.59 ? 268  THR E OG1 1 
ATOM   13587 C  CG2 . THR E  1 268 ? 12.004  -70.838 -29.978  1.00 153.38 ? 268  THR E CG2 1 
ATOM   13588 N  N   . GLY E  1 269 ? 10.286  -68.539 -31.698  1.00 164.48 ? 269  GLY E N   1 
ATOM   13589 C  CA  . GLY E  1 269 ? 10.779  -67.609 -32.695  1.00 166.64 ? 269  GLY E CA  1 
ATOM   13590 C  C   . GLY E  1 269 ? 12.135  -68.017 -33.236  1.00 175.25 ? 269  GLY E C   1 
ATOM   13591 O  O   . GLY E  1 269 ? 12.848  -68.834 -32.655  1.00 185.80 ? 269  GLY E O   1 
ATOM   13592 N  N   . GLU E  1 270 ? 12.494  -67.431 -34.380  1.00 179.37 ? 270  GLU E N   1 
ATOM   13593 C  CA  . GLU E  1 270 ? 13.734  -67.774 -35.065  1.00 179.01 ? 270  GLU E CA  1 
ATOM   13594 C  C   . GLU E  1 270 ? 14.702  -66.606 -35.166  1.00 178.60 ? 270  GLU E C   1 
ATOM   13595 O  O   . GLU E  1 270 ? 15.753  -66.744 -35.805  1.00 170.57 ? 270  GLU E O   1 
ATOM   13596 C  CB  . GLU E  1 270 ? 13.440  -68.318 -36.472  1.00 181.09 ? 270  GLU E CB  1 
ATOM   13597 C  CG  . GLU E  1 270 ? 12.584  -69.575 -36.487  1.00 190.76 ? 270  GLU E CG  1 
ATOM   13598 C  CD  . GLU E  1 270 ? 13.360  -70.830 -36.113  1.00 209.56 ? 270  GLU E CD  1 
ATOM   13599 O  OE1 . GLU E  1 270 ? 14.556  -70.728 -35.762  1.00 210.92 ? 270  GLU E OE1 1 
ATOM   13600 O  OE2 . GLU E  1 270 ? 12.766  -71.927 -36.161  1.00 218.19 ? 270  GLU E OE2 1 
ATOM   13601 N  N   . GLN E  1 271 ? 14.379  -65.463 -34.563  1.00 181.30 ? 271  GLN E N   1 
ATOM   13602 C  CA  . GLN E  1 271 ? 15.251  -64.299 -34.559  1.00 173.92 ? 271  GLN E CA  1 
ATOM   13603 C  C   . GLN E  1 271 ? 15.194  -63.624 -33.196  1.00 174.29 ? 271  GLN E C   1 
ATOM   13604 O  O   . GLN E  1 271 ? 14.113  -63.478 -32.618  1.00 173.97 ? 271  GLN E O   1 
ATOM   13605 C  CB  . GLN E  1 271 ? 14.848  -63.306 -35.650  1.00 173.11 ? 271  GLN E CB  1 
ATOM   13606 C  CG  . GLN E  1 271 ? 15.787  -62.129 -35.793  1.00 177.21 ? 271  GLN E CG  1 
ATOM   13607 C  CD  . GLN E  1 271 ? 15.355  -61.183 -36.894  1.00 199.07 ? 271  GLN E CD  1 
ATOM   13608 O  OE1 . GLN E  1 271 ? 14.689  -60.179 -36.641  1.00 200.30 ? 271  GLN E OE1 1 
ATOM   13609 N  NE2 . GLN E  1 271 ? 15.725  -61.504 -38.127  1.00 210.90 ? 271  GLN E NE2 1 
ATOM   13610 N  N   . MET E  1 272 ? 16.360  -63.211 -32.689  1.00 193.21 ? 272  MET E N   1 
ATOM   13611 C  CA  . MET E  1 272 ? 16.435  -62.548 -31.388  1.00 208.79 ? 272  MET E CA  1 
ATOM   13612 C  C   . MET E  1 272 ? 15.659  -61.236 -31.401  1.00 225.16 ? 272  MET E C   1 
ATOM   13613 O  O   . MET E  1 272 ? 15.772  -60.444 -32.341  1.00 233.74 ? 272  MET E O   1 
ATOM   13614 C  CB  . MET E  1 272 ? 17.897  -62.288 -31.009  1.00 196.08 ? 272  MET E CB  1 
ATOM   13615 C  CG  . MET E  1 272 ? 18.766  -63.531 -30.976  1.00 196.98 ? 272  MET E CG  1 
ATOM   13616 S  SD  . MET E  1 272 ? 18.441  -64.547 -29.526  1.00 214.89 ? 272  MET E SD  1 
ATOM   13617 C  CE  . MET E  1 272 ? 19.640  -65.860 -29.749  1.00 227.29 ? 272  MET E CE  1 
ATOM   13618 N  N   . ALA E  1 273 ? 14.854  -61.020 -30.355  1.00 210.72 ? 273  ALA E N   1 
ATOM   13619 C  CA  . ALA E  1 273 ? 14.143  -59.759 -30.133  1.00 181.90 ? 273  ALA E CA  1 
ATOM   13620 C  C   . ALA E  1 273 ? 13.254  -59.383 -31.314  1.00 170.07 ? 273  ALA E C   1 
ATOM   13621 O  O   . ALA E  1 273 ? 13.027  -58.201 -31.589  1.00 172.80 ? 273  ALA E O   1 
ATOM   13622 C  CB  . ALA E  1 273 ? 15.120  -58.623 -29.821  1.00 187.61 ? 273  ALA E CB  1 
ATOM   13623 N  N   . ALA E  1 274 ? 12.728  -60.385 -32.008  1.00 163.26 ? 274  ALA E N   1 
ATOM   13624 C  CA  . ALA E  1 274 ? 11.753  -60.155 -33.060  1.00 164.06 ? 274  ALA E CA  1 
ATOM   13625 C  C   . ALA E  1 274 ? 10.352  -60.020 -32.506  1.00 159.01 ? 274  ALA E C   1 
ATOM   13626 O  O   . ALA E  1 274 ? 9.414   -59.784 -33.275  1.00 159.38 ? 274  ALA E O   1 
ATOM   13627 C  CB  . ALA E  1 274 ? 11.794  -61.293 -34.085  1.00 187.27 ? 274  ALA E CB  1 
ATOM   13628 N  N   . TYR E  1 275 ? 10.202  -60.190 -31.196  1.00 167.02 ? 275  TYR E N   1 
ATOM   13629 C  CA  . TYR E  1 275 ? 8.910   -60.146 -30.526  1.00 163.84 ? 275  TYR E CA  1 
ATOM   13630 C  C   . TYR E  1 275 ? 7.967   -61.189 -31.110  1.00 162.53 ? 275  TYR E C   1 
ATOM   13631 O  O   . TYR E  1 275 ? 6.786   -60.927 -31.348  1.00 162.44 ? 275  TYR E O   1 
ATOM   13632 C  CB  . TYR E  1 275 ? 8.289   -58.748 -30.563  1.00 165.11 ? 275  TYR E CB  1 
ATOM   13633 C  CG  . TYR E  1 275 ? 7.964   -58.243 -29.175  1.00 180.00 ? 275  TYR E CG  1 
ATOM   13634 C  CD1 . TYR E  1 275 ? 8.935   -57.634 -28.389  1.00 178.40 ? 275  TYR E CD1 1 
ATOM   13635 C  CD2 . TYR E  1 275 ? 6.695   -58.400 -28.638  1.00 198.51 ? 275  TYR E CD2 1 
ATOM   13636 C  CE1 . TYR E  1 275 ? 8.645   -57.181 -27.112  1.00 166.78 ? 275  TYR E CE1 1 
ATOM   13637 C  CE2 . TYR E  1 275 ? 6.396   -57.950 -27.363  1.00 191.79 ? 275  TYR E CE2 1 
ATOM   13638 C  CZ  . TYR E  1 275 ? 7.374   -57.342 -26.606  1.00 165.48 ? 275  TYR E CZ  1 
ATOM   13639 O  OH  . TYR E  1 275 ? 7.073   -56.896 -25.341  1.00 164.32 ? 275  TYR E OH  1 
ATOM   13640 N  N   . PHE E  1 276 ? 8.514   -62.371 -31.389  1.00 160.65 ? 276  PHE E N   1 
ATOM   13641 C  CA  . PHE E  1 276 ? 7.708   -63.534 -31.727  1.00 171.71 ? 276  PHE E CA  1 
ATOM   13642 C  C   . PHE E  1 276 ? 6.693   -63.787 -30.622  1.00 149.15 ? 276  PHE E C   1 
ATOM   13643 O  O   . PHE E  1 276 ? 7.060   -64.208 -29.522  1.00 142.07 ? 276  PHE E O   1 
ATOM   13644 C  CB  . PHE E  1 276 ? 8.609   -64.752 -31.934  1.00 174.98 ? 276  PHE E CB  1 
ATOM   13645 C  CG  . PHE E  1 276 ? 7.875   -65.989 -32.353  1.00 166.65 ? 276  PHE E CG  1 
ATOM   13646 C  CD1 . PHE E  1 276 ? 7.606   -66.225 -33.690  1.00 182.16 ? 276  PHE E CD1 1 
ATOM   13647 C  CD2 . PHE E  1 276 ? 7.472   -66.924 -31.416  1.00 149.83 ? 276  PHE E CD2 1 
ATOM   13648 C  CE1 . PHE E  1 276 ? 6.938   -67.362 -34.082  1.00 187.04 ? 276  PHE E CE1 1 
ATOM   13649 C  CE2 . PHE E  1 276 ? 6.802   -68.065 -31.803  1.00 153.64 ? 276  PHE E CE2 1 
ATOM   13650 C  CZ  . PHE E  1 276 ? 6.537   -68.285 -33.138  1.00 170.55 ? 276  PHE E CZ  1 
ATOM   13651 N  N   . GLY E  1 277 ? 5.414   -63.552 -30.909  1.00 154.94 ? 277  GLY E N   1 
ATOM   13652 C  CA  . GLY E  1 277 ? 4.361   -63.708 -29.924  1.00 153.41 ? 277  GLY E CA  1 
ATOM   13653 C  C   . GLY E  1 277 ? 3.679   -62.425 -29.505  1.00 152.45 ? 277  GLY E C   1 
ATOM   13654 O  O   . GLY E  1 277 ? 2.849   -62.459 -28.590  1.00 151.51 ? 277  GLY E O   1 
ATOM   13655 N  N   . PHE E  1 278 ? 4.009   -61.296 -30.135  1.00 173.34 ? 278  PHE E N   1 
ATOM   13656 C  CA  . PHE E  1 278 ? 3.358   -60.032 -29.806  1.00 180.03 ? 278  PHE E CA  1 
ATOM   13657 C  C   . PHE E  1 278 ? 1.848   -60.126 -29.966  1.00 178.03 ? 278  PHE E C   1 
ATOM   13658 O  O   . PHE E  1 278 ? 1.093   -59.630 -29.123  1.00 182.80 ? 278  PHE E O   1 
ATOM   13659 C  CB  . PHE E  1 278 ? 3.914   -58.923 -30.694  1.00 186.03 ? 278  PHE E CB  1 
ATOM   13660 C  CG  . PHE E  1 278 ? 3.273   -57.585 -30.471  1.00 193.24 ? 278  PHE E CG  1 
ATOM   13661 C  CD1 . PHE E  1 278 ? 3.669   -56.788 -29.414  1.00 199.87 ? 278  PHE E CD1 1 
ATOM   13662 C  CD2 . PHE E  1 278 ? 2.293   -57.114 -31.329  1.00 188.66 ? 278  PHE E CD2 1 
ATOM   13663 C  CE1 . PHE E  1 278 ? 3.092   -55.551 -29.204  1.00 196.66 ? 278  PHE E CE1 1 
ATOM   13664 C  CE2 . PHE E  1 278 ? 1.714   -55.877 -31.128  1.00 185.98 ? 278  PHE E CE2 1 
ATOM   13665 C  CZ  . PHE E  1 278 ? 2.114   -55.094 -30.063  1.00 193.78 ? 278  PHE E CZ  1 
ATOM   13666 N  N   . SER E  1 279 ? 1.390   -60.744 -31.050  1.00 177.56 ? 279  SER E N   1 
ATOM   13667 C  CA  . SER E  1 279 ? -0.026  -60.963 -31.295  1.00 164.88 ? 279  SER E CA  1 
ATOM   13668 C  C   . SER E  1 279 ? -0.233  -62.390 -31.776  1.00 164.62 ? 279  SER E C   1 
ATOM   13669 O  O   . SER E  1 279 ? 0.583   -62.925 -32.533  1.00 174.62 ? 279  SER E O   1 
ATOM   13670 C  CB  . SER E  1 279 ? -0.572  -59.973 -32.325  1.00 169.15 ? 279  SER E CB  1 
ATOM   13671 O  OG  . SER E  1 279 ? 0.071   -60.148 -33.573  1.00 192.04 ? 279  SER E OG  1 
ATOM   13672 N  N   . VAL E  1 280 ? -1.334  -63.000 -31.338  1.00 142.50 ? 280  VAL E N   1 
ATOM   13673 C  CA  . VAL E  1 280 ? -1.694  -64.352 -31.739  1.00 147.53 ? 280  VAL E CA  1 
ATOM   13674 C  C   . VAL E  1 280 ? -3.180  -64.390 -32.059  1.00 154.28 ? 280  VAL E C   1 
ATOM   13675 O  O   . VAL E  1 280 ? -3.960  -63.547 -31.614  1.00 154.09 ? 280  VAL E O   1 
ATOM   13676 C  CB  . VAL E  1 280 ? -1.357  -65.399 -30.656  1.00 146.68 ? 280  VAL E CB  1 
ATOM   13677 C  CG1 . VAL E  1 280 ? 0.149   -65.591 -30.556  1.00 141.28 ? 280  VAL E CG1 1 
ATOM   13678 C  CG2 . VAL E  1 280 ? -1.937  -64.977 -29.324  1.00 149.85 ? 280  VAL E CG2 1 
ATOM   13679 N  N   . ALA E  1 281 ? -3.560  -65.380 -32.859  1.00 145.40 ? 281  ALA E N   1 
ATOM   13680 C  CA  . ALA E  1 281 ? -4.949  -65.578 -33.236  1.00 153.41 ? 281  ALA E CA  1 
ATOM   13681 C  C   . ALA E  1 281 ? -5.147  -67.046 -33.567  1.00 161.14 ? 281  ALA E C   1 
ATOM   13682 O  O   . ALA E  1 281 ? -4.202  -67.742 -33.944  1.00 160.76 ? 281  ALA E O   1 
ATOM   13683 C  CB  . ALA E  1 281 ? -5.353  -64.698 -34.423  1.00 163.52 ? 281  ALA E CB  1 
ATOM   13684 N  N   . ALA E  1 282 ? -6.375  -67.521 -33.396  1.00 169.62 ? 282  ALA E N   1 
ATOM   13685 C  CA  . ALA E  1 282 ? -6.698  -68.919 -33.661  1.00 178.09 ? 282  ALA E CA  1 
ATOM   13686 C  C   . ALA E  1 282 ? -7.993  -68.999 -34.458  1.00 187.55 ? 282  ALA E C   1 
ATOM   13687 O  O   . ALA E  1 282 ? -9.062  -68.640 -33.953  1.00 196.74 ? 282  ALA E O   1 
ATOM   13688 C  CB  . ALA E  1 282 ? -6.802  -69.709 -32.358  1.00 178.48 ? 282  ALA E CB  1 
ATOM   13689 N  N   . THR E  1 283 ? -7.897  -69.477 -35.697  1.00 193.76 ? 283  THR E N   1 
ATOM   13690 C  CA  . THR E  1 283 ? -9.077  -69.705 -36.519  1.00 211.16 ? 283  THR E CA  1 
ATOM   13691 C  C   . THR E  1 283 ? -8.735  -70.737 -37.585  1.00 217.85 ? 283  THR E C   1 
ATOM   13692 O  O   . THR E  1 283 ? -7.612  -70.761 -38.096  1.00 213.54 ? 283  THR E O   1 
ATOM   13693 C  CB  . THR E  1 283 ? -9.576  -68.401 -37.158  1.00 211.00 ? 283  THR E CB  1 
ATOM   13694 O  OG1 . THR E  1 283 ? -10.645 -68.681 -38.073  1.00 225.92 ? 283  THR E OG1 1 
ATOM   13695 C  CG2 . THR E  1 283 ? -8.446  -67.701 -37.900  1.00 193.83 ? 283  THR E CG2 1 
ATOM   13696 N  N   . ASP E  1 284 ? -9.702  -71.598 -37.899  1.00 220.14 ? 284  ASP E N   1 
ATOM   13697 C  CA  . ASP E  1 284 ? -9.537  -72.608 -38.944  1.00 220.47 ? 284  ASP E CA  1 
ATOM   13698 C  C   . ASP E  1 284 ? -9.537  -71.929 -40.310  1.00 213.67 ? 284  ASP E C   1 
ATOM   13699 O  O   . ASP E  1 284 ? -10.555 -71.370 -40.731  1.00 218.20 ? 284  ASP E O   1 
ATOM   13700 C  CB  . ASP E  1 284 ? -10.648 -73.650 -38.843  1.00 226.05 ? 284  ASP E CB  1 
ATOM   13701 C  CG  . ASP E  1 284 ? -10.546 -74.716 -39.915  1.00 232.25 ? 284  ASP E CG  1 
ATOM   13702 O  OD1 . ASP E  1 284 ? -9.410  -75.063 -40.302  1.00 235.50 ? 284  ASP E OD1 1 
ATOM   13703 O  OD2 . ASP E  1 284 ? -11.601 -75.212 -40.367  1.00 232.67 ? 284  ASP E OD2 1 
ATOM   13704 N  N   . ILE E  1 285 ? -8.399  -71.970 -41.004  1.00 208.89 ? 285  ILE E N   1 
ATOM   13705 C  CA  . ILE E  1 285 ? -8.241  -71.234 -42.255  1.00 210.09 ? 285  ILE E CA  1 
ATOM   13706 C  C   . ILE E  1 285 ? -8.374  -72.114 -43.497  1.00 213.85 ? 285  ILE E C   1 
ATOM   13707 O  O   . ILE E  1 285 ? -8.584  -71.581 -44.597  1.00 212.42 ? 285  ILE E O   1 
ATOM   13708 C  CB  . ILE E  1 285 ? -6.885  -70.498 -42.283  1.00 206.47 ? 285  ILE E CB  1 
ATOM   13709 C  CG1 . ILE E  1 285 ? -6.966  -69.244 -43.156  1.00 204.53 ? 285  ILE E CG1 1 
ATOM   13710 C  CG2 . ILE E  1 285 ? -5.781  -71.424 -42.766  1.00 215.88 ? 285  ILE E CG2 1 
ATOM   13711 C  CD1 . ILE E  1 285 ? -7.747  -68.124 -42.516  1.00 211.81 ? 285  ILE E CD1 1 
ATOM   13712 N  N   . ASN E  1 286 ? -8.248  -73.435 -43.359  1.00 219.73 ? 286  ASN E N   1 
ATOM   13713 C  CA  . ASN E  1 286 ? -8.241  -74.344 -44.500  1.00 220.19 ? 286  ASN E CA  1 
ATOM   13714 C  C   . ASN E  1 286 ? -9.399  -75.335 -44.467  1.00 221.54 ? 286  ASN E C   1 
ATOM   13715 O  O   . ASN E  1 286 ? -9.330  -76.382 -45.117  1.00 221.03 ? 286  ASN E O   1 
ATOM   13716 C  CB  . ASN E  1 286 ? -6.907  -75.089 -44.567  1.00 218.88 ? 286  ASN E CB  1 
ATOM   13717 C  CG  . ASN E  1 286 ? -6.564  -75.779 -43.262  1.00 223.65 ? 286  ASN E CG  1 
ATOM   13718 O  OD1 . ASN E  1 286 ? -6.980  -75.342 -42.190  1.00 218.82 ? 286  ASN E OD1 1 
ATOM   13719 N  ND2 . ASN E  1 286 ? -5.813  -76.871 -43.347  1.00 224.68 ? 286  ASN E ND2 1 
ATOM   13720 N  N   . GLY E  1 287 ? -10.468 -75.015 -43.739  1.00 219.41 ? 287  GLY E N   1 
ATOM   13721 C  CA  . GLY E  1 287 ? -11.683 -75.810 -43.727  1.00 220.97 ? 287  GLY E CA  1 
ATOM   13722 C  C   . GLY E  1 287 ? -11.527 -77.259 -43.304  1.00 220.23 ? 287  GLY E C   1 
ATOM   13723 O  O   . GLY E  1 287 ? -12.019 -78.160 -43.990  1.00 231.27 ? 287  GLY E O   1 
ATOM   13724 N  N   . ASP E  1 288 ? -10.856 -77.502 -42.175  1.00 224.93 ? 288  ASP E N   1 
ATOM   13725 C  CA  . ASP E  1 288 ? -10.708 -78.849 -41.632  1.00 234.01 ? 288  ASP E CA  1 
ATOM   13726 C  C   . ASP E  1 288 ? -11.220 -78.972 -40.200  1.00 226.37 ? 288  ASP E C   1 
ATOM   13727 O  O   . ASP E  1 288 ? -11.015 -80.016 -39.568  1.00 222.68 ? 288  ASP E O   1 
ATOM   13728 C  CB  . ASP E  1 288 ? -9.244  -79.309 -41.706  1.00 242.19 ? 288  ASP E CB  1 
ATOM   13729 C  CG  . ASP E  1 288 ? -8.264  -78.288 -41.134  1.00 238.55 ? 288  ASP E CG  1 
ATOM   13730 O  OD1 . ASP E  1 288 ? -8.578  -77.080 -41.125  1.00 243.39 ? 288  ASP E OD1 1 
ATOM   13731 O  OD2 . ASP E  1 288 ? -7.163  -78.698 -40.705  1.00 232.71 ? 288  ASP E OD2 1 
ATOM   13732 N  N   . ASP E  1 289 ? -11.870 -77.935 -39.671  1.00 233.10 ? 289  ASP E N   1 
ATOM   13733 C  CA  . ASP E  1 289 ? -12.417 -77.877 -38.318  1.00 241.67 ? 289  ASP E CA  1 
ATOM   13734 C  C   . ASP E  1 289 ? -11.334 -77.928 -37.251  1.00 232.74 ? 289  ASP E C   1 
ATOM   13735 O  O   . ASP E  1 289 ? -11.647 -78.090 -36.062  1.00 228.63 ? 289  ASP E O   1 
ATOM   13736 C  CB  . ASP E  1 289 ? -13.440 -78.990 -38.061  1.00 256.90 ? 289  ASP E CB  1 
ATOM   13737 C  CG  . ASP E  1 289 ? -14.608 -78.941 -39.023  1.00 268.99 ? 289  ASP E CG  1 
ATOM   13738 O  OD1 . ASP E  1 289 ? -14.489 -79.509 -40.128  1.00 275.40 ? 289  ASP E OD1 1 
ATOM   13739 O  OD2 . ASP E  1 289 ? -15.646 -78.336 -38.675  1.00 272.02 ? 289  ASP E OD2 1 
ATOM   13740 N  N   . TYR E  1 290 ? -10.071 -77.800 -37.640  1.00 225.01 ? 290  TYR E N   1 
ATOM   13741 C  CA  . TYR E  1 290 ? -8.957  -77.666 -36.710  1.00 218.30 ? 290  TYR E CA  1 
ATOM   13742 C  C   . TYR E  1 290 ? -8.499  -76.211 -36.708  1.00 215.67 ? 290  TYR E C   1 
ATOM   13743 O  O   . TYR E  1 290 ? -8.041  -75.696 -37.735  1.00 216.76 ? 290  TYR E O   1 
ATOM   13744 C  CB  . TYR E  1 290 ? -7.817  -78.606 -37.090  1.00 216.16 ? 290  TYR E CB  1 
ATOM   13745 C  CG  . TYR E  1 290 ? -8.088  -80.058 -36.767  1.00 220.34 ? 290  TYR E CG  1 
ATOM   13746 C  CD1 . TYR E  1 290 ? -8.709  -80.424 -35.579  1.00 230.36 ? 290  TYR E CD1 1 
ATOM   13747 C  CD2 . TYR E  1 290 ? -7.718  -81.062 -37.648  1.00 216.69 ? 290  TYR E CD2 1 
ATOM   13748 C  CE1 . TYR E  1 290 ? -8.953  -81.752 -35.283  1.00 232.97 ? 290  TYR E CE1 1 
ATOM   13749 C  CE2 . TYR E  1 290 ? -7.959  -82.387 -37.362  1.00 217.27 ? 290  TYR E CE2 1 
ATOM   13750 C  CZ  . TYR E  1 290 ? -8.575  -82.730 -36.179  1.00 217.63 ? 290  TYR E CZ  1 
ATOM   13751 O  OH  . TYR E  1 290 ? -8.816  -84.053 -35.889  1.00 215.19 ? 290  TYR E OH  1 
ATOM   13752 N  N   . ALA E  1 291 ? -8.658  -75.545 -35.566  1.00 215.93 ? 291  ALA E N   1 
ATOM   13753 C  CA  . ALA E  1 291 ? -8.189  -74.172 -35.428  1.00 216.36 ? 291  ALA E CA  1 
ATOM   13754 C  C   . ALA E  1 291 ? -6.691  -74.086 -35.698  1.00 204.46 ? 291  ALA E C   1 
ATOM   13755 O  O   . ALA E  1 291 ? -5.920  -74.963 -35.301  1.00 215.48 ? 291  ALA E O   1 
ATOM   13756 C  CB  . ALA E  1 291 ? -8.507  -73.644 -34.027  1.00 232.07 ? 291  ALA E CB  1 
ATOM   13757 N  N   . ASP E  1 292 ? -6.279  -73.013 -36.371  1.00 194.32 ? 292  ASP E N   1 
ATOM   13758 C  CA  . ASP E  1 292 ? -4.896  -72.826 -36.787  1.00 190.74 ? 292  ASP E CA  1 
ATOM   13759 C  C   . ASP E  1 292 ? -4.288  -71.627 -36.069  1.00 199.71 ? 292  ASP E C   1 
ATOM   13760 O  O   . ASP E  1 292 ? -4.984  -70.664 -35.735  1.00 220.07 ? 292  ASP E O   1 
ATOM   13761 C  CB  . ASP E  1 292 ? -4.803  -72.638 -38.306  1.00 206.00 ? 292  ASP E CB  1 
ATOM   13762 C  CG  . ASP E  1 292 ? -5.463  -73.772 -39.074  1.00 220.87 ? 292  ASP E CG  1 
ATOM   13763 O  OD1 . ASP E  1 292 ? -5.270  -74.944 -38.685  1.00 232.50 ? 292  ASP E OD1 1 
ATOM   13764 O  OD2 . ASP E  1 292 ? -6.173  -73.497 -40.065  1.00 213.15 ? 292  ASP E OD2 1 
ATOM   13765 N  N   . VAL E  1 293 ? -2.974  -71.693 -35.841  1.00 189.91 ? 293  VAL E N   1 
ATOM   13766 C  CA  . VAL E  1 293 ? -2.254  -70.723 -35.016  1.00 176.43 ? 293  VAL E CA  1 
ATOM   13767 C  C   . VAL E  1 293 ? -1.551  -69.706 -35.905  1.00 169.72 ? 293  VAL E C   1 
ATOM   13768 O  O   . VAL E  1 293 ? -0.806  -70.077 -36.823  1.00 170.31 ? 293  VAL E O   1 
ATOM   13769 C  CB  . VAL E  1 293 ? -1.248  -71.428 -34.092  1.00 167.19 ? 293  VAL E CB  1 
ATOM   13770 C  CG1 . VAL E  1 293 ? -0.526  -70.417 -33.229  1.00 164.37 ? 293  VAL E CG1 1 
ATOM   13771 C  CG2 . VAL E  1 293 ? -1.956  -72.455 -33.229  1.00 170.21 ? 293  VAL E CG2 1 
ATOM   13772 N  N   . PHE E  1 294 ? -1.790  -68.423 -35.633  1.00 175.35 ? 294  PHE E N   1 
ATOM   13773 C  CA  . PHE E  1 294 ? -1.144  -67.311 -36.321  1.00 170.60 ? 294  PHE E CA  1 
ATOM   13774 C  C   . PHE E  1 294 ? -0.348  -66.510 -35.298  1.00 164.97 ? 294  PHE E C   1 
ATOM   13775 O  O   . PHE E  1 294 ? -0.929  -65.940 -34.368  1.00 175.00 ? 294  PHE E O   1 
ATOM   13776 C  CB  . PHE E  1 294 ? -2.177  -66.417 -37.012  1.00 176.55 ? 294  PHE E CB  1 
ATOM   13777 C  CG  . PHE E  1 294 ? -2.976  -67.111 -38.088  1.00 189.54 ? 294  PHE E CG  1 
ATOM   13778 C  CD1 . PHE E  1 294 ? -4.119  -67.826 -37.765  1.00 197.50 ? 294  PHE E CD1 1 
ATOM   13779 C  CD2 . PHE E  1 294 ? -2.602  -67.026 -39.420  1.00 204.38 ? 294  PHE E CD2 1 
ATOM   13780 C  CE1 . PHE E  1 294 ? -4.866  -68.457 -38.744  1.00 212.25 ? 294  PHE E CE1 1 
ATOM   13781 C  CE2 . PHE E  1 294 ? -3.347  -67.656 -40.407  1.00 214.87 ? 294  PHE E CE2 1 
ATOM   13782 C  CZ  . PHE E  1 294 ? -4.480  -68.372 -40.066  1.00 221.71 ? 294  PHE E CZ  1 
ATOM   13783 N  N   . ILE E  1 295 ? 0.970   -66.451 -35.472  1.00 152.43 ? 295  ILE E N   1 
ATOM   13784 C  CA  . ILE E  1 295 ? 1.863   -65.799 -34.517  1.00 144.61 ? 295  ILE E CA  1 
ATOM   13785 C  C   . ILE E  1 295 ? 2.540   -64.621 -35.199  1.00 142.68 ? 295  ILE E C   1 
ATOM   13786 O  O   . ILE E  1 295 ? 3.254   -64.800 -36.192  1.00 144.94 ? 295  ILE E O   1 
ATOM   13787 C  CB  . ILE E  1 295 ? 2.905   -66.777 -33.970  1.00 147.75 ? 295  ILE E CB  1 
ATOM   13788 C  CG1 . ILE E  1 295 ? 2.201   -67.997 -33.382  1.00 162.98 ? 295  ILE E CG1 1 
ATOM   13789 C  CG2 . ILE E  1 295 ? 3.774   -66.087 -32.934  1.00 147.88 ? 295  ILE E CG2 1 
ATOM   13790 C  CD1 . ILE E  1 295 ? 3.132   -69.121 -33.019  1.00 166.83 ? 295  ILE E CD1 1 
ATOM   13791 N  N   . GLY E  1 296 ? 2.350   -63.426 -34.644  1.00 143.24 ? 296  GLY E N   1 
ATOM   13792 C  CA  . GLY E  1 296 ? 2.957   -62.231 -35.199  1.00 142.09 ? 296  GLY E CA  1 
ATOM   13793 C  C   . GLY E  1 296 ? 4.294   -61.923 -34.544  1.00 138.04 ? 296  GLY E C   1 
ATOM   13794 O  O   . GLY E  1 296 ? 4.449   -62.045 -33.334  1.00 134.52 ? 296  GLY E O   1 
ATOM   13795 N  N   . ALA E  1 297 ? 5.262   -61.535 -35.370  1.00 157.21 ? 297  ALA E N   1 
ATOM   13796 C  CA  . ALA E  1 297 ? 6.579   -61.099 -34.908  1.00 156.92 ? 297  ALA E CA  1 
ATOM   13797 C  C   . ALA E  1 297 ? 6.870   -59.771 -35.588  1.00 156.66 ? 297  ALA E C   1 
ATOM   13798 O  O   . ALA E  1 297 ? 7.669   -59.702 -36.532  1.00 159.73 ? 297  ALA E O   1 
ATOM   13799 C  CB  . ALA E  1 297 ? 7.657   -62.137 -35.212  1.00 156.92 ? 297  ALA E CB  1 
ATOM   13800 N  N   . PRO E  1 298 ? 6.259   -58.686 -35.102  1.00 153.27 ? 298  PRO E N   1 
ATOM   13801 C  CA  . PRO E  1 298 ? 6.301   -57.411 -35.834  1.00 156.22 ? 298  PRO E CA  1 
ATOM   13802 C  C   . PRO E  1 298 ? 7.682   -56.804 -35.923  1.00 159.01 ? 298  PRO E C   1 
ATOM   13803 O  O   . PRO E  1 298 ? 7.896   -55.895 -36.736  1.00 162.35 ? 298  PRO E O   1 
ATOM   13804 C  CB  . PRO E  1 298 ? 5.355   -56.509 -35.023  1.00 178.71 ? 298  PRO E CB  1 
ATOM   13805 C  CG  . PRO E  1 298 ? 4.556   -57.447 -34.157  1.00 171.70 ? 298  PRO E CG  1 
ATOM   13806 C  CD  . PRO E  1 298 ? 5.488   -58.580 -33.857  1.00 152.45 ? 298  PRO E CD  1 
ATOM   13807 N  N   . LEU E  1 299 ? 8.633   -57.293 -35.138  1.00 171.47 ? 299  LEU E N   1 
ATOM   13808 C  CA  . LEU E  1 299 ? 9.974   -56.737 -35.107  1.00 180.77 ? 299  LEU E CA  1 
ATOM   13809 C  C   . LEU E  1 299 ? 10.945  -57.618 -35.864  1.00 175.76 ? 299  LEU E C   1 
ATOM   13810 O  O   . LEU E  1 299 ? 12.156  -57.375 -35.826  1.00 183.94 ? 299  LEU E O   1 
ATOM   13811 C  CB  . LEU E  1 299 ? 10.444  -56.559 -33.663  1.00 197.11 ? 299  LEU E CB  1 
ATOM   13812 C  CG  . LEU E  1 299 ? 9.496   -55.785 -32.750  1.00 207.51 ? 299  LEU E CG  1 
ATOM   13813 C  CD1 . LEU E  1 299 ? 10.107  -55.599 -31.369  1.00 214.95 ? 299  LEU E CD1 1 
ATOM   13814 C  CD2 . LEU E  1 299 ? 9.132   -54.441 -33.367  1.00 201.74 ? 299  LEU E CD2 1 
ATOM   13815 N  N   . PHE E  1 300 ? 10.434  -58.634 -36.551  1.00 167.49 ? 300  PHE E N   1 
ATOM   13816 C  CA  . PHE E  1 300 ? 11.281  -59.524 -37.325  1.00 170.56 ? 300  PHE E CA  1 
ATOM   13817 C  C   . PHE E  1 300 ? 12.044  -58.757 -38.392  1.00 176.40 ? 300  PHE E C   1 
ATOM   13818 O  O   . PHE E  1 300 ? 11.467  -57.965 -39.141  1.00 182.81 ? 300  PHE E O   1 
ATOM   13819 C  CB  . PHE E  1 300 ? 10.436  -60.618 -37.970  1.00 181.25 ? 300  PHE E CB  1 
ATOM   13820 C  CG  . PHE E  1 300 ? 11.243  -61.648 -38.701  1.00 200.85 ? 300  PHE E CG  1 
ATOM   13821 C  CD1 . PHE E  1 300 ? 11.725  -62.764 -38.040  1.00 219.30 ? 300  PHE E CD1 1 
ATOM   13822 C  CD2 . PHE E  1 300 ? 11.521  -61.502 -40.052  1.00 194.67 ? 300  PHE E CD2 1 
ATOM   13823 C  CE1 . PHE E  1 300 ? 12.472  -63.717 -38.710  1.00 225.00 ? 300  PHE E CE1 1 
ATOM   13824 C  CE2 . PHE E  1 300 ? 12.267  -62.451 -40.729  1.00 200.46 ? 300  PHE E CE2 1 
ATOM   13825 C  CZ  . PHE E  1 300 ? 12.743  -63.561 -40.057  1.00 215.37 ? 300  PHE E CZ  1 
ATOM   13826 N  N   . MET E  1 301 ? 13.342  -59.011 -38.468  1.00 174.72 ? 301  MET E N   1 
ATOM   13827 C  CA  . MET E  1 301 ? 14.200  -58.419 -39.478  1.00 180.58 ? 301  MET E CA  1 
ATOM   13828 C  C   . MET E  1 301 ? 14.553  -59.481 -40.504  1.00 183.30 ? 301  MET E C   1 
ATOM   13829 O  O   . MET E  1 301 ? 15.030  -60.563 -40.149  1.00 192.98 ? 301  MET E O   1 
ATOM   13830 C  CB  . MET E  1 301 ? 15.469  -57.839 -38.865  1.00 183.53 ? 301  MET E CB  1 
ATOM   13831 C  CG  . MET E  1 301 ? 15.231  -56.930 -37.697  1.00 182.90 ? 301  MET E CG  1 
ATOM   13832 S  SD  . MET E  1 301 ? 16.817  -56.318 -37.135  1.00 210.15 ? 301  MET E SD  1 
ATOM   13833 C  CE  . MET E  1 301 ? 17.299  -55.307 -38.534  1.00 209.67 ? 301  MET E CE  1 
ATOM   13834 N  N   . ASP E  1 302 ? 14.298  -59.175 -41.769  1.00 181.71 ? 302  ASP E N   1 
ATOM   13835 C  CA  . ASP E  1 302 ? 14.678  -60.026 -42.880  1.00 185.20 ? 302  ASP E CA  1 
ATOM   13836 C  C   . ASP E  1 302 ? 15.831  -59.382 -43.639  1.00 195.43 ? 302  ASP E C   1 
ATOM   13837 O  O   . ASP E  1 302 ? 16.142  -58.201 -43.464  1.00 200.14 ? 302  ASP E O   1 
ATOM   13838 C  CB  . ASP E  1 302 ? 13.463  -60.269 -43.785  1.00 185.06 ? 302  ASP E CB  1 
ATOM   13839 C  CG  . ASP E  1 302 ? 13.813  -60.969 -45.077  1.00 199.69 ? 302  ASP E CG  1 
ATOM   13840 O  OD1 . ASP E  1 302 ? 14.072  -62.190 -45.046  1.00 209.19 ? 302  ASP E OD1 1 
ATOM   13841 O  OD2 . ASP E  1 302 ? 13.831  -60.293 -46.126  1.00 206.75 ? 302  ASP E OD2 1 
ATOM   13842 N  N   . ARG E  1 303 ? 16.451  -60.167 -44.516  1.00 195.72 ? 303  ARG E N   1 
ATOM   13843 C  CA  . ARG E  1 303 ? 17.558  -59.695 -45.331  1.00 196.48 ? 303  ARG E CA  1 
ATOM   13844 C  C   . ARG E  1 303 ? 17.029  -59.189 -46.669  1.00 201.47 ? 303  ARG E C   1 
ATOM   13845 O  O   . ARG E  1 303 ? 16.205  -59.841 -47.312  1.00 190.65 ? 303  ARG E O   1 
ATOM   13846 C  CB  . ARG E  1 303 ? 18.567  -60.823 -45.545  1.00 196.29 ? 303  ARG E CB  1 
ATOM   13847 C  CG  . ARG E  1 303 ? 19.839  -60.376 -46.221  1.00 205.65 ? 303  ARG E CG  1 
ATOM   13848 C  CD  . ARG E  1 303 ? 20.638  -59.422 -45.353  1.00 201.56 ? 303  ARG E CD  1 
ATOM   13849 N  NE  . ARG E  1 303 ? 21.391  -60.128 -44.322  1.00 208.25 ? 303  ARG E NE  1 
ATOM   13850 C  CZ  . ARG E  1 303 ? 22.279  -59.548 -43.522  1.00 220.73 ? 303  ARG E CZ  1 
ATOM   13851 N  NH1 . ARG E  1 303 ? 22.528  -58.252 -43.643  1.00 234.34 ? 303  ARG E NH1 1 
ATOM   13852 N  NH2 . ARG E  1 303 ? 22.922  -60.261 -42.609  1.00 208.06 ? 303  ARG E NH2 1 
ATOM   13853 N  N   . GLY E  1 304 ? 17.521  -58.032 -47.101  1.00 202.41 ? 304  GLY E N   1 
ATOM   13854 C  CA  . GLY E  1 304 ? 17.106  -57.470 -48.366  1.00 203.02 ? 304  GLY E CA  1 
ATOM   13855 C  C   . GLY E  1 304 ? 17.903  -58.012 -49.536  1.00 208.89 ? 304  GLY E C   1 
ATOM   13856 O  O   . GLY E  1 304 ? 18.825  -58.813 -49.394  1.00 205.81 ? 304  GLY E O   1 
ATOM   13857 N  N   . SER E  1 305 ? 17.525  -57.549 -50.730  1.00 240.06 ? 305  SER E N   1 
ATOM   13858 C  CA  . SER E  1 305 ? 18.218  -57.982 -51.938  1.00 249.68 ? 305  SER E CA  1 
ATOM   13859 C  C   . SER E  1 305 ? 19.636  -57.431 -51.983  1.00 255.96 ? 305  SER E C   1 
ATOM   13860 O  O   . SER E  1 305 ? 20.527  -58.047 -52.579  1.00 252.99 ? 305  SER E O   1 
ATOM   13861 C  CB  . SER E  1 305 ? 17.433  -57.551 -53.177  1.00 238.95 ? 305  SER E CB  1 
ATOM   13862 O  OG  . SER E  1 305 ? 16.110  -58.067 -53.158  1.00 229.82 ? 305  SER E OG  1 
ATOM   13863 N  N   . ASP E  1 306 ? 19.863  -56.288 -51.344  1.00 258.38 ? 306  ASP E N   1 
ATOM   13864 C  CA  . ASP E  1 306 ? 21.161  -55.633 -51.316  1.00 250.75 ? 306  ASP E CA  1 
ATOM   13865 C  C   . ASP E  1 306 ? 22.063  -56.147 -50.207  1.00 241.05 ? 306  ASP E C   1 
ATOM   13866 O  O   . ASP E  1 306 ? 23.186  -55.653 -50.066  1.00 237.95 ? 306  ASP E O   1 
ATOM   13867 C  CB  . ASP E  1 306 ? 20.977  -54.121 -51.164  1.00 248.18 ? 306  ASP E CB  1 
ATOM   13868 C  CG  . ASP E  1 306 ? 19.825  -53.762 -50.244  1.00 249.01 ? 306  ASP E CG  1 
ATOM   13869 O  OD1 . ASP E  1 306 ? 19.568  -54.505 -49.270  1.00 237.87 ? 306  ASP E OD1 1 
ATOM   13870 O  OD2 . ASP E  1 306 ? 19.163  -52.739 -50.512  1.00 256.02 ? 306  ASP E OD2 1 
ATOM   13871 N  N   . GLY E  1 307 ? 21.610  -57.123 -49.426  1.00 242.43 ? 307  GLY E N   1 
ATOM   13872 C  CA  . GLY E  1 307 ? 22.390  -57.647 -48.333  1.00 240.92 ? 307  GLY E CA  1 
ATOM   13873 C  C   . GLY E  1 307 ? 22.238  -56.892 -47.032  1.00 230.77 ? 307  GLY E C   1 
ATOM   13874 O  O   . GLY E  1 307 ? 22.833  -57.298 -46.025  1.00 228.32 ? 307  GLY E O   1 
ATOM   13875 N  N   . LYS E  1 308 ? 21.489  -55.795 -47.024  1.00 219.04 ? 308  LYS E N   1 
ATOM   13876 C  CA  . LYS E  1 308 ? 21.267  -55.022 -45.814  1.00 225.50 ? 308  LYS E CA  1 
ATOM   13877 C  C   . LYS E  1 308 ? 20.027  -55.525 -45.081  1.00 223.16 ? 308  LYS E C   1 
ATOM   13878 O  O   . LYS E  1 308 ? 19.018  -55.870 -45.702  1.00 218.09 ? 308  LYS E O   1 
ATOM   13879 C  CB  . LYS E  1 308 ? 21.130  -53.537 -46.153  1.00 231.66 ? 308  LYS E CB  1 
ATOM   13880 C  CG  . LYS E  1 308 ? 21.263  -52.602 -44.966  1.00 241.54 ? 308  LYS E CG  1 
ATOM   13881 C  CD  . LYS E  1 308 ? 20.980  -51.164 -45.370  1.00 234.58 ? 308  LYS E CD  1 
ATOM   13882 C  CE  . LYS E  1 308 ? 21.980  -50.670 -46.405  1.00 217.65 ? 308  LYS E CE  1 
ATOM   13883 N  NZ  . LYS E  1 308 ? 23.380  -50.704 -45.899  1.00 216.84 ? 308  LYS E NZ  1 
ATOM   13884 N  N   . LEU E  1 309 ? 20.119  -55.576 -43.752  1.00 220.84 ? 309  LEU E N   1 
ATOM   13885 C  CA  . LEU E  1 309 ? 18.987  -55.972 -42.926  1.00 210.52 ? 309  LEU E CA  1 
ATOM   13886 C  C   . LEU E  1 309 ? 17.866  -54.945 -43.027  1.00 215.94 ? 309  LEU E C   1 
ATOM   13887 O  O   . LEU E  1 309 ? 18.104  -53.744 -43.179  1.00 226.56 ? 309  LEU E O   1 
ATOM   13888 C  CB  . LEU E  1 309 ? 19.422  -56.125 -41.468  1.00 204.27 ? 309  LEU E CB  1 
ATOM   13889 C  CG  . LEU E  1 309 ? 20.387  -57.271 -41.168  1.00 204.47 ? 309  LEU E CG  1 
ATOM   13890 C  CD1 . LEU E  1 309 ? 20.888  -57.168 -39.741  1.00 208.40 ? 309  LEU E CD1 1 
ATOM   13891 C  CD2 . LEU E  1 309 ? 19.717  -58.615 -41.409  1.00 196.84 ? 309  LEU E CD2 1 
ATOM   13892 N  N   . GLN E  1 310 ? 16.629  -55.424 -42.931  1.00 195.31 ? 310  GLN E N   1 
ATOM   13893 C  CA  . GLN E  1 310 ? 15.489  -54.521 -42.883  1.00 190.01 ? 310  GLN E CA  1 
ATOM   13894 C  C   . GLN E  1 310 ? 14.413  -55.106 -41.982  1.00 187.29 ? 310  GLN E C   1 
ATOM   13895 O  O   . GLN E  1 310 ? 14.034  -56.271 -42.135  1.00 181.69 ? 310  GLN E O   1 
ATOM   13896 C  CB  . GLN E  1 310 ? 14.929  -54.255 -44.284  1.00 194.58 ? 310  GLN E CB  1 
ATOM   13897 C  CG  . GLN E  1 310 ? 14.712  -55.506 -45.122  1.00 201.05 ? 310  GLN E CG  1 
ATOM   13898 C  CD  . GLN E  1 310 ? 13.972  -55.205 -46.408  1.00 210.64 ? 310  GLN E CD  1 
ATOM   13899 O  OE1 . GLN E  1 310 ? 14.008  -54.080 -46.901  1.00 220.79 ? 310  GLN E OE1 1 
ATOM   13900 N  NE2 . GLN E  1 310 ? 13.294  -56.208 -46.959  1.00 211.72 ? 310  GLN E NE2 1 
ATOM   13901 N  N   . GLU E  1 311 ? 13.940  -54.294 -41.040  1.00 199.80 ? 311  GLU E N   1 
ATOM   13902 C  CA  . GLU E  1 311 ? 12.862  -54.676 -40.132  1.00 198.58 ? 311  GLU E CA  1 
ATOM   13903 C  C   . GLU E  1 311 ? 11.530  -54.612 -40.869  1.00 214.90 ? 311  GLU E C   1 
ATOM   13904 O  O   . GLU E  1 311 ? 11.061  -53.524 -41.215  1.00 238.73 ? 311  GLU E O   1 
ATOM   13905 C  CB  . GLU E  1 311 ? 12.834  -53.756 -38.918  1.00 185.98 ? 311  GLU E CB  1 
ATOM   13906 C  CG  . GLU E  1 311 ? 11.722  -54.075 -37.944  1.00 193.95 ? 311  GLU E CG  1 
ATOM   13907 C  CD  . GLU E  1 311 ? 11.600  -53.024 -36.865  1.00 207.06 ? 311  GLU E CD  1 
ATOM   13908 O  OE1 . GLU E  1 311 ? 12.514  -52.179 -36.758  1.00 208.16 ? 311  GLU E OE1 1 
ATOM   13909 O  OE2 . GLU E  1 311 ? 10.583  -53.024 -36.140  1.00 212.70 ? 311  GLU E OE2 1 
ATOM   13910 N  N   . VAL E  1 312 ? 10.908  -55.767 -41.097  1.00 204.73 ? 312  VAL E N   1 
ATOM   13911 C  CA  . VAL E  1 312 ? 9.628   -55.812 -41.801  1.00 197.72 ? 312  VAL E CA  1 
ATOM   13912 C  C   . VAL E  1 312 ? 8.537   -56.529 -41.026  1.00 169.59 ? 312  VAL E C   1 
ATOM   13913 O  O   . VAL E  1 312 ? 7.348   -56.385 -41.368  1.00 168.75 ? 312  VAL E O   1 
ATOM   13914 C  CB  . VAL E  1 312 ? 9.799   -56.455 -43.197  1.00 218.27 ? 312  VAL E CB  1 
ATOM   13915 C  CG1 . VAL E  1 312 ? 10.703  -55.603 -44.078  1.00 214.30 ? 312  VAL E CG1 1 
ATOM   13916 C  CG2 . VAL E  1 312 ? 10.357  -57.863 -43.066  1.00 222.24 ? 312  VAL E CG2 1 
ATOM   13917 N  N   . GLY E  1 313 ? 8.860   -57.309 -40.000  1.00 174.49 ? 313  GLY E N   1 
ATOM   13918 C  CA  . GLY E  1 313 ? 7.860   -58.051 -39.263  1.00 178.65 ? 313  GLY E CA  1 
ATOM   13919 C  C   . GLY E  1 313 ? 7.513   -59.348 -39.964  1.00 176.58 ? 313  GLY E C   1 
ATOM   13920 O  O   . GLY E  1 313 ? 7.579   -59.425 -41.193  1.00 179.43 ? 313  GLY E O   1 
ATOM   13921 N  N   . GLN E  1 314 ? 7.117   -60.367 -39.204  1.00 183.04 ? 314  GLN E N   1 
ATOM   13922 C  CA  . GLN E  1 314 ? 6.815   -61.666 -39.788  1.00 188.85 ? 314  GLN E CA  1 
ATOM   13923 C  C   . GLN E  1 314 ? 5.674   -62.326 -39.028  1.00 185.71 ? 314  GLN E C   1 
ATOM   13924 O  O   . GLN E  1 314 ? 5.608   -62.253 -37.798  1.00 184.73 ? 314  GLN E O   1 
ATOM   13925 C  CB  . GLN E  1 314 ? 8.044   -62.583 -39.779  1.00 190.47 ? 314  GLN E CB  1 
ATOM   13926 C  CG  . GLN E  1 314 ? 7.850   -63.890 -40.532  1.00 179.81 ? 314  GLN E CG  1 
ATOM   13927 C  CD  . GLN E  1 314 ? 9.051   -64.805 -40.435  1.00 170.48 ? 314  GLN E CD  1 
ATOM   13928 O  OE1 . GLN E  1 314 ? 9.301   -65.411 -39.394  1.00 177.01 ? 314  GLN E OE1 1 
ATOM   13929 N  NE2 . GLN E  1 314 ? 9.796   -64.922 -41.527  1.00 173.76 ? 314  GLN E NE2 1 
ATOM   13930 N  N   . VAL E  1 315 ? 4.786   -62.977 -39.773  1.00 182.51 ? 315  VAL E N   1 
ATOM   13931 C  CA  . VAL E  1 315 ? 3.725   -63.801 -39.212  1.00 173.62 ? 315  VAL E CA  1 
ATOM   13932 C  C   . VAL E  1 315 ? 3.922   -65.232 -39.692  1.00 178.10 ? 315  VAL E C   1 
ATOM   13933 O  O   . VAL E  1 315 ? 4.048   -65.478 -40.898  1.00 177.08 ? 315  VAL E O   1 
ATOM   13934 C  CB  . VAL E  1 315 ? 2.336   -63.273 -39.607  1.00 174.27 ? 315  VAL E CB  1 
ATOM   13935 C  CG1 . VAL E  1 315 ? 1.259   -64.223 -39.132  1.00 181.48 ? 315  VAL E CG1 1 
ATOM   13936 C  CG2 . VAL E  1 315 ? 2.122   -61.881 -39.032  1.00 163.03 ? 315  VAL E CG2 1 
ATOM   13937 N  N   . SER E  1 316 ? 3.943   -66.172 -38.754  1.00 184.28 ? 316  SER E N   1 
ATOM   13938 C  CA  . SER E  1 316 ? 4.047   -67.589 -39.070  1.00 188.14 ? 316  SER E CA  1 
ATOM   13939 C  C   . SER E  1 316 ? 2.660   -68.218 -39.081  1.00 182.27 ? 316  SER E C   1 
ATOM   13940 O  O   . SER E  1 316 ? 1.861   -67.993 -38.166  1.00 177.48 ? 316  SER E O   1 
ATOM   13941 C  CB  . SER E  1 316 ? 4.950   -68.306 -38.066  1.00 185.78 ? 316  SER E CB  1 
ATOM   13942 O  OG  . SER E  1 316 ? 4.397   -68.270 -36.764  1.00 176.42 ? 316  SER E OG  1 
ATOM   13943 N  N   . VAL E  1 317 ? 2.386   -69.014 -40.109  1.00 187.91 ? 317  VAL E N   1 
ATOM   13944 C  CA  . VAL E  1 317 ? 1.102   -69.683 -40.276  1.00 199.55 ? 317  VAL E CA  1 
ATOM   13945 C  C   . VAL E  1 317 ? 1.307   -71.172 -40.033  1.00 207.90 ? 317  VAL E C   1 
ATOM   13946 O  O   . VAL E  1 317 ? 2.033   -71.837 -40.783  1.00 199.25 ? 317  VAL E O   1 
ATOM   13947 C  CB  . VAL E  1 317 ? 0.512   -69.422 -41.669  1.00 199.51 ? 317  VAL E CB  1 
ATOM   13948 C  CG1 . VAL E  1 317 ? -0.876  -70.016 -41.774  1.00 207.33 ? 317  VAL E CG1 1 
ATOM   13949 C  CG2 . VAL E  1 317 ? 0.493   -67.928 -41.953  1.00 192.55 ? 317  VAL E CG2 1 
ATOM   13950 N  N   . SER E  1 318 ? 0.674   -71.693 -38.982  1.00 210.10 ? 318  SER E N   1 
ATOM   13951 C  CA  . SER E  1 318 ? 0.817   -73.089 -38.573  1.00 208.13 ? 318  SER E CA  1 
ATOM   13952 C  C   . SER E  1 318 ? -0.528  -73.799 -38.701  1.00 212.92 ? 318  SER E C   1 
ATOM   13953 O  O   . SER E  1 318 ? -1.460  -73.516 -37.942  1.00 212.37 ? 318  SER E O   1 
ATOM   13954 C  CB  . SER E  1 318 ? 1.359   -73.174 -37.150  1.00 202.70 ? 318  SER E CB  1 
ATOM   13955 O  OG  . SER E  1 318 ? 2.602   -72.497 -37.055  1.00 196.48 ? 318  SER E OG  1 
ATOM   13956 N  N   . LEU E  1 319 ? -0.627  -74.713 -39.666  1.00 208.59 ? 319  LEU E N   1 
ATOM   13957 C  CA  . LEU E  1 319 ? -1.850  -75.469 -39.922  1.00 212.90 ? 319  LEU E CA  1 
ATOM   13958 C  C   . LEU E  1 319 ? -1.903  -76.713 -39.034  1.00 204.73 ? 319  LEU E C   1 
ATOM   13959 O  O   . LEU E  1 319 ? -1.010  -77.564 -39.094  1.00 210.87 ? 319  LEU E O   1 
ATOM   13960 C  CB  . LEU E  1 319 ? -1.945  -75.853 -41.400  1.00 224.97 ? 319  LEU E CB  1 
ATOM   13961 C  CG  . LEU E  1 319 ? -2.609  -74.868 -42.375  1.00 232.20 ? 319  LEU E CG  1 
ATOM   13962 C  CD1 . LEU E  1 319 ? -1.986  -73.480 -42.306  1.00 227.54 ? 319  LEU E CD1 1 
ATOM   13963 C  CD2 . LEU E  1 319 ? -2.551  -75.400 -43.800  1.00 244.93 ? 319  LEU E CD2 1 
ATOM   13964 N  N   . GLN E  1 320 ? -2.942  -76.803 -38.202  1.00 204.41 ? 320  GLN E N   1 
ATOM   13965 C  CA  . GLN E  1 320 ? -3.139  -77.950 -37.319  1.00 204.18 ? 320  GLN E CA  1 
ATOM   13966 C  C   . GLN E  1 320 ? -3.568  -79.193 -38.096  1.00 221.16 ? 320  GLN E C   1 
ATOM   13967 O  O   . GLN E  1 320 ? -4.378  -79.116 -39.025  1.00 229.60 ? 320  GLN E O   1 
ATOM   13968 C  CB  . GLN E  1 320 ? -4.194  -77.621 -36.264  1.00 209.98 ? 320  GLN E CB  1 
ATOM   13969 C  CG  . GLN E  1 320 ? -4.462  -78.739 -35.262  1.00 217.58 ? 320  GLN E CG  1 
ATOM   13970 C  CD  . GLN E  1 320 ? -5.637  -78.439 -34.348  1.00 221.72 ? 320  GLN E CD  1 
ATOM   13971 O  OE1 . GLN E  1 320 ? -6.084  -79.297 -33.587  1.00 216.68 ? 320  GLN E OE1 1 
ATOM   13972 N  NE2 . GLN E  1 320 ? -6.149  -77.218 -34.428  1.00 227.58 ? 320  GLN E NE2 1 
ATOM   13973 N  N   . ARG E  1 321 ? -3.025  -80.348 -37.702  1.00 241.77 ? 321  ARG E N   1 
ATOM   13974 C  CA  . ARG E  1 321 ? -3.404  -81.642 -38.258  1.00 247.56 ? 321  ARG E CA  1 
ATOM   13975 C  C   . ARG E  1 321 ? -3.865  -82.595 -37.159  1.00 233.32 ? 321  ARG E C   1 
ATOM   13976 O  O   . ARG E  1 321 ? -3.496  -82.451 -35.989  1.00 221.20 ? 321  ARG E O   1 
ATOM   13977 C  CB  . ARG E  1 321 ? -2.249  -82.269 -39.054  1.00 244.22 ? 321  ARG E CB  1 
ATOM   13978 C  CG  . ARG E  1 321 ? -1.662  -81.335 -40.098  1.00 242.32 ? 321  ARG E CG  1 
ATOM   13979 C  CD  . ARG E  1 321 ? -2.638  -81.186 -41.255  1.00 251.38 ? 321  ARG E CD  1 
ATOM   13980 N  NE  . ARG E  1 321 ? -2.122  -80.358 -42.342  1.00 255.49 ? 321  ARG E NE  1 
ATOM   13981 C  CZ  . ARG E  1 321 ? -2.779  -80.112 -43.474  1.00 245.39 ? 321  ARG E CZ  1 
ATOM   13982 N  NH1 . ARG E  1 321 ? -3.985  -80.628 -43.677  1.00 241.16 ? 321  ARG E NH1 1 
ATOM   13983 N  NH2 . ARG E  1 321 ? -2.233  -79.343 -44.405  1.00 239.44 ? 321  ARG E NH2 1 
ATOM   13984 N  N   . ALA E  1 322 ? -4.703  -83.561 -37.552  1.00 228.31 ? 322  ALA E N   1 
ATOM   13985 C  CA  . ALA E  1 322 ? -5.221  -84.542 -36.603  1.00 227.39 ? 322  ALA E CA  1 
ATOM   13986 C  C   . ALA E  1 322 ? -4.111  -85.415 -36.033  1.00 240.46 ? 322  ALA E C   1 
ATOM   13987 O  O   . ALA E  1 322 ? -4.248  -85.942 -34.924  1.00 247.84 ? 322  ALA E O   1 
ATOM   13988 C  CB  . ALA E  1 322 ? -6.289  -85.412 -37.268  1.00 226.23 ? 322  ALA E CB  1 
ATOM   13989 N  N   . SER E  1 323 ? -3.013  -85.591 -36.775  1.00 246.28 ? 323  SER E N   1 
ATOM   13990 C  CA  . SER E  1 323 ? -1.897  -86.404 -36.304  1.00 244.81 ? 323  SER E CA  1 
ATOM   13991 C  C   . SER E  1 323 ? -1.078  -85.712 -35.225  1.00 246.08 ? 323  SER E C   1 
ATOM   13992 O  O   . SER E  1 323 ? -0.092  -86.293 -34.757  1.00 247.24 ? 323  SER E O   1 
ATOM   13993 C  CB  . SER E  1 323 ? -0.986  -86.793 -37.472  1.00 239.02 ? 323  SER E CB  1 
ATOM   13994 O  OG  . SER E  1 323 ? -1.688  -87.552 -38.437  1.00 257.90 ? 323  SER E OG  1 
ATOM   13995 N  N   . GLY E  1 324 ? -1.449  -84.492 -34.834  1.00 247.00 ? 324  GLY E N   1 
ATOM   13996 C  CA  . GLY E  1 324 ? -0.795  -83.767 -33.772  1.00 244.94 ? 324  GLY E CA  1 
ATOM   13997 C  C   . GLY E  1 324 ? 0.246   -82.764 -34.230  1.00 248.00 ? 324  GLY E C   1 
ATOM   13998 O  O   . GLY E  1 324 ? 0.557   -81.832 -33.479  1.00 242.54 ? 324  GLY E O   1 
ATOM   13999 N  N   . ASP E  1 325 ? 0.791   -82.928 -35.435  1.00 254.84 ? 325  ASP E N   1 
ATOM   14000 C  CA  . ASP E  1 325 ? 1.844   -82.052 -35.929  1.00 246.28 ? 325  ASP E CA  1 
ATOM   14001 C  C   . ASP E  1 325 ? 1.277   -80.696 -36.352  1.00 252.44 ? 325  ASP E C   1 
ATOM   14002 O  O   . ASP E  1 325 ? 0.084   -80.411 -36.222  1.00 267.72 ? 325  ASP E O   1 
ATOM   14003 C  CB  . ASP E  1 325 ? 2.574   -82.714 -37.093  1.00 246.51 ? 325  ASP E CB  1 
ATOM   14004 C  CG  . ASP E  1 325 ? 2.966   -84.141 -36.791  1.00 256.51 ? 325  ASP E CG  1 
ATOM   14005 O  OD1 . ASP E  1 325 ? 4.029   -84.337 -36.163  1.00 268.46 ? 325  ASP E OD1 1 
ATOM   14006 O  OD2 . ASP E  1 325 ? 2.215   -85.064 -37.173  1.00 248.53 ? 325  ASP E OD2 1 
ATOM   14007 N  N   . PHE E  1 326 ? 2.165   -79.848 -36.870  1.00 243.40 ? 326  PHE E N   1 
ATOM   14008 C  CA  . PHE E  1 326 ? 1.798   -78.541 -37.401  1.00 243.58 ? 326  PHE E CA  1 
ATOM   14009 C  C   . PHE E  1 326 ? 2.568   -78.301 -38.690  1.00 243.38 ? 326  PHE E C   1 
ATOM   14010 O  O   . PHE E  1 326 ? 3.773   -78.560 -38.748  1.00 255.41 ? 326  PHE E O   1 
ATOM   14011 C  CB  . PHE E  1 326 ? 2.098   -77.421 -36.397  1.00 229.73 ? 326  PHE E CB  1 
ATOM   14012 C  CG  . PHE E  1 326 ? 1.131   -77.352 -35.247  1.00 232.14 ? 326  PHE E CG  1 
ATOM   14013 C  CD1 . PHE E  1 326 ? 1.321   -78.127 -34.114  1.00 229.74 ? 326  PHE E CD1 1 
ATOM   14014 C  CD2 . PHE E  1 326 ? 0.038   -76.502 -35.297  1.00 230.62 ? 326  PHE E CD2 1 
ATOM   14015 C  CE1 . PHE E  1 326 ? 0.433   -78.060 -33.054  1.00 225.01 ? 326  PHE E CE1 1 
ATOM   14016 C  CE2 . PHE E  1 326 ? -0.852  -76.431 -34.241  1.00 227.06 ? 326  PHE E CE2 1 
ATOM   14017 C  CZ  . PHE E  1 326 ? -0.654  -77.211 -33.118  1.00 222.38 ? 326  PHE E CZ  1 
ATOM   14018 N  N   . GLN E  1 327 ? 1.880   -77.806 -39.716  1.00 220.69 ? 327  GLN E N   1 
ATOM   14019 C  CA  . GLN E  1 327 ? 2.524   -77.365 -40.952  1.00 204.78 ? 327  GLN E CA  1 
ATOM   14020 C  C   . GLN E  1 327 ? 2.704   -75.854 -40.878  1.00 203.51 ? 327  GLN E C   1 
ATOM   14021 O  O   . GLN E  1 327 ? 1.746   -75.097 -41.046  1.00 204.85 ? 327  GLN E O   1 
ATOM   14022 C  CB  . GLN E  1 327 ? 1.706   -77.762 -42.174  1.00 209.57 ? 327  GLN E CB  1 
ATOM   14023 C  CG  . GLN E  1 327 ? 1.351   -79.232 -42.250  1.00 223.20 ? 327  GLN E CG  1 
ATOM   14024 C  CD  . GLN E  1 327 ? 0.835   -79.618 -43.623  1.00 245.77 ? 327  GLN E CD  1 
ATOM   14025 O  OE1 . GLN E  1 327 ? 0.215   -78.807 -44.312  1.00 247.63 ? 327  GLN E OE1 1 
ATOM   14026 N  NE2 . GLN E  1 327 ? 1.090   -80.857 -44.030  1.00 256.38 ? 327  GLN E NE2 1 
ATOM   14027 N  N   . THR E  1 328 ? 3.935   -75.412 -40.648  1.00 208.60 ? 328  THR E N   1 
ATOM   14028 C  CA  . THR E  1 328 ? 4.227   -74.005 -40.412  1.00 192.97 ? 328  THR E CA  1 
ATOM   14029 C  C   . THR E  1 328 ? 4.875   -73.385 -41.642  1.00 193.28 ? 328  THR E C   1 
ATOM   14030 O  O   . THR E  1 328 ? 5.837   -73.932 -42.190  1.00 214.60 ? 328  THR E O   1 
ATOM   14031 C  CB  . THR E  1 328 ? 5.144   -73.826 -39.199  1.00 187.56 ? 328  THR E CB  1 
ATOM   14032 O  OG1 . THR E  1 328 ? 4.541   -74.427 -38.046  1.00 194.41 ? 328  THR E OG1 1 
ATOM   14033 C  CG2 . THR E  1 328 ? 5.392   -72.350 -38.929  1.00 179.66 ? 328  THR E CG2 1 
ATOM   14034 N  N   . THR E  1 329 ? 4.343   -72.246 -42.068  1.00 180.12 ? 329  THR E N   1 
ATOM   14035 C  CA  . THR E  1 329 ? 4.974   -71.390 -43.058  1.00 190.76 ? 329  THR E CA  1 
ATOM   14036 C  C   . THR E  1 329 ? 5.136   -70.008 -42.440  1.00 187.00 ? 329  THR E C   1 
ATOM   14037 O  O   . THR E  1 329 ? 4.651   -69.739 -41.340  1.00 180.11 ? 329  THR E O   1 
ATOM   14038 C  CB  . THR E  1 329 ? 4.158   -71.333 -44.358  1.00 194.86 ? 329  THR E CB  1 
ATOM   14039 O  OG1 . THR E  1 329 ? 4.671   -70.299 -45.206  1.00 201.10 ? 329  THR E OG1 1 
ATOM   14040 C  CG2 . THR E  1 329 ? 2.690   -71.068 -44.068  1.00 195.29 ? 329  THR E CG2 1 
ATOM   14041 N  N   . LYS E  1 330 ? 5.824   -69.120 -43.147  1.00 192.65 ? 330  LYS E N   1 
ATOM   14042 C  CA  . LYS E  1 330 ? 6.116   -67.796 -42.619  1.00 180.25 ? 330  LYS E CA  1 
ATOM   14043 C  C   . LYS E  1 330 ? 5.783   -66.741 -43.658  1.00 184.25 ? 330  LYS E C   1 
ATOM   14044 O  O   . LYS E  1 330 ? 6.077   -66.907 -44.845  1.00 197.94 ? 330  LYS E O   1 
ATOM   14045 C  CB  . LYS E  1 330 ? 7.584   -67.676 -42.197  1.00 175.29 ? 330  LYS E CB  1 
ATOM   14046 C  CG  . LYS E  1 330 ? 7.890   -68.302 -40.843  1.00 188.18 ? 330  LYS E CG  1 
ATOM   14047 C  CD  . LYS E  1 330 ? 9.389   -68.382 -40.585  1.00 209.10 ? 330  LYS E CD  1 
ATOM   14048 C  CE  . LYS E  1 330 ? 9.682   -68.873 -39.172  1.00 205.75 ? 330  LYS E CE  1 
ATOM   14049 N  NZ  . LYS E  1 330 ? 8.941   -70.126 -38.851  1.00 205.27 ? 330  LYS E NZ  1 
ATOM   14050 N  N   . LEU E  1 331 ? 5.159   -65.658 -43.204  1.00 177.50 ? 331  LEU E N   1 
ATOM   14051 C  CA  . LEU E  1 331 ? 4.721   -64.570 -44.072  1.00 177.89 ? 331  LEU E CA  1 
ATOM   14052 C  C   . LEU E  1 331 ? 5.441   -63.295 -43.651  1.00 172.22 ? 331  LEU E C   1 
ATOM   14053 O  O   . LEU E  1 331 ? 5.241   -62.801 -42.536  1.00 166.69 ? 331  LEU E O   1 
ATOM   14054 C  CB  . LEU E  1 331 ? 3.204   -64.399 -44.004  1.00 182.67 ? 331  LEU E CB  1 
ATOM   14055 C  CG  . LEU E  1 331 ? 2.585   -63.440 -45.022  1.00 193.64 ? 331  LEU E CG  1 
ATOM   14056 C  CD1 . LEU E  1 331 ? 2.891   -63.904 -46.437  1.00 191.92 ? 331  LEU E CD1 1 
ATOM   14057 C  CD2 . LEU E  1 331 ? 1.083   -63.321 -44.806  1.00 200.60 ? 331  LEU E CD2 1 
ATOM   14058 N  N   . ASN E  1 332 ? 6.278   -62.767 -44.536  1.00 182.10 ? 332  ASN E N   1 
ATOM   14059 C  CA  . ASN E  1 332 ? 7.039   -61.563 -44.246  1.00 179.25 ? 332  ASN E CA  1 
ATOM   14060 C  C   . ASN E  1 332 ? 6.245   -60.322 -44.631  1.00 184.59 ? 332  ASN E C   1 
ATOM   14061 O  O   . ASN E  1 332 ? 5.460   -60.333 -45.582  1.00 194.02 ? 332  ASN E O   1 
ATOM   14062 C  CB  . ASN E  1 332 ? 8.377   -61.578 -44.991  1.00 181.86 ? 332  ASN E CB  1 
ATOM   14063 C  CG  . ASN E  1 332 ? 9.385   -62.527 -44.365  1.00 183.56 ? 332  ASN E CG  1 
ATOM   14064 O  OD1 . ASN E  1 332 ? 9.038   -63.352 -43.520  1.00 192.40 ? 332  ASN E OD1 1 
ATOM   14065 N  ND2 . ASN E  1 332 ? 10.643  -62.409 -44.776  1.00 185.95 ? 332  ASN E ND2 1 
ATOM   14066 N  N   . GLY E  1 333 ? 6.457   -59.247 -43.876  1.00 190.39 ? 333  GLY E N   1 
ATOM   14067 C  CA  . GLY E  1 333 ? 5.823   -57.980 -44.175  1.00 189.19 ? 333  GLY E CA  1 
ATOM   14068 C  C   . GLY E  1 333 ? 6.383   -57.336 -45.432  1.00 200.44 ? 333  GLY E C   1 
ATOM   14069 O  O   . GLY E  1 333 ? 7.361   -57.790 -46.027  1.00 213.65 ? 333  GLY E O   1 
ATOM   14070 N  N   . PHE E  1 334 ? 5.732   -56.243 -45.843  1.00 200.79 ? 334  PHE E N   1 
ATOM   14071 C  CA  . PHE E  1 334 ? 6.050   -55.559 -47.093  1.00 202.04 ? 334  PHE E CA  1 
ATOM   14072 C  C   . PHE E  1 334 ? 6.775   -54.236 -46.913  1.00 191.31 ? 334  PHE E C   1 
ATOM   14073 O  O   . PHE E  1 334 ? 7.523   -53.834 -47.808  1.00 186.54 ? 334  PHE E O   1 
ATOM   14074 C  CB  . PHE E  1 334 ? 4.772   -55.297 -47.906  1.00 210.45 ? 334  PHE E CB  1 
ATOM   14075 C  CG  . PHE E  1 334 ? 3.907   -56.512 -48.090  1.00 222.52 ? 334  PHE E CG  1 
ATOM   14076 C  CD1 . PHE E  1 334 ? 4.084   -57.350 -49.180  1.00 216.51 ? 334  PHE E CD1 1 
ATOM   14077 C  CD2 . PHE E  1 334 ? 2.912   -56.814 -47.173  1.00 229.93 ? 334  PHE E CD2 1 
ATOM   14078 C  CE1 . PHE E  1 334 ? 3.287   -58.470 -49.351  1.00 211.29 ? 334  PHE E CE1 1 
ATOM   14079 C  CE2 . PHE E  1 334 ? 2.113   -57.932 -47.338  1.00 222.69 ? 334  PHE E CE2 1 
ATOM   14080 C  CZ  . PHE E  1 334 ? 2.301   -58.761 -48.430  1.00 212.76 ? 334  PHE E CZ  1 
ATOM   14081 N  N   . GLU E  1 335 ? 6.558   -53.536 -45.802  1.00 185.22 ? 335  GLU E N   1 
ATOM   14082 C  CA  . GLU E  1 335 ? 7.139   -52.220 -45.582  1.00 189.25 ? 335  GLU E CA  1 
ATOM   14083 C  C   . GLU E  1 335 ? 8.084   -52.226 -44.384  1.00 176.95 ? 335  GLU E C   1 
ATOM   14084 O  O   . GLU E  1 335 ? 7.786   -52.824 -43.344  1.00 172.18 ? 335  GLU E O   1 
ATOM   14085 C  CB  . GLU E  1 335 ? 6.038   -51.175 -45.392  1.00 196.52 ? 335  GLU E CB  1 
ATOM   14086 C  CG  . GLU E  1 335 ? 5.401   -50.728 -46.700  1.00 180.09 ? 335  GLU E CG  1 
ATOM   14087 C  CD  . GLU E  1 335 ? 4.636   -49.432 -46.557  1.00 179.17 ? 335  GLU E CD  1 
ATOM   14088 O  OE1 . GLU E  1 335 ? 3.604   -49.276 -47.242  1.00 184.98 ? 335  GLU E OE1 1 
ATOM   14089 O  OE2 . GLU E  1 335 ? 5.062   -48.577 -45.751  1.00 178.08 ? 335  GLU E OE2 1 
ATOM   14090 N  N   . VAL E  1 336 ? 9.216   -51.528 -44.536  1.00 178.84 ? 336  VAL E N   1 
ATOM   14091 C  CA  . VAL E  1 336 ? 10.210  -51.410 -43.472  1.00 178.87 ? 336  VAL E CA  1 
ATOM   14092 C  C   . VAL E  1 336 ? 9.653   -50.586 -42.315  1.00 206.86 ? 336  VAL E C   1 
ATOM   14093 O  O   . VAL E  1 336 ? 8.994   -49.557 -42.520  1.00 221.15 ? 336  VAL E O   1 
ATOM   14094 C  CB  . VAL E  1 336 ? 11.505  -50.789 -44.026  1.00 183.73 ? 336  VAL E CB  1 
ATOM   14095 C  CG1 . VAL E  1 336 ? 12.664  -51.022 -43.072  1.00 184.47 ? 336  VAL E CG1 1 
ATOM   14096 C  CG2 . VAL E  1 336 ? 11.819  -51.364 -45.395  1.00 186.99 ? 336  VAL E CG2 1 
ATOM   14097 N  N   . PHE E  1 337 ? 9.893   -51.056 -41.089  1.00 219.71 ? 337  PHE E N   1 
ATOM   14098 C  CA  . PHE E  1 337 ? 9.498   -50.394 -39.846  1.00 213.84 ? 337  PHE E CA  1 
ATOM   14099 C  C   . PHE E  1 337 ? 7.988   -50.287 -39.687  1.00 196.91 ? 337  PHE E C   1 
ATOM   14100 O  O   . PHE E  1 337 ? 7.511   -49.615 -38.762  1.00 189.49 ? 337  PHE E O   1 
ATOM   14101 C  CB  . PHE E  1 337 ? 10.132  -49.001 -39.714  1.00 214.02 ? 337  PHE E CB  1 
ATOM   14102 C  CG  . PHE E  1 337 ? 11.633  -49.023 -39.642  1.00 215.07 ? 337  PHE E CG  1 
ATOM   14103 C  CD1 . PHE E  1 337 ? 12.302  -50.150 -39.195  1.00 212.33 ? 337  PHE E CD1 1 
ATOM   14104 C  CD2 . PHE E  1 337 ? 12.374  -47.914 -40.016  1.00 220.21 ? 337  PHE E CD2 1 
ATOM   14105 C  CE1 . PHE E  1 337 ? 13.681  -50.174 -39.127  1.00 209.71 ? 337  PHE E CE1 1 
ATOM   14106 C  CE2 . PHE E  1 337 ? 13.756  -47.931 -39.949  1.00 218.23 ? 337  PHE E CE2 1 
ATOM   14107 C  CZ  . PHE E  1 337 ? 14.409  -49.063 -39.504  1.00 213.22 ? 337  PHE E CZ  1 
ATOM   14108 N  N   . ALA E  1 338 ? 7.219   -50.936 -40.561  1.00 186.77 ? 338  ALA E N   1 
ATOM   14109 C  CA  . ALA E  1 338 ? 5.769   -50.896 -40.471  1.00 193.00 ? 338  ALA E CA  1 
ATOM   14110 C  C   . ALA E  1 338 ? 5.244   -51.776 -39.354  1.00 187.85 ? 338  ALA E C   1 
ATOM   14111 O  O   . ALA E  1 338 ? 4.082   -51.628 -38.958  1.00 191.22 ? 338  ALA E O   1 
ATOM   14112 C  CB  . ALA E  1 338 ? 5.147   -51.337 -41.798  1.00 199.51 ? 338  ALA E CB  1 
ATOM   14113 N  N   . ARG E  1 339 ? 6.075   -52.687 -38.854  1.00 187.07 ? 339  ARG E N   1 
ATOM   14114 C  CA  . ARG E  1 339 ? 5.684   -53.625 -37.812  1.00 182.93 ? 339  ARG E CA  1 
ATOM   14115 C  C   . ARG E  1 339 ? 4.482   -54.449 -38.267  1.00 183.12 ? 339  ARG E C   1 
ATOM   14116 O  O   . ARG E  1 339 ? 3.470   -54.562 -37.572  1.00 181.44 ? 339  ARG E O   1 
ATOM   14117 C  CB  . ARG E  1 339 ? 5.417   -52.905 -36.491  1.00 180.06 ? 339  ARG E CB  1 
ATOM   14118 C  CG  . ARG E  1 339 ? 6.661   -52.239 -35.933  1.00 181.81 ? 339  ARG E CG  1 
ATOM   14119 C  CD  . ARG E  1 339 ? 6.441   -51.745 -34.523  1.00 189.99 ? 339  ARG E CD  1 
ATOM   14120 N  NE  . ARG E  1 339 ? 7.580   -50.979 -34.029  1.00 203.84 ? 339  ARG E NE  1 
ATOM   14121 C  CZ  . ARG E  1 339 ? 7.659   -50.472 -32.803  1.00 201.88 ? 339  ARG E CZ  1 
ATOM   14122 N  NH1 . ARG E  1 339 ? 6.663   -50.653 -31.945  1.00 191.43 ? 339  ARG E NH1 1 
ATOM   14123 N  NH2 . ARG E  1 339 ? 8.731   -49.784 -32.433  1.00 199.72 ? 339  ARG E NH2 1 
ATOM   14124 N  N   . PHE E  1 340 ? 4.605   -55.006 -39.472  1.00 178.43 ? 340  PHE E N   1 
ATOM   14125 C  CA  . PHE E  1 340 ? 3.657   -55.988 -39.977  1.00 182.26 ? 340  PHE E CA  1 
ATOM   14126 C  C   . PHE E  1 340 ? 3.506   -57.124 -38.974  1.00 177.39 ? 340  PHE E C   1 
ATOM   14127 O  O   . PHE E  1 340 ? 4.494   -57.718 -38.537  1.00 188.18 ? 340  PHE E O   1 
ATOM   14128 C  CB  . PHE E  1 340 ? 4.153   -56.510 -41.333  1.00 188.67 ? 340  PHE E CB  1 
ATOM   14129 C  CG  . PHE E  1 340 ? 3.289   -57.582 -41.948  1.00 194.46 ? 340  PHE E CG  1 
ATOM   14130 C  CD1 . PHE E  1 340 ? 2.231   -57.247 -42.779  1.00 187.36 ? 340  PHE E CD1 1 
ATOM   14131 C  CD2 . PHE E  1 340 ? 3.561   -58.925 -41.726  1.00 196.52 ? 340  PHE E CD2 1 
ATOM   14132 C  CE1 . PHE E  1 340 ? 1.444   -58.230 -43.351  1.00 191.19 ? 340  PHE E CE1 1 
ATOM   14133 C  CE2 . PHE E  1 340 ? 2.778   -59.911 -42.296  1.00 193.56 ? 340  PHE E CE2 1 
ATOM   14134 C  CZ  . PHE E  1 340 ? 1.719   -59.563 -43.110  1.00 194.08 ? 340  PHE E CZ  1 
ATOM   14135 N  N   . GLY E  1 341 ? 2.264   -57.431 -38.618  1.00 169.94 ? 341  GLY E N   1 
ATOM   14136 C  CA  . GLY E  1 341 ? 1.983   -58.452 -37.632  1.00 164.98 ? 341  GLY E CA  1 
ATOM   14137 C  C   . GLY E  1 341 ? 1.655   -57.946 -36.245  1.00 169.18 ? 341  GLY E C   1 
ATOM   14138 O  O   . GLY E  1 341 ? 1.562   -58.758 -35.318  1.00 171.75 ? 341  GLY E O   1 
ATOM   14139 N  N   . SER E  1 342 ? 1.499   -56.633 -36.067  1.00 180.44 ? 342  SER E N   1 
ATOM   14140 C  CA  . SER E  1 342 ? 1.174   -56.097 -34.750  1.00 178.91 ? 342  SER E CA  1 
ATOM   14141 C  C   . SER E  1 342 ? -0.219  -56.514 -34.293  1.00 179.68 ? 342  SER E C   1 
ATOM   14142 O  O   . SER E  1 342 ? -0.440  -56.714 -33.094  1.00 180.79 ? 342  SER E O   1 
ATOM   14143 C  CB  . SER E  1 342 ? 1.301   -54.575 -34.763  1.00 180.87 ? 342  SER E CB  1 
ATOM   14144 O  OG  . SER E  1 342 ? 2.635   -54.183 -35.037  1.00 182.82 ? 342  SER E OG  1 
ATOM   14145 N  N   . ALA E  1 343 ? -1.167  -56.645 -35.220  1.00 179.78 ? 343  ALA E N   1 
ATOM   14146 C  CA  . ALA E  1 343 ? -2.516  -57.088 -34.894  1.00 175.65 ? 343  ALA E CA  1 
ATOM   14147 C  C   . ALA E  1 343 ? -2.985  -58.098 -35.931  1.00 164.38 ? 343  ALA E C   1 
ATOM   14148 O  O   . ALA E  1 343 ? -2.756  -57.924 -37.133  1.00 158.94 ? 343  ALA E O   1 
ATOM   14149 C  CB  . ALA E  1 343 ? -3.498  -55.912 -34.826  1.00 173.41 ? 343  ALA E CB  1 
ATOM   14150 N  N   . ILE E  1 344 ? -3.646  -59.152 -35.457  1.00 164.84 ? 344  ILE E N   1 
ATOM   14151 C  CA  . ILE E  1 344 ? -4.141  -60.238 -36.295  1.00 159.83 ? 344  ILE E CA  1 
ATOM   14152 C  C   . ILE E  1 344 ? -5.591  -60.488 -35.900  1.00 185.31 ? 344  ILE E C   1 
ATOM   14153 O  O   . ILE E  1 344 ? -5.865  -60.902 -34.766  1.00 200.50 ? 344  ILE E O   1 
ATOM   14154 C  CB  . ILE E  1 344 ? -3.306  -61.516 -36.143  1.00 157.75 ? 344  ILE E CB  1 
ATOM   14155 C  CG1 . ILE E  1 344 ? -1.813  -61.217 -36.320  1.00 155.94 ? 344  ILE E CG1 1 
ATOM   14156 C  CG2 . ILE E  1 344 ? -3.773  -62.572 -37.127  1.00 164.93 ? 344  ILE E CG2 1 
ATOM   14157 C  CD1 . ILE E  1 344 ? -0.907  -62.400 -36.036  1.00 158.33 ? 344  ILE E CD1 1 
ATOM   14158 N  N   . ALA E  1 345 ? -6.516  -60.215 -36.812  1.00 188.93 ? 345  ALA E N   1 
ATOM   14159 C  CA  . ALA E  1 345 ? -7.943  -60.377 -36.535  1.00 179.18 ? 345  ALA E CA  1 
ATOM   14160 C  C   . ALA E  1 345 ? -8.541  -61.412 -37.473  1.00 182.69 ? 345  ALA E C   1 
ATOM   14161 O  O   . ALA E  1 345 ? -8.566  -61.188 -38.698  1.00 184.64 ? 345  ALA E O   1 
ATOM   14162 C  CB  . ALA E  1 345 ? -8.682  -59.046 -36.677  1.00 176.24 ? 345  ALA E CB  1 
ATOM   14163 N  N   . PRO E  1 346 ? -9.004  -62.555 -36.969  1.00 203.42 ? 346  PRO E N   1 
ATOM   14164 C  CA  . PRO E  1 346 ? -9.755  -63.483 -37.823  1.00 209.71 ? 346  PRO E CA  1 
ATOM   14165 C  C   . PRO E  1 346 ? -11.021 -62.816 -38.338  1.00 216.41 ? 346  PRO E C   1 
ATOM   14166 O  O   . PRO E  1 346 ? -11.761 -62.183 -37.581  1.00 226.52 ? 346  PRO E O   1 
ATOM   14167 C  CB  . PRO E  1 346 ? -10.069 -64.656 -36.888  1.00 224.72 ? 346  PRO E CB  1 
ATOM   14168 C  CG  . PRO E  1 346 ? -9.080  -64.542 -35.772  1.00 231.20 ? 346  PRO E CG  1 
ATOM   14169 C  CD  . PRO E  1 346 ? -8.846  -63.068 -35.600  1.00 218.62 ? 346  PRO E CD  1 
ATOM   14170 N  N   . LEU E  1 347 ? -11.260 -62.950 -39.640  1.00 207.62 ? 347  LEU E N   1 
ATOM   14171 C  CA  . LEU E  1 347 ? -12.354 -62.257 -40.306  1.00 208.01 ? 347  LEU E CA  1 
ATOM   14172 C  C   . LEU E  1 347 ? -13.553 -63.151 -40.582  1.00 208.11 ? 347  LEU E C   1 
ATOM   14173 O  O   . LEU E  1 347 ? -14.563 -62.666 -41.105  1.00 210.80 ? 347  LEU E O   1 
ATOM   14174 C  CB  . LEU E  1 347 ? -11.859 -61.652 -41.621  1.00 202.81 ? 347  LEU E CB  1 
ATOM   14175 C  CG  . LEU E  1 347 ? -10.616 -60.771 -41.504  1.00 198.72 ? 347  LEU E CG  1 
ATOM   14176 C  CD1 . LEU E  1 347 ? -10.191 -60.255 -42.869  1.00 203.71 ? 347  LEU E CD1 1 
ATOM   14177 C  CD2 . LEU E  1 347 ? -10.865 -59.623 -40.543  1.00 201.69 ? 347  LEU E CD2 1 
ATOM   14178 N  N   . GLY E  1 348 ? -13.475 -64.437 -40.245  1.00 205.21 ? 348  GLY E N   1 
ATOM   14179 C  CA  . GLY E  1 348 ? -14.497 -65.333 -40.734  1.00 214.46 ? 348  GLY E CA  1 
ATOM   14180 C  C   . GLY E  1 348 ? -14.264 -65.583 -42.211  1.00 217.73 ? 348  GLY E C   1 
ATOM   14181 O  O   . GLY E  1 348 ? -13.133 -65.545 -42.703  1.00 221.63 ? 348  GLY E O   1 
ATOM   14182 N  N   . ASP E  1 349 ? -15.349 -65.837 -42.936  1.00 207.79 ? 349  ASP E N   1 
ATOM   14183 C  CA  . ASP E  1 349 ? -15.278 -65.993 -44.388  1.00 207.53 ? 349  ASP E CA  1 
ATOM   14184 C  C   . ASP E  1 349 ? -15.706 -64.659 -44.993  1.00 202.75 ? 349  ASP E C   1 
ATOM   14185 O  O   . ASP E  1 349 ? -16.873 -64.455 -45.328  1.00 203.71 ? 349  ASP E O   1 
ATOM   14186 C  CB  . ASP E  1 349 ? -16.147 -67.146 -44.866  1.00 214.78 ? 349  ASP E CB  1 
ATOM   14187 C  CG  . ASP E  1 349 ? -15.733 -67.648 -46.231  1.00 224.87 ? 349  ASP E CG  1 
ATOM   14188 O  OD1 . ASP E  1 349 ? -14.978 -66.932 -46.925  1.00 232.05 ? 349  ASP E OD1 1 
ATOM   14189 O  OD2 . ASP E  1 349 ? -16.157 -68.760 -46.605  1.00 232.02 ? 349  ASP E OD2 1 
ATOM   14190 N  N   . LEU E  1 350 ? -14.738 -63.744 -45.124  1.00 203.05 ? 350  LEU E N   1 
ATOM   14191 C  CA  . LEU E  1 350 ? -15.027 -62.380 -45.562  1.00 198.82 ? 350  LEU E CA  1 
ATOM   14192 C  C   . LEU E  1 350 ? -15.774 -62.336 -46.886  1.00 200.45 ? 350  LEU E C   1 
ATOM   14193 O  O   . LEU E  1 350 ? -16.623 -61.461 -47.091  1.00 206.53 ? 350  LEU E O   1 
ATOM   14194 C  CB  . LEU E  1 350 ? -13.726 -61.585 -45.684  1.00 194.31 ? 350  LEU E CB  1 
ATOM   14195 C  CG  . LEU E  1 350 ? -13.888 -60.106 -46.048  1.00 190.21 ? 350  LEU E CG  1 
ATOM   14196 C  CD1 . LEU E  1 350 ? -14.668 -59.360 -44.978  1.00 198.45 ? 350  LEU E CD1 1 
ATOM   14197 C  CD2 . LEU E  1 350 ? -12.544 -59.449 -46.289  1.00 186.70 ? 350  LEU E CD2 1 
ATOM   14198 N  N   . ASP E  1 351 ? -15.484 -63.266 -47.790  1.00 203.03 ? 351  ASP E N   1 
ATOM   14199 C  CA  . ASP E  1 351 ? -16.070 -63.258 -49.121  1.00 215.08 ? 351  ASP E CA  1 
ATOM   14200 C  C   . ASP E  1 351 ? -16.996 -64.443 -49.364  1.00 214.70 ? 351  ASP E C   1 
ATOM   14201 O  O   . ASP E  1 351 ? -17.505 -64.602 -50.480  1.00 220.05 ? 351  ASP E O   1 
ATOM   14202 C  CB  . ASP E  1 351 ? -14.956 -63.196 -50.171  1.00 228.33 ? 351  ASP E CB  1 
ATOM   14203 C  CG  . ASP E  1 351 ? -13.855 -64.210 -49.921  1.00 234.50 ? 351  ASP E CG  1 
ATOM   14204 O  OD1 . ASP E  1 351 ? -13.483 -64.411 -48.743  1.00 240.24 ? 351  ASP E OD1 1 
ATOM   14205 O  OD2 . ASP E  1 351 ? -13.336 -64.779 -50.905  1.00 238.92 ? 351  ASP E OD2 1 
ATOM   14206 N  N   . GLN E  1 352 ? -17.258 -65.249 -48.334  1.00 210.92 ? 352  GLN E N   1 
ATOM   14207 C  CA  . GLN E  1 352 ? -18.193 -66.372 -48.410  1.00 219.82 ? 352  GLN E CA  1 
ATOM   14208 C  C   . GLN E  1 352 ? -17.831 -67.329 -49.543  1.00 241.33 ? 352  GLN E C   1 
ATOM   14209 O  O   . GLN E  1 352 ? -18.656 -67.667 -50.395  1.00 248.24 ? 352  GLN E O   1 
ATOM   14210 C  CB  . GLN E  1 352 ? -19.632 -65.874 -48.549  1.00 216.54 ? 352  GLN E CB  1 
ATOM   14211 C  CG  . GLN E  1 352 ? -20.172 -65.119 -47.338  1.00 213.97 ? 352  GLN E CG  1 
ATOM   14212 C  CD  . GLN E  1 352 ? -20.290 -65.975 -46.085  1.00 213.79 ? 352  GLN E CD  1 
ATOM   14213 O  OE1 . GLN E  1 352 ? -19.299 -66.483 -45.557  1.00 217.58 ? 352  GLN E OE1 1 
ATOM   14214 N  NE2 . GLN E  1 352 ? -21.516 -66.145 -45.608  1.00 215.52 ? 352  GLN E NE2 1 
ATOM   14215 N  N   . ASP E  1 353 ? -16.574 -67.772 -49.545  1.00 250.52 ? 353  ASP E N   1 
ATOM   14216 C  CA  . ASP E  1 353 ? -16.083 -68.733 -50.524  1.00 252.23 ? 353  ASP E CA  1 
ATOM   14217 C  C   . ASP E  1 353 ? -15.924 -70.137 -49.950  1.00 248.33 ? 353  ASP E C   1 
ATOM   14218 O  O   . ASP E  1 353 ? -15.518 -71.049 -50.677  1.00 254.59 ? 353  ASP E O   1 
ATOM   14219 C  CB  . ASP E  1 353 ? -14.741 -68.260 -51.106  1.00 254.23 ? 353  ASP E CB  1 
ATOM   14220 C  CG  . ASP E  1 353 ? -13.661 -68.038 -50.031  1.00 253.69 ? 353  ASP E CG  1 
ATOM   14221 O  OD1 . ASP E  1 353 ? -13.807 -68.529 -48.892  1.00 252.16 ? 353  ASP E OD1 1 
ATOM   14222 O  OD2 . ASP E  1 353 ? -12.646 -67.371 -50.327  1.00 251.16 ? 353  ASP E OD2 1 
ATOM   14223 N  N   . GLY E  1 354 ? -16.235 -70.333 -48.672  1.00 245.19 ? 354  GLY E N   1 
ATOM   14224 C  CA  . GLY E  1 354 ? -16.095 -71.623 -48.034  1.00 249.29 ? 354  GLY E CA  1 
ATOM   14225 C  C   . GLY E  1 354 ? -14.834 -71.775 -47.218  1.00 244.41 ? 354  GLY E C   1 
ATOM   14226 O  O   . GLY E  1 354 ? -14.638 -72.827 -46.596  1.00 248.23 ? 354  GLY E O   1 
ATOM   14227 N  N   . PHE E  1 355 ? -13.972 -70.763 -47.200  1.00 236.26 ? 355  PHE E N   1 
ATOM   14228 C  CA  . PHE E  1 355 ? -12.728 -70.801 -46.449  1.00 230.49 ? 355  PHE E CA  1 
ATOM   14229 C  C   . PHE E  1 355 ? -12.576 -69.502 -45.678  1.00 225.98 ? 355  PHE E C   1 
ATOM   14230 O  O   . PHE E  1 355 ? -12.764 -68.416 -46.236  1.00 222.56 ? 355  PHE E O   1 
ATOM   14231 C  CB  . PHE E  1 355 ? -11.527 -71.017 -47.370  1.00 240.49 ? 355  PHE E CB  1 
ATOM   14232 C  CG  . PHE E  1 355 ? -11.561 -72.323 -48.100  1.00 244.82 ? 355  PHE E CG  1 
ATOM   14233 C  CD1 . PHE E  1 355 ? -11.275 -73.507 -47.443  1.00 250.47 ? 355  PHE E CD1 1 
ATOM   14234 C  CD2 . PHE E  1 355 ? -11.898 -72.369 -49.440  1.00 242.69 ? 355  PHE E CD2 1 
ATOM   14235 C  CE1 . PHE E  1 355 ? -11.312 -74.711 -48.113  1.00 253.36 ? 355  PHE E CE1 1 
ATOM   14236 C  CE2 . PHE E  1 355 ? -11.938 -73.569 -50.116  1.00 247.61 ? 355  PHE E CE2 1 
ATOM   14237 C  CZ  . PHE E  1 355 ? -11.644 -74.743 -49.453  1.00 251.83 ? 355  PHE E CZ  1 
ATOM   14238 N  N   . ASN E  1 356 ? -12.256 -69.620 -44.394  1.00 220.34 ? 356  ASN E N   1 
ATOM   14239 C  CA  . ASN E  1 356 ? -12.078 -68.440 -43.563  1.00 217.76 ? 356  ASN E CA  1 
ATOM   14240 C  C   . ASN E  1 356 ? -10.903 -67.601 -44.050  1.00 218.20 ? 356  ASN E C   1 
ATOM   14241 O  O   . ASN E  1 356 ? -9.973  -68.098 -44.693  1.00 220.27 ? 356  ASN E O   1 
ATOM   14242 C  CB  . ASN E  1 356 ? -11.867 -68.841 -42.108  1.00 217.73 ? 356  ASN E CB  1 
ATOM   14243 C  CG  . ASN E  1 356 ? -13.141 -69.315 -41.455  1.00 234.24 ? 356  ASN E CG  1 
ATOM   14244 O  OD1 . ASN E  1 356 ? -14.234 -68.881 -41.816  1.00 249.33 ? 356  ASN E OD1 1 
ATOM   14245 N  ND2 . ASN E  1 356 ? -13.012 -70.218 -40.494  1.00 232.67 ? 356  ASN E ND2 1 
ATOM   14246 N  N   . ASP E  1 357 ? -10.973 -66.308 -43.759  1.00 215.95 ? 357  ASP E N   1 
ATOM   14247 C  CA  . ASP E  1 357 ? -9.978  -65.331 -44.168  1.00 214.93 ? 357  ASP E CA  1 
ATOM   14248 C  C   . ASP E  1 357 ? -9.466  -64.598 -42.933  1.00 200.52 ? 357  ASP E C   1 
ATOM   14249 O  O   . ASP E  1 357 ? -10.020 -64.723 -41.836  1.00 197.30 ? 357  ASP E O   1 
ATOM   14250 C  CB  . ASP E  1 357 ? -10.570 -64.360 -45.194  1.00 225.58 ? 357  ASP E CB  1 
ATOM   14251 C  CG  . ASP E  1 357 ? -11.313 -65.080 -46.306  1.00 226.76 ? 357  ASP E CG  1 
ATOM   14252 O  OD1 . ASP E  1 357 ? -10.762 -66.057 -46.861  1.00 221.95 ? 357  ASP E OD1 1 
ATOM   14253 O  OD2 . ASP E  1 357 ? -12.456 -64.683 -46.615  1.00 232.43 ? 357  ASP E OD2 1 
ATOM   14254 N  N   . ILE E  1 358 ? -8.389  -63.832 -43.107  1.00 195.92 ? 358  ILE E N   1 
ATOM   14255 C  CA  . ILE E  1 358 ? -7.742  -63.176 -41.976  1.00 189.40 ? 358  ILE E CA  1 
ATOM   14256 C  C   . ILE E  1 358 ? -7.147  -61.848 -42.426  1.00 183.58 ? 358  ILE E C   1 
ATOM   14257 O  O   . ILE E  1 358 ? -6.810  -61.660 -43.598  1.00 186.11 ? 358  ILE E O   1 
ATOM   14258 C  CB  . ILE E  1 358 ? -6.676  -64.101 -41.343  1.00 189.39 ? 358  ILE E CB  1 
ATOM   14259 C  CG1 . ILE E  1 358 ? -6.437  -63.714 -39.882  1.00 198.84 ? 358  ILE E CG1 1 
ATOM   14260 C  CG2 . ILE E  1 358 ? -5.387  -64.075 -42.153  1.00 188.36 ? 358  ILE E CG2 1 
ATOM   14261 C  CD1 . ILE E  1 358 ? -6.031  -64.873 -38.999  1.00 196.00 ? 358  ILE E CD1 1 
ATOM   14262 N  N   . ALA E  1 359 ? -7.069  -60.904 -41.489  1.00 174.08 ? 359  ALA E N   1 
ATOM   14263 C  CA  . ALA E  1 359 ? -6.428  -59.613 -41.704  1.00 169.69 ? 359  ALA E CA  1 
ATOM   14264 C  C   . ALA E  1 359 ? -5.189  -59.474 -40.822  1.00 176.31 ? 359  ALA E C   1 
ATOM   14265 O  O   . ALA E  1 359 ? -5.192  -59.887 -39.657  1.00 172.01 ? 359  ALA E O   1 
ATOM   14266 C  CB  . ALA E  1 359 ? -7.400  -58.463 -41.429  1.00 167.23 ? 359  ALA E CB  1 
ATOM   14267 N  N   . ILE E  1 360 ? -4.130  -58.886 -41.383  1.00 184.47 ? 360  ILE E N   1 
ATOM   14268 C  CA  . ILE E  1 360 ? -2.897  -58.588 -40.657  1.00 173.68 ? 360  ILE E CA  1 
ATOM   14269 C  C   . ILE E  1 360 ? -2.544  -57.125 -40.886  1.00 177.47 ? 360  ILE E C   1 
ATOM   14270 O  O   . ILE E  1 360 ? -2.491  -56.671 -42.035  1.00 194.46 ? 360  ILE E O   1 
ATOM   14271 C  CB  . ILE E  1 360 ? -1.730  -59.491 -41.100  1.00 165.18 ? 360  ILE E CB  1 
ATOM   14272 C  CG1 . ILE E  1 360 ? -2.105  -60.969 -40.972  1.00 168.98 ? 360  ILE E CG1 1 
ATOM   14273 C  CG2 . ILE E  1 360 ? -0.489  -59.180 -40.286  1.00 166.78 ? 360  ILE E CG2 1 
ATOM   14274 C  CD1 . ILE E  1 360 ? -1.065  -61.915 -41.532  1.00 170.69 ? 360  ILE E CD1 1 
ATOM   14275 N  N   . ALA E  1 361 ? -2.286  -56.393 -39.804  1.00 162.12 ? 361  ALA E N   1 
ATOM   14276 C  CA  . ALA E  1 361 ? -2.088  -54.952 -39.874  1.00 161.65 ? 361  ALA E CA  1 
ATOM   14277 C  C   . ALA E  1 361 ? -0.620  -54.568 -39.736  1.00 162.37 ? 361  ALA E C   1 
ATOM   14278 O  O   . ALA E  1 361 ? 0.141   -55.211 -39.006  1.00 183.76 ? 361  ALA E O   1 
ATOM   14279 C  CB  . ALA E  1 361 ? -2.908  -54.239 -38.799  1.00 158.42 ? 361  ALA E CB  1 
ATOM   14280 N  N   . ALA E  1 362 ? -0.228  -53.516 -40.457  1.00 167.59 ? 362  ALA E N   1 
ATOM   14281 C  CA  . ALA E  1 362 ? 1.073   -52.868 -40.314  1.00 166.71 ? 362  ALA E CA  1 
ATOM   14282 C  C   . ALA E  1 362 ? 0.816   -51.425 -39.892  1.00 166.62 ? 362  ALA E C   1 
ATOM   14283 O  O   . ALA E  1 362 ? 0.793   -50.514 -40.735  1.00 176.50 ? 362  ALA E O   1 
ATOM   14284 C  CB  . ALA E  1 362 ? 1.883   -52.943 -41.607  1.00 183.89 ? 362  ALA E CB  1 
ATOM   14285 N  N   . PRO E  1 363 ? 0.636   -51.178 -38.589  1.00 176.78 ? 363  PRO E N   1 
ATOM   14286 C  CA  . PRO E  1 363 ? 0.103   -49.880 -38.139  1.00 183.82 ? 363  PRO E CA  1 
ATOM   14287 C  C   . PRO E  1 363 ? 0.967   -48.681 -38.492  1.00 182.06 ? 363  PRO E C   1 
ATOM   14288 O  O   . PRO E  1 363 ? 0.475   -47.546 -38.424  1.00 183.65 ? 363  PRO E O   1 
ATOM   14289 C  CB  . PRO E  1 363 ? -0.001  -50.052 -36.615  1.00 182.52 ? 363  PRO E CB  1 
ATOM   14290 C  CG  . PRO E  1 363 ? -0.007  -51.538 -36.394  1.00 170.35 ? 363  PRO E CG  1 
ATOM   14291 C  CD  . PRO E  1 363 ? 0.878   -52.095 -37.465  1.00 172.17 ? 363  PRO E CD  1 
ATOM   14292 N  N   . TYR E  1 364 ? 2.220   -48.880 -38.891  1.00 177.98 ? 364  TYR E N   1 
ATOM   14293 C  CA  . TYR E  1 364 ? 3.117   -47.765 -39.166  1.00 185.05 ? 364  TYR E CA  1 
ATOM   14294 C  C   . TYR E  1 364 ? 3.599   -47.770 -40.611  1.00 193.38 ? 364  TYR E C   1 
ATOM   14295 O  O   . TYR E  1 364 ? 4.580   -47.093 -40.938  1.00 201.18 ? 364  TYR E O   1 
ATOM   14296 C  CB  . TYR E  1 364 ? 4.303   -47.795 -38.200  1.00 188.55 ? 364  TYR E CB  1 
ATOM   14297 C  CG  . TYR E  1 364 ? 3.883   -47.976 -36.762  1.00 195.57 ? 364  TYR E CG  1 
ATOM   14298 C  CD1 . TYR E  1 364 ? 3.223   -46.964 -36.077  1.00 196.81 ? 364  TYR E CD1 1 
ATOM   14299 C  CD2 . TYR E  1 364 ? 4.120   -49.170 -36.097  1.00 207.99 ? 364  TYR E CD2 1 
ATOM   14300 C  CE1 . TYR E  1 364 ? 2.828   -47.131 -34.762  1.00 193.38 ? 364  TYR E CE1 1 
ATOM   14301 C  CE2 . TYR E  1 364 ? 3.727   -49.346 -34.783  1.00 206.08 ? 364  TYR E CE2 1 
ATOM   14302 C  CZ  . TYR E  1 364 ? 3.082   -48.323 -34.122  1.00 186.02 ? 364  TYR E CZ  1 
ATOM   14303 O  OH  . TYR E  1 364 ? 2.688   -48.488 -32.815  1.00 168.62 ? 364  TYR E OH  1 
ATOM   14304 N  N   . GLY E  1 365 ? 2.907   -48.498 -41.484  1.00 194.26 ? 365  GLY E N   1 
ATOM   14305 C  CA  . GLY E  1 365 ? 3.229   -48.534 -42.893  1.00 195.09 ? 365  GLY E CA  1 
ATOM   14306 C  C   . GLY E  1 365 ? 2.477   -47.475 -43.675  1.00 209.62 ? 365  GLY E C   1 
ATOM   14307 O  O   . GLY E  1 365 ? 1.797   -46.608 -43.123  1.00 218.73 ? 365  GLY E O   1 
ATOM   14308 N  N   . GLY E  1 366 ? 2.619   -47.548 -44.996  1.00 220.33 ? 366  GLY E N   1 
ATOM   14309 C  CA  . GLY E  1 366 ? 1.931   -46.620 -45.870  1.00 221.55 ? 366  GLY E CA  1 
ATOM   14310 C  C   . GLY E  1 366 ? 2.590   -45.255 -45.863  1.00 215.02 ? 366  GLY E C   1 
ATOM   14311 O  O   . GLY E  1 366 ? 3.562   -44.995 -45.152  1.00 221.44 ? 366  GLY E O   1 
ATOM   14312 N  N   . GLU E  1 367 ? 2.058   -44.369 -46.706  1.00 203.51 ? 367  GLU E N   1 
ATOM   14313 C  CA  . GLU E  1 367 ? 2.579   -43.011 -46.773  1.00 204.31 ? 367  GLU E CA  1 
ATOM   14314 C  C   . GLU E  1 367 ? 2.415   -42.305 -45.432  1.00 208.59 ? 367  GLU E C   1 
ATOM   14315 O  O   . GLU E  1 367 ? 1.376   -42.415 -44.774  1.00 219.58 ? 367  GLU E O   1 
ATOM   14316 C  CB  . GLU E  1 367 ? 1.867   -42.217 -47.866  1.00 213.07 ? 367  GLU E CB  1 
ATOM   14317 C  CG  . GLU E  1 367 ? 0.360   -42.169 -47.710  1.00 222.37 ? 367  GLU E CG  1 
ATOM   14318 C  CD  . GLU E  1 367 ? -0.299  -41.295 -48.755  1.00 243.58 ? 367  GLU E CD  1 
ATOM   14319 O  OE1 . GLU E  1 367 ? -1.429  -40.824 -48.510  1.00 244.61 ? 367  GLU E OE1 1 
ATOM   14320 O  OE2 . GLU E  1 367 ? 0.324   -41.060 -49.812  1.00 255.18 ? 367  GLU E OE2 1 
ATOM   14321 N  N   . ASP E  1 368 ? 3.454   -41.573 -45.034  1.00 190.44 ? 368  ASP E N   1 
ATOM   14322 C  CA  . ASP E  1 368 ? 3.473   -40.790 -43.803  1.00 190.50 ? 368  ASP E CA  1 
ATOM   14323 C  C   . ASP E  1 368 ? 3.271   -41.654 -42.560  1.00 194.31 ? 368  ASP E C   1 
ATOM   14324 O  O   . ASP E  1 368 ? 2.827   -41.152 -41.522  1.00 192.09 ? 368  ASP E O   1 
ATOM   14325 C  CB  . ASP E  1 368 ? 2.429   -39.671 -43.848  1.00 196.76 ? 368  ASP E CB  1 
ATOM   14326 C  CG  . ASP E  1 368 ? 2.833   -38.469 -43.029  1.00 212.80 ? 368  ASP E CG  1 
ATOM   14327 O  OD1 . ASP E  1 368 ? 3.686   -38.622 -42.132  1.00 208.50 ? 368  ASP E OD1 1 
ATOM   14328 O  OD2 . ASP E  1 368 ? 2.310   -37.366 -43.292  1.00 232.28 ? 368  ASP E OD2 1 
ATOM   14329 N  N   . LYS E  1 369 ? 3.585   -42.950 -42.654  1.00 211.27 ? 369  LYS E N   1 
ATOM   14330 C  CA  . LYS E  1 369 ? 3.449   -43.897 -41.542  1.00 203.27 ? 369  LYS E CA  1 
ATOM   14331 C  C   . LYS E  1 369 ? 2.072   -43.799 -40.888  1.00 203.50 ? 369  LYS E C   1 
ATOM   14332 O  O   . LYS E  1 369 ? 1.939   -43.643 -39.671  1.00 192.72 ? 369  LYS E O   1 
ATOM   14333 C  CB  . LYS E  1 369 ? 4.564   -43.699 -40.515  1.00 201.82 ? 369  LYS E CB  1 
ATOM   14334 C  CG  . LYS E  1 369 ? 5.962   -43.773 -41.109  1.00 208.68 ? 369  LYS E CG  1 
ATOM   14335 C  CD  . LYS E  1 369 ? 6.954   -44.397 -40.137  1.00 211.91 ? 369  LYS E CD  1 
ATOM   14336 C  CE  . LYS E  1 369 ? 6.984   -43.664 -38.805  1.00 213.97 ? 369  LYS E CE  1 
ATOM   14337 N  NZ  . LYS E  1 369 ? 7.895   -44.340 -37.838  1.00 193.55 ? 369  LYS E NZ  1 
ATOM   14338 N  N   . LYS E  1 370 ? 1.034   -43.884 -41.721  1.00 213.69 ? 370  LYS E N   1 
ATOM   14339 C  CA  . LYS E  1 370 ? -0.343  -43.734 -41.264  1.00 200.17 ? 370  LYS E CA  1 
ATOM   14340 C  C   . LYS E  1 370 ? -0.974  -45.062 -40.876  1.00 209.10 ? 370  LYS E C   1 
ATOM   14341 O  O   . LYS E  1 370 ? -1.689  -45.136 -39.873  1.00 222.96 ? 370  LYS E O   1 
ATOM   14342 C  CB  . LYS E  1 370 ? -1.192  -43.073 -42.352  1.00 193.92 ? 370  LYS E CB  1 
ATOM   14343 C  CG  . LYS E  1 370 ? -0.930  -41.595 -42.550  1.00 202.46 ? 370  LYS E CG  1 
ATOM   14344 C  CD  . LYS E  1 370 ? -1.905  -41.013 -43.561  1.00 214.35 ? 370  LYS E CD  1 
ATOM   14345 C  CE  . LYS E  1 370 ? -1.427  -39.677 -44.104  1.00 213.43 ? 370  LYS E CE  1 
ATOM   14346 N  NZ  . LYS E  1 370 ? -2.428  -39.079 -45.032  1.00 213.43 ? 370  LYS E NZ  1 
ATOM   14347 N  N   . GLY E  1 371 ? -0.722  -46.109 -41.650  1.00 203.05 ? 371  GLY E N   1 
ATOM   14348 C  CA  . GLY E  1 371 ? -1.171  -47.447 -41.305  1.00 192.80 ? 371  GLY E CA  1 
ATOM   14349 C  C   . GLY E  1 371 ? -1.797  -48.181 -42.475  1.00 193.66 ? 371  GLY E C   1 
ATOM   14350 O  O   . GLY E  1 371 ? -2.454  -47.589 -43.335  1.00 215.61 ? 371  GLY E O   1 
ATOM   14351 N  N   . ILE E  1 372 ? -1.598  -49.500 -42.500  1.00 170.46 ? 372  ILE E N   1 
ATOM   14352 C  CA  . ILE E  1 372 ? -2.095  -50.372 -43.560  1.00 173.40 ? 372  ILE E CA  1 
ATOM   14353 C  C   . ILE E  1 372 ? -2.645  -51.643 -42.924  1.00 180.15 ? 372  ILE E C   1 
ATOM   14354 O  O   . ILE E  1 372 ? -2.069  -52.166 -41.965  1.00 187.24 ? 372  ILE E O   1 
ATOM   14355 C  CB  . ILE E  1 372 ? -0.988  -50.719 -44.580  1.00 181.62 ? 372  ILE E CB  1 
ATOM   14356 C  CG1 . ILE E  1 372 ? -0.394  -49.455 -45.207  1.00 199.20 ? 372  ILE E CG1 1 
ATOM   14357 C  CG2 . ILE E  1 372 ? -1.517  -51.647 -45.661  1.00 189.75 ? 372  ILE E CG2 1 
ATOM   14358 C  CD1 . ILE E  1 372 ? -1.326  -48.751 -46.173  1.00 194.98 ? 372  ILE E CD1 1 
ATOM   14359 N  N   . VAL E  1 373 ? -3.750  -52.150 -43.468  1.00 188.06 ? 373  VAL E N   1 
ATOM   14360 C  CA  . VAL E  1 373 ? -4.299  -53.448 -43.091  1.00 183.85 ? 373  VAL E CA  1 
ATOM   14361 C  C   . VAL E  1 373 ? -4.370  -54.316 -44.338  1.00 197.36 ? 373  VAL E C   1 
ATOM   14362 O  O   . VAL E  1 373 ? -4.944  -53.909 -45.355  1.00 214.54 ? 373  VAL E O   1 
ATOM   14363 C  CB  . VAL E  1 373 ? -5.685  -53.320 -42.433  1.00 170.41 ? 373  VAL E CB  1 
ATOM   14364 C  CG1 . VAL E  1 373 ? -6.276  -54.698 -42.171  1.00 170.80 ? 373  VAL E CG1 1 
ATOM   14365 C  CG2 . VAL E  1 373 ? -5.579  -52.537 -41.139  1.00 168.41 ? 373  VAL E CG2 1 
ATOM   14366 N  N   . TYR E  1 374 ? -3.797  -55.511 -44.253  1.00 180.68 ? 374  TYR E N   1 
ATOM   14367 C  CA  . TYR E  1 374 ? -3.746  -56.434 -45.375  1.00 178.48 ? 374  TYR E CA  1 
ATOM   14368 C  C   . TYR E  1 374 ? -4.771  -57.543 -45.175  1.00 179.23 ? 374  TYR E C   1 
ATOM   14369 O  O   . TYR E  1 374 ? -4.892  -58.098 -44.079  1.00 178.00 ? 374  TYR E O   1 
ATOM   14370 C  CB  . TYR E  1 374 ? -2.340  -57.015 -45.533  1.00 179.67 ? 374  TYR E CB  1 
ATOM   14371 C  CG  . TYR E  1 374 ? -1.256  -55.984 -45.816  1.00 180.38 ? 374  TYR E CG  1 
ATOM   14372 C  CD1 . TYR E  1 374 ? -0.980  -55.574 -47.116  1.00 189.64 ? 374  TYR E CD1 1 
ATOM   14373 C  CD2 . TYR E  1 374 ? -0.492  -55.444 -44.787  1.00 176.52 ? 374  TYR E CD2 1 
ATOM   14374 C  CE1 . TYR E  1 374 ? 0.014   -54.643 -47.381  1.00 185.45 ? 374  TYR E CE1 1 
ATOM   14375 C  CE2 . TYR E  1 374 ? 0.505   -54.515 -45.043  1.00 174.72 ? 374  TYR E CE2 1 
ATOM   14376 C  CZ  . TYR E  1 374 ? 0.754   -54.119 -46.341  1.00 175.80 ? 374  TYR E CZ  1 
ATOM   14377 O  OH  . TYR E  1 374 ? 1.743   -53.196 -46.599  1.00 177.60 ? 374  TYR E OH  1 
ATOM   14378 N  N   . ILE E  1 375 ? -5.523  -57.839 -46.231  1.00 179.74 ? 375  ILE E N   1 
ATOM   14379 C  CA  . ILE E  1 375 ? -6.548  -58.875 -46.222  1.00 181.79 ? 375  ILE E CA  1 
ATOM   14380 C  C   . ILE E  1 375 ? -6.006  -60.110 -46.930  1.00 194.37 ? 375  ILE E C   1 
ATOM   14381 O  O   . ILE E  1 375 ? -5.539  -60.023 -48.073  1.00 207.62 ? 375  ILE E O   1 
ATOM   14382 C  CB  . ILE E  1 375 ? -7.835  -58.376 -46.897  1.00 174.51 ? 375  ILE E CB  1 
ATOM   14383 C  CG1 . ILE E  1 375 ? -8.240  -57.022 -46.309  1.00 176.92 ? 375  ILE E CG1 1 
ATOM   14384 C  CG2 . ILE E  1 375 ? -8.937  -59.405 -46.757  1.00 177.63 ? 375  ILE E CG2 1 
ATOM   14385 C  CD1 . ILE E  1 375 ? -8.399  -57.030 -44.804  1.00 181.47 ? 375  ILE E CD1 1 
ATOM   14386 N  N   . PHE E  1 376 ? -6.060  -61.259 -46.259  1.00 188.52 ? 376  PHE E N   1 
ATOM   14387 C  CA  . PHE E  1 376 ? -5.590  -62.517 -46.823  1.00 185.34 ? 376  PHE E CA  1 
ATOM   14388 C  C   . PHE E  1 376 ? -6.720  -63.536 -46.836  1.00 191.41 ? 376  PHE E C   1 
ATOM   14389 O  O   . PHE E  1 376 ? -7.437  -63.688 -45.841  1.00 195.02 ? 376  PHE E O   1 
ATOM   14390 C  CB  . PHE E  1 376 ? -4.400  -63.061 -46.038  1.00 175.63 ? 376  PHE E CB  1 
ATOM   14391 C  CG  . PHE E  1 376 ? -3.203  -62.174 -46.083  1.00 170.79 ? 376  PHE E CG  1 
ATOM   14392 C  CD1 . PHE E  1 376 ? -2.370  -62.174 -47.182  1.00 172.39 ? 376  PHE E CD1 1 
ATOM   14393 C  CD2 . PHE E  1 376 ? -2.926  -61.318 -45.037  1.00 168.06 ? 376  PHE E CD2 1 
ATOM   14394 C  CE1 . PHE E  1 376 ? -1.269  -61.352 -47.228  1.00 169.60 ? 376  PHE E CE1 1 
ATOM   14395 C  CE2 . PHE E  1 376 ? -1.827  -60.491 -45.077  1.00 166.96 ? 376  PHE E CE2 1 
ATOM   14396 C  CZ  . PHE E  1 376 ? -0.997  -60.508 -46.174  1.00 163.98 ? 376  PHE E CZ  1 
ATOM   14397 N  N   . ASN E  1 377 ? -6.864  -64.238 -47.957  1.00 199.02 ? 377  ASN E N   1 
ATOM   14398 C  CA  . ASN E  1 377 ? -7.914  -65.231 -48.131  1.00 206.23 ? 377  ASN E CA  1 
ATOM   14399 C  C   . ASN E  1 377 ? -7.363  -66.634 -47.914  1.00 218.34 ? 377  ASN E C   1 
ATOM   14400 O  O   . ASN E  1 377 ? -6.198  -66.910 -48.217  1.00 231.90 ? 377  ASN E O   1 
ATOM   14401 C  CB  . ASN E  1 377 ? -8.534  -65.129 -49.527  1.00 206.04 ? 377  ASN E CB  1 
ATOM   14402 C  CG  . ASN E  1 377 ? -9.242  -63.805 -49.761  1.00 203.97 ? 377  ASN E CG  1 
ATOM   14403 O  OD1 . ASN E  1 377 ? -8.638  -62.838 -50.224  1.00 205.51 ? 377  ASN E OD1 1 
ATOM   14404 N  ND2 . ASN E  1 377 ? -10.533 -63.762 -49.454  1.00 205.12 ? 377  ASN E ND2 1 
ATOM   14405 N  N   . GLY E  1 378 ? -8.201  -67.513 -47.358  1.00 218.38 ? 378  GLY E N   1 
ATOM   14406 C  CA  . GLY E  1 378 ? -7.835  -68.904 -47.210  1.00 219.42 ? 378  GLY E CA  1 
ATOM   14407 C  C   . GLY E  1 378 ? -8.124  -69.717 -48.461  1.00 229.56 ? 378  GLY E C   1 
ATOM   14408 O  O   . GLY E  1 378 ? -8.869  -69.304 -49.348  1.00 224.58 ? 378  GLY E O   1 
ATOM   14409 N  N   . ARG E  1 379 ? -7.530  -70.907 -48.512  1.00 237.72 ? 379  ARG E N   1 
ATOM   14410 C  CA  . ARG E  1 379 ? -7.770  -71.856 -49.594  1.00 238.36 ? 379  ARG E CA  1 
ATOM   14411 C  C   . ARG E  1 379 ? -7.471  -73.254 -49.069  1.00 238.61 ? 379  ARG E C   1 
ATOM   14412 O  O   . ARG E  1 379 ? -7.059  -73.433 -47.918  1.00 236.62 ? 379  ARG E O   1 
ATOM   14413 C  CB  . ARG E  1 379 ? -6.928  -71.528 -50.832  1.00 226.34 ? 379  ARG E CB  1 
ATOM   14414 C  CG  . ARG E  1 379 ? -5.485  -71.192 -50.520  1.00 219.45 ? 379  ARG E CG  1 
ATOM   14415 C  CD  . ARG E  1 379 ? -4.744  -70.584 -51.698  1.00 222.89 ? 379  ARG E CD  1 
ATOM   14416 N  NE  . ARG E  1 379 ? -3.352  -70.318 -51.345  1.00 230.55 ? 379  ARG E NE  1 
ATOM   14417 C  CZ  . ARG E  1 379 ? -2.457  -69.758 -52.154  1.00 234.69 ? 379  ARG E CZ  1 
ATOM   14418 N  NH1 . ARG E  1 379 ? -2.798  -69.394 -53.384  1.00 233.37 ? 379  ARG E NH1 1 
ATOM   14419 N  NH2 . ARG E  1 379 ? -1.215  -69.563 -51.730  1.00 231.35 ? 379  ARG E NH2 1 
ATOM   14420 N  N   . SER E  1 380 ? -7.706  -74.251 -49.926  1.00 223.06 ? 380  SER E N   1 
ATOM   14421 C  CA  . SER E  1 380 ? -7.554  -75.644 -49.520  1.00 219.03 ? 380  SER E CA  1 
ATOM   14422 C  C   . SER E  1 380 ? -6.163  -75.923 -48.965  1.00 215.44 ? 380  SER E C   1 
ATOM   14423 O  O   . SER E  1 380 ? -6.009  -76.694 -48.012  1.00 215.26 ? 380  SER E O   1 
ATOM   14424 C  CB  . SER E  1 380 ? -7.853  -76.561 -50.706  1.00 220.32 ? 380  SER E CB  1 
ATOM   14425 O  OG  . SER E  1 380 ? -6.911  -76.363 -51.747  1.00 215.25 ? 380  SER E OG  1 
ATOM   14426 N  N   . THR E  1 381 ? -5.140  -75.289 -49.532  1.00 210.25 ? 381  THR E N   1 
ATOM   14427 C  CA  . THR E  1 381 ? -3.761  -75.504 -49.114  1.00 207.89 ? 381  THR E CA  1 
ATOM   14428 C  C   . THR E  1 381 ? -3.340  -74.554 -48.002  1.00 207.03 ? 381  THR E C   1 
ATOM   14429 O  O   . THR E  1 381 ? -2.205  -74.638 -47.522  1.00 204.62 ? 381  THR E O   1 
ATOM   14430 C  CB  . THR E  1 381 ? -2.821  -75.361 -50.319  1.00 217.21 ? 381  THR E CB  1 
ATOM   14431 O  OG1 . THR E  1 381 ? -3.414  -75.993 -51.459  1.00 237.22 ? 381  THR E OG1 1 
ATOM   14432 C  CG2 . THR E  1 381 ? -1.476  -76.037 -50.051  1.00 207.73 ? 381  THR E CG2 1 
ATOM   14433 N  N   . GLY E  1 382 ? -4.225  -73.665 -47.568  1.00 209.46 ? 382  GLY E N   1 
ATOM   14434 C  CA  . GLY E  1 382 ? -3.878  -72.757 -46.498  1.00 207.84 ? 382  GLY E CA  1 
ATOM   14435 C  C   . GLY E  1 382 ? -4.165  -71.303 -46.803  1.00 205.81 ? 382  GLY E C   1 
ATOM   14436 O  O   . GLY E  1 382 ? -5.143  -70.987 -47.484  1.00 214.14 ? 382  GLY E O   1 
ATOM   14437 N  N   . LEU E  1 383 ? -3.337  -70.407 -46.271  1.00 211.51 ? 383  LEU E N   1 
ATOM   14438 C  CA  . LEU E  1 383 ? -3.524  -68.973 -46.441  1.00 211.91 ? 383  LEU E CA  1 
ATOM   14439 C  C   . LEU E  1 383 ? -2.847  -68.480 -47.716  1.00 207.64 ? 383  LEU E C   1 
ATOM   14440 O  O   . LEU E  1 383 ? -1.729  -68.890 -48.040  1.00 210.11 ? 383  LEU E O   1 
ATOM   14441 C  CB  . LEU E  1 383 ? -2.973  -68.215 -45.231  1.00 209.40 ? 383  LEU E CB  1 
ATOM   14442 C  CG  . LEU E  1 383 ? -3.281  -66.716 -45.183  1.00 202.13 ? 383  LEU E CG  1 
ATOM   14443 C  CD1 . LEU E  1 383 ? -4.782  -66.492 -45.083  1.00 201.57 ? 383  LEU E CD1 1 
ATOM   14444 C  CD2 . LEU E  1 383 ? -2.556  -66.046 -44.028  1.00 198.98 ? 383  LEU E CD2 1 
ATOM   14445 N  N   . ASN E  1 384 ? -3.539  -67.604 -48.443  1.00 200.16 ? 384  ASN E N   1 
ATOM   14446 C  CA  . ASN E  1 384 ? -2.962  -66.968 -49.622  1.00 197.68 ? 384  ASN E CA  1 
ATOM   14447 C  C   . ASN E  1 384 ? -1.935  -65.924 -49.197  1.00 194.29 ? 384  ASN E C   1 
ATOM   14448 O  O   . ASN E  1 384 ? -2.273  -64.952 -48.513  1.00 197.48 ? 384  ASN E O   1 
ATOM   14449 C  CB  . ASN E  1 384 ? -4.058  -66.333 -50.470  1.00 197.60 ? 384  ASN E CB  1 
ATOM   14450 C  CG  . ASN E  1 384 ? -3.547  -65.843 -51.802  1.00 198.25 ? 384  ASN E CG  1 
ATOM   14451 O  OD1 . ASN E  1 384 ? -2.424  -66.149 -52.194  1.00 209.83 ? 384  ASN E OD1 1 
ATOM   14452 N  ND2 . ASN E  1 384 ? -4.373  -65.086 -52.512  1.00 197.35 ? 384  ASN E ND2 1 
ATOM   14453 N  N   . ALA E  1 385 ? -0.675  -66.136 -49.589  1.00 196.52 ? 385  ALA E N   1 
ATOM   14454 C  CA  . ALA E  1 385 ? 0.408   -65.254 -49.160  1.00 194.40 ? 385  ALA E CA  1 
ATOM   14455 C  C   . ALA E  1 385 ? 0.277   -63.848 -49.734  1.00 190.27 ? 385  ALA E C   1 
ATOM   14456 O  O   . ALA E  1 385 ? 0.806   -62.895 -49.151  1.00 187.49 ? 385  ALA E O   1 
ATOM   14457 C  CB  . ALA E  1 385 ? 1.757   -65.856 -49.550  1.00 196.51 ? 385  ALA E CB  1 
ATOM   14458 N  N   . VAL E  1 386 ? -0.390  -63.695 -50.874  1.00 182.30 ? 386  VAL E N   1 
ATOM   14459 C  CA  . VAL E  1 386 ? -0.561  -62.378 -51.487  1.00 180.23 ? 386  VAL E CA  1 
ATOM   14460 C  C   . VAL E  1 386 ? -1.888  -61.770 -51.044  1.00 178.23 ? 386  VAL E C   1 
ATOM   14461 O  O   . VAL E  1 386 ? -2.923  -62.453 -51.062  1.00 180.76 ? 386  VAL E O   1 
ATOM   14462 C  CB  . VAL E  1 386 ? -0.456  -62.454 -53.019  1.00 196.25 ? 386  VAL E CB  1 
ATOM   14463 C  CG1 . VAL E  1 386 ? 0.983   -62.739 -53.433  1.00 194.63 ? 386  VAL E CG1 1 
ATOM   14464 C  CG2 . VAL E  1 386 ? -1.394  -63.510 -53.580  1.00 209.13 ? 386  VAL E CG2 1 
ATOM   14465 N  N   . PRO E  1 387 ? -1.898  -60.511 -50.602  1.00 187.02 ? 387  PRO E N   1 
ATOM   14466 C  CA  . PRO E  1 387 ? -3.153  -59.897 -50.154  1.00 185.97 ? 387  PRO E CA  1 
ATOM   14467 C  C   . PRO E  1 387 ? -4.065  -59.557 -51.323  1.00 205.31 ? 387  PRO E C   1 
ATOM   14468 O  O   . PRO E  1 387 ? -3.608  -59.159 -52.396  1.00 222.50 ? 387  PRO E O   1 
ATOM   14469 C  CB  . PRO E  1 387 ? -2.687  -58.629 -49.433  1.00 180.65 ? 387  PRO E CB  1 
ATOM   14470 C  CG  . PRO E  1 387 ? -1.400  -58.279 -50.108  1.00 180.45 ? 387  PRO E CG  1 
ATOM   14471 C  CD  . PRO E  1 387 ? -0.752  -59.594 -50.464  1.00 183.30 ? 387  PRO E CD  1 
ATOM   14472 N  N   . SER E  1 388 ? -5.372  -59.707 -51.103  1.00 210.17 ? 388  SER E N   1 
ATOM   14473 C  CA  . SER E  1 388 ? -6.363  -59.373 -52.116  1.00 203.71 ? 388  SER E CA  1 
ATOM   14474 C  C   . SER E  1 388 ? -6.940  -57.980 -51.934  1.00 200.77 ? 388  SER E C   1 
ATOM   14475 O  O   . SER E  1 388 ? -7.691  -57.518 -52.801  1.00 202.93 ? 388  SER E O   1 
ATOM   14476 C  CB  . SER E  1 388 ? -7.507  -60.396 -52.115  1.00 204.52 ? 388  SER E CB  1 
ATOM   14477 O  OG  . SER E  1 388 ? -8.174  -60.420 -50.865  1.00 206.09 ? 388  SER E OG  1 
ATOM   14478 N  N   . GLN E  1 389 ? -6.620  -57.308 -50.832  1.00 204.06 ? 389  GLN E N   1 
ATOM   14479 C  CA  . GLN E  1 389 ? -7.101  -55.956 -50.599  1.00 203.77 ? 389  GLN E CA  1 
ATOM   14480 C  C   . GLN E  1 389 ? -6.174  -55.253 -49.619  1.00 195.73 ? 389  GLN E C   1 
ATOM   14481 O  O   . GLN E  1 389 ? -5.690  -55.863 -48.662  1.00 190.10 ? 389  GLN E O   1 
ATOM   14482 C  CB  . GLN E  1 389 ? -8.531  -55.960 -50.064  1.00 204.05 ? 389  GLN E CB  1 
ATOM   14483 C  CG  . GLN E  1 389 ? -9.188  -54.598 -50.071  1.00 205.05 ? 389  GLN E CG  1 
ATOM   14484 C  CD  . GLN E  1 389 ? -10.669 -54.680 -49.789  1.00 206.05 ? 389  GLN E CD  1 
ATOM   14485 O  OE1 . GLN E  1 389 ? -11.179 -55.730 -49.400  1.00 201.86 ? 389  GLN E OE1 1 
ATOM   14486 N  NE2 . GLN E  1 389 ? -11.367 -53.565 -49.965  1.00 212.49 ? 389  GLN E NE2 1 
ATOM   14487 N  N   . ILE E  1 390 ? -5.958  -53.963 -49.853  1.00 208.63 ? 390  ILE E N   1 
ATOM   14488 C  CA  . ILE E  1 390 ? -5.089  -53.136 -49.024  1.00 203.33 ? 390  ILE E CA  1 
ATOM   14489 C  C   . ILE E  1 390 ? -5.930  -52.012 -48.434  1.00 211.52 ? 390  ILE E C   1 
ATOM   14490 O  O   . ILE E  1 390 ? -6.512  -51.209 -49.175  1.00 236.01 ? 390  ILE E O   1 
ATOM   14491 C  CB  . ILE E  1 390 ? -3.897  -52.578 -49.817  1.00 219.88 ? 390  ILE E CB  1 
ATOM   14492 C  CG1 . ILE E  1 390 ? -3.041  -53.709 -50.406  1.00 226.41 ? 390  ILE E CG1 1 
ATOM   14493 C  CG2 . ILE E  1 390 ? -3.056  -51.676 -48.936  1.00 213.37 ? 390  ILE E CG2 1 
ATOM   14494 C  CD1 . ILE E  1 390 ? -3.467  -54.158 -51.795  1.00 236.53 ? 390  ILE E CD1 1 
ATOM   14495 N  N   . LEU E  1 391 ? -6.013  -51.971 -47.107  1.00 190.82 ? 391  LEU E N   1 
ATOM   14496 C  CA  . LEU E  1 391 ? -6.731  -50.914 -46.403  1.00 187.40 ? 391  LEU E CA  1 
ATOM   14497 C  C   . LEU E  1 391 ? -5.753  -49.802 -46.042  1.00 185.89 ? 391  LEU E C   1 
ATOM   14498 O  O   . LEU E  1 391 ? -4.796  -50.032 -45.298  1.00 182.29 ? 391  LEU E O   1 
ATOM   14499 C  CB  . LEU E  1 391 ? -7.407  -51.470 -45.152  1.00 184.56 ? 391  LEU E CB  1 
ATOM   14500 C  CG  . LEU E  1 391 ? -8.831  -52.009 -45.301  1.00 187.21 ? 391  LEU E CG  1 
ATOM   14501 C  CD1 . LEU E  1 391 ? -8.944  -53.016 -46.431  1.00 190.38 ? 391  LEU E CD1 1 
ATOM   14502 C  CD2 . LEU E  1 391 ? -9.257  -52.646 -43.996  1.00 185.08 ? 391  LEU E CD2 1 
ATOM   14503 N  N   . GLU E  1 392 ? -6.014  -48.596 -46.535  1.00 200.28 ? 392  GLU E N   1 
ATOM   14504 C  CA  . GLU E  1 392 ? -5.104  -47.472 -46.364  1.00 202.63 ? 392  GLU E CA  1 
ATOM   14505 C  C   . GLU E  1 392 ? -5.622  -46.523 -45.293  1.00 201.47 ? 392  GLU E C   1 
ATOM   14506 O  O   . GLU E  1 392 ? -6.828  -46.279 -45.192  1.00 203.97 ? 392  GLU E O   1 
ATOM   14507 C  CB  . GLU E  1 392 ? -4.915  -46.708 -47.680  1.00 241.28 ? 392  GLU E CB  1 
ATOM   14508 C  CG  . GLU E  1 392 ? -4.157  -47.465 -48.773  1.00 254.31 ? 392  GLU E CG  1 
ATOM   14509 C  CD  . GLU E  1 392 ? -2.714  -47.000 -48.928  1.00 257.00 ? 392  GLU E CD  1 
ATOM   14510 O  OE1 . GLU E  1 392 ? -2.276  -46.131 -48.145  1.00 260.80 ? 392  GLU E OE1 1 
ATOM   14511 O  OE2 . GLU E  1 392 ? -2.020  -47.502 -49.840  1.00 254.07 ? 392  GLU E OE2 1 
ATOM   14512 N  N   . GLY E  1 393 ? -4.698  -46.011 -44.482  1.00 211.84 ? 393  GLY E N   1 
ATOM   14513 C  CA  . GLY E  1 393 ? -5.033  -44.962 -43.530  1.00 224.06 ? 393  GLY E CA  1 
ATOM   14514 C  C   . GLY E  1 393 ? -5.158  -43.607 -44.216  1.00 225.70 ? 393  GLY E C   1 
ATOM   14515 O  O   . GLY E  1 393 ? -4.420  -43.281 -45.146  1.00 227.98 ? 393  GLY E O   1 
ATOM   14516 N  N   . GLN E  1 394 ? -6.115  -42.815 -43.741  1.00 221.56 ? 394  GLN E N   1 
ATOM   14517 C  CA  . GLN E  1 394 ? -6.410  -41.513 -44.314  1.00 231.06 ? 394  GLN E CA  1 
ATOM   14518 C  C   . GLN E  1 394 ? -6.030  -40.353 -43.404  1.00 247.49 ? 394  GLN E C   1 
ATOM   14519 O  O   . GLN E  1 394 ? -6.106  -39.200 -43.838  1.00 262.41 ? 394  GLN E O   1 
ATOM   14520 C  CB  . GLN E  1 394 ? -7.908  -41.415 -44.650  1.00 234.33 ? 394  GLN E CB  1 
ATOM   14521 C  CG  . GLN E  1 394 ? -8.448  -42.551 -45.509  1.00 225.95 ? 394  GLN E CG  1 
ATOM   14522 C  CD  . GLN E  1 394 ? -7.886  -42.566 -46.917  1.00 235.64 ? 394  GLN E CD  1 
ATOM   14523 O  OE1 . GLN E  1 394 ? -7.350  -41.569 -47.400  1.00 248.89 ? 394  GLN E OE1 1 
ATOM   14524 N  NE2 . GLN E  1 394 ? -8.015  -43.705 -47.588  1.00 227.62 ? 394  GLN E NE2 1 
ATOM   14525 N  N   . TRP E  1 395 ? -5.642  -40.622 -42.161  1.00 241.56 ? 395  TRP E N   1 
ATOM   14526 C  CA  . TRP E  1 395 ? -5.504  -39.600 -41.128  1.00 239.74 ? 395  TRP E CA  1 
ATOM   14527 C  C   . TRP E  1 395 ? -4.032  -39.347 -40.835  1.00 251.02 ? 395  TRP E C   1 
ATOM   14528 O  O   . TRP E  1 395 ? -3.317  -40.257 -40.404  1.00 247.79 ? 395  TRP E O   1 
ATOM   14529 C  CB  . TRP E  1 395 ? -6.249  -40.023 -39.865  1.00 226.26 ? 395  TRP E CB  1 
ATOM   14530 C  CG  . TRP E  1 395 ? -7.670  -40.375 -40.152  1.00 230.93 ? 395  TRP E CG  1 
ATOM   14531 C  CD1 . TRP E  1 395 ? -8.763  -39.566 -40.016  1.00 241.89 ? 395  TRP E CD1 1 
ATOM   14532 C  CD2 . TRP E  1 395 ? -8.150  -41.613 -40.684  1.00 230.54 ? 395  TRP E CD2 1 
ATOM   14533 N  NE1 . TRP E  1 395 ? -9.898  -40.237 -40.402  1.00 246.16 ? 395  TRP E NE1 1 
ATOM   14534 C  CE2 . TRP E  1 395 ? -9.547  -41.495 -40.819  1.00 243.87 ? 395  TRP E CE2 1 
ATOM   14535 C  CE3 . TRP E  1 395 ? -7.536  -42.816 -41.043  1.00 225.47 ? 395  TRP E CE3 1 
ATOM   14536 C  CZ2 . TRP E  1 395 ? -10.339 -42.533 -41.303  1.00 248.95 ? 395  TRP E CZ2 1 
ATOM   14537 C  CZ3 . TRP E  1 395 ? -8.322  -43.844 -41.528  1.00 231.81 ? 395  TRP E CZ3 1 
ATOM   14538 C  CH2 . TRP E  1 395 ? -9.708  -43.695 -41.654  1.00 244.09 ? 395  TRP E CH2 1 
ATOM   14539 N  N   . ALA E  1 396 ? -3.587  -38.117 -41.074  1.00 261.48 ? 396  ALA E N   1 
ATOM   14540 C  CA  . ALA E  1 396 ? -2.202  -37.757 -40.820  1.00 256.41 ? 396  ALA E CA  1 
ATOM   14541 C  C   . ALA E  1 396 ? -1.914  -37.731 -39.321  1.00 261.86 ? 396  ALA E C   1 
ATOM   14542 O  O   . ALA E  1 396 ? -2.817  -37.661 -38.480  1.00 261.93 ? 396  ALA E O   1 
ATOM   14543 C  CB  . ALA E  1 396 ? -1.873  -36.400 -41.446  1.00 253.46 ? 396  ALA E CB  1 
ATOM   14544 N  N   . ALA E  1 397 ? -0.626  -37.790 -38.994  1.00 253.42 ? 397  ALA E N   1 
ATOM   14545 C  CA  . ALA E  1 397 ? -0.178  -37.870 -37.610  1.00 238.86 ? 397  ALA E CA  1 
ATOM   14546 C  C   . ALA E  1 397 ? 0.081   -36.470 -37.078  1.00 250.05 ? 397  ALA E C   1 
ATOM   14547 O  O   . ALA E  1 397 ? 1.085   -35.842 -37.430  1.00 262.95 ? 397  ALA E O   1 
ATOM   14548 C  CB  . ALA E  1 397 ? 1.088   -38.716 -37.505  1.00 222.21 ? 397  ALA E CB  1 
ATOM   14549 N  N   . ARG E  1 398 ? -0.816  -35.984 -36.227  1.00 246.59 ? 398  ARG E N   1 
ATOM   14550 C  CA  . ARG E  1 398 ? -0.508  -34.800 -35.452  1.00 248.04 ? 398  ARG E CA  1 
ATOM   14551 C  C   . ARG E  1 398 ? 0.682   -35.105 -34.549  1.00 235.76 ? 398  ARG E C   1 
ATOM   14552 O  O   . ARG E  1 398 ? 1.064   -36.266 -34.358  1.00 215.92 ? 398  ARG E O   1 
ATOM   14553 C  CB  . ARG E  1 398 ? -1.720  -34.373 -34.629  1.00 252.57 ? 398  ARG E CB  1 
ATOM   14554 C  CG  . ARG E  1 398 ? -3.049  -34.680 -35.306  1.00 252.03 ? 398  ARG E CG  1 
ATOM   14555 C  CD  . ARG E  1 398 ? -4.172  -34.783 -34.288  1.00 254.43 ? 398  ARG E CD  1 
ATOM   14556 N  NE  . ARG E  1 398 ? -5.406  -35.270 -34.896  1.00 247.89 ? 398  ARG E NE  1 
ATOM   14557 C  CZ  . ARG E  1 398 ? -6.521  -35.528 -34.222  1.00 238.22 ? 398  ARG E CZ  1 
ATOM   14558 N  NH1 . ARG E  1 398 ? -6.563  -35.347 -32.909  1.00 234.71 ? 398  ARG E NH1 1 
ATOM   14559 N  NH2 . ARG E  1 398 ? -7.596  -35.969 -34.862  1.00 236.78 ? 398  ARG E NH2 1 
ATOM   14560 N  N   . SER E  1 399 ? 1.282   -34.050 -34.000  1.00 246.63 ? 399  SER E N   1 
ATOM   14561 C  CA  . SER E  1 399 ? 2.442   -34.238 -33.141  1.00 228.96 ? 399  SER E CA  1 
ATOM   14562 C  C   . SER E  1 399 ? 2.105   -35.204 -32.011  1.00 206.99 ? 399  SER E C   1 
ATOM   14563 O  O   . SER E  1 399 ? 1.060   -35.085 -31.365  1.00 209.26 ? 399  SER E O   1 
ATOM   14564 C  CB  . SER E  1 399 ? 2.925   -32.884 -32.603  1.00 232.86 ? 399  SER E CB  1 
ATOM   14565 O  OG  . SER E  1 399 ? 1.862   -32.106 -32.078  1.00 224.61 ? 399  SER E OG  1 
ATOM   14566 N  N   . GLY E  1 400 ? 2.983   -36.182 -31.807  1.00 201.33 ? 400  GLY E N   1 
ATOM   14567 C  CA  . GLY E  1 400 ? 2.860   -37.165 -30.745  1.00 203.12 ? 400  GLY E CA  1 
ATOM   14568 C  C   . GLY E  1 400 ? 2.801   -38.580 -31.286  1.00 208.69 ? 400  GLY E C   1 
ATOM   14569 O  O   . GLY E  1 400 ? 3.685   -38.971 -32.050  1.00 216.78 ? 400  GLY E O   1 
ATOM   14570 N  N   . CYS E  1 401 ? 1.759   -39.362 -30.930  1.00 209.47 ? 401  CYS E N   1 
ATOM   14571 C  CA  . CYS E  1 401 ? 1.726   -40.721 -31.463  1.00 216.62 ? 401  CYS E CA  1 
ATOM   14572 C  C   . CYS E  1 401 ? 1.325   -40.748 -32.936  1.00 212.32 ? 401  CYS E C   1 
ATOM   14573 O  O   . CYS E  1 401 ? 0.532   -39.917 -33.392  1.00 218.35 ? 401  CYS E O   1 
ATOM   14574 C  CB  . CYS E  1 401 ? 0.776   -41.615 -30.671  1.00 227.46 ? 401  CYS E CB  1 
ATOM   14575 S  SG  . CYS E  1 401 ? 1.477   -42.694 -29.366  1.00 238.99 ? 401  CYS E SG  1 
ATOM   14576 N  N   . PRO E  1 402 ? 1.873   -41.696 -33.693  1.00 207.03 ? 402  PRO E N   1 
ATOM   14577 C  CA  . PRO E  1 402 ? 1.421   -41.919 -35.062  1.00 209.40 ? 402  PRO E CA  1 
ATOM   14578 C  C   . PRO E  1 402 ? -0.010  -42.419 -35.074  1.00 206.26 ? 402  PRO E C   1 
ATOM   14579 O  O   . PRO E  1 402 ? -0.514  -42.896 -34.045  1.00 203.82 ? 402  PRO E O   1 
ATOM   14580 C  CB  . PRO E  1 402 ? 2.393   -42.988 -35.586  1.00 203.88 ? 402  PRO E CB  1 
ATOM   14581 C  CG  . PRO E  1 402 ? 2.870   -43.687 -34.374  1.00 204.51 ? 402  PRO E CG  1 
ATOM   14582 C  CD  . PRO E  1 402 ? 2.937   -42.638 -33.301  1.00 207.81 ? 402  PRO E CD  1 
ATOM   14583 N  N   . PRO E  1 403 ? -0.694  -42.333 -36.219  1.00 214.00 ? 403  PRO E N   1 
ATOM   14584 C  CA  . PRO E  1 403 ? -2.111  -42.726 -36.253  1.00 209.89 ? 403  PRO E CA  1 
ATOM   14585 C  C   . PRO E  1 403 ? -2.353  -44.134 -35.763  1.00 191.25 ? 403  PRO E C   1 
ATOM   14586 O  O   . PRO E  1 403 ? -3.385  -44.391 -35.129  1.00 189.20 ? 403  PRO E O   1 
ATOM   14587 C  CB  . PRO E  1 403 ? -2.480  -42.573 -37.736  1.00 230.30 ? 403  PRO E CB  1 
ATOM   14588 C  CG  . PRO E  1 403 ? -1.464  -41.637 -38.290  1.00 225.10 ? 403  PRO E CG  1 
ATOM   14589 C  CD  . PRO E  1 403 ? -0.204  -41.929 -37.547  1.00 217.04 ? 403  PRO E CD  1 
ATOM   14590 N  N   . SER E  1 404 ? -1.421  -45.051 -36.024  1.00 176.05 ? 404  SER E N   1 
ATOM   14591 C  CA  . SER E  1 404 ? -1.519  -46.428 -35.546  1.00 174.17 ? 404  SER E CA  1 
ATOM   14592 C  C   . SER E  1 404 ? -2.771  -47.112 -36.093  1.00 192.21 ? 404  SER E C   1 
ATOM   14593 O  O   . SER E  1 404 ? -3.415  -47.910 -35.407  1.00 208.88 ? 404  SER E O   1 
ATOM   14594 C  CB  . SER E  1 404 ? -1.491  -46.473 -34.017  1.00 169.82 ? 404  SER E CB  1 
ATOM   14595 O  OG  . SER E  1 404 ? -0.373  -45.765 -33.508  1.00 169.91 ? 404  SER E OG  1 
ATOM   14596 N  N   . PHE E  1 405 ? -3.124  -46.783 -37.337  1.00 186.30 ? 405  PHE E N   1 
ATOM   14597 C  CA  . PHE E  1 405 ? -4.254  -47.412 -38.015  1.00 178.31 ? 405  PHE E CA  1 
ATOM   14598 C  C   . PHE E  1 405 ? -4.008  -48.906 -38.180  1.00 165.72 ? 405  PHE E C   1 
ATOM   14599 O  O   . PHE E  1 405 ? -3.057  -49.315 -38.849  1.00 164.48 ? 405  PHE E O   1 
ATOM   14600 C  CB  . PHE E  1 405 ? -4.478  -46.737 -39.372  1.00 180.44 ? 405  PHE E CB  1 
ATOM   14601 C  CG  . PHE E  1 405 ? -5.571  -47.357 -40.204  1.00 176.16 ? 405  PHE E CG  1 
ATOM   14602 C  CD1 . PHE E  1 405 ? -6.891  -46.980 -40.031  1.00 180.95 ? 405  PHE E CD1 1 
ATOM   14603 C  CD2 . PHE E  1 405 ? -5.272  -48.283 -41.191  1.00 174.46 ? 405  PHE E CD2 1 
ATOM   14604 C  CE1 . PHE E  1 405 ? -7.892  -47.539 -40.800  1.00 183.12 ? 405  PHE E CE1 1 
ATOM   14605 C  CE2 . PHE E  1 405 ? -6.271  -48.842 -41.965  1.00 176.66 ? 405  PHE E CE2 1 
ATOM   14606 C  CZ  . PHE E  1 405 ? -7.581  -48.469 -41.769  1.00 180.57 ? 405  PHE E CZ  1 
ATOM   14607 N  N   . GLY E  1 406 ? -4.862  -49.720 -37.558  1.00 169.49 ? 406  GLY E N   1 
ATOM   14608 C  CA  . GLY E  1 406 ? -4.742  -51.162 -37.602  1.00 166.86 ? 406  GLY E CA  1 
ATOM   14609 C  C   . GLY E  1 406 ? -4.201  -51.796 -36.339  1.00 178.95 ? 406  GLY E C   1 
ATOM   14610 O  O   . GLY E  1 406 ? -4.209  -53.028 -36.238  1.00 194.88 ? 406  GLY E O   1 
ATOM   14611 N  N   . TYR E  1 407 ? -3.747  -50.990 -35.374  1.00 199.28 ? 407  TYR E N   1 
ATOM   14612 C  CA  . TYR E  1 407 ? -3.092  -51.527 -34.184  1.00 188.62 ? 407  TYR E CA  1 
ATOM   14613 C  C   . TYR E  1 407 ? -3.965  -52.530 -33.438  1.00 176.50 ? 407  TYR E C   1 
ATOM   14614 O  O   . TYR E  1 407 ? -3.440  -53.457 -32.813  1.00 167.85 ? 407  TYR E O   1 
ATOM   14615 C  CB  . TYR E  1 407 ? -2.688  -50.384 -33.259  1.00 180.48 ? 407  TYR E CB  1 
ATOM   14616 C  CG  . TYR E  1 407 ? -1.944  -50.841 -32.031  1.00 186.18 ? 407  TYR E CG  1 
ATOM   14617 C  CD1 . TYR E  1 407 ? -0.582  -51.103 -32.080  1.00 179.86 ? 407  TYR E CD1 1 
ATOM   14618 C  CD2 . TYR E  1 407 ? -2.600  -51.003 -30.818  1.00 204.45 ? 407  TYR E CD2 1 
ATOM   14619 C  CE1 . TYR E  1 407 ? 0.107   -51.521 -30.956  1.00 191.89 ? 407  TYR E CE1 1 
ATOM   14620 C  CE2 . TYR E  1 407 ? -1.921  -51.418 -29.688  1.00 210.21 ? 407  TYR E CE2 1 
ATOM   14621 C  CZ  . TYR E  1 407 ? -0.568  -51.675 -29.762  1.00 206.87 ? 407  TYR E CZ  1 
ATOM   14622 O  OH  . TYR E  1 407 ? 0.105   -52.088 -28.636  1.00 205.25 ? 407  TYR E OH  1 
ATOM   14623 N  N   . SER E  1 408 ? -5.286  -52.370 -33.484  1.00 177.97 ? 408  SER E N   1 
ATOM   14624 C  CA  . SER E  1 408 ? -6.202  -53.362 -32.936  1.00 180.92 ? 408  SER E CA  1 
ATOM   14625 C  C   . SER E  1 408 ? -7.367  -53.544 -33.896  1.00 186.16 ? 408  SER E C   1 
ATOM   14626 O  O   . SER E  1 408 ? -7.810  -52.580 -34.525  1.00 194.88 ? 408  SER E O   1 
ATOM   14627 C  CB  . SER E  1 408 ? -6.722  -52.948 -31.559  1.00 184.93 ? 408  SER E CB  1 
ATOM   14628 O  OG  . SER E  1 408 ? -7.417  -51.717 -31.639  1.00 193.46 ? 408  SER E OG  1 
ATOM   14629 N  N   . MET E  1 409 ? -7.865  -54.775 -34.007  1.00 175.31 ? 409  MET E N   1 
ATOM   14630 C  CA  . MET E  1 409 ? -9.000  -55.028 -34.883  1.00 173.76 ? 409  MET E CA  1 
ATOM   14631 C  C   . MET E  1 409 ? -9.660  -56.350 -34.517  1.00 190.10 ? 409  MET E C   1 
ATOM   14632 O  O   . MET E  1 409 ? -9.053  -57.214 -33.878  1.00 191.85 ? 409  MET E O   1 
ATOM   14633 C  CB  . MET E  1 409 ? -8.571  -55.022 -36.353  1.00 169.21 ? 409  MET E CB  1 
ATOM   14634 C  CG  . MET E  1 409 ? -7.305  -55.797 -36.629  1.00 167.82 ? 409  MET E CG  1 
ATOM   14635 S  SD  . MET E  1 409 ? -6.718  -55.500 -38.301  1.00 168.88 ? 409  MET E SD  1 
ATOM   14636 C  CE  . MET E  1 409 ? -5.502  -56.798 -38.465  1.00 179.57 ? 409  MET E CE  1 
ATOM   14637 N  N   . LYS E  1 410 ? -10.919 -56.491 -34.938  1.00 200.26 ? 410  LYS E N   1 
ATOM   14638 C  CA  . LYS E  1 410 ? -11.704 -57.697 -34.698  1.00 203.43 ? 410  LYS E CA  1 
ATOM   14639 C  C   . LYS E  1 410 ? -12.672 -57.920 -35.853  1.00 193.73 ? 410  LYS E C   1 
ATOM   14640 O  O   . LYS E  1 410 ? -13.243 -56.963 -36.382  1.00 191.26 ? 410  LYS E O   1 
ATOM   14641 C  CB  . LYS E  1 410 ? -12.482 -57.612 -33.382  1.00 216.22 ? 410  LYS E CB  1 
ATOM   14642 C  CG  . LYS E  1 410 ? -13.119 -58.925 -32.973  1.00 224.63 ? 410  LYS E CG  1 
ATOM   14643 C  CD  . LYS E  1 410 ? -12.071 -59.920 -32.502  1.00 229.15 ? 410  LYS E CD  1 
ATOM   14644 C  CE  . LYS E  1 410 ? -12.520 -61.355 -32.742  1.00 234.04 ? 410  LYS E CE  1 
ATOM   14645 N  NZ  . LYS E  1 410 ? -13.896 -61.610 -32.228  1.00 247.78 ? 410  LYS E NZ  1 
ATOM   14646 N  N   . GLY E  1 411 ? -12.838 -59.182 -36.249  1.00 197.00 ? 411  GLY E N   1 
ATOM   14647 C  CA  . GLY E  1 411 ? -13.757 -59.522 -37.318  1.00 201.22 ? 411  GLY E CA  1 
ATOM   14648 C  C   . GLY E  1 411 ? -14.694 -60.677 -37.023  1.00 209.12 ? 411  GLY E C   1 
ATOM   14649 O  O   . GLY E  1 411 ? -14.942 -61.014 -35.859  1.00 210.49 ? 411  GLY E O   1 
ATOM   14650 N  N   . ALA E  1 412 ? -15.204 -61.293 -38.093  1.00 205.66 ? 412  ALA E N   1 
ATOM   14651 C  CA  . ALA E  1 412 ? -16.052 -62.481 -38.036  1.00 211.10 ? 412  ALA E CA  1 
ATOM   14652 C  C   . ALA E  1 412 ? -17.436 -62.197 -37.459  1.00 216.62 ? 412  ALA E C   1 
ATOM   14653 O  O   . ALA E  1 412 ? -18.067 -63.095 -36.896  1.00 229.50 ? 412  ALA E O   1 
ATOM   14654 C  CB  . ALA E  1 412 ? -15.380 -63.614 -37.251  1.00 211.94 ? 412  ALA E CB  1 
ATOM   14655 N  N   . THR E  1 413 ? -17.922 -60.961 -37.586  1.00 208.79 ? 413  THR E N   1 
ATOM   14656 C  CA  . THR E  1 413 ? -19.262 -60.593 -37.138  1.00 207.88 ? 413  THR E CA  1 
ATOM   14657 C  C   . THR E  1 413 ? -19.977 -59.790 -38.218  1.00 209.60 ? 413  THR E C   1 
ATOM   14658 O  O   . THR E  1 413 ? -19.455 -58.773 -38.683  1.00 212.77 ? 413  THR E O   1 
ATOM   14659 C  CB  . THR E  1 413 ? -19.214 -59.791 -35.838  1.00 204.93 ? 413  THR E CB  1 
ATOM   14660 O  OG1 . THR E  1 413 ? -18.665 -60.601 -34.792  1.00 210.90 ? 413  THR E OG1 1 
ATOM   14661 C  CG2 . THR E  1 413 ? -20.612 -59.354 -35.443  1.00 208.34 ? 413  THR E CG2 1 
ATOM   14662 N  N   . ASP E  1 414 ? -21.179 -60.239 -38.599  1.00 217.69 ? 414  ASP E N   1 
ATOM   14663 C  CA  . ASP E  1 414 ? -21.978 -59.594 -39.648  1.00 222.81 ? 414  ASP E CA  1 
ATOM   14664 C  C   . ASP E  1 414 ? -22.905 -58.549 -39.031  1.00 226.99 ? 414  ASP E C   1 
ATOM   14665 O  O   . ASP E  1 414 ? -24.032 -58.843 -38.624  1.00 221.40 ? 414  ASP E O   1 
ATOM   14666 C  CB  . ASP E  1 414 ? -22.762 -60.638 -40.430  1.00 222.05 ? 414  ASP E CB  1 
ATOM   14667 C  CG  . ASP E  1 414 ? -23.486 -60.046 -41.616  1.00 229.57 ? 414  ASP E CG  1 
ATOM   14668 O  OD1 . ASP E  1 414 ? -23.086 -58.954 -42.079  1.00 229.53 ? 414  ASP E OD1 1 
ATOM   14669 O  OD2 . ASP E  1 414 ? -24.454 -60.677 -42.085  1.00 240.58 ? 414  ASP E OD2 1 
ATOM   14670 N  N   . ILE E  1 415 ? -22.431 -57.301 -38.989  1.00 231.58 ? 415  ILE E N   1 
ATOM   14671 C  CA  . ILE E  1 415 ? -23.124 -56.250 -38.245  1.00 219.61 ? 415  ILE E CA  1 
ATOM   14672 C  C   . ILE E  1 415 ? -24.312 -55.670 -38.997  1.00 220.13 ? 415  ILE E C   1 
ATOM   14673 O  O   . ILE E  1 415 ? -25.192 -55.066 -38.374  1.00 224.92 ? 415  ILE E O   1 
ATOM   14674 C  CB  . ILE E  1 415 ? -22.154 -55.111 -37.884  1.00 230.06 ? 415  ILE E CB  1 
ATOM   14675 C  CG1 . ILE E  1 415 ? -22.663 -54.331 -36.674  1.00 228.56 ? 415  ILE E CG1 1 
ATOM   14676 C  CG2 . ILE E  1 415 ? -21.974 -54.163 -39.058  1.00 230.77 ? 415  ILE E CG2 1 
ATOM   14677 C  CD1 . ILE E  1 415 ? -21.733 -53.246 -36.206  1.00 232.47 ? 415  ILE E CD1 1 
ATOM   14678 N  N   . ASP E  1 416 ? -24.384 -55.844 -40.313  1.00 224.32 ? 416  ASP E N   1 
ATOM   14679 C  CA  . ASP E  1 416 ? -25.473 -55.274 -41.092  1.00 231.10 ? 416  ASP E CA  1 
ATOM   14680 C  C   . ASP E  1 416 ? -26.363 -56.341 -41.706  1.00 235.32 ? 416  ASP E C   1 
ATOM   14681 O  O   . ASP E  1 416 ? -27.219 -56.018 -42.538  1.00 240.42 ? 416  ASP E O   1 
ATOM   14682 C  CB  . ASP E  1 416 ? -24.916 -54.347 -42.176  1.00 243.30 ? 416  ASP E CB  1 
ATOM   14683 C  CG  . ASP E  1 416 ? -24.077 -55.082 -43.200  1.00 251.30 ? 416  ASP E CG  1 
ATOM   14684 O  OD1 . ASP E  1 416 ? -23.539 -56.157 -42.866  1.00 244.91 ? 416  ASP E OD1 1 
ATOM   14685 O  OD2 . ASP E  1 416 ? -23.946 -54.580 -44.337  1.00 265.45 ? 416  ASP E OD2 1 
ATOM   14686 N  N   . LYS E  1 417 ? -26.192 -57.601 -41.299  1.00 229.14 ? 417  LYS E N   1 
ATOM   14687 C  CA  . LYS E  1 417 ? -27.037 -58.710 -41.748  1.00 232.06 ? 417  LYS E CA  1 
ATOM   14688 C  C   . LYS E  1 417 ? -27.097 -58.808 -43.269  1.00 237.96 ? 417  LYS E C   1 
ATOM   14689 O  O   . LYS E  1 417 ? -28.124 -59.182 -43.840  1.00 240.96 ? 417  LYS E O   1 
ATOM   14690 C  CB  . LYS E  1 417 ? -28.444 -58.595 -41.157  1.00 244.37 ? 417  LYS E CB  1 
ATOM   14691 C  CG  . LYS E  1 417 ? -28.482 -58.617 -39.634  1.00 245.42 ? 417  LYS E CG  1 
ATOM   14692 C  CD  . LYS E  1 417 ? -28.156 -59.995 -39.071  1.00 232.42 ? 417  LYS E CD  1 
ATOM   14693 C  CE  . LYS E  1 417 ? -29.180 -61.030 -39.518  1.00 235.34 ? 417  LYS E CE  1 
ATOM   14694 N  NZ  . LYS E  1 417 ? -28.896 -62.386 -38.971  1.00 234.24 ? 417  LYS E NZ  1 
ATOM   14695 N  N   . ASN E  1 418 ? -25.995 -58.480 -43.942  1.00 264.27 ? 418  ASN E N   1 
ATOM   14696 C  CA  . ASN E  1 418 ? -25.930 -58.536 -45.398  1.00 266.05 ? 418  ASN E CA  1 
ATOM   14697 C  C   . ASN E  1 418 ? -25.397 -59.869 -45.901  1.00 250.44 ? 418  ASN E C   1 
ATOM   14698 O  O   . ASN E  1 418 ? -25.245 -60.043 -47.115  1.00 243.16 ? 418  ASN E O   1 
ATOM   14699 C  CB  . ASN E  1 418 ? -25.069 -57.393 -45.954  1.00 266.91 ? 418  ASN E CB  1 
ATOM   14700 C  CG  . ASN E  1 418 ? -23.577 -57.707 -45.926  1.00 241.43 ? 418  ASN E CG  1 
ATOM   14701 O  OD1 . ASN E  1 418 ? -23.084 -58.376 -45.018  1.00 227.99 ? 418  ASN E OD1 1 
ATOM   14702 N  ND2 . ASN E  1 418 ? -22.851 -57.209 -46.926  1.00 237.05 ? 418  ASN E ND2 1 
ATOM   14703 N  N   . GLY E  1 419 ? -25.088 -60.801 -44.999  1.00 237.89 ? 419  GLY E N   1 
ATOM   14704 C  CA  . GLY E  1 419 ? -24.576 -62.104 -45.364  1.00 237.69 ? 419  GLY E CA  1 
ATOM   14705 C  C   . GLY E  1 419 ? -23.071 -62.230 -45.331  1.00 246.60 ? 419  GLY E C   1 
ATOM   14706 O  O   . GLY E  1 419 ? -22.557 -63.329 -45.568  1.00 254.09 ? 419  GLY E O   1 
ATOM   14707 N  N   . TYR E  1 420 ? -22.349 -61.148 -45.037  1.00 243.87 ? 420  TYR E N   1 
ATOM   14708 C  CA  . TYR E  1 420 ? -20.896 -61.159 -45.047  1.00 240.87 ? 420  TYR E CA  1 
ATOM   14709 C  C   . TYR E  1 420 ? -20.335 -60.579 -43.754  1.00 232.79 ? 420  TYR E C   1 
ATOM   14710 O  O   . TYR E  1 420 ? -20.842 -59.564 -43.256  1.00 250.74 ? 420  TYR E O   1 
ATOM   14711 C  CB  . TYR E  1 420 ? -20.362 -60.359 -46.247  1.00 242.59 ? 420  TYR E CB  1 
ATOM   14712 C  CG  . TYR E  1 420 ? -20.796 -60.903 -47.592  1.00 236.35 ? 420  TYR E CG  1 
ATOM   14713 C  CD1 . TYR E  1 420 ? -22.043 -60.594 -48.125  1.00 236.85 ? 420  TYR E CD1 1 
ATOM   14714 C  CD2 . TYR E  1 420 ? -19.956 -61.727 -48.329  1.00 224.22 ? 420  TYR E CD2 1 
ATOM   14715 C  CE1 . TYR E  1 420 ? -22.438 -61.092 -49.350  1.00 232.77 ? 420  TYR E CE1 1 
ATOM   14716 C  CE2 . TYR E  1 420 ? -20.342 -62.227 -49.552  1.00 222.58 ? 420  TYR E CE2 1 
ATOM   14717 C  CZ  . TYR E  1 420 ? -21.582 -61.906 -50.059  1.00 229.47 ? 420  TYR E CZ  1 
ATOM   14718 O  OH  . TYR E  1 420 ? -21.962 -62.410 -51.281  1.00 244.51 ? 420  TYR E OH  1 
ATOM   14719 N  N   . PRO E  1 421 ? -19.302 -61.204 -43.179  1.00 206.38 ? 421  PRO E N   1 
ATOM   14720 C  CA  . PRO E  1 421 ? -18.701 -60.656 -41.956  1.00 206.39 ? 421  PRO E CA  1 
ATOM   14721 C  C   . PRO E  1 421 ? -17.923 -59.381 -42.244  1.00 197.57 ? 421  PRO E C   1 
ATOM   14722 O  O   . PRO E  1 421 ? -17.295 -59.237 -43.294  1.00 195.38 ? 421  PRO E O   1 
ATOM   14723 C  CB  . PRO E  1 421 ? -17.779 -61.783 -41.475  1.00 202.84 ? 421  PRO E CB  1 
ATOM   14724 C  CG  . PRO E  1 421 ? -17.438 -62.530 -42.704  1.00 204.80 ? 421  PRO E CG  1 
ATOM   14725 C  CD  . PRO E  1 421 ? -18.677 -62.480 -43.567  1.00 206.86 ? 421  PRO E CD  1 
ATOM   14726 N  N   . ASP E  1 422 ? -17.976 -58.448 -41.295  1.00 210.68 ? 422  ASP E N   1 
ATOM   14727 C  CA  . ASP E  1 422 ? -17.392 -57.121 -41.430  1.00 203.94 ? 422  ASP E CA  1 
ATOM   14728 C  C   . ASP E  1 422 ? -16.178 -57.001 -40.510  1.00 206.52 ? 422  ASP E C   1 
ATOM   14729 O  O   . ASP E  1 422 ? -15.807 -57.943 -39.804  1.00 206.26 ? 422  ASP E O   1 
ATOM   14730 C  CB  . ASP E  1 422 ? -18.435 -56.042 -41.127  1.00 205.37 ? 422  ASP E CB  1 
ATOM   14731 C  CG  . ASP E  1 422 ? -19.744 -56.272 -41.868  1.00 222.41 ? 422  ASP E CG  1 
ATOM   14732 O  OD1 . ASP E  1 422 ? -20.570 -57.069 -41.376  1.00 229.38 ? 422  ASP E OD1 1 
ATOM   14733 O  OD2 . ASP E  1 422 ? -19.946 -55.676 -42.948  1.00 232.74 ? 422  ASP E OD2 1 
ATOM   14734 N  N   . LEU E  1 423 ? -15.553 -55.822 -40.529  1.00 212.78 ? 423  LEU E N   1 
ATOM   14735 C  CA  . LEU E  1 423 ? -14.267 -55.615 -39.875  1.00 204.14 ? 423  LEU E CA  1 
ATOM   14736 C  C   . LEU E  1 423 ? -14.183 -54.234 -39.242  1.00 214.27 ? 423  LEU E C   1 
ATOM   14737 O  O   . LEU E  1 423 ? -14.427 -53.226 -39.911  1.00 221.13 ? 423  LEU E O   1 
ATOM   14738 C  CB  . LEU E  1 423 ? -13.128 -55.794 -40.881  1.00 200.63 ? 423  LEU E CB  1 
ATOM   14739 C  CG  . LEU E  1 423 ? -11.758 -55.323 -40.409  1.00 202.04 ? 423  LEU E CG  1 
ATOM   14740 C  CD1 . LEU E  1 423 ? -11.279 -56.171 -39.243  1.00 220.60 ? 423  LEU E CD1 1 
ATOM   14741 C  CD2 . LEU E  1 423 ? -10.767 -55.356 -41.562  1.00 197.53 ? 423  LEU E CD2 1 
ATOM   14742 N  N   . ILE E  1 424 ? -13.824 -54.189 -37.957  1.00 215.14 ? 424  ILE E N   1 
ATOM   14743 C  CA  . ILE E  1 424 ? -13.552 -52.938 -37.252  1.00 215.17 ? 424  ILE E CA  1 
ATOM   14744 C  C   . ILE E  1 424 ? -12.046 -52.762 -37.128  1.00 208.64 ? 424  ILE E C   1 
ATOM   14745 O  O   . ILE E  1 424 ? -11.334 -53.700 -36.747  1.00 186.71 ? 424  ILE E O   1 
ATOM   14746 C  CB  . ILE E  1 424 ? -14.219 -52.909 -35.866  1.00 215.81 ? 424  ILE E CB  1 
ATOM   14747 C  CG1 . ILE E  1 424 ? -15.726 -53.141 -35.984  1.00 248.71 ? 424  ILE E CG1 1 
ATOM   14748 C  CG2 . ILE E  1 424 ? -13.951 -51.580 -35.173  1.00 199.58 ? 424  ILE E CG2 1 
ATOM   14749 C  CD1 . ILE E  1 424 ? -16.418 -53.324 -34.647  1.00 260.43 ? 424  ILE E CD1 1 
ATOM   14750 N  N   . VAL E  1 425 ? -11.562 -51.556 -37.433  1.00 223.10 ? 425  VAL E N   1 
ATOM   14751 C  CA  . VAL E  1 425 ? -10.140 -51.225 -37.382  1.00 221.16 ? 425  VAL E CA  1 
ATOM   14752 C  C   . VAL E  1 425 ? -9.951  -50.003 -36.488  1.00 216.39 ? 425  VAL E C   1 
ATOM   14753 O  O   . VAL E  1 425 ? -10.498 -48.930 -36.771  1.00 211.21 ? 425  VAL E O   1 
ATOM   14754 C  CB  . VAL E  1 425 ? -9.564  -50.963 -38.782  1.00 208.50 ? 425  VAL E CB  1 
ATOM   14755 C  CG1 . VAL E  1 425 ? -8.106  -50.554 -38.684  1.00 210.31 ? 425  VAL E CG1 1 
ATOM   14756 C  CG2 . VAL E  1 425 ? -9.729  -52.191 -39.665  1.00 191.76 ? 425  VAL E CG2 1 
ATOM   14757 N  N   . GLY E  1 426 ? -9.173  -50.165 -35.419  1.00 218.15 ? 426  GLY E N   1 
ATOM   14758 C  CA  . GLY E  1 426 ? -8.909  -49.074 -34.496  1.00 213.33 ? 426  GLY E CA  1 
ATOM   14759 C  C   . GLY E  1 426 ? -7.652  -48.302 -34.865  1.00 217.26 ? 426  GLY E C   1 
ATOM   14760 O  O   . GLY E  1 426 ? -6.670  -48.869 -35.338  1.00 226.45 ? 426  GLY E O   1 
ATOM   14761 N  N   . ALA E  1 427 ? -7.694  -46.986 -34.626  1.00 210.11 ? 427  ALA E N   1 
ATOM   14762 C  CA  . ALA E  1 427 ? -6.545  -46.101 -34.840  1.00 199.06 ? 427  ALA E CA  1 
ATOM   14763 C  C   . ALA E  1 427 ? -6.463  -45.148 -33.646  1.00 211.24 ? 427  ALA E C   1 
ATOM   14764 O  O   . ALA E  1 427 ? -6.925  -44.006 -33.699  1.00 232.93 ? 427  ALA E O   1 
ATOM   14765 C  CB  . ALA E  1 427 ? -6.661  -45.348 -36.164  1.00 191.15 ? 427  ALA E CB  1 
ATOM   14766 N  N   . PHE E  1 428 ? -5.852  -45.619 -32.558  1.00 198.07 ? 428  PHE E N   1 
ATOM   14767 C  CA  . PHE E  1 428 ? -5.888  -44.862 -31.313  1.00 192.09 ? 428  PHE E CA  1 
ATOM   14768 C  C   . PHE E  1 428 ? -5.062  -43.583 -31.379  1.00 188.50 ? 428  PHE E C   1 
ATOM   14769 O  O   . PHE E  1 428 ? -5.333  -42.649 -30.618  1.00 191.08 ? 428  PHE E O   1 
ATOM   14770 C  CB  . PHE E  1 428 ? -5.416  -45.745 -30.156  1.00 191.76 ? 428  PHE E CB  1 
ATOM   14771 C  CG  . PHE E  1 428 ? -3.957  -46.078 -30.208  1.00 182.59 ? 428  PHE E CG  1 
ATOM   14772 C  CD1 . PHE E  1 428 ? -3.009  -45.227 -29.661  1.00 179.44 ? 428  PHE E CD1 1 
ATOM   14773 C  CD2 . PHE E  1 428 ? -3.531  -47.237 -30.823  1.00 180.39 ? 428  PHE E CD2 1 
ATOM   14774 C  CE1 . PHE E  1 428 ? -1.666  -45.530 -29.726  1.00 176.88 ? 428  PHE E CE1 1 
ATOM   14775 C  CE2 . PHE E  1 428 ? -2.190  -47.550 -30.883  1.00 181.75 ? 428  PHE E CE2 1 
ATOM   14776 C  CZ  . PHE E  1 428 ? -1.254  -46.694 -30.335  1.00 175.88 ? 428  PHE E CZ  1 
ATOM   14777 N  N   . GLY E  1 429 ? -4.063  -43.515 -32.263  1.00 181.70 ? 429  GLY E N   1 
ATOM   14778 C  CA  . GLY E  1 429 ? -3.219  -42.335 -32.336  1.00 184.11 ? 429  GLY E CA  1 
ATOM   14779 C  C   . GLY E  1 429 ? -3.945  -41.088 -32.789  1.00 192.37 ? 429  GLY E C   1 
ATOM   14780 O  O   . GLY E  1 429 ? -3.485  -39.976 -32.509  1.00 192.34 ? 429  GLY E O   1 
ATOM   14781 N  N   . VAL E  1 430 ? -5.071  -41.251 -33.482  1.00 214.16 ? 430  VAL E N   1 
ATOM   14782 C  CA  . VAL E  1 430 ? -5.922  -40.151 -33.907  1.00 222.43 ? 430  VAL E CA  1 
ATOM   14783 C  C   . VAL E  1 430 ? -7.320  -40.264 -33.314  1.00 220.54 ? 430  VAL E C   1 
ATOM   14784 O  O   . VAL E  1 430 ? -8.233  -39.564 -33.754  1.00 238.69 ? 430  VAL E O   1 
ATOM   14785 C  CB  . VAL E  1 430 ? -5.985  -40.053 -35.444  1.00 218.81 ? 430  VAL E CB  1 
ATOM   14786 C  CG1 . VAL E  1 430 ? -4.659  -39.555 -36.011  1.00 205.85 ? 430  VAL E CG1 1 
ATOM   14787 C  CG2 . VAL E  1 430 ? -6.355  -41.397 -36.045  1.00 222.11 ? 430  VAL E CG2 1 
ATOM   14788 N  N   . ASP E  1 431 ? -7.502  -41.149 -32.332  1.00 208.26 ? 431  ASP E N   1 
ATOM   14789 C  CA  . ASP E  1 431 ? -8.763  -41.341 -31.614  1.00 213.45 ? 431  ASP E CA  1 
ATOM   14790 C  C   . ASP E  1 431 ? -9.918  -41.611 -32.578  1.00 218.74 ? 431  ASP E C   1 
ATOM   14791 O  O   . ASP E  1 431 ? -10.921 -40.893 -32.605  1.00 237.05 ? 431  ASP E O   1 
ATOM   14792 C  CB  . ASP E  1 431 ? -9.069  -40.130 -30.729  1.00 221.98 ? 431  ASP E CB  1 
ATOM   14793 C  CG  . ASP E  1 431 ? -7.928  -39.786 -29.790  1.00 212.21 ? 431  ASP E CG  1 
ATOM   14794 O  OD1 . ASP E  1 431 ? -7.712  -40.531 -28.813  1.00 201.80 ? 431  ASP E OD1 1 
ATOM   14795 O  OD2 . ASP E  1 431 ? -7.236  -38.779 -30.038  1.00 218.70 ? 431  ASP E OD2 1 
ATOM   14796 N  N   . ARG E  1 432 ? -9.776  -42.685 -33.354  1.00 205.92 ? 432  ARG E N   1 
ATOM   14797 C  CA  . ARG E  1 432 ? -10.753 -42.980 -34.389  1.00 209.10 ? 432  ARG E CA  1 
ATOM   14798 C  C   . ARG E  1 432 ? -10.924 -44.484 -34.559  1.00 219.33 ? 432  ARG E C   1 
ATOM   14799 O  O   . ARG E  1 432 ? -9.991  -45.267 -34.353  1.00 241.35 ? 432  ARG E O   1 
ATOM   14800 C  CB  . ARG E  1 432 ? -10.338 -42.348 -35.717  1.00 212.33 ? 432  ARG E CB  1 
ATOM   14801 C  CG  . ARG E  1 432 ? -11.490 -41.808 -36.507  1.00 219.88 ? 432  ARG E CG  1 
ATOM   14802 C  CD  . ARG E  1 432 ? -11.913 -40.502 -35.903  1.00 227.43 ? 432  ARG E CD  1 
ATOM   14803 N  NE  . ARG E  1 432 ? -10.844 -39.507 -35.915  1.00 228.00 ? 432  ARG E NE  1 
ATOM   14804 C  CZ  . ARG E  1 432 ? -10.778 -38.497 -36.778  1.00 240.30 ? 432  ARG E CZ  1 
ATOM   14805 N  NH1 . ARG E  1 432 ? -11.719 -38.348 -37.703  1.00 254.65 ? 432  ARG E NH1 1 
ATOM   14806 N  NH2 . ARG E  1 432 ? -9.772  -37.633 -36.718  1.00 235.35 ? 432  ARG E NH2 1 
ATOM   14807 N  N   . ALA E  1 433 ? -12.132 -44.876 -34.953  1.00 206.14 ? 433  ALA E N   1 
ATOM   14808 C  CA  . ALA E  1 433 ? -12.437 -46.245 -35.338  1.00 202.93 ? 433  ALA E CA  1 
ATOM   14809 C  C   . ALA E  1 433 ? -13.269 -46.221 -36.610  1.00 207.09 ? 433  ALA E C   1 
ATOM   14810 O  O   . ALA E  1 433 ? -14.169 -45.389 -36.757  1.00 213.96 ? 433  ALA E O   1 
ATOM   14811 C  CB  . ALA E  1 433 ? -13.177 -46.988 -34.224  1.00 209.98 ? 433  ALA E CB  1 
ATOM   14812 N  N   . ILE E  1 434 ? -12.958 -47.123 -37.537  1.00 201.61 ? 434  ILE E N   1 
ATOM   14813 C  CA  . ILE E  1 434 ? -13.569 -47.124 -38.859  1.00 214.77 ? 434  ILE E CA  1 
ATOM   14814 C  C   . ILE E  1 434 ? -14.167 -48.496 -39.139  1.00 214.77 ? 434  ILE E C   1 
ATOM   14815 O  O   . ILE E  1 434 ? -13.492 -49.518 -38.976  1.00 204.79 ? 434  ILE E O   1 
ATOM   14816 C  CB  . ILE E  1 434 ? -12.554 -46.740 -39.950  1.00 219.01 ? 434  ILE E CB  1 
ATOM   14817 C  CG1 . ILE E  1 434 ? -11.863 -45.424 -39.584  1.00 224.51 ? 434  ILE E CG1 1 
ATOM   14818 C  CG2 . ILE E  1 434 ? -13.254 -46.616 -41.293  1.00 229.70 ? 434  ILE E CG2 1 
ATOM   14819 C  CD1 . ILE E  1 434 ? -10.539 -45.602 -38.850  1.00 216.05 ? 434  ILE E CD1 1 
ATOM   14820 N  N   . LEU E  1 435 ? -15.430 -48.516 -39.564  1.00 227.14 ? 435  LEU E N   1 
ATOM   14821 C  CA  . LEU E  1 435 ? -16.130 -49.742 -39.932  1.00 225.46 ? 435  LEU E CA  1 
ATOM   14822 C  C   . LEU E  1 435 ? -16.106 -49.922 -41.447  1.00 250.56 ? 435  LEU E C   1 
ATOM   14823 O  O   . LEU E  1 435 ? -16.640 -49.086 -42.183  1.00 267.68 ? 435  LEU E O   1 
ATOM   14824 C  CB  . LEU E  1 435 ? -17.573 -49.718 -39.428  1.00 219.67 ? 435  LEU E CB  1 
ATOM   14825 C  CG  . LEU E  1 435 ? -18.445 -50.915 -39.817  1.00 216.19 ? 435  LEU E CG  1 
ATOM   14826 C  CD1 . LEU E  1 435 ? -17.990 -52.181 -39.109  1.00 212.23 ? 435  LEU E CD1 1 
ATOM   14827 C  CD2 . LEU E  1 435 ? -19.909 -50.633 -39.528  1.00 220.90 ? 435  LEU E CD2 1 
ATOM   14828 N  N   . TYR E  1 436 ? -15.500 -51.015 -41.907  1.00 246.08 ? 436  TYR E N   1 
ATOM   14829 C  CA  . TYR E  1 436 ? -15.510 -51.381 -43.317  1.00 250.59 ? 436  TYR E CA  1 
ATOM   14830 C  C   . TYR E  1 436 ? -16.516 -52.501 -43.550  1.00 238.09 ? 436  TYR E C   1 
ATOM   14831 O  O   . TYR E  1 436 ? -16.447 -53.552 -42.905  1.00 237.77 ? 436  TYR E O   1 
ATOM   14832 C  CB  . TYR E  1 436 ? -14.118 -51.807 -43.789  1.00 248.89 ? 436  TYR E CB  1 
ATOM   14833 C  CG  . TYR E  1 436 ? -13.107 -50.681 -43.826  1.00 241.73 ? 436  TYR E CG  1 
ATOM   14834 C  CD1 . TYR E  1 436 ? -13.041 -49.820 -44.915  1.00 240.12 ? 436  TYR E CD1 1 
ATOM   14835 C  CD2 . TYR E  1 436 ? -12.219 -50.479 -42.775  1.00 240.73 ? 436  TYR E CD2 1 
ATOM   14836 C  CE1 . TYR E  1 436 ? -12.120 -48.792 -44.960  1.00 239.55 ? 436  TYR E CE1 1 
ATOM   14837 C  CE2 . TYR E  1 436 ? -11.292 -49.449 -42.811  1.00 240.52 ? 436  TYR E CE2 1 
ATOM   14838 C  CZ  . TYR E  1 436 ? -11.249 -48.610 -43.907  1.00 236.35 ? 436  TYR E CZ  1 
ATOM   14839 O  OH  . TYR E  1 436 ? -10.330 -47.585 -43.950  1.00 249.78 ? 436  TYR E OH  1 
ATOM   14840 N  N   . ARG E  1 437 ? -17.441 -52.274 -44.476  1.00 218.50 ? 437  ARG E N   1 
ATOM   14841 C  CA  . ARG E  1 437 ? -18.490 -53.231 -44.784  1.00 213.19 ? 437  ARG E CA  1 
ATOM   14842 C  C   . ARG E  1 437 ? -18.094 -54.052 -46.002  1.00 216.50 ? 437  ARG E C   1 
ATOM   14843 O  O   . ARG E  1 437 ? -17.592 -53.510 -46.990  1.00 227.27 ? 437  ARG E O   1 
ATOM   14844 C  CB  . ARG E  1 437 ? -19.815 -52.513 -45.036  1.00 219.08 ? 437  ARG E CB  1 
ATOM   14845 C  CG  . ARG E  1 437 ? -20.353 -51.786 -43.821  1.00 221.19 ? 437  ARG E CG  1 
ATOM   14846 C  CD  . ARG E  1 437 ? -21.701 -51.165 -44.119  1.00 229.95 ? 437  ARG E CD  1 
ATOM   14847 N  NE  . ARG E  1 437 ? -21.575 -50.030 -45.030  1.00 242.97 ? 437  ARG E NE  1 
ATOM   14848 C  CZ  . ARG E  1 437 ? -22.463 -49.728 -45.971  1.00 252.87 ? 437  ARG E CZ  1 
ATOM   14849 N  NH1 . ARG E  1 437 ? -23.534 -50.489 -46.135  1.00 256.81 ? 437  ARG E NH1 1 
ATOM   14850 N  NH2 . ARG E  1 437 ? -22.276 -48.677 -46.760  1.00 248.91 ? 437  ARG E NH2 1 
ATOM   14851 N  N   . ALA E  1 438 ? -18.305 -55.363 -45.918  1.00 214.94 ? 438  ALA E N   1 
ATOM   14852 C  CA  . ALA E  1 438 ? -17.982 -56.254 -47.023  1.00 224.91 ? 438  ALA E CA  1 
ATOM   14853 C  C   . ALA E  1 438 ? -19.051 -56.155 -48.106  1.00 241.76 ? 438  ALA E C   1 
ATOM   14854 O  O   . ALA E  1 438 ? -20.243 -56.323 -47.832  1.00 253.88 ? 438  ALA E O   1 
ATOM   14855 C  CB  . ALA E  1 438 ? -17.857 -57.693 -46.525  1.00 217.50 ? 438  ALA E CB  1 
ATOM   14856 N  N   . ARG E  1 439 ? -18.620 -55.896 -49.341  1.00 233.90 ? 439  ARG E N   1 
ATOM   14857 C  CA  . ARG E  1 439 ? -19.541 -55.823 -50.467  1.00 216.61 ? 439  ARG E CA  1 
ATOM   14858 C  C   . ARG E  1 439 ? -19.859 -57.227 -50.976  1.00 215.65 ? 439  ARG E C   1 
ATOM   14859 O  O   . ARG E  1 439 ? -18.986 -58.099 -50.976  1.00 212.80 ? 439  ARG E O   1 
ATOM   14860 C  CB  . ARG E  1 439 ? -18.936 -54.986 -51.596  1.00 207.66 ? 439  ARG E CB  1 
ATOM   14861 C  CG  . ARG E  1 439 ? -18.668 -53.544 -51.205  1.00 203.85 ? 439  ARG E CG  1 
ATOM   14862 C  CD  . ARG E  1 439 ? -17.689 -52.844 -52.143  1.00 201.60 ? 439  ARG E CD  1 
ATOM   14863 N  NE  . ARG E  1 439 ? -18.155 -52.766 -53.524  1.00 202.39 ? 439  ARG E NE  1 
ATOM   14864 C  CZ  . ARG E  1 439 ? -17.429 -52.269 -54.521  1.00 208.06 ? 439  ARG E CZ  1 
ATOM   14865 N  NH1 . ARG E  1 439 ? -16.210 -51.806 -54.284  1.00 199.76 ? 439  ARG E NH1 1 
ATOM   14866 N  NH2 . ARG E  1 439 ? -17.919 -52.233 -55.753  1.00 223.75 ? 439  ARG E NH2 1 
ATOM   14867 N  N   . PRO E  1 440 ? -21.096 -57.477 -51.406  1.00 215.97 ? 440  PRO E N   1 
ATOM   14868 C  CA  . PRO E  1 440 ? -21.429 -58.798 -51.952  1.00 220.74 ? 440  PRO E CA  1 
ATOM   14869 C  C   . PRO E  1 440 ? -20.601 -59.096 -53.193  1.00 224.77 ? 440  PRO E C   1 
ATOM   14870 O  O   . PRO E  1 440 ? -20.279 -58.208 -53.983  1.00 232.15 ? 440  PRO E O   1 
ATOM   14871 C  CB  . PRO E  1 440 ? -22.923 -58.684 -52.281  1.00 219.15 ? 440  PRO E CB  1 
ATOM   14872 C  CG  . PRO E  1 440 ? -23.416 -57.549 -51.433  1.00 218.56 ? 440  PRO E CG  1 
ATOM   14873 C  CD  . PRO E  1 440 ? -22.271 -56.589 -51.349  1.00 217.73 ? 440  PRO E CD  1 
ATOM   14874 N  N   . VAL E  1 441 ? -20.257 -60.369 -53.363  1.00 213.88 ? 441  VAL E N   1 
ATOM   14875 C  CA  . VAL E  1 441 ? -19.369 -60.809 -54.435  1.00 213.38 ? 441  VAL E CA  1 
ATOM   14876 C  C   . VAL E  1 441 ? -20.207 -61.516 -55.493  1.00 226.88 ? 441  VAL E C   1 
ATOM   14877 O  O   . VAL E  1 441 ? -20.862 -62.525 -55.206  1.00 235.55 ? 441  VAL E O   1 
ATOM   14878 C  CB  . VAL E  1 441 ? -18.251 -61.717 -53.905  1.00 208.75 ? 441  VAL E CB  1 
ATOM   14879 C  CG1 . VAL E  1 441 ? -17.328 -62.145 -55.033  1.00 212.75 ? 441  VAL E CG1 1 
ATOM   14880 C  CG2 . VAL E  1 441 ? -17.463 -60.996 -52.826  1.00 204.69 ? 441  VAL E CG2 1 
ATOM   14881 N  N   . ILE E  1 442 ? -20.199 -60.973 -56.708  1.00 227.35 ? 442  ILE E N   1 
ATOM   14882 C  CA  . ILE E  1 442 ? -20.938 -61.522 -57.841  1.00 219.00 ? 442  ILE E CA  1 
ATOM   14883 C  C   . ILE E  1 442 ? -19.976 -62.345 -58.690  1.00 233.61 ? 442  ILE E C   1 
ATOM   14884 O  O   . ILE E  1 442 ? -18.949 -61.831 -59.151  1.00 241.29 ? 442  ILE E O   1 
ATOM   14885 C  CB  . ILE E  1 442 ? -21.594 -60.413 -58.678  1.00 208.73 ? 442  ILE E CB  1 
ATOM   14886 C  CG1 . ILE E  1 442 ? -22.347 -59.425 -57.785  1.00 205.72 ? 442  ILE E CG1 1 
ATOM   14887 C  CG2 . ILE E  1 442 ? -22.534 -61.011 -59.713  1.00 212.82 ? 442  ILE E CG2 1 
ATOM   14888 C  CD1 . ILE E  1 442 ? -23.514 -60.032 -57.055  1.00 209.19 ? 442  ILE E CD1 1 
ATOM   14889 N  N   . THR E  1 443 ? -20.285 -63.626 -58.876  1.00 240.74 ? 443  THR E N   1 
ATOM   14890 C  CA  . THR E  1 443 ? -19.555 -64.482 -59.805  1.00 242.10 ? 443  THR E CA  1 
ATOM   14891 C  C   . THR E  1 443 ? -20.308 -64.527 -61.131  1.00 254.64 ? 443  THR E C   1 
ATOM   14892 O  O   . THR E  1 443 ? -21.485 -64.905 -61.170  1.00 260.30 ? 443  THR E O   1 
ATOM   14893 C  CB  . THR E  1 443 ? -19.372 -65.885 -59.227  1.00 230.04 ? 443  THR E CB  1 
ATOM   14894 O  OG1 . THR E  1 443 ? -18.496 -65.822 -58.094  1.00 222.95 ? 443  THR E OG1 1 
ATOM   14895 C  CG2 . THR E  1 443 ? -18.772 -66.816 -60.264  1.00 232.22 ? 443  THR E CG2 1 
ATOM   14896 N  N   . VAL E  1 444 ? -19.635 -64.139 -62.211  1.00 252.61 ? 444  VAL E N   1 
ATOM   14897 C  CA  . VAL E  1 444 ? -20.235 -64.054 -63.538  1.00 247.42 ? 444  VAL E CA  1 
ATOM   14898 C  C   . VAL E  1 444 ? -19.568 -65.070 -64.458  1.00 247.57 ? 444  VAL E C   1 
ATOM   14899 O  O   . VAL E  1 444 ? -18.334 -65.152 -64.516  1.00 253.18 ? 444  VAL E O   1 
ATOM   14900 C  CB  . VAL E  1 444 ? -20.126 -62.627 -64.106  1.00 234.31 ? 444  VAL E CB  1 
ATOM   14901 C  CG1 . VAL E  1 444 ? -18.710 -62.082 -63.942  1.00 232.80 ? 444  VAL E CG1 1 
ATOM   14902 C  CG2 . VAL E  1 444 ? -20.537 -62.599 -65.568  1.00 234.88 ? 444  VAL E CG2 1 
ATOM   14903 N  N   . ASN E  1 445 ? -20.383 -65.845 -65.172  1.00 237.54 ? 445  ASN E N   1 
ATOM   14904 C  CA  . ASN E  1 445 ? -19.908 -66.771 -66.199  1.00 235.59 ? 445  ASN E CA  1 
ATOM   14905 C  C   . ASN E  1 445 ? -20.440 -66.304 -67.552  1.00 238.99 ? 445  ASN E C   1 
ATOM   14906 O  O   . ASN E  1 445 ? -21.630 -66.456 -67.851  1.00 242.01 ? 445  ASN E O   1 
ATOM   14907 C  CB  . ASN E  1 445 ? -20.341 -68.201 -65.893  1.00 237.90 ? 445  ASN E CB  1 
ATOM   14908 C  CG  . ASN E  1 445 ? -19.537 -68.828 -64.770  1.00 237.68 ? 445  ASN E CG  1 
ATOM   14909 O  OD1 . ASN E  1 445 ? -20.099 -69.320 -63.795  1.00 236.53 ? 445  ASN E OD1 1 
ATOM   14910 N  ND2 . ASN E  1 445 ? -18.214 -68.822 -64.908  1.00 239.24 ? 445  ASN E ND2 1 
ATOM   14911 N  N   . ALA E  1 446 ? -19.564 -65.709 -68.357  1.00 243.57 ? 446  ALA E N   1 
ATOM   14912 C  CA  . ALA E  1 446 ? -19.930 -65.235 -69.681  1.00 244.61 ? 446  ALA E CA  1 
ATOM   14913 C  C   . ALA E  1 446 ? -19.505 -66.235 -70.753  1.00 249.95 ? 446  ALA E C   1 
ATOM   14914 O  O   . ALA E  1 446 ? -18.474 -66.902 -70.639  1.00 238.30 ? 446  ALA E O   1 
ATOM   14915 C  CB  . ALA E  1 446 ? -19.304 -63.867 -69.962  1.00 240.16 ? 446  ALA E CB  1 
ATOM   14916 N  N   . GLY E  1 447 ? -20.327 -66.337 -71.792  1.00 277.36 ? 447  GLY E N   1 
ATOM   14917 C  CA  . GLY E  1 447 ? -20.047 -67.219 -72.908  1.00 286.51 ? 447  GLY E CA  1 
ATOM   14918 C  C   . GLY E  1 447 ? -20.133 -66.469 -74.221  1.00 285.35 ? 447  GLY E C   1 
ATOM   14919 O  O   . GLY E  1 447 ? -20.806 -65.445 -74.330  1.00 297.85 ? 447  GLY E O   1 
ATOM   14920 N  N   . LEU E  1 448 ? -19.436 -66.994 -75.229  1.00 262.24 ? 448  LEU E N   1 
ATOM   14921 C  CA  . LEU E  1 448 ? -19.436 -66.347 -76.542  1.00 257.83 ? 448  LEU E CA  1 
ATOM   14922 C  C   . LEU E  1 448 ? -19.234 -67.399 -77.625  1.00 263.76 ? 448  LEU E C   1 
ATOM   14923 O  O   . LEU E  1 448 ? -18.179 -68.039 -77.681  1.00 275.23 ? 448  LEU E O   1 
ATOM   14924 C  CB  . LEU E  1 448 ? -18.359 -65.266 -76.612  1.00 253.58 ? 448  LEU E CB  1 
ATOM   14925 C  CG  . LEU E  1 448 ? -18.394 -64.364 -77.847  1.00 255.79 ? 448  LEU E CG  1 
ATOM   14926 C  CD1 . LEU E  1 448 ? -19.742 -63.676 -77.949  1.00 258.12 ? 448  LEU E CD1 1 
ATOM   14927 C  CD2 . LEU E  1 448 ? -17.276 -63.345 -77.774  1.00 255.45 ? 448  LEU E CD2 1 
ATOM   14928 N  N   . GLU E  1 449 ? -20.248 -67.588 -78.467  1.00 264.68 ? 449  GLU E N   1 
ATOM   14929 C  CA  . GLU E  1 449 ? -20.186 -68.504 -79.599  1.00 269.11 ? 449  GLU E CA  1 
ATOM   14930 C  C   . GLU E  1 449 ? -20.288 -67.728 -80.905  1.00 270.01 ? 449  GLU E C   1 
ATOM   14931 O  O   . GLU E  1 449 ? -21.115 -66.820 -81.035  1.00 267.81 ? 449  GLU E O   1 
ATOM   14932 C  CB  . GLU E  1 449 ? -21.302 -69.549 -79.530  1.00 277.72 ? 449  GLU E CB  1 
ATOM   14933 C  CG  . GLU E  1 449 ? -21.272 -70.401 -78.274  1.00 283.90 ? 449  GLU E CG  1 
ATOM   14934 C  CD  . GLU E  1 449 ? -22.460 -71.333 -78.175  1.00 294.33 ? 449  GLU E CD  1 
ATOM   14935 O  OE1 . GLU E  1 449 ? -22.765 -71.792 -77.052  1.00 292.76 ? 449  GLU E OE1 1 
ATOM   14936 O  OE2 . GLU E  1 449 ? -23.094 -71.598 -79.217  1.00 298.64 ? 449  GLU E OE2 1 
ATOM   14937 N  N   . VAL E  1 450 ? -19.449 -68.092 -81.870  1.00 272.94 ? 450  VAL E N   1 
ATOM   14938 C  CA  . VAL E  1 450 ? -19.463 -67.507 -83.206  1.00 273.92 ? 450  VAL E CA  1 
ATOM   14939 C  C   . VAL E  1 450 ? -19.577 -68.645 -84.211  1.00 275.08 ? 450  VAL E C   1 
ATOM   14940 O  O   . VAL E  1 450 ? -18.605 -69.375 -84.441  1.00 271.18 ? 450  VAL E O   1 
ATOM   14941 C  CB  . VAL E  1 450 ? -18.215 -66.658 -83.485  1.00 274.23 ? 450  VAL E CB  1 
ATOM   14942 C  CG1 . VAL E  1 450 ? -18.261 -66.106 -84.902  1.00 276.49 ? 450  VAL E CG1 1 
ATOM   14943 C  CG2 . VAL E  1 450 ? -18.104 -65.530 -82.472  1.00 274.12 ? 450  VAL E CG2 1 
ATOM   14944 N  N   . TYR E  1 451 ? -20.755 -68.800 -84.806  1.00 284.34 ? 451  TYR E N   1 
ATOM   14945 C  CA  . TYR E  1 451 ? -20.972 -69.834 -85.814  1.00 295.05 ? 451  TYR E CA  1 
ATOM   14946 C  C   . TYR E  1 451 ? -21.641 -69.239 -87.057  1.00 302.64 ? 451  TYR E C   1 
ATOM   14947 O  O   . TYR E  1 451 ? -22.683 -68.594 -86.952  1.00 303.84 ? 451  TYR E O   1 
ATOM   14948 C  CB  . TYR E  1 451 ? -21.809 -70.989 -85.240  1.00 291.35 ? 451  TYR E CB  1 
ATOM   14949 C  CG  . TYR E  1 451 ? -23.027 -70.570 -84.439  1.00 286.59 ? 451  TYR E CG  1 
ATOM   14950 C  CD1 . TYR E  1 451 ? -22.942 -70.343 -83.069  1.00 279.36 ? 451  TYR E CD1 1 
ATOM   14951 C  CD2 . TYR E  1 451 ? -24.266 -70.424 -85.051  1.00 290.30 ? 451  TYR E CD2 1 
ATOM   14952 C  CE1 . TYR E  1 451 ? -24.054 -69.967 -82.338  1.00 279.68 ? 451  TYR E CE1 1 
ATOM   14953 C  CE2 . TYR E  1 451 ? -25.380 -70.050 -84.329  1.00 287.06 ? 451  TYR E CE2 1 
ATOM   14954 C  CZ  . TYR E  1 451 ? -25.271 -69.823 -82.975  1.00 282.37 ? 451  TYR E CZ  1 
ATOM   14955 O  OH  . TYR E  1 451 ? -26.386 -69.451 -82.263  1.00 280.33 ? 451  TYR E OH  1 
ATOM   14956 N  N   . PRO E  1 452 ? -21.047 -69.459 -88.246  1.00 303.06 ? 452  PRO E N   1 
ATOM   14957 C  CA  . PRO E  1 452 ? -19.811 -70.214 -88.488  1.00 302.56 ? 452  PRO E CA  1 
ATOM   14958 C  C   . PRO E  1 452 ? -18.534 -69.458 -88.128  1.00 298.49 ? 452  PRO E C   1 
ATOM   14959 O  O   . PRO E  1 452 ? -18.540 -68.233 -87.996  1.00 291.09 ? 452  PRO E O   1 
ATOM   14960 C  CB  . PRO E  1 452 ? -19.862 -70.480 -89.993  1.00 298.65 ? 452  PRO E CB  1 
ATOM   14961 C  CG  . PRO E  1 452 ? -20.589 -69.310 -90.537  1.00 299.32 ? 452  PRO E CG  1 
ATOM   14962 C  CD  . PRO E  1 452 ? -21.627 -68.953 -89.503  1.00 302.85 ? 452  PRO E CD  1 
ATOM   14963 N  N   . SER E  1 453 ? -17.440 -70.210 -87.976  1.00 301.90 ? 453  SER E N   1 
ATOM   14964 C  CA  . SER E  1 453 ? -16.133 -69.597 -87.767  1.00 289.24 ? 453  SER E CA  1 
ATOM   14965 C  C   . SER E  1 453 ? -15.597 -68.987 -89.054  1.00 287.10 ? 453  SER E C   1 
ATOM   14966 O  O   . SER E  1 453 ? -14.911 -67.959 -89.022  1.00 279.46 ? 453  SER E O   1 
ATOM   14967 C  CB  . SER E  1 453 ? -15.150 -70.634 -87.224  1.00 285.39 ? 453  SER E CB  1 
ATOM   14968 O  OG  . SER E  1 453 ? -15.048 -71.750 -88.092  1.00 287.59 ? 453  SER E OG  1 
ATOM   14969 N  N   . ILE E  1 454 ? -15.886 -69.612 -90.190  1.00 306.15 ? 454  ILE E N   1 
ATOM   14970 C  CA  . ILE E  1 454 ? -15.331 -69.217 -91.478  1.00 310.42 ? 454  ILE E CA  1 
ATOM   14971 C  C   . ILE E  1 454 ? -16.448 -68.567 -92.284  1.00 323.72 ? 454  ILE E C   1 
ATOM   14972 O  O   . ILE E  1 454 ? -17.429 -69.224 -92.658  1.00 324.49 ? 454  ILE E O   1 
ATOM   14973 C  CB  . ILE E  1 454 ? -14.710 -70.409 -92.221  1.00 303.69 ? 454  ILE E CB  1 
ATOM   14974 C  CG1 . ILE E  1 454 ? -15.597 -71.650 -92.091  1.00 304.30 ? 454  ILE E CG1 1 
ATOM   14975 C  CG2 . ILE E  1 454 ? -13.316 -70.696 -91.687  1.00 293.79 ? 454  ILE E CG2 1 
ATOM   14976 C  CD1 . ILE E  1 454 ? -15.042 -72.874 -92.772  1.00 304.29 ? 454  ILE E CD1 1 
ATOM   14977 N  N   . LEU E  1 455 ? -16.307 -67.270 -92.541  1.00 336.76 ? 455  LEU E N   1 
ATOM   14978 C  CA  . LEU E  1 455 ? -17.292 -66.509 -93.303  1.00 343.58 ? 455  LEU E CA  1 
ATOM   14979 C  C   . LEU E  1 455 ? -16.926 -66.503 -94.783  1.00 345.18 ? 455  LEU E C   1 
ATOM   14980 O  O   . LEU E  1 455 ? -15.841 -66.041 -95.159  1.00 350.49 ? 455  LEU E O   1 
ATOM   14981 C  CB  . LEU E  1 455 ? -17.386 -65.080 -92.770  1.00 335.25 ? 455  LEU E CB  1 
ATOM   14982 C  CG  . LEU E  1 455 ? -17.648 -64.948 -91.267  1.00 319.77 ? 455  LEU E CG  1 
ATOM   14983 C  CD1 . LEU E  1 455 ? -17.718 -63.483 -90.867  1.00 312.70 ? 455  LEU E CD1 1 
ATOM   14984 C  CD2 . LEU E  1 455 ? -18.920 -65.677 -90.875  1.00 317.84 ? 455  LEU E CD2 1 
ATOM   14985 N  N   . ASN E  1 456 ? -17.822 -67.027 -95.615  1.00 334.27 ? 456  ASN E N   1 
ATOM   14986 C  CA  . ASN E  1 456 ? -17.601 -66.988 -97.050  1.00 324.15 ? 456  ASN E CA  1 
ATOM   14987 C  C   . ASN E  1 456 ? -17.645 -65.541 -97.532  1.00 316.60 ? 456  ASN E C   1 
ATOM   14988 O  O   . ASN E  1 456 ? -18.267 -64.673 -96.914  1.00 307.16 ? 456  ASN E O   1 
ATOM   14989 C  CB  . ASN E  1 456 ? -18.657 -67.826 -97.775  1.00 322.89 ? 456  ASN E CB  1 
ATOM   14990 C  CG  . ASN E  1 456 ? -18.354 -68.002 -99.251  1.00 332.74 ? 456  ASN E CG  1 
ATOM   14991 O  OD1 . ASN E  1 456 ? -18.803 -67.219 -100.088 1.00 339.83 ? 456  ASN E OD1 1 
ATOM   14992 N  ND2 . ASN E  1 456 ? -17.599 -69.044 -99.580  1.00 334.33 ? 456  ASN E ND2 1 
ATOM   14993 N  N   . GLN E  1 457 ? -16.985 -65.284 -98.662  1.00 316.22 ? 457  GLN E N   1 
ATOM   14994 C  CA  . GLN E  1 457 ? -16.998 -63.931 -99.204  1.00 315.94 ? 457  GLN E CA  1 
ATOM   14995 C  C   . GLN E  1 457 ? -18.339 -63.594 -99.839  1.00 318.62 ? 457  GLN E C   1 
ATOM   14996 O  O   . GLN E  1 457 ? -18.641 -62.412 -100.045 1.00 323.84 ? 457  GLN E O   1 
ATOM   14997 C  CB  . GLN E  1 457 ? -15.862 -63.759 -100.217 1.00 323.51 ? 457  GLN E CB  1 
ATOM   14998 C  CG  . GLN E  1 457 ? -15.705 -62.342 -100.743 1.00 320.65 ? 457  GLN E CG  1 
ATOM   14999 C  CD  . GLN E  1 457 ? -15.639 -61.320 -99.622  1.00 301.48 ? 457  GLN E CD  1 
ATOM   15000 O  OE1 . GLN E  1 457 ? -14.798 -61.417 -98.729  1.00 290.36 ? 457  GLN E OE1 1 
ATOM   15001 N  NE2 . GLN E  1 457 ? -16.544 -60.348 -99.651  1.00 301.65 ? 457  GLN E NE2 1 
ATOM   15002 N  N   . ASP E  1 458 ? -19.168 -64.602 -100.112 1.00 321.67 ? 458  ASP E N   1 
ATOM   15003 C  CA  . ASP E  1 458 ? -20.480 -64.380 -100.725 1.00 314.47 ? 458  ASP E CA  1 
ATOM   15004 C  C   . ASP E  1 458 ? -21.402 -65.516 -100.269 1.00 314.35 ? 458  ASP E C   1 
ATOM   15005 O  O   . ASP E  1 458 ? -21.551 -66.531 -100.954 1.00 319.29 ? 458  ASP E O   1 
ATOM   15006 C  CB  . ASP E  1 458 ? -20.379 -64.301 -102.240 1.00 308.03 ? 458  ASP E CB  1 
ATOM   15007 C  CG  . ASP E  1 458 ? -21.716 -64.018 -102.892 1.00 304.76 ? 458  ASP E CG  1 
ATOM   15008 O  OD1 . ASP E  1 458 ? -22.124 -62.837 -102.949 1.00 298.29 ? 458  ASP E OD1 1 
ATOM   15009 O  OD2 . ASP E  1 458 ? -22.369 -64.983 -103.335 1.00 312.03 ? 458  ASP E OD2 1 
ATOM   15010 N  N   . ASN E  1 459 ? -22.012 -65.333 -99.098  1.00 296.37 ? 459  ASN E N   1 
ATOM   15011 C  CA  . ASN E  1 459 ? -22.951 -66.300 -98.526  1.00 292.61 ? 459  ASN E CA  1 
ATOM   15012 C  C   . ASN E  1 459 ? -24.187 -65.519 -98.085  1.00 287.67 ? 459  ASN E C   1 
ATOM   15013 O  O   . ASN E  1 459 ? -24.317 -65.141 -96.918  1.00 289.26 ? 459  ASN E O   1 
ATOM   15014 C  CB  . ASN E  1 459 ? -22.323 -67.070 -97.361  1.00 291.51 ? 459  ASN E CB  1 
ATOM   15015 C  CG  . ASN E  1 459 ? -23.309 -68.009 -96.686  1.00 316.90 ? 459  ASN E CG  1 
ATOM   15016 O  OD1 . ASN E  1 459 ? -24.270 -68.464 -97.308  1.00 301.40 ? 459  ASN E OD1 1 
ATOM   15017 N  ND2 . ASN E  1 459 ? -23.079 -68.305 -95.411  1.00 408.98 ? 459  ASN E ND2 1 
ATOM   15018 N  N   . LYS E  1 460 ? -25.116 -65.322 -99.012  1.00 291.83 ? 460  LYS E N   1 
ATOM   15019 C  CA  . LYS E  1 460 ? -26.321 -64.545 -98.759  1.00 287.83 ? 460  LYS E CA  1 
ATOM   15020 C  C   . LYS E  1 460 ? -27.423 -65.466 -98.244  1.00 293.99 ? 460  LYS E C   1 
ATOM   15021 O  O   . LYS E  1 460 ? -27.868 -66.369 -98.962  1.00 297.20 ? 460  LYS E O   1 
ATOM   15022 C  CB  . LYS E  1 460 ? -26.738 -63.823 -100.039 1.00 289.96 ? 460  LYS E CB  1 
ATOM   15023 C  CG  . LYS E  1 460 ? -25.689 -62.821 -100.512 1.00 283.86 ? 460  LYS E CG  1 
ATOM   15024 C  CD  . LYS E  1 460 ? -25.920 -62.375 -101.951 1.00 289.82 ? 460  LYS E CD  1 
ATOM   15025 C  CE  . LYS E  1 460 ? -25.786 -63.540 -102.928 1.00 293.87 ? 460  LYS E CE  1 
ATOM   15026 N  NZ  . LYS E  1 460 ? -25.878 -63.090 -104.346 1.00 289.35 ? 460  LYS E NZ  1 
ATOM   15027 N  N   . THR E  1 461 ? -27.863 -65.240 -97.002  1.00 298.65 ? 461  THR E N   1 
ATOM   15028 C  CA  . THR E  1 461 ? -28.842 -66.131 -96.386  1.00 309.81 ? 461  THR E CA  1 
ATOM   15029 C  C   . THR E  1 461 ? -29.923 -65.387 -95.606  1.00 313.12 ? 461  THR E C   1 
ATOM   15030 O  O   . THR E  1 461 ? -31.115 -65.529 -95.903  1.00 318.25 ? 461  THR E O   1 
ATOM   15031 C  CB  . THR E  1 461 ? -28.133 -67.124 -95.461  1.00 309.21 ? 461  THR E CB  1 
ATOM   15032 O  OG1 . THR E  1 461 ? -27.139 -67.845 -96.199  1.00 318.90 ? 461  THR E OG1 1 
ATOM   15033 C  CG2 . THR E  1 461 ? -29.131 -68.102 -94.857  1.00 312.51 ? 461  THR E CG2 1 
ATOM   15034 N  N   . CYS E  1 462 ? -29.525 -64.603 -94.604  1.00 311.58 ? 462  CYS E N   1 
ATOM   15035 C  CA  . CYS E  1 462 ? -30.494 -63.822 -93.844  1.00 316.26 ? 462  CYS E CA  1 
ATOM   15036 C  C   . CYS E  1 462 ? -31.198 -62.817 -94.748  1.00 302.52 ? 462  CYS E C   1 
ATOM   15037 O  O   . CYS E  1 462 ? -30.622 -62.291 -95.704  1.00 296.66 ? 462  CYS E O   1 
ATOM   15038 C  CB  . CYS E  1 462 ? -29.817 -63.079 -92.695  1.00 325.66 ? 462  CYS E CB  1 
ATOM   15039 S  SG  . CYS E  1 462 ? -28.457 -62.059 -93.261  1.00 359.53 ? 462  CYS E SG  1 
ATOM   15040 N  N   . SER E  1 463 ? -32.455 -62.536 -94.423  1.00 297.90 ? 463  SER E N   1 
ATOM   15041 C  CA  . SER E  1 463 ? -33.251 -61.626 -95.235  1.00 301.28 ? 463  SER E CA  1 
ATOM   15042 C  C   . SER E  1 463 ? -32.729 -60.191 -95.150  1.00 296.37 ? 463  SER E C   1 
ATOM   15043 O  O   . SER E  1 463 ? -32.402 -59.686 -94.071  1.00 290.44 ? 463  SER E O   1 
ATOM   15044 C  CB  . SER E  1 463 ? -34.715 -61.682 -94.799  1.00 298.27 ? 463  SER E CB  1 
ATOM   15045 O  OG  . SER E  1 463 ? -34.843 -61.474 -93.405  1.00 286.39 ? 463  SER E OG  1 
ATOM   15046 N  N   . LEU E  1 464 ? -32.655 -59.539 -96.310  1.00 288.21 ? 464  LEU E N   1 
ATOM   15047 C  CA  . LEU E  1 464 ? -32.217 -58.155 -96.437  1.00 273.19 ? 464  LEU E CA  1 
ATOM   15048 C  C   . LEU E  1 464 ? -32.619 -57.674 -97.826  1.00 288.64 ? 464  LEU E C   1 
ATOM   15049 O  O   . LEU E  1 464 ? -32.707 -58.490 -98.750  1.00 293.91 ? 464  LEU E O   1 
ATOM   15050 C  CB  . LEU E  1 464 ? -30.697 -58.041 -96.233  1.00 252.82 ? 464  LEU E CB  1 
ATOM   15051 C  CG  . LEU E  1 464 ? -30.024 -56.667 -96.194  1.00 250.69 ? 464  LEU E CG  1 
ATOM   15052 C  CD1 . LEU E  1 464 ? -30.334 -55.941 -94.891  1.00 246.10 ? 464  LEU E CD1 1 
ATOM   15053 C  CD2 . LEU E  1 464 ? -28.526 -56.800 -96.392  1.00 249.72 ? 464  LEU E CD2 1 
ATOM   15054 N  N   . PRO E  1 465 ? -32.878 -56.365 -98.012  1.00 287.20 ? 465  PRO E N   1 
ATOM   15055 C  CA  . PRO E  1 465 ? -33.207 -55.937 -99.379  1.00 273.71 ? 465  PRO E CA  1 
ATOM   15056 C  C   . PRO E  1 465 ? -32.035 -56.087 -100.344 1.00 268.36 ? 465  PRO E C   1 
ATOM   15057 O  O   . PRO E  1 465 ? -31.416 -55.087 -100.703 1.00 268.18 ? 465  PRO E O   1 
ATOM   15058 C  CB  . PRO E  1 465 ? -33.578 -54.460 -99.206  1.00 265.99 ? 465  PRO E CB  1 
ATOM   15059 C  CG  . PRO E  1 465 ? -34.028 -54.345 -97.796  1.00 266.99 ? 465  PRO E CG  1 
ATOM   15060 C  CD  . PRO E  1 465 ? -33.175 -55.315 -97.021  1.00 275.70 ? 465  PRO E CD  1 
ATOM   15061 N  N   . LYS E  1 470 ? -29.973 -59.415 -99.342  1.00 289.93 ? 470  LYS E N   1 
ATOM   15062 C  CA  . LYS E  1 470 ? -29.231 -60.562 -98.827  1.00 285.83 ? 470  LYS E CA  1 
ATOM   15063 C  C   . LYS E  1 470 ? -27.731 -60.345 -99.001  1.00 285.63 ? 470  LYS E C   1 
ATOM   15064 O  O   . LYS E  1 470 ? -27.251 -60.093 -100.106 1.00 288.37 ? 470  LYS E O   1 
ATOM   15065 C  CB  . LYS E  1 470 ? -29.668 -61.856 -99.526  1.00 290.55 ? 470  LYS E CB  1 
ATOM   15066 C  CG  . LYS E  1 470 ? -30.962 -62.493 -99.006  1.00 287.77 ? 470  LYS E CG  1 
ATOM   15067 C  CD  . LYS E  1 470 ? -32.154 -61.557 -99.074  1.00 285.36 ? 470  LYS E CD  1 
ATOM   15068 C  CE  . LYS E  1 470 ? -32.591 -61.322 -100.504 1.00 284.95 ? 470  LYS E CE  1 
ATOM   15069 N  NZ  . LYS E  1 470 ? -33.759 -60.405 -100.570 1.00 279.59 ? 470  LYS E NZ  1 
ATOM   15070 N  N   . VAL E  1 471 ? -26.993 -60.435 -97.893  1.00 276.12 ? 471  VAL E N   1 
ATOM   15071 C  CA  . VAL E  1 471 ? -25.545 -60.283 -97.892  1.00 276.97 ? 471  VAL E CA  1 
ATOM   15072 C  C   . VAL E  1 471 ? -24.940 -61.329 -96.959  1.00 281.77 ? 471  VAL E C   1 
ATOM   15073 O  O   . VAL E  1 471 ? -25.632 -61.943 -96.144  1.00 285.66 ? 471  VAL E O   1 
ATOM   15074 C  CB  . VAL E  1 471 ? -25.141 -58.850 -97.473  1.00 275.77 ? 471  VAL E CB  1 
ATOM   15075 C  CG1 . VAL E  1 471 ? -25.432 -58.636 -96.005  1.00 284.95 ? 471  VAL E CG1 1 
ATOM   15076 C  CG2 . VAL E  1 471 ? -23.686 -58.546 -97.821  1.00 270.26 ? 471  VAL E CG2 1 
ATOM   15077 N  N   . SER E  1 472 ? -23.632 -61.555 -97.115  1.00 287.46 ? 472  SER E N   1 
ATOM   15078 C  CA  . SER E  1 472 ? -22.877 -62.485 -96.275  1.00 287.82 ? 472  SER E CA  1 
ATOM   15079 C  C   . SER E  1 472 ? -23.031 -62.194 -94.784  1.00 290.11 ? 472  SER E C   1 
ATOM   15080 O  O   . SER E  1 472 ? -22.403 -61.268 -94.261  1.00 289.01 ? 472  SER E O   1 
ATOM   15081 C  CB  . SER E  1 472 ? -21.394 -62.449 -96.647  1.00 278.18 ? 472  SER E CB  1 
ATOM   15082 O  OG  . SER E  1 472 ? -21.197 -62.807 -98.002  1.00 280.94 ? 472  SER E OG  1 
ATOM   15083 N  N   . CYS E  1 473 ? -23.849 -62.985 -94.088  1.00 292.01 ? 473  CYS E N   1 
ATOM   15084 C  CA  . CYS E  1 473 ? -24.169 -62.742 -92.687  1.00 294.95 ? 473  CYS E CA  1 
ATOM   15085 C  C   . CYS E  1 473 ? -23.974 -63.997 -91.845  1.00 294.75 ? 473  CYS E C   1 
ATOM   15086 O  O   . CYS E  1 473 ? -23.898 -65.117 -92.359  1.00 292.42 ? 473  CYS E O   1 
ATOM   15087 C  CB  . CYS E  1 473 ? -25.597 -62.227 -92.523  1.00 303.37 ? 473  CYS E CB  1 
ATOM   15088 S  SG  . CYS E  1 473 ? -26.851 -63.290 -93.227  1.00 334.71 ? 473  CYS E SG  1 
ATOM   15089 N  N   . PHE E  1 474 ? -23.922 -63.784 -90.528  1.00 303.21 ? 474  PHE E N   1 
ATOM   15090 C  CA  . PHE E  1 474 ? -23.680 -64.838 -89.551  1.00 313.13 ? 474  PHE E CA  1 
ATOM   15091 C  C   . PHE E  1 474 ? -24.398 -64.497 -88.250  1.00 315.24 ? 474  PHE E C   1 
ATOM   15092 O  O   . PHE E  1 474 ? -24.796 -63.352 -88.018  1.00 313.14 ? 474  PHE E O   1 
ATOM   15093 C  CB  . PHE E  1 474 ? -22.175 -65.026 -89.310  1.00 310.36 ? 474  PHE E CB  1 
ATOM   15094 C  CG  . PHE E  1 474 ? -21.476 -63.773 -88.858  1.00 299.91 ? 474  PHE E CG  1 
ATOM   15095 C  CD1 . PHE E  1 474 ? -21.030 -62.844 -89.785  1.00 295.49 ? 474  PHE E CD1 1 
ATOM   15096 C  CD2 . PHE E  1 474 ? -21.252 -63.528 -87.514  1.00 292.93 ? 474  PHE E CD2 1 
ATOM   15097 C  CE1 . PHE E  1 474 ? -20.387 -61.688 -89.380  1.00 289.73 ? 474  PHE E CE1 1 
ATOM   15098 C  CE2 . PHE E  1 474 ? -20.604 -62.376 -87.103  1.00 285.70 ? 474  PHE E CE2 1 
ATOM   15099 C  CZ  . PHE E  1 474 ? -20.172 -61.456 -88.037  1.00 287.83 ? 474  PHE E CZ  1 
ATOM   15100 N  N   . ASN E  1 475 ? -24.576 -65.515 -87.410  1.00 320.35 ? 475  ASN E N   1 
ATOM   15101 C  CA  . ASN E  1 475 ? -25.283 -65.389 -86.140  1.00 313.03 ? 475  ASN E CA  1 
ATOM   15102 C  C   . ASN E  1 475 ? -24.295 -65.198 -84.997  1.00 311.67 ? 475  ASN E C   1 
ATOM   15103 O  O   . ASN E  1 475 ? -23.316 -65.944 -84.884  1.00 316.47 ? 475  ASN E O   1 
ATOM   15104 C  CB  . ASN E  1 475 ? -26.151 -66.621 -85.877  1.00 314.21 ? 475  ASN E CB  1 
ATOM   15105 C  CG  . ASN E  1 475 ? -27.218 -66.817 -86.937  1.00 320.81 ? 475  ASN E CG  1 
ATOM   15106 O  OD1 . ASN E  1 475 ? -26.995 -67.489 -87.944  1.00 327.25 ? 475  ASN E OD1 1 
ATOM   15107 N  ND2 . ASN E  1 475 ? -28.388 -66.229 -86.714  1.00 318.66 ? 475  ASN E ND2 1 
ATOM   15108 N  N   . VAL E  1 476 ? -24.557 -64.207 -84.149  1.00 311.62 ? 476  VAL E N   1 
ATOM   15109 C  CA  . VAL E  1 476 ? -23.759 -63.947 -82.955  1.00 313.18 ? 476  VAL E CA  1 
ATOM   15110 C  C   . VAL E  1 476 ? -24.614 -64.292 -81.741  1.00 317.17 ? 476  VAL E C   1 
ATOM   15111 O  O   . VAL E  1 476 ? -25.591 -63.595 -81.442  1.00 315.11 ? 476  VAL E O   1 
ATOM   15112 C  CB  . VAL E  1 476 ? -23.272 -62.495 -82.899  1.00 307.98 ? 476  VAL E CB  1 
ATOM   15113 C  CG1 . VAL E  1 476 ? -22.443 -62.270 -81.645  1.00 307.05 ? 476  VAL E CG1 1 
ATOM   15114 C  CG2 . VAL E  1 476 ? -22.463 -62.164 -84.142  1.00 302.71 ? 476  VAL E CG2 1 
ATOM   15115 N  N   . ARG E  1 477 ? -24.267 -65.376 -81.049  1.00 318.47 ? 477  ARG E N   1 
ATOM   15116 C  CA  . ARG E  1 477 ? -24.994 -65.819 -79.862  1.00 316.74 ? 477  ARG E CA  1 
ATOM   15117 C  C   . ARG E  1 477 ? -24.110 -65.660 -78.627  1.00 307.64 ? 477  ARG E C   1 
ATOM   15118 O  O   . ARG E  1 477 ? -23.048 -66.286 -78.535  1.00 300.39 ? 477  ARG E O   1 
ATOM   15119 C  CB  . ARG E  1 477 ? -25.459 -67.270 -80.021  1.00 323.51 ? 477  ARG E CB  1 
ATOM   15120 C  CG  . ARG E  1 477 ? -26.323 -67.785 -78.870  1.00 326.80 ? 477  ARG E CG  1 
ATOM   15121 C  CD  . ARG E  1 477 ? -26.927 -69.155 -79.174  1.00 330.56 ? 477  ARG E CD  1 
ATOM   15122 N  NE  . ARG E  1 477 ? -27.778 -69.644 -78.090  1.00 332.81 ? 477  ARG E NE  1 
ATOM   15123 C  CZ  . ARG E  1 477 ? -27.363 -70.446 -77.115  1.00 330.05 ? 477  ARG E CZ  1 
ATOM   15124 N  NH1 . ARG E  1 477 ? -26.102 -70.858 -77.085  1.00 322.81 ? 477  ARG E NH1 1 
ATOM   15125 N  NH2 . ARG E  1 477 ? -28.207 -70.840 -76.170  1.00 331.49 ? 477  ARG E NH2 1 
ATOM   15126 N  N   . PHE E  1 478 ? -24.553 -64.827 -77.683  1.00 308.46 ? 478  PHE E N   1 
ATOM   15127 C  CA  . PHE E  1 478 ? -23.848 -64.583 -76.429  1.00 305.15 ? 478  PHE E CA  1 
ATOM   15128 C  C   . PHE E  1 478 ? -24.772 -64.920 -75.265  1.00 307.47 ? 478  PHE E C   1 
ATOM   15129 O  O   . PHE E  1 478 ? -25.928 -64.485 -75.242  1.00 313.66 ? 478  PHE E O   1 
ATOM   15130 C  CB  . PHE E  1 478 ? -23.378 -63.123 -76.330  1.00 300.40 ? 478  PHE E CB  1 
ATOM   15131 C  CG  . PHE E  1 478 ? -24.495 -62.114 -76.392  1.00 295.54 ? 478  PHE E CG  1 
ATOM   15132 C  CD1 . PHE E  1 478 ? -25.009 -61.697 -77.609  1.00 297.10 ? 478  PHE E CD1 1 
ATOM   15133 C  CD2 . PHE E  1 478 ? -25.030 -61.584 -75.229  1.00 291.58 ? 478  PHE E CD2 1 
ATOM   15134 C  CE1 . PHE E  1 478 ? -26.037 -60.776 -77.664  1.00 296.90 ? 478  PHE E CE1 1 
ATOM   15135 C  CE2 . PHE E  1 478 ? -26.057 -60.665 -75.278  1.00 291.76 ? 478  PHE E CE2 1 
ATOM   15136 C  CZ  . PHE E  1 478 ? -26.561 -60.259 -76.496  1.00 294.64 ? 478  PHE E CZ  1 
ATOM   15137 N  N   . CYS E  1 479 ? -24.266 -65.691 -74.304  1.00 294.38 ? 479  CYS E N   1 
ATOM   15138 C  CA  . CYS E  1 479 ? -25.037 -66.093 -73.136  1.00 293.99 ? 479  CYS E CA  1 
ATOM   15139 C  C   . CYS E  1 479 ? -24.461 -65.443 -71.884  1.00 277.27 ? 479  CYS E C   1 
ATOM   15140 O  O   . CYS E  1 479 ? -23.259 -65.176 -71.802  1.00 267.18 ? 479  CYS E O   1 
ATOM   15141 C  CB  . CYS E  1 479 ? -25.042 -67.612 -72.965  1.00 301.96 ? 479  CYS E CB  1 
ATOM   15142 S  SG  . CYS E  1 479 ? -25.782 -68.571 -74.325  1.00 328.50 ? 479  CYS E SG  1 
ATOM   15143 N  N   . LEU E  1 480 ? -25.326 -65.212 -70.895  1.00 278.44 ? 480  LEU E N   1 
ATOM   15144 C  CA  . LEU E  1 480 ? -24.943 -64.487 -69.690  1.00 271.90 ? 480  LEU E CA  1 
ATOM   15145 C  C   . LEU E  1 480 ? -25.631 -65.088 -68.473  1.00 267.82 ? 480  LEU E C   1 
ATOM   15146 O  O   . LEU E  1 480 ? -26.848 -65.294 -68.477  1.00 272.98 ? 480  LEU E O   1 
ATOM   15147 C  CB  . LEU E  1 480 ? -25.298 -63.000 -69.811  1.00 269.21 ? 480  LEU E CB  1 
ATOM   15148 C  CG  . LEU E  1 480 ? -24.517 -62.040 -68.911  1.00 249.29 ? 480  LEU E CG  1 
ATOM   15149 C  CD1 . LEU E  1 480 ? -23.025 -62.247 -69.091  1.00 233.62 ? 480  LEU E CD1 1 
ATOM   15150 C  CD2 . LEU E  1 480 ? -24.903 -60.596 -69.188  1.00 249.21 ? 480  LEU E CD2 1 
ATOM   15151 N  N   . LYS E  1 481 ? -24.845 -65.376 -67.440  1.00 251.80 ? 481  LYS E N   1 
ATOM   15152 C  CA  . LYS E  1 481 ? -25.351 -65.955 -66.205  1.00 246.40 ? 481  LYS E CA  1 
ATOM   15153 C  C   . LYS E  1 481 ? -24.558 -65.389 -65.036  1.00 247.13 ? 481  LYS E C   1 
ATOM   15154 O  O   . LYS E  1 481 ? -23.335 -65.252 -65.119  1.00 246.21 ? 481  LYS E O   1 
ATOM   15155 C  CB  . LYS E  1 481 ? -25.253 -67.484 -66.231  1.00 250.86 ? 481  LYS E CB  1 
ATOM   15156 C  CG  . LYS E  1 481 ? -25.871 -68.171 -65.031  1.00 263.24 ? 481  LYS E CG  1 
ATOM   15157 C  CD  . LYS E  1 481 ? -25.835 -69.675 -65.204  1.00 276.10 ? 481  LYS E CD  1 
ATOM   15158 C  CE  . LYS E  1 481 ? -24.410 -70.200 -65.078  1.00 279.97 ? 481  LYS E CE  1 
ATOM   15159 N  NZ  . LYS E  1 481 ? -23.817 -69.932 -63.734  1.00 277.45 ? 481  LYS E NZ  1 
ATOM   15160 N  N   . ALA E  1 482 ? -25.259 -65.049 -63.955  1.00 262.18 ? 482  ALA E N   1 
ATOM   15161 C  CA  . ALA E  1 482 ? -24.639 -64.445 -62.784  1.00 259.12 ? 482  ALA E CA  1 
ATOM   15162 C  C   . ALA E  1 482 ? -25.249 -65.036 -61.519  1.00 263.81 ? 482  ALA E C   1 
ATOM   15163 O  O   . ALA E  1 482 ? -26.353 -65.589 -61.536  1.00 271.34 ? 482  ALA E O   1 
ATOM   15164 C  CB  . ALA E  1 482 ? -24.790 -62.917 -62.786  1.00 256.49 ? 482  ALA E CB  1 
ATOM   15165 N  N   . ASP E  1 483 ? -24.508 -64.925 -60.417  1.00 256.55 ? 483  ASP E N   1 
ATOM   15166 C  CA  . ASP E  1 483 ? -24.988 -65.414 -59.132  1.00 250.99 ? 483  ASP E CA  1 
ATOM   15167 C  C   . ASP E  1 483 ? -24.175 -64.774 -58.015  1.00 246.26 ? 483  ASP E C   1 
ATOM   15168 O  O   . ASP E  1 483 ? -23.079 -64.249 -58.236  1.00 239.98 ? 483  ASP E O   1 
ATOM   15169 C  CB  . ASP E  1 483 ? -24.906 -66.944 -59.057  1.00 251.35 ? 483  ASP E CB  1 
ATOM   15170 C  CG  . ASP E  1 483 ? -25.774 -67.523 -57.959  1.00 259.99 ? 483  ASP E CG  1 
ATOM   15171 O  OD1 . ASP E  1 483 ? -26.873 -66.983 -57.716  1.00 270.61 ? 483  ASP E OD1 1 
ATOM   15172 O  OD2 . ASP E  1 483 ? -25.356 -68.523 -57.339  1.00 258.28 ? 483  ASP E OD2 1 
ATOM   15173 N  N   . GLY E  1 484 ? -24.738 -64.822 -56.807  1.00 246.93 ? 484  GLY E N   1 
ATOM   15174 C  CA  . GLY E  1 484 ? -24.083 -64.301 -55.624  1.00 247.33 ? 484  GLY E CA  1 
ATOM   15175 C  C   . GLY E  1 484 ? -24.448 -65.160 -54.433  1.00 246.01 ? 484  GLY E C   1 
ATOM   15176 O  O   . GLY E  1 484 ? -25.337 -66.011 -54.504  1.00 251.69 ? 484  GLY E O   1 
ATOM   15177 N  N   . LYS E  1 485 ? -23.749 -64.928 -53.319  1.00 243.87 ? 485  LYS E N   1 
ATOM   15178 C  CA  . LYS E  1 485 ? -23.926 -65.761 -52.124  1.00 244.66 ? 485  LYS E CA  1 
ATOM   15179 C  C   . LYS E  1 485 ? -23.951 -64.851 -50.895  1.00 254.45 ? 485  LYS E C   1 
ATOM   15180 O  O   . LYS E  1 485 ? -22.911 -64.547 -50.303  1.00 254.03 ? 485  LYS E O   1 
ATOM   15181 C  CB  . LYS E  1 485 ? -22.842 -66.824 -52.023  1.00 241.22 ? 485  LYS E CB  1 
ATOM   15182 C  CG  . LYS E  1 485 ? -23.177 -67.941 -51.040  1.00 243.98 ? 485  LYS E CG  1 
ATOM   15183 C  CD  . LYS E  1 485 ? -22.226 -69.119 -51.189  1.00 245.34 ? 485  LYS E CD  1 
ATOM   15184 C  CE  . LYS E  1 485 ? -22.632 -70.276 -50.288  1.00 248.03 ? 485  LYS E CE  1 
ATOM   15185 N  NZ  . LYS E  1 485 ? -21.722 -71.447 -50.425  1.00 246.77 ? 485  LYS E NZ  1 
ATOM   15186 N  N   . GLY E  1 486 ? -25.152 -64.445 -50.509  1.00 271.76 ? 486  GLY E N   1 
ATOM   15187 C  CA  . GLY E  1 486 ? -25.389 -63.534 -49.399  1.00 278.10 ? 486  GLY E CA  1 
ATOM   15188 C  C   . GLY E  1 486 ? -26.784 -62.938 -49.516  1.00 282.42 ? 486  GLY E C   1 
ATOM   15189 O  O   . GLY E  1 486 ? -27.687 -63.554 -50.085  1.00 283.96 ? 486  GLY E O   1 
ATOM   15190 N  N   . VAL E  1 487 ? -26.943 -61.734 -48.976  1.00 290.02 ? 487  VAL E N   1 
ATOM   15191 C  CA  . VAL E  1 487 ? -28.196 -60.990 -49.098  1.00 288.64 ? 487  VAL E CA  1 
ATOM   15192 C  C   . VAL E  1 487 ? -27.989 -59.977 -50.218  1.00 290.85 ? 487  VAL E C   1 
ATOM   15193 O  O   . VAL E  1 487 ? -27.329 -58.951 -50.037  1.00 292.25 ? 487  VAL E O   1 
ATOM   15194 C  CB  . VAL E  1 487 ? -28.607 -60.321 -47.784  1.00 279.33 ? 487  VAL E CB  1 
ATOM   15195 C  CG1 . VAL E  1 487 ? -29.835 -59.445 -47.994  1.00 265.91 ? 487  VAL E CG1 1 
ATOM   15196 C  CG2 . VAL E  1 487 ? -28.904 -61.370 -46.719  1.00 281.70 ? 487  VAL E CG2 1 
ATOM   15197 N  N   . LEU E  1 488 ? -28.538 -60.282 -51.386  1.00 278.03 ? 488  LEU E N   1 
ATOM   15198 C  CA  . LEU E  1 488 ? -28.493 -59.424 -52.559  1.00 272.78 ? 488  LEU E CA  1 
ATOM   15199 C  C   . LEU E  1 488 ? -29.828 -59.568 -53.268  1.00 267.92 ? 488  LEU E C   1 
ATOM   15200 O  O   . LEU E  1 488 ? -30.518 -60.581 -53.100  1.00 267.57 ? 488  LEU E O   1 
ATOM   15201 C  CB  . LEU E  1 488 ? -27.344 -59.792 -53.512  1.00 269.08 ? 488  LEU E CB  1 
ATOM   15202 C  CG  . LEU E  1 488 ? -27.235 -61.203 -54.096  1.00 264.40 ? 488  LEU E CG  1 
ATOM   15203 C  CD1 . LEU E  1 488 ? -26.456 -61.150 -55.398  1.00 259.76 ? 488  LEU E CD1 1 
ATOM   15204 C  CD2 . LEU E  1 488 ? -26.560 -62.160 -53.132  1.00 258.92 ? 488  LEU E CD2 1 
ATOM   15205 N  N   . PRO E  1 489 ? -30.233 -58.569 -54.050  1.00 258.22 ? 489  PRO E N   1 
ATOM   15206 C  CA  . PRO E  1 489 ? -31.484 -58.700 -54.802  1.00 262.00 ? 489  PRO E CA  1 
ATOM   15207 C  C   . PRO E  1 489 ? -31.396 -59.825 -55.822  1.00 263.44 ? 489  PRO E C   1 
ATOM   15208 O  O   . PRO E  1 489 ? -30.314 -60.308 -56.166  1.00 261.01 ? 489  PRO E O   1 
ATOM   15209 C  CB  . PRO E  1 489 ? -31.642 -57.336 -55.484  1.00 256.18 ? 489  PRO E CB  1 
ATOM   15210 C  CG  . PRO E  1 489 ? -30.267 -56.769 -55.524  1.00 250.93 ? 489  PRO E CG  1 
ATOM   15211 C  CD  . PRO E  1 489 ? -29.586 -57.268 -54.285  1.00 253.50 ? 489  PRO E CD  1 
ATOM   15212 N  N   . ARG E  1 490 ? -32.566 -60.254 -56.297  1.00 260.41 ? 490  ARG E N   1 
ATOM   15213 C  CA  . ARG E  1 490 ? -32.603 -61.279 -57.335  1.00 247.19 ? 490  ARG E CA  1 
ATOM   15214 C  C   . ARG E  1 490 ? -32.239 -60.695 -58.695  1.00 240.54 ? 490  ARG E C   1 
ATOM   15215 O  O   . ARG E  1 490 ? -31.437 -61.274 -59.437  1.00 234.74 ? 490  ARG E O   1 
ATOM   15216 C  CB  . ARG E  1 490 ? -33.993 -61.932 -57.389  1.00 244.58 ? 490  ARG E CB  1 
ATOM   15217 C  CG  . ARG E  1 490 ? -34.903 -61.575 -56.220  1.00 250.77 ? 490  ARG E CG  1 
ATOM   15218 C  CD  . ARG E  1 490 ? -35.994 -62.617 -56.021  1.00 249.46 ? 490  ARG E CD  1 
ATOM   15219 N  NE  . ARG E  1 490 ? -36.871 -62.273 -54.906  1.00 251.95 ? 490  ARG E NE  1 
ATOM   15220 C  CZ  . ARG E  1 490 ? -36.617 -62.561 -53.633  1.00 247.76 ? 490  ARG E CZ  1 
ATOM   15221 N  NH1 . ARG E  1 490 ? -35.505 -63.203 -53.300  1.00 246.84 ? 490  ARG E NH1 1 
ATOM   15222 N  NH2 . ARG E  1 490 ? -37.478 -62.205 -52.690  1.00 247.77 ? 490  ARG E NH2 1 
ATOM   15223 N  N   . LYS E  1 491 ? -32.805 -59.536 -59.021  1.00 238.91 ? 491  LYS E N   1 
ATOM   15224 C  CA  . LYS E  1 491 ? -32.689 -58.942 -60.349  1.00 241.11 ? 491  LYS E CA  1 
ATOM   15225 C  C   . LYS E  1 491 ? -31.440 -58.067 -60.421  1.00 242.32 ? 491  LYS E C   1 
ATOM   15226 O  O   . LYS E  1 491 ? -31.384 -56.998 -59.802  1.00 240.66 ? 491  LYS E O   1 
ATOM   15227 C  CB  . LYS E  1 491 ? -33.946 -58.141 -60.677  1.00 235.66 ? 491  LYS E CB  1 
ATOM   15228 C  CG  . LYS E  1 491 ? -35.234 -58.948 -60.583  1.00 237.06 ? 491  LYS E CG  1 
ATOM   15229 C  CD  . LYS E  1 491 ? -35.189 -60.152 -61.506  1.00 244.84 ? 491  LYS E CD  1 
ATOM   15230 C  CE  . LYS E  1 491 ? -36.425 -61.021 -61.347  1.00 257.52 ? 491  LYS E CE  1 
ATOM   15231 N  NZ  . LYS E  1 491 ? -36.397 -62.200 -62.257  1.00 260.46 ? 491  LYS E NZ  1 
ATOM   15232 N  N   . LEU E  1 492 ? -30.429 -58.532 -61.157  1.00 241.94 ? 492  LEU E N   1 
ATOM   15233 C  CA  . LEU E  1 492 ? -29.224 -57.758 -61.438  1.00 234.18 ? 492  LEU E CA  1 
ATOM   15234 C  C   . LEU E  1 492 ? -29.272 -57.258 -62.881  1.00 229.80 ? 492  LEU E C   1 
ATOM   15235 O  O   . LEU E  1 492 ? -29.289 -58.062 -63.820  1.00 231.11 ? 492  LEU E O   1 
ATOM   15236 C  CB  . LEU E  1 492 ? -27.973 -58.600 -61.194  1.00 232.06 ? 492  LEU E CB  1 
ATOM   15237 C  CG  . LEU E  1 492 ? -27.854 -59.244 -59.807  1.00 235.00 ? 492  LEU E CG  1 
ATOM   15238 C  CD1 . LEU E  1 492 ? -26.691 -60.225 -59.768  1.00 246.53 ? 492  LEU E CD1 1 
ATOM   15239 C  CD2 . LEU E  1 492 ? -27.704 -58.182 -58.724  1.00 230.61 ? 492  LEU E CD2 1 
ATOM   15240 N  N   . ASN E  1 493 ? -29.298 -55.934 -63.052  1.00 230.95 ? 493  ASN E N   1 
ATOM   15241 C  CA  . ASN E  1 493 ? -29.381 -55.306 -64.370  1.00 230.33 ? 493  ASN E CA  1 
ATOM   15242 C  C   . ASN E  1 493 ? -27.993 -55.087 -64.968  1.00 224.46 ? 493  ASN E C   1 
ATOM   15243 O  O   . ASN E  1 493 ? -27.198 -54.308 -64.431  1.00 218.75 ? 493  ASN E O   1 
ATOM   15244 C  CB  . ASN E  1 493 ? -30.126 -53.975 -64.275  1.00 241.99 ? 493  ASN E CB  1 
ATOM   15245 C  CG  . ASN E  1 493 ? -31.625 -54.153 -64.164  1.00 249.93 ? 493  ASN E CG  1 
ATOM   15246 O  OD1 . ASN E  1 493 ? -32.383 -53.611 -64.969  1.00 246.93 ? 493  ASN E OD1 1 
ATOM   15247 N  ND2 . ASN E  1 493 ? -32.063 -54.925 -63.174  1.00 260.18 ? 493  ASN E ND2 1 
ATOM   15248 N  N   . PHE E  1 494 ? -27.731 -55.717 -66.114  1.00 220.03 ? 494  PHE E N   1 
ATOM   15249 C  CA  . PHE E  1 494 ? -26.458 -55.604 -66.816  1.00 215.55 ? 494  PHE E CA  1 
ATOM   15250 C  C   . PHE E  1 494 ? -26.593 -54.720 -68.049  1.00 224.37 ? 494  PHE E C   1 
ATOM   15251 O  O   . PHE E  1 494 ? -27.619 -54.749 -68.737  1.00 231.70 ? 494  PHE E O   1 
ATOM   15252 C  CB  . PHE E  1 494 ? -25.943 -56.981 -67.245  1.00 206.50 ? 494  PHE E CB  1 
ATOM   15253 C  CG  . PHE E  1 494 ? -25.360 -57.785 -66.129  1.00 205.02 ? 494  PHE E CG  1 
ATOM   15254 C  CD1 . PHE E  1 494 ? -26.182 -58.481 -65.262  1.00 208.71 ? 494  PHE E CD1 1 
ATOM   15255 C  CD2 . PHE E  1 494 ? -23.990 -57.853 -65.950  1.00 202.51 ? 494  PHE E CD2 1 
ATOM   15256 C  CE1 . PHE E  1 494 ? -25.653 -59.222 -64.233  1.00 209.27 ? 494  PHE E CE1 1 
ATOM   15257 C  CE2 . PHE E  1 494 ? -23.453 -58.595 -64.921  1.00 210.22 ? 494  PHE E CE2 1 
ATOM   15258 C  CZ  . PHE E  1 494 ? -24.286 -59.282 -64.062  1.00 213.79 ? 494  PHE E CZ  1 
ATOM   15259 N  N   . GLN E  1 495 ? -25.545 -53.950 -68.337  1.00 227.63 ? 495  GLN E N   1 
ATOM   15260 C  CA  . GLN E  1 495 ? -25.429 -53.189 -69.579  1.00 227.43 ? 495  GLN E CA  1 
ATOM   15261 C  C   . GLN E  1 495 ? -24.287 -53.795 -70.385  1.00 215.20 ? 495  GLN E C   1 
ATOM   15262 O  O   . GLN E  1 495 ? -23.123 -53.717 -69.978  1.00 212.47 ? 495  GLN E O   1 
ATOM   15263 C  CB  . GLN E  1 495 ? -25.189 -51.704 -69.314  1.00 235.52 ? 495  GLN E CB  1 
ATOM   15264 C  CG  . GLN E  1 495 ? -25.257 -50.843 -70.572  1.00 237.09 ? 495  GLN E CG  1 
ATOM   15265 C  CD  . GLN E  1 495 ? -24.853 -49.399 -70.333  1.00 228.95 ? 495  GLN E CD  1 
ATOM   15266 O  OE1 . GLN E  1 495 ? -24.454 -49.026 -69.232  1.00 223.82 ? 495  GLN E OE1 1 
ATOM   15267 N  NE2 . GLN E  1 495 ? -24.955 -48.579 -71.373  1.00 224.19 ? 495  GLN E NE2 1 
ATOM   15268 N  N   . VAL E  1 496 ? -24.618 -54.399 -71.523  1.00 221.09 ? 496  VAL E N   1 
ATOM   15269 C  CA  . VAL E  1 496 ? -23.665 -55.154 -72.331  1.00 225.32 ? 496  VAL E CA  1 
ATOM   15270 C  C   . VAL E  1 496 ? -23.401 -54.404 -73.633  1.00 225.25 ? 496  VAL E C   1 
ATOM   15271 O  O   . VAL E  1 496 ? -24.340 -53.943 -74.296  1.00 223.67 ? 496  VAL E O   1 
ATOM   15272 C  CB  . VAL E  1 496 ? -24.178 -56.579 -72.595  1.00 232.46 ? 496  VAL E CB  1 
ATOM   15273 C  CG1 . VAL E  1 496 ? -23.167 -57.371 -73.398  1.00 236.20 ? 496  VAL E CG1 1 
ATOM   15274 C  CG2 . VAL E  1 496 ? -24.489 -57.279 -71.276  1.00 232.83 ? 496  VAL E CG2 1 
ATOM   15275 N  N   . GLU E  1 497 ? -22.120 -54.268 -73.988  1.00 228.48 ? 497  GLU E N   1 
ATOM   15276 C  CA  . GLU E  1 497 ? -21.687 -53.661 -75.240  1.00 221.58 ? 497  GLU E CA  1 
ATOM   15277 C  C   . GLU E  1 497 ? -20.917 -54.680 -76.068  1.00 225.58 ? 497  GLU E C   1 
ATOM   15278 O  O   . GLU E  1 497 ? -20.095 -55.433 -75.537  1.00 229.54 ? 497  GLU E O   1 
ATOM   15279 C  CB  . GLU E  1 497 ? -20.798 -52.430 -75.002  1.00 219.16 ? 497  GLU E CB  1 
ATOM   15280 C  CG  . GLU E  1 497 ? -21.223 -51.545 -73.843  1.00 226.44 ? 497  GLU E CG  1 
ATOM   15281 C  CD  . GLU E  1 497 ? -22.552 -50.857 -74.084  1.00 224.33 ? 497  GLU E CD  1 
ATOM   15282 O  OE1 . GLU E  1 497 ? -23.304 -50.669 -73.106  1.00 231.80 ? 497  GLU E OE1 1 
ATOM   15283 O  OE2 . GLU E  1 497 ? -22.844 -50.502 -75.246  1.00 214.71 ? 497  GLU E OE2 1 
ATOM   15284 N  N   . LEU E  1 498 ? -21.183 -54.696 -77.372  1.00 231.65 ? 498  LEU E N   1 
ATOM   15285 C  CA  . LEU E  1 498 ? -20.483 -55.561 -78.313  1.00 240.42 ? 498  LEU E CA  1 
ATOM   15286 C  C   . LEU E  1 498 ? -19.855 -54.705 -79.405  1.00 240.17 ? 498  LEU E C   1 
ATOM   15287 O  O   . LEU E  1 498 ? -20.501 -53.793 -79.932  1.00 232.53 ? 498  LEU E O   1 
ATOM   15288 C  CB  . LEU E  1 498 ? -21.430 -56.602 -78.923  1.00 240.07 ? 498  LEU E CB  1 
ATOM   15289 C  CG  . LEU E  1 498 ? -21.539 -57.977 -78.253  1.00 237.25 ? 498  LEU E CG  1 
ATOM   15290 C  CD1 . LEU E  1 498 ? -22.040 -57.869 -76.821  1.00 234.92 ? 498  LEU E CD1 1 
ATOM   15291 C  CD2 . LEU E  1 498 ? -22.453 -58.877 -79.062  1.00 240.88 ? 498  LEU E CD2 1 
ATOM   15292 N  N   . LEU E  1 499 ? -18.596 -54.993 -79.739  1.00 256.63 ? 499  LEU E N   1 
ATOM   15293 C  CA  . LEU E  1 499 ? -17.881 -54.286 -80.798  1.00 256.73 ? 499  LEU E CA  1 
ATOM   15294 C  C   . LEU E  1 499 ? -17.309 -55.290 -81.787  1.00 257.92 ? 499  LEU E C   1 
ATOM   15295 O  O   . LEU E  1 499 ? -16.498 -56.144 -81.413  1.00 258.13 ? 499  LEU E O   1 
ATOM   15296 C  CB  . LEU E  1 499 ? -16.760 -53.410 -80.228  1.00 259.84 ? 499  LEU E CB  1 
ATOM   15297 C  CG  . LEU E  1 499 ? -17.106 -52.416 -79.117  1.00 261.30 ? 499  LEU E CG  1 
ATOM   15298 C  CD1 . LEU E  1 499 ? -15.835 -51.957 -78.409  1.00 259.61 ? 499  LEU E CD1 1 
ATOM   15299 C  CD2 . LEU E  1 499 ? -17.862 -51.235 -79.688  1.00 257.93 ? 499  LEU E CD2 1 
ATOM   15300 N  N   . LEU E  1 500 ? -17.723 -55.175 -83.046  1.00 255.19 ? 500  LEU E N   1 
ATOM   15301 C  CA  . LEU E  1 500 ? -17.219 -56.029 -84.112  1.00 256.52 ? 500  LEU E CA  1 
ATOM   15302 C  C   . LEU E  1 500 ? -15.952 -55.440 -84.716  1.00 259.54 ? 500  LEU E C   1 
ATOM   15303 O  O   . LEU E  1 500 ? -15.846 -54.224 -84.899  1.00 265.42 ? 500  LEU E O   1 
ATOM   15304 C  CB  . LEU E  1 500 ? -18.274 -56.199 -85.205  1.00 251.33 ? 500  LEU E CB  1 
ATOM   15305 C  CG  . LEU E  1 500 ? -19.585 -56.882 -84.822  1.00 258.01 ? 500  LEU E CG  1 
ATOM   15306 C  CD1 . LEU E  1 500 ? -20.618 -56.699 -85.918  1.00 260.71 ? 500  LEU E CD1 1 
ATOM   15307 C  CD2 . LEU E  1 500 ? -19.354 -58.361 -84.554  1.00 267.40 ? 500  LEU E CD2 1 
ATOM   15308 N  N   . ASP E  1 501 ? -14.999 -56.315 -85.035  1.00 250.59 ? 501  ASP E N   1 
ATOM   15309 C  CA  . ASP E  1 501 ? -13.767 -55.921 -85.716  1.00 245.73 ? 501  ASP E CA  1 
ATOM   15310 C  C   . ASP E  1 501 ? -13.055 -54.796 -84.971  1.00 244.66 ? 501  ASP E C   1 
ATOM   15311 O  O   . ASP E  1 501 ? -12.703 -53.761 -85.543  1.00 240.45 ? 501  ASP E O   1 
ATOM   15312 C  CB  . ASP E  1 501 ? -14.057 -55.515 -87.161  1.00 250.89 ? 501  ASP E CB  1 
ATOM   15313 C  CG  . ASP E  1 501 ? -12.805 -55.428 -88.001  1.00 266.69 ? 501  ASP E CG  1 
ATOM   15314 O  OD1 . ASP E  1 501 ? -11.842 -56.170 -87.715  1.00 270.97 ? 501  ASP E OD1 1 
ATOM   15315 O  OD2 . ASP E  1 501 ? -12.784 -54.610 -88.945  1.00 280.58 ? 501  ASP E OD2 1 
ATOM   15316 N  N   . LYS E  1 502 ? -12.849 -54.997 -83.668  1.00 260.27 ? 502  LYS E N   1 
ATOM   15317 C  CA  . LYS E  1 502 ? -12.226 -53.945 -82.872  1.00 262.80 ? 502  LYS E CA  1 
ATOM   15318 C  C   . LYS E  1 502 ? -10.779 -53.701 -83.286  1.00 257.62 ? 502  LYS E C   1 
ATOM   15319 O  O   . LYS E  1 502 ? -10.315 -52.555 -83.273  1.00 262.28 ? 502  LYS E O   1 
ATOM   15320 C  CB  . LYS E  1 502 ? -12.285 -54.264 -81.383  1.00 256.95 ? 502  LYS E CB  1 
ATOM   15321 C  CG  . LYS E  1 502 ? -11.698 -53.113 -80.599  1.00 256.62 ? 502  LYS E CG  1 
ATOM   15322 C  CD  . LYS E  1 502 ? -11.547 -53.368 -79.136  1.00 244.30 ? 502  LYS E CD  1 
ATOM   15323 C  CE  . LYS E  1 502 ? -10.982 -52.121 -78.477  1.00 239.88 ? 502  LYS E CE  1 
ATOM   15324 N  NZ  . LYS E  1 502 ? -11.911 -50.968 -78.584  1.00 236.72 ? 502  LYS E NZ  1 
ATOM   15325 N  N   . LEU E  1 503 ? -10.047 -54.764 -83.633  1.00 243.34 ? 503  LEU E N   1 
ATOM   15326 C  CA  . LEU E  1 503 ? -8.624  -54.691 -83.962  1.00 246.03 ? 503  LEU E CA  1 
ATOM   15327 C  C   . LEU E  1 503 ? -8.280  -53.495 -84.845  1.00 246.93 ? 503  LEU E C   1 
ATOM   15328 O  O   . LEU E  1 503 ? -7.178  -52.946 -84.754  1.00 249.44 ? 503  LEU E O   1 
ATOM   15329 C  CB  . LEU E  1 503 ? -8.176  -55.985 -84.647  1.00 255.00 ? 503  LEU E CB  1 
ATOM   15330 C  CG  . LEU E  1 503 ? -7.546  -57.069 -83.768  1.00 266.12 ? 503  LEU E CG  1 
ATOM   15331 C  CD1 . LEU E  1 503 ? -8.296  -57.228 -82.449  1.00 265.96 ? 503  LEU E CD1 1 
ATOM   15332 C  CD2 . LEU E  1 503 ? -7.485  -58.392 -84.520  1.00 267.73 ? 503  LEU E CD2 1 
ATOM   15333 N  N   . LYS E  1 504 ? -9.219  -53.079 -85.692  1.00 249.19 ? 504  LYS E N   1 
ATOM   15334 C  CA  . LYS E  1 504 ? -9.073  -51.861 -86.484  1.00 259.46 ? 504  LYS E CA  1 
ATOM   15335 C  C   . LYS E  1 504 ? -9.302  -50.648 -85.588  1.00 256.53 ? 504  LYS E C   1 
ATOM   15336 O  O   . LYS E  1 504 ? -10.424 -50.411 -85.129  1.00 255.53 ? 504  LYS E O   1 
ATOM   15337 C  CB  . LYS E  1 504 ? -10.050 -51.869 -87.655  1.00 267.76 ? 504  LYS E CB  1 
ATOM   15338 C  CG  . LYS E  1 504 ? -9.735  -52.905 -88.722  1.00 278.40 ? 504  LYS E CG  1 
ATOM   15339 C  CD  . LYS E  1 504 ? -8.417  -52.603 -89.421  1.00 281.27 ? 504  LYS E CD  1 
ATOM   15340 C  CE  . LYS E  1 504 ? -8.191  -53.545 -90.596  1.00 277.07 ? 504  LYS E CE  1 
ATOM   15341 N  NZ  . LYS E  1 504 ? -6.931  -53.236 -91.325  1.00 272.38 ? 504  LYS E NZ  1 
ATOM   15342 N  N   . GLN E  1 505 ? -8.239  -49.887 -85.327  1.00 264.65 ? 505  GLN E N   1 
ATOM   15343 C  CA  . GLN E  1 505 ? -8.344  -48.685 -84.510  1.00 263.37 ? 505  GLN E CA  1 
ATOM   15344 C  C   . GLN E  1 505 ? -9.247  -47.652 -85.183  1.00 275.65 ? 505  GLN E C   1 
ATOM   15345 O  O   . GLN E  1 505 ? -9.509  -47.704 -86.389  1.00 295.05 ? 505  GLN E O   1 
ATOM   15346 C  CB  . GLN E  1 505 ? -6.958  -48.091 -84.254  1.00 254.99 ? 505  GLN E CB  1 
ATOM   15347 C  CG  . GLN E  1 505 ? -6.022  -48.998 -83.459  1.00 253.41 ? 505  GLN E CG  1 
ATOM   15348 C  CD  . GLN E  1 505 ? -6.397  -49.099 -81.987  1.00 251.52 ? 505  GLN E CD  1 
ATOM   15349 O  OE1 . GLN E  1 505 ? -7.257  -48.365 -81.498  1.00 257.56 ? 505  GLN E OE1 1 
ATOM   15350 N  NE2 . GLN E  1 505 ? -5.745  -50.010 -81.273  1.00 242.17 ? 505  GLN E NE2 1 
ATOM   15351 N  N   . LYS E  1 506 ? -9.727  -46.698 -84.380  1.00 268.56 ? 506  LYS E N   1 
ATOM   15352 C  CA  . LYS E  1 506 ? -10.602 -45.640 -84.875  1.00 268.04 ? 506  LYS E CA  1 
ATOM   15353 C  C   . LYS E  1 506 ? -9.923  -44.821 -85.966  1.00 291.48 ? 506  LYS E C   1 
ATOM   15354 O  O   . LYS E  1 506 ? -9.074  -43.968 -85.685  1.00 296.85 ? 506  LYS E O   1 
ATOM   15355 C  CB  . LYS E  1 506 ? -11.046 -44.729 -83.730  1.00 248.07 ? 506  LYS E CB  1 
ATOM   15356 C  CG  . LYS E  1 506 ? -12.120 -43.741 -84.137  1.00 242.66 ? 506  LYS E CG  1 
ATOM   15357 C  CD  . LYS E  1 506 ? -13.298 -44.454 -84.778  1.00 240.07 ? 506  LYS E CD  1 
ATOM   15358 C  CE  . LYS E  1 506 ? -14.375 -43.464 -85.180  1.00 238.90 ? 506  LYS E CE  1 
ATOM   15359 N  NZ  . LYS E  1 506 ? -14.910 -42.728 -84.003  1.00 242.30 ? 506  LYS E NZ  1 
ATOM   15360 N  N   . GLY E  1 507 ? -10.301 -45.081 -87.215  1.00 306.26 ? 507  GLY E N   1 
ATOM   15361 C  CA  . GLY E  1 507 ? -9.754  -44.379 -88.357  1.00 306.06 ? 507  GLY E CA  1 
ATOM   15362 C  C   . GLY E  1 507 ? -9.444  -45.350 -89.476  1.00 298.28 ? 507  GLY E C   1 
ATOM   15363 O  O   . GLY E  1 507 ? -9.271  -44.957 -90.634  1.00 298.24 ? 507  GLY E O   1 
ATOM   15364 N  N   . ALA E  1 508 ? -9.364  -46.633 -89.128  1.00 284.46 ? 508  ALA E N   1 
ATOM   15365 C  CA  . ALA E  1 508 ? -9.054  -47.681 -90.090  1.00 278.38 ? 508  ALA E CA  1 
ATOM   15366 C  C   . ALA E  1 508 ? -10.258 -48.000 -90.965  1.00 287.80 ? 508  ALA E C   1 
ATOM   15367 O  O   . ALA E  1 508 ? -11.178 -47.186 -91.094  1.00 299.31 ? 508  ALA E O   1 
ATOM   15368 C  CB  . ALA E  1 508 ? -8.576  -48.943 -89.374  1.00 272.73 ? 508  ALA E CB  1 
ATOM   15369 N  N   . ILE E  1 509 ? -10.256 -49.185 -91.570  1.00 278.63 ? 509  ILE E N   1 
ATOM   15370 C  CA  . ILE E  1 509 ? -11.344 -49.647 -92.426  1.00 280.80 ? 509  ILE E CA  1 
ATOM   15371 C  C   . ILE E  1 509 ? -12.054 -50.791 -91.708  1.00 270.21 ? 509  ILE E C   1 
ATOM   15372 O  O   . ILE E  1 509 ? -11.467 -51.853 -91.462  1.00 272.45 ? 509  ILE E O   1 
ATOM   15373 C  CB  . ILE E  1 509 ? -10.833 -50.068 -93.811  1.00 292.32 ? 509  ILE E CB  1 
ATOM   15374 C  CG1 . ILE E  1 509 ? -11.924 -50.808 -94.591  1.00 285.06 ? 509  ILE E CG1 1 
ATOM   15375 C  CG2 . ILE E  1 509 ? -9.541  -50.881 -93.710  1.00 292.02 ? 509  ILE E CG2 1 
ATOM   15376 C  CD1 . ILE E  1 509 ? -13.103 -49.946 -94.982  1.00 276.48 ? 509  ILE E CD1 1 
ATOM   15377 N  N   . ARG E  1 510 ? -13.312 -50.563 -91.341  1.00 260.00 ? 510  ARG E N   1 
ATOM   15378 C  CA  . ARG E  1 510 ? -14.101 -51.532 -90.596  1.00 256.02 ? 510  ARG E CA  1 
ATOM   15379 C  C   . ARG E  1 510 ? -14.788 -52.469 -91.581  1.00 269.78 ? 510  ARG E C   1 
ATOM   15380 O  O   . ARG E  1 510 ? -15.006 -52.122 -92.743  1.00 288.37 ? 510  ARG E O   1 
ATOM   15381 C  CB  . ARG E  1 510 ? -15.138 -50.822 -89.718  1.00 246.57 ? 510  ARG E CB  1 
ATOM   15382 C  CG  . ARG E  1 510 ? -15.698 -51.662 -88.576  1.00 243.16 ? 510  ARG E CG  1 
ATOM   15383 C  CD  . ARG E  1 510 ? -14.686 -51.810 -87.447  1.00 240.34 ? 510  ARG E CD  1 
ATOM   15384 N  NE  . ARG E  1 510 ? -14.330 -50.517 -86.868  1.00 234.11 ? 510  ARG E NE  1 
ATOM   15385 C  CZ  . ARG E  1 510 ? -13.679 -50.366 -85.719  1.00 230.97 ? 510  ARG E CZ  1 
ATOM   15386 N  NH1 . ARG E  1 510 ? -13.310 -51.430 -85.020  1.00 231.74 ? 510  ARG E NH1 1 
ATOM   15387 N  NH2 . ARG E  1 510 ? -13.400 -49.152 -85.266  1.00 227.42 ? 510  ARG E NH2 1 
ATOM   15388 N  N   . ARG E  1 511 ? -15.127 -53.675 -91.112  1.00 259.48 ? 511  ARG E N   1 
ATOM   15389 C  CA  . ARG E  1 511 ? -15.685 -54.686 -92.001  1.00 261.56 ? 511  ARG E CA  1 
ATOM   15390 C  C   . ARG E  1 511 ? -16.933 -55.392 -91.481  1.00 256.15 ? 511  ARG E C   1 
ATOM   15391 O  O   . ARG E  1 511 ? -17.476 -56.243 -92.196  1.00 253.53 ? 511  ARG E O   1 
ATOM   15392 C  CB  . ARG E  1 511 ? -14.620 -55.744 -92.337  1.00 270.87 ? 511  ARG E CB  1 
ATOM   15393 C  CG  . ARG E  1 511 ? -13.393 -55.184 -93.048  1.00 275.93 ? 511  ARG E CG  1 
ATOM   15394 C  CD  . ARG E  1 511 ? -12.183 -56.083 -92.874  1.00 270.57 ? 511  ARG E CD  1 
ATOM   15395 N  NE  . ARG E  1 511 ? -11.823 -56.243 -91.471  1.00 267.42 ? 511  ARG E NE  1 
ATOM   15396 C  CZ  . ARG E  1 511 ? -10.827 -57.006 -91.043  1.00 268.12 ? 511  ARG E CZ  1 
ATOM   15397 N  NH1 . ARG E  1 511 ? -10.091 -57.686 -91.912  1.00 267.57 ? 511  ARG E NH1 1 
ATOM   15398 N  NH2 . ARG E  1 511 ? -10.568 -57.095 -89.745  1.00 273.04 ? 511  ARG E NH2 1 
ATOM   15399 N  N   . ALA E  1 512 ? -17.405 -55.081 -90.277  1.00 267.93 ? 512  ALA E N   1 
ATOM   15400 C  CA  . ALA E  1 512 ? -18.588 -55.734 -89.735  1.00 275.46 ? 512  ALA E CA  1 
ATOM   15401 C  C   . ALA E  1 512 ? -19.522 -54.711 -89.102  1.00 277.21 ? 512  ALA E C   1 
ATOM   15402 O  O   . ALA E  1 512 ? -19.088 -53.657 -88.628  1.00 279.78 ? 512  ALA E O   1 
ATOM   15403 C  CB  . ALA E  1 512 ? -18.209 -56.806 -88.707  1.00 275.94 ? 512  ALA E CB  1 
ATOM   15404 N  N   . LEU E  1 513 ? -20.812 -55.051 -89.084  1.00 272.43 ? 513  LEU E N   1 
ATOM   15405 C  CA  . LEU E  1 513 ? -21.856 -54.235 -88.476  1.00 269.19 ? 513  LEU E CA  1 
ATOM   15406 C  C   . LEU E  1 513 ? -23.160 -55.022 -88.507  1.00 268.19 ? 513  LEU E C   1 
ATOM   15407 O  O   . LEU E  1 513 ? -23.424 -55.749 -89.468  1.00 272.98 ? 513  LEU E O   1 
ATOM   15408 C  CB  . LEU E  1 513 ? -22.012 -52.883 -89.194  1.00 265.39 ? 513  LEU E CB  1 
ATOM   15409 C  CG  . LEU E  1 513 ? -22.516 -52.817 -90.637  1.00 265.01 ? 513  LEU E CG  1 
ATOM   15410 C  CD1 . LEU E  1 513 ? -24.012 -52.568 -90.665  1.00 266.03 ? 513  LEU E CD1 1 
ATOM   15411 C  CD2 . LEU E  1 513 ? -21.783 -51.736 -91.404  1.00 266.23 ? 513  LEU E CD2 1 
ATOM   15412 N  N   . PHE E  1 514 ? -23.951 -54.890 -87.442  1.00 262.84 ? 514  PHE E N   1 
ATOM   15413 C  CA  . PHE E  1 514 ? -25.146 -55.703 -87.257  1.00 258.40 ? 514  PHE E CA  1 
ATOM   15414 C  C   . PHE E  1 514 ? -26.147 -55.497 -88.392  1.00 267.39 ? 514  PHE E C   1 
ATOM   15415 O  O   . PHE E  1 514 ? -26.121 -54.497 -89.115  1.00 269.15 ? 514  PHE E O   1 
ATOM   15416 C  CB  . PHE E  1 514 ? -25.808 -55.389 -85.915  1.00 254.86 ? 514  PHE E CB  1 
ATOM   15417 C  CG  . PHE E  1 514 ? -25.014 -55.849 -84.726  1.00 254.39 ? 514  PHE E CG  1 
ATOM   15418 C  CD1 . PHE E  1 514 ? -23.824 -55.230 -84.383  1.00 259.40 ? 514  PHE E CD1 1 
ATOM   15419 C  CD2 . PHE E  1 514 ? -25.454 -56.912 -83.960  1.00 251.38 ? 514  PHE E CD2 1 
ATOM   15420 C  CE1 . PHE E  1 514 ? -23.091 -55.660 -83.293  1.00 253.72 ? 514  PHE E CE1 1 
ATOM   15421 C  CE2 . PHE E  1 514 ? -24.728 -57.345 -82.868  1.00 252.06 ? 514  PHE E CE2 1 
ATOM   15422 C  CZ  . PHE E  1 514 ? -23.544 -56.718 -82.535  1.00 251.40 ? 514  PHE E CZ  1 
ATOM   15423 N  N   . LEU E  1 515 ? -27.053 -56.469 -88.530  1.00 276.04 ? 515  LEU E N   1 
ATOM   15424 C  CA  . LEU E  1 515 ? -27.949 -56.501 -89.683  1.00 276.80 ? 515  LEU E CA  1 
ATOM   15425 C  C   . LEU E  1 515 ? -28.990 -55.389 -89.616  1.00 275.57 ? 515  LEU E C   1 
ATOM   15426 O  O   . LEU E  1 515 ? -29.182 -54.650 -90.588  1.00 282.16 ? 515  LEU E O   1 
ATOM   15427 C  CB  . LEU E  1 515 ? -28.625 -57.869 -89.780  1.00 279.83 ? 515  LEU E CB  1 
ATOM   15428 C  CG  . LEU E  1 515 ? -29.526 -58.097 -90.997  1.00 291.16 ? 515  LEU E CG  1 
ATOM   15429 C  CD1 . LEU E  1 515 ? -28.735 -58.002 -92.296  1.00 295.33 ? 515  LEU E CD1 1 
ATOM   15430 C  CD2 . LEU E  1 515 ? -30.236 -59.439 -90.899  1.00 291.83 ? 515  LEU E CD2 1 
ATOM   15431 N  N   . TYR E  1 516 ? -29.674 -55.252 -88.483  1.00 278.27 ? 516  TYR E N   1 
ATOM   15432 C  CA  . TYR E  1 516 ? -30.718 -54.244 -88.349  1.00 281.25 ? 516  TYR E CA  1 
ATOM   15433 C  C   . TYR E  1 516 ? -30.229 -52.978 -87.665  1.00 272.02 ? 516  TYR E C   1 
ATOM   15434 O  O   . TYR E  1 516 ? -30.714 -51.886 -87.983  1.00 274.67 ? 516  TYR E O   1 
ATOM   15435 C  CB  . TYR E  1 516 ? -31.913 -54.812 -87.575  1.00 286.31 ? 516  TYR E CB  1 
ATOM   15436 C  CG  . TYR E  1 516 ? -33.245 -54.160 -87.905  1.00 290.16 ? 516  TYR E CG  1 
ATOM   15437 C  CD1 . TYR E  1 516 ? -33.349 -53.192 -88.902  1.00 287.81 ? 516  TYR E CD1 1 
ATOM   15438 C  CD2 . TYR E  1 516 ? -34.395 -54.510 -87.212  1.00 291.67 ? 516  TYR E CD2 1 
ATOM   15439 C  CE1 . TYR E  1 516 ? -34.567 -52.597 -89.198  1.00 289.25 ? 516  TYR E CE1 1 
ATOM   15440 C  CE2 . TYR E  1 516 ? -35.613 -53.922 -87.500  1.00 291.09 ? 516  TYR E CE2 1 
ATOM   15441 C  CZ  . TYR E  1 516 ? -35.695 -52.967 -88.493  1.00 285.57 ? 516  TYR E CZ  1 
ATOM   15442 O  OH  . TYR E  1 516 ? -36.910 -52.384 -88.776  1.00 269.96 ? 516  TYR E OH  1 
ATOM   15443 N  N   . SER E  1 517 ? -29.279 -53.099 -86.735  1.00 248.68 ? 517  SER E N   1 
ATOM   15444 C  CA  . SER E  1 517 ? -28.746 -51.927 -86.053  1.00 248.85 ? 517  SER E CA  1 
ATOM   15445 C  C   . SER E  1 517 ? -27.959 -51.024 -86.992  1.00 256.95 ? 517  SER E C   1 
ATOM   15446 O  O   . SER E  1 517 ? -27.808 -49.833 -86.700  1.00 263.41 ? 517  SER E O   1 
ATOM   15447 C  CB  . SER E  1 517 ? -27.863 -52.354 -84.875  1.00 240.82 ? 517  SER E CB  1 
ATOM   15448 O  OG  . SER E  1 517 ? -27.356 -51.230 -84.176  1.00 237.14 ? 517  SER E OG  1 
ATOM   15449 N  N   . ARG E  1 518 ? -27.453 -51.566 -88.103  1.00 254.93 ? 518  ARG E N   1 
ATOM   15450 C  CA  . ARG E  1 518 ? -26.660 -50.806 -89.072  1.00 249.93 ? 518  ARG E CA  1 
ATOM   15451 C  C   . ARG E  1 518 ? -25.502 -50.082 -88.390  1.00 245.97 ? 518  ARG E C   1 
ATOM   15452 O  O   . ARG E  1 518 ? -25.149 -48.957 -88.747  1.00 240.16 ? 518  ARG E O   1 
ATOM   15453 C  CB  . ARG E  1 518 ? -27.527 -49.818 -89.853  1.00 258.26 ? 518  ARG E CB  1 
ATOM   15454 C  CG  . ARG E  1 518 ? -28.894 -50.351 -90.254  1.00 267.27 ? 518  ARG E CG  1 
ATOM   15455 C  CD  . ARG E  1 518 ? -28.781 -51.581 -91.134  1.00 270.12 ? 518  ARG E CD  1 
ATOM   15456 N  NE  . ARG E  1 518 ? -29.996 -51.812 -91.913  1.00 269.89 ? 518  ARG E NE  1 
ATOM   15457 C  CZ  . ARG E  1 518 ? -30.232 -51.287 -93.112  1.00 260.07 ? 518  ARG E CZ  1 
ATOM   15458 N  NH1 . ARG E  1 518 ? -29.335 -50.492 -93.679  1.00 262.74 ? 518  ARG E NH1 1 
ATOM   15459 N  NH2 . ARG E  1 518 ? -31.366 -51.559 -93.743  1.00 252.85 ? 518  ARG E NH2 1 
ATOM   15460 N  N   . SER E  1 519 ? -24.905 -50.734 -87.392  1.00 252.14 ? 519  SER E N   1 
ATOM   15461 C  CA  . SER E  1 519 ? -23.888 -50.089 -86.572  1.00 262.17 ? 519  SER E CA  1 
ATOM   15462 C  C   . SER E  1 519 ? -22.953 -51.128 -85.964  1.00 262.66 ? 519  SER E C   1 
ATOM   15463 O  O   . SER E  1 519 ? -23.420 -52.084 -85.328  1.00 265.57 ? 519  SER E O   1 
ATOM   15464 C  CB  . SER E  1 519 ? -24.552 -49.249 -85.477  1.00 260.59 ? 519  SER E CB  1 
ATOM   15465 O  OG  . SER E  1 519 ? -23.590 -48.594 -84.668  1.00 258.08 ? 519  SER E OG  1 
ATOM   15466 N  N   . PRO E  1 520 ? -21.618 -50.978 -86.147  1.00 262.99 ? 520  PRO E N   1 
ATOM   15467 C  CA  . PRO E  1 520 ? -20.663 -51.989 -85.667  1.00 257.40 ? 520  PRO E CA  1 
ATOM   15468 C  C   . PRO E  1 520 ? -20.800 -52.326 -84.190  1.00 253.66 ? 520  PRO E C   1 
ATOM   15469 O  O   . PRO E  1 520 ? -20.241 -53.326 -83.728  1.00 254.67 ? 520  PRO E O   1 
ATOM   15470 C  CB  . PRO E  1 520 ? -19.301 -51.343 -85.956  1.00 252.98 ? 520  PRO E CB  1 
ATOM   15471 C  CG  . PRO E  1 520 ? -19.548 -50.458 -87.123  1.00 257.17 ? 520  PRO E CG  1 
ATOM   15472 C  CD  . PRO E  1 520 ? -20.967 -49.952 -86.980  1.00 262.24 ? 520  PRO E CD  1 
ATOM   15473 N  N   . SER E  1 521 ? -21.511 -51.490 -83.438  1.00 238.98 ? 521  SER E N   1 
ATOM   15474 C  CA  . SER E  1 521 ? -21.714 -51.702 -82.015  1.00 228.91 ? 521  SER E CA  1 
ATOM   15475 C  C   . SER E  1 521 ? -23.204 -51.748 -81.707  1.00 235.15 ? 521  SER E C   1 
ATOM   15476 O  O   . SER E  1 521 ? -24.011 -51.063 -82.344  1.00 230.78 ? 521  SER E O   1 
ATOM   15477 C  CB  . SER E  1 521 ? -21.034 -50.605 -81.173  1.00 224.55 ? 521  SER E CB  1 
ATOM   15478 O  OG  . SER E  1 521 ? -21.404 -49.300 -81.589  1.00 222.76 ? 521  SER E OG  1 
ATOM   15479 N  N   . HIS E  1 522 ? -23.562 -52.573 -80.725  1.00 250.45 ? 522  HIS E N   1 
ATOM   15480 C  CA  . HIS E  1 522 ? -24.944 -52.719 -80.291  1.00 259.03 ? 522  HIS E CA  1 
ATOM   15481 C  C   . HIS E  1 522 ? -24.976 -52.666 -78.773  1.00 253.40 ? 522  HIS E C   1 
ATOM   15482 O  O   . HIS E  1 522 ? -24.282 -53.440 -78.106  1.00 243.28 ? 522  HIS E O   1 
ATOM   15483 C  CB  . HIS E  1 522 ? -25.558 -54.035 -80.799  1.00 256.17 ? 522  HIS E CB  1 
ATOM   15484 C  CG  . HIS E  1 522 ? -26.971 -54.259 -80.351  1.00 258.62 ? 522  HIS E CG  1 
ATOM   15485 N  ND1 . HIS E  1 522 ? -27.293 -54.989 -79.227  1.00 252.80 ? 522  HIS E ND1 1 
ATOM   15486 C  CD2 . HIS E  1 522 ? -28.148 -53.849 -80.882  1.00 260.81 ? 522  HIS E CD2 1 
ATOM   15487 C  CE1 . HIS E  1 522 ? -28.606 -55.016 -79.082  1.00 251.87 ? 522  HIS E CE1 1 
ATOM   15488 N  NE2 . HIS E  1 522 ? -29.149 -54.332 -80.073  1.00 258.81 ? 522  HIS E NE2 1 
ATOM   15489 N  N   . SER E  1 523 ? -25.770 -51.752 -78.234  1.00 264.86 ? 523  SER E N   1 
ATOM   15490 C  CA  . SER E  1 523 ? -25.944 -51.619 -76.798  1.00 256.04 ? 523  SER E CA  1 
ATOM   15491 C  C   . SER E  1 523 ? -27.259 -52.270 -76.394  1.00 264.03 ? 523  SER E C   1 
ATOM   15492 O  O   . SER E  1 523 ? -28.244 -52.227 -77.137  1.00 266.75 ? 523  SER E O   1 
ATOM   15493 C  CB  . SER E  1 523 ? -25.932 -50.146 -76.381  1.00 251.25 ? 523  SER E CB  1 
ATOM   15494 O  OG  . SER E  1 523 ? -26.046 -50.005 -74.978  1.00 254.59 ? 523  SER E OG  1 
ATOM   15495 N  N   . LYS E  1 524 ? -27.267 -52.876 -75.210  1.00 264.91 ? 524  LYS E N   1 
ATOM   15496 C  CA  . LYS E  1 524 ? -28.463 -53.545 -74.724  1.00 267.23 ? 524  LYS E CA  1 
ATOM   15497 C  C   . LYS E  1 524 ? -28.450 -53.566 -73.206  1.00 266.56 ? 524  LYS E C   1 
ATOM   15498 O  O   . LYS E  1 524 ? -27.464 -53.979 -72.588  1.00 255.41 ? 524  LYS E O   1 
ATOM   15499 C  CB  . LYS E  1 524 ? -28.571 -54.971 -75.273  1.00 257.87 ? 524  LYS E CB  1 
ATOM   15500 C  CG  . LYS E  1 524 ? -29.783 -55.739 -74.763  1.00 256.15 ? 524  LYS E CG  1 
ATOM   15501 C  CD  . LYS E  1 524 ? -31.087 -55.065 -75.174  1.00 255.61 ? 524  LYS E CD  1 
ATOM   15502 C  CE  . LYS E  1 524 ? -32.285 -55.662 -74.446  1.00 253.25 ? 524  LYS E CE  1 
ATOM   15503 N  NZ  . LYS E  1 524 ? -32.515 -57.094 -74.769  1.00 253.84 ? 524  LYS E NZ  1 
ATOM   15504 N  N   . ASN E  1 525 ? -29.548 -53.107 -72.618  1.00 262.91 ? 525  ASN E N   1 
ATOM   15505 C  CA  . ASN E  1 525 ? -29.741 -53.149 -71.179  1.00 253.78 ? 525  ASN E CA  1 
ATOM   15506 C  C   . ASN E  1 525 ? -30.361 -54.499 -70.855  1.00 255.02 ? 525  ASN E C   1 
ATOM   15507 O  O   . ASN E  1 525 ? -31.402 -54.859 -71.417  1.00 270.44 ? 525  ASN E O   1 
ATOM   15508 C  CB  . ASN E  1 525 ? -30.645 -51.994 -70.741  1.00 248.06 ? 525  ASN E CB  1 
ATOM   15509 C  CG  . ASN E  1 525 ? -29.963 -50.653 -70.895  1.00 254.65 ? 525  ASN E CG  1 
ATOM   15510 O  OD1 . ASN E  1 525 ? -28.747 -50.550 -70.730  1.00 220.59 ? 525  ASN E OD1 1 
ATOM   15511 N  ND2 . ASN E  1 525 ? -30.719 -49.627 -71.242  1.00 340.17 ? 525  ASN E ND2 1 
ATOM   15512 N  N   . MET E  1 526 ? -29.751 -55.227 -69.924  1.00 235.06 ? 526  MET E N   1 
ATOM   15513 C  CA  . MET E  1 526 ? -30.106 -56.625 -69.703  1.00 228.00 ? 526  MET E CA  1 
ATOM   15514 C  C   . MET E  1 526 ? -30.416 -56.850 -68.233  1.00 228.51 ? 526  MET E C   1 
ATOM   15515 O  O   . MET E  1 526 ? -29.513 -56.831 -67.391  1.00 230.98 ? 526  MET E O   1 
ATOM   15516 C  CB  . MET E  1 526 ? -28.983 -57.555 -70.168  1.00 225.20 ? 526  MET E CB  1 
ATOM   15517 C  CG  . MET E  1 526 ? -29.493 -58.869 -70.730  1.00 233.80 ? 526  MET E CG  1 
ATOM   15518 S  SD  . MET E  1 526 ? -28.225 -60.096 -71.093  1.00 233.62 ? 526  MET E SD  1 
ATOM   15519 C  CE  . MET E  1 526 ? -29.251 -61.529 -71.425  1.00 240.82 ? 526  MET E CE  1 
ATOM   15520 N  N   . THR E  1 527 ? -31.690 -57.064 -67.931  1.00 239.98 ? 527  THR E N   1 
ATOM   15521 C  CA  . THR E  1 527 ? -32.102 -57.548 -66.624  1.00 252.10 ? 527  THR E CA  1 
ATOM   15522 C  C   . THR E  1 527 ? -32.033 -59.071 -66.630  1.00 254.16 ? 527  THR E C   1 
ATOM   15523 O  O   . THR E  1 527 ? -32.749 -59.729 -67.394  1.00 259.89 ? 527  THR E O   1 
ATOM   15524 C  CB  . THR E  1 527 ? -33.513 -57.073 -66.288  1.00 260.12 ? 527  THR E CB  1 
ATOM   15525 O  OG1 . THR E  1 527 ? -33.509 -55.648 -66.138  1.00 263.59 ? 527  THR E OG1 1 
ATOM   15526 C  CG2 . THR E  1 527 ? -33.998 -57.729 -65.005  1.00 259.15 ? 527  THR E CG2 1 
ATOM   15527 N  N   . ILE E  1 528 ? -31.155 -59.625 -65.800  1.00 241.76 ? 528  ILE E N   1 
ATOM   15528 C  CA  . ILE E  1 528 ? -31.065 -61.065 -65.617  1.00 238.45 ? 528  ILE E CA  1 
ATOM   15529 C  C   . ILE E  1 528 ? -31.282 -61.359 -64.142  1.00 239.10 ? 528  ILE E C   1 
ATOM   15530 O  O   . ILE E  1 528 ? -30.988 -60.531 -63.273  1.00 234.69 ? 528  ILE E O   1 
ATOM   15531 C  CB  . ILE E  1 528 ? -29.721 -61.652 -66.108  1.00 234.04 ? 528  ILE E CB  1 
ATOM   15532 C  CG1 . ILE E  1 528 ? -28.596 -61.371 -65.110  1.00 230.30 ? 528  ILE E CG1 1 
ATOM   15533 C  CG2 . ILE E  1 528 ? -29.357 -61.103 -67.479  1.00 238.98 ? 528  ILE E CG2 1 
ATOM   15534 C  CD1 . ILE E  1 528 ? -27.284 -62.016 -65.485  1.00 228.01 ? 528  ILE E CD1 1 
ATOM   15535 N  N   . SER E  1 529 ? -31.791 -62.554 -63.859  1.00 240.16 ? 529  SER E N   1 
ATOM   15536 C  CA  . SER E  1 529 ? -32.044 -62.998 -62.495  1.00 244.45 ? 529  SER E CA  1 
ATOM   15537 C  C   . SER E  1 529 ? -30.966 -63.986 -62.091  1.00 240.90 ? 529  SER E C   1 
ATOM   15538 O  O   . SER E  1 529 ? -30.654 -64.912 -62.847  1.00 242.10 ? 529  SER E O   1 
ATOM   15539 C  CB  . SER E  1 529 ? -33.421 -63.653 -62.376  1.00 258.90 ? 529  SER E CB  1 
ATOM   15540 O  OG  . SER E  1 529 ? -33.471 -64.860 -63.122  1.00 261.80 ? 529  SER E OG  1 
ATOM   15541 N  N   . ARG E  1 530 ? -30.387 -63.785 -60.916  1.00 255.15 ? 530  ARG E N   1 
ATOM   15542 C  CA  . ARG E  1 530 ? -29.368 -64.722 -60.486  1.00 261.54 ? 530  ARG E CA  1 
ATOM   15543 C  C   . ARG E  1 530 ? -30.052 -66.006 -60.038  1.00 264.82 ? 530  ARG E C   1 
ATOM   15544 O  O   . ARG E  1 530 ? -31.205 -65.993 -59.592  1.00 270.74 ? 530  ARG E O   1 
ATOM   15545 C  CB  . ARG E  1 530 ? -28.529 -64.151 -59.341  1.00 263.85 ? 530  ARG E CB  1 
ATOM   15546 C  CG  . ARG E  1 530 ? -28.953 -64.621 -57.964  1.00 266.98 ? 530  ARG E CG  1 
ATOM   15547 C  CD  . ARG E  1 530 ? -28.150 -63.951 -56.865  1.00 263.51 ? 530  ARG E CD  1 
ATOM   15548 N  NE  . ARG E  1 530 ? -28.296 -64.664 -55.598  1.00 266.28 ? 530  ARG E NE  1 
ATOM   15549 C  CZ  . ARG E  1 530 ? -29.340 -64.574 -54.779  1.00 267.05 ? 530  ARG E CZ  1 
ATOM   15550 N  NH1 . ARG E  1 530 ? -30.384 -63.814 -55.083  1.00 265.37 ? 530  ARG E NH1 1 
ATOM   15551 N  NH2 . ARG E  1 530 ? -29.352 -65.285 -53.661  1.00 270.85 ? 530  ARG E NH2 1 
ATOM   15552 N  N   . GLY E  1 531 ? -29.357 -67.125 -60.207  1.00 268.07 ? 531  GLY E N   1 
ATOM   15553 C  CA  . GLY E  1 531 ? -29.868 -68.374 -59.684  1.00 281.61 ? 531  GLY E CA  1 
ATOM   15554 C  C   . GLY E  1 531 ? -30.883 -69.104 -60.542  1.00 294.93 ? 531  GLY E C   1 
ATOM   15555 O  O   . GLY E  1 531 ? -30.986 -70.335 -60.457  1.00 310.90 ? 531  GLY E O   1 
ATOM   15556 N  N   . GLY E  1 532 ? -31.650 -68.386 -61.360  1.00 280.66 ? 532  GLY E N   1 
ATOM   15557 C  CA  . GLY E  1 532 ? -32.718 -69.025 -62.107  1.00 283.55 ? 532  GLY E CA  1 
ATOM   15558 C  C   . GLY E  1 532 ? -32.224 -69.905 -63.238  1.00 293.71 ? 532  GLY E C   1 
ATOM   15559 O  O   . GLY E  1 532 ? -32.146 -71.128 -63.096  1.00 303.30 ? 532  GLY E O   1 
ATOM   15560 N  N   . LEU E  1 533 ? -31.862 -69.286 -64.357  1.00 293.38 ? 533  LEU E N   1 
ATOM   15561 C  CA  . LEU E  1 533 ? -31.352 -69.988 -65.525  1.00 289.61 ? 533  LEU E CA  1 
ATOM   15562 C  C   . LEU E  1 533 ? -30.453 -69.020 -66.273  1.00 275.95 ? 533  LEU E C   1 
ATOM   15563 O  O   . LEU E  1 533 ? -30.440 -67.817 -66.000  1.00 279.86 ? 533  LEU E O   1 
ATOM   15564 C  CB  . LEU E  1 533 ? -32.471 -70.497 -66.454  1.00 294.73 ? 533  LEU E CB  1 
ATOM   15565 C  CG  . LEU E  1 533 ? -33.618 -71.410 -66.002  1.00 297.08 ? 533  LEU E CG  1 
ATOM   15566 C  CD1 . LEU E  1 533 ? -34.661 -71.518 -67.106  1.00 294.89 ? 533  LEU E CD1 1 
ATOM   15567 C  CD2 . LEU E  1 533 ? -33.113 -72.793 -65.626  1.00 302.05 ? 533  LEU E CD2 1 
ATOM   15568 N  N   . MET E  1 534 ? -29.677 -69.555 -67.206  1.00 259.14 ? 534  MET E N   1 
ATOM   15569 C  CA  . MET E  1 534 ? -28.827 -68.705 -68.021  1.00 254.85 ? 534  MET E CA  1 
ATOM   15570 C  C   . MET E  1 534 ? -29.673 -68.079 -69.117  1.00 266.06 ? 534  MET E C   1 
ATOM   15571 O  O   . MET E  1 534 ? -30.314 -68.791 -69.896  1.00 277.55 ? 534  MET E O   1 
ATOM   15572 C  CB  . MET E  1 534 ? -27.681 -69.511 -68.629  1.00 254.24 ? 534  MET E CB  1 
ATOM   15573 C  CG  . MET E  1 534 ? -26.700 -68.671 -69.426  1.00 252.41 ? 534  MET E CG  1 
ATOM   15574 S  SD  . MET E  1 534 ? -25.493 -69.697 -70.275  1.00 258.04 ? 534  MET E SD  1 
ATOM   15575 C  CE  . MET E  1 534 ? -24.835 -70.634 -68.901  1.00 262.94 ? 534  MET E CE  1 
ATOM   15576 N  N   . GLN E  1 535 ? -29.669 -66.750 -69.183  1.00 260.24 ? 535  GLN E N   1 
ATOM   15577 C  CA  . GLN E  1 535 ? -30.398 -66.031 -70.220  1.00 253.71 ? 535  GLN E CA  1 
ATOM   15578 C  C   . GLN E  1 535 ? -29.455 -65.712 -71.372  1.00 251.31 ? 535  GLN E C   1 
ATOM   15579 O  O   . GLN E  1 535 ? -28.413 -65.077 -71.176  1.00 244.42 ? 535  GLN E O   1 
ATOM   15580 C  CB  . GLN E  1 535 ? -31.026 -64.750 -69.674  1.00 240.83 ? 535  GLN E CB  1 
ATOM   15581 C  CG  . GLN E  1 535 ? -32.371 -64.953 -68.993  1.00 237.39 ? 535  GLN E CG  1 
ATOM   15582 C  CD  . GLN E  1 535 ? -32.901 -63.675 -68.383  1.00 232.70 ? 535  GLN E CD  1 
ATOM   15583 O  OE1 . GLN E  1 535 ? -32.136 -62.769 -68.063  1.00 227.25 ? 535  GLN E OE1 1 
ATOM   15584 N  NE2 . GLN E  1 535 ? -34.217 -63.589 -68.231  1.00 235.16 ? 535  GLN E NE2 1 
ATOM   15585 N  N   . CYS E  1 536 ? -29.829 -66.147 -72.568  1.00 273.53 ? 536  CYS E N   1 
ATOM   15586 C  CA  . CYS E  1 536 ? -29.024 -65.976 -73.763  1.00 273.84 ? 536  CYS E CA  1 
ATOM   15587 C  C   . CYS E  1 536 ? -29.844 -65.227 -74.809  1.00 262.99 ? 536  CYS E C   1 
ATOM   15588 O  O   . CYS E  1 536 ? -31.076 -65.189 -74.744  1.00 265.20 ? 536  CYS E O   1 
ATOM   15589 C  CB  . CYS E  1 536 ? -28.556 -67.344 -74.277  1.00 290.60 ? 536  CYS E CB  1 
ATOM   15590 S  SG  . CYS E  1 536 ? -27.085 -67.342 -75.299  1.00 318.37 ? 536  CYS E SG  1 
ATOM   15591 N  N   . GLU E  1 537 ? -29.157 -64.625 -75.779  1.00 258.31 ? 537  GLU E N   1 
ATOM   15592 C  CA  . GLU E  1 537 ? -29.843 -63.862 -76.816  1.00 257.28 ? 537  GLU E CA  1 
ATOM   15593 C  C   . GLU E  1 537 ? -29.038 -63.893 -78.109  1.00 265.27 ? 537  GLU E C   1 
ATOM   15594 O  O   . GLU E  1 537 ? -27.820 -63.691 -78.089  1.00 277.60 ? 537  GLU E O   1 
ATOM   15595 C  CB  . GLU E  1 537 ? -30.071 -62.417 -76.362  1.00 252.16 ? 537  GLU E CB  1 
ATOM   15596 C  CG  . GLU E  1 537 ? -30.451 -61.469 -77.478  1.00 250.83 ? 537  GLU E CG  1 
ATOM   15597 C  CD  . GLU E  1 537 ? -30.802 -60.088 -76.968  1.00 251.84 ? 537  GLU E CD  1 
ATOM   15598 O  OE1 . GLU E  1 537 ? -31.388 -59.988 -75.870  1.00 253.27 ? 537  GLU E OE1 1 
ATOM   15599 O  OE2 . GLU E  1 537 ? -30.505 -59.101 -77.673  1.00 253.47 ? 537  GLU E OE2 1 
ATOM   15600 N  N   . GLU E  1 538 ? -29.720 -64.147 -79.224  1.00 266.55 ? 538  GLU E N   1 
ATOM   15601 C  CA  . GLU E  1 538 ? -29.093 -64.220 -80.535  1.00 266.68 ? 538  GLU E CA  1 
ATOM   15602 C  C   . GLU E  1 538 ? -29.388 -62.970 -81.366  1.00 272.63 ? 538  GLU E C   1 
ATOM   15603 O  O   . GLU E  1 538 ? -30.411 -62.302 -81.185  1.00 270.27 ? 538  GLU E O   1 
ATOM   15604 C  CB  . GLU E  1 538 ? -29.568 -65.480 -81.270  1.00 271.99 ? 538  GLU E CB  1 
ATOM   15605 C  CG  . GLU E  1 538 ? -28.761 -65.868 -82.503  1.00 278.10 ? 538  GLU E CG  1 
ATOM   15606 C  CD  . GLU E  1 538 ? -29.412 -66.994 -83.286  1.00 287.09 ? 538  GLU E CD  1 
ATOM   15607 O  OE1 . GLU E  1 538 ? -30.462 -67.501 -82.838  1.00 289.34 ? 538  GLU E OE1 1 
ATOM   15608 O  OE2 . GLU E  1 538 ? -28.873 -67.380 -84.345  1.00 294.08 ? 538  GLU E OE2 1 
ATOM   15609 N  N   . LEU E  1 539 ? -28.470 -62.660 -82.282  1.00 278.17 ? 539  LEU E N   1 
ATOM   15610 C  CA  . LEU E  1 539 ? -28.597 -61.517 -83.175  1.00 279.14 ? 539  LEU E CA  1 
ATOM   15611 C  C   . LEU E  1 539 ? -27.680 -61.774 -84.364  1.00 276.33 ? 539  LEU E C   1 
ATOM   15612 O  O   . LEU E  1 539 ? -26.705 -62.519 -84.256  1.00 274.20 ? 539  LEU E O   1 
ATOM   15613 C  CB  . LEU E  1 539 ? -28.247 -60.198 -82.472  1.00 269.24 ? 539  LEU E CB  1 
ATOM   15614 C  CG  . LEU E  1 539 ? -28.844 -58.891 -83.008  1.00 271.72 ? 539  LEU E CG  1 
ATOM   15615 C  CD1 . LEU E  1 539 ? -30.364 -58.937 -82.982  1.00 274.19 ? 539  LEU E CD1 1 
ATOM   15616 C  CD2 . LEU E  1 539 ? -28.345 -57.711 -82.192  1.00 268.46 ? 539  LEU E CD2 1 
ATOM   15617 N  N   . ILE E  1 540 ? -28.004 -61.159 -85.500  1.00 266.55 ? 540  ILE E N   1 
ATOM   15618 C  CA  . ILE E  1 540 ? -27.315 -61.403 -86.763  1.00 258.31 ? 540  ILE E CA  1 
ATOM   15619 C  C   . ILE E  1 540 ? -26.459 -60.198 -87.133  1.00 256.10 ? 540  ILE E C   1 
ATOM   15620 O  O   . ILE E  1 540 ? -26.936 -59.058 -87.120  1.00 255.08 ? 540  ILE E O   1 
ATOM   15621 C  CB  . ILE E  1 540 ? -28.306 -61.733 -87.888  1.00 260.26 ? 540  ILE E CB  1 
ATOM   15622 C  CG1 . ILE E  1 540 ? -29.087 -63.013 -87.572  1.00 264.05 ? 540  ILE E CG1 1 
ATOM   15623 C  CG2 . ILE E  1 540 ? -27.582 -61.850 -89.213  1.00 261.93 ? 540  ILE E CG2 1 
ATOM   15624 C  CD1 . ILE E  1 540 ? -30.062 -63.416 -88.661  1.00 267.14 ? 540  ILE E CD1 1 
ATOM   15625 N  N   . ALA E  1 541 ? -25.190 -60.459 -87.455  1.00 259.68 ? 541  ALA E N   1 
ATOM   15626 C  CA  . ALA E  1 541 ? -24.257 -59.480 -87.995  1.00 258.18 ? 541  ALA E CA  1 
ATOM   15627 C  C   . ALA E  1 541 ? -23.785 -59.966 -89.362  1.00 263.85 ? 541  ALA E C   1 
ATOM   15628 O  O   . ALA E  1 541 ? -23.767 -61.171 -89.631  1.00 268.53 ? 541  ALA E O   1 
ATOM   15629 C  CB  . ALA E  1 541 ? -23.048 -59.256 -87.058  1.00 256.23 ? 541  ALA E CB  1 
ATOM   15630 N  N   . TYR E  1 542 ? -23.404 -59.030 -90.239  1.00 262.81 ? 542  TYR E N   1 
ATOM   15631 C  CA  . TYR E  1 542 ? -22.942 -59.388 -91.572  1.00 265.52 ? 542  TYR E CA  1 
ATOM   15632 C  C   . TYR E  1 542 ? -21.607 -58.734 -91.912  1.00 259.36 ? 542  TYR E C   1 
ATOM   15633 O  O   . TYR E  1 542 ? -21.185 -57.744 -91.307  1.00 253.03 ? 542  TYR E O   1 
ATOM   15634 C  CB  . TYR E  1 542 ? -23.967 -59.014 -92.651  1.00 270.35 ? 542  TYR E CB  1 
ATOM   15635 C  CG  . TYR E  1 542 ? -24.107 -57.532 -92.900  1.00 268.79 ? 542  TYR E CG  1 
ATOM   15636 C  CD1 . TYR E  1 542 ? -24.936 -56.744 -92.110  1.00 271.48 ? 542  TYR E CD1 1 
ATOM   15637 C  CD2 . TYR E  1 542 ? -23.404 -56.916 -93.926  1.00 260.22 ? 542  TYR E CD2 1 
ATOM   15638 C  CE1 . TYR E  1 542 ? -25.063 -55.386 -92.342  1.00 261.53 ? 542  TYR E CE1 1 
ATOM   15639 C  CE2 . TYR E  1 542 ? -23.524 -55.565 -94.164  1.00 254.15 ? 542  TYR E CE2 1 
ATOM   15640 C  CZ  . TYR E  1 542 ? -24.352 -54.802 -93.370  1.00 250.14 ? 542  TYR E CZ  1 
ATOM   15641 O  OH  . TYR E  1 542 ? -24.471 -53.452 -93.609  1.00 246.78 ? 542  TYR E OH  1 
ATOM   15642 N  N   . LEU E  1 543 ? -20.937 -59.336 -92.894  1.00 264.56 ? 543  LEU E N   1 
ATOM   15643 C  CA  . LEU E  1 543 ? -19.689 -58.840 -93.453  1.00 267.78 ? 543  LEU E CA  1 
ATOM   15644 C  C   . LEU E  1 543 ? -19.958 -57.899 -94.626  1.00 274.19 ? 543  LEU E C   1 
ATOM   15645 O  O   . LEU E  1 543 ? -20.947 -58.052 -95.349  1.00 277.45 ? 543  LEU E O   1 
ATOM   15646 C  CB  . LEU E  1 543 ? -18.829 -60.013 -93.908  1.00 279.64 ? 543  LEU E CB  1 
ATOM   15647 C  CG  . LEU E  1 543 ? -17.503 -59.729 -94.609  1.00 293.74 ? 543  LEU E CG  1 
ATOM   15648 C  CD1 . LEU E  1 543 ? -16.517 -59.060 -93.654  1.00 290.83 ? 543  LEU E CD1 1 
ATOM   15649 C  CD2 . LEU E  1 543 ? -16.925 -61.008 -95.197  1.00 299.60 ? 543  LEU E CD2 1 
ATOM   15650 N  N   . ARG E  1 544 ? -19.045 -56.944 -94.830  1.00 274.67 ? 544  ARG E N   1 
ATOM   15651 C  CA  . ARG E  1 544 ? -19.082 -56.062 -95.993  1.00 284.59 ? 544  ARG E CA  1 
ATOM   15652 C  C   . ARG E  1 544 ? -18.637 -56.769 -97.274  1.00 290.96 ? 544  ARG E C   1 
ATOM   15653 O  O   . ARG E  1 544 ? -17.928 -57.779 -97.251  1.00 300.88 ? 544  ARG E O   1 
ATOM   15654 C  CB  . ARG E  1 544 ? -18.206 -54.821 -95.775  1.00 274.49 ? 544  ARG E CB  1 
ATOM   15655 C  CG  . ARG E  1 544 ? -18.759 -53.790 -94.792  1.00 262.47 ? 544  ARG E CG  1 
ATOM   15656 C  CD  . ARG E  1 544 ? -18.026 -52.459 -94.953  1.00 260.82 ? 544  ARG E CD  1 
ATOM   15657 N  NE  . ARG E  1 544 ? -18.608 -51.378 -94.160  1.00 263.85 ? 544  ARG E NE  1 
ATOM   15658 C  CZ  . ARG E  1 544 ? -18.499 -51.259 -92.840  1.00 273.13 ? 544  ARG E CZ  1 
ATOM   15659 N  NH1 . ARG E  1 544 ? -17.839 -52.168 -92.137  1.00 276.05 ? 544  ARG E NH1 1 
ATOM   15660 N  NH2 . ARG E  1 544 ? -19.061 -50.231 -92.218  1.00 272.10 ? 544  ARG E NH2 1 
ATOM   15661 N  N   . ASP E  1 545 ? -19.090 -56.225 -98.399  1.00 278.34 ? 545  ASP E N   1 
ATOM   15662 C  CA  . ASP E  1 545 ? -18.751 -56.722 -99.725  1.00 277.78 ? 545  ASP E CA  1 
ATOM   15663 C  C   . ASP E  1 545 ? -17.240 -56.699 -99.985  1.00 288.40 ? 545  ASP E C   1 
ATOM   15664 O  O   . ASP E  1 545 ? -16.475 -55.964 -99.354  1.00 286.36 ? 545  ASP E O   1 
ATOM   15665 C  CB  . ASP E  1 545 ? -19.488 -55.910 -100.785 1.00 276.80 ? 545  ASP E CB  1 
ATOM   15666 C  CG  . ASP E  1 545 ? -19.257 -56.439 -102.180 1.00 287.33 ? 545  ASP E CG  1 
ATOM   15667 O  OD1 . ASP E  1 545 ? -19.978 -57.372 -102.580 1.00 295.29 ? 545  ASP E OD1 1 
ATOM   15668 O  OD2 . ASP E  1 545 ? -18.359 -55.922 -102.877 1.00 289.05 ? 545  ASP E OD2 1 
ATOM   15669 N  N   . GLU E  1 546 ? -16.824 -57.536 -100.948 1.00 297.16 ? 546  GLU E N   1 
ATOM   15670 C  CA  . GLU E  1 546 ? -15.420 -57.647 -101.350 1.00 296.72 ? 546  GLU E CA  1 
ATOM   15671 C  C   . GLU E  1 546 ? -14.870 -56.336 -101.911 1.00 291.77 ? 546  GLU E C   1 
ATOM   15672 O  O   . GLU E  1 546 ? -13.739 -55.947 -101.596 1.00 293.68 ? 546  GLU E O   1 
ATOM   15673 C  CB  . GLU E  1 546 ? -15.273 -58.764 -102.391 1.00 295.43 ? 546  GLU E CB  1 
ATOM   15674 C  CG  . GLU E  1 546 ? -13.851 -59.026 -102.870 1.00 286.72 ? 546  GLU E CG  1 
ATOM   15675 C  CD  . GLU E  1 546 ? -13.767 -60.175 -103.860 1.00 280.94 ? 546  GLU E CD  1 
ATOM   15676 O  OE1 . GLU E  1 546 ? -14.818 -60.762 -104.198 1.00 285.37 ? 546  GLU E OE1 1 
ATOM   15677 O  OE2 . GLU E  1 546 ? -12.642 -60.489 -104.301 1.00 279.23 ? 546  GLU E OE2 1 
ATOM   15678 N  N   . SER E  1 547 ? -15.649 -55.637 -102.740 1.00 269.07 ? 547  SER E N   1 
ATOM   15679 C  CA  . SER E  1 547 ? -15.135 -54.445 -103.406 1.00 270.21 ? 547  SER E CA  1 
ATOM   15680 C  C   . SER E  1 547 ? -15.000 -53.249 -102.472 1.00 265.76 ? 547  SER E C   1 
ATOM   15681 O  O   . SER E  1 547 ? -14.403 -52.242 -102.866 1.00 267.42 ? 547  SER E O   1 
ATOM   15682 C  CB  . SER E  1 547 ? -16.036 -54.070 -104.592 1.00 275.27 ? 547  SER E CB  1 
ATOM   15683 O  OG  . SER E  1 547 ? -16.016 -55.056 -105.611 1.00 280.46 ? 547  SER E OG  1 
ATOM   15684 N  N   . GLU E  1 548 ? -15.533 -53.336 -101.254 1.00 274.65 ? 548  GLU E N   1 
ATOM   15685 C  CA  . GLU E  1 548 ? -15.499 -52.231 -100.305 1.00 275.34 ? 548  GLU E CA  1 
ATOM   15686 C  C   . GLU E  1 548 ? -14.231 -52.192 -99.463  1.00 275.38 ? 548  GLU E C   1 
ATOM   15687 O  O   . GLU E  1 548 ? -13.973 -51.175 -98.804  1.00 271.85 ? 548  GLU E O   1 
ATOM   15688 C  CB  . GLU E  1 548 ? -16.717 -52.299 -99.379  1.00 268.29 ? 548  GLU E CB  1 
ATOM   15689 C  CG  . GLU E  1 548 ? -18.040 -52.171 -100.114 1.00 262.06 ? 548  GLU E CG  1 
ATOM   15690 C  CD  . GLU E  1 548 ? -19.218 -52.050 -99.174  1.00 252.03 ? 548  GLU E CD  1 
ATOM   15691 O  OE1 . GLU E  1 548 ? -20.332 -51.755 -99.651  1.00 258.91 ? 548  GLU E OE1 1 
ATOM   15692 O  OE2 . GLU E  1 548 ? -19.033 -52.252 -97.957  1.00 248.47 ? 548  GLU E OE2 1 
ATOM   15693 N  N   . PHE E  1 549 ? -13.448 -53.269 -99.452  1.00 282.94 ? 549  PHE E N   1 
ATOM   15694 C  CA  . PHE E  1 549 ? -12.206 -53.298 -98.682  1.00 282.72 ? 549  PHE E CA  1 
ATOM   15695 C  C   . PHE E  1 549 ? -11.306 -54.388 -99.241  1.00 284.98 ? 549  PHE E C   1 
ATOM   15696 O  O   . PHE E  1 549 ? -11.740 -55.536 -99.389  1.00 292.51 ? 549  PHE E O   1 
ATOM   15697 C  CB  . PHE E  1 549 ? -12.489 -53.523 -97.193  1.00 274.38 ? 549  PHE E CB  1 
ATOM   15698 C  CG  . PHE E  1 549 ? -13.102 -54.859 -96.882  1.00 275.47 ? 549  PHE E CG  1 
ATOM   15699 C  CD1 . PHE E  1 549 ? -14.465 -55.053 -97.011  1.00 279.57 ? 549  PHE E CD1 1 
ATOM   15700 C  CD2 . PHE E  1 549 ? -12.319 -55.916 -96.448  1.00 277.89 ? 549  PHE E CD2 1 
ATOM   15701 C  CE1 . PHE E  1 549 ? -15.036 -56.277 -96.723  1.00 288.97 ? 549  PHE E CE1 1 
ATOM   15702 C  CE2 . PHE E  1 549 ? -12.886 -57.147 -96.160  1.00 286.36 ? 549  PHE E CE2 1 
ATOM   15703 C  CZ  . PHE E  1 549 ? -14.248 -57.325 -96.299  1.00 292.22 ? 549  PHE E CZ  1 
ATOM   15704 N  N   . ARG E  1 550 ? -10.072 -54.022 -99.598  1.00 276.90 ? 550  ARG E N   1 
ATOM   15705 C  CA  . ARG E  1 550 ? -9.099  -54.995 -100.079 1.00 277.90 ? 550  ARG E CA  1 
ATOM   15706 C  C   . ARG E  1 550 ? -8.446  -55.778 -98.945  1.00 283.61 ? 550  ARG E C   1 
ATOM   15707 O  O   . ARG E  1 550 ? -7.735  -56.754 -99.214  1.00 286.54 ? 550  ARG E O   1 
ATOM   15708 C  CB  . ARG E  1 550 ? -8.029  -54.298 -100.933 1.00 273.15 ? 550  ARG E CB  1 
ATOM   15709 C  CG  . ARG E  1 550 ? -7.448  -53.023 -100.333 1.00 268.09 ? 550  ARG E CG  1 
ATOM   15710 C  CD  . ARG E  1 550 ? -6.406  -52.403 -101.263 1.00 265.47 ? 550  ARG E CD  1 
ATOM   15711 N  NE  . ARG E  1 550 ? -5.662  -51.313 -100.633 1.00 263.69 ? 550  ARG E NE  1 
ATOM   15712 C  CZ  . ARG E  1 550 ? -5.945  -50.022 -100.778 1.00 264.35 ? 550  ARG E CZ  1 
ATOM   15713 N  NH1 . ARG E  1 550 ? -6.962  -49.642 -101.540 1.00 266.64 ? 550  ARG E NH1 1 
ATOM   15714 N  NH2 . ARG E  1 550 ? -5.205  -49.109 -100.164 1.00 262.99 ? 550  ARG E NH2 1 
ATOM   15715 N  N   . ASP E  1 551 ? -8.670  -55.374 -97.695  1.00 286.21 ? 551  ASP E N   1 
ATOM   15716 C  CA  . ASP E  1 551 ? -8.038  -55.977 -96.522  1.00 282.06 ? 551  ASP E CA  1 
ATOM   15717 C  C   . ASP E  1 551 ? -8.827  -57.218 -96.111  1.00 286.04 ? 551  ASP E C   1 
ATOM   15718 O  O   . ASP E  1 551 ? -9.757  -57.151 -95.305  1.00 280.22 ? 551  ASP E O   1 
ATOM   15719 C  CB  . ASP E  1 551 ? -7.967  -54.961 -95.386  1.00 272.94 ? 551  ASP E CB  1 
ATOM   15720 C  CG  . ASP E  1 551 ? -6.997  -55.366 -94.287  1.00 273.67 ? 551  ASP E CG  1 
ATOM   15721 O  OD1 . ASP E  1 551 ? -6.670  -56.566 -94.166  1.00 276.08 ? 551  ASP E OD1 1 
ATOM   15722 O  OD2 . ASP E  1 551 ? -6.573  -54.471 -93.527  1.00 275.28 ? 551  ASP E OD2 1 
ATOM   15723 N  N   . LYS E  1 552 ? -8.441  -58.375 -96.656  1.00 292.29 ? 552  LYS E N   1 
ATOM   15724 C  CA  . LYS E  1 552 ? -9.070  -59.649 -96.316  1.00 292.30 ? 552  LYS E CA  1 
ATOM   15725 C  C   . LYS E  1 552 ? -8.154  -60.532 -95.478  1.00 289.68 ? 552  LYS E C   1 
ATOM   15726 O  O   . LYS E  1 552 ? -8.417  -61.729 -95.324  1.00 290.90 ? 552  LYS E O   1 
ATOM   15727 C  CB  . LYS E  1 552 ? -9.498  -60.403 -97.578  1.00 289.25 ? 552  LYS E CB  1 
ATOM   15728 C  CG  . LYS E  1 552 ? -10.701 -59.825 -98.302  1.00 284.37 ? 552  LYS E CG  1 
ATOM   15729 C  CD  . LYS E  1 552 ? -10.262 -58.898 -99.417  1.00 283.14 ? 552  LYS E CD  1 
ATOM   15730 C  CE  . LYS E  1 552 ? -11.410 -58.584 -100.355 1.00 286.21 ? 552  LYS E CE  1 
ATOM   15731 N  NZ  . LYS E  1 552 ? -11.009 -57.671 -101.464 1.00 290.23 ? 552  LYS E NZ  1 
ATOM   15732 N  N   . LEU E  1 553 ? -7.095  -59.956 -94.915  1.00 281.50 ? 553  LEU E N   1 
ATOM   15733 C  CA  . LEU E  1 553 ? -6.116  -60.704 -94.142  1.00 281.76 ? 553  LEU E CA  1 
ATOM   15734 C  C   . LEU E  1 553 ? -6.211  -60.453 -92.647  1.00 268.68 ? 553  LEU E C   1 
ATOM   15735 O  O   . LEU E  1 553 ? -5.814  -61.314 -91.861  1.00 266.62 ? 553  LEU E O   1 
ATOM   15736 C  CB  . LEU E  1 553 ? -4.692  -60.369 -94.613  1.00 284.66 ? 553  LEU E CB  1 
ATOM   15737 C  CG  . LEU E  1 553 ? -4.336  -60.560 -96.093  1.00 274.62 ? 553  LEU E CG  1 
ATOM   15738 C  CD1 . LEU E  1 553 ? -4.966  -61.831 -96.650  1.00 278.05 ? 553  LEU E CD1 1 
ATOM   15739 C  CD2 . LEU E  1 553 ? -4.714  -59.345 -96.932  1.00 263.96 ? 553  LEU E CD2 1 
ATOM   15740 N  N   . THR E  1 554 ? -6.727  -59.301 -92.239  1.00 260.40 ? 554  THR E N   1 
ATOM   15741 C  CA  . THR E  1 554 ? -6.818  -58.914 -90.837  1.00 254.57 ? 554  THR E CA  1 
ATOM   15742 C  C   . THR E  1 554 ? -7.961  -59.664 -90.162  1.00 258.95 ? 554  THR E C   1 
ATOM   15743 O  O   . THR E  1 554 ? -9.130  -59.348 -90.413  1.00 266.62 ? 554  THR E O   1 
ATOM   15744 C  CB  . THR E  1 554 ? -7.017  -57.404 -90.713  1.00 251.54 ? 554  THR E CB  1 
ATOM   15745 O  OG1 . THR E  1 554 ? -5.932  -56.723 -91.355  1.00 251.72 ? 554  THR E OG1 1 
ATOM   15746 C  CG2 . THR E  1 554 ? -7.070  -56.996 -89.252  1.00 245.84 ? 554  THR E CG2 1 
ATOM   15747 N  N   . PRO E  1 555 ? -7.672  -60.696 -89.365  1.00 247.12 ? 555  PRO E N   1 
ATOM   15748 C  CA  . PRO E  1 555 ? -8.750  -61.463 -88.723  1.00 246.03 ? 555  PRO E CA  1 
ATOM   15749 C  C   . PRO E  1 555 ? -9.726  -60.574 -87.963  1.00 241.29 ? 555  PRO E C   1 
ATOM   15750 O  O   . PRO E  1 555 ? -9.332  -59.641 -87.261  1.00 234.05 ? 555  PRO E O   1 
ATOM   15751 C  CB  . PRO E  1 555 ? -7.997  -62.410 -87.783  1.00 244.11 ? 555  PRO E CB  1 
ATOM   15752 C  CG  . PRO E  1 555 ? -6.706  -61.730 -87.519  1.00 243.45 ? 555  PRO E CG  1 
ATOM   15753 C  CD  . PRO E  1 555 ? -6.354  -61.034 -88.800  1.00 245.91 ? 555  PRO E CD  1 
ATOM   15754 N  N   . ILE E  1 556 ? -11.013 -60.886 -88.096  1.00 248.81 ? 556  ILE E N   1 
ATOM   15755 C  CA  . ILE E  1 556 ? -12.084 -60.071 -87.529  1.00 246.19 ? 556  ILE E CA  1 
ATOM   15756 C  C   . ILE E  1 556 ? -12.395 -60.624 -86.144  1.00 242.61 ? 556  ILE E C   1 
ATOM   15757 O  O   . ILE E  1 556 ? -13.006 -61.684 -86.003  1.00 241.36 ? 556  ILE E O   1 
ATOM   15758 C  CB  . ILE E  1 556 ? -13.327 -60.055 -88.418  1.00 249.08 ? 556  ILE E CB  1 
ATOM   15759 C  CG1 . ILE E  1 556 ? -12.967 -59.556 -89.818  1.00 261.39 ? 556  ILE E CG1 1 
ATOM   15760 C  CG2 . ILE E  1 556 ? -14.421 -59.201 -87.783  1.00 239.12 ? 556  ILE E CG2 1 
ATOM   15761 C  CD1 . ILE E  1 556 ? -14.151 -59.457 -90.759  1.00 272.38 ? 556  ILE E CD1 1 
ATOM   15762 N  N   . THR E  1 557 ? -11.950 -59.910 -85.118  1.00 252.47 ? 557  THR E N   1 
ATOM   15763 C  CA  . THR E  1 557 ? -12.184 -60.309 -83.740  1.00 255.96 ? 557  THR E CA  1 
ATOM   15764 C  C   . THR E  1 557 ? -13.512 -59.724 -83.274  1.00 251.83 ? 557  THR E C   1 
ATOM   15765 O  O   . THR E  1 557 ? -13.707 -58.503 -83.312  1.00 240.51 ? 557  THR E O   1 
ATOM   15766 C  CB  . THR E  1 557 ? -11.037 -59.842 -82.845  1.00 254.98 ? 557  THR E CB  1 
ATOM   15767 O  OG1 . THR E  1 557 ? -9.831  -60.515 -83.227  1.00 247.66 ? 557  THR E OG1 1 
ATOM   15768 C  CG2 . THR E  1 557 ? -11.344 -60.143 -81.388  1.00 257.59 ? 557  THR E CG2 1 
ATOM   15769 N  N   . ILE E  1 558 ? -14.418 -60.591 -82.837  1.00 258.42 ? 558  ILE E N   1 
ATOM   15770 C  CA  . ILE E  1 558 ? -15.679 -60.166 -82.240  1.00 258.04 ? 558  ILE E CA  1 
ATOM   15771 C  C   . ILE E  1 558 ? -15.432 -59.945 -80.755  1.00 261.84 ? 558  ILE E C   1 
ATOM   15772 O  O   . ILE E  1 558 ? -15.071 -60.881 -80.032  1.00 262.34 ? 558  ILE E O   1 
ATOM   15773 C  CB  . ILE E  1 558 ? -16.792 -61.204 -82.461  1.00 259.84 ? 558  ILE E CB  1 
ATOM   15774 C  CG1 . ILE E  1 558 ? -17.161 -61.334 -83.945  1.00 255.52 ? 558  ILE E CG1 1 
ATOM   15775 C  CG2 . ILE E  1 558 ? -18.016 -60.855 -81.627  1.00 263.99 ? 558  ILE E CG2 1 
ATOM   15776 C  CD1 . ILE E  1 558 ? -16.301 -62.312 -84.719  1.00 258.89 ? 558  ILE E CD1 1 
ATOM   15777 N  N   . PHE E  1 559 ? -15.635 -58.717 -80.293  1.00 265.91 ? 559  PHE E N   1 
ATOM   15778 C  CA  . PHE E  1 559 ? -15.381 -58.360 -78.904  1.00 262.75 ? 559  PHE E CA  1 
ATOM   15779 C  C   . PHE E  1 559 ? -16.699 -58.181 -78.164  1.00 265.65 ? 559  PHE E C   1 
ATOM   15780 O  O   . PHE E  1 559 ? -17.601 -57.488 -78.646  1.00 283.72 ? 559  PHE E O   1 
ATOM   15781 C  CB  . PHE E  1 559 ? -14.534 -57.090 -78.800  1.00 254.86 ? 559  PHE E CB  1 
ATOM   15782 C  CG  . PHE E  1 559 ? -14.340 -56.616 -77.389  1.00 248.02 ? 559  PHE E CG  1 
ATOM   15783 C  CD1 . PHE E  1 559 ? -13.456 -57.263 -76.544  1.00 249.31 ? 559  PHE E CD1 1 
ATOM   15784 C  CD2 . PHE E  1 559 ? -15.047 -55.528 -76.907  1.00 244.81 ? 559  PHE E CD2 1 
ATOM   15785 C  CE1 . PHE E  1 559 ? -13.285 -56.838 -75.244  1.00 251.83 ? 559  PHE E CE1 1 
ATOM   15786 C  CE2 . PHE E  1 559 ? -14.875 -55.094 -75.611  1.00 244.38 ? 559  PHE E CE2 1 
ATOM   15787 C  CZ  . PHE E  1 559 ? -13.999 -55.752 -74.776  1.00 250.49 ? 559  PHE E CZ  1 
ATOM   15788 N  N   . MET E  1 560 ? -16.805 -58.816 -76.999  1.00 248.75 ? 560  MET E N   1 
ATOM   15789 C  CA  . MET E  1 560 ? -17.974 -58.718 -76.136  1.00 246.60 ? 560  MET E CA  1 
ATOM   15790 C  C   . MET E  1 560 ? -17.554 -58.180 -74.778  1.00 241.12 ? 560  MET E C   1 
ATOM   15791 O  O   . MET E  1 560 ? -16.680 -58.757 -74.125  1.00 250.08 ? 560  MET E O   1 
ATOM   15792 C  CB  . MET E  1 560 ? -18.652 -60.076 -75.968  1.00 253.57 ? 560  MET E CB  1 
ATOM   15793 C  CG  . MET E  1 560 ? -19.720 -60.086 -74.893  1.00 258.47 ? 560  MET E CG  1 
ATOM   15794 S  SD  . MET E  1 560 ? -20.414 -61.724 -74.628  1.00 278.40 ? 560  MET E SD  1 
ATOM   15795 C  CE  . MET E  1 560 ? -21.339 -61.468 -73.114  1.00 269.04 ? 560  MET E CE  1 
ATOM   15796 N  N   . GLU E  1 561 ? -18.190 -57.093 -74.349  1.00 229.06 ? 561  GLU E N   1 
ATOM   15797 C  CA  . GLU E  1 561 ? -17.903 -56.452 -73.074  1.00 222.52 ? 561  GLU E CA  1 
ATOM   15798 C  C   . GLU E  1 561 ? -19.177 -56.387 -72.244  1.00 222.68 ? 561  GLU E C   1 
ATOM   15799 O  O   . GLU E  1 561 ? -20.262 -56.152 -72.781  1.00 237.54 ? 561  GLU E O   1 
ATOM   15800 C  CB  . GLU E  1 561 ? -17.346 -55.042 -73.292  1.00 219.07 ? 561  GLU E CB  1 
ATOM   15801 C  CG  . GLU E  1 561 ? -17.047 -54.258 -72.029  1.00 215.03 ? 561  GLU E CG  1 
ATOM   15802 C  CD  . GLU E  1 561 ? -16.625 -52.836 -72.335  1.00 218.42 ? 561  GLU E CD  1 
ATOM   15803 O  OE1 . GLU E  1 561 ? -16.765 -52.415 -73.505  1.00 214.68 ? 561  GLU E OE1 1 
ATOM   15804 O  OE2 . GLU E  1 561 ? -16.145 -52.143 -71.414  1.00 232.22 ? 561  GLU E OE2 1 
ATOM   15805 N  N   . TYR E  1 562 ? -19.053 -56.593 -70.934  1.00 214.63 ? 562  TYR E N   1 
ATOM   15806 C  CA  . TYR E  1 562 ? -20.223 -56.557 -70.069  1.00 220.23 ? 562  TYR E CA  1 
ATOM   15807 C  C   . TYR E  1 562 ? -19.889 -55.876 -68.749  1.00 225.43 ? 562  TYR E C   1 
ATOM   15808 O  O   . TYR E  1 562 ? -18.765 -55.972 -68.248  1.00 238.44 ? 562  TYR E O   1 
ATOM   15809 C  CB  . TYR E  1 562 ? -20.781 -57.964 -69.822  1.00 219.06 ? 562  TYR E CB  1 
ATOM   15810 C  CG  . TYR E  1 562 ? -19.786 -58.945 -69.254  1.00 219.41 ? 562  TYR E CG  1 
ATOM   15811 C  CD1 . TYR E  1 562 ? -19.619 -59.090 -67.883  1.00 223.92 ? 562  TYR E CD1 1 
ATOM   15812 C  CD2 . TYR E  1 562 ? -19.017 -59.734 -70.095  1.00 221.67 ? 562  TYR E CD2 1 
ATOM   15813 C  CE1 . TYR E  1 562 ? -18.710 -59.994 -67.368  1.00 226.96 ? 562  TYR E CE1 1 
ATOM   15814 C  CE2 . TYR E  1 562 ? -18.109 -60.634 -69.592  1.00 228.82 ? 562  TYR E CE2 1 
ATOM   15815 C  CZ  . TYR E  1 562 ? -17.960 -60.764 -68.230  1.00 234.03 ? 562  TYR E CZ  1 
ATOM   15816 O  OH  . TYR E  1 562 ? -17.049 -61.669 -67.739  1.00 246.82 ? 562  TYR E OH  1 
ATOM   15817 N  N   . ARG E  1 563 ? -20.890 -55.192 -68.188  1.00 211.58 ? 563  ARG E N   1 
ATOM   15818 C  CA  . ARG E  1 563 ? -20.751 -54.475 -66.928  1.00 206.24 ? 563  ARG E CA  1 
ATOM   15819 C  C   . ARG E  1 563 ? -22.074 -54.538 -66.176  1.00 207.07 ? 563  ARG E C   1 
ATOM   15820 O  O   . ARG E  1 563 ? -23.095 -54.987 -66.706  1.00 209.95 ? 563  ARG E O   1 
ATOM   15821 C  CB  . ARG E  1 563 ? -20.345 -53.006 -67.134  1.00 210.74 ? 563  ARG E CB  1 
ATOM   15822 C  CG  . ARG E  1 563 ? -19.052 -52.751 -67.908  1.00 224.06 ? 563  ARG E CG  1 
ATOM   15823 C  CD  . ARG E  1 563 ? -18.775 -51.248 -67.976  1.00 231.63 ? 563  ARG E CD  1 
ATOM   15824 N  NE  . ARG E  1 563 ? -17.423 -50.927 -68.429  1.00 231.03 ? 563  ARG E NE  1 
ATOM   15825 C  CZ  . ARG E  1 563 ? -16.964 -49.688 -68.598  1.00 224.44 ? 563  ARG E CZ  1 
ATOM   15826 N  NH1 . ARG E  1 563 ? -17.747 -48.644 -68.355  1.00 224.45 ? 563  ARG E NH1 1 
ATOM   15827 N  NH2 . ARG E  1 563 ? -15.721 -49.491 -69.020  1.00 218.21 ? 563  ARG E NH2 1 
ATOM   15828 N  N   . LEU E  1 564 ? -22.045 -54.083 -64.925  1.00 217.51 ? 564  LEU E N   1 
ATOM   15829 C  CA  . LEU E  1 564 ? -23.223 -54.050 -64.071  1.00 224.28 ? 564  LEU E CA  1 
ATOM   15830 C  C   . LEU E  1 564 ? -23.585 -52.622 -63.680  1.00 229.83 ? 564  LEU E C   1 
ATOM   15831 O  O   . LEU E  1 564 ? -22.708 -51.772 -63.497  1.00 221.45 ? 564  LEU E O   1 
ATOM   15832 C  CB  . LEU E  1 564 ? -22.974 -54.888 -62.803  1.00 226.32 ? 564  LEU E CB  1 
ATOM   15833 C  CG  . LEU E  1 564 ? -24.019 -54.944 -61.680  1.00 233.71 ? 564  LEU E CG  1 
ATOM   15834 C  CD1 . LEU E  1 564 ? -25.419 -55.331 -62.151  1.00 243.08 ? 564  LEU E CD1 1 
ATOM   15835 C  CD2 . LEU E  1 564 ? -23.543 -55.886 -60.581  1.00 235.10 ? 564  LEU E CD2 1 
ATOM   15836 N  N   . ASP E  1 565 ? -24.893 -52.369 -63.545  1.00 248.07 ? 565  ASP E N   1 
ATOM   15837 C  CA  . ASP E  1 565 ? -25.416 -51.160 -62.904  1.00 254.63 ? 565  ASP E CA  1 
ATOM   15838 C  C   . ASP E  1 565 ? -25.501 -51.440 -61.406  1.00 247.98 ? 565  ASP E C   1 
ATOM   15839 O  O   . ASP E  1 565 ? -26.463 -52.036 -60.917  1.00 245.63 ? 565  ASP E O   1 
ATOM   15840 C  CB  . ASP E  1 565 ? -26.767 -50.757 -63.486  1.00 261.46 ? 565  ASP E CB  1 
ATOM   15841 C  CG  . ASP E  1 565 ? -27.128 -49.300 -63.189  1.00 272.08 ? 565  ASP E CG  1 
ATOM   15842 O  OD1 . ASP E  1 565 ? -26.637 -48.749 -62.177  1.00 284.05 ? 565  ASP E OD1 1 
ATOM   15843 O  OD2 . ASP E  1 565 ? -27.911 -48.707 -63.962  1.00 265.68 ? 565  ASP E OD2 1 
ATOM   15844 N  N   . TYR E  1 566 ? -24.464 -51.030 -60.669  1.00 240.72 ? 566  TYR E N   1 
ATOM   15845 C  CA  . TYR E  1 566 ? -24.425 -51.294 -59.233  1.00 236.51 ? 566  TYR E CA  1 
ATOM   15846 C  C   . TYR E  1 566 ? -25.570 -50.589 -58.510  1.00 233.38 ? 566  TYR E C   1 
ATOM   15847 O  O   . TYR E  1 566 ? -26.111 -51.112 -57.529  1.00 230.92 ? 566  TYR E O   1 
ATOM   15848 C  CB  . TYR E  1 566 ? -23.085 -50.844 -58.657  1.00 242.71 ? 566  TYR E CB  1 
ATOM   15849 C  CG  . TYR E  1 566 ? -21.889 -51.420 -59.370  1.00 251.39 ? 566  TYR E CG  1 
ATOM   15850 C  CD1 . TYR E  1 566 ? -21.314 -50.730 -60.425  1.00 252.08 ? 566  TYR E CD1 1 
ATOM   15851 C  CD2 . TYR E  1 566 ? -21.325 -52.635 -58.994  1.00 251.73 ? 566  TYR E CD2 1 
ATOM   15852 C  CE1 . TYR E  1 566 ? -20.217 -51.222 -61.092  1.00 244.84 ? 566  TYR E CE1 1 
ATOM   15853 C  CE2 . TYR E  1 566 ? -20.215 -53.142 -59.663  1.00 243.81 ? 566  TYR E CE2 1 
ATOM   15854 C  CZ  . TYR E  1 566 ? -19.670 -52.426 -60.711  1.00 236.10 ? 566  TYR E CZ  1 
ATOM   15855 O  OH  . TYR E  1 566 ? -18.573 -52.901 -61.390  1.00 221.80 ? 566  TYR E OH  1 
ATOM   15856 N  N   . ARG E  1 567 ? -25.914 -49.375 -58.959  1.00 236.98 ? 567  ARG E N   1 
ATOM   15857 C  CA  . ARG E  1 567 ? -26.909 -48.542 -58.284  1.00 238.69 ? 567  ARG E CA  1 
ATOM   15858 C  C   . ARG E  1 567 ? -28.235 -49.268 -58.089  1.00 245.80 ? 567  ARG E C   1 
ATOM   15859 O  O   . ARG E  1 567 ? -28.862 -49.153 -57.031  1.00 251.81 ? 567  ARG E O   1 
ATOM   15860 C  CB  . ARG E  1 567 ? -27.128 -47.259 -59.084  1.00 233.36 ? 567  ARG E CB  1 
ATOM   15861 C  CG  . ARG E  1 567 ? -25.865 -46.450 -59.298  1.00 233.45 ? 567  ARG E CG  1 
ATOM   15862 C  CD  . ARG E  1 567 ? -26.195 -45.068 -59.817  1.00 233.86 ? 567  ARG E CD  1 
ATOM   15863 N  NE  . ARG E  1 567 ? -24.999 -44.313 -60.174  1.00 236.23 ? 567  ARG E NE  1 
ATOM   15864 C  CZ  . ARG E  1 567 ? -25.007 -43.028 -60.510  1.00 233.85 ? 567  ARG E CZ  1 
ATOM   15865 N  NH1 . ARG E  1 567 ? -26.152 -42.357 -60.531  1.00 228.55 ? 567  ARG E NH1 1 
ATOM   15866 N  NH2 . ARG E  1 567 ? -23.875 -42.414 -60.831  1.00 233.96 ? 567  ARG E NH2 1 
ATOM   15867 N  N   . THR E  1 568 ? -28.689 -50.008 -59.100  1.00 250.89 ? 568  THR E N   1 
ATOM   15868 C  CA  . THR E  1 568 ? -29.920 -50.778 -58.961  1.00 257.54 ? 568  THR E CA  1 
ATOM   15869 C  C   . THR E  1 568 ? -29.695 -52.125 -58.289  1.00 262.57 ? 568  THR E C   1 
ATOM   15870 O  O   . THR E  1 568 ? -30.666 -52.850 -58.048  1.00 269.64 ? 568  THR E O   1 
ATOM   15871 C  CB  . THR E  1 568 ? -30.578 -50.994 -60.326  1.00 252.65 ? 568  THR E CB  1 
ATOM   15872 O  OG1 . THR E  1 568 ? -31.923 -51.450 -60.140  1.00 258.70 ? 568  THR E OG1 1 
ATOM   15873 C  CG2 . THR E  1 568 ? -29.808 -52.037 -61.123  1.00 249.25 ? 568  THR E CG2 1 
ATOM   15874 N  N   . ALA E  1 569 ? -28.447 -52.483 -57.994  1.00 242.67 ? 569  ALA E N   1 
ATOM   15875 C  CA  . ALA E  1 569 ? -28.130 -53.693 -57.248  1.00 233.62 ? 569  ALA E CA  1 
ATOM   15876 C  C   . ALA E  1 569 ? -27.603 -53.380 -55.853  1.00 242.02 ? 569  ALA E C   1 
ATOM   15877 O  O   . ALA E  1 569 ? -27.164 -54.293 -55.145  1.00 254.87 ? 569  ALA E O   1 
ATOM   15878 C  CB  . ALA E  1 569 ? -27.122 -54.547 -58.021  1.00 227.99 ? 569  ALA E CB  1 
ATOM   15879 N  N   . ALA E  1 570 ? -27.640 -52.115 -55.442  1.00 237.48 ? 570  ALA E N   1 
ATOM   15880 C  CA  . ALA E  1 570 ? -27.184 -51.708 -54.123  1.00 237.80 ? 570  ALA E CA  1 
ATOM   15881 C  C   . ALA E  1 570 ? -28.214 -52.100 -53.067  1.00 236.95 ? 570  ALA E C   1 
ATOM   15882 O  O   . ALA E  1 570 ? -29.337 -52.505 -53.374  1.00 241.67 ? 570  ALA E O   1 
ATOM   15883 C  CB  . ALA E  1 570 ? -26.920 -50.203 -54.085  1.00 240.29 ? 570  ALA E CB  1 
ATOM   15884 N  N   . ASP E  1 571 ? -27.815 -51.993 -51.802  1.00 245.68 ? 571  ASP E N   1 
ATOM   15885 C  CA  . ASP E  1 571 ? -28.682 -52.365 -50.697  1.00 250.29 ? 571  ASP E CA  1 
ATOM   15886 C  C   . ASP E  1 571 ? -29.314 -51.123 -50.063  1.00 242.53 ? 571  ASP E C   1 
ATOM   15887 O  O   . ASP E  1 571 ? -29.041 -49.982 -50.448  1.00 237.35 ? 571  ASP E O   1 
ATOM   15888 C  CB  . ASP E  1 571 ? -27.894 -53.175 -49.668  1.00 263.99 ? 571  ASP E CB  1 
ATOM   15889 C  CG  . ASP E  1 571 ? -28.782 -54.061 -48.820  1.00 275.57 ? 571  ASP E CG  1 
ATOM   15890 O  OD1 . ASP E  1 571 ? -29.823 -54.521 -49.335  1.00 282.69 ? 571  ASP E OD1 1 
ATOM   15891 O  OD2 . ASP E  1 571 ? -28.436 -54.299 -47.643  1.00 274.72 ? 571  ASP E OD2 1 
ATOM   15892 N  N   . THR E  1 572 ? -30.174 -51.360 -49.063  1.00 243.09 ? 572  THR E N   1 
ATOM   15893 C  CA  . THR E  1 572 ? -30.801 -50.260 -48.335  1.00 249.40 ? 572  THR E CA  1 
ATOM   15894 C  C   . THR E  1 572 ? -29.760 -49.394 -47.644  1.00 249.82 ? 572  THR E C   1 
ATOM   15895 O  O   . THR E  1 572 ? -29.996 -48.203 -47.410  1.00 239.92 ? 572  THR E O   1 
ATOM   15896 C  CB  . THR E  1 572 ? -31.812 -50.804 -47.318  1.00 250.63 ? 572  THR E CB  1 
ATOM   15897 O  OG1 . THR E  1 572 ? -32.381 -49.721 -46.572  1.00 249.28 ? 572  THR E OG1 1 
ATOM   15898 C  CG2 . THR E  1 572 ? -31.152 -51.788 -46.361  1.00 249.87 ? 572  THR E CG2 1 
ATOM   15899 N  N   . THR E  1 573 ? -28.610 -49.973 -47.310  1.00 249.58 ? 573  THR E N   1 
ATOM   15900 C  CA  . THR E  1 573 ? -27.507 -49.253 -46.695  1.00 243.45 ? 573  THR E CA  1 
ATOM   15901 C  C   . THR E  1 573 ? -26.556 -48.650 -47.721  1.00 236.44 ? 573  THR E C   1 
ATOM   15902 O  O   . THR E  1 573 ? -25.529 -48.084 -47.334  1.00 245.29 ? 573  THR E O   1 
ATOM   15903 C  CB  . THR E  1 573 ? -26.728 -50.182 -45.754  1.00 236.60 ? 573  THR E CB  1 
ATOM   15904 O  OG1 . THR E  1 573 ? -26.113 -51.234 -46.511  1.00 223.89 ? 573  THR E OG1 1 
ATOM   15905 C  CG2 . THR E  1 573 ? -27.653 -50.790 -44.703  1.00 231.63 ? 573  THR E CG2 1 
ATOM   15906 N  N   . GLY E  1 574 ? -26.861 -48.757 -49.012  1.00 221.19 ? 574  GLY E N   1 
ATOM   15907 C  CA  . GLY E  1 574 ? -25.995 -48.188 -50.023  1.00 216.91 ? 574  GLY E CA  1 
ATOM   15908 C  C   . GLY E  1 574 ? -24.765 -49.004 -50.331  1.00 214.63 ? 574  GLY E C   1 
ATOM   15909 O  O   . GLY E  1 574 ? -23.805 -48.471 -50.897  1.00 213.06 ? 574  GLY E O   1 
ATOM   15910 N  N   . LEU E  1 575 ? -24.758 -50.282 -49.965  1.00 208.53 ? 575  LEU E N   1 
ATOM   15911 C  CA  . LEU E  1 575 ? -23.608 -51.157 -50.167  1.00 207.26 ? 575  LEU E CA  1 
ATOM   15912 C  C   . LEU E  1 575 ? -23.688 -51.775 -51.556  1.00 211.24 ? 575  LEU E C   1 
ATOM   15913 O  O   . LEU E  1 575 ? -24.532 -52.641 -51.810  1.00 212.77 ? 575  LEU E O   1 
ATOM   15914 C  CB  . LEU E  1 575 ? -23.566 -52.236 -49.092  1.00 209.66 ? 575  LEU E CB  1 
ATOM   15915 C  CG  . LEU E  1 575 ? -22.188 -52.841 -48.854  1.00 223.04 ? 575  LEU E CG  1 
ATOM   15916 C  CD1 . LEU E  1 575 ? -21.188 -51.736 -48.571  1.00 233.19 ? 575  LEU E CD1 1 
ATOM   15917 C  CD2 . LEU E  1 575 ? -22.256 -53.814 -47.692  1.00 229.44 ? 575  LEU E CD2 1 
ATOM   15918 N  N   . GLN E  1 576 ? -22.803 -51.344 -52.448  1.00 218.35 ? 576  GLN E N   1 
ATOM   15919 C  CA  . GLN E  1 576 ? -22.819 -51.829 -53.827  1.00 214.22 ? 576  GLN E CA  1 
ATOM   15920 C  C   . GLN E  1 576 ? -22.013 -53.117 -53.953  1.00 214.72 ? 576  GLN E C   1 
ATOM   15921 O  O   . GLN E  1 576 ? -20.903 -53.200 -53.413  1.00 214.77 ? 576  GLN E O   1 
ATOM   15922 C  CB  . GLN E  1 576 ? -22.263 -50.782 -54.777  1.00 213.00 ? 576  GLN E CB  1 
ATOM   15923 C  CG  . GLN E  1 576 ? -22.779 -49.378 -54.527  1.00 226.76 ? 576  GLN E CG  1 
ATOM   15924 C  CD  . GLN E  1 576 ? -22.147 -48.361 -55.454  1.00 244.31 ? 576  GLN E CD  1 
ATOM   15925 O  OE1 . GLN E  1 576 ? -21.232 -48.680 -56.215  1.00 244.37 ? 576  GLN E OE1 1 
ATOM   15926 N  NE2 . GLN E  1 576 ? -22.639 -47.129 -55.402  1.00 256.49 ? 576  GLN E NE2 1 
ATOM   15927 N  N   . PRO E  1 577 ? -22.538 -54.137 -54.641  1.00 209.90 ? 577  PRO E N   1 
ATOM   15928 C  CA  . PRO E  1 577 ? -21.793 -55.393 -54.805  1.00 222.53 ? 577  PRO E CA  1 
ATOM   15929 C  C   . PRO E  1 577 ? -20.517 -55.226 -55.622  1.00 232.68 ? 577  PRO E C   1 
ATOM   15930 O  O   . PRO E  1 577 ? -20.216 -54.126 -56.098  1.00 241.89 ? 577  PRO E O   1 
ATOM   15931 C  CB  . PRO E  1 577 ? -22.802 -56.305 -55.518  1.00 218.62 ? 577  PRO E CB  1 
ATOM   15932 C  CG  . PRO E  1 577 ? -24.143 -55.701 -55.230  1.00 221.24 ? 577  PRO E CG  1 
ATOM   15933 C  CD  . PRO E  1 577 ? -23.893 -54.223 -55.204  1.00 215.65 ? 577  PRO E CD  1 
ATOM   15934 N  N   . ILE E  1 578 ? -19.764 -56.316 -55.800  1.00 232.16 ? 578  ILE E N   1 
ATOM   15935 C  CA  . ILE E  1 578 ? -18.501 -56.282 -56.532  1.00 232.12 ? 578  ILE E CA  1 
ATOM   15936 C  C   . ILE E  1 578 ? -18.241 -57.654 -57.142  1.00 233.67 ? 578  ILE E C   1 
ATOM   15937 O  O   . ILE E  1 578 ? -18.612 -58.686 -56.576  1.00 238.70 ? 578  ILE E O   1 
ATOM   15938 C  CB  . ILE E  1 578 ? -17.327 -55.842 -55.625  1.00 210.00 ? 578  ILE E CB  1 
ATOM   15939 C  CG1 . ILE E  1 578 ? -16.082 -55.553 -56.464  1.00 209.01 ? 578  ILE E CG1 1 
ATOM   15940 C  CG2 . ILE E  1 578 ? -17.024 -56.907 -54.577  1.00 199.33 ? 578  ILE E CG2 1 
ATOM   15941 C  CD1 . ILE E  1 578 ? -16.290 -54.481 -57.517  1.00 198.43 ? 578  ILE E CD1 1 
ATOM   15942 N  N   . LEU E  1 579 ? -17.602 -57.657 -58.313  1.00 223.93 ? 579  LEU E N   1 
ATOM   15943 C  CA  . LEU E  1 579 ? -17.290 -58.884 -59.038  1.00 198.92 ? 579  LEU E CA  1 
ATOM   15944 C  C   . LEU E  1 579 ? -16.096 -59.623 -58.438  1.00 191.69 ? 579  LEU E C   1 
ATOM   15945 O  O   . LEU E  1 579 ? -15.182 -59.023 -57.857  1.00 188.25 ? 579  LEU E O   1 
ATOM   15946 C  CB  . LEU E  1 579 ? -17.013 -58.581 -60.515  1.00 194.74 ? 579  LEU E CB  1 
ATOM   15947 C  CG  . LEU E  1 579 ? -18.171 -58.047 -61.371  1.00 196.56 ? 579  LEU E CG  1 
ATOM   15948 C  CD1 . LEU E  1 579 ? -17.694 -57.656 -62.766  1.00 196.94 ? 579  LEU E CD1 1 
ATOM   15949 C  CD2 . LEU E  1 579 ? -19.287 -59.070 -61.472  1.00 201.03 ? 579  LEU E CD2 1 
ATOM   15950 N  N   . ASN E  1 580 ? -16.134 -60.951 -58.565  1.00 192.08 ? 580  ASN E N   1 
ATOM   15951 C  CA  . ASN E  1 580 ? -15.002 -61.779 -58.183  1.00 196.89 ? 580  ASN E CA  1 
ATOM   15952 C  C   . ASN E  1 580 ? -13.797 -61.413 -59.043  1.00 215.41 ? 580  ASN E C   1 
ATOM   15953 O  O   . ASN E  1 580 ? -13.934 -61.049 -60.211  1.00 223.53 ? 580  ASN E O   1 
ATOM   15954 C  CB  . ASN E  1 580 ? -15.354 -63.256 -58.337  1.00 194.97 ? 580  ASN E CB  1 
ATOM   15955 C  CG  . ASN E  1 580 ? -14.270 -64.158 -57.817  1.00 193.66 ? 580  ASN E CG  1 
ATOM   15956 O  OD1 . ASN E  1 580 ? -13.481 -64.705 -58.582  1.00 194.61 ? 580  ASN E OD1 1 
ATOM   15957 N  ND2 . ASN E  1 580 ? -14.210 -64.303 -56.497  1.00 191.74 ? 580  ASN E ND2 1 
ATOM   15958 N  N   . GLN E  1 581 ? -12.601 -61.539 -58.464  1.00 219.29 ? 581  GLN E N   1 
ATOM   15959 C  CA  . GLN E  1 581 ? -11.441 -60.832 -59.006  1.00 207.54 ? 581  GLN E CA  1 
ATOM   15960 C  C   . GLN E  1 581 ? -10.759 -61.513 -60.192  1.00 197.11 ? 581  GLN E C   1 
ATOM   15961 O  O   . GLN E  1 581 ? -10.239 -60.817 -61.072  1.00 197.04 ? 581  GLN E O   1 
ATOM   15962 C  CB  . GLN E  1 581 ? -10.397 -60.626 -57.917  1.00 214.73 ? 581  GLN E CB  1 
ATOM   15963 C  CG  . GLN E  1 581 ? -9.931  -61.893 -57.215  1.00 207.82 ? 581  GLN E CG  1 
ATOM   15964 C  CD  . GLN E  1 581 ? -8.420  -61.901 -57.019  1.00 205.04 ? 581  GLN E CD  1 
ATOM   15965 O  OE1 . GLN E  1 581 ? -7.700  -61.121 -57.643  1.00 211.80 ? 581  GLN E OE1 1 
ATOM   15966 N  NE2 . GLN E  1 581 ? -7.939  -62.760 -56.130  1.00 203.38 ? 581  GLN E NE2 1 
ATOM   15967 N  N   . PHE E  1 582 ? -10.701 -62.844 -60.240  1.00 209.29 ? 582  PHE E N   1 
ATOM   15968 C  CA  . PHE E  1 582 ? -9.915  -63.454 -61.308  1.00 220.51 ? 582  PHE E CA  1 
ATOM   15969 C  C   . PHE E  1 582 ? -10.633 -63.463 -62.656  1.00 243.13 ? 582  PHE E C   1 
ATOM   15970 O  O   . PHE E  1 582 ? -9.972  -63.548 -63.695  1.00 244.46 ? 582  PHE E O   1 
ATOM   15971 C  CB  . PHE E  1 582 ? -9.538  -64.876 -60.913  1.00 226.81 ? 582  PHE E CB  1 
ATOM   15972 C  CG  . PHE E  1 582 ? -8.238  -65.338 -61.495  1.00 229.16 ? 582  PHE E CG  1 
ATOM   15973 C  CD1 . PHE E  1 582 ? -7.061  -64.653 -61.228  1.00 233.13 ? 582  PHE E CD1 1 
ATOM   15974 C  CD2 . PHE E  1 582 ? -8.185  -66.459 -62.301  1.00 220.87 ? 582  PHE E CD2 1 
ATOM   15975 C  CE1 . PHE E  1 582 ? -5.853  -65.080 -61.766  1.00 226.09 ? 582  PHE E CE1 1 
ATOM   15976 C  CE2 . PHE E  1 582 ? -6.986  -66.892 -62.839  1.00 216.90 ? 582  PHE E CE2 1 
ATOM   15977 C  CZ  . PHE E  1 582 ? -5.817  -66.203 -62.572  1.00 216.42 ? 582  PHE E CZ  1 
ATOM   15978 N  N   . THR E  1 583 ? -11.966 -63.386 -62.674  1.00 260.02 ? 583  THR E N   1 
ATOM   15979 C  CA  . THR E  1 583 ? -12.624 -63.452 -63.979  1.00 266.20 ? 583  THR E CA  1 
ATOM   15980 C  C   . THR E  1 583 ? -13.746 -62.429 -64.176  1.00 248.64 ? 583  THR E C   1 
ATOM   15981 O  O   . THR E  1 583 ? -14.842 -62.813 -64.601  1.00 245.48 ? 583  THR E O   1 
ATOM   15982 C  CB  . THR E  1 583 ? -13.164 -64.856 -64.249  1.00 263.84 ? 583  THR E CB  1 
ATOM   15983 O  OG1 . THR E  1 583 ? -12.315 -65.837 -63.635  1.00 265.04 ? 583  THR E OG1 1 
ATOM   15984 C  CG2 . THR E  1 583 ? -13.193 -65.108 -65.761  1.00 257.35 ? 583  THR E CG2 1 
ATOM   15985 N  N   . PRO E  1 584 ? -13.557 -61.138 -63.875  1.00 239.76 ? 584  PRO E N   1 
ATOM   15986 C  CA  . PRO E  1 584 ? -14.651 -60.187 -64.116  1.00 244.17 ? 584  PRO E CA  1 
ATOM   15987 C  C   . PRO E  1 584 ? -14.728 -59.732 -65.557  1.00 252.71 ? 584  PRO E C   1 
ATOM   15988 O  O   . PRO E  1 584 ? -15.786 -59.256 -65.988  1.00 262.74 ? 584  PRO E O   1 
ATOM   15989 C  CB  . PRO E  1 584 ? -14.301 -59.021 -63.194  1.00 240.12 ? 584  PRO E CB  1 
ATOM   15990 C  CG  . PRO E  1 584 ? -12.813 -59.000 -63.263  1.00 231.55 ? 584  PRO E CG  1 
ATOM   15991 C  CD  . PRO E  1 584 ? -12.399 -60.457 -63.265  1.00 233.67 ? 584  PRO E CD  1 
ATOM   15992 N  N   . ALA E  1 585 ? -13.628 -59.831 -66.286  1.00 237.72 ? 585  ALA E N   1 
ATOM   15993 C  CA  . ALA E  1 585 ? -13.443 -59.226 -67.588  1.00 238.14 ? 585  ALA E CA  1 
ATOM   15994 C  C   . ALA E  1 585 ? -14.419 -59.733 -68.648  1.00 249.55 ? 585  ALA E C   1 
ATOM   15995 O  O   . ALA E  1 585 ? -15.011 -60.815 -68.562  1.00 262.94 ? 585  ALA E O   1 
ATOM   15996 C  CB  . ALA E  1 585 ? -12.033 -59.497 -68.086  1.00 227.67 ? 585  ALA E CB  1 
ATOM   15997 N  N   . ASN E  1 586 ? -14.533 -58.911 -69.685  1.00 239.94 ? 586  ASN E N   1 
ATOM   15998 C  CA  . ASN E  1 586 ? -15.076 -59.188 -71.009  1.00 237.04 ? 586  ASN E CA  1 
ATOM   15999 C  C   . ASN E  1 586 ? -14.420 -60.408 -71.655  1.00 229.13 ? 586  ASN E C   1 
ATOM   16000 O  O   . ASN E  1 586 ? -13.406 -60.907 -71.151  1.00 229.85 ? 586  ASN E O   1 
ATOM   16001 C  CB  . ASN E  1 586 ? -14.822 -57.948 -71.855  1.00 245.01 ? 586  ASN E CB  1 
ATOM   16002 C  CG  . ASN E  1 586 ? -13.409 -57.487 -71.705  1.00 269.51 ? 586  ASN E CG  1 
ATOM   16003 O  OD1 . ASN E  1 586 ? -12.496 -58.311 -71.645  1.00 249.02 ? 586  ASN E OD1 1 
ATOM   16004 N  ND2 . ASN E  1 586 ? -13.192 -56.193 -71.610  1.00 347.51 ? 586  ASN E ND2 1 
ATOM   16005 N  N   . ILE E  1 587 ? -14.971 -60.900 -72.770  1.00 228.70 ? 587  ILE E N   1 
ATOM   16006 C  CA  . ILE E  1 587 ? -14.384 -62.030 -73.481  1.00 233.53 ? 587  ILE E CA  1 
ATOM   16007 C  C   . ILE E  1 587 ? -14.398 -61.781 -74.985  1.00 238.13 ? 587  ILE E C   1 
ATOM   16008 O  O   . ILE E  1 587 ? -15.202 -61.006 -75.506  1.00 235.78 ? 587  ILE E O   1 
ATOM   16009 C  CB  . ILE E  1 587 ? -15.100 -63.359 -73.165  1.00 237.98 ? 587  ILE E CB  1 
ATOM   16010 C  CG1 . ILE E  1 587 ? -16.611 -63.187 -73.271  1.00 238.90 ? 587  ILE E CG1 1 
ATOM   16011 C  CG2 . ILE E  1 587 ? -14.701 -63.852 -71.782  1.00 243.16 ? 587  ILE E CG2 1 
ATOM   16012 C  CD1 . ILE E  1 587 ? -17.377 -64.466 -73.019  1.00 243.86 ? 587  ILE E CD1 1 
ATOM   16013 N  N   . SER E  1 588 ? -13.482 -62.460 -75.682  1.00 251.13 ? 588  SER E N   1 
ATOM   16014 C  CA  . SER E  1 588 ? -13.307 -62.296 -77.117  1.00 256.93 ? 588  SER E CA  1 
ATOM   16015 C  C   . SER E  1 588 ? -13.152 -63.647 -77.811  1.00 257.78 ? 588  SER E C   1 
ATOM   16016 O  O   . SER E  1 588 ? -12.624 -64.610 -77.244  1.00 262.11 ? 588  SER E O   1 
ATOM   16017 C  CB  . SER E  1 588 ? -12.090 -61.411 -77.432  1.00 263.48 ? 588  SER E CB  1 
ATOM   16018 O  OG  . SER E  1 588 ? -10.890 -61.992 -76.948  1.00 266.29 ? 588  SER E OG  1 
ATOM   16019 N  N   . ARG E  1 589 ? -13.635 -63.699 -79.053  1.00 243.55 ? 589  ARG E N   1 
ATOM   16020 C  CA  . ARG E  1 589 ? -13.461 -64.820 -79.966  1.00 240.61 ? 589  ARG E CA  1 
ATOM   16021 C  C   . ARG E  1 589 ? -13.206 -64.216 -81.342  1.00 249.27 ? 589  ARG E C   1 
ATOM   16022 O  O   . ARG E  1 589 ? -13.094 -62.995 -81.484  1.00 255.14 ? 589  ARG E O   1 
ATOM   16023 C  CB  . ARG E  1 589 ? -14.666 -65.770 -79.945  1.00 240.35 ? 589  ARG E CB  1 
ATOM   16024 C  CG  . ARG E  1 589 ? -14.337 -67.196 -80.384  1.00 244.45 ? 589  ARG E CG  1 
ATOM   16025 C  CD  . ARG E  1 589 ? -15.582 -68.053 -80.521  1.00 247.04 ? 589  ARG E CD  1 
ATOM   16026 N  NE  . ARG E  1 589 ? -15.284 -69.350 -81.121  1.00 249.86 ? 589  ARG E NE  1 
ATOM   16027 C  CZ  . ARG E  1 589 ? -16.192 -70.283 -81.393  1.00 253.41 ? 589  ARG E CZ  1 
ATOM   16028 N  NH1 . ARG E  1 589 ? -17.473 -70.075 -81.114  1.00 259.88 ? 589  ARG E NH1 1 
ATOM   16029 N  NH2 . ARG E  1 589 ? -15.816 -71.430 -81.940  1.00 252.32 ? 589  ARG E NH2 1 
ATOM   16030 N  N   . GLN E  1 590 ? -13.107 -65.052 -82.372  1.00 250.75 ? 590  GLN E N   1 
ATOM   16031 C  CA  . GLN E  1 590 ? -12.738 -64.500 -83.668  1.00 256.96 ? 590  GLN E CA  1 
ATOM   16032 C  C   . GLN E  1 590 ? -13.231 -65.399 -84.790  1.00 264.93 ? 590  GLN E C   1 
ATOM   16033 O  O   . GLN E  1 590 ? -13.355 -66.617 -84.629  1.00 276.10 ? 590  GLN E O   1 
ATOM   16034 C  CB  . GLN E  1 590 ? -11.219 -64.304 -83.776  1.00 253.55 ? 590  GLN E CB  1 
ATOM   16035 C  CG  . GLN E  1 590 ? -10.410 -65.572 -83.565  1.00 253.83 ? 590  GLN E CG  1 
ATOM   16036 C  CD  . GLN E  1 590 ? -8.920  -65.315 -83.543  1.00 252.24 ? 590  GLN E CD  1 
ATOM   16037 O  OE1 . GLN E  1 590 ? -8.477  -64.167 -83.519  1.00 250.32 ? 590  GLN E OE1 1 
ATOM   16038 N  NE2 . GLN E  1 590 ? -8.135  -66.386 -83.533  1.00 254.62 ? 590  GLN E NE2 1 
ATOM   16039 N  N   . ALA E  1 591 ? -13.525 -64.769 -85.922  1.00 259.01 ? 591  ALA E N   1 
ATOM   16040 C  CA  . ALA E  1 591 ? -13.925 -65.476 -87.123  1.00 258.53 ? 591  ALA E CA  1 
ATOM   16041 C  C   . ALA E  1 591 ? -13.005 -65.095 -88.277  1.00 260.66 ? 591  ALA E C   1 
ATOM   16042 O  O   . ALA E  1 591 ? -12.031 -64.362 -88.093  1.00 259.67 ? 591  ALA E O   1 
ATOM   16043 C  CB  . ALA E  1 591 ? -15.367 -65.166 -87.463  1.00 262.15 ? 591  ALA E CB  1 
ATOM   16044 N  N   . ASP F  2 3   ? 48.322  -42.834 -37.389  1.00 209.86 ? 113  ASP F N   1 
ATOM   16045 C  CA  . ASP F  2 3   ? 47.789  -41.735 -36.596  1.00 209.25 ? 113  ASP F CA  1 
ATOM   16046 C  C   . ASP F  2 3   ? 46.419  -41.299 -37.109  1.00 219.93 ? 113  ASP F C   1 
ATOM   16047 O  O   . ASP F  2 3   ? 46.286  -40.872 -38.255  1.00 228.33 ? 113  ASP F O   1 
ATOM   16048 C  CB  . ASP F  2 3   ? 48.751  -40.556 -36.608  1.00 201.83 ? 113  ASP F CB  1 
ATOM   16049 C  CG  . ASP F  2 3   ? 48.321  -39.463 -35.673  1.00 199.27 ? 113  ASP F CG  1 
ATOM   16050 O  OD1 . ASP F  2 3   ? 47.606  -39.778 -34.700  1.00 192.62 ? 113  ASP F OD1 1 
ATOM   16051 O  OD2 . ASP F  2 3   ? 48.684  -38.295 -35.915  1.00 203.66 ? 113  ASP F OD2 1 
ATOM   16052 N  N   . TYR F  2 4   ? 45.400  -41.398 -36.248  1.00 231.50 ? 114  TYR F N   1 
ATOM   16053 C  CA  . TYR F  2 4   ? 44.039  -41.114 -36.682  1.00 233.51 ? 114  TYR F CA  1 
ATOM   16054 C  C   . TYR F  2 4   ? 43.148  -40.791 -35.494  1.00 231.08 ? 114  TYR F C   1 
ATOM   16055 O  O   . TYR F  2 4   ? 43.254  -41.461 -34.458  1.00 225.55 ? 114  TYR F O   1 
ATOM   16056 C  CB  . TYR F  2 4   ? 43.467  -42.302 -37.462  1.00 241.45 ? 114  TYR F CB  1 
ATOM   16057 C  CG  . TYR F  2 4   ? 42.130  -42.020 -38.096  1.00 272.95 ? 114  TYR F CG  1 
ATOM   16058 C  CD1 . TYR F  2 4   ? 42.044  -41.310 -39.285  1.00 289.30 ? 114  TYR F CD1 1 
ATOM   16059 C  CD2 . TYR F  2 4   ? 40.952  -42.477 -37.518  1.00 283.20 ? 114  TYR F CD2 1 
ATOM   16060 C  CE1 . TYR F  2 4   ? 40.824  -41.049 -39.875  1.00 303.49 ? 114  TYR F CE1 1 
ATOM   16061 C  CE2 . TYR F  2 4   ? 39.723  -42.221 -38.101  1.00 299.56 ? 114  TYR F CE2 1 
ATOM   16062 C  CZ  . TYR F  2 4   ? 39.665  -41.507 -39.282  1.00 309.09 ? 114  TYR F CZ  1 
ATOM   16063 O  OH  . TYR F  2 4   ? 38.450  -41.246 -39.875  1.00 310.79 ? 114  TYR F OH  1 
ATOM   16064 N  N   . PRO F  2 5   ? 42.294  -39.770 -35.595  1.00 237.89 ? 115  PRO F N   1 
ATOM   16065 C  CA  . PRO F  2 5   ? 41.413  -39.408 -34.474  1.00 237.25 ? 115  PRO F CA  1 
ATOM   16066 C  C   . PRO F  2 5   ? 40.431  -40.512 -34.101  1.00 230.18 ? 115  PRO F C   1 
ATOM   16067 O  O   . PRO F  2 5   ? 39.935  -41.247 -34.956  1.00 227.97 ? 115  PRO F O   1 
ATOM   16068 C  CB  . PRO F  2 5   ? 40.681  -38.165 -34.994  1.00 249.81 ? 115  PRO F CB  1 
ATOM   16069 C  CG  . PRO F  2 5   ? 41.589  -37.601 -36.043  1.00 258.51 ? 115  PRO F CG  1 
ATOM   16070 C  CD  . PRO F  2 5   ? 42.219  -38.798 -36.697  1.00 254.01 ? 115  PRO F CD  1 
ATOM   16071 N  N   . VAL F  2 6   ? 40.144  -40.610 -32.801  1.00 248.88 ? 116  VAL F N   1 
ATOM   16072 C  CA  . VAL F  2 6   ? 39.250  -41.627 -32.248  1.00 245.79 ? 116  VAL F CA  1 
ATOM   16073 C  C   . VAL F  2 6   ? 38.412  -41.002 -31.137  1.00 244.22 ? 116  VAL F C   1 
ATOM   16074 O  O   . VAL F  2 6   ? 38.940  -40.272 -30.290  1.00 237.95 ? 116  VAL F O   1 
ATOM   16075 C  CB  . VAL F  2 6   ? 40.034  -42.842 -31.714  1.00 240.57 ? 116  VAL F CB  1 
ATOM   16076 C  CG1 . VAL F  2 6   ? 39.161  -43.686 -30.799  1.00 228.49 ? 116  VAL F CG1 1 
ATOM   16077 C  CG2 . VAL F  2 6   ? 40.560  -43.683 -32.870  1.00 237.43 ? 116  VAL F CG2 1 
ATOM   16078 N  N   . ASP F  2 7   ? 37.106  -41.278 -31.145  1.00 231.50 ? 117  ASP F N   1 
ATOM   16079 C  CA  . ASP F  2 7   ? 36.190  -40.861 -30.089  1.00 224.19 ? 117  ASP F CA  1 
ATOM   16080 C  C   . ASP F  2 7   ? 35.653  -42.089 -29.358  1.00 205.66 ? 117  ASP F C   1 
ATOM   16081 O  O   . ASP F  2 7   ? 35.324  -43.098 -29.989  1.00 204.66 ? 117  ASP F O   1 
ATOM   16082 C  CB  . ASP F  2 7   ? 35.025  -40.044 -30.660  1.00 237.94 ? 117  ASP F CB  1 
ATOM   16083 C  CG  . ASP F  2 7   ? 35.481  -38.763 -31.339  1.00 249.97 ? 117  ASP F CG  1 
ATOM   16084 O  OD1 . ASP F  2 7   ? 36.581  -38.264 -31.012  1.00 252.61 ? 117  ASP F OD1 1 
ATOM   16085 O  OD2 . ASP F  2 7   ? 34.740  -38.262 -32.212  1.00 249.94 ? 117  ASP F OD2 1 
ATOM   16086 N  N   . LEU F  2 8   ? 35.569  -42.006 -28.028  1.00 205.07 ? 118  LEU F N   1 
ATOM   16087 C  CA  . LEU F  2 8   ? 35.104  -43.130 -27.209  1.00 208.59 ? 118  LEU F CA  1 
ATOM   16088 C  C   . LEU F  2 8   ? 34.141  -42.627 -26.139  1.00 218.75 ? 118  LEU F C   1 
ATOM   16089 O  O   . LEU F  2 8   ? 34.539  -41.874 -25.246  1.00 220.96 ? 118  LEU F O   1 
ATOM   16090 C  CB  . LEU F  2 8   ? 36.282  -43.871 -26.575  1.00 207.83 ? 118  LEU F CB  1 
ATOM   16091 C  CG  . LEU F  2 8   ? 36.009  -45.209 -25.866  1.00 208.40 ? 118  LEU F CG  1 
ATOM   16092 C  CD1 . LEU F  2 8   ? 35.639  -45.017 -24.398  1.00 208.74 ? 118  LEU F CD1 1 
ATOM   16093 C  CD2 . LEU F  2 8   ? 34.932  -46.004 -26.586  1.00 208.57 ? 118  LEU F CD2 1 
ATOM   16094 N  N   . TYR F  2 9   ? 32.880  -43.044 -26.221  1.00 229.74 ? 119  TYR F N   1 
ATOM   16095 C  CA  . TYR F  2 9   ? 31.867  -42.717 -25.223  1.00 226.11 ? 119  TYR F CA  1 
ATOM   16096 C  C   . TYR F  2 9   ? 31.692  -43.892 -24.264  1.00 207.12 ? 119  TYR F C   1 
ATOM   16097 O  O   . TYR F  2 9   ? 31.594  -45.044 -24.698  1.00 203.92 ? 119  TYR F O   1 
ATOM   16098 C  CB  . TYR F  2 9   ? 30.534  -42.379 -25.892  1.00 236.76 ? 119  TYR F CB  1 
ATOM   16099 C  CG  . TYR F  2 9   ? 29.551  -41.620 -25.022  1.00 237.87 ? 119  TYR F CG  1 
ATOM   16100 C  CD1 . TYR F  2 9   ? 29.557  -40.230 -24.984  1.00 246.52 ? 119  TYR F CD1 1 
ATOM   16101 C  CD2 . TYR F  2 9   ? 28.612  -42.290 -24.248  1.00 235.60 ? 119  TYR F CD2 1 
ATOM   16102 C  CE1 . TYR F  2 9   ? 28.659  -39.530 -24.198  1.00 244.06 ? 119  TYR F CE1 1 
ATOM   16103 C  CE2 . TYR F  2 9   ? 27.710  -41.597 -23.457  1.00 238.63 ? 119  TYR F CE2 1 
ATOM   16104 C  CZ  . TYR F  2 9   ? 27.739  -40.218 -23.437  1.00 237.99 ? 119  TYR F CZ  1 
ATOM   16105 O  OH  . TYR F  2 9   ? 26.845  -39.523 -22.653  1.00 238.98 ? 119  TYR F OH  1 
ATOM   16106 N  N   . TYR F  2 10  ? 31.651  -43.599 -22.965  1.00 202.77 ? 120  TYR F N   1 
ATOM   16107 C  CA  . TYR F  2 10  ? 31.564  -44.615 -21.920  1.00 205.94 ? 120  TYR F CA  1 
ATOM   16108 C  C   . TYR F  2 10  ? 30.148  -44.620 -21.352  1.00 208.28 ? 120  TYR F C   1 
ATOM   16109 O  O   . TYR F  2 10  ? 29.760  -43.697 -20.629  1.00 218.31 ? 120  TYR F O   1 
ATOM   16110 C  CB  . TYR F  2 10  ? 32.593  -44.361 -20.825  1.00 205.10 ? 120  TYR F CB  1 
ATOM   16111 C  CG  . TYR F  2 10  ? 32.888  -45.563 -19.954  1.00 204.78 ? 120  TYR F CG  1 
ATOM   16112 C  CD1 . TYR F  2 10  ? 33.672  -46.609 -20.422  1.00 202.31 ? 120  TYR F CD1 1 
ATOM   16113 C  CD2 . TYR F  2 10  ? 32.389  -45.647 -18.662  1.00 214.66 ? 120  TYR F CD2 1 
ATOM   16114 C  CE1 . TYR F  2 10  ? 33.950  -47.705 -19.627  1.00 205.79 ? 120  TYR F CE1 1 
ATOM   16115 C  CE2 . TYR F  2 10  ? 32.660  -46.739 -17.860  1.00 216.20 ? 120  TYR F CE2 1 
ATOM   16116 C  CZ  . TYR F  2 10  ? 33.441  -47.765 -18.347  1.00 211.47 ? 120  TYR F CZ  1 
ATOM   16117 O  OH  . TYR F  2 10  ? 33.712  -48.852 -17.551  1.00 209.46 ? 120  TYR F OH  1 
ATOM   16118 N  N   . LEU F  2 11  ? 29.374  -45.644 -21.697  1.00 195.53 ? 121  LEU F N   1 
ATOM   16119 C  CA  . LEU F  2 11  ? 27.985  -45.776 -21.262  1.00 195.24 ? 121  LEU F CA  1 
ATOM   16120 C  C   . LEU F  2 11  ? 27.917  -46.760 -20.093  1.00 197.95 ? 121  LEU F C   1 
ATOM   16121 O  O   . LEU F  2 11  ? 28.057  -47.971 -20.280  1.00 204.37 ? 121  LEU F O   1 
ATOM   16122 C  CB  . LEU F  2 11  ? 27.111  -46.225 -22.426  1.00 203.70 ? 121  LEU F CB  1 
ATOM   16123 C  CG  . LEU F  2 11  ? 25.600  -46.056 -22.263  1.00 208.55 ? 121  LEU F CG  1 
ATOM   16124 C  CD1 . LEU F  2 11  ? 25.255  -44.601 -21.985  1.00 209.77 ? 121  LEU F CD1 1 
ATOM   16125 C  CD2 . LEU F  2 11  ? 24.879  -46.554 -23.505  1.00 219.24 ? 121  LEU F CD2 1 
ATOM   16126 N  N   . MET F  2 12  ? 27.717  -46.240 -18.883  1.00 201.18 ? 122  MET F N   1 
ATOM   16127 C  CA  . MET F  2 12  ? 27.683  -47.063 -17.680  1.00 196.13 ? 122  MET F CA  1 
ATOM   16128 C  C   . MET F  2 12  ? 26.251  -47.283 -17.200  1.00 193.59 ? 122  MET F C   1 
ATOM   16129 O  O   . MET F  2 12  ? 25.436  -46.355 -17.186  1.00 192.00 ? 122  MET F O   1 
ATOM   16130 C  CB  . MET F  2 12  ? 28.507  -46.429 -16.561  1.00 199.92 ? 122  MET F CB  1 
ATOM   16131 C  CG  . MET F  2 12  ? 28.775  -47.371 -15.406  1.00 210.61 ? 122  MET F CG  1 
ATOM   16132 S  SD  . MET F  2 12  ? 28.982  -46.501 -13.848  1.00 241.84 ? 122  MET F SD  1 
ATOM   16133 C  CE  . MET F  2 12  ? 30.452  -45.543 -14.194  1.00 232.03 ? 122  MET F CE  1 
ATOM   16134 N  N   . ASP F  2 13  ? 25.964  -48.512 -16.772  1.00 194.45 ? 123  ASP F N   1 
ATOM   16135 C  CA  . ASP F  2 13  ? 24.674  -48.873 -16.193  1.00 197.97 ? 123  ASP F CA  1 
ATOM   16136 C  C   . ASP F  2 13  ? 24.708  -48.623 -14.690  1.00 200.67 ? 123  ASP F C   1 
ATOM   16137 O  O   . ASP F  2 13  ? 25.478  -49.263 -13.968  1.00 217.91 ? 123  ASP F O   1 
ATOM   16138 C  CB  . ASP F  2 13  ? 24.349  -50.340 -16.480  1.00 200.68 ? 123  ASP F CB  1 
ATOM   16139 C  CG  . ASP F  2 13  ? 23.068  -50.802 -15.817  1.00 204.36 ? 123  ASP F CG  1 
ATOM   16140 O  OD1 . ASP F  2 13  ? 22.159  -49.971 -15.616  1.00 215.75 ? 123  ASP F OD1 1 
ATOM   16141 O  OD2 . ASP F  2 13  ? 22.977  -52.004 -15.493  1.00 204.61 ? 123  ASP F OD2 1 
ATOM   16142 N  N   . LEU F  2 14  ? 23.862  -47.712 -14.215  1.00 191.14 ? 124  LEU F N   1 
ATOM   16143 C  CA  . LEU F  2 14  ? 23.820  -47.373 -12.802  1.00 186.55 ? 124  LEU F CA  1 
ATOM   16144 C  C   . LEU F  2 14  ? 22.747  -48.152 -12.054  1.00 188.02 ? 124  LEU F C   1 
ATOM   16145 O  O   . LEU F  2 14  ? 22.387  -47.777 -10.934  1.00 195.79 ? 124  LEU F O   1 
ATOM   16146 C  CB  . LEU F  2 14  ? 23.600  -45.872 -12.617  1.00 192.64 ? 124  LEU F CB  1 
ATOM   16147 C  CG  . LEU F  2 14  ? 24.781  -44.934 -12.869  1.00 182.90 ? 124  LEU F CG  1 
ATOM   16148 C  CD1 . LEU F  2 14  ? 24.402  -43.500 -12.531  1.00 183.73 ? 124  LEU F CD1 1 
ATOM   16149 C  CD2 . LEU F  2 14  ? 25.993  -45.367 -12.072  1.00 180.79 ? 124  LEU F CD2 1 
ATOM   16150 N  N   . SER F  2 15  ? 22.234  -49.229 -12.645  1.00 193.71 ? 125  SER F N   1 
ATOM   16151 C  CA  . SER F  2 15  ? 21.139  -49.973 -12.041  1.00 201.43 ? 125  SER F CA  1 
ATOM   16152 C  C   . SER F  2 15  ? 21.588  -50.655 -10.750  1.00 192.19 ? 125  SER F C   1 
ATOM   16153 O  O   . SER F  2 15  ? 22.761  -50.631 -10.363  1.00 186.07 ? 125  SER F O   1 
ATOM   16154 C  CB  . SER F  2 15  ? 20.591  -51.009 -13.019  1.00 209.18 ? 125  SER F CB  1 
ATOM   16155 O  OG  . SER F  2 15  ? 21.549  -52.017 -13.295  1.00 209.51 ? 125  SER F OG  1 
ATOM   16156 N  N   . ALA F  2 16  ? 20.627  -51.313 -10.099  1.00 191.01 ? 126  ALA F N   1 
ATOM   16157 C  CA  . ALA F  2 16  ? 20.875  -51.859 -8.773   1.00 193.85 ? 126  ALA F CA  1 
ATOM   16158 C  C   . ALA F  2 16  ? 21.830  -53.039 -8.827   1.00 186.88 ? 126  ALA F C   1 
ATOM   16159 O  O   . ALA F  2 16  ? 22.611  -53.250 -7.894   1.00 185.91 ? 126  ALA F O   1 
ATOM   16160 C  CB  . ALA F  2 16  ? 19.552  -52.269 -8.129   1.00 208.99 ? 126  ALA F CB  1 
ATOM   16161 N  N   . SER F  2 17  ? 21.818  -53.787 -9.923   1.00 187.56 ? 127  SER F N   1 
ATOM   16162 C  CA  . SER F  2 17  ? 22.616  -54.995 -10.037  1.00 199.89 ? 127  SER F CA  1 
ATOM   16163 C  C   . SER F  2 17  ? 24.082  -54.706 -10.293  1.00 191.54 ? 127  SER F C   1 
ATOM   16164 O  O   . SER F  2 17  ? 24.843  -55.639 -10.571  1.00 199.37 ? 127  SER F O   1 
ATOM   16165 C  CB  . SER F  2 17  ? 22.063  -55.886 -11.152  1.00 221.21 ? 127  SER F CB  1 
ATOM   16166 O  OG  . SER F  2 17  ? 21.904  -55.153 -12.354  1.00 224.64 ? 127  SER F OG  1 
ATOM   16167 N  N   . MET F  2 18  ? 24.499  -53.446 -10.210  1.00 188.97 ? 128  MET F N   1 
ATOM   16168 C  CA  . MET F  2 18  ? 25.855  -53.058 -10.559  1.00 188.98 ? 128  MET F CA  1 
ATOM   16169 C  C   . MET F  2 18  ? 26.705  -52.696 -9.348   1.00 186.14 ? 128  MET F C   1 
ATOM   16170 O  O   . MET F  2 18  ? 27.856  -52.275 -9.515   1.00 183.10 ? 128  MET F O   1 
ATOM   16171 C  CB  . MET F  2 18  ? 25.819  -51.890 -11.542  1.00 191.47 ? 128  MET F CB  1 
ATOM   16172 C  CG  . MET F  2 18  ? 25.314  -52.277 -12.914  1.00 203.24 ? 128  MET F CG  1 
ATOM   16173 S  SD  . MET F  2 18  ? 26.493  -53.351 -13.745  1.00 216.64 ? 128  MET F SD  1 
ATOM   16174 C  CE  . MET F  2 18  ? 27.941  -52.296 -13.790  1.00 228.99 ? 128  MET F CE  1 
ATOM   16175 N  N   . ASP F  2 19  ? 26.183  -52.879 -8.134   1.00 177.60 ? 129  ASP F N   1 
ATOM   16176 C  CA  . ASP F  2 19  ? 26.965  -52.562 -6.946   1.00 173.35 ? 129  ASP F CA  1 
ATOM   16177 C  C   . ASP F  2 19  ? 28.122  -53.533 -6.764   1.00 195.53 ? 129  ASP F C   1 
ATOM   16178 O  O   . ASP F  2 19  ? 29.182  -53.149 -6.253   1.00 200.64 ? 129  ASP F O   1 
ATOM   16179 C  CB  . ASP F  2 19  ? 26.063  -52.557 -5.715   1.00 178.69 ? 129  ASP F CB  1 
ATOM   16180 C  CG  . ASP F  2 19  ? 26.827  -52.294 -4.442   1.00 180.47 ? 129  ASP F CG  1 
ATOM   16181 O  OD1 . ASP F  2 19  ? 27.124  -51.114 -4.160   1.00 179.32 ? 129  ASP F OD1 1 
ATOM   16182 O  OD2 . ASP F  2 19  ? 27.129  -53.271 -3.723   1.00 183.63 ? 129  ASP F OD2 1 
ATOM   16183 N  N   . ASP F  2 20  ? 27.948  -54.779 -7.204   1.00 219.46 ? 130  ASP F N   1 
ATOM   16184 C  CA  . ASP F  2 20  ? 28.987  -55.797 -7.134   1.00 212.11 ? 130  ASP F CA  1 
ATOM   16185 C  C   . ASP F  2 20  ? 30.034  -55.620 -8.217   1.00 191.36 ? 130  ASP F C   1 
ATOM   16186 O  O   . ASP F  2 20  ? 31.109  -56.225 -8.140   1.00 193.14 ? 130  ASP F O   1 
ATOM   16187 C  CB  . ASP F  2 20  ? 28.353  -57.187 -7.263   1.00 216.15 ? 130  ASP F CB  1 
ATOM   16188 C  CG  . ASP F  2 20  ? 27.416  -57.297 -8.468   1.00 209.42 ? 130  ASP F CG  1 
ATOM   16189 O  OD1 . ASP F  2 20  ? 26.743  -56.296 -8.793   1.00 220.96 ? 130  ASP F OD1 1 
ATOM   16190 O  OD2 . ASP F  2 20  ? 27.331  -58.381 -9.084   1.00 196.46 ? 130  ASP F OD2 1 
ATOM   16191 N  N   . ASP F  2 21  ? 29.742  -54.798 -9.210   1.00 180.13 ? 131  ASP F N   1 
ATOM   16192 C  CA  . ASP F  2 21  ? 30.608  -54.601 -10.348  1.00 183.65 ? 131  ASP F CA  1 
ATOM   16193 C  C   . ASP F  2 21  ? 31.063  -53.161 -10.448  1.00 183.85 ? 131  ASP F C   1 
ATOM   16194 O  O   . ASP F  2 21  ? 31.796  -52.818 -11.382  1.00 201.42 ? 131  ASP F O   1 
ATOM   16195 C  CB  . ASP F  2 21  ? 29.876  -55.032 -11.621  1.00 187.57 ? 131  ASP F CB  1 
ATOM   16196 C  CG  . ASP F  2 21  ? 29.031  -56.269 -11.394  1.00 197.17 ? 131  ASP F CG  1 
ATOM   16197 O  OD1 . ASP F  2 21  ? 29.577  -57.254 -10.849  1.00 198.40 ? 131  ASP F OD1 1 
ATOM   16198 O  OD2 . ASP F  2 21  ? 27.823  -56.251 -11.722  1.00 206.70 ? 131  ASP F OD2 1 
ATOM   16199 N  N   . LEU F  2 22  ? 30.640  -52.313 -9.510   1.00 179.21 ? 132  LEU F N   1 
ATOM   16200 C  CA  . LEU F  2 22  ? 30.947  -50.891 -9.576   1.00 191.59 ? 132  LEU F CA  1 
ATOM   16201 C  C   . LEU F  2 22  ? 32.452  -50.646 -9.550   1.00 204.09 ? 132  LEU F C   1 
ATOM   16202 O  O   . LEU F  2 22  ? 32.988  -49.923 -10.399  1.00 209.49 ? 132  LEU F O   1 
ATOM   16203 C  CB  . LEU F  2 22  ? 30.253  -50.171 -8.421   1.00 201.28 ? 132  LEU F CB  1 
ATOM   16204 C  CG  . LEU F  2 22  ? 30.494  -48.670 -8.297   1.00 200.88 ? 132  LEU F CG  1 
ATOM   16205 C  CD1 . LEU F  2 22  ? 29.986  -47.940 -9.534   1.00 184.83 ? 132  LEU F CD1 1 
ATOM   16206 C  CD2 . LEU F  2 22  ? 29.833  -48.135 -7.036   1.00 214.19 ? 132  LEU F CD2 1 
ATOM   16207 N  N   . ASN F  2 23  ? 33.156  -51.252 -8.587   1.00 202.66 ? 133  ASN F N   1 
ATOM   16208 C  CA  . ASN F  2 23  ? 34.588  -51.010 -8.444   1.00 204.18 ? 133  ASN F CA  1 
ATOM   16209 C  C   . ASN F  2 23  ? 35.391  -51.515 -9.639   1.00 215.21 ? 133  ASN F C   1 
ATOM   16210 O  O   . ASN F  2 23  ? 36.501  -51.025 -9.877   1.00 223.14 ? 133  ASN F O   1 
ATOM   16211 C  CB  . ASN F  2 23  ? 35.103  -51.665 -7.162   1.00 208.63 ? 133  ASN F CB  1 
ATOM   16212 C  CG  . ASN F  2 23  ? 34.852  -53.157 -7.134   1.00 217.82 ? 133  ASN F CG  1 
ATOM   16213 O  OD1 . ASN F  2 23  ? 33.859  -53.639 -7.678   1.00 215.16 ? 133  ASN F OD1 1 
ATOM   16214 N  ND2 . ASN F  2 23  ? 35.762  -53.900 -6.514   1.00 222.39 ? 133  ASN F ND2 1 
ATOM   16215 N  N   . THR F  2 24  ? 34.857  -52.476 -10.396  1.00 202.09 ? 134  THR F N   1 
ATOM   16216 C  CA  . THR F  2 24  ? 35.532  -52.940 -11.602  1.00 183.78 ? 134  THR F CA  1 
ATOM   16217 C  C   . THR F  2 24  ? 35.341  -51.958 -12.747  1.00 182.19 ? 134  THR F C   1 
ATOM   16218 O  O   . THR F  2 24  ? 36.189  -51.877 -13.642  1.00 186.21 ? 134  THR F O   1 
ATOM   16219 C  CB  . THR F  2 24  ? 35.024  -54.329 -11.999  1.00 180.83 ? 134  THR F CB  1 
ATOM   16220 O  OG1 . THR F  2 24  ? 33.606  -54.286 -12.192  1.00 178.91 ? 134  THR F OG1 1 
ATOM   16221 C  CG2 . THR F  2 24  ? 35.344  -55.349 -10.916  1.00 179.11 ? 134  THR F CG2 1 
ATOM   16222 N  N   . ILE F  2 25  ? 34.236  -51.213 -12.732  1.00 182.07 ? 135  ILE F N   1 
ATOM   16223 C  CA  . ILE F  2 25  ? 33.953  -50.251 -13.789  1.00 181.47 ? 135  ILE F CA  1 
ATOM   16224 C  C   . ILE F  2 25  ? 34.808  -49.007 -13.613  1.00 182.01 ? 135  ILE F C   1 
ATOM   16225 O  O   . ILE F  2 25  ? 35.320  -48.448 -14.589  1.00 184.76 ? 135  ILE F O   1 
ATOM   16226 C  CB  . ILE F  2 25  ? 32.452  -49.911 -13.799  1.00 178.85 ? 135  ILE F CB  1 
ATOM   16227 C  CG1 . ILE F  2 25  ? 31.624  -51.165 -14.067  1.00 180.31 ? 135  ILE F CG1 1 
ATOM   16228 C  CG2 . ILE F  2 25  ? 32.138  -48.846 -14.831  1.00 179.64 ? 135  ILE F CG2 1 
ATOM   16229 C  CD1 . ILE F  2 25  ? 32.205  -52.043 -15.143  1.00 185.01 ? 135  ILE F CD1 1 
ATOM   16230 N  N   . LYS F  2 26  ? 34.998  -48.570 -12.365  1.00 189.05 ? 136  LYS F N   1 
ATOM   16231 C  CA  . LYS F  2 26  ? 35.854  -47.418 -12.112  1.00 192.02 ? 136  LYS F CA  1 
ATOM   16232 C  C   . LYS F  2 26  ? 37.309  -47.742 -12.417  1.00 200.06 ? 136  LYS F C   1 
ATOM   16233 O  O   . LYS F  2 26  ? 38.049  -46.878 -12.901  1.00 202.26 ? 136  LYS F O   1 
ATOM   16234 C  CB  . LYS F  2 26  ? 35.697  -46.951 -10.662  1.00 201.06 ? 136  LYS F CB  1 
ATOM   16235 C  CG  . LYS F  2 26  ? 34.278  -46.537 -10.278  1.00 205.36 ? 136  LYS F CG  1 
ATOM   16236 C  CD  . LYS F  2 26  ? 34.213  -45.997 -8.852   1.00 213.97 ? 136  LYS F CD  1 
ATOM   16237 C  CE  . LYS F  2 26  ? 32.782  -45.676 -8.442   1.00 207.22 ? 136  LYS F CE  1 
ATOM   16238 N  NZ  . LYS F  2 26  ? 32.693  -45.181 -7.040   1.00 206.75 ? 136  LYS F NZ  1 
ATOM   16239 N  N   . GLU F  2 27  ? 37.728  -48.983 -12.172  1.00 209.02 ? 137  GLU F N   1 
ATOM   16240 C  CA  . GLU F  2 27  ? 39.073  -49.392 -12.544  1.00 208.26 ? 137  GLU F CA  1 
ATOM   16241 C  C   . GLU F  2 27  ? 39.205  -49.565 -14.043  1.00 204.15 ? 137  GLU F C   1 
ATOM   16242 O  O   . GLU F  2 27  ? 40.329  -49.632 -14.552  1.00 208.19 ? 137  GLU F O   1 
ATOM   16243 C  CB  . GLU F  2 27  ? 39.445  -50.690 -11.825  1.00 211.15 ? 137  GLU F CB  1 
ATOM   16244 C  CG  . GLU F  2 27  ? 39.966  -50.485 -10.413  1.00 215.03 ? 137  GLU F CG  1 
ATOM   16245 C  CD  . GLU F  2 27  ? 40.672  -51.709 -9.873   1.00 214.11 ? 137  GLU F CD  1 
ATOM   16246 O  OE1 . GLU F  2 27  ? 40.890  -51.776 -8.644   1.00 213.54 ? 137  GLU F OE1 1 
ATOM   16247 O  OE2 . GLU F  2 27  ? 40.992  -52.612 -10.675  1.00 212.73 ? 137  GLU F OE2 1 
ATOM   16248 N  N   . LEU F  2 28  ? 38.084  -49.629 -14.752  1.00 197.45 ? 138  LEU F N   1 
ATOM   16249 C  CA  . LEU F  2 28  ? 38.090  -49.630 -16.204  1.00 195.32 ? 138  LEU F CA  1 
ATOM   16250 C  C   . LEU F  2 28  ? 38.145  -48.223 -16.771  1.00 193.70 ? 138  LEU F C   1 
ATOM   16251 O  O   . LEU F  2 28  ? 38.786  -48.004 -17.804  1.00 197.62 ? 138  LEU F O   1 
ATOM   16252 C  CB  . LEU F  2 28  ? 36.848  -50.352 -16.730  1.00 193.04 ? 138  LEU F CB  1 
ATOM   16253 C  CG  . LEU F  2 28  ? 36.656  -50.367 -18.242  1.00 188.53 ? 138  LEU F CG  1 
ATOM   16254 C  CD1 . LEU F  2 28  ? 37.905  -50.873 -18.937  1.00 185.69 ? 138  LEU F CD1 1 
ATOM   16255 C  CD2 . LEU F  2 28  ? 35.464  -51.230 -18.596  1.00 189.42 ? 138  LEU F CD2 1 
ATOM   16256 N  N   . GLY F  2 29  ? 37.498  -47.266 -16.114  1.00 191.31 ? 139  GLY F N   1 
ATOM   16257 C  CA  . GLY F  2 29  ? 37.542  -45.886 -16.544  1.00 190.37 ? 139  GLY F CA  1 
ATOM   16258 C  C   . GLY F  2 29  ? 38.933  -45.291 -16.491  1.00 189.18 ? 139  GLY F C   1 
ATOM   16259 O  O   . GLY F  2 29  ? 39.442  -44.796 -17.502  1.00 180.24 ? 139  GLY F O   1 
ATOM   16260 N  N   . SER F  2 30  ? 39.559  -45.331 -15.311  1.00 190.82 ? 140  SER F N   1 
ATOM   16261 C  CA  . SER F  2 30  ? 40.885  -44.742 -15.165  1.00 191.71 ? 140  SER F CA  1 
ATOM   16262 C  C   . SER F  2 30  ? 41.907  -45.472 -16.026  1.00 194.32 ? 140  SER F C   1 
ATOM   16263 O  O   . SER F  2 30  ? 42.782  -44.843 -16.631  1.00 197.12 ? 140  SER F O   1 
ATOM   16264 C  CB  . SER F  2 30  ? 41.303  -44.749 -13.693  1.00 190.44 ? 140  SER F CB  1 
ATOM   16265 O  OG  . SER F  2 30  ? 41.473  -46.070 -13.207  1.00 193.81 ? 140  SER F OG  1 
ATOM   16266 N  N   . ARG F  2 31  ? 41.781  -46.797 -16.133  1.00 190.72 ? 141  ARG F N   1 
ATOM   16267 C  CA  . ARG F  2 31  ? 42.726  -47.563 -16.939  1.00 185.93 ? 141  ARG F CA  1 
ATOM   16268 C  C   . ARG F  2 31  ? 42.565  -47.241 -18.415  1.00 174.95 ? 141  ARG F C   1 
ATOM   16269 O  O   . ARG F  2 31  ? 43.554  -47.146 -19.152  1.00 165.34 ? 141  ARG F O   1 
ATOM   16270 C  CB  . ARG F  2 31  ? 42.524  -49.055 -16.695  1.00 187.62 ? 141  ARG F CB  1 
ATOM   16271 C  CG  . ARG F  2 31  ? 43.613  -49.940 -17.255  1.00 185.15 ? 141  ARG F CG  1 
ATOM   16272 C  CD  . ARG F  2 31  ? 43.396  -51.370 -16.810  1.00 192.82 ? 141  ARG F CD  1 
ATOM   16273 N  NE  . ARG F  2 31  ? 44.488  -52.250 -17.215  1.00 191.60 ? 141  ARG F NE  1 
ATOM   16274 C  CZ  . ARG F  2 31  ? 44.572  -53.532 -16.877  1.00 199.33 ? 141  ARG F CZ  1 
ATOM   16275 N  NH1 . ARG F  2 31  ? 43.629  -54.084 -16.124  1.00 209.28 ? 141  ARG F NH1 1 
ATOM   16276 N  NH2 . ARG F  2 31  ? 45.602  -54.262 -17.281  1.00 198.19 ? 141  ARG F NH2 1 
ATOM   16277 N  N   . LEU F  2 32  ? 41.321  -47.059 -18.858  1.00 183.81 ? 142  LEU F N   1 
ATOM   16278 C  CA  . LEU F  2 32  ? 41.072  -46.650 -20.232  1.00 177.44 ? 142  LEU F CA  1 
ATOM   16279 C  C   . LEU F  2 32  ? 41.467  -45.196 -20.446  1.00 177.34 ? 142  LEU F C   1 
ATOM   16280 O  O   . LEU F  2 32  ? 41.820  -44.806 -21.565  1.00 174.03 ? 142  LEU F O   1 
ATOM   16281 C  CB  . LEU F  2 32  ? 39.598  -46.888 -20.573  1.00 180.09 ? 142  LEU F CB  1 
ATOM   16282 C  CG  . LEU F  2 32  ? 38.998  -46.455 -21.911  1.00 187.76 ? 142  LEU F CG  1 
ATOM   16283 C  CD1 . LEU F  2 32  ? 37.996  -47.493 -22.405  1.00 178.69 ? 142  LEU F CD1 1 
ATOM   16284 C  CD2 . LEU F  2 32  ? 38.332  -45.096 -21.778  1.00 207.84 ? 142  LEU F CD2 1 
ATOM   16285 N  N   . SER F  2 33  ? 41.453  -44.394 -19.384  1.00 176.07 ? 143  SER F N   1 
ATOM   16286 C  CA  . SER F  2 33  ? 41.839  -42.993 -19.484  1.00 179.33 ? 143  SER F CA  1 
ATOM   16287 C  C   . SER F  2 33  ? 43.352  -42.852 -19.414  1.00 180.79 ? 143  SER F C   1 
ATOM   16288 O  O   . SER F  2 33  ? 43.869  -41.806 -19.004  1.00 174.74 ? 143  SER F O   1 
ATOM   16289 C  CB  . SER F  2 33  ? 41.181  -42.166 -18.380  1.00 186.00 ? 143  SER F CB  1 
ATOM   16290 O  OG  . SER F  2 33  ? 41.577  -40.809 -18.467  1.00 197.06 ? 143  SER F OG  1 
ATOM   16291 N  N   . LYS F  2 34  ? 44.066  -43.904 -19.808  1.00 193.52 ? 144  LYS F N   1 
ATOM   16292 C  CA  . LYS F  2 34  ? 45.521  -43.890 -19.805  1.00 200.29 ? 144  LYS F CA  1 
ATOM   16293 C  C   . LYS F  2 34  ? 46.056  -44.484 -21.100  1.00 190.96 ? 144  LYS F C   1 
ATOM   16294 O  O   . LYS F  2 34  ? 46.878  -43.867 -21.786  1.00 179.30 ? 144  LYS F O   1 
ATOM   16295 C  CB  . LYS F  2 34  ? 46.057  -44.668 -18.602  1.00 208.66 ? 144  LYS F CB  1 
ATOM   16296 C  CG  . LYS F  2 34  ? 47.536  -45.034 -18.688  1.00 215.23 ? 144  LYS F CG  1 
ATOM   16297 C  CD  . LYS F  2 34  ? 48.442  -43.808 -18.713  1.00 223.29 ? 144  LYS F CD  1 
ATOM   16298 C  CE  . LYS F  2 34  ? 49.906  -44.206 -18.885  1.00 214.92 ? 144  LYS F CE  1 
ATOM   16299 N  NZ  . LYS F  2 34  ? 50.813  -43.027 -18.966  1.00 208.07 ? 144  LYS F NZ  1 
ATOM   16300 N  N   . GLU F  2 35  ? 45.572  -45.673 -21.456  1.00 196.03 ? 145  GLU F N   1 
ATOM   16301 C  CA  . GLU F  2 35  ? 46.100  -46.362 -22.623  1.00 205.63 ? 145  GLU F CA  1 
ATOM   16302 C  C   . GLU F  2 35  ? 45.637  -45.735 -23.931  1.00 197.63 ? 145  GLU F C   1 
ATOM   16303 O  O   . GLU F  2 35  ? 46.225  -46.023 -24.979  1.00 192.62 ? 145  GLU F O   1 
ATOM   16304 C  CB  . GLU F  2 35  ? 45.694  -47.840 -22.570  1.00 216.39 ? 145  GLU F CB  1 
ATOM   16305 C  CG  . GLU F  2 35  ? 45.999  -48.546 -21.242  1.00 217.24 ? 145  GLU F CG  1 
ATOM   16306 C  CD  . GLU F  2 35  ? 47.483  -48.720 -20.970  1.00 214.17 ? 145  GLU F CD  1 
ATOM   16307 O  OE1 . GLU F  2 35  ? 48.272  -48.760 -21.938  1.00 214.80 ? 145  GLU F OE1 1 
ATOM   16308 O  OE2 . GLU F  2 35  ? 47.859  -48.818 -19.781  1.00 211.14 ? 145  GLU F OE2 1 
ATOM   16309 N  N   . MET F  2 36  ? 44.624  -44.866 -23.891  1.00 195.32 ? 146  MET F N   1 
ATOM   16310 C  CA  . MET F  2 36  ? 44.122  -44.258 -25.118  1.00 196.56 ? 146  MET F CA  1 
ATOM   16311 C  C   . MET F  2 36  ? 45.114  -43.275 -25.707  1.00 196.70 ? 146  MET F C   1 
ATOM   16312 O  O   . MET F  2 36  ? 45.216  -43.157 -26.933  1.00 198.31 ? 146  MET F O   1 
ATOM   16313 C  CB  . MET F  2 36  ? 42.799  -43.548 -24.851  1.00 200.65 ? 146  MET F CB  1 
ATOM   16314 C  CG  . MET F  2 36  ? 41.608  -44.466 -24.839  1.00 224.81 ? 146  MET F CG  1 
ATOM   16315 S  SD  . MET F  2 36  ? 41.476  -45.332 -26.413  1.00 278.98 ? 146  MET F SD  1 
ATOM   16316 C  CE  . MET F  2 36  ? 41.270  -43.971 -27.558  1.00 250.53 ? 146  MET F CE  1 
ATOM   16317 N  N   . SER F  2 37  ? 45.865  -42.580 -24.856  1.00 200.44 ? 147  SER F N   1 
ATOM   16318 C  CA  . SER F  2 37  ? 46.823  -41.600 -25.336  1.00 215.64 ? 147  SER F CA  1 
ATOM   16319 C  C   . SER F  2 37  ? 48.025  -42.251 -25.997  1.00 221.84 ? 147  SER F C   1 
ATOM   16320 O  O   . SER F  2 37  ? 48.840  -41.543 -26.599  1.00 239.65 ? 147  SER F O   1 
ATOM   16321 C  CB  . SER F  2 37  ? 47.273  -40.711 -24.173  1.00 218.55 ? 147  SER F CB  1 
ATOM   16322 O  OG  . SER F  2 37  ? 48.230  -39.754 -24.591  1.00 233.57 ? 147  SER F OG  1 
ATOM   16323 N  N   . LYS F  2 38  ? 48.140  -43.576 -25.917  1.00 211.67 ? 148  LYS F N   1 
ATOM   16324 C  CA  . LYS F  2 38  ? 49.284  -44.287 -26.470  1.00 224.34 ? 148  LYS F CA  1 
ATOM   16325 C  C   . LYS F  2 38  ? 49.227  -44.344 -27.991  1.00 249.84 ? 148  LYS F C   1 
ATOM   16326 O  O   . LYS F  2 38  ? 50.068  -43.746 -28.672  1.00 267.04 ? 148  LYS F O   1 
ATOM   16327 C  CB  . LYS F  2 38  ? 49.356  -45.705 -25.892  1.00 219.00 ? 148  LYS F CB  1 
ATOM   16328 C  CG  . LYS F  2 38  ? 49.662  -45.760 -24.401  1.00 217.20 ? 148  LYS F CG  1 
ATOM   16329 C  CD  . LYS F  2 38  ? 51.030  -45.178 -24.086  1.00 226.26 ? 148  LYS F CD  1 
ATOM   16330 C  CE  . LYS F  2 38  ? 51.333  -45.243 -22.595  1.00 224.77 ? 148  LYS F CE  1 
ATOM   16331 N  NZ  . LYS F  2 38  ? 51.345  -46.640 -22.079  1.00 213.60 ? 148  LYS F NZ  1 
ATOM   16332 N  N   . LEU F  2 39  ? 48.234  -45.046 -28.536  1.00 240.32 ? 149  LEU F N   1 
ATOM   16333 C  CA  . LEU F  2 39  ? 48.177  -45.294 -29.972  1.00 230.88 ? 149  LEU F CA  1 
ATOM   16334 C  C   . LEU F  2 39  ? 47.660  -44.108 -30.775  1.00 247.97 ? 149  LEU F C   1 
ATOM   16335 O  O   . LEU F  2 39  ? 47.633  -44.186 -32.008  1.00 252.41 ? 149  LEU F O   1 
ATOM   16336 C  CB  . LEU F  2 39  ? 47.313  -46.523 -30.259  1.00 210.73 ? 149  LEU F CB  1 
ATOM   16337 C  CG  . LEU F  2 39  ? 48.073  -47.748 -30.770  1.00 212.28 ? 149  LEU F CG  1 
ATOM   16338 C  CD1 . LEU F  2 39  ? 47.119  -48.902 -30.997  1.00 220.71 ? 149  LEU F CD1 1 
ATOM   16339 C  CD2 . LEU F  2 39  ? 48.830  -47.419 -32.049  1.00 217.59 ? 149  LEU F CD2 1 
ATOM   16340 N  N   . THR F  2 40  ? 47.248  -43.023 -30.125  1.00 243.08 ? 150  THR F N   1 
ATOM   16341 C  CA  . THR F  2 40  ? 46.781  -41.855 -30.856  1.00 230.68 ? 150  THR F CA  1 
ATOM   16342 C  C   . THR F  2 40  ? 46.944  -40.617 -29.993  1.00 209.26 ? 150  THR F C   1 
ATOM   16343 O  O   . THR F  2 40  ? 46.955  -40.690 -28.761  1.00 202.70 ? 150  THR F O   1 
ATOM   16344 C  CB  . THR F  2 40  ? 45.316  -41.990 -31.290  1.00 232.82 ? 150  THR F CB  1 
ATOM   16345 O  OG1 . THR F  2 40  ? 44.921  -40.812 -32.008  1.00 226.88 ? 150  THR F OG1 1 
ATOM   16346 C  CG2 . THR F  2 40  ? 44.410  -42.169 -30.076  1.00 236.64 ? 150  THR F CG2 1 
ATOM   16347 N  N   . SER F  2 41  ? 47.080  -39.480 -30.666  1.00 207.56 ? 151  SER F N   1 
ATOM   16348 C  CA  . SER F  2 41  ? 47.134  -38.183 -30.011  1.00 217.21 ? 151  SER F CA  1 
ATOM   16349 C  C   . SER F  2 41  ? 45.797  -37.459 -30.062  1.00 220.59 ? 151  SER F C   1 
ATOM   16350 O  O   . SER F  2 41  ? 45.535  -36.603 -29.210  1.00 214.31 ? 151  SER F O   1 
ATOM   16351 C  CB  . SER F  2 41  ? 48.225  -37.308 -30.641  1.00 232.03 ? 151  SER F CB  1 
ATOM   16352 O  OG  . SER F  2 41  ? 48.094  -37.262 -32.048  1.00 245.00 ? 151  SER F OG  1 
ATOM   16353 N  N   . ASN F  2 42  ? 44.956  -37.773 -31.051  1.00 213.46 ? 152  ASN F N   1 
ATOM   16354 C  CA  . ASN F  2 42  ? 43.620  -37.183 -31.170  1.00 215.92 ? 152  ASN F CA  1 
ATOM   16355 C  C   . ASN F  2 42  ? 42.624  -38.060 -30.424  1.00 217.33 ? 152  ASN F C   1 
ATOM   16356 O  O   . ASN F  2 42  ? 41.905  -38.879 -31.001  1.00 206.05 ? 152  ASN F O   1 
ATOM   16357 C  CB  . ASN F  2 42  ? 43.226  -37.034 -32.628  1.00 221.33 ? 152  ASN F CB  1 
ATOM   16358 C  CG  . ASN F  2 42  ? 44.338  -36.487 -33.463  1.00 246.38 ? 152  ASN F CG  1 
ATOM   16359 O  OD1 . ASN F  2 42  ? 44.881  -37.175 -34.325  1.00 244.24 ? 152  ASN F OD1 1 
ATOM   16360 N  ND2 . ASN F  2 42  ? 44.705  -35.240 -33.201  1.00 268.50 ? 152  ASN F ND2 1 
ATOM   16361 N  N   . PHE F  2 43  ? 42.580  -37.877 -29.110  1.00 233.85 ? 153  PHE F N   1 
ATOM   16362 C  CA  . PHE F  2 43  ? 41.749  -38.698 -28.244  1.00 225.05 ? 153  PHE F CA  1 
ATOM   16363 C  C   . PHE F  2 43  ? 40.807  -37.811 -27.441  1.00 228.41 ? 153  PHE F C   1 
ATOM   16364 O  O   . PHE F  2 43  ? 41.258  -36.965 -26.661  1.00 241.03 ? 153  PHE F O   1 
ATOM   16365 C  CB  . PHE F  2 43  ? 42.616  -39.550 -27.321  1.00 209.15 ? 153  PHE F CB  1 
ATOM   16366 C  CG  . PHE F  2 43  ? 41.929  -39.954 -26.062  1.00 214.62 ? 153  PHE F CG  1 
ATOM   16367 C  CD1 . PHE F  2 43  ? 40.889  -40.866 -26.098  1.00 220.08 ? 153  PHE F CD1 1 
ATOM   16368 C  CD2 . PHE F  2 43  ? 42.318  -39.427 -24.843  1.00 224.39 ? 153  PHE F CD2 1 
ATOM   16369 C  CE1 . PHE F  2 43  ? 40.245  -41.247 -24.943  1.00 230.75 ? 153  PHE F CE1 1 
ATOM   16370 C  CE2 . PHE F  2 43  ? 41.679  -39.806 -23.678  1.00 239.87 ? 153  PHE F CE2 1 
ATOM   16371 C  CZ  . PHE F  2 43  ? 40.642  -40.720 -23.729  1.00 243.49 ? 153  PHE F CZ  1 
ATOM   16372 N  N   . ARG F  2 44  ? 39.504  -38.017 -27.626  1.00 205.73 ? 154  ARG F N   1 
ATOM   16373 C  CA  . ARG F  2 44  ? 38.474  -37.348 -26.842  1.00 197.98 ? 154  ARG F CA  1 
ATOM   16374 C  C   . ARG F  2 44  ? 37.477  -38.397 -26.382  1.00 195.25 ? 154  ARG F C   1 
ATOM   16375 O  O   . ARG F  2 44  ? 37.032  -39.222 -27.185  1.00 207.07 ? 154  ARG F O   1 
ATOM   16376 C  CB  . ARG F  2 44  ? 37.758  -36.259 -27.647  1.00 213.27 ? 154  ARG F CB  1 
ATOM   16377 C  CG  . ARG F  2 44  ? 38.660  -35.128 -28.098  1.00 232.94 ? 154  ARG F CG  1 
ATOM   16378 C  CD  . ARG F  2 44  ? 37.862  -33.977 -28.696  1.00 240.67 ? 154  ARG F CD  1 
ATOM   16379 N  NE  . ARG F  2 44  ? 36.939  -34.406 -29.742  1.00 240.68 ? 154  ARG F NE  1 
ATOM   16380 C  CZ  . ARG F  2 44  ? 36.156  -33.578 -30.427  1.00 236.07 ? 154  ARG F CZ  1 
ATOM   16381 N  NH1 . ARG F  2 44  ? 36.185  -32.276 -30.177  1.00 238.37 ? 154  ARG F NH1 1 
ATOM   16382 N  NH2 . ARG F  2 44  ? 35.343  -34.050 -31.360  1.00 233.90 ? 154  ARG F NH2 1 
ATOM   16383 N  N   . LEU F  2 45  ? 37.134  -38.378 -25.095  1.00 193.43 ? 155  LEU F N   1 
ATOM   16384 C  CA  . LEU F  2 45  ? 36.231  -39.373 -24.536  1.00 201.86 ? 155  LEU F CA  1 
ATOM   16385 C  C   . LEU F  2 45  ? 35.116  -38.709 -23.736  1.00 212.88 ? 155  LEU F C   1 
ATOM   16386 O  O   . LEU F  2 45  ? 35.292  -37.624 -23.174  1.00 226.73 ? 155  LEU F O   1 
ATOM   16387 C  CB  . LEU F  2 45  ? 36.990  -40.381 -23.659  1.00 206.33 ? 155  LEU F CB  1 
ATOM   16388 C  CG  . LEU F  2 45  ? 37.272  -40.047 -22.193  1.00 216.67 ? 155  LEU F CG  1 
ATOM   16389 C  CD1 . LEU F  2 45  ? 37.901  -41.250 -21.510  1.00 204.72 ? 155  LEU F CD1 1 
ATOM   16390 C  CD2 . LEU F  2 45  ? 38.161  -38.815 -22.049  1.00 230.20 ? 155  LEU F CD2 1 
ATOM   16391 N  N   . GLY F  2 46  ? 33.958  -39.378 -23.700  1.00 206.75 ? 156  GLY F N   1 
ATOM   16392 C  CA  . GLY F  2 46  ? 32.792  -38.892 -22.981  1.00 204.83 ? 156  GLY F CA  1 
ATOM   16393 C  C   . GLY F  2 46  ? 32.218  -39.902 -22.006  1.00 202.53 ? 156  GLY F C   1 
ATOM   16394 O  O   . GLY F  2 46  ? 32.832  -40.946 -21.765  1.00 202.97 ? 156  GLY F O   1 
ATOM   16395 N  N   . PHE F  2 47  ? 31.040  -39.619 -21.448  1.00 209.61 ? 157  PHE F N   1 
ATOM   16396 C  CA  . PHE F  2 47  ? 30.454  -40.493 -20.439  1.00 206.50 ? 157  PHE F CA  1 
ATOM   16397 C  C   . PHE F  2 47  ? 28.950  -40.272 -20.354  1.00 209.15 ? 157  PHE F C   1 
ATOM   16398 O  O   . PHE F  2 47  ? 28.470  -39.147 -20.515  1.00 210.14 ? 157  PHE F O   1 
ATOM   16399 C  CB  . PHE F  2 47  ? 31.088  -40.257 -19.063  1.00 213.77 ? 157  PHE F CB  1 
ATOM   16400 C  CG  . PHE F  2 47  ? 30.461  -41.063 -17.960  1.00 216.07 ? 157  PHE F CG  1 
ATOM   16401 C  CD1 . PHE F  2 47  ? 30.770  -42.404 -17.805  1.00 220.68 ? 157  PHE F CD1 1 
ATOM   16402 C  CD2 . PHE F  2 47  ? 29.560  -40.483 -17.082  1.00 215.36 ? 157  PHE F CD2 1 
ATOM   16403 C  CE1 . PHE F  2 47  ? 30.197  -43.150 -16.791  1.00 222.03 ? 157  PHE F CE1 1 
ATOM   16404 C  CE2 . PHE F  2 47  ? 28.982  -41.225 -16.066  1.00 219.76 ? 157  PHE F CE2 1 
ATOM   16405 C  CZ  . PHE F  2 47  ? 29.302  -42.560 -15.921  1.00 223.17 ? 157  PHE F CZ  1 
ATOM   16406 N  N   . GLY F  2 48  ? 28.226  -41.352 -20.089  1.00 215.73 ? 158  GLY F N   1 
ATOM   16407 C  CA  . GLY F  2 48  ? 26.784  -41.292 -19.915  1.00 220.14 ? 158  GLY F CA  1 
ATOM   16408 C  C   . GLY F  2 48  ? 26.310  -42.440 -19.053  1.00 217.92 ? 158  GLY F C   1 
ATOM   16409 O  O   . GLY F  2 48  ? 26.917  -43.516 -19.034  1.00 220.12 ? 158  GLY F O   1 
ATOM   16410 N  N   . SER F  2 49  ? 25.216  -42.211 -18.332  1.00 208.99 ? 159  SER F N   1 
ATOM   16411 C  CA  . SER F  2 49  ? 24.677  -43.202 -17.410  1.00 204.65 ? 159  SER F CA  1 
ATOM   16412 C  C   . SER F  2 49  ? 23.192  -43.424 -17.669  1.00 213.13 ? 159  SER F C   1 
ATOM   16413 O  O   . SER F  2 49  ? 22.488  -42.528 -18.146  1.00 217.08 ? 159  SER F O   1 
ATOM   16414 C  CB  . SER F  2 49  ? 24.902  -42.774 -15.960  1.00 205.71 ? 159  SER F CB  1 
ATOM   16415 O  OG  . SER F  2 49  ? 24.364  -41.485 -15.731  1.00 215.80 ? 159  SER F OG  1 
ATOM   16416 N  N   . PHE F  2 50  ? 22.721  -44.633 -17.354  1.00 209.55 ? 160  PHE F N   1 
ATOM   16417 C  CA  . PHE F  2 50  ? 21.320  -44.992 -17.544  1.00 223.41 ? 160  PHE F CA  1 
ATOM   16418 C  C   . PHE F  2 50  ? 20.892  -45.965 -16.454  1.00 210.61 ? 160  PHE F C   1 
ATOM   16419 O  O   . PHE F  2 50  ? 21.721  -46.624 -15.820  1.00 194.58 ? 160  PHE F O   1 
ATOM   16420 C  CB  . PHE F  2 50  ? 21.070  -45.617 -18.921  1.00 241.06 ? 160  PHE F CB  1 
ATOM   16421 C  CG  . PHE F  2 50  ? 21.731  -46.952 -19.108  1.00 239.19 ? 160  PHE F CG  1 
ATOM   16422 C  CD1 . PHE F  2 50  ? 23.045  -47.030 -19.530  1.00 246.30 ? 160  PHE F CD1 1 
ATOM   16423 C  CD2 . PHE F  2 50  ? 21.036  -48.129 -18.870  1.00 232.63 ? 160  PHE F CD2 1 
ATOM   16424 C  CE1 . PHE F  2 50  ? 23.659  -48.252 -19.706  1.00 244.25 ? 160  PHE F CE1 1 
ATOM   16425 C  CE2 . PHE F  2 50  ? 21.644  -49.355 -19.040  1.00 232.94 ? 160  PHE F CE2 1 
ATOM   16426 C  CZ  . PHE F  2 50  ? 22.955  -49.417 -19.464  1.00 238.40 ? 160  PHE F CZ  1 
ATOM   16427 N  N   . VAL F  2 51  ? 19.575  -46.054 -16.249  1.00 219.43 ? 161  VAL F N   1 
ATOM   16428 C  CA  . VAL F  2 51  ? 18.993  -47.020 -15.321  1.00 211.07 ? 161  VAL F CA  1 
ATOM   16429 C  C   . VAL F  2 51  ? 17.793  -47.696 -15.973  1.00 216.13 ? 161  VAL F C   1 
ATOM   16430 O  O   . VAL F  2 51  ? 17.883  -48.846 -16.417  1.00 221.33 ? 161  VAL F O   1 
ATOM   16431 C  CB  . VAL F  2 51  ? 18.582  -46.353 -13.995  1.00 209.67 ? 161  VAL F CB  1 
ATOM   16432 C  CG1 . VAL F  2 51  ? 18.041  -47.388 -13.026  1.00 210.75 ? 161  VAL F CG1 1 
ATOM   16433 C  CG2 . VAL F  2 51  ? 19.756  -45.616 -13.373  1.00 212.38 ? 161  VAL F CG2 1 
ATOM   16434 N  N   . GLU F  2 52  ? 16.675  -46.976 -16.059  1.00 206.80 ? 162  GLU F N   1 
ATOM   16435 C  CA  . GLU F  2 52  ? 15.408  -47.545 -16.504  1.00 210.24 ? 162  GLU F CA  1 
ATOM   16436 C  C   . GLU F  2 52  ? 14.402  -46.411 -16.657  1.00 213.98 ? 162  GLU F C   1 
ATOM   16437 O  O   . GLU F  2 52  ? 14.593  -45.320 -16.115  1.00 219.05 ? 162  GLU F O   1 
ATOM   16438 C  CB  . GLU F  2 52  ? 14.896  -48.600 -15.513  1.00 220.15 ? 162  GLU F CB  1 
ATOM   16439 C  CG  . GLU F  2 52  ? 13.722  -49.434 -15.997  1.00 232.02 ? 162  GLU F CG  1 
ATOM   16440 C  CD  . GLU F  2 52  ? 14.111  -50.387 -17.109  1.00 232.27 ? 162  GLU F CD  1 
ATOM   16441 O  OE1 . GLU F  2 52  ? 14.194  -49.941 -18.273  1.00 230.84 ? 162  GLU F OE1 1 
ATOM   16442 O  OE2 . GLU F  2 52  ? 14.348  -51.579 -16.814  1.00 232.30 ? 162  GLU F OE2 1 
ATOM   16443 N  N   . LYS F  2 53  ? 13.324  -46.684 -17.386  1.00 209.80 ? 163  LYS F N   1 
ATOM   16444 C  CA  . LYS F  2 53  ? 12.260  -45.693 -17.552  1.00 216.67 ? 163  LYS F CA  1 
ATOM   16445 C  C   . LYS F  2 53  ? 11.521  -45.495 -16.233  1.00 225.27 ? 163  LYS F C   1 
ATOM   16446 O  O   . LYS F  2 53  ? 11.031  -46.473 -15.653  1.00 229.16 ? 163  LYS F O   1 
ATOM   16447 C  CB  . LYS F  2 53  ? 11.284  -46.119 -18.644  1.00 227.45 ? 163  LYS F CB  1 
ATOM   16448 C  CG  . LYS F  2 53  ? 11.856  -46.105 -20.055  1.00 228.32 ? 163  LYS F CG  1 
ATOM   16449 C  CD  . LYS F  2 53  ? 10.766  -46.379 -21.082  1.00 237.42 ? 163  LYS F CD  1 
ATOM   16450 C  CE  . LYS F  2 53  ? 11.300  -46.310 -22.505  1.00 230.95 ? 163  LYS F CE  1 
ATOM   16451 N  NZ  . LYS F  2 53  ? 11.826  -44.954 -22.839  1.00 225.57 ? 163  LYS F NZ  1 
ATOM   16452 N  N   . PRO F  2 54  ? 11.430  -44.265 -15.717  1.00 227.90 ? 164  PRO F N   1 
ATOM   16453 C  CA  . PRO F  2 54  ? 10.830  -44.050 -14.392  1.00 232.33 ? 164  PRO F CA  1 
ATOM   16454 C  C   . PRO F  2 54  ? 9.314   -44.181 -14.369  1.00 242.67 ? 164  PRO F C   1 
ATOM   16455 O  O   . PRO F  2 54  ? 8.629   -43.247 -13.940  1.00 255.30 ? 164  PRO F O   1 
ATOM   16456 C  CB  . PRO F  2 54  ? 11.265  -42.620 -14.049  1.00 225.10 ? 164  PRO F CB  1 
ATOM   16457 C  CG  . PRO F  2 54  ? 11.405  -41.952 -15.374  1.00 216.51 ? 164  PRO F CG  1 
ATOM   16458 C  CD  . PRO F  2 54  ? 11.907  -43.010 -16.323  1.00 218.24 ? 164  PRO F CD  1 
ATOM   16459 N  N   . VAL F  2 55  ? 8.768   -45.309 -14.832  1.00 239.50 ? 165  VAL F N   1 
ATOM   16460 C  CA  . VAL F  2 55  ? 7.325   -45.527 -14.851  1.00 245.88 ? 165  VAL F CA  1 
ATOM   16461 C  C   . VAL F  2 55  ? 7.027   -46.940 -14.363  1.00 236.96 ? 165  VAL F C   1 
ATOM   16462 O  O   . VAL F  2 55  ? 7.822   -47.865 -14.555  1.00 230.64 ? 165  VAL F O   1 
ATOM   16463 C  CB  . VAL F  2 55  ? 6.716   -45.309 -16.261  1.00 255.57 ? 165  VAL F CB  1 
ATOM   16464 C  CG1 . VAL F  2 55  ? 5.195   -45.238 -16.189  1.00 269.39 ? 165  VAL F CG1 1 
ATOM   16465 C  CG2 . VAL F  2 55  ? 7.271   -44.053 -16.919  1.00 250.69 ? 165  VAL F CG2 1 
ATOM   16466 N  N   . SER F  2 56  ? 5.882   -47.092 -13.700  1.00 240.66 ? 166  SER F N   1 
ATOM   16467 C  CA  . SER F  2 56  ? 5.357   -48.404 -13.337  1.00 244.75 ? 166  SER F CA  1 
ATOM   16468 C  C   . SER F  2 56  ? 5.157   -49.200 -14.624  1.00 246.73 ? 166  SER F C   1 
ATOM   16469 O  O   . SER F  2 56  ? 4.806   -48.626 -15.652  1.00 248.44 ? 166  SER F O   1 
ATOM   16470 C  CB  . SER F  2 56  ? 4.040   -48.260 -12.565  1.00 252.39 ? 166  SER F CB  1 
ATOM   16471 O  OG  . SER F  2 56  ? 3.743   -49.416 -11.801  1.00 255.79 ? 166  SER F OG  1 
ATOM   16472 N  N   . PRO F  2 57  ? 5.356   -50.526 -14.580  1.00 247.30 ? 167  PRO F N   1 
ATOM   16473 C  CA  . PRO F  2 57  ? 5.656   -51.381 -13.427  1.00 246.96 ? 167  PRO F CA  1 
ATOM   16474 C  C   . PRO F  2 57  ? 7.146   -51.548 -13.124  1.00 238.95 ? 167  PRO F C   1 
ATOM   16475 O  O   . PRO F  2 57  ? 7.499   -52.320 -12.233  1.00 238.79 ? 167  PRO F O   1 
ATOM   16476 C  CB  . PRO F  2 57  ? 5.051   -52.718 -13.846  1.00 252.86 ? 167  PRO F CB  1 
ATOM   16477 C  CG  . PRO F  2 57  ? 5.268   -52.752 -15.321  1.00 251.72 ? 167  PRO F CG  1 
ATOM   16478 C  CD  . PRO F  2 57  ? 5.160   -51.324 -15.806  1.00 249.96 ? 167  PRO F CD  1 
ATOM   16479 N  N   . PHE F  2 58  ? 8.004   -50.842 -13.865  1.00 241.17 ? 168  PHE F N   1 
ATOM   16480 C  CA  . PHE F  2 58  ? 9.445   -51.024 -13.708  1.00 228.30 ? 168  PHE F CA  1 
ATOM   16481 C  C   . PHE F  2 58  ? 9.959   -50.493 -12.374  1.00 222.96 ? 168  PHE F C   1 
ATOM   16482 O  O   . PHE F  2 58  ? 10.961  -50.999 -11.857  1.00 219.09 ? 168  PHE F O   1 
ATOM   16483 C  CB  . PHE F  2 58  ? 10.171  -50.359 -14.873  1.00 230.04 ? 168  PHE F CB  1 
ATOM   16484 C  CG  . PHE F  2 58  ? 9.715   -50.848 -16.215  1.00 241.24 ? 168  PHE F CG  1 
ATOM   16485 C  CD1 . PHE F  2 58  ? 9.428   -52.190 -16.414  1.00 247.11 ? 168  PHE F CD1 1 
ATOM   16486 C  CD2 . PHE F  2 58  ? 9.552   -49.970 -17.272  1.00 249.61 ? 168  PHE F CD2 1 
ATOM   16487 C  CE1 . PHE F  2 58  ? 9.001   -52.648 -17.646  1.00 255.93 ? 168  PHE F CE1 1 
ATOM   16488 C  CE2 . PHE F  2 58  ? 9.123   -50.421 -18.507  1.00 256.12 ? 168  PHE F CE2 1 
ATOM   16489 C  CZ  . PHE F  2 58  ? 8.848   -51.762 -18.694  1.00 257.84 ? 168  PHE F CZ  1 
ATOM   16490 N  N   . VAL F  2 59  ? 9.312   -49.472 -11.813  1.00 229.62 ? 169  VAL F N   1 
ATOM   16491 C  CA  . VAL F  2 59  ? 9.654   -48.947 -10.497  1.00 224.17 ? 169  VAL F CA  1 
ATOM   16492 C  C   . VAL F  2 59  ? 8.379   -48.859 -9.675   1.00 234.57 ? 169  VAL F C   1 
ATOM   16493 O  O   . VAL F  2 59  ? 7.314   -48.519 -10.204  1.00 248.47 ? 169  VAL F O   1 
ATOM   16494 C  CB  . VAL F  2 59  ? 10.331  -47.563 -10.571  1.00 219.62 ? 169  VAL F CB  1 
ATOM   16495 C  CG1 . VAL F  2 59  ? 10.968  -47.218 -9.230   1.00 217.97 ? 169  VAL F CG1 1 
ATOM   16496 C  CG2 . VAL F  2 59  ? 11.355  -47.527 -11.683  1.00 213.79 ? 169  VAL F CG2 1 
ATOM   16497 N  N   . LYS F  2 60  ? 8.487   -49.156 -8.382   1.00 233.13 ? 170  LYS F N   1 
ATOM   16498 C  CA  . LYS F  2 60  ? 7.330   -49.022 -7.510   1.00 247.67 ? 170  LYS F CA  1 
ATOM   16499 C  C   . LYS F  2 60  ? 6.918   -47.559 -7.408   1.00 244.57 ? 170  LYS F C   1 
ATOM   16500 O  O   . LYS F  2 60  ? 7.759   -46.655 -7.401   1.00 235.87 ? 170  LYS F O   1 
ATOM   16501 C  CB  . LYS F  2 60  ? 7.621   -49.592 -6.120   1.00 249.46 ? 170  LYS F CB  1 
ATOM   16502 C  CG  . LYS F  2 60  ? 7.428   -51.100 -6.016   1.00 253.53 ? 170  LYS F CG  1 
ATOM   16503 C  CD  . LYS F  2 60  ? 7.459   -51.565 -4.567   1.00 257.40 ? 170  LYS F CD  1 
ATOM   16504 C  CE  . LYS F  2 60  ? 7.148   -53.054 -4.435   1.00 262.98 ? 170  LYS F CE  1 
ATOM   16505 N  NZ  . LYS F  2 60  ? 8.093   -53.915 -5.203   1.00 256.74 ? 170  LYS F NZ  1 
ATOM   16506 N  N   . THR F  2 61  ? 5.606   -47.331 -7.342   1.00 247.71 ? 171  THR F N   1 
ATOM   16507 C  CA  . THR F  2 61  ? 5.029   -45.995 -7.370   1.00 249.85 ? 171  THR F CA  1 
ATOM   16508 C  C   . THR F  2 61  ? 4.611   -45.513 -5.985   1.00 254.25 ? 171  THR F C   1 
ATOM   16509 O  O   . THR F  2 61  ? 3.677   -44.711 -5.862   1.00 261.89 ? 171  THR F O   1 
ATOM   16510 C  CB  . THR F  2 61  ? 3.840   -45.960 -8.327   1.00 255.08 ? 171  THR F CB  1 
ATOM   16511 O  OG1 . THR F  2 61  ? 3.035   -47.130 -8.134   1.00 260.82 ? 171  THR F OG1 1 
ATOM   16512 C  CG2 . THR F  2 61  ? 4.322   -45.922 -9.766   1.00 250.72 ? 171  THR F CG2 1 
ATOM   16513 N  N   . THR F  2 62  ? 5.289   -45.987 -4.933   1.00 258.24 ? 172  THR F N   1 
ATOM   16514 C  CA  . THR F  2 62  ? 5.062   -45.510 -3.574   1.00 260.51 ? 172  THR F CA  1 
ATOM   16515 C  C   . THR F  2 62  ? 5.933   -44.284 -3.295   1.00 252.79 ? 172  THR F C   1 
ATOM   16516 O  O   . THR F  2 62  ? 7.095   -44.246 -3.710   1.00 247.00 ? 172  THR F O   1 
ATOM   16517 C  CB  . THR F  2 62  ? 5.372   -46.610 -2.562   1.00 260.13 ? 172  THR F CB  1 
ATOM   16518 O  OG1 . THR F  2 62  ? 6.724   -47.063 -2.730   1.00 251.77 ? 172  THR F OG1 1 
ATOM   16519 C  CG2 . THR F  2 62  ? 4.418   -47.788 -2.747   1.00 264.54 ? 172  THR F CG2 1 
ATOM   16520 N  N   . PRO F  2 63  ? 5.388   -43.272 -2.606   1.00 257.26 ? 173  PRO F N   1 
ATOM   16521 C  CA  . PRO F  2 63  ? 6.122   -42.002 -2.439   1.00 254.16 ? 173  PRO F CA  1 
ATOM   16522 C  C   . PRO F  2 63  ? 7.541   -42.146 -1.899   1.00 248.75 ? 173  PRO F C   1 
ATOM   16523 O  O   . PRO F  2 63  ? 8.398   -41.309 -2.213   1.00 244.36 ? 173  PRO F O   1 
ATOM   16524 C  CB  . PRO F  2 63  ? 5.224   -41.203 -1.479   1.00 261.66 ? 173  PRO F CB  1 
ATOM   16525 C  CG  . PRO F  2 63  ? 4.295   -42.209 -0.867   1.00 267.96 ? 173  PRO F CG  1 
ATOM   16526 C  CD  . PRO F  2 63  ? 4.085   -43.245 -1.922   1.00 265.95 ? 173  PRO F CD  1 
ATOM   16527 N  N   . GLU F  2 64  ? 7.826   -43.183 -1.111   1.00 257.27 ? 174  GLU F N   1 
ATOM   16528 C  CA  . GLU F  2 64  ? 9.173   -43.350 -0.572   1.00 245.18 ? 174  GLU F CA  1 
ATOM   16529 C  C   . GLU F  2 64  ? 10.115  -43.985 -1.586   1.00 237.75 ? 174  GLU F C   1 
ATOM   16530 O  O   . GLU F  2 64  ? 11.281  -43.588 -1.687   1.00 232.45 ? 174  GLU F O   1 
ATOM   16531 C  CB  . GLU F  2 64  ? 9.126   -44.195 0.700    1.00 256.21 ? 174  GLU F CB  1 
ATOM   16532 C  CG  . GLU F  2 64  ? 10.487  -44.511 1.294    1.00 246.24 ? 174  GLU F CG  1 
ATOM   16533 C  CD  . GLU F  2 64  ? 10.386  -45.380 2.529    1.00 251.90 ? 174  GLU F CD  1 
ATOM   16534 O  OE1 . GLU F  2 64  ? 9.257   -45.578 3.026    1.00 259.44 ? 174  GLU F OE1 1 
ATOM   16535 O  OE2 . GLU F  2 64  ? 11.431  -45.869 3.000    1.00 249.80 ? 174  GLU F OE2 1 
ATOM   16536 N  N   . GLU F  2 65  ? 9.628   -44.958 -2.352   1.00 237.85 ? 175  GLU F N   1 
ATOM   16537 C  CA  . GLU F  2 65  ? 10.466  -45.705 -3.280   1.00 237.65 ? 175  GLU F CA  1 
ATOM   16538 C  C   . GLU F  2 65  ? 10.654  -44.988 -4.610   1.00 245.10 ? 175  GLU F C   1 
ATOM   16539 O  O   . GLU F  2 65  ? 11.296  -45.535 -5.515   1.00 229.65 ? 175  GLU F O   1 
ATOM   16540 C  CB  . GLU F  2 65  ? 9.865   -47.094 -3.507   1.00 243.88 ? 175  GLU F CB  1 
ATOM   16541 C  CG  . GLU F  2 65  ? 10.860  -48.152 -3.947   1.00 251.13 ? 175  GLU F CG  1 
ATOM   16542 C  CD  . GLU F  2 65  ? 10.310  -49.549 -3.781   1.00 270.42 ? 175  GLU F CD  1 
ATOM   16543 O  OE1 . GLU F  2 65  ? 9.530   -49.763 -2.830   1.00 279.95 ? 175  GLU F OE1 1 
ATOM   16544 O  OE2 . GLU F  2 65  ? 10.654  -50.430 -4.597   1.00 270.44 ? 175  GLU F OE2 1 
ATOM   16545 N  N   . ILE F  2 66  ? 10.113  -43.784 -4.750   1.00 250.32 ? 176  ILE F N   1 
ATOM   16546 C  CA  . ILE F  2 66  ? 10.380  -42.961 -5.921   1.00 243.04 ? 176  ILE F CA  1 
ATOM   16547 C  C   . ILE F  2 66  ? 11.656  -42.156 -5.738   1.00 239.31 ? 176  ILE F C   1 
ATOM   16548 O  O   . ILE F  2 66  ? 12.525  -42.140 -6.613   1.00 234.29 ? 176  ILE F O   1 
ATOM   16549 C  CB  . ILE F  2 66  ? 9.176   -42.043 -6.210   1.00 230.75 ? 176  ILE F CB  1 
ATOM   16550 C  CG1 . ILE F  2 66  ? 7.922   -42.876 -6.480   1.00 241.24 ? 176  ILE F CG1 1 
ATOM   16551 C  CG2 . ILE F  2 66  ? 9.485   -41.140 -7.391   1.00 228.29 ? 176  ILE F CG2 1 
ATOM   16552 C  CD1 . ILE F  2 66  ? 6.672   -42.052 -6.678   1.00 259.81 ? 176  ILE F CD1 1 
ATOM   16553 N  N   . ALA F  2 67  ? 11.778  -41.476 -4.596   1.00 229.70 ? 177  ALA F N   1 
ATOM   16554 C  CA  . ALA F  2 67  ? 12.991  -40.735 -4.277   1.00 221.80 ? 177  ALA F CA  1 
ATOM   16555 C  C   . ALA F  2 67  ? 14.106  -41.638 -3.772   1.00 220.56 ? 177  ALA F C   1 
ATOM   16556 O  O   . ALA F  2 67  ? 15.276  -41.238 -3.800   1.00 211.89 ? 177  ALA F O   1 
ATOM   16557 C  CB  . ALA F  2 67  ? 12.690  -39.653 -3.237   1.00 224.49 ? 177  ALA F CB  1 
ATOM   16558 N  N   . ASN F  2 68  ? 13.774  -42.841 -3.310   1.00 220.96 ? 178  ASN F N   1 
ATOM   16559 C  CA  . ASN F  2 68  ? 14.767  -43.799 -2.832   1.00 215.23 ? 178  ASN F CA  1 
ATOM   16560 C  C   . ASN F  2 68  ? 14.326  -45.188 -3.257   1.00 215.64 ? 178  ASN F C   1 
ATOM   16561 O  O   . ASN F  2 68  ? 13.685  -45.916 -2.489   1.00 220.58 ? 178  ASN F O   1 
ATOM   16562 C  CB  . ASN F  2 68  ? 14.939  -43.727 -1.317   1.00 219.40 ? 178  ASN F CB  1 
ATOM   16563 C  CG  . ASN F  2 68  ? 15.997  -44.686 -0.808   1.00 217.37 ? 178  ASN F CG  1 
ATOM   16564 O  OD1 . ASN F  2 68  ? 17.008  -44.917 -1.467   1.00 211.68 ? 178  ASN F OD1 1 
ATOM   16565 N  ND2 . ASN F  2 68  ? 15.760  -45.263 0.363    1.00 222.55 ? 178  ASN F ND2 1 
ATOM   16566 N  N   . PRO F  2 69  ? 14.662  -45.597 -4.483   1.00 213.44 ? 179  PRO F N   1 
ATOM   16567 C  CA  . PRO F  2 69  ? 14.250  -46.929 -4.948   1.00 220.61 ? 179  PRO F CA  1 
ATOM   16568 C  C   . PRO F  2 69  ? 14.971  -48.070 -4.246   1.00 236.39 ? 179  PRO F C   1 
ATOM   16569 O  O   . PRO F  2 69  ? 14.577  -49.229 -4.434   1.00 246.33 ? 179  PRO F O   1 
ATOM   16570 C  CB  . PRO F  2 69  ? 14.562  -46.888 -6.452   1.00 216.22 ? 179  PRO F CB  1 
ATOM   16571 C  CG  . PRO F  2 69  ? 15.620  -45.855 -6.595   1.00 209.26 ? 179  PRO F CG  1 
ATOM   16572 C  CD  . PRO F  2 69  ? 15.334  -44.822 -5.539   1.00 209.71 ? 179  PRO F CD  1 
ATOM   16573 N  N   . CYS F  2 70  ? 15.990  -47.790 -3.428   1.00 236.75 ? 180  CYS F N   1 
ATOM   16574 C  CA  . CYS F  2 70  ? 16.644  -48.817 -2.629   1.00 229.16 ? 180  CYS F CA  1 
ATOM   16575 C  C   . CYS F  2 70  ? 16.027  -48.945 -1.249   1.00 241.31 ? 180  CYS F C   1 
ATOM   16576 O  O   . CYS F  2 70  ? 16.698  -49.409 -0.318   1.00 247.60 ? 180  CYS F O   1 
ATOM   16577 C  CB  . CYS F  2 70  ? 18.142  -48.537 -2.488   1.00 216.94 ? 180  CYS F CB  1 
ATOM   16578 S  SG  . CYS F  2 70  ? 19.068  -48.527 -4.015   1.00 202.76 ? 180  CYS F SG  1 
ATOM   16579 N  N   . SER F  2 71  ? 14.770  -48.540 -1.097   1.00 226.47 ? 181  SER F N   1 
ATOM   16580 C  CA  . SER F  2 71  ? 14.088  -48.668 0.174    1.00 230.05 ? 181  SER F CA  1 
ATOM   16581 C  C   . SER F  2 71  ? 13.813  -50.141 0.455    1.00 233.99 ? 181  SER F C   1 
ATOM   16582 O  O   . SER F  2 71  ? 14.024  -51.009 -0.395   1.00 236.70 ? 181  SER F O   1 
ATOM   16583 C  CB  . SER F  2 71  ? 12.788  -47.864 0.156    1.00 234.31 ? 181  SER F CB  1 
ATOM   16584 O  OG  . SER F  2 71  ? 12.102  -47.969 1.385    1.00 241.93 ? 181  SER F OG  1 
ATOM   16585 N  N   . SER F  2 72  ? 13.344  -50.421 1.673    1.00 246.09 ? 182  SER F N   1 
ATOM   16586 C  CA  . SER F  2 72  ? 12.996  -51.773 2.107    1.00 259.07 ? 182  SER F CA  1 
ATOM   16587 C  C   . SER F  2 72  ? 14.201  -52.707 2.192    1.00 253.01 ? 182  SER F C   1 
ATOM   16588 O  O   . SER F  2 72  ? 14.051  -53.890 2.518    1.00 254.04 ? 182  SER F O   1 
ATOM   16589 C  CB  . SER F  2 72  ? 11.932  -52.375 1.180    1.00 269.27 ? 182  SER F CB  1 
ATOM   16590 O  OG  . SER F  2 72  ? 11.708  -53.746 1.465    1.00 280.70 ? 182  SER F OG  1 
ATOM   16591 N  N   . ILE F  2 73  ? 15.396  -52.199 1.916    1.00 237.47 ? 183  ILE F N   1 
ATOM   16592 C  CA  . ILE F  2 73  ? 16.597  -53.017 2.022    1.00 235.72 ? 183  ILE F CA  1 
ATOM   16593 C  C   . ILE F  2 73  ? 17.192  -52.933 3.438    1.00 243.08 ? 183  ILE F C   1 
ATOM   16594 O  O   . ILE F  2 73  ? 17.402  -53.970 4.074    1.00 243.84 ? 183  ILE F O   1 
ATOM   16595 C  CB  . ILE F  2 73  ? 17.636  -52.625 0.949    1.00 226.94 ? 183  ILE F CB  1 
ATOM   16596 C  CG1 . ILE F  2 73  ? 17.018  -52.696 -0.449   1.00 222.72 ? 183  ILE F CG1 1 
ATOM   16597 C  CG2 . ILE F  2 73  ? 18.862  -53.517 1.054    1.00 242.78 ? 183  ILE F CG2 1 
ATOM   16598 C  CD1 . ILE F  2 73  ? 17.942  -52.221 -1.549   1.00 214.61 ? 183  ILE F CD1 1 
ATOM   16599 N  N   . PRO F  2 74  ? 17.453  -51.710 3.954    1.00 258.15 ? 184  PRO F N   1 
ATOM   16600 C  CA  . PRO F  2 74  ? 17.364  -50.347 3.402    1.00 253.33 ? 184  PRO F CA  1 
ATOM   16601 C  C   . PRO F  2 74  ? 18.701  -49.823 2.860    1.00 236.46 ? 184  PRO F C   1 
ATOM   16602 O  O   . PRO F  2 74  ? 19.752  -50.307 3.283    1.00 234.37 ? 184  PRO F O   1 
ATOM   16603 C  CB  . PRO F  2 74  ? 16.912  -49.528 4.609    1.00 262.24 ? 184  PRO F CB  1 
ATOM   16604 C  CG  . PRO F  2 74  ? 17.592  -50.204 5.760    1.00 267.39 ? 184  PRO F CG  1 
ATOM   16605 C  CD  . PRO F  2 74  ? 17.705  -51.677 5.407    1.00 267.64 ? 184  PRO F CD  1 
ATOM   16606 N  N   . TYR F  2 75  ? 18.658  -48.851 1.948    1.00 224.47 ? 185  TYR F N   1 
ATOM   16607 C  CA  . TYR F  2 75  ? 19.864  -48.229 1.411    1.00 223.41 ? 185  TYR F CA  1 
ATOM   16608 C  C   . TYR F  2 75  ? 19.484  -46.935 0.708    1.00 228.41 ? 185  TYR F C   1 
ATOM   16609 O  O   . TYR F  2 75  ? 18.360  -46.786 0.218    1.00 224.21 ? 185  TYR F O   1 
ATOM   16610 C  CB  . TYR F  2 75  ? 20.606  -49.162 0.440    1.00 220.31 ? 185  TYR F CB  1 
ATOM   16611 C  CG  . TYR F  2 75  ? 21.941  -48.629 -0.052   1.00 217.14 ? 185  TYR F CG  1 
ATOM   16612 C  CD1 . TYR F  2 75  ? 23.028  -48.520 0.808    1.00 219.14 ? 185  TYR F CD1 1 
ATOM   16613 C  CD2 . TYR F  2 75  ? 22.122  -48.260 -1.380   1.00 212.01 ? 185  TYR F CD2 1 
ATOM   16614 C  CE1 . TYR F  2 75  ? 24.250  -48.042 0.365    1.00 218.29 ? 185  TYR F CE1 1 
ATOM   16615 C  CE2 . TYR F  2 75  ? 23.342  -47.785 -1.834   1.00 206.30 ? 185  TYR F CE2 1 
ATOM   16616 C  CZ  . TYR F  2 75  ? 24.400  -47.677 -0.958   1.00 207.00 ? 185  TYR F CZ  1 
ATOM   16617 O  OH  . TYR F  2 75  ? 25.611  -47.204 -1.413   1.00 195.25 ? 185  TYR F OH  1 
ATOM   16618 N  N   . PHE F  2 76  ? 20.427  -46.001 0.676    1.00 234.37 ? 186  PHE F N   1 
ATOM   16619 C  CA  . PHE F  2 76  ? 20.248  -44.717 0.012    1.00 229.52 ? 186  PHE F CA  1 
ATOM   16620 C  C   . PHE F  2 76  ? 20.874  -44.787 -1.378   1.00 222.62 ? 186  PHE F C   1 
ATOM   16621 O  O   . PHE F  2 76  ? 22.077  -45.040 -1.507   1.00 218.46 ? 186  PHE F O   1 
ATOM   16622 C  CB  . PHE F  2 76  ? 20.876  -43.593 0.835    1.00 238.63 ? 186  PHE F CB  1 
ATOM   16623 C  CG  . PHE F  2 76  ? 20.705  -42.231 0.228    1.00 250.61 ? 186  PHE F CG  1 
ATOM   16624 C  CD1 . PHE F  2 76  ? 19.529  -41.524 0.406    1.00 252.34 ? 186  PHE F CD1 1 
ATOM   16625 C  CD2 . PHE F  2 76  ? 21.719  -41.659 -0.523   1.00 254.62 ? 186  PHE F CD2 1 
ATOM   16626 C  CE1 . PHE F  2 76  ? 19.366  -40.271 -0.155   1.00 255.60 ? 186  PHE F CE1 1 
ATOM   16627 C  CE2 . PHE F  2 76  ? 21.564  -40.407 -1.087   1.00 251.54 ? 186  PHE F CE2 1 
ATOM   16628 C  CZ  . PHE F  2 76  ? 20.385  -39.712 -0.903   1.00 251.62 ? 186  PHE F CZ  1 
ATOM   16629 N  N   . CYS F  2 77  ? 20.063  -44.577 -2.413   1.00 219.99 ? 187  CYS F N   1 
ATOM   16630 C  CA  . CYS F  2 77  ? 20.573  -44.552 -3.775   1.00 217.75 ? 187  CYS F CA  1 
ATOM   16631 C  C   . CYS F  2 77  ? 19.803  -43.525 -4.594   1.00 212.81 ? 187  CYS F C   1 
ATOM   16632 O  O   . CYS F  2 77  ? 18.755  -43.020 -4.183   1.00 222.53 ? 187  CYS F O   1 
ATOM   16633 C  CB  . CYS F  2 77  ? 20.503  -45.932 -4.430   1.00 230.25 ? 187  CYS F CB  1 
ATOM   16634 S  SG  . CYS F  2 77  ? 18.856  -46.604 -4.617   1.00 276.43 ? 187  CYS F SG  1 
ATOM   16635 N  N   . LEU F  2 78  ? 20.352  -43.216 -5.766   1.00 202.87 ? 188  LEU F N   1 
ATOM   16636 C  CA  . LEU F  2 78  ? 19.757  -42.242 -6.668   1.00 213.66 ? 188  LEU F CA  1 
ATOM   16637 C  C   . LEU F  2 78  ? 18.394  -42.716 -7.181   1.00 220.49 ? 188  LEU F C   1 
ATOM   16638 O  O   . LEU F  2 78  ? 18.148  -43.921 -7.299   1.00 222.50 ? 188  LEU F O   1 
ATOM   16639 C  CB  . LEU F  2 78  ? 20.700  -41.993 -7.842   1.00 212.51 ? 188  LEU F CB  1 
ATOM   16640 C  CG  . LEU F  2 78  ? 22.147  -41.658 -7.471   1.00 199.46 ? 188  LEU F CG  1 
ATOM   16641 C  CD1 . LEU F  2 78  ? 22.966  -41.367 -8.720   1.00 192.69 ? 188  LEU F CD1 1 
ATOM   16642 C  CD2 . LEU F  2 78  ? 22.221  -40.499 -6.487   1.00 200.30 ? 188  LEU F CD2 1 
ATOM   16643 N  N   . PRO F  2 79  ? 17.485  -41.786 -7.486   1.00 210.83 ? 189  PRO F N   1 
ATOM   16644 C  CA  . PRO F  2 79  ? 16.194  -42.167 -8.072   1.00 207.73 ? 189  PRO F CA  1 
ATOM   16645 C  C   . PRO F  2 79  ? 16.377  -42.771 -9.456   1.00 216.86 ? 189  PRO F C   1 
ATOM   16646 O  O   . PRO F  2 79  ? 17.434  -42.674 -10.080  1.00 230.24 ? 189  PRO F O   1 
ATOM   16647 C  CB  . PRO F  2 79  ? 15.426  -40.843 -8.141   1.00 206.73 ? 189  PRO F CB  1 
ATOM   16648 C  CG  . PRO F  2 79  ? 16.488  -39.795 -8.174   1.00 205.12 ? 189  PRO F CG  1 
ATOM   16649 C  CD  . PRO F  2 79  ? 17.595  -40.327 -7.309   1.00 207.64 ? 189  PRO F CD  1 
ATOM   16650 N  N   . THR F  2 80  ? 15.309  -43.395 -9.944   1.00 206.07 ? 190  THR F N   1 
ATOM   16651 C  CA  . THR F  2 80  ? 15.345  -44.062 -11.238  1.00 205.67 ? 190  THR F CA  1 
ATOM   16652 C  C   . THR F  2 80  ? 15.201  -43.048 -12.366  1.00 207.62 ? 190  THR F C   1 
ATOM   16653 O  O   . THR F  2 80  ? 14.275  -42.232 -12.365  1.00 219.53 ? 190  THR F O   1 
ATOM   16654 C  CB  . THR F  2 80  ? 14.235  -45.106 -11.326  1.00 212.41 ? 190  THR F CB  1 
ATOM   16655 O  OG1 . THR F  2 80  ? 14.316  -45.986 -10.198  1.00 222.32 ? 190  THR F OG1 1 
ATOM   16656 C  CG2 . THR F  2 80  ? 14.369  -45.912 -12.607  1.00 215.50 ? 190  THR F CG2 1 
ATOM   16657 N  N   . PHE F  2 81  ? 16.127  -43.092 -13.323  1.00 212.97 ? 191  PHE F N   1 
ATOM   16658 C  CA  . PHE F  2 81  ? 16.091  -42.211 -14.481  1.00 214.18 ? 191  PHE F CA  1 
ATOM   16659 C  C   . PHE F  2 81  ? 16.413  -42.998 -15.743  1.00 219.70 ? 191  PHE F C   1 
ATOM   16660 O  O   . PHE F  2 81  ? 17.153  -43.984 -15.709  1.00 219.33 ? 191  PHE F O   1 
ATOM   16661 C  CB  . PHE F  2 81  ? 17.058  -41.033 -14.314  1.00 221.39 ? 191  PHE F CB  1 
ATOM   16662 C  CG  . PHE F  2 81  ? 18.478  -41.443 -14.050  1.00 215.97 ? 191  PHE F CG  1 
ATOM   16663 C  CD1 . PHE F  2 81  ? 19.354  -41.691 -15.093  1.00 213.29 ? 191  PHE F CD1 1 
ATOM   16664 C  CD2 . PHE F  2 81  ? 18.941  -41.568 -12.750  1.00 216.44 ? 191  PHE F CD2 1 
ATOM   16665 C  CE1 . PHE F  2 81  ? 20.663  -42.063 -14.844  1.00 211.72 ? 191  PHE F CE1 1 
ATOM   16666 C  CE2 . PHE F  2 81  ? 20.249  -41.938 -12.493  1.00 209.48 ? 191  PHE F CE2 1 
ATOM   16667 C  CZ  . PHE F  2 81  ? 21.111  -42.186 -13.541  1.00 209.76 ? 191  PHE F CZ  1 
ATOM   16668 N  N   . GLY F  2 82  ? 15.845  -42.550 -16.862  1.00 229.75 ? 192  GLY F N   1 
ATOM   16669 C  CA  . GLY F  2 82  ? 16.050  -43.206 -18.140  1.00 227.25 ? 192  GLY F CA  1 
ATOM   16670 C  C   . GLY F  2 82  ? 17.475  -43.151 -18.651  1.00 218.06 ? 192  GLY F C   1 
ATOM   16671 O  O   . GLY F  2 82  ? 18.134  -44.188 -18.773  1.00 212.82 ? 192  GLY F O   1 
ATOM   16672 N  N   . PHE F  2 83  ? 17.962  -41.947 -18.954  1.00 220.56 ? 193  PHE F N   1 
ATOM   16673 C  CA  . PHE F  2 83  ? 19.320  -41.776 -19.456  1.00 213.05 ? 193  PHE F CA  1 
ATOM   16674 C  C   . PHE F  2 83  ? 19.763  -40.338 -19.244  1.00 213.62 ? 193  PHE F C   1 
ATOM   16675 O  O   . PHE F  2 83  ? 19.040  -39.403 -19.603  1.00 211.25 ? 193  PHE F O   1 
ATOM   16676 C  CB  . PHE F  2 83  ? 19.422  -42.134 -20.939  1.00 219.60 ? 193  PHE F CB  1 
ATOM   16677 C  CG  . PHE F  2 83  ? 20.604  -41.511 -21.628  1.00 222.00 ? 193  PHE F CG  1 
ATOM   16678 C  CD1 . PHE F  2 83  ? 21.892  -41.934 -21.341  1.00 221.04 ? 193  PHE F CD1 1 
ATOM   16679 C  CD2 . PHE F  2 83  ? 20.428  -40.502 -22.560  1.00 229.13 ? 193  PHE F CD2 1 
ATOM   16680 C  CE1 . PHE F  2 83  ? 22.981  -41.367 -21.971  1.00 219.55 ? 193  PHE F CE1 1 
ATOM   16681 C  CE2 . PHE F  2 83  ? 21.515  -39.930 -23.194  1.00 234.72 ? 193  PHE F CE2 1 
ATOM   16682 C  CZ  . PHE F  2 83  ? 22.793  -40.364 -22.898  1.00 226.06 ? 193  PHE F CZ  1 
ATOM   16683 N  N   . LYS F  2 84  ? 20.957  -40.170 -18.681  1.00 227.08 ? 194  LYS F N   1 
ATOM   16684 C  CA  . LYS F  2 84  ? 21.544  -38.860 -18.432  1.00 233.56 ? 194  LYS F CA  1 
ATOM   16685 C  C   . LYS F  2 84  ? 22.860  -38.751 -19.187  1.00 226.92 ? 194  LYS F C   1 
ATOM   16686 O  O   . LYS F  2 84  ? 23.763  -39.571 -18.989  1.00 221.81 ? 194  LYS F O   1 
ATOM   16687 C  CB  . LYS F  2 84  ? 21.769  -38.636 -16.936  1.00 236.35 ? 194  LYS F CB  1 
ATOM   16688 C  CG  . LYS F  2 84  ? 20.491  -38.484 -16.134  1.00 245.98 ? 194  LYS F CG  1 
ATOM   16689 C  CD  . LYS F  2 84  ? 20.791  -38.197 -14.672  1.00 253.14 ? 194  LYS F CD  1 
ATOM   16690 C  CE  . LYS F  2 84  ? 19.510  -37.994 -13.875  1.00 269.13 ? 194  LYS F CE  1 
ATOM   16691 N  NZ  . LYS F  2 84  ? 19.773  -37.685 -12.440  1.00 277.28 ? 194  LYS F NZ  1 
ATOM   16692 N  N   . HIS F  2 85  ? 22.963  -37.748 -20.055  1.00 222.29 ? 195  HIS F N   1 
ATOM   16693 C  CA  . HIS F  2 85  ? 24.217  -37.430 -20.730  1.00 220.27 ? 195  HIS F CA  1 
ATOM   16694 C  C   . HIS F  2 85  ? 25.024  -36.501 -19.828  1.00 222.01 ? 195  HIS F C   1 
ATOM   16695 O  O   . HIS F  2 85  ? 24.674  -35.328 -19.659  1.00 213.97 ? 195  HIS F O   1 
ATOM   16696 C  CB  . HIS F  2 85  ? 23.957  -36.797 -22.094  1.00 221.36 ? 195  HIS F CB  1 
ATOM   16697 C  CG  . HIS F  2 85  ? 25.201  -36.336 -22.788  1.00 221.07 ? 195  HIS F CG  1 
ATOM   16698 N  ND1 . HIS F  2 85  ? 26.261  -37.177 -23.053  1.00 212.01 ? 195  HIS F ND1 1 
ATOM   16699 C  CD2 . HIS F  2 85  ? 25.558  -35.120 -23.264  1.00 232.29 ? 195  HIS F CD2 1 
ATOM   16700 C  CE1 . HIS F  2 85  ? 27.216  -36.500 -23.664  1.00 213.24 ? 195  HIS F CE1 1 
ATOM   16701 N  NE2 . HIS F  2 85  ? 26.815  -35.250 -23.806  1.00 226.14 ? 195  HIS F NE2 1 
ATOM   16702 N  N   . ILE F  2 86  ? 26.094  -37.026 -19.235  1.00 232.33 ? 196  ILE F N   1 
ATOM   16703 C  CA  . ILE F  2 86  ? 26.865  -36.270 -18.254  1.00 233.32 ? 196  ILE F CA  1 
ATOM   16704 C  C   . ILE F  2 86  ? 28.019  -35.539 -18.928  1.00 228.39 ? 196  ILE F C   1 
ATOM   16705 O  O   . ILE F  2 86  ? 28.111  -34.308 -18.854  1.00 225.47 ? 196  ILE F O   1 
ATOM   16706 C  CB  . ILE F  2 86  ? 27.377  -37.188 -17.129  1.00 221.04 ? 196  ILE F CB  1 
ATOM   16707 C  CG1 . ILE F  2 86  ? 26.205  -37.910 -16.461  1.00 222.80 ? 196  ILE F CG1 1 
ATOM   16708 C  CG2 . ILE F  2 86  ? 28.164  -36.387 -16.104  1.00 214.03 ? 196  ILE F CG2 1 
ATOM   16709 C  CD1 . ILE F  2 86  ? 26.599  -38.760 -15.275  1.00 215.35 ? 196  ILE F CD1 1 
ATOM   16710 N  N   . LEU F  2 87  ? 28.894  -36.282 -19.596  1.00 221.00 ? 197  LEU F N   1 
ATOM   16711 C  CA  . LEU F  2 87  ? 30.127  -35.720 -20.153  1.00 222.34 ? 197  LEU F CA  1 
ATOM   16712 C  C   . LEU F  2 87  ? 30.157  -35.791 -21.675  1.00 215.70 ? 197  LEU F C   1 
ATOM   16713 O  O   . LEU F  2 87  ? 30.257  -36.897 -22.238  1.00 211.98 ? 197  LEU F O   1 
ATOM   16714 C  CB  . LEU F  2 87  ? 31.344  -36.440 -19.570  1.00 221.66 ? 197  LEU F CB  1 
ATOM   16715 C  CG  . LEU F  2 87  ? 32.712  -35.953 -20.055  1.00 227.73 ? 197  LEU F CG  1 
ATOM   16716 C  CD1 . LEU F  2 87  ? 32.917  -34.503 -19.660  1.00 248.32 ? 197  LEU F CD1 1 
ATOM   16717 C  CD2 . LEU F  2 87  ? 33.828  -36.823 -19.496  1.00 214.63 ? 197  LEU F CD2 1 
ATOM   16718 N  N   . PRO F  2 88  ? 30.060  -34.662 -22.378  1.00 211.57 ? 198  PRO F N   1 
ATOM   16719 C  CA  . PRO F  2 88  ? 30.356  -34.659 -23.815  1.00 202.29 ? 198  PRO F CA  1 
ATOM   16720 C  C   . PRO F  2 88  ? 31.822  -34.981 -24.055  1.00 204.45 ? 198  PRO F C   1 
ATOM   16721 O  O   . PRO F  2 88  ? 32.699  -34.572 -23.290  1.00 202.78 ? 198  PRO F O   1 
ATOM   16722 C  CB  . PRO F  2 88  ? 30.015  -33.228 -24.247  1.00 210.87 ? 198  PRO F CB  1 
ATOM   16723 C  CG  . PRO F  2 88  ? 29.088  -32.717 -23.189  1.00 224.47 ? 198  PRO F CG  1 
ATOM   16724 C  CD  . PRO F  2 88  ? 29.558  -33.359 -21.915  1.00 226.63 ? 198  PRO F CD  1 
ATOM   16725 N  N   . LEU F  2 89  ? 32.087  -35.720 -25.131  1.00 191.51 ? 199  LEU F N   1 
ATOM   16726 C  CA  . LEU F  2 89  ? 33.435  -36.221 -25.368  1.00 192.62 ? 199  LEU F CA  1 
ATOM   16727 C  C   . LEU F  2 89  ? 34.407  -35.072 -25.604  1.00 191.80 ? 199  LEU F C   1 
ATOM   16728 O  O   . LEU F  2 89  ? 34.186  -34.218 -26.466  1.00 195.53 ? 199  LEU F O   1 
ATOM   16729 C  CB  . LEU F  2 89  ? 33.439  -37.200 -26.545  1.00 197.72 ? 199  LEU F CB  1 
ATOM   16730 C  CG  . LEU F  2 89  ? 32.993  -36.773 -27.942  1.00 204.48 ? 199  LEU F CG  1 
ATOM   16731 C  CD1 . LEU F  2 89  ? 34.209  -36.434 -28.791  1.00 211.02 ? 199  LEU F CD1 1 
ATOM   16732 C  CD2 . LEU F  2 89  ? 32.156  -37.865 -28.600  1.00 209.63 ? 199  LEU F CD2 1 
ATOM   16733 N  N   . THR F  2 90  ? 35.478  -35.047 -24.813  1.00 202.46 ? 200  THR F N   1 
ATOM   16734 C  CA  . THR F  2 90  ? 36.471  -33.986 -24.879  1.00 211.41 ? 200  THR F CA  1 
ATOM   16735 C  C   . THR F  2 90  ? 37.841  -34.575 -24.573  1.00 213.25 ? 200  THR F C   1 
ATOM   16736 O  O   . THR F  2 90  ? 37.963  -35.715 -24.115  1.00 191.92 ? 200  THR F O   1 
ATOM   16737 C  CB  . THR F  2 90  ? 36.140  -32.844 -23.910  1.00 208.39 ? 200  THR F CB  1 
ATOM   16738 O  OG1 . THR F  2 90  ? 37.120  -31.807 -24.038  1.00 213.51 ? 200  THR F OG1 1 
ATOM   16739 C  CG2 . THR F  2 90  ? 36.128  -33.351 -22.481  1.00 198.45 ? 200  THR F CG2 1 
ATOM   16740 N  N   . ASN F  2 91  ? 38.881  -33.773 -24.824  1.00 239.18 ? 201  ASN F N   1 
ATOM   16741 C  CA  . ASN F  2 91  ? 40.243  -34.239 -24.584  1.00 235.83 ? 201  ASN F CA  1 
ATOM   16742 C  C   . ASN F  2 91  ? 40.542  -34.365 -23.099  1.00 236.08 ? 201  ASN F C   1 
ATOM   16743 O  O   . ASN F  2 91  ? 41.298  -35.259 -22.698  1.00 219.26 ? 201  ASN F O   1 
ATOM   16744 C  CB  . ASN F  2 91  ? 41.258  -33.287 -25.221  1.00 233.16 ? 201  ASN F CB  1 
ATOM   16745 C  CG  . ASN F  2 91  ? 41.214  -33.309 -26.731  1.00 223.85 ? 201  ASN F CG  1 
ATOM   16746 O  OD1 . ASN F  2 91  ? 40.428  -32.593 -27.349  1.00 222.64 ? 201  ASN F OD1 1 
ATOM   16747 N  ND2 . ASN F  2 91  ? 42.068  -34.126 -27.336  1.00 214.11 ? 201  ASN F ND2 1 
ATOM   16748 N  N   . ASP F  2 92  ? 39.955  -33.494 -22.276  1.00 251.47 ? 202  ASP F N   1 
ATOM   16749 C  CA  . ASP F  2 92  ? 40.187  -33.521 -20.839  1.00 248.15 ? 202  ASP F CA  1 
ATOM   16750 C  C   . ASP F  2 92  ? 39.834  -34.892 -20.280  1.00 234.66 ? 202  ASP F C   1 
ATOM   16751 O  O   . ASP F  2 92  ? 38.657  -35.216 -20.096  1.00 233.42 ? 202  ASP F O   1 
ATOM   16752 C  CB  . ASP F  2 92  ? 39.379  -32.420 -20.140  1.00 242.03 ? 202  ASP F CB  1 
ATOM   16753 C  CG  . ASP F  2 92  ? 39.925  -32.078 -18.759  1.00 237.37 ? 202  ASP F CG  1 
ATOM   16754 O  OD1 . ASP F  2 92  ? 41.091  -32.420 -18.472  1.00 241.81 ? 202  ASP F OD1 1 
ATOM   16755 O  OD2 . ASP F  2 92  ? 39.192  -31.453 -17.961  1.00 227.83 ? 202  ASP F OD2 1 
ATOM   16756 N  N   . ALA F  2 93  ? 40.854  -35.704 -20.014  1.00 213.55 ? 203  ALA F N   1 
ATOM   16757 C  CA  . ALA F  2 93  ? 40.652  -37.082 -19.602  1.00 197.43 ? 203  ALA F CA  1 
ATOM   16758 C  C   . ALA F  2 93  ? 40.644  -37.233 -18.091  1.00 199.68 ? 203  ALA F C   1 
ATOM   16759 O  O   . ALA F  2 93  ? 40.092  -38.214 -17.582  1.00 201.99 ? 203  ALA F O   1 
ATOM   16760 C  CB  . ALA F  2 93  ? 41.735  -37.985 -20.212  1.00 190.41 ? 203  ALA F CB  1 
ATOM   16761 N  N   . GLU F  2 94  ? 41.220  -36.271 -17.371  1.00 207.89 ? 204  GLU F N   1 
ATOM   16762 C  CA  . GLU F  2 94  ? 41.176  -36.298 -15.918  1.00 209.66 ? 204  GLU F CA  1 
ATOM   16763 C  C   . GLU F  2 94  ? 39.833  -35.830 -15.391  1.00 215.65 ? 204  GLU F C   1 
ATOM   16764 O  O   . GLU F  2 94  ? 39.479  -36.146 -14.251  1.00 218.05 ? 204  GLU F O   1 
ATOM   16765 C  CB  . GLU F  2 94  ? 42.288  -35.417 -15.344  1.00 211.92 ? 204  GLU F CB  1 
ATOM   16766 C  CG  . GLU F  2 94  ? 43.686  -35.927 -15.634  1.00 209.66 ? 204  GLU F CG  1 
ATOM   16767 C  CD  . GLU F  2 94  ? 43.924  -37.310 -15.079  1.00 214.54 ? 204  GLU F CD  1 
ATOM   16768 O  OE1 . GLU F  2 94  ? 43.428  -37.600 -13.969  1.00 213.96 ? 204  GLU F OE1 1 
ATOM   16769 O  OE2 . GLU F  2 94  ? 44.601  -38.111 -15.757  1.00 221.22 ? 204  GLU F OE2 1 
ATOM   16770 N  N   . ARG F  2 95  ? 39.075  -35.100 -16.209  1.00 211.87 ? 205  ARG F N   1 
ATOM   16771 C  CA  . ARG F  2 95  ? 37.696  -34.789 -15.868  1.00 209.43 ? 205  ARG F CA  1 
ATOM   16772 C  C   . ARG F  2 95  ? 36.821  -36.020 -16.020  1.00 206.23 ? 205  ARG F C   1 
ATOM   16773 O  O   . ARG F  2 95  ? 35.836  -36.178 -15.292  1.00 216.17 ? 205  ARG F O   1 
ATOM   16774 C  CB  . ARG F  2 95  ? 37.185  -33.655 -16.755  1.00 215.54 ? 205  ARG F CB  1 
ATOM   16775 C  CG  . ARG F  2 95  ? 35.808  -33.140 -16.395  1.00 213.08 ? 205  ARG F CG  1 
ATOM   16776 C  CD  . ARG F  2 95  ? 35.756  -32.644 -14.970  1.00 210.96 ? 205  ARG F CD  1 
ATOM   16777 N  NE  . ARG F  2 95  ? 34.414  -32.192 -14.633  1.00 213.14 ? 205  ARG F NE  1 
ATOM   16778 C  CZ  . ARG F  2 95  ? 33.973  -30.958 -14.850  1.00 220.64 ? 205  ARG F CZ  1 
ATOM   16779 N  NH1 . ARG F  2 95  ? 34.769  -30.054 -15.408  1.00 227.86 ? 205  ARG F NH1 1 
ATOM   16780 N  NH2 . ARG F  2 95  ? 32.735  -30.630 -14.513  1.00 217.88 ? 205  ARG F NH2 1 
ATOM   16781 N  N   . PHE F  2 96  ? 37.169  -36.893 -16.965  1.00 191.97 ? 206  PHE F N   1 
ATOM   16782 C  CA  . PHE F  2 96  ? 36.454  -38.152 -17.130  1.00 191.68 ? 206  PHE F CA  1 
ATOM   16783 C  C   . PHE F  2 96  ? 36.578  -39.011 -15.883  1.00 194.18 ? 206  PHE F C   1 
ATOM   16784 O  O   . PHE F  2 96  ? 35.589  -39.571 -15.400  1.00 193.41 ? 206  PHE F O   1 
ATOM   16785 C  CB  . PHE F  2 96  ? 36.999  -38.892 -18.351  1.00 192.50 ? 206  PHE F CB  1 
ATOM   16786 C  CG  . PHE F  2 96  ? 36.529  -40.313 -18.465  1.00 199.90 ? 206  PHE F CG  1 
ATOM   16787 C  CD1 . PHE F  2 96  ? 35.285  -40.607 -18.995  1.00 208.93 ? 206  PHE F CD1 1 
ATOM   16788 C  CD2 . PHE F  2 96  ? 37.341  -41.359 -18.050  1.00 195.97 ? 206  PHE F CD2 1 
ATOM   16789 C  CE1 . PHE F  2 96  ? 34.855  -41.919 -19.107  1.00 202.98 ? 206  PHE F CE1 1 
ATOM   16790 C  CE2 . PHE F  2 96  ? 36.916  -42.672 -18.158  1.00 191.38 ? 206  PHE F CE2 1 
ATOM   16791 C  CZ  . PHE F  2 96  ? 35.672  -42.951 -18.688  1.00 194.40 ? 206  PHE F CZ  1 
ATOM   16792 N  N   . ASN F  2 97  ? 37.796  -39.130 -15.351  1.00 194.90 ? 207  ASN F N   1 
ATOM   16793 C  CA  . ASN F  2 97  ? 38.009  -39.961 -14.172  1.00 199.06 ? 207  ASN F CA  1 
ATOM   16794 C  C   . ASN F  2 97  ? 37.239  -39.424 -12.976  1.00 206.45 ? 207  ASN F C   1 
ATOM   16795 O  O   . ASN F  2 97  ? 36.649  -40.196 -12.212  1.00 213.95 ? 207  ASN F O   1 
ATOM   16796 C  CB  . ASN F  2 97  ? 39.498  -40.043 -13.854  1.00 198.11 ? 207  ASN F CB  1 
ATOM   16797 C  CG  . ASN F  2 97  ? 40.275  -40.772 -14.922  1.00 204.73 ? 207  ASN F CG  1 
ATOM   16798 O  OD1 . ASN F  2 97  ? 39.724  -41.597 -15.648  1.00 213.20 ? 207  ASN F OD1 1 
ATOM   16799 N  ND2 . ASN F  2 97  ? 41.563  -40.468 -15.029  1.00 214.08 ? 207  ASN F ND2 1 
ATOM   16800 N  N   . GLU F  2 98  ? 37.232  -38.099 -12.802  1.00 224.72 ? 208  GLU F N   1 
ATOM   16801 C  CA  . GLU F  2 98  ? 36.562  -37.479 -11.664  1.00 233.92 ? 208  GLU F CA  1 
ATOM   16802 C  C   . GLU F  2 98  ? 35.061  -37.741 -11.656  1.00 230.44 ? 208  GLU F C   1 
ATOM   16803 O  O   . GLU F  2 98  ? 34.423  -37.606 -10.605  1.00 227.26 ? 208  GLU F O   1 
ATOM   16804 C  CB  . GLU F  2 98  ? 36.823  -35.972 -11.680  1.00 234.89 ? 208  GLU F CB  1 
ATOM   16805 C  CG  . GLU F  2 98  ? 38.265  -35.583 -11.415  1.00 229.51 ? 208  GLU F CG  1 
ATOM   16806 C  CD  . GLU F  2 98  ? 38.577  -34.166 -11.866  1.00 226.77 ? 208  GLU F CD  1 
ATOM   16807 O  OE1 . GLU F  2 98  ? 37.631  -33.413 -12.190  1.00 216.37 ? 208  GLU F OE1 1 
ATOM   16808 O  OE2 . GLU F  2 98  ? 39.771  -33.806 -11.905  1.00 231.41 ? 208  GLU F OE2 1 
ATOM   16809 N  N   . ILE F  2 99  ? 34.486  -38.111 -12.796  1.00 223.74 ? 209  ILE F N   1 
ATOM   16810 C  CA  . ILE F  2 99  ? 33.058  -38.397 -12.879  1.00 209.98 ? 209  ILE F CA  1 
ATOM   16811 C  C   . ILE F  2 99  ? 32.760  -39.835 -12.484  1.00 196.60 ? 209  ILE F C   1 
ATOM   16812 O  O   . ILE F  2 99  ? 31.792  -40.101 -11.766  1.00 191.33 ? 209  ILE F O   1 
ATOM   16813 C  CB  . ILE F  2 99  ? 32.552  -38.087 -14.301  1.00 202.59 ? 209  ILE F CB  1 
ATOM   16814 C  CG1 . ILE F  2 99  ? 32.731  -36.601 -14.613  1.00 198.94 ? 209  ILE F CG1 1 
ATOM   16815 C  CG2 . ILE F  2 99  ? 31.095  -38.502 -14.450  1.00 208.16 ? 209  ILE F CG2 1 
ATOM   16816 C  CD1 . ILE F  2 99  ? 32.423  -36.242 -16.043  1.00 197.67 ? 209  ILE F CD1 1 
ATOM   16817 N  N   . VAL F  2 100 ? 33.587  -40.774 -12.946  1.00 188.12 ? 210  VAL F N   1 
ATOM   16818 C  CA  . VAL F  2 100 ? 33.366  -42.186 -12.651  1.00 186.50 ? 210  VAL F CA  1 
ATOM   16819 C  C   . VAL F  2 100 ? 33.514  -42.463 -11.161  1.00 181.54 ? 210  VAL F C   1 
ATOM   16820 O  O   . VAL F  2 100 ? 32.814  -43.321 -10.609  1.00 178.18 ? 210  VAL F O   1 
ATOM   16821 C  CB  . VAL F  2 100 ? 34.335  -43.042 -13.488  1.00 190.57 ? 210  VAL F CB  1 
ATOM   16822 C  CG1 . VAL F  2 100 ? 33.971  -44.514 -13.399  1.00 198.12 ? 210  VAL F CG1 1 
ATOM   16823 C  CG2 . VAL F  2 100 ? 34.343  -42.573 -14.937  1.00 189.75 ? 210  VAL F CG2 1 
ATOM   16824 N  N   . LYS F  2 101 ? 34.395  -41.727 -10.480  1.00 198.50 ? 211  LYS F N   1 
ATOM   16825 C  CA  . LYS F  2 101 ? 34.627  -41.972 -9.061   1.00 208.07 ? 211  LYS F CA  1 
ATOM   16826 C  C   . LYS F  2 101 ? 33.387  -41.657 -8.236   1.00 208.02 ? 211  LYS F C   1 
ATOM   16827 O  O   . LYS F  2 101 ? 33.022  -42.420 -7.334   1.00 214.94 ? 211  LYS F O   1 
ATOM   16828 C  CB  . LYS F  2 101 ? 35.814  -41.138 -8.577   1.00 225.55 ? 211  LYS F CB  1 
ATOM   16829 C  CG  . LYS F  2 101 ? 37.118  -41.408 -9.319   1.00 230.00 ? 211  LYS F CG  1 
ATOM   16830 C  CD  . LYS F  2 101 ? 38.078  -40.229 -9.186   1.00 242.53 ? 211  LYS F CD  1 
ATOM   16831 C  CE  . LYS F  2 101 ? 39.326  -40.404 -10.043  1.00 242.63 ? 211  LYS F CE  1 
ATOM   16832 N  NZ  . LYS F  2 101 ? 40.228  -39.218 -9.956   1.00 239.77 ? 211  LYS F NZ  1 
ATOM   16833 N  N   . ASN F  2 102 ? 32.711  -40.557 -8.548   1.00 200.12 ? 212  ASN F N   1 
ATOM   16834 C  CA  . ASN F  2 102 ? 31.597  -40.092 -7.736   1.00 211.27 ? 212  ASN F CA  1 
ATOM   16835 C  C   . ASN F  2 102 ? 30.293  -40.806 -8.054   1.00 202.67 ? 212  ASN F C   1 
ATOM   16836 O  O   . ASN F  2 102 ? 29.268  -40.489 -7.441   1.00 209.19 ? 212  ASN F O   1 
ATOM   16837 C  CB  . ASN F  2 102 ? 31.412  -38.586 -7.928   1.00 226.79 ? 212  ASN F CB  1 
ATOM   16838 C  CG  . ASN F  2 102 ? 32.702  -37.818 -7.747   1.00 230.41 ? 212  ASN F CG  1 
ATOM   16839 O  OD1 . ASN F  2 102 ? 33.789  -38.400 -7.756   1.00 225.07 ? 212  ASN F OD1 1 
ATOM   16840 N  ND2 . ASN F  2 102 ? 32.593  -36.501 -7.599   1.00 234.97 ? 212  ASN F ND2 1 
ATOM   16841 N  N   . GLN F  2 103 ? 30.302  -41.747 -8.993   1.00 187.01 ? 213  GLN F N   1 
ATOM   16842 C  CA  . GLN F  2 103 ? 29.072  -42.409 -9.400   1.00 184.06 ? 213  GLN F CA  1 
ATOM   16843 C  C   . GLN F  2 103 ? 28.525  -43.301 -8.291   1.00 183.49 ? 213  GLN F C   1 
ATOM   16844 O  O   . GLN F  2 103 ? 29.239  -44.145 -7.739   1.00 184.10 ? 213  GLN F O   1 
ATOM   16845 C  CB  . GLN F  2 103 ? 29.306  -43.214 -10.677  1.00 184.00 ? 213  GLN F CB  1 
ATOM   16846 C  CG  . GLN F  2 103 ? 29.515  -42.348 -11.918  1.00 186.04 ? 213  GLN F CG  1 
ATOM   16847 C  CD  . GLN F  2 103 ? 28.300  -41.499 -12.269  1.00 199.93 ? 213  GLN F CD  1 
ATOM   16848 O  OE1 . GLN F  2 103 ? 27.164  -41.837 -11.931  1.00 201.83 ? 213  GLN F OE1 1 
ATOM   16849 N  NE2 . GLN F  2 103 ? 28.541  -40.386 -12.951  1.00 205.80 ? 213  GLN F NE2 1 
ATOM   16850 N  N   . LYS F  2 104 ? 27.258  -43.089 -7.953   1.00 194.25 ? 214  LYS F N   1 
ATOM   16851 C  CA  . LYS F  2 104 ? 26.534  -43.899 -6.985   1.00 204.43 ? 214  LYS F CA  1 
ATOM   16852 C  C   . LYS F  2 104 ? 25.551  -44.821 -7.703   1.00 205.73 ? 214  LYS F C   1 
ATOM   16853 O  O   . LYS F  2 104 ? 25.246  -44.653 -8.887   1.00 205.63 ? 214  LYS F O   1 
ATOM   16854 C  CB  . LYS F  2 104 ? 25.799  -43.009 -5.976   1.00 213.05 ? 214  LYS F CB  1 
ATOM   16855 C  CG  . LYS F  2 104 ? 26.703  -42.099 -5.148   1.00 196.43 ? 214  LYS F CG  1 
ATOM   16856 C  CD  . LYS F  2 104 ? 25.902  -41.337 -4.096   1.00 191.24 ? 214  LYS F CD  1 
ATOM   16857 C  CE  . LYS F  2 104 ? 26.755  -40.307 -3.362   1.00 193.27 ? 214  LYS F CE  1 
ATOM   16858 N  NZ  . LYS F  2 104 ? 27.269  -39.240 -4.267   1.00 192.60 ? 214  LYS F NZ  1 
ATOM   16859 N  N   . ILE F  2 105 ? 25.057  -45.810 -6.964   1.00 198.41 ? 215  ILE F N   1 
ATOM   16860 C  CA  . ILE F  2 105 ? 24.134  -46.802 -7.506   1.00 187.32 ? 215  ILE F CA  1 
ATOM   16861 C  C   . ILE F  2 105 ? 22.720  -46.236 -7.523   1.00 192.60 ? 215  ILE F C   1 
ATOM   16862 O  O   . ILE F  2 105 ? 22.359  -45.378 -6.710   1.00 195.36 ? 215  ILE F O   1 
ATOM   16863 C  CB  . ILE F  2 105 ? 24.198  -48.108 -6.690   1.00 180.65 ? 215  ILE F CB  1 
ATOM   16864 C  CG1 . ILE F  2 105 ? 25.641  -48.419 -6.288   1.00 181.17 ? 215  ILE F CG1 1 
ATOM   16865 C  CG2 . ILE F  2 105 ? 23.605  -49.262 -7.484   1.00 180.05 ? 215  ILE F CG2 1 
ATOM   16866 C  CD1 . ILE F  2 105 ? 25.987  -48.007 -4.868   1.00 180.11 ? 215  ILE F CD1 1 
ATOM   16867 N  N   . SER F  2 106 ? 21.923  -46.681 -8.495   1.00 196.67 ? 216  SER F N   1 
ATOM   16868 C  CA  . SER F  2 106 ? 20.489  -46.445 -8.528   1.00 195.44 ? 216  SER F CA  1 
ATOM   16869 C  C   . SER F  2 106 ? 19.767  -47.779 -8.327   1.00 197.42 ? 216  SER F C   1 
ATOM   16870 O  O   . SER F  2 106 ? 20.360  -48.749 -7.830   1.00 195.64 ? 216  SER F O   1 
ATOM   16871 C  CB  . SER F  2 106 ? 20.103  -45.758 -9.835   1.00 192.53 ? 216  SER F CB  1 
ATOM   16872 O  OG  . SER F  2 106 ? 20.788  -44.531 -9.980   1.00 194.19 ? 216  SER F OG  1 
ATOM   16873 N  N   . ALA F  2 107 ? 18.496  -47.835 -8.718   1.00 192.81 ? 217  ALA F N   1 
ATOM   16874 C  CA  . ALA F  2 107 ? 17.744  -49.071 -8.559   1.00 193.10 ? 217  ALA F CA  1 
ATOM   16875 C  C   . ALA F  2 107 ? 16.479  -49.030 -9.402   1.00 199.58 ? 217  ALA F C   1 
ATOM   16876 O  O   . ALA F  2 107 ? 16.066  -47.983 -9.907   1.00 201.78 ? 217  ALA F O   1 
ATOM   16877 C  CB  . ALA F  2 107 ? 17.397  -49.325 -7.091   1.00 196.92 ? 217  ALA F CB  1 
ATOM   16878 N  N   . ASN F  2 108 ? 15.875  -50.205 -9.540   1.00 199.12 ? 218  ASN F N   1 
ATOM   16879 C  CA  . ASN F  2 108 ? 14.567  -50.424 -10.148  1.00 203.85 ? 218  ASN F CA  1 
ATOM   16880 C  C   . ASN F  2 108 ? 14.110  -51.807 -9.692   1.00 208.33 ? 218  ASN F C   1 
ATOM   16881 O  O   . ASN F  2 108 ? 14.617  -52.332 -8.695   1.00 212.57 ? 218  ASN F O   1 
ATOM   16882 C  CB  . ASN F  2 108 ? 14.641  -50.280 -11.675  1.00 205.80 ? 218  ASN F CB  1 
ATOM   16883 C  CG  . ASN F  2 108 ? 15.481  -51.356 -12.311  1.00 211.32 ? 218  ASN F CG  1 
ATOM   16884 O  OD1 . ASN F  2 108 ? 14.960  -52.280 -12.934  1.00 217.60 ? 218  ASN F OD1 1 
ATOM   16885 N  ND2 . ASN F  2 108 ? 16.794  -51.253 -12.148  1.00 211.93 ? 218  ASN F ND2 1 
ATOM   16886 N  N   . ILE F  2 109 ? 13.182  -52.417 -10.423  1.00 212.42 ? 219  ILE F N   1 
ATOM   16887 C  CA  . ILE F  2 109 ? 12.618  -53.704 -10.033  1.00 222.78 ? 219  ILE F CA  1 
ATOM   16888 C  C   . ILE F  2 109 ? 13.032  -54.823 -10.985  1.00 220.74 ? 219  ILE F C   1 
ATOM   16889 O  O   . ILE F  2 109 ? 13.556  -55.851 -10.553  1.00 217.79 ? 219  ILE F O   1 
ATOM   16890 C  CB  . ILE F  2 109 ? 11.079  -53.626 -9.909   1.00 233.79 ? 219  ILE F CB  1 
ATOM   16891 C  CG1 . ILE F  2 109 ? 10.669  -52.402 -9.101   1.00 241.71 ? 219  ILE F CG1 1 
ATOM   16892 C  CG2 . ILE F  2 109 ? 10.549  -54.894 -9.264   1.00 232.48 ? 219  ILE F CG2 1 
ATOM   16893 C  CD1 . ILE F  2 109 ? 9.176   -52.240 -8.990   1.00 243.01 ? 219  ILE F CD1 1 
ATOM   16894 N  N   . ASP F  2 110 ? 12.830  -54.632 -12.283  1.00 222.70 ? 220  ASP F N   1 
ATOM   16895 C  CA  . ASP F  2 110 ? 12.906  -55.727 -13.242  1.00 228.91 ? 220  ASP F CA  1 
ATOM   16896 C  C   . ASP F  2 110 ? 14.305  -55.792 -13.843  1.00 232.06 ? 220  ASP F C   1 
ATOM   16897 O  O   . ASP F  2 110 ? 14.834  -54.778 -14.316  1.00 229.93 ? 220  ASP F O   1 
ATOM   16898 C  CB  . ASP F  2 110 ? 11.843  -55.574 -14.331  1.00 232.62 ? 220  ASP F CB  1 
ATOM   16899 C  CG  . ASP F  2 110 ? 12.140  -54.441 -15.287  1.00 230.71 ? 220  ASP F CG  1 
ATOM   16900 O  OD1 . ASP F  2 110 ? 12.860  -53.500 -14.893  1.00 221.23 ? 220  ASP F OD1 1 
ATOM   16901 O  OD2 . ASP F  2 110 ? 11.638  -54.483 -16.430  1.00 234.78 ? 220  ASP F OD2 1 
ATOM   16902 N  N   . THR F  2 111 ? 14.894  -56.994 -13.802  1.00 231.62 ? 221  THR F N   1 
ATOM   16903 C  CA  . THR F  2 111 ? 16.305  -57.220 -14.121  1.00 226.15 ? 221  THR F CA  1 
ATOM   16904 C  C   . THR F  2 111 ? 16.781  -56.592 -15.430  1.00 219.11 ? 221  THR F C   1 
ATOM   16905 O  O   . THR F  2 111 ? 17.857  -55.977 -15.427  1.00 210.18 ? 221  THR F O   1 
ATOM   16906 C  CB  . THR F  2 111 ? 16.571  -58.731 -14.102  1.00 224.93 ? 221  THR F CB  1 
ATOM   16907 O  OG1 . THR F  2 111 ? 16.066  -59.286 -12.883  1.00 227.16 ? 221  THR F OG1 1 
ATOM   16908 C  CG2 . THR F  2 111 ? 18.057  -59.016 -14.205  1.00 221.43 ? 221  THR F CG2 1 
ATOM   16909 N  N   . PRO F  2 112 ? 16.081  -56.708 -16.559  1.00 220.35 ? 222  PRO F N   1 
ATOM   16910 C  CA  . PRO F  2 112 ? 16.542  -55.998 -17.757  1.00 224.07 ? 222  PRO F CA  1 
ATOM   16911 C  C   . PRO F  2 112 ? 16.330  -54.501 -17.600  1.00 228.90 ? 222  PRO F C   1 
ATOM   16912 O  O   . PRO F  2 112 ? 15.429  -54.048 -16.890  1.00 225.33 ? 222  PRO F O   1 
ATOM   16913 C  CB  . PRO F  2 112 ? 15.669  -56.579 -18.874  1.00 230.69 ? 222  PRO F CB  1 
ATOM   16914 C  CG  . PRO F  2 112 ? 14.431  -57.018 -18.179  1.00 236.24 ? 222  PRO F CG  1 
ATOM   16915 C  CD  . PRO F  2 112 ? 14.884  -57.522 -16.842  1.00 234.20 ? 222  PRO F CD  1 
ATOM   16916 N  N   . GLU F  2 113 ? 17.167  -53.726 -18.285  1.00 234.38 ? 223  GLU F N   1 
ATOM   16917 C  CA  . GLU F  2 113 ? 17.196  -52.282 -18.096  1.00 225.79 ? 223  GLU F CA  1 
ATOM   16918 C  C   . GLU F  2 113 ? 16.953  -51.573 -19.424  1.00 221.72 ? 223  GLU F C   1 
ATOM   16919 O  O   . GLU F  2 113 ? 16.768  -52.199 -20.468  1.00 226.91 ? 223  GLU F O   1 
ATOM   16920 C  CB  . GLU F  2 113 ? 18.525  -51.842 -17.473  1.00 219.58 ? 223  GLU F CB  1 
ATOM   16921 C  CG  . GLU F  2 113 ? 19.011  -52.712 -16.306  1.00 220.36 ? 223  GLU F CG  1 
ATOM   16922 C  CD  . GLU F  2 113 ? 18.098  -52.705 -15.078  1.00 220.44 ? 223  GLU F CD  1 
ATOM   16923 O  OE1 . GLU F  2 113 ? 16.971  -52.163 -15.133  1.00 225.48 ? 223  GLU F OE1 1 
ATOM   16924 O  OE2 . GLU F  2 113 ? 18.519  -53.256 -14.039  1.00 212.39 ? 223  GLU F OE2 1 
ATOM   16925 N  N   . GLY F  2 114 ? 16.939  -50.246 -19.371  1.00 224.95 ? 224  GLY F N   1 
ATOM   16926 C  CA  . GLY F  2 114 ? 16.708  -49.458 -20.564  1.00 235.76 ? 224  GLY F CA  1 
ATOM   16927 C  C   . GLY F  2 114 ? 18.001  -49.059 -21.238  1.00 227.47 ? 224  GLY F C   1 
ATOM   16928 O  O   . GLY F  2 114 ? 18.218  -47.880 -21.537  1.00 221.03 ? 224  GLY F O   1 
ATOM   16929 N  N   . GLY F  2 115 ? 18.874  -50.039 -21.477  1.00 230.91 ? 225  GLY F N   1 
ATOM   16930 C  CA  . GLY F  2 115 ? 20.152  -49.735 -22.094  1.00 229.75 ? 225  GLY F CA  1 
ATOM   16931 C  C   . GLY F  2 115 ? 20.002  -49.189 -23.499  1.00 230.55 ? 225  GLY F C   1 
ATOM   16932 O  O   . GLY F  2 115 ? 20.748  -48.299 -23.914  1.00 227.22 ? 225  GLY F O   1 
ATOM   16933 N  N   . PHE F  2 116 ? 19.023  -49.702 -24.243  1.00 221.17 ? 226  PHE F N   1 
ATOM   16934 C  CA  . PHE F  2 116 ? 18.868  -49.288 -25.629  1.00 219.59 ? 226  PHE F CA  1 
ATOM   16935 C  C   . PHE F  2 116 ? 18.452  -47.828 -25.739  1.00 223.06 ? 226  PHE F C   1 
ATOM   16936 O  O   . PHE F  2 116 ? 18.824  -47.156 -26.708  1.00 233.94 ? 226  PHE F O   1 
ATOM   16937 C  CB  . PHE F  2 116 ? 17.863  -50.199 -26.328  1.00 226.95 ? 226  PHE F CB  1 
ATOM   16938 C  CG  . PHE F  2 116 ? 18.349  -51.610 -26.498  1.00 228.95 ? 226  PHE F CG  1 
ATOM   16939 C  CD1 . PHE F  2 116 ? 19.692  -51.914 -26.353  1.00 217.20 ? 226  PHE F CD1 1 
ATOM   16940 C  CD2 . PHE F  2 116 ? 17.469  -52.630 -26.823  1.00 244.07 ? 226  PHE F CD2 1 
ATOM   16941 C  CE1 . PHE F  2 116 ? 20.147  -53.209 -26.512  1.00 225.16 ? 226  PHE F CE1 1 
ATOM   16942 C  CE2 . PHE F  2 116 ? 17.917  -53.928 -26.987  1.00 245.25 ? 226  PHE F CE2 1 
ATOM   16943 C  CZ  . PHE F  2 116 ? 19.258  -54.218 -26.832  1.00 239.29 ? 226  PHE F CZ  1 
ATOM   16944 N  N   . ASP F  2 117 ? 17.698  -47.317 -24.761  1.00 231.19 ? 227  ASP F N   1 
ATOM   16945 C  CA  . ASP F  2 117 ? 17.374  -45.893 -24.750  1.00 237.87 ? 227  ASP F CA  1 
ATOM   16946 C  C   . ASP F  2 117 ? 18.642  -45.049 -24.729  1.00 233.79 ? 227  ASP F C   1 
ATOM   16947 O  O   . ASP F  2 117 ? 18.756  -44.057 -25.458  1.00 227.61 ? 227  ASP F O   1 
ATOM   16948 C  CB  . ASP F  2 117 ? 16.485  -45.556 -23.550  1.00 246.47 ? 227  ASP F CB  1 
ATOM   16949 C  CG  . ASP F  2 117 ? 15.006  -45.698 -23.859  1.00 257.63 ? 227  ASP F CG  1 
ATOM   16950 O  OD1 . ASP F  2 117 ? 14.660  -46.448 -24.792  1.00 260.72 ? 227  ASP F OD1 1 
ATOM   16951 O  OD2 . ASP F  2 117 ? 14.188  -45.052 -23.169  1.00 257.57 ? 227  ASP F OD2 1 
ATOM   16952 N  N   . ALA F  2 118 ? 19.610  -45.435 -23.893  1.00 233.31 ? 228  ALA F N   1 
ATOM   16953 C  CA  . ALA F  2 118 ? 20.862  -44.694 -23.802  1.00 230.53 ? 228  ALA F CA  1 
ATOM   16954 C  C   . ALA F  2 118 ? 21.687  -44.818 -25.077  1.00 223.05 ? 228  ALA F C   1 
ATOM   16955 O  O   . ALA F  2 118 ? 22.314  -43.846 -25.512  1.00 227.91 ? 228  ALA F O   1 
ATOM   16956 C  CB  . ALA F  2 118 ? 21.664  -45.178 -22.595  1.00 232.65 ? 228  ALA F CB  1 
ATOM   16957 N  N   . ILE F  2 119 ? 21.712  -46.007 -25.683  1.00 213.96 ? 229  ILE F N   1 
ATOM   16958 C  CA  . ILE F  2 119 ? 22.472  -46.194 -26.916  1.00 214.71 ? 229  ILE F CA  1 
ATOM   16959 C  C   . ILE F  2 119 ? 21.888  -45.341 -28.034  1.00 215.82 ? 229  ILE F C   1 
ATOM   16960 O  O   . ILE F  2 119 ? 22.622  -44.714 -28.807  1.00 216.12 ? 229  ILE F O   1 
ATOM   16961 C  CB  . ILE F  2 119 ? 22.502  -47.684 -27.299  1.00 216.71 ? 229  ILE F CB  1 
ATOM   16962 C  CG1 . ILE F  2 119 ? 23.130  -48.504 -26.169  1.00 214.55 ? 229  ILE F CG1 1 
ATOM   16963 C  CG2 . ILE F  2 119 ? 23.263  -47.874 -28.603  1.00 216.98 ? 229  ILE F CG2 1 
ATOM   16964 C  CD1 . ILE F  2 119 ? 23.177  -49.990 -26.443  1.00 216.51 ? 229  ILE F CD1 1 
ATOM   16965 N  N   . MET F  2 120 ? 20.558  -45.296 -28.131  1.00 228.22 ? 230  MET F N   1 
ATOM   16966 C  CA  . MET F  2 120 ? 19.919  -44.538 -29.201  1.00 228.81 ? 230  MET F CA  1 
ATOM   16967 C  C   . MET F  2 120 ? 20.165  -43.044 -29.048  1.00 228.36 ? 230  MET F C   1 
ATOM   16968 O  O   . MET F  2 120 ? 20.481  -42.359 -30.028  1.00 226.00 ? 230  MET F O   1 
ATOM   16969 C  CB  . MET F  2 120 ? 18.420  -44.826 -29.226  1.00 236.45 ? 230  MET F CB  1 
ATOM   16970 C  CG  . MET F  2 120 ? 17.659  -43.987 -30.235  1.00 247.49 ? 230  MET F CG  1 
ATOM   16971 S  SD  . MET F  2 120 ? 18.231  -44.269 -31.918  1.00 252.09 ? 230  MET F SD  1 
ATOM   16972 C  CE  . MET F  2 120 ? 17.571  -45.904 -32.215  1.00 257.90 ? 230  MET F CE  1 
ATOM   16973 N  N   . GLN F  2 121 ? 20.029  -42.522 -27.826  1.00 245.62 ? 231  GLN F N   1 
ATOM   16974 C  CA  . GLN F  2 121 ? 20.194  -41.087 -27.616  1.00 258.33 ? 231  GLN F CA  1 
ATOM   16975 C  C   . GLN F  2 121 ? 21.646  -40.661 -27.808  1.00 258.31 ? 231  GLN F C   1 
ATOM   16976 O  O   . GLN F  2 121 ? 21.914  -39.580 -28.344  1.00 262.08 ? 231  GLN F O   1 
ATOM   16977 C  CB  . GLN F  2 121 ? 19.692  -40.702 -26.222  1.00 254.73 ? 231  GLN F CB  1 
ATOM   16978 C  CG  . GLN F  2 121 ? 18.199  -40.930 -26.012  1.00 251.73 ? 231  GLN F CG  1 
ATOM   16979 C  CD  . GLN F  2 121 ? 17.347  -40.212 -27.040  1.00 261.54 ? 231  GLN F CD  1 
ATOM   16980 O  OE1 . GLN F  2 121 ? 17.516  -39.016 -27.278  1.00 267.23 ? 231  GLN F OE1 1 
ATOM   16981 N  NE2 . GLN F  2 121 ? 16.427  -40.944 -27.661  1.00 263.49 ? 231  GLN F NE2 1 
ATOM   16982 N  N   . ALA F  2 122 ? 22.596  -41.502 -27.390  1.00 242.13 ? 232  ALA F N   1 
ATOM   16983 C  CA  . ALA F  2 122 ? 24.005  -41.159 -27.550  1.00 227.83 ? 232  ALA F CA  1 
ATOM   16984 C  C   . ALA F  2 122 ? 24.447  -41.265 -29.002  1.00 229.97 ? 232  ALA F C   1 
ATOM   16985 O  O   . ALA F  2 122 ? 25.403  -40.596 -29.409  1.00 235.63 ? 232  ALA F O   1 
ATOM   16986 C  CB  . ALA F  2 122 ? 24.869  -42.055 -26.665  1.00 221.32 ? 232  ALA F CB  1 
ATOM   16987 N  N   . ALA F  2 123 ? 23.772  -42.098 -29.792  1.00 234.18 ? 233  ALA F N   1 
ATOM   16988 C  CA  . ALA F  2 123 ? 24.155  -42.274 -31.187  1.00 237.08 ? 233  ALA F CA  1 
ATOM   16989 C  C   . ALA F  2 123 ? 23.668  -41.119 -32.053  1.00 242.50 ? 233  ALA F C   1 
ATOM   16990 O  O   . ALA F  2 123 ? 24.456  -40.506 -32.781  1.00 244.95 ? 233  ALA F O   1 
ATOM   16991 C  CB  . ALA F  2 123 ? 23.613  -43.601 -31.718  1.00 242.45 ? 233  ALA F CB  1 
ATOM   16992 N  N   . VAL F  2 124 ? 22.374  -40.802 -31.981  1.00 242.74 ? 234  VAL F N   1 
ATOM   16993 C  CA  . VAL F  2 124 ? 21.804  -39.808 -32.887  1.00 247.85 ? 234  VAL F CA  1 
ATOM   16994 C  C   . VAL F  2 124 ? 22.320  -38.415 -32.558  1.00 251.67 ? 234  VAL F C   1 
ATOM   16995 O  O   . VAL F  2 124 ? 22.643  -37.632 -33.459  1.00 254.52 ? 234  VAL F O   1 
ATOM   16996 C  CB  . VAL F  2 124 ? 20.268  -39.866 -32.843  1.00 247.93 ? 234  VAL F CB  1 
ATOM   16997 C  CG1 . VAL F  2 124 ? 19.677  -38.906 -33.860  1.00 255.90 ? 234  VAL F CG1 1 
ATOM   16998 C  CG2 . VAL F  2 124 ? 19.790  -41.281 -33.099  1.00 249.12 ? 234  VAL F CG2 1 
ATOM   16999 N  N   . CYS F  2 125 ? 22.408  -38.080 -31.272  1.00 251.22 ? 235  CYS F N   1 
ATOM   17000 C  CA  . CYS F  2 125 ? 22.865  -36.756 -30.868  1.00 251.44 ? 235  CYS F CA  1 
ATOM   17001 C  C   . CYS F  2 125 ? 24.321  -36.533 -31.254  1.00 245.91 ? 235  CYS F C   1 
ATOM   17002 O  O   . CYS F  2 125 ? 25.227  -36.778 -30.451  1.00 240.78 ? 235  CYS F O   1 
ATOM   17003 C  CB  . CYS F  2 125 ? 22.691  -36.563 -29.360  1.00 242.06 ? 235  CYS F CB  1 
ATOM   17004 S  SG  . CYS F  2 125 ? 20.989  -36.679 -28.758  1.00 239.02 ? 235  CYS F SG  1 
ATOM   17005 N  N   . LYS F  2 126 ? 24.557  -36.060 -32.479  1.00 249.17 ? 236  LYS F N   1 
ATOM   17006 C  CA  . LYS F  2 126 ? 25.908  -35.735 -32.918  1.00 243.56 ? 236  LYS F CA  1 
ATOM   17007 C  C   . LYS F  2 126 ? 26.384  -34.392 -32.390  1.00 241.17 ? 236  LYS F C   1 
ATOM   17008 O  O   . LYS F  2 126 ? 27.550  -34.040 -32.593  1.00 244.71 ? 236  LYS F O   1 
ATOM   17009 C  CB  . LYS F  2 126 ? 25.988  -35.726 -34.448  1.00 250.43 ? 236  LYS F CB  1 
ATOM   17010 C  CG  . LYS F  2 126 ? 25.868  -37.088 -35.110  1.00 252.62 ? 236  LYS F CG  1 
ATOM   17011 C  CD  . LYS F  2 126 ? 25.932  -36.950 -36.624  1.00 269.75 ? 236  LYS F CD  1 
ATOM   17012 C  CE  . LYS F  2 126 ? 25.927  -38.304 -37.311  1.00 272.79 ? 236  LYS F CE  1 
ATOM   17013 N  NZ  . LYS F  2 126 ? 25.957  -38.171 -38.795  1.00 277.91 ? 236  LYS F NZ  1 
ATOM   17014 N  N   . GLU F  2 127 ? 25.511  -33.637 -31.730  1.00 235.21 ? 237  GLU F N   1 
ATOM   17015 C  CA  . GLU F  2 127 ? 25.824  -32.298 -31.257  1.00 235.43 ? 237  GLU F CA  1 
ATOM   17016 C  C   . GLU F  2 127 ? 26.051  -32.278 -29.752  1.00 230.47 ? 237  GLU F C   1 
ATOM   17017 O  O   . GLU F  2 127 ? 27.126  -31.880 -29.291  1.00 229.35 ? 237  GLU F O   1 
ATOM   17018 C  CB  . GLU F  2 127 ? 24.690  -31.341 -31.642  1.00 251.98 ? 237  GLU F CB  1 
ATOM   17019 C  CG  . GLU F  2 127 ? 24.342  -31.374 -33.121  1.00 261.46 ? 237  GLU F CG  1 
ATOM   17020 C  CD  . GLU F  2 127 ? 23.048  -30.651 -33.430  1.00 269.95 ? 237  GLU F CD  1 
ATOM   17021 O  OE1 . GLU F  2 127 ? 22.678  -30.574 -34.619  1.00 271.45 ? 237  GLU F OE1 1 
ATOM   17022 O  OE2 . GLU F  2 127 ? 22.394  -30.171 -32.480  1.00 276.20 ? 237  GLU F OE2 1 
ATOM   17023 N  N   . LYS F  2 128 ? 25.056  -32.706 -28.971  1.00 226.09 ? 238  LYS F N   1 
ATOM   17024 C  CA  . LYS F  2 128 ? 25.179  -32.679 -27.520  1.00 224.03 ? 238  LYS F CA  1 
ATOM   17025 C  C   . LYS F  2 128 ? 26.188  -33.699 -27.021  1.00 223.76 ? 238  LYS F C   1 
ATOM   17026 O  O   . LYS F  2 128 ? 26.681  -33.570 -25.897  1.00 234.71 ? 238  LYS F O   1 
ATOM   17027 C  CB  . LYS F  2 128 ? 23.813  -32.919 -26.873  1.00 220.70 ? 238  LYS F CB  1 
ATOM   17028 C  CG  . LYS F  2 128 ? 22.702  -32.035 -27.435  1.00 224.94 ? 238  LYS F CG  1 
ATOM   17029 C  CD  . LYS F  2 128 ? 21.431  -32.093 -26.597  1.00 224.92 ? 238  LYS F CD  1 
ATOM   17030 C  CE  . LYS F  2 128 ? 21.602  -31.391 -25.261  1.00 220.36 ? 238  LYS F CE  1 
ATOM   17031 N  NZ  . LYS F  2 128 ? 20.320  -31.307 -24.505  1.00 216.63 ? 238  LYS F NZ  1 
ATOM   17032 N  N   . ILE F  2 129 ? 26.503  -34.704 -27.829  1.00 215.21 ? 239  ILE F N   1 
ATOM   17033 C  CA  . ILE F  2 129 ? 27.599  -35.616 -27.518  1.00 215.80 ? 239  ILE F CA  1 
ATOM   17034 C  C   . ILE F  2 129 ? 28.880  -35.164 -28.199  1.00 222.46 ? 239  ILE F C   1 
ATOM   17035 O  O   . ILE F  2 129 ? 29.956  -35.199 -27.597  1.00 229.68 ? 239  ILE F O   1 
ATOM   17036 C  CB  . ILE F  2 129 ? 27.224  -37.059 -27.907  1.00 218.76 ? 239  ILE F CB  1 
ATOM   17037 C  CG1 . ILE F  2 129 ? 26.427  -37.731 -26.787  1.00 215.38 ? 239  ILE F CG1 1 
ATOM   17038 C  CG2 . ILE F  2 129 ? 28.472  -37.866 -28.235  1.00 222.96 ? 239  ILE F CG2 1 
ATOM   17039 C  CD1 . ILE F  2 129 ? 25.011  -37.206 -26.627  1.00 226.57 ? 239  ILE F CD1 1 
ATOM   17040 N  N   . GLY F  2 130 ? 28.774  -34.726 -29.452  1.00 227.72 ? 240  GLY F N   1 
ATOM   17041 C  CA  . GLY F  2 130 ? 29.886  -34.138 -30.174  1.00 241.54 ? 240  GLY F CA  1 
ATOM   17042 C  C   . GLY F  2 130 ? 30.762  -35.126 -30.914  1.00 241.07 ? 240  GLY F C   1 
ATOM   17043 O  O   . GLY F  2 130 ? 31.957  -35.244 -30.627  1.00 248.99 ? 240  GLY F O   1 
ATOM   17044 N  N   . TRP F  2 131 ? 30.184  -35.829 -31.883  1.00 235.71 ? 241  TRP F N   1 
ATOM   17045 C  CA  . TRP F  2 131 ? 30.945  -36.768 -32.693  1.00 234.06 ? 241  TRP F CA  1 
ATOM   17046 C  C   . TRP F  2 131 ? 31.711  -36.036 -33.787  1.00 249.46 ? 241  TRP F C   1 
ATOM   17047 O  O   . TRP F  2 131 ? 31.171  -35.154 -34.461  1.00 263.53 ? 241  TRP F O   1 
ATOM   17048 C  CB  . TRP F  2 131 ? 30.014  -37.800 -33.323  1.00 239.22 ? 241  TRP F CB  1 
ATOM   17049 C  CG  . TRP F  2 131 ? 29.313  -38.653 -32.327  1.00 239.95 ? 241  TRP F CG  1 
ATOM   17050 C  CD1 . TRP F  2 131 ? 28.008  -38.557 -31.945  1.00 248.38 ? 241  TRP F CD1 1 
ATOM   17051 C  CD2 . TRP F  2 131 ? 29.876  -39.729 -31.571  1.00 230.92 ? 241  TRP F CD2 1 
ATOM   17052 N  NE1 . TRP F  2 131 ? 27.720  -39.513 -31.004  1.00 247.48 ? 241  TRP F NE1 1 
ATOM   17053 C  CE2 . TRP F  2 131 ? 28.850  -40.245 -30.755  1.00 233.67 ? 241  TRP F CE2 1 
ATOM   17054 C  CE3 . TRP F  2 131 ? 31.146  -40.309 -31.507  1.00 227.62 ? 241  TRP F CE3 1 
ATOM   17055 C  CZ2 . TRP F  2 131 ? 29.055  -41.312 -29.887  1.00 223.68 ? 241  TRP F CZ2 1 
ATOM   17056 C  CZ3 . TRP F  2 131 ? 31.347  -41.367 -30.644  1.00 221.03 ? 241  TRP F CZ3 1 
ATOM   17057 C  CH2 . TRP F  2 131 ? 30.307  -41.858 -29.846  1.00 218.45 ? 241  TRP F CH2 1 
ATOM   17058 N  N   . ARG F  2 132 ? 32.972  -36.417 -33.973  1.00 248.95 ? 242  ARG F N   1 
ATOM   17059 C  CA  . ARG F  2 132 ? 33.793  -35.831 -35.020  1.00 259.84 ? 242  ARG F CA  1 
ATOM   17060 C  C   . ARG F  2 132 ? 33.261  -36.189 -36.408  1.00 262.11 ? 242  ARG F C   1 
ATOM   17061 O  O   . ARG F  2 132 ? 32.434  -37.089 -36.581  1.00 258.36 ? 242  ARG F O   1 
ATOM   17062 C  CB  . ARG F  2 132 ? 35.244  -36.294 -34.906  1.00 251.69 ? 242  ARG F CB  1 
ATOM   17063 C  CG  . ARG F  2 132 ? 36.155  -35.351 -34.157  1.00 244.91 ? 242  ARG F CG  1 
ATOM   17064 C  CD  . ARG F  2 132 ? 37.566  -35.903 -34.130  1.00 238.59 ? 242  ARG F CD  1 
ATOM   17065 N  NE  . ARG F  2 132 ? 38.496  -35.001 -33.461  1.00 231.68 ? 242  ARG F NE  1 
ATOM   17066 C  CZ  . ARG F  2 132 ? 38.999  -35.203 -32.250  1.00 220.67 ? 242  ARG F CZ  1 
ATOM   17067 N  NH1 . ARG F  2 132 ? 38.663  -36.284 -31.561  1.00 213.37 ? 242  ARG F NH1 1 
ATOM   17068 N  NH2 . ARG F  2 132 ? 39.842  -34.322 -31.729  1.00 220.53 ? 242  ARG F NH2 1 
ATOM   17069 N  N   . ASN F  2 133 ? 33.750  -35.453 -37.411  1.00 266.96 ? 243  ASN F N   1 
ATOM   17070 C  CA  . ASN F  2 133 ? 33.382  -35.742 -38.795  1.00 267.65 ? 243  ASN F CA  1 
ATOM   17071 C  C   . ASN F  2 133 ? 33.928  -37.093 -39.227  1.00 263.11 ? 243  ASN F C   1 
ATOM   17072 O  O   . ASN F  2 133 ? 33.171  -38.006 -39.576  1.00 267.63 ? 243  ASN F O   1 
ATOM   17073 C  CB  . ASN F  2 133 ? 33.924  -34.665 -39.738  1.00 273.63 ? 243  ASN F CB  1 
ATOM   17074 C  CG  . ASN F  2 133 ? 32.972  -33.512 -39.951  1.00 276.30 ? 243  ASN F CG  1 
ATOM   17075 O  OD1 . ASN F  2 133 ? 31.822  -33.534 -39.510  1.00 276.07 ? 243  ASN F OD1 1 
ATOM   17076 N  ND2 . ASN F  2 133 ? 33.449  -32.501 -40.671  1.00 276.78 ? 243  ASN F ND2 1 
ATOM   17077 N  N   . ASP F  2 134 ? 35.248  -37.235 -39.209  1.00 248.33 ? 244  ASP F N   1 
ATOM   17078 C  CA  . ASP F  2 134 ? 35.934  -38.437 -39.666  1.00 247.56 ? 244  ASP F CA  1 
ATOM   17079 C  C   . ASP F  2 134 ? 36.753  -38.997 -38.510  1.00 244.37 ? 244  ASP F C   1 
ATOM   17080 O  O   . ASP F  2 134 ? 37.923  -38.652 -38.339  1.00 247.29 ? 244  ASP F O   1 
ATOM   17081 C  CB  . ASP F  2 134 ? 36.797  -38.115 -40.866  1.00 259.66 ? 244  ASP F CB  1 
ATOM   17082 C  CG  . ASP F  2 134 ? 36.032  -37.364 -41.936  1.00 275.60 ? 244  ASP F CG  1 
ATOM   17083 O  OD1 . ASP F  2 134 ? 35.991  -36.117 -41.873  1.00 285.90 ? 244  ASP F OD1 1 
ATOM   17084 O  OD2 . ASP F  2 134 ? 35.456  -38.021 -42.828  1.00 276.58 ? 244  ASP F OD2 1 
ATOM   17085 N  N   . SER F  2 135 ? 36.127  -39.859 -37.715  1.00 241.01 ? 245  SER F N   1 
ATOM   17086 C  CA  . SER F  2 135 ? 36.798  -40.510 -36.602  1.00 230.07 ? 245  SER F CA  1 
ATOM   17087 C  C   . SER F  2 135 ? 36.111  -41.841 -36.344  1.00 235.40 ? 245  SER F C   1 
ATOM   17088 O  O   . SER F  2 135 ? 35.075  -42.157 -36.937  1.00 243.62 ? 245  SER F O   1 
ATOM   17089 C  CB  . SER F  2 135 ? 36.791  -39.637 -35.344  1.00 226.10 ? 245  SER F CB  1 
ATOM   17090 O  OG  . SER F  2 135 ? 35.489  -39.549 -34.794  1.00 225.66 ? 245  SER F OG  1 
ATOM   17091 N  N   . LEU F  2 136 ? 36.697  -42.623 -35.442  1.00 237.73 ? 246  LEU F N   1 
ATOM   17092 C  CA  . LEU F  2 136 ? 36.143  -43.922 -35.064  1.00 234.02 ? 246  LEU F CA  1 
ATOM   17093 C  C   . LEU F  2 136 ? 35.187  -43.708 -33.898  1.00 229.43 ? 246  LEU F C   1 
ATOM   17094 O  O   . LEU F  2 136 ? 35.611  -43.523 -32.754  1.00 229.58 ? 246  LEU F O   1 
ATOM   17095 C  CB  . LEU F  2 136 ? 37.257  -44.905 -34.722  1.00 225.77 ? 246  LEU F CB  1 
ATOM   17096 C  CG  . LEU F  2 136 ? 38.276  -45.172 -35.835  1.00 226.43 ? 246  LEU F CG  1 
ATOM   17097 C  CD1 . LEU F  2 136 ? 39.284  -46.224 -35.402  1.00 215.45 ? 246  LEU F CD1 1 
ATOM   17098 C  CD2 . LEU F  2 136 ? 37.583  -45.599 -37.126  1.00 241.65 ? 246  LEU F CD2 1 
ATOM   17099 N  N   . HIS F  2 137 ? 33.889  -43.709 -34.195  1.00 224.35 ? 247  HIS F N   1 
ATOM   17100 C  CA  . HIS F  2 137 ? 32.846  -43.500 -33.191  1.00 226.53 ? 247  HIS F CA  1 
ATOM   17101 C  C   . HIS F  2 137 ? 32.621  -44.812 -32.447  1.00 222.18 ? 247  HIS F C   1 
ATOM   17102 O  O   . HIS F  2 137 ? 31.868  -45.682 -32.887  1.00 223.31 ? 247  HIS F O   1 
ATOM   17103 C  CB  . HIS F  2 137 ? 31.564  -43.005 -33.848  1.00 239.75 ? 247  HIS F CB  1 
ATOM   17104 C  CG  . HIS F  2 137 ? 31.761  -41.830 -34.755  1.00 241.06 ? 247  HIS F CG  1 
ATOM   17105 N  ND1 . HIS F  2 137 ? 30.983  -41.615 -35.873  1.00 245.27 ? 247  HIS F ND1 1 
ATOM   17106 C  CD2 . HIS F  2 137 ? 32.644  -40.805 -34.709  1.00 237.55 ? 247  HIS F CD2 1 
ATOM   17107 C  CE1 . HIS F  2 137 ? 31.380  -40.510 -36.477  1.00 250.62 ? 247  HIS F CE1 1 
ATOM   17108 N  NE2 . HIS F  2 137 ? 32.387  -39.999 -35.791  1.00 245.00 ? 247  HIS F NE2 1 
ATOM   17109 N  N   . LEU F  2 138 ? 33.288  -44.961 -31.306  1.00 222.17 ? 248  LEU F N   1 
ATOM   17110 C  CA  . LEU F  2 138 ? 33.206  -46.170 -30.495  1.00 217.23 ? 248  LEU F CA  1 
ATOM   17111 C  C   . LEU F  2 138 ? 32.337  -45.913 -29.269  1.00 224.70 ? 248  LEU F C   1 
ATOM   17112 O  O   . LEU F  2 138 ? 32.509  -44.899 -28.583  1.00 232.30 ? 248  LEU F O   1 
ATOM   17113 C  CB  . LEU F  2 138 ? 34.597  -46.633 -30.070  1.00 194.26 ? 248  LEU F CB  1 
ATOM   17114 C  CG  . LEU F  2 138 ? 35.649  -46.694 -31.175  1.00 187.25 ? 248  LEU F CG  1 
ATOM   17115 C  CD1 . LEU F  2 138 ? 36.956  -47.219 -30.613  1.00 174.34 ? 248  LEU F CD1 1 
ATOM   17116 C  CD2 . LEU F  2 138 ? 35.165  -47.553 -32.332  1.00 194.14 ? 248  LEU F CD2 1 
ATOM   17117 N  N   . LEU F  2 139 ? 31.413  -46.835 -28.992  1.00 217.39 ? 249  LEU F N   1 
ATOM   17118 C  CA  . LEU F  2 139 ? 30.453  -46.699 -27.893  1.00 208.60 ? 249  LEU F CA  1 
ATOM   17119 C  C   . LEU F  2 139 ? 30.536  -47.937 -27.001  1.00 205.45 ? 249  LEU F C   1 
ATOM   17120 O  O   . LEU F  2 139 ? 29.979  -48.985 -27.339  1.00 207.15 ? 249  LEU F O   1 
ATOM   17121 C  CB  . LEU F  2 139 ? 29.038  -46.497 -28.429  1.00 213.71 ? 249  LEU F CB  1 
ATOM   17122 C  CG  . LEU F  2 139 ? 28.086  -45.598 -27.630  1.00 221.49 ? 249  LEU F CG  1 
ATOM   17123 C  CD1 . LEU F  2 139 ? 26.856  -45.248 -28.457  1.00 232.57 ? 249  LEU F CD1 1 
ATOM   17124 C  CD2 . LEU F  2 139 ? 27.677  -46.250 -26.319  1.00 222.59 ? 249  LEU F CD2 1 
ATOM   17125 N  N   . VAL F  2 140 ? 31.245  -47.822 -25.879  1.00 201.64 ? 250  VAL F N   1 
ATOM   17126 C  CA  . VAL F  2 140 ? 31.366  -48.916 -24.916  1.00 195.62 ? 250  VAL F CA  1 
ATOM   17127 C  C   . VAL F  2 140 ? 30.097  -49.002 -24.074  1.00 204.39 ? 250  VAL F C   1 
ATOM   17128 O  O   . VAL F  2 140 ? 29.720  -48.040 -23.397  1.00 204.40 ? 250  VAL F O   1 
ATOM   17129 C  CB  . VAL F  2 140 ? 32.603  -48.739 -24.027  1.00 189.53 ? 250  VAL F CB  1 
ATOM   17130 C  CG1 . VAL F  2 140 ? 32.519  -49.664 -22.821  1.00 193.21 ? 250  VAL F CG1 1 
ATOM   17131 C  CG2 . VAL F  2 140 ? 33.862  -49.024 -24.822  1.00 195.32 ? 250  VAL F CG2 1 
ATOM   17132 N  N   . PHE F  2 141 ? 29.450  -50.166 -24.098  1.00 207.00 ? 251  PHE F N   1 
ATOM   17133 C  CA  . PHE F  2 141 ? 28.217  -50.422 -23.362  1.00 208.00 ? 251  PHE F CA  1 
ATOM   17134 C  C   . PHE F  2 141 ? 28.507  -51.383 -22.214  1.00 204.63 ? 251  PHE F C   1 
ATOM   17135 O  O   . PHE F  2 141 ? 29.020  -52.485 -22.438  1.00 209.92 ? 251  PHE F O   1 
ATOM   17136 C  CB  . PHE F  2 141 ? 27.146  -50.996 -24.291  1.00 212.16 ? 251  PHE F CB  1 
ATOM   17137 C  CG  . PHE F  2 141 ? 25.847  -51.305 -23.607  1.00 210.00 ? 251  PHE F CG  1 
ATOM   17138 C  CD1 . PHE F  2 141 ? 24.945  -50.297 -23.316  1.00 216.95 ? 251  PHE F CD1 1 
ATOM   17139 C  CD2 . PHE F  2 141 ? 25.525  -52.607 -23.263  1.00 217.41 ? 251  PHE F CD2 1 
ATOM   17140 C  CE1 . PHE F  2 141 ? 23.745  -50.581 -22.691  1.00 232.13 ? 251  PHE F CE1 1 
ATOM   17141 C  CE2 . PHE F  2 141 ? 24.329  -52.898 -22.637  1.00 232.60 ? 251  PHE F CE2 1 
ATOM   17142 C  CZ  . PHE F  2 141 ? 23.437  -51.884 -22.349  1.00 239.14 ? 251  PHE F CZ  1 
ATOM   17143 N  N   . VAL F  2 142 ? 28.186  -50.965 -20.992  1.00 203.40 ? 252  VAL F N   1 
ATOM   17144 C  CA  . VAL F  2 142 ? 28.460  -51.750 -19.792  1.00 199.32 ? 252  VAL F CA  1 
ATOM   17145 C  C   . VAL F  2 142 ? 27.160  -51.940 -19.020  1.00 202.25 ? 252  VAL F C   1 
ATOM   17146 O  O   . VAL F  2 142 ? 26.518  -50.958 -18.628  1.00 211.59 ? 252  VAL F O   1 
ATOM   17147 C  CB  . VAL F  2 142 ? 29.522  -51.080 -18.912  1.00 192.93 ? 252  VAL F CB  1 
ATOM   17148 C  CG1 . VAL F  2 142 ? 29.649  -51.818 -17.602  1.00 195.69 ? 252  VAL F CG1 1 
ATOM   17149 C  CG2 . VAL F  2 142 ? 30.857  -51.038 -19.642  1.00 190.57 ? 252  VAL F CG2 1 
ATOM   17150 N  N   . SER F  2 143 ? 26.780  -53.199 -18.798  1.00 193.52 ? 253  SER F N   1 
ATOM   17151 C  CA  . SER F  2 143 ? 25.649  -53.557 -17.951  1.00 194.44 ? 253  SER F CA  1 
ATOM   17152 C  C   . SER F  2 143 ? 25.762  -55.035 -17.605  1.00 204.67 ? 253  SER F C   1 
ATOM   17153 O  O   . SER F  2 143 ? 26.261  -55.830 -18.406  1.00 207.18 ? 253  SER F O   1 
ATOM   17154 C  CB  . SER F  2 143 ? 24.305  -53.264 -18.630  1.00 202.79 ? 253  SER F CB  1 
ATOM   17155 O  OG  . SER F  2 143 ? 24.101  -54.109 -19.746  1.00 212.19 ? 253  SER F OG  1 
ATOM   17156 N  N   . ASP F  2 144 ? 25.308  -55.399 -16.402  1.00 223.03 ? 254  ASP F N   1 
ATOM   17157 C  CA  . ASP F  2 144 ? 25.395  -56.777 -15.928  1.00 227.83 ? 254  ASP F CA  1 
ATOM   17158 C  C   . ASP F  2 144 ? 24.067  -57.522 -16.036  1.00 236.16 ? 254  ASP F C   1 
ATOM   17159 O  O   . ASP F  2 144 ? 23.834  -58.485 -15.295  1.00 236.85 ? 254  ASP F O   1 
ATOM   17160 C  CB  . ASP F  2 144 ? 25.920  -56.820 -14.490  1.00 213.36 ? 254  ASP F CB  1 
ATOM   17161 C  CG  . ASP F  2 144 ? 24.926  -56.274 -13.478  1.00 206.55 ? 254  ASP F CG  1 
ATOM   17162 O  OD1 . ASP F  2 144 ? 24.082  -55.435 -13.856  1.00 210.74 ? 254  ASP F OD1 1 
ATOM   17163 O  OD2 . ASP F  2 144 ? 25.005  -56.673 -12.295  1.00 202.71 ? 254  ASP F OD2 1 
ATOM   17164 N  N   . ALA F  2 145 ? 23.192  -57.102 -16.948  1.00 240.25 ? 255  ALA F N   1 
ATOM   17165 C  CA  . ALA F  2 145 ? 21.911  -57.763 -17.148  1.00 234.44 ? 255  ALA F CA  1 
ATOM   17166 C  C   . ALA F  2 145 ? 21.434  -57.513 -18.574  1.00 230.00 ? 255  ALA F C   1 
ATOM   17167 O  O   . ALA F  2 145 ? 22.099  -56.843 -19.369  1.00 227.29 ? 255  ALA F O   1 
ATOM   17168 C  CB  . ALA F  2 145 ? 20.876  -57.278 -16.130  1.00 230.37 ? 255  ALA F CB  1 
ATOM   17169 N  N   . ASP F  2 146 ? 20.253  -58.043 -18.883  1.00 227.07 ? 256  ASP F N   1 
ATOM   17170 C  CA  . ASP F  2 146 ? 19.642  -57.857 -20.189  1.00 226.10 ? 256  ASP F CA  1 
ATOM   17171 C  C   . ASP F  2 146 ? 19.180  -56.407 -20.343  1.00 234.40 ? 256  ASP F C   1 
ATOM   17172 O  O   . ASP F  2 146 ? 19.359  -55.567 -19.456  1.00 239.04 ? 256  ASP F O   1 
ATOM   17173 C  CB  . ASP F  2 146 ? 18.482  -58.833 -20.368  1.00 225.85 ? 256  ASP F CB  1 
ATOM   17174 C  CG  . ASP F  2 146 ? 18.138  -59.079 -21.826  1.00 221.37 ? 256  ASP F CG  1 
ATOM   17175 O  OD1 . ASP F  2 146 ? 18.339  -58.165 -22.655  1.00 212.28 ? 256  ASP F OD1 1 
ATOM   17176 O  OD2 . ASP F  2 146 ? 17.667  -60.192 -22.139  1.00 226.65 ? 256  ASP F OD2 1 
ATOM   17177 N  N   . SER F  2 147 ? 18.590  -56.104 -21.498  1.00 245.78 ? 257  SER F N   1 
ATOM   17178 C  CA  . SER F  2 147 ? 18.059  -54.776 -21.759  1.00 241.92 ? 257  SER F CA  1 
ATOM   17179 C  C   . SER F  2 147 ? 16.743  -54.878 -22.520  1.00 227.25 ? 257  SER F C   1 
ATOM   17180 O  O   . SER F  2 147 ? 16.548  -55.783 -23.337  1.00 222.21 ? 257  SER F O   1 
ATOM   17181 C  CB  . SER F  2 147 ? 19.067  -53.910 -22.533  1.00 246.96 ? 257  SER F CB  1 
ATOM   17182 O  OG  . SER F  2 147 ? 19.482  -54.545 -23.729  1.00 258.09 ? 257  SER F OG  1 
ATOM   17183 N  N   . HIS F  2 148 ? 15.836  -53.953 -22.215  1.00 226.26 ? 258  HIS F N   1 
ATOM   17184 C  CA  . HIS F  2 148 ? 14.531  -53.895 -22.858  1.00 233.76 ? 258  HIS F CA  1 
ATOM   17185 C  C   . HIS F  2 148 ? 14.646  -53.326 -24.267  1.00 243.55 ? 258  HIS F C   1 
ATOM   17186 O  O   . HIS F  2 148 ? 15.443  -52.417 -24.518  1.00 251.87 ? 258  HIS F O   1 
ATOM   17187 C  CB  . HIS F  2 148 ? 13.577  -53.027 -22.038  1.00 239.58 ? 258  HIS F CB  1 
ATOM   17188 C  CG  . HIS F  2 148 ? 13.092  -53.675 -20.780  1.00 248.02 ? 258  HIS F CG  1 
ATOM   17189 N  ND1 . HIS F  2 148 ? 12.138  -54.670 -20.775  1.00 260.77 ? 258  HIS F ND1 1 
ATOM   17190 C  CD2 . HIS F  2 148 ? 13.422  -53.464 -19.484  1.00 247.08 ? 258  HIS F CD2 1 
ATOM   17191 C  CE1 . HIS F  2 148 ? 11.903  -55.046 -19.531  1.00 259.60 ? 258  HIS F CE1 1 
ATOM   17192 N  NE2 . HIS F  2 148 ? 12.669  -54.329 -18.728  1.00 254.98 ? 258  HIS F NE2 1 
ATOM   17193 N  N   . PHE F  2 149 ? 13.844  -53.868 -25.188  1.00 242.10 ? 259  PHE F N   1 
ATOM   17194 C  CA  . PHE F  2 149 ? 13.726  -53.304 -26.530  1.00 238.18 ? 259  PHE F CA  1 
ATOM   17195 C  C   . PHE F  2 149 ? 12.290  -52.882 -26.838  1.00 239.88 ? 259  PHE F C   1 
ATOM   17196 O  O   . PHE F  2 149 ? 11.488  -52.677 -25.920  1.00 240.84 ? 259  PHE F O   1 
ATOM   17197 C  CB  . PHE F  2 149 ? 14.242  -54.294 -27.582  1.00 235.75 ? 259  PHE F CB  1 
ATOM   17198 C  CG  . PHE F  2 149 ? 13.781  -55.712 -27.378  1.00 234.47 ? 259  PHE F CG  1 
ATOM   17199 C  CD1 . PHE F  2 149 ? 14.509  -56.580 -26.579  1.00 228.81 ? 259  PHE F CD1 1 
ATOM   17200 C  CD2 . PHE F  2 149 ? 12.647  -56.191 -28.015  1.00 238.09 ? 259  PHE F CD2 1 
ATOM   17201 C  CE1 . PHE F  2 149 ? 14.102  -57.886 -26.397  1.00 230.18 ? 259  PHE F CE1 1 
ATOM   17202 C  CE2 . PHE F  2 149 ? 12.237  -57.501 -27.837  1.00 242.90 ? 259  PHE F CE2 1 
ATOM   17203 C  CZ  . PHE F  2 149 ? 12.964  -58.347 -27.025  1.00 238.96 ? 259  PHE F CZ  1 
ATOM   17204 N  N   . GLY F  2 150 ? 11.966  -52.732 -28.123  1.00 235.64 ? 260  GLY F N   1 
ATOM   17205 C  CA  . GLY F  2 150 ? 10.673  -52.229 -28.558  1.00 243.31 ? 260  GLY F CA  1 
ATOM   17206 C  C   . GLY F  2 150 ? 9.460   -52.929 -27.977  1.00 249.27 ? 260  GLY F C   1 
ATOM   17207 O  O   . GLY F  2 150 ? 9.513   -54.123 -27.664  1.00 250.06 ? 260  GLY F O   1 
ATOM   17208 N  N   . MET F  2 151 ? 8.360   -52.186 -27.828  1.00 254.01 ? 261  MET F N   1 
ATOM   17209 C  CA  . MET F  2 151 ? 7.035   -52.667 -27.435  1.00 261.39 ? 261  MET F CA  1 
ATOM   17210 C  C   . MET F  2 151 ? 6.988   -53.200 -26.006  1.00 258.36 ? 261  MET F C   1 
ATOM   17211 O  O   . MET F  2 151 ? 5.904   -53.593 -25.539  1.00 264.45 ? 261  MET F O   1 
ATOM   17212 C  CB  . MET F  2 151 ? 6.493   -53.737 -28.394  1.00 269.71 ? 261  MET F CB  1 
ATOM   17213 C  CG  . MET F  2 151 ? 6.091   -53.186 -29.757  1.00 276.07 ? 261  MET F CG  1 
ATOM   17214 S  SD  . MET F  2 151 ? 6.038   -54.443 -31.044  1.00 283.73 ? 261  MET F SD  1 
ATOM   17215 C  CE  . MET F  2 151 ? 4.766   -53.785 -32.120  1.00 295.24 ? 261  MET F CE  1 
ATOM   17216 N  N   . ASP F  2 152 ? 8.114   -53.228 -25.292  1.00 249.83 ? 262  ASP F N   1 
ATOM   17217 C  CA  . ASP F  2 152 ? 8.114   -53.640 -23.896  1.00 250.19 ? 262  ASP F CA  1 
ATOM   17218 C  C   . ASP F  2 152 ? 7.527   -52.576 -22.981  1.00 246.82 ? 262  ASP F C   1 
ATOM   17219 O  O   . ASP F  2 152 ? 7.063   -52.907 -21.883  1.00 248.02 ? 262  ASP F O   1 
ATOM   17220 C  CB  . ASP F  2 152 ? 9.537   -53.997 -23.453  1.00 253.11 ? 262  ASP F CB  1 
ATOM   17221 C  CG  . ASP F  2 152 ? 9.976   -55.375 -23.939  1.00 260.78 ? 262  ASP F CG  1 
ATOM   17222 O  OD1 . ASP F  2 152 ? 9.110   -56.269 -24.079  1.00 256.86 ? 262  ASP F OD1 1 
ATOM   17223 O  OD2 . ASP F  2 152 ? 11.191  -55.564 -24.180  1.00 262.88 ? 262  ASP F OD2 1 
ATOM   17224 N  N   . SER F  2 153 ? 7.504   -51.319 -23.420  1.00 245.95 ? 263  SER F N   1 
ATOM   17225 C  CA  . SER F  2 153 ? 6.929   -50.234 -22.636  1.00 246.27 ? 263  SER F CA  1 
ATOM   17226 C  C   . SER F  2 153 ? 5.408   -50.214 -22.704  1.00 255.44 ? 263  SER F C   1 
ATOM   17227 O  O   . SER F  2 153 ? 4.777   -49.382 -22.040  1.00 256.99 ? 263  SER F O   1 
ATOM   17228 C  CB  . SER F  2 153 ? 7.513   -48.893 -23.098  1.00 242.53 ? 263  SER F CB  1 
ATOM   17229 O  OG  . SER F  2 153 ? 7.359   -48.719 -24.495  1.00 246.50 ? 263  SER F OG  1 
ATOM   17230 N  N   . LYS F  2 154 ? 4.810   -51.122 -23.479  1.00 262.00 ? 264  LYS F N   1 
ATOM   17231 C  CA  . LYS F  2 154 ? 3.358   -51.220 -23.542  1.00 271.49 ? 264  LYS F CA  1 
ATOM   17232 C  C   . LYS F  2 154 ? 2.766   -51.518 -22.173  1.00 272.80 ? 264  LYS F C   1 
ATOM   17233 O  O   . LYS F  2 154 ? 1.657   -51.066 -21.864  1.00 278.77 ? 264  LYS F O   1 
ATOM   17234 C  CB  . LYS F  2 154 ? 2.963   -52.301 -24.548  1.00 278.28 ? 264  LYS F CB  1 
ATOM   17235 C  CG  . LYS F  2 154 ? 1.473   -52.534 -24.690  1.00 289.08 ? 264  LYS F CG  1 
ATOM   17236 C  CD  . LYS F  2 154 ? 1.207   -53.502 -25.831  1.00 295.98 ? 264  LYS F CD  1 
ATOM   17237 C  CE  . LYS F  2 154 ? -0.223  -54.006 -25.815  1.00 307.12 ? 264  LYS F CE  1 
ATOM   17238 N  NZ  . LYS F  2 154 ? -1.202  -52.897 -25.801  1.00 311.86 ? 264  LYS F NZ  1 
ATOM   17239 N  N   . LEU F  2 155 ? 3.487   -52.279 -21.345  1.00 267.86 ? 265  LEU F N   1 
ATOM   17240 C  CA  . LEU F  2 155 ? 3.026   -52.539 -19.986  1.00 269.10 ? 265  LEU F CA  1 
ATOM   17241 C  C   . LEU F  2 155 ? 2.952   -51.246 -19.188  1.00 266.22 ? 265  LEU F C   1 
ATOM   17242 O  O   . LEU F  2 155 ? 2.033   -51.050 -18.384  1.00 270.84 ? 265  LEU F O   1 
ATOM   17243 C  CB  . LEU F  2 155 ? 3.957   -53.539 -19.297  1.00 264.24 ? 265  LEU F CB  1 
ATOM   17244 C  CG  . LEU F  2 155 ? 4.263   -54.845 -20.036  1.00 266.19 ? 265  LEU F CG  1 
ATOM   17245 C  CD1 . LEU F  2 155 ? 5.291   -55.660 -19.274  1.00 260.83 ? 265  LEU F CD1 1 
ATOM   17246 C  CD2 . LEU F  2 155 ? 2.995   -55.650 -20.244  1.00 276.63 ? 265  LEU F CD2 1 
ATOM   17247 N  N   . ALA F  2 156 ? 3.897   -50.340 -19.415  1.00 259.24 ? 266  ALA F N   1 
ATOM   17248 C  CA  . ALA F  2 156 ? 3.927   -49.080 -18.693  1.00 256.61 ? 266  ALA F CA  1 
ATOM   17249 C  C   . ALA F  2 156 ? 2.892   -48.089 -19.195  1.00 262.70 ? 266  ALA F C   1 
ATOM   17250 O  O   . ALA F  2 156 ? 2.640   -47.089 -18.516  1.00 262.63 ? 266  ALA F O   1 
ATOM   17251 C  CB  . ALA F  2 156 ? 5.319   -48.454 -18.790  1.00 247.75 ? 266  ALA F CB  1 
ATOM   17252 N  N   . GLY F  2 157 ? 2.294   -48.341 -20.355  1.00 268.47 ? 267  GLY F N   1 
ATOM   17253 C  CA  . GLY F  2 157 ? 1.371   -47.400 -20.947  1.00 274.72 ? 267  GLY F CA  1 
ATOM   17254 C  C   . GLY F  2 157 ? 1.997   -46.489 -21.973  1.00 272.13 ? 267  GLY F C   1 
ATOM   17255 O  O   . GLY F  2 157 ? 1.488   -45.385 -22.207  1.00 275.54 ? 267  GLY F O   1 
ATOM   17256 N  N   . ILE F  2 158 ? 3.094   -46.911 -22.587  1.00 266.65 ? 268  ILE F N   1 
ATOM   17257 C  CA  . ILE F  2 158 ? 3.808   -46.128 -23.585  1.00 264.17 ? 268  ILE F CA  1 
ATOM   17258 C  C   . ILE F  2 158 ? 3.673   -46.860 -24.915  1.00 268.74 ? 268  ILE F C   1 
ATOM   17259 O  O   . ILE F  2 158 ? 4.169   -47.984 -25.066  1.00 266.68 ? 268  ILE F O   1 
ATOM   17260 C  CB  . ILE F  2 158 ? 5.276   -45.931 -23.192  1.00 254.24 ? 268  ILE F CB  1 
ATOM   17261 C  CG1 . ILE F  2 158 ? 5.382   -45.498 -21.724  1.00 250.42 ? 268  ILE F CG1 1 
ATOM   17262 C  CG2 . ILE F  2 158 ? 5.931   -44.901 -24.090  1.00 253.46 ? 268  ILE F CG2 1 
ATOM   17263 C  CD1 . ILE F  2 158 ? 6.808   -45.404 -21.211  1.00 241.24 ? 268  ILE F CD1 1 
ATOM   17264 N  N   . VAL F  2 159 ? 2.979   -46.247 -25.876  1.00 275.71 ? 269  VAL F N   1 
ATOM   17265 C  CA  . VAL F  2 159 ? 2.735   -46.878 -27.165  1.00 281.64 ? 269  VAL F CA  1 
ATOM   17266 C  C   . VAL F  2 159 ? 3.203   -46.023 -28.339  1.00 282.41 ? 269  VAL F C   1 
ATOM   17267 O  O   . VAL F  2 159 ? 2.977   -46.393 -29.492  1.00 288.31 ? 269  VAL F O   1 
ATOM   17268 C  CB  . VAL F  2 159 ? 1.253   -47.264 -27.326  1.00 292.25 ? 269  VAL F CB  1 
ATOM   17269 C  CG1 . VAL F  2 159 ? 0.910   -48.414 -26.397  1.00 292.36 ? 269  VAL F CG1 1 
ATOM   17270 C  CG2 . VAL F  2 159 ? 0.375   -46.073 -27.031  1.00 296.71 ? 269  VAL F CG2 1 
ATOM   17271 N  N   . CYS F  2 160 ? 3.849   -44.878 -28.076  1.00 277.25 ? 270  CYS F N   1 
ATOM   17272 C  CA  . CYS F  2 160 ? 4.436   -44.075 -29.152  1.00 277.69 ? 270  CYS F CA  1 
ATOM   17273 C  C   . CYS F  2 160 ? 5.840   -44.591 -29.448  1.00 270.06 ? 270  CYS F C   1 
ATOM   17274 O  O   . CYS F  2 160 ? 6.697   -44.562 -28.553  1.00 261.62 ? 270  CYS F O   1 
ATOM   17275 C  CB  . CYS F  2 160 ? 4.508   -42.595 -28.784  1.00 276.55 ? 270  CYS F CB  1 
ATOM   17276 S  SG  . CYS F  2 160 ? 2.964   -41.681 -28.421  1.00 285.53 ? 270  CYS F SG  1 
ATOM   17277 N  N   . PRO F  2 161 ? 6.111   -45.085 -30.659  1.00 273.12 ? 271  PRO F N   1 
ATOM   17278 C  CA  . PRO F  2 161 ? 7.437   -45.643 -30.965  1.00 271.97 ? 271  PRO F CA  1 
ATOM   17279 C  C   . PRO F  2 161 ? 8.546   -44.602 -30.865  1.00 274.70 ? 271  PRO F C   1 
ATOM   17280 O  O   . PRO F  2 161 ? 8.308   -43.393 -30.858  1.00 280.20 ? 271  PRO F O   1 
ATOM   17281 C  CB  . PRO F  2 161 ? 7.283   -46.150 -32.406  1.00 273.48 ? 271  PRO F CB  1 
ATOM   17282 C  CG  . PRO F  2 161 ? 5.809   -46.348 -32.593  1.00 283.34 ? 271  PRO F CG  1 
ATOM   17283 C  CD  . PRO F  2 161 ? 5.164   -45.261 -31.773  1.00 283.69 ? 271  PRO F CD  1 
ATOM   17284 N  N   . ASN F  2 162 ? 9.782   -45.097 -30.782  1.00 274.56 ? 272  ASN F N   1 
ATOM   17285 C  CA  . ASN F  2 162 ? 10.957  -44.232 -30.730  1.00 272.46 ? 272  ASN F CA  1 
ATOM   17286 C  C   . ASN F  2 162 ? 11.339  -43.789 -32.141  1.00 274.59 ? 272  ASN F C   1 
ATOM   17287 O  O   . ASN F  2 162 ? 11.569  -44.627 -33.020  1.00 273.67 ? 272  ASN F O   1 
ATOM   17288 C  CB  . ASN F  2 162 ? 12.121  -44.955 -30.054  1.00 267.99 ? 272  ASN F CB  1 
ATOM   17289 C  CG  . ASN F  2 162 ? 13.261  -44.016 -29.682  1.00 269.46 ? 272  ASN F CG  1 
ATOM   17290 O  OD1 . ASN F  2 162 ? 14.130  -43.716 -30.502  1.00 268.45 ? 272  ASN F OD1 1 
ATOM   17291 N  ND2 . ASN F  2 162 ? 13.269  -43.562 -28.433  1.00 261.65 ? 272  ASN F ND2 1 
ATOM   17292 N  N   . ASP F  2 163 ? 11.381  -42.473 -32.364  1.00 270.85 ? 273  ASP F N   1 
ATOM   17293 C  CA  . ASP F  2 163 ? 11.728  -41.914 -33.665  1.00 271.06 ? 273  ASP F CA  1 
ATOM   17294 C  C   . ASP F  2 163 ? 13.219  -41.980 -33.967  1.00 267.59 ? 273  ASP F C   1 
ATOM   17295 O  O   . ASP F  2 163 ? 13.612  -41.755 -35.117  1.00 269.22 ? 273  ASP F O   1 
ATOM   17296 C  CB  . ASP F  2 163 ? 11.262  -40.457 -33.754  1.00 273.29 ? 273  ASP F CB  1 
ATOM   17297 C  CG  . ASP F  2 163 ? 11.735  -39.618 -32.580  1.00 274.13 ? 273  ASP F CG  1 
ATOM   17298 O  OD1 . ASP F  2 163 ? 12.569  -40.107 -31.787  1.00 264.95 ? 273  ASP F OD1 1 
ATOM   17299 O  OD2 . ASP F  2 163 ? 11.270  -38.467 -32.447  1.00 286.51 ? 273  ASP F OD2 1 
ATOM   17300 N  N   . GLY F  2 164 ? 14.051  -42.268 -32.971  1.00 262.87 ? 274  GLY F N   1 
ATOM   17301 C  CA  . GLY F  2 164 ? 15.482  -42.302 -33.172  1.00 256.93 ? 274  GLY F CA  1 
ATOM   17302 C  C   . GLY F  2 164 ? 16.046  -40.926 -33.436  1.00 257.02 ? 274  GLY F C   1 
ATOM   17303 O  O   . GLY F  2 164 ? 16.783  -40.718 -34.405  1.00 265.28 ? 274  GLY F O   1 
ATOM   17304 N  N   . LEU F  2 165 ? 15.695  -39.970 -32.582  1.00 247.82 ? 275  LEU F N   1 
ATOM   17305 C  CA  . LEU F  2 165 ? 16.159  -38.599 -32.709  1.00 251.35 ? 275  LEU F CA  1 
ATOM   17306 C  C   . LEU F  2 165 ? 16.765  -38.154 -31.387  1.00 262.17 ? 275  LEU F C   1 
ATOM   17307 O  O   . LEU F  2 165 ? 16.766  -38.890 -30.395  1.00 267.88 ? 275  LEU F O   1 
ATOM   17308 C  CB  . LEU F  2 165 ? 15.022  -37.667 -33.138  1.00 248.06 ? 275  LEU F CB  1 
ATOM   17309 C  CG  . LEU F  2 165 ? 14.463  -37.976 -34.524  1.00 254.04 ? 275  LEU F CG  1 
ATOM   17310 C  CD1 . LEU F  2 165 ? 13.318  -37.038 -34.848  1.00 263.17 ? 275  LEU F CD1 1 
ATOM   17311 C  CD2 . LEU F  2 165 ? 15.562  -37.882 -35.572  1.00 255.17 ? 275  LEU F CD2 1 
ATOM   17312 N  N   . CYS F  2 166 ? 17.293  -36.932 -31.380  1.00 269.63 ? 276  CYS F N   1 
ATOM   17313 C  CA  . CYS F  2 166 ? 17.961  -36.387 -30.203  1.00 276.63 ? 276  CYS F CA  1 
ATOM   17314 C  C   . CYS F  2 166 ? 16.924  -35.781 -29.261  1.00 277.82 ? 276  CYS F C   1 
ATOM   17315 O  O   . CYS F  2 166 ? 16.293  -34.768 -29.585  1.00 278.85 ? 276  CYS F O   1 
ATOM   17316 C  CB  . CYS F  2 166 ? 19.010  -35.360 -30.617  1.00 278.15 ? 276  CYS F CB  1 
ATOM   17317 S  SG  . CYS F  2 166 ? 20.138  -34.911 -29.282  1.00 298.79 ? 276  CYS F SG  1 
ATOM   17318 N  N   . HIS F  2 167 ? 16.731  -36.415 -28.102  1.00 271.89 ? 277  HIS F N   1 
ATOM   17319 C  CA  . HIS F  2 167 ? 15.767  -35.950 -27.109  1.00 260.71 ? 277  HIS F CA  1 
ATOM   17320 C  C   . HIS F  2 167 ? 16.428  -35.701 -25.757  1.00 249.52 ? 277  HIS F C   1 
ATOM   17321 O  O   . HIS F  2 167 ? 16.063  -36.329 -24.758  1.00 252.15 ? 277  HIS F O   1 
ATOM   17322 C  CB  . HIS F  2 167 ? 14.631  -36.964 -26.954  1.00 250.48 ? 277  HIS F CB  1 
ATOM   17323 C  CG  . HIS F  2 167 ? 13.759  -37.085 -28.165  1.00 245.11 ? 277  HIS F CG  1 
ATOM   17324 N  ND1 . HIS F  2 167 ? 12.949  -36.061 -28.605  1.00 243.65 ? 277  HIS F ND1 1 
ATOM   17325 C  CD2 . HIS F  2 167 ? 13.573  -38.110 -29.030  1.00 243.33 ? 277  HIS F CD2 1 
ATOM   17326 C  CE1 . HIS F  2 167 ? 12.300  -36.449 -29.688  1.00 246.90 ? 277  HIS F CE1 1 
ATOM   17327 N  NE2 . HIS F  2 167 ? 12.662  -37.689 -29.967  1.00 249.10 ? 277  HIS F NE2 1 
ATOM   17328 N  N   . LEU F  2 168 ? 17.403  -34.796 -25.711  1.00 227.08 ? 278  LEU F N   1 
ATOM   17329 C  CA  . LEU F  2 168 ? 18.086  -34.434 -24.475  1.00 211.28 ? 278  LEU F CA  1 
ATOM   17330 C  C   . LEU F  2 168 ? 17.684  -33.018 -24.081  1.00 216.09 ? 278  LEU F C   1 
ATOM   17331 O  O   . LEU F  2 168 ? 17.883  -32.072 -24.853  1.00 220.39 ? 278  LEU F O   1 
ATOM   17332 C  CB  . LEU F  2 168 ? 19.602  -34.559 -24.629  1.00 206.00 ? 278  LEU F CB  1 
ATOM   17333 C  CG  . LEU F  2 168 ? 20.110  -35.968 -24.951  1.00 201.18 ? 278  LEU F CG  1 
ATOM   17334 C  CD1 . LEU F  2 168 ? 21.615  -35.977 -25.154  1.00 198.80 ? 278  LEU F CD1 1 
ATOM   17335 C  CD2 . LEU F  2 168 ? 19.713  -36.936 -23.853  1.00 197.63 ? 278  LEU F CD2 1 
ATOM   17336 N  N   . ASP F  2 169 ? 17.116  -32.879 -22.883  1.00 222.90 ? 279  ASP F N   1 
ATOM   17337 C  CA  . ASP F  2 169 ? 16.622  -31.597 -22.394  1.00 241.26 ? 279  ASP F CA  1 
ATOM   17338 C  C   . ASP F  2 169 ? 17.741  -30.683 -21.910  1.00 232.13 ? 279  ASP F C   1 
ATOM   17339 O  O   . ASP F  2 169 ? 18.922  -30.930 -22.181  1.00 219.80 ? 279  ASP F O   1 
ATOM   17340 C  CB  . ASP F  2 169 ? 15.618  -31.823 -21.259  1.00 250.72 ? 279  ASP F CB  1 
ATOM   17341 C  CG  . ASP F  2 169 ? 16.131  -32.802 -20.202  1.00 229.76 ? 279  ASP F CG  1 
ATOM   17342 O  OD1 . ASP F  2 169 ? 17.355  -33.051 -20.146  1.00 214.36 ? 279  ASP F OD1 1 
ATOM   17343 O  OD2 . ASP F  2 169 ? 15.307  -33.328 -19.423  1.00 216.76 ? 279  ASP F OD2 1 
ATOM   17344 N  N   . SER F  2 170 ? 17.372  -29.626 -21.180  1.00 230.85 ? 280  SER F N   1 
ATOM   17345 C  CA  . SER F  2 170 ? 18.362  -28.706 -20.638  1.00 223.84 ? 280  SER F CA  1 
ATOM   17346 C  C   . SER F  2 170 ? 19.190  -29.355 -19.543  1.00 220.30 ? 280  SER F C   1 
ATOM   17347 O  O   . SER F  2 170 ? 20.296  -28.886 -19.250  1.00 217.21 ? 280  SER F O   1 
ATOM   17348 C  CB  . SER F  2 170 ? 17.674  -27.451 -20.099  1.00 229.57 ? 280  SER F CB  1 
ATOM   17349 O  OG  . SER F  2 170 ? 16.681  -27.794 -19.146  1.00 230.09 ? 280  SER F OG  1 
ATOM   17350 N  N   . LYS F  2 171 ? 18.685  -30.426 -18.941  1.00 220.36 ? 281  LYS F N   1 
ATOM   17351 C  CA  . LYS F  2 171 ? 19.416  -31.185 -17.943  1.00 213.51 ? 281  LYS F CA  1 
ATOM   17352 C  C   . LYS F  2 171 ? 20.299  -32.246 -18.573  1.00 213.70 ? 281  LYS F C   1 
ATOM   17353 O  O   . LYS F  2 171 ? 20.914  -33.036 -17.849  1.00 214.09 ? 281  LYS F O   1 
ATOM   17354 C  CB  . LYS F  2 171 ? 18.436  -31.832 -16.959  1.00 218.82 ? 281  LYS F CB  1 
ATOM   17355 C  CG  . LYS F  2 171 ? 17.629  -30.826 -16.148  1.00 235.68 ? 281  LYS F CG  1 
ATOM   17356 C  CD  . LYS F  2 171 ? 16.648  -31.508 -15.208  1.00 243.27 ? 281  LYS F CD  1 
ATOM   17357 C  CE  . LYS F  2 171 ? 15.857  -30.484 -14.406  1.00 250.33 ? 281  LYS F CE  1 
ATOM   17358 N  NZ  . LYS F  2 171 ? 14.879  -31.131 -13.490  1.00 253.19 ? 281  LYS F NZ  1 
ATOM   17359 N  N   . ASN F  2 172 ? 20.374  -32.274 -19.905  1.00 209.96 ? 282  ASN F N   1 
ATOM   17360 C  CA  . ASN F  2 172 ? 21.123  -33.280 -20.651  1.00 210.15 ? 282  ASN F CA  1 
ATOM   17361 C  C   . ASN F  2 172 ? 20.652  -34.692 -20.323  1.00 207.95 ? 282  ASN F C   1 
ATOM   17362 O  O   . ASN F  2 172 ? 21.449  -35.635 -20.292  1.00 203.27 ? 282  ASN F O   1 
ATOM   17363 C  CB  . ASN F  2 172 ? 22.628  -33.144 -20.407  1.00 208.60 ? 282  ASN F CB  1 
ATOM   17364 C  CG  . ASN F  2 172 ? 23.250  -32.035 -21.221  1.00 218.13 ? 282  ASN F CG  1 
ATOM   17365 O  OD1 . ASN F  2 172 ? 22.853  -31.793 -22.360  1.00 221.02 ? 282  ASN F OD1 1 
ATOM   17366 N  ND2 . ASN F  2 172 ? 24.233  -31.355 -20.645  1.00 223.23 ? 282  ASN F ND2 1 
ATOM   17367 N  N   . GLU F  2 173 ? 19.357  -34.850 -20.077  1.00 219.23 ? 283  GLU F N   1 
ATOM   17368 C  CA  . GLU F  2 173 ? 18.764  -36.141 -19.773  1.00 219.84 ? 283  GLU F CA  1 
ATOM   17369 C  C   . GLU F  2 173 ? 17.797  -36.536 -20.879  1.00 216.47 ? 283  GLU F C   1 
ATOM   17370 O  O   . GLU F  2 173 ? 17.353  -35.704 -21.673  1.00 219.00 ? 283  GLU F O   1 
ATOM   17371 C  CB  . GLU F  2 173 ? 18.032  -36.107 -18.428  1.00 237.22 ? 283  GLU F CB  1 
ATOM   17372 C  CG  . GLU F  2 173 ? 18.863  -35.541 -17.292  1.00 244.31 ? 283  GLU F CG  1 
ATOM   17373 C  CD  . GLU F  2 173 ? 18.101  -35.481 -15.983  1.00 247.89 ? 283  GLU F CD  1 
ATOM   17374 O  OE1 . GLU F  2 173 ? 17.069  -36.175 -15.865  1.00 252.23 ? 283  GLU F OE1 1 
ATOM   17375 O  OE2 . GLU F  2 173 ? 18.537  -34.746 -15.071  1.00 241.00 ? 283  GLU F OE2 1 
ATOM   17376 N  N   . TYR F  2 174 ? 17.464  -37.824 -20.918  1.00 207.42 ? 284  TYR F N   1 
ATOM   17377 C  CA  . TYR F  2 174 ? 16.462  -38.305 -21.859  1.00 213.86 ? 284  TYR F CA  1 
ATOM   17378 C  C   . TYR F  2 174 ? 15.084  -37.822 -21.421  1.00 228.72 ? 284  TYR F C   1 
ATOM   17379 O  O   . TYR F  2 174 ? 14.435  -38.454 -20.582  1.00 236.29 ? 284  TYR F O   1 
ATOM   17380 C  CB  . TYR F  2 174 ? 16.506  -39.831 -21.956  1.00 218.79 ? 284  TYR F CB  1 
ATOM   17381 C  CG  . TYR F  2 174 ? 15.764  -40.419 -23.140  1.00 236.65 ? 284  TYR F CG  1 
ATOM   17382 C  CD1 . TYR F  2 174 ? 15.149  -39.605 -24.084  1.00 245.34 ? 284  TYR F CD1 1 
ATOM   17383 C  CD2 . TYR F  2 174 ? 15.670  -41.794 -23.306  1.00 248.64 ? 284  TYR F CD2 1 
ATOM   17384 C  CE1 . TYR F  2 174 ? 14.467  -40.147 -25.161  1.00 255.97 ? 284  TYR F CE1 1 
ATOM   17385 C  CE2 . TYR F  2 174 ? 14.991  -42.344 -24.379  1.00 250.08 ? 284  TYR F CE2 1 
ATOM   17386 C  CZ  . TYR F  2 174 ? 14.391  -41.518 -25.303  1.00 253.75 ? 284  TYR F CZ  1 
ATOM   17387 O  OH  . TYR F  2 174 ? 13.716  -42.067 -26.369  1.00 249.99 ? 284  TYR F OH  1 
ATOM   17388 N  N   . SER F  2 175 ? 14.644  -36.685 -21.969  1.00 238.76 ? 285  SER F N   1 
ATOM   17389 C  CA  . SER F  2 175 ? 13.361  -36.108 -21.578  1.00 240.47 ? 285  SER F CA  1 
ATOM   17390 C  C   . SER F  2 175 ? 12.186  -36.908 -22.123  1.00 237.83 ? 285  SER F C   1 
ATOM   17391 O  O   . SER F  2 175 ? 11.131  -36.975 -21.483  1.00 231.79 ? 285  SER F O   1 
ATOM   17392 C  CB  . SER F  2 175 ? 13.270  -34.658 -22.055  1.00 252.30 ? 285  SER F CB  1 
ATOM   17393 O  OG  . SER F  2 175 ? 13.341  -34.581 -23.470  1.00 251.33 ? 285  SER F OG  1 
ATOM   17394 N  N   . MET F  2 176 ? 12.339  -37.505 -23.299  1.00 235.40 ? 286  MET F N   1 
ATOM   17395 C  CA  . MET F  2 176 ? 11.272  -38.287 -23.924  1.00 241.29 ? 286  MET F CA  1 
ATOM   17396 C  C   . MET F  2 176 ? 11.453  -39.774 -23.654  1.00 244.66 ? 286  MET F C   1 
ATOM   17397 O  O   . MET F  2 176 ? 11.303  -40.611 -24.544  1.00 239.47 ? 286  MET F O   1 
ATOM   17398 C  CB  . MET F  2 176 ? 11.227  -38.000 -25.419  1.00 237.91 ? 286  MET F CB  1 
ATOM   17399 C  CG  . MET F  2 176 ? 11.167  -36.521 -25.756  1.00 238.49 ? 286  MET F CG  1 
ATOM   17400 S  SD  . MET F  2 176 ? 9.627   -35.760 -25.217  1.00 246.22 ? 286  MET F SD  1 
ATOM   17401 C  CE  . MET F  2 176 ? 8.480   -36.488 -26.381  1.00 253.99 ? 286  MET F CE  1 
ATOM   17402 N  N   . SER F  2 177 ? 11.775  -40.115 -22.405  1.00 248.57 ? 287  SER F N   1 
ATOM   17403 C  CA  . SER F  2 177 ? 11.943  -41.505 -21.996  1.00 235.07 ? 287  SER F CA  1 
ATOM   17404 C  C   . SER F  2 177 ? 10.623  -42.128 -21.571  1.00 243.54 ? 287  SER F C   1 
ATOM   17405 O  O   . SER F  2 177 ? 10.365  -43.298 -21.869  1.00 256.49 ? 287  SER F O   1 
ATOM   17406 C  CB  . SER F  2 177 ? 12.962  -41.612 -20.856  1.00 221.09 ? 287  SER F CB  1 
ATOM   17407 O  OG  . SER F  2 177 ? 13.166  -42.965 -20.479  1.00 220.42 ? 287  SER F OG  1 
ATOM   17408 N  N   . THR F  2 178 ? 9.776   -41.363 -20.888  1.00 235.19 ? 288  THR F N   1 
ATOM   17409 C  CA  . THR F  2 178 ? 8.452   -41.819 -20.492  1.00 232.33 ? 288  THR F CA  1 
ATOM   17410 C  C   . THR F  2 178 ? 7.423   -41.559 -21.573  1.00 239.93 ? 288  THR F C   1 
ATOM   17411 O  O   . THR F  2 178 ? 6.237   -41.838 -21.369  1.00 245.87 ? 288  THR F O   1 
ATOM   17412 C  CB  . THR F  2 178 ? 8.007   -41.118 -19.208  1.00 233.36 ? 288  THR F CB  1 
ATOM   17413 O  OG1 . THR F  2 178 ? 7.727   -39.740 -19.493  1.00 236.68 ? 288  THR F OG1 1 
ATOM   17414 C  CG2 . THR F  2 178 ? 9.098   -41.197 -18.158  1.00 226.46 ? 288  THR F CG2 1 
ATOM   17415 N  N   . VAL F  2 179 ? 7.856   -41.022 -22.709  1.00 240.68 ? 289  VAL F N   1 
ATOM   17416 C  CA  . VAL F  2 179 ? 6.962   -40.708 -23.802  1.00 256.77 ? 289  VAL F CA  1 
ATOM   17417 C  C   . VAL F  2 179 ? 7.160   -41.645 -24.985  1.00 257.04 ? 289  VAL F C   1 
ATOM   17418 O  O   . VAL F  2 179 ? 6.193   -41.932 -25.699  1.00 269.82 ? 289  VAL F O   1 
ATOM   17419 C  CB  . VAL F  2 179 ? 7.137   -39.237 -24.235  1.00 259.32 ? 289  VAL F CB  1 
ATOM   17420 C  CG1 . VAL F  2 179 ? 5.943   -38.779 -25.066  1.00 270.76 ? 289  VAL F CG1 1 
ATOM   17421 C  CG2 . VAL F  2 179 ? 7.333   -38.346 -23.017  1.00 258.82 ? 289  VAL F CG2 1 
ATOM   17422 N  N   . LEU F  2 180 ? 8.372   -42.143 -25.200  1.00 242.79 ? 290  LEU F N   1 
ATOM   17423 C  CA  . LEU F  2 180 ? 8.692   -42.971 -26.348  1.00 245.47 ? 290  LEU F CA  1 
ATOM   17424 C  C   . LEU F  2 180 ? 9.014   -44.395 -25.916  1.00 248.80 ? 290  LEU F C   1 
ATOM   17425 O  O   . LEU F  2 180 ? 9.539   -44.631 -24.823  1.00 246.99 ? 290  LEU F O   1 
ATOM   17426 C  CB  . LEU F  2 180 ? 9.882   -42.390 -27.112  1.00 241.98 ? 290  LEU F CB  1 
ATOM   17427 C  CG  . LEU F  2 180 ? 9.754   -40.906 -27.450  1.00 244.24 ? 290  LEU F CG  1 
ATOM   17428 C  CD1 . LEU F  2 180 ? 10.991  -40.421 -28.186  1.00 246.66 ? 290  LEU F CD1 1 
ATOM   17429 C  CD2 . LEU F  2 180 ? 8.497   -40.656 -28.266  1.00 258.35 ? 290  LEU F CD2 1 
ATOM   17430 N  N   . GLU F  2 181 ? 8.713   -45.344 -26.799  1.00 244.14 ? 291  GLU F N   1 
ATOM   17431 C  CA  . GLU F  2 181 ? 9.064   -46.730 -26.551  1.00 242.23 ? 291  GLU F CA  1 
ATOM   17432 C  C   . GLU F  2 181 ? 10.577  -46.910 -26.582  1.00 238.93 ? 291  GLU F C   1 
ATOM   17433 O  O   . GLU F  2 181 ? 11.333  -46.032 -27.009  1.00 233.27 ? 291  GLU F O   1 
ATOM   17434 C  CB  . GLU F  2 181 ? 8.429   -47.651 -27.591  1.00 248.86 ? 291  GLU F CB  1 
ATOM   17435 C  CG  . GLU F  2 181 ? 6.919   -47.681 -27.577  1.00 268.53 ? 291  GLU F CG  1 
ATOM   17436 C  CD  . GLU F  2 181 ? 6.360   -48.579 -28.662  1.00 280.97 ? 291  GLU F CD  1 
ATOM   17437 O  OE1 . GLU F  2 181 ? 7.151   -49.045 -29.511  1.00 274.85 ? 291  GLU F OE1 1 
ATOM   17438 O  OE2 . GLU F  2 181 ? 5.131   -48.808 -28.676  1.00 294.12 ? 291  GLU F OE2 1 
ATOM   17439 N  N   . TYR F  2 182 ? 11.014  -48.070 -26.108  1.00 250.57 ? 292  TYR F N   1 
ATOM   17440 C  CA  . TYR F  2 182 ? 12.388  -48.475 -26.320  1.00 251.82 ? 292  TYR F CA  1 
ATOM   17441 C  C   . TYR F  2 182 ? 12.616  -48.720 -27.812  1.00 251.73 ? 292  TYR F C   1 
ATOM   17442 O  O   . TYR F  2 182 ? 11.691  -49.102 -28.533  1.00 253.48 ? 292  TYR F O   1 
ATOM   17443 C  CB  . TYR F  2 182 ? 12.704  -49.747 -25.540  1.00 256.60 ? 292  TYR F CB  1 
ATOM   17444 C  CG  . TYR F  2 182 ? 12.439  -49.678 -24.051  1.00 256.92 ? 292  TYR F CG  1 
ATOM   17445 C  CD1 . TYR F  2 182 ? 11.200  -50.026 -23.524  1.00 257.19 ? 292  TYR F CD1 1 
ATOM   17446 C  CD2 . TYR F  2 182 ? 13.439  -49.292 -23.170  1.00 253.30 ? 292  TYR F CD2 1 
ATOM   17447 C  CE1 . TYR F  2 182 ? 10.964  -49.974 -22.160  1.00 248.69 ? 292  TYR F CE1 1 
ATOM   17448 C  CE2 . TYR F  2 182 ? 13.213  -49.238 -21.810  1.00 245.98 ? 292  TYR F CE2 1 
ATOM   17449 C  CZ  . TYR F  2 182 ? 11.977  -49.580 -21.309  1.00 238.70 ? 292  TYR F CZ  1 
ATOM   17450 O  OH  . TYR F  2 182 ? 11.760  -49.521 -19.951  1.00 232.15 ? 292  TYR F OH  1 
ATOM   17451 N  N   . PRO F  2 183 ? 13.827  -48.480 -28.306  1.00 246.96 ? 293  PRO F N   1 
ATOM   17452 C  CA  . PRO F  2 183 ? 14.127  -48.796 -29.705  1.00 248.15 ? 293  PRO F CA  1 
ATOM   17453 C  C   . PRO F  2 183 ? 14.353  -50.286 -29.915  1.00 237.88 ? 293  PRO F C   1 
ATOM   17454 O  O   . PRO F  2 183 ? 14.807  -51.005 -29.023  1.00 231.77 ? 293  PRO F O   1 
ATOM   17455 C  CB  . PRO F  2 183 ? 15.406  -47.997 -29.979  1.00 247.96 ? 293  PRO F CB  1 
ATOM   17456 C  CG  . PRO F  2 183 ? 16.061  -47.888 -28.650  1.00 242.91 ? 293  PRO F CG  1 
ATOM   17457 C  CD  . PRO F  2 183 ? 14.952  -47.799 -27.639  1.00 240.51 ? 293  PRO F CD  1 
ATOM   17458 N  N   . THR F  2 184 ? 14.019  -50.745 -31.119  1.00 233.14 ? 294  THR F N   1 
ATOM   17459 C  CA  . THR F  2 184 ? 14.248  -52.128 -31.505  1.00 234.90 ? 294  THR F CA  1 
ATOM   17460 C  C   . THR F  2 184 ? 15.648  -52.277 -32.094  1.00 230.47 ? 294  THR F C   1 
ATOM   17461 O  O   . THR F  2 184 ? 16.334  -51.294 -32.382  1.00 233.54 ? 294  THR F O   1 
ATOM   17462 C  CB  . THR F  2 184 ? 13.201  -52.588 -32.518  1.00 244.94 ? 294  THR F CB  1 
ATOM   17463 O  OG1 . THR F  2 184 ? 13.461  -51.971 -33.783  1.00 248.29 ? 294  THR F OG1 1 
ATOM   17464 C  CG2 . THR F  2 184 ? 11.806  -52.191 -32.056  1.00 250.35 ? 294  THR F CG2 1 
ATOM   17465 N  N   . ILE F  2 185 ? 16.073  -53.529 -32.277  1.00 230.76 ? 295  ILE F N   1 
ATOM   17466 C  CA  . ILE F  2 185 ? 17.369  -53.775 -32.906  1.00 227.51 ? 295  ILE F CA  1 
ATOM   17467 C  C   . ILE F  2 185 ? 17.380  -53.232 -34.329  1.00 232.79 ? 295  ILE F C   1 
ATOM   17468 O  O   . ILE F  2 185 ? 18.396  -52.708 -34.803  1.00 229.63 ? 295  ILE F O   1 
ATOM   17469 C  CB  . ILE F  2 185 ? 17.716  -55.275 -32.861  1.00 228.10 ? 295  ILE F CB  1 
ATOM   17470 C  CG1 . ILE F  2 185 ? 17.872  -55.741 -31.411  1.00 222.65 ? 295  ILE F CG1 1 
ATOM   17471 C  CG2 . ILE F  2 185 ? 18.987  -55.563 -33.655  1.00 226.07 ? 295  ILE F CG2 1 
ATOM   17472 C  CD1 . ILE F  2 185 ? 18.411  -57.149 -31.271  1.00 225.21 ? 295  ILE F CD1 1 
ATOM   17473 N  N   . GLY F  2 186 ? 16.245  -53.328 -35.023  1.00 241.51 ? 296  GLY F N   1 
ATOM   17474 C  CA  . GLY F  2 186 ? 16.148  -52.731 -36.345  1.00 254.51 ? 296  GLY F CA  1 
ATOM   17475 C  C   . GLY F  2 186 ? 16.363  -51.230 -36.322  1.00 245.48 ? 296  GLY F C   1 
ATOM   17476 O  O   . GLY F  2 186 ? 17.077  -50.680 -37.165  1.00 245.48 ? 296  GLY F O   1 
ATOM   17477 N  N   . GLN F  2 187 ? 15.751  -50.548 -35.352  1.00 249.53 ? 297  GLN F N   1 
ATOM   17478 C  CA  . GLN F  2 187 ? 15.931  -49.106 -35.234  1.00 254.10 ? 297  GLN F CA  1 
ATOM   17479 C  C   . GLN F  2 187 ? 17.372  -48.759 -34.885  1.00 244.30 ? 297  GLN F C   1 
ATOM   17480 O  O   . GLN F  2 187 ? 17.944  -47.819 -35.450  1.00 252.28 ? 297  GLN F O   1 
ATOM   17481 C  CB  . GLN F  2 187 ? 14.969  -48.548 -34.186  1.00 253.14 ? 297  GLN F CB  1 
ATOM   17482 C  CG  . GLN F  2 187 ? 13.496  -48.748 -34.516  1.00 262.51 ? 297  GLN F CG  1 
ATOM   17483 C  CD  . GLN F  2 187 ? 12.575  -48.110 -33.489  1.00 267.46 ? 297  GLN F CD  1 
ATOM   17484 O  OE1 . GLN F  2 187 ? 12.885  -47.062 -32.923  1.00 263.44 ? 297  GLN F OE1 1 
ATOM   17485 N  NE2 . GLN F  2 187 ? 11.437  -48.749 -33.237  1.00 270.47 ? 297  GLN F NE2 1 
ATOM   17486 N  N   . LEU F  2 188 ? 17.975  -49.507 -33.957  1.00 227.34 ? 298  LEU F N   1 
ATOM   17487 C  CA  . LEU F  2 188 ? 19.360  -49.245 -33.583  1.00 221.14 ? 298  LEU F CA  1 
ATOM   17488 C  C   . LEU F  2 188 ? 20.294  -49.443 -34.767  1.00 221.00 ? 298  LEU F C   1 
ATOM   17489 O  O   . LEU F  2 188 ? 21.216  -48.647 -34.981  1.00 218.91 ? 298  LEU F O   1 
ATOM   17490 C  CB  . LEU F  2 188 ? 19.768  -50.145 -32.419  1.00 216.74 ? 298  LEU F CB  1 
ATOM   17491 C  CG  . LEU F  2 188 ? 19.175  -49.770 -31.060  1.00 219.51 ? 298  LEU F CG  1 
ATOM   17492 C  CD1 . LEU F  2 188 ? 19.484  -50.841 -30.036  1.00 220.30 ? 298  LEU F CD1 1 
ATOM   17493 C  CD2 . LEU F  2 188 ? 19.700  -48.420 -30.591  1.00 221.61 ? 298  LEU F CD2 1 
ATOM   17494 N  N   . ILE F  2 189 ? 20.071  -50.502 -35.547  1.00 226.00 ? 299  ILE F N   1 
ATOM   17495 C  CA  . ILE F  2 189 ? 20.897  -50.739 -36.725  1.00 242.16 ? 299  ILE F CA  1 
ATOM   17496 C  C   . ILE F  2 189 ? 20.738  -49.598 -37.721  1.00 254.26 ? 299  ILE F C   1 
ATOM   17497 O  O   . ILE F  2 189 ? 21.709  -49.185 -38.368  1.00 258.37 ? 299  ILE F O   1 
ATOM   17498 C  CB  . ILE F  2 189 ? 20.545  -52.106 -37.346  1.00 245.03 ? 299  ILE F CB  1 
ATOM   17499 C  CG1 . ILE F  2 189 ? 21.026  -53.243 -36.439  1.00 231.54 ? 299  ILE F CG1 1 
ATOM   17500 C  CG2 . ILE F  2 189 ? 21.143  -52.246 -38.742  1.00 249.83 ? 299  ILE F CG2 1 
ATOM   17501 C  CD1 . ILE F  2 189 ? 20.681  -54.627 -36.947  1.00 232.15 ? 299  ILE F CD1 1 
ATOM   17502 N  N   . ASP F  2 190 ? 19.532  -49.033 -37.817  1.00 246.71 ? 300  ASP F N   1 
ATOM   17503 C  CA  . ASP F  2 190 ? 19.276  -47.961 -38.771  1.00 246.92 ? 300  ASP F CA  1 
ATOM   17504 C  C   . ASP F  2 190 ? 19.891  -46.635 -38.337  1.00 243.90 ? 300  ASP F C   1 
ATOM   17505 O  O   . ASP F  2 190 ? 20.061  -45.745 -39.176  1.00 248.57 ? 300  ASP F O   1 
ATOM   17506 C  CB  . ASP F  2 190 ? 17.764  -47.805 -38.980  1.00 251.36 ? 300  ASP F CB  1 
ATOM   17507 C  CG  . ASP F  2 190 ? 17.415  -46.858 -40.121  1.00 259.83 ? 300  ASP F CG  1 
ATOM   17508 O  OD1 . ASP F  2 190 ? 18.135  -46.854 -41.143  1.00 262.73 ? 300  ASP F OD1 1 
ATOM   17509 O  OD2 . ASP F  2 190 ? 16.412  -46.122 -39.998  1.00 264.12 ? 300  ASP F OD2 1 
ATOM   17510 N  N   . LYS F  2 191 ? 20.256  -46.488 -37.060  1.00 234.77 ? 301  LYS F N   1 
ATOM   17511 C  CA  . LYS F  2 191 ? 20.835  -45.248 -36.564  1.00 226.32 ? 301  LYS F CA  1 
ATOM   17512 C  C   . LYS F  2 191 ? 22.296  -45.380 -36.164  1.00 218.65 ? 301  LYS F C   1 
ATOM   17513 O  O   . LYS F  2 191 ? 22.972  -44.357 -36.010  1.00 217.65 ? 301  LYS F O   1 
ATOM   17514 C  CB  . LYS F  2 191 ? 20.032  -44.713 -35.367  1.00 224.05 ? 301  LYS F CB  1 
ATOM   17515 C  CG  . LYS F  2 191 ? 18.720  -44.037 -35.754  1.00 231.92 ? 301  LYS F CG  1 
ATOM   17516 C  CD  . LYS F  2 191 ? 18.956  -42.813 -36.636  1.00 236.70 ? 301  LYS F CD  1 
ATOM   17517 C  CE  . LYS F  2 191 ? 17.643  -42.236 -37.153  1.00 245.77 ? 301  LYS F CE  1 
ATOM   17518 N  NZ  . LYS F  2 191 ? 17.858  -41.030 -38.000  1.00 251.25 ? 301  LYS F NZ  1 
ATOM   17519 N  N   . LEU F  2 192 ? 22.806  -46.598 -36.011  1.00 215.29 ? 302  LEU F N   1 
ATOM   17520 C  CA  . LEU F  2 192 ? 24.217  -46.794 -35.722  1.00 211.03 ? 302  LEU F CA  1 
ATOM   17521 C  C   . LEU F  2 192 ? 25.057  -46.789 -36.985  1.00 212.75 ? 302  LEU F C   1 
ATOM   17522 O  O   . LEU F  2 192 ? 26.290  -46.829 -36.899  1.00 210.88 ? 302  LEU F O   1 
ATOM   17523 C  CB  . LEU F  2 192 ? 24.429  -48.108 -34.965  1.00 205.69 ? 302  LEU F CB  1 
ATOM   17524 C  CG  . LEU F  2 192 ? 24.030  -48.122 -33.489  1.00 204.27 ? 302  LEU F CG  1 
ATOM   17525 C  CD1 . LEU F  2 192 ? 24.335  -49.475 -32.876  1.00 199.63 ? 302  LEU F CD1 1 
ATOM   17526 C  CD2 . LEU F  2 192 ? 24.739  -47.016 -32.722  1.00 204.41 ? 302  LEU F CD2 1 
ATOM   17527 N  N   . VAL F  2 193 ? 24.418  -46.751 -38.149  1.00 220.22 ? 303  VAL F N   1 
ATOM   17528 C  CA  . VAL F  2 193 ? 25.111  -46.662 -39.420  1.00 224.75 ? 303  VAL F CA  1 
ATOM   17529 C  C   . VAL F  2 193 ? 25.007  -45.263 -40.009  1.00 230.73 ? 303  VAL F C   1 
ATOM   17530 O  O   . VAL F  2 193 ? 25.970  -44.759 -40.590  1.00 239.34 ? 303  VAL F O   1 
ATOM   17531 C  CB  . VAL F  2 193 ? 24.580  -47.722 -40.410  1.00 231.72 ? 303  VAL F CB  1 
ATOM   17532 C  CG1 . VAL F  2 193 ? 25.340  -47.650 -41.731  1.00 236.90 ? 303  VAL F CG1 1 
ATOM   17533 C  CG2 . VAL F  2 193 ? 24.688  -49.112 -39.811  1.00 227.64 ? 303  VAL F CG2 1 
ATOM   17534 N  N   . GLN F  2 194 ? 23.846  -44.618 -39.858  1.00 241.75 ? 304  GLN F N   1 
ATOM   17535 C  CA  . GLN F  2 194 ? 23.708  -43.224 -40.266  1.00 246.81 ? 304  GLN F CA  1 
ATOM   17536 C  C   . GLN F  2 194 ? 24.696  -42.340 -39.526  1.00 244.21 ? 304  GLN F C   1 
ATOM   17537 O  O   . GLN F  2 194 ? 25.125  -41.306 -40.051  1.00 250.29 ? 304  GLN F O   1 
ATOM   17538 C  CB  . GLN F  2 194 ? 22.284  -42.740 -40.011  1.00 246.10 ? 304  GLN F CB  1 
ATOM   17539 C  CG  . GLN F  2 194 ? 21.241  -43.336 -40.931  1.00 251.01 ? 304  GLN F CG  1 
ATOM   17540 C  CD  . GLN F  2 194 ? 19.853  -42.827 -40.615  1.00 255.39 ? 304  GLN F CD  1 
ATOM   17541 O  OE1 . GLN F  2 194 ? 19.688  -41.891 -39.832  1.00 252.70 ? 304  GLN F OE1 1 
ATOM   17542 N  NE2 . GLN F  2 194 ? 18.844  -43.445 -41.216  1.00 262.64 ? 304  GLN F NE2 1 
ATOM   17543 N  N   . ASN F  2 195 ? 25.057  -42.726 -38.307  1.00 237.79 ? 305  ASN F N   1 
ATOM   17544 C  CA  . ASN F  2 195 ? 26.066  -42.029 -37.529  1.00 239.68 ? 305  ASN F CA  1 
ATOM   17545 C  C   . ASN F  2 195 ? 27.387  -42.781 -37.500  1.00 240.69 ? 305  ASN F C   1 
ATOM   17546 O  O   . ASN F  2 195 ? 28.380  -42.241 -37.002  1.00 244.81 ? 305  ASN F O   1 
ATOM   17547 C  CB  . ASN F  2 195 ? 25.558  -41.806 -36.099  1.00 243.28 ? 305  ASN F CB  1 
ATOM   17548 C  CG  . ASN F  2 195 ? 24.100  -41.372 -36.057  1.00 251.31 ? 305  ASN F CG  1 
ATOM   17549 O  OD1 . ASN F  2 195 ? 23.656  -40.559 -36.869  1.00 258.69 ? 305  ASN F OD1 1 
ATOM   17550 N  ND2 . ASN F  2 195 ? 23.346  -41.923 -35.113  1.00 252.15 ? 305  ASN F ND2 1 
ATOM   17551 N  N   . ASN F  2 196 ? 27.412  -44.004 -38.035  1.00 238.62 ? 306  ASN F N   1 
ATOM   17552 C  CA  . ASN F  2 196 ? 28.596  -44.852 -38.093  1.00 241.84 ? 306  ASN F CA  1 
ATOM   17553 C  C   . ASN F  2 196 ? 29.204  -45.043 -36.708  1.00 234.20 ? 306  ASN F C   1 
ATOM   17554 O  O   . ASN F  2 196 ? 30.222  -44.423 -36.379  1.00 228.01 ? 306  ASN F O   1 
ATOM   17555 C  CB  . ASN F  2 196 ? 29.628  -44.263 -39.058  1.00 250.56 ? 306  ASN F CB  1 
ATOM   17556 C  CG  . ASN F  2 196 ? 30.794  -45.200 -39.308  1.00 254.34 ? 306  ASN F CG  1 
ATOM   17557 O  OD1 . ASN F  2 196 ? 30.644  -46.422 -39.260  1.00 247.49 ? 306  ASN F OD1 1 
ATOM   17558 N  ND2 . ASN F  2 196 ? 31.968  -44.630 -39.568  1.00 258.72 ? 306  ASN F ND2 1 
ATOM   17559 N  N   . VAL F  2 197 ? 28.589  -45.898 -35.893  1.00 226.91 ? 307  VAL F N   1 
ATOM   17560 C  CA  . VAL F  2 197 ? 29.011  -46.137 -34.517  1.00 217.94 ? 307  VAL F CA  1 
ATOM   17561 C  C   . VAL F  2 197 ? 29.274  -47.626 -34.335  1.00 227.72 ? 307  VAL F C   1 
ATOM   17562 O  O   . VAL F  2 197 ? 28.438  -48.459 -34.703  1.00 235.40 ? 307  VAL F O   1 
ATOM   17563 C  CB  . VAL F  2 197 ? 27.956  -45.644 -33.510  1.00 216.05 ? 307  VAL F CB  1 
ATOM   17564 C  CG1 . VAL F  2 197 ? 28.440  -45.851 -32.088  1.00 211.91 ? 307  VAL F CG1 1 
ATOM   17565 C  CG2 . VAL F  2 197 ? 27.633  -44.181 -33.751  1.00 222.37 ? 307  VAL F CG2 1 
ATOM   17566 N  N   . LEU F  2 198 ? 30.441  -47.956 -33.780  1.00 232.46 ? 308  LEU F N   1 
ATOM   17567 C  CA  . LEU F  2 198 ? 30.793  -49.331 -33.433  1.00 224.34 ? 308  LEU F CA  1 
ATOM   17568 C  C   . LEU F  2 198 ? 30.442  -49.579 -31.968  1.00 210.54 ? 308  LEU F C   1 
ATOM   17569 O  O   . LEU F  2 198 ? 31.029  -48.971 -31.067  1.00 206.81 ? 308  LEU F O   1 
ATOM   17570 C  CB  . LEU F  2 198 ? 32.271  -49.599 -33.701  1.00 224.08 ? 308  LEU F CB  1 
ATOM   17571 C  CG  . LEU F  2 198 ? 32.730  -49.548 -35.159  1.00 234.05 ? 308  LEU F CG  1 
ATOM   17572 C  CD1 . LEU F  2 198 ? 34.210  -49.874 -35.252  1.00 232.03 ? 308  LEU F CD1 1 
ATOM   17573 C  CD2 . LEU F  2 198 ? 31.917  -50.509 -36.020  1.00 247.74 ? 308  LEU F CD2 1 
ATOM   17574 N  N   . LEU F  2 199 ? 29.483  -50.473 -31.733  1.00 201.84 ? 309  LEU F N   1 
ATOM   17575 C  CA  . LEU F  2 199 ? 28.941  -50.730 -30.401  1.00 202.69 ? 309  LEU F CA  1 
ATOM   17576 C  C   . LEU F  2 199 ? 29.662  -51.923 -29.778  1.00 210.49 ? 309  LEU F C   1 
ATOM   17577 O  O   . LEU F  2 199 ? 29.539  -53.054 -30.260  1.00 225.16 ? 309  LEU F O   1 
ATOM   17578 C  CB  . LEU F  2 199 ? 27.436  -50.979 -30.481  1.00 207.45 ? 309  LEU F CB  1 
ATOM   17579 C  CG  . LEU F  2 199 ? 26.671  -51.108 -29.165  1.00 201.37 ? 309  LEU F CG  1 
ATOM   17580 C  CD1 . LEU F  2 199 ? 26.872  -49.860 -28.329  1.00 203.42 ? 309  LEU F CD1 1 
ATOM   17581 C  CD2 . LEU F  2 199 ? 25.197  -51.332 -29.435  1.00 202.98 ? 309  LEU F CD2 1 
ATOM   17582 N  N   . ILE F  2 200 ? 30.419  -51.670 -28.715  1.00 205.82 ? 310  ILE F N   1 
ATOM   17583 C  CA  . ILE F  2 200 ? 31.129  -52.710 -27.978  1.00 196.61 ? 310  ILE F CA  1 
ATOM   17584 C  C   . ILE F  2 200 ? 30.292  -53.112 -26.772  1.00 200.99 ? 310  ILE F C   1 
ATOM   17585 O  O   . ILE F  2 200 ? 29.994  -52.278 -25.908  1.00 204.33 ? 310  ILE F O   1 
ATOM   17586 C  CB  . ILE F  2 200 ? 32.522  -52.237 -27.545  1.00 194.93 ? 310  ILE F CB  1 
ATOM   17587 C  CG1 . ILE F  2 200 ? 33.398  -51.976 -28.769  1.00 202.92 ? 310  ILE F CG1 1 
ATOM   17588 C  CG2 . ILE F  2 200 ? 33.150  -53.253 -26.617  1.00 194.02 ? 310  ILE F CG2 1 
ATOM   17589 C  CD1 . ILE F  2 200 ? 34.762  -51.433 -28.424  1.00 202.37 ? 310  ILE F CD1 1 
ATOM   17590 N  N   . PHE F  2 201 ? 29.911  -54.385 -26.711  1.00 209.23 ? 311  PHE F N   1 
ATOM   17591 C  CA  . PHE F  2 201 ? 29.167  -54.929 -25.579  1.00 211.40 ? 311  PHE F CA  1 
ATOM   17592 C  C   . PHE F  2 201 ? 30.139  -55.426 -24.513  1.00 209.58 ? 311  PHE F C   1 
ATOM   17593 O  O   . PHE F  2 201 ? 30.990  -56.276 -24.794  1.00 216.72 ? 311  PHE F O   1 
ATOM   17594 C  CB  . PHE F  2 201 ? 28.250  -56.063 -26.033  1.00 210.06 ? 311  PHE F CB  1 
ATOM   17595 C  CG  . PHE F  2 201 ? 27.057  -55.604 -26.824  1.00 212.69 ? 311  PHE F CG  1 
ATOM   17596 C  CD1 . PHE F  2 201 ? 26.367  -54.456 -26.469  1.00 207.31 ? 311  PHE F CD1 1 
ATOM   17597 C  CD2 . PHE F  2 201 ? 26.627  -56.326 -27.925  1.00 221.10 ? 311  PHE F CD2 1 
ATOM   17598 C  CE1 . PHE F  2 201 ? 25.269  -54.038 -27.198  1.00 209.98 ? 311  PHE F CE1 1 
ATOM   17599 C  CE2 . PHE F  2 201 ? 25.533  -55.915 -28.657  1.00 222.50 ? 311  PHE F CE2 1 
ATOM   17600 C  CZ  . PHE F  2 201 ? 24.853  -54.768 -28.294  1.00 213.93 ? 311  PHE F CZ  1 
ATOM   17601 N  N   . ALA F  2 202 ? 30.015  -54.895 -23.298  1.00 199.74 ? 312  ALA F N   1 
ATOM   17602 C  CA  . ALA F  2 202 ? 30.856  -55.275 -22.162  1.00 197.72 ? 312  ALA F CA  1 
ATOM   17603 C  C   . ALA F  2 202 ? 29.957  -55.718 -21.007  1.00 204.18 ? 312  ALA F C   1 
ATOM   17604 O  O   . ALA F  2 202 ? 29.572  -54.906 -20.161  1.00 209.63 ? 312  ALA F O   1 
ATOM   17605 C  CB  . ALA F  2 202 ? 31.765  -54.122 -21.753  1.00 195.57 ? 312  ALA F CB  1 
ATOM   17606 N  N   . VAL F  2 203 ? 29.631  -57.011 -20.967  1.00 195.34 ? 313  VAL F N   1 
ATOM   17607 C  CA  . VAL F  2 203 ? 28.702  -57.541 -19.974  1.00 196.47 ? 313  VAL F CA  1 
ATOM   17608 C  C   . VAL F  2 203 ? 29.388  -58.585 -19.104  1.00 195.70 ? 313  VAL F C   1 
ATOM   17609 O  O   . VAL F  2 203 ? 30.606  -58.775 -19.179  1.00 194.83 ? 313  VAL F O   1 
ATOM   17610 C  CB  . VAL F  2 203 ? 27.455  -58.139 -20.647  1.00 201.86 ? 313  VAL F CB  1 
ATOM   17611 C  CG1 . VAL F  2 203 ? 26.712  -57.070 -21.430  1.00 207.31 ? 313  VAL F CG1 1 
ATOM   17612 C  CG2 . VAL F  2 203 ? 27.850  -59.288 -21.553  1.00 205.18 ? 313  VAL F CG2 1 
ATOM   17613 N  N   . THR F  2 204 ? 28.611  -59.256 -18.265  1.00 208.43 ? 314  THR F N   1 
ATOM   17614 C  CA  . THR F  2 204 ? 29.105  -60.336 -17.427  1.00 214.55 ? 314  THR F CA  1 
ATOM   17615 C  C   . THR F  2 204 ? 28.998  -61.673 -18.157  1.00 222.41 ? 314  THR F C   1 
ATOM   17616 O  O   . THR F  2 204 ? 28.391  -61.780 -19.225  1.00 229.72 ? 314  THR F O   1 
ATOM   17617 C  CB  . THR F  2 204 ? 28.341  -60.376 -16.107  1.00 219.78 ? 314  THR F CB  1 
ATOM   17618 O  OG1 . THR F  2 204 ? 26.931  -60.403 -16.369  1.00 223.72 ? 314  THR F OG1 1 
ATOM   17619 C  CG2 . THR F  2 204 ? 28.681  -59.152 -15.271  1.00 210.93 ? 314  THR F CG2 1 
ATOM   17620 N  N   . GLN F  2 205 ? 29.609  -62.702 -17.558  1.00 219.78 ? 315  GLN F N   1 
ATOM   17621 C  CA  . GLN F  2 205 ? 29.678  -64.023 -18.181  1.00 219.96 ? 315  GLN F CA  1 
ATOM   17622 C  C   . GLN F  2 205 ? 28.303  -64.537 -18.596  1.00 235.14 ? 315  GLN F C   1 
ATOM   17623 O  O   . GLN F  2 205 ? 28.101  -64.950 -19.744  1.00 242.94 ? 315  GLN F O   1 
ATOM   17624 C  CB  . GLN F  2 205 ? 30.338  -65.019 -17.226  1.00 223.70 ? 315  GLN F CB  1 
ATOM   17625 C  CG  . GLN F  2 205 ? 31.782  -64.707 -16.890  1.00 227.67 ? 315  GLN F CG  1 
ATOM   17626 C  CD  . GLN F  2 205 ? 32.489  -65.878 -16.232  1.00 232.98 ? 315  GLN F CD  1 
ATOM   17627 O  OE1 . GLN F  2 205 ? 32.054  -67.027 -16.343  1.00 219.71 ? 315  GLN F OE1 1 
ATOM   17628 N  NE2 . GLN F  2 205 ? 33.592  -65.594 -15.550  1.00 239.03 ? 315  GLN F NE2 1 
ATOM   17629 N  N   . GLU F  2 206 ? 27.340  -64.516 -17.671  1.00 246.41 ? 316  GLU F N   1 
ATOM   17630 C  CA  . GLU F  2 206 ? 26.024  -65.079 -17.946  1.00 249.85 ? 316  GLU F CA  1 
ATOM   17631 C  C   . GLU F  2 206 ? 25.264  -64.306 -19.009  1.00 240.10 ? 316  GLU F C   1 
ATOM   17632 O  O   . GLU F  2 206 ? 24.269  -64.820 -19.532  1.00 251.64 ? 316  GLU F O   1 
ATOM   17633 C  CB  . GLU F  2 206 ? 25.187  -65.124 -16.667  1.00 247.23 ? 316  GLU F CB  1 
ATOM   17634 C  CG  . GLU F  2 206 ? 24.864  -63.753 -16.093  1.00 234.54 ? 316  GLU F CG  1 
ATOM   17635 C  CD  . GLU F  2 206 ? 25.994  -63.184 -15.262  1.00 229.69 ? 316  GLU F CD  1 
ATOM   17636 O  OE1 . GLU F  2 206 ? 27.028  -63.867 -15.112  1.00 237.43 ? 316  GLU F OE1 1 
ATOM   17637 O  OE2 . GLU F  2 206 ? 25.848  -62.053 -14.756  1.00 223.71 ? 316  GLU F OE2 1 
ATOM   17638 N  N   . GLN F  2 207 ? 25.708  -63.100 -19.350  1.00 204.45 ? 317  GLN F N   1 
ATOM   17639 C  CA  . GLN F  2 207 ? 25.012  -62.266 -20.312  1.00 202.91 ? 317  GLN F CA  1 
ATOM   17640 C  C   . GLN F  2 207 ? 25.715  -62.211 -21.660  1.00 196.88 ? 317  GLN F C   1 
ATOM   17641 O  O   . GLN F  2 207 ? 25.224  -61.541 -22.575  1.00 197.22 ? 317  GLN F O   1 
ATOM   17642 C  CB  . GLN F  2 207 ? 24.851  -60.852 -19.746  1.00 208.42 ? 317  GLN F CB  1 
ATOM   17643 C  CG  . GLN F  2 207 ? 23.452  -60.285 -19.886  1.00 222.57 ? 317  GLN F CG  1 
ATOM   17644 C  CD  . GLN F  2 207 ? 22.440  -61.022 -19.035  1.00 231.56 ? 317  GLN F CD  1 
ATOM   17645 O  OE1 . GLN F  2 207 ? 22.792  -61.639 -18.029  1.00 224.47 ? 317  GLN F OE1 1 
ATOM   17646 N  NE2 . GLN F  2 207 ? 21.174  -60.964 -19.435  1.00 241.56 ? 317  GLN F NE2 1 
ATOM   17647 N  N   . VAL F  2 208 ? 26.832  -62.919 -21.820  1.00 199.40 ? 318  VAL F N   1 
ATOM   17648 C  CA  . VAL F  2 208 ? 27.564  -62.880 -23.082  1.00 193.89 ? 318  VAL F CA  1 
ATOM   17649 C  C   . VAL F  2 208 ? 26.857  -63.720 -24.139  1.00 192.90 ? 318  VAL F C   1 
ATOM   17650 O  O   . VAL F  2 208 ? 26.627  -63.258 -25.263  1.00 192.23 ? 318  VAL F O   1 
ATOM   17651 C  CB  . VAL F  2 208 ? 29.022  -63.331 -22.869  1.00 190.74 ? 318  VAL F CB  1 
ATOM   17652 C  CG1 . VAL F  2 208 ? 29.756  -63.416 -24.199  1.00 198.65 ? 318  VAL F CG1 1 
ATOM   17653 C  CG2 . VAL F  2 208 ? 29.742  -62.378 -21.933  1.00 192.42 ? 318  VAL F CG2 1 
ATOM   17654 N  N   . HIS F  2 209 ? 26.473  -64.954 -23.788  1.00 199.15 ? 319  HIS F N   1 
ATOM   17655 C  CA  . HIS F  2 209 ? 25.821  -65.831 -24.758  1.00 204.80 ? 319  HIS F CA  1 
ATOM   17656 C  C   . HIS F  2 209 ? 24.574  -65.181 -25.334  1.00 220.29 ? 319  HIS F C   1 
ATOM   17657 O  O   . HIS F  2 209 ? 24.189  -65.470 -26.472  1.00 234.04 ? 319  HIS F O   1 
ATOM   17658 C  CB  . HIS F  2 209 ? 25.465  -67.167 -24.103  1.00 214.84 ? 319  HIS F CB  1 
ATOM   17659 C  CG  . HIS F  2 209 ? 24.955  -68.198 -25.063  1.00 226.12 ? 319  HIS F CG  1 
ATOM   17660 N  ND1 . HIS F  2 209 ? 23.635  -68.261 -25.457  1.00 225.78 ? 319  HIS F ND1 1 
ATOM   17661 C  CD2 . HIS F  2 209 ? 25.585  -69.216 -25.697  1.00 222.56 ? 319  HIS F CD2 1 
ATOM   17662 C  CE1 . HIS F  2 209 ? 23.476  -69.267 -26.298  1.00 236.42 ? 319  HIS F CE1 1 
ATOM   17663 N  NE2 . HIS F  2 209 ? 24.644  -69.863 -26.461  1.00 240.06 ? 319  HIS F NE2 1 
ATOM   17664 N  N   . LEU F  2 210 ? 23.944  -64.293 -24.567  1.00 208.38 ? 320  LEU F N   1 
ATOM   17665 C  CA  . LEU F  2 210 ? 22.805  -63.530 -25.060  1.00 215.48 ? 320  LEU F CA  1 
ATOM   17666 C  C   . LEU F  2 210 ? 23.274  -62.396 -25.966  1.00 208.97 ? 320  LEU F C   1 
ATOM   17667 O  O   . LEU F  2 210 ? 22.915  -62.338 -27.147  1.00 206.32 ? 320  LEU F O   1 
ATOM   17668 C  CB  . LEU F  2 210 ? 21.991  -63.002 -23.871  1.00 214.50 ? 320  LEU F CB  1 
ATOM   17669 C  CG  . LEU F  2 210 ? 20.572  -62.440 -24.025  1.00 222.22 ? 320  LEU F CG  1 
ATOM   17670 C  CD1 . LEU F  2 210 ? 19.916  -62.357 -22.655  1.00 226.72 ? 320  LEU F CD1 1 
ATOM   17671 C  CD2 . LEU F  2 210 ? 20.561  -61.070 -24.682  1.00 213.70 ? 320  LEU F CD2 1 
ATOM   17672 N  N   . TYR F  2 211 ? 24.104  -61.499 -25.432  1.00 208.17 ? 321  TYR F N   1 
ATOM   17673 C  CA  . TYR F  2 211 ? 24.484  -60.301 -26.171  1.00 204.19 ? 321  TYR F CA  1 
ATOM   17674 C  C   . TYR F  2 211 ? 25.342  -60.607 -27.392  1.00 201.13 ? 321  TYR F C   1 
ATOM   17675 O  O   . TYR F  2 211 ? 25.417  -59.770 -28.298  1.00 193.52 ? 321  TYR F O   1 
ATOM   17676 C  CB  . TYR F  2 211 ? 25.214  -59.323 -25.245  1.00 201.83 ? 321  TYR F CB  1 
ATOM   17677 C  CG  . TYR F  2 211 ? 24.297  -58.465 -24.397  1.00 210.06 ? 321  TYR F CG  1 
ATOM   17678 C  CD1 . TYR F  2 211 ? 23.532  -59.024 -23.382  1.00 222.87 ? 321  TYR F CD1 1 
ATOM   17679 C  CD2 . TYR F  2 211 ? 24.218  -57.092 -24.593  1.00 218.03 ? 321  TYR F CD2 1 
ATOM   17680 C  CE1 . TYR F  2 211 ? 22.697  -58.242 -22.601  1.00 232.51 ? 321  TYR F CE1 1 
ATOM   17681 C  CE2 . TYR F  2 211 ? 23.390  -56.302 -23.814  1.00 226.04 ? 321  TYR F CE2 1 
ATOM   17682 C  CZ  . TYR F  2 211 ? 22.631  -56.882 -22.819  1.00 233.42 ? 321  TYR F CZ  1 
ATOM   17683 O  OH  . TYR F  2 211 ? 21.806  -56.098 -22.042  1.00 235.99 ? 321  TYR F OH  1 
ATOM   17684 N  N   . GLU F  2 212 ? 25.977  -61.783 -27.453  1.00 218.51 ? 322  GLU F N   1 
ATOM   17685 C  CA  . GLU F  2 212 ? 26.767  -62.113 -28.635  1.00 216.54 ? 322  GLU F CA  1 
ATOM   17686 C  C   . GLU F  2 212 ? 25.876  -62.328 -29.845  1.00 209.42 ? 322  GLU F C   1 
ATOM   17687 O  O   . GLU F  2 212 ? 26.272  -62.012 -30.972  1.00 212.61 ? 322  GLU F O   1 
ATOM   17688 C  CB  . GLU F  2 212 ? 27.617  -63.360 -28.395  1.00 223.46 ? 322  GLU F CB  1 
ATOM   17689 C  CG  . GLU F  2 212 ? 28.570  -63.666 -29.545  1.00 226.70 ? 322  GLU F CG  1 
ATOM   17690 C  CD  . GLU F  2 212 ? 29.400  -64.909 -29.309  1.00 235.41 ? 322  GLU F CD  1 
ATOM   17691 O  OE1 . GLU F  2 212 ? 29.250  -65.527 -28.234  1.00 237.06 ? 322  GLU F OE1 1 
ATOM   17692 O  OE2 . GLU F  2 212 ? 30.209  -65.264 -30.193  1.00 239.95 ? 322  GLU F OE2 1 
ATOM   17693 N  N   . ASN F  2 213 ? 24.672  -62.855 -29.632  1.00 207.39 ? 323  ASN F N   1 
ATOM   17694 C  CA  . ASN F  2 213 ? 23.730  -62.986 -30.731  1.00 214.68 ? 323  ASN F CA  1 
ATOM   17695 C  C   . ASN F  2 213 ? 23.184  -61.631 -31.148  1.00 213.77 ? 323  ASN F C   1 
ATOM   17696 O  O   . ASN F  2 213 ? 22.747  -61.470 -32.292  1.00 218.95 ? 323  ASN F O   1 
ATOM   17697 C  CB  . ASN F  2 213 ? 22.590  -63.930 -30.339  1.00 225.45 ? 323  ASN F CB  1 
ATOM   17698 C  CG  . ASN F  2 213 ? 23.072  -65.350 -30.074  1.00 223.96 ? 323  ASN F CG  1 
ATOM   17699 O  OD1 . ASN F  2 213 ? 22.734  -65.953 -29.053  1.00 224.88 ? 323  ASN F OD1 1 
ATOM   17700 N  ND2 . ASN F  2 213 ? 23.870  -65.887 -30.991  1.00 225.71 ? 323  ASN F ND2 1 
ATOM   17701 N  N   . TYR F  2 214 ? 23.209  -60.653 -30.244  1.00 207.88 ? 324  TYR F N   1 
ATOM   17702 C  CA  . TYR F  2 214 ? 22.873  -59.290 -30.629  1.00 222.68 ? 324  TYR F CA  1 
ATOM   17703 C  C   . TYR F  2 214 ? 23.946  -58.703 -31.534  1.00 227.79 ? 324  TYR F C   1 
ATOM   17704 O  O   . TYR F  2 214 ? 23.633  -58.063 -32.546  1.00 236.18 ? 324  TYR F O   1 
ATOM   17705 C  CB  . TYR F  2 214 ? 22.693  -58.427 -29.381  1.00 222.23 ? 324  TYR F CB  1 
ATOM   17706 C  CG  . TYR F  2 214 ? 21.404  -58.675 -28.625  1.00 227.51 ? 324  TYR F CG  1 
ATOM   17707 C  CD1 . TYR F  2 214 ? 20.454  -59.573 -29.098  1.00 234.41 ? 324  TYR F CD1 1 
ATOM   17708 C  CD2 . TYR F  2 214 ? 21.146  -58.015 -27.432  1.00 222.89 ? 324  TYR F CD2 1 
ATOM   17709 C  CE1 . TYR F  2 214 ? 19.280  -59.797 -28.401  1.00 243.25 ? 324  TYR F CE1 1 
ATOM   17710 C  CE2 . TYR F  2 214 ? 19.981  -58.233 -26.732  1.00 225.91 ? 324  TYR F CE2 1 
ATOM   17711 C  CZ  . TYR F  2 214 ? 19.052  -59.123 -27.219  1.00 243.76 ? 324  TYR F CZ  1 
ATOM   17712 O  OH  . TYR F  2 214 ? 17.892  -59.334 -26.512  1.00 253.17 ? 324  TYR F OH  1 
ATOM   17713 N  N   . ALA F  2 215 ? 25.219  -58.929 -31.196  1.00 220.43 ? 325  ALA F N   1 
ATOM   17714 C  CA  . ALA F  2 215 ? 26.324  -58.429 -32.006  1.00 212.77 ? 325  ALA F CA  1 
ATOM   17715 C  C   . ALA F  2 215 ? 26.355  -59.059 -33.388  1.00 208.54 ? 325  ALA F C   1 
ATOM   17716 O  O   . ALA F  2 215 ? 26.930  -58.473 -34.311  1.00 208.93 ? 325  ALA F O   1 
ATOM   17717 C  CB  . ALA F  2 215 ? 27.654  -58.674 -31.291  1.00 211.75 ? 325  ALA F CB  1 
ATOM   17718 N  N   . LYS F  2 216 ? 25.769  -60.246 -33.544  1.00 223.35 ? 326  LYS F N   1 
ATOM   17719 C  CA  . LYS F  2 216 ? 25.696  -60.865 -34.861  1.00 236.32 ? 326  LYS F CA  1 
ATOM   17720 C  C   . LYS F  2 216 ? 24.722  -60.114 -35.761  1.00 246.40 ? 326  LYS F C   1 
ATOM   17721 O  O   . LYS F  2 216 ? 24.945  -60.000 -36.971  1.00 265.63 ? 326  LYS F O   1 
ATOM   17722 C  CB  . LYS F  2 216 ? 25.288  -62.332 -34.723  1.00 239.47 ? 326  LYS F CB  1 
ATOM   17723 C  CG  . LYS F  2 216 ? 26.312  -63.196 -34.001  1.00 233.23 ? 326  LYS F CG  1 
ATOM   17724 C  CD  . LYS F  2 216 ? 25.844  -64.641 -33.913  1.00 235.15 ? 326  LYS F CD  1 
ATOM   17725 C  CE  . LYS F  2 216 ? 26.845  -65.500 -33.163  1.00 230.37 ? 326  LYS F CE  1 
ATOM   17726 N  NZ  . LYS F  2 216 ? 26.407  -66.919 -33.109  1.00 233.96 ? 326  LYS F NZ  1 
ATOM   17727 N  N   . LEU F  2 217 ? 23.631  -59.602 -35.189  1.00 221.69 ? 327  LEU F N   1 
ATOM   17728 C  CA  . LEU F  2 217 ? 22.679  -58.823 -35.973  1.00 227.08 ? 327  LEU F CA  1 
ATOM   17729 C  C   . LEU F  2 217 ? 23.243  -57.451 -36.312  1.00 223.38 ? 327  LEU F C   1 
ATOM   17730 O  O   . LEU F  2 217 ? 23.277  -57.050 -37.481  1.00 228.05 ? 327  LEU F O   1 
ATOM   17731 C  CB  . LEU F  2 217 ? 21.368  -58.683 -35.206  1.00 228.79 ? 327  LEU F CB  1 
ATOM   17732 C  CG  . LEU F  2 217 ? 20.762  -60.012 -34.767  1.00 232.88 ? 327  LEU F CG  1 
ATOM   17733 C  CD1 . LEU F  2 217 ? 19.452  -59.776 -34.045  1.00 235.33 ? 327  LEU F CD1 1 
ATOM   17734 C  CD2 . LEU F  2 217 ? 20.571  -60.942 -35.956  1.00 241.61 ? 327  LEU F CD2 1 
ATOM   17735 N  N   . ILE F  2 218 ? 23.671  -56.711 -35.294  1.00 231.41 ? 328  ILE F N   1 
ATOM   17736 C  CA  . ILE F  2 218 ? 24.204  -55.360 -35.453  1.00 229.48 ? 328  ILE F CA  1 
ATOM   17737 C  C   . ILE F  2 218 ? 25.551  -55.400 -36.167  1.00 223.29 ? 328  ILE F C   1 
ATOM   17738 O  O   . ILE F  2 218 ? 26.520  -55.961 -35.632  1.00 215.76 ? 328  ILE F O   1 
ATOM   17739 C  CB  . ILE F  2 218 ? 24.320  -54.658 -34.093  1.00 222.69 ? 328  ILE F CB  1 
ATOM   17740 C  CG1 . ILE F  2 218 ? 23.017  -54.826 -33.311  1.00 233.06 ? 328  ILE F CG1 1 
ATOM   17741 C  CG2 . ILE F  2 218 ? 24.662  -53.188 -34.274  1.00 222.45 ? 328  ILE F CG2 1 
ATOM   17742 C  CD1 . ILE F  2 218 ? 23.039  -54.187 -31.946  1.00 232.54 ? 328  ILE F CD1 1 
ATOM   17743 N  N   . PRO F  2 219 ? 25.660  -54.808 -37.358  1.00 218.90 ? 329  PRO F N   1 
ATOM   17744 C  CA  . PRO F  2 219 ? 26.933  -54.840 -38.087  1.00 221.51 ? 329  PRO F CA  1 
ATOM   17745 C  C   . PRO F  2 219 ? 28.011  -54.030 -37.381  1.00 207.58 ? 329  PRO F C   1 
ATOM   17746 O  O   . PRO F  2 219 ? 27.772  -52.923 -36.895  1.00 204.48 ? 329  PRO F O   1 
ATOM   17747 C  CB  . PRO F  2 219 ? 26.575  -54.238 -39.452  1.00 231.59 ? 329  PRO F CB  1 
ATOM   17748 C  CG  . PRO F  2 219 ? 25.373  -53.401 -39.196  1.00 225.97 ? 329  PRO F CG  1 
ATOM   17749 C  CD  . PRO F  2 219 ? 24.604  -54.114 -38.116  1.00 222.75 ? 329  PRO F CD  1 
ATOM   17750 N  N   . GLY F  2 220 ? 29.211  -54.606 -37.316  1.00 216.84 ? 330  GLY F N   1 
ATOM   17751 C  CA  . GLY F  2 220 ? 30.338  -53.955 -36.688  1.00 214.52 ? 330  GLY F CA  1 
ATOM   17752 C  C   . GLY F  2 220 ? 30.388  -54.095 -35.186  1.00 222.21 ? 330  GLY F C   1 
ATOM   17753 O  O   . GLY F  2 220 ? 31.470  -53.957 -34.600  1.00 219.23 ? 330  GLY F O   1 
ATOM   17754 N  N   . ALA F  2 221 ? 29.251  -54.349 -34.545  1.00 222.33 ? 331  ALA F N   1 
ATOM   17755 C  CA  . ALA F  2 221 ? 29.194  -54.479 -33.096  1.00 220.54 ? 331  ALA F CA  1 
ATOM   17756 C  C   . ALA F  2 221 ? 29.854  -55.774 -32.629  1.00 221.26 ? 331  ALA F C   1 
ATOM   17757 O  O   . ALA F  2 221 ? 29.583  -56.854 -33.163  1.00 220.25 ? 331  ALA F O   1 
ATOM   17758 C  CB  . ALA F  2 221 ? 27.743  -54.429 -32.623  1.00 224.84 ? 331  ALA F CB  1 
ATOM   17759 N  N   . THR F  2 222 ? 30.728  -55.658 -31.632  1.00 211.57 ? 332  THR F N   1 
ATOM   17760 C  CA  . THR F  2 222 ? 31.431  -56.783 -31.032  1.00 205.98 ? 332  THR F CA  1 
ATOM   17761 C  C   . THR F  2 222 ? 31.016  -56.926 -29.572  1.00 191.27 ? 332  THR F C   1 
ATOM   17762 O  O   . THR F  2 222 ? 30.244  -56.126 -29.038  1.00 192.59 ? 332  THR F O   1 
ATOM   17763 C  CB  . THR F  2 222 ? 32.950  -56.608 -31.141  1.00 202.16 ? 332  THR F CB  1 
ATOM   17764 O  OG1 . THR F  2 222 ? 33.378  -55.559 -30.261  1.00 207.19 ? 332  THR F OG1 1 
ATOM   17765 C  CG2 . THR F  2 222 ? 33.338  -56.252 -32.565  1.00 207.72 ? 332  THR F CG2 1 
ATOM   17766 N  N   . VAL F  2 223 ? 31.530  -57.970 -28.923  1.00 191.97 ? 333  VAL F N   1 
ATOM   17767 C  CA  . VAL F  2 223 ? 31.187  -58.264 -27.539  1.00 192.72 ? 333  VAL F CA  1 
ATOM   17768 C  C   . VAL F  2 223 ? 32.458  -58.313 -26.698  1.00 189.81 ? 333  VAL F C   1 
ATOM   17769 O  O   . VAL F  2 223 ? 33.568  -58.440 -27.216  1.00 199.80 ? 333  VAL F O   1 
ATOM   17770 C  CB  . VAL F  2 223 ? 30.402  -59.579 -27.429  1.00 194.26 ? 333  VAL F CB  1 
ATOM   17771 C  CG1 . VAL F  2 223 ? 28.972  -59.362 -27.893  1.00 209.10 ? 333  VAL F CG1 1 
ATOM   17772 C  CG2 . VAL F  2 223 ? 31.076  -60.647 -28.268  1.00 202.89 ? 333  VAL F CG2 1 
ATOM   17773 N  N   . GLY F  2 224 ? 32.281  -58.229 -25.378  1.00 191.25 ? 334  GLY F N   1 
ATOM   17774 C  CA  . GLY F  2 224 ? 33.406  -58.247 -24.457  1.00 197.94 ? 334  GLY F CA  1 
ATOM   17775 C  C   . GLY F  2 224 ? 33.003  -58.717 -23.078  1.00 204.30 ? 334  GLY F C   1 
ATOM   17776 O  O   . GLY F  2 224 ? 31.830  -58.648 -22.698  1.00 229.54 ? 334  GLY F O   1 
ATOM   17777 N  N   . LEU F  2 225 ? 33.992  -59.197 -22.323  1.00 176.02 ? 335  LEU F N   1 
ATOM   17778 C  CA  . LEU F  2 225 ? 33.766  -59.728 -20.983  1.00 185.04 ? 335  LEU F CA  1 
ATOM   17779 C  C   . LEU F  2 225 ? 34.311  -58.793 -19.907  1.00 198.09 ? 335  LEU F C   1 
ATOM   17780 O  O   . LEU F  2 225 ? 35.367  -58.172 -20.081  1.00 202.80 ? 335  LEU F O   1 
ATOM   17781 C  CB  . LEU F  2 225 ? 34.396  -61.114 -20.832  1.00 191.09 ? 335  LEU F CB  1 
ATOM   17782 C  CG  . LEU F  2 225 ? 34.090  -61.855 -19.525  1.00 202.14 ? 335  LEU F CG  1 
ATOM   17783 C  CD1 . LEU F  2 225 ? 32.589  -62.067 -19.339  1.00 191.62 ? 335  LEU F CD1 1 
ATOM   17784 C  CD2 . LEU F  2 225 ? 34.828  -63.182 -19.471  1.00 213.88 ? 335  LEU F CD2 1 
ATOM   17785 N  N   . LEU F  2 226 ? 33.592  -58.722 -18.782  1.00 208.58 ? 336  LEU F N   1 
ATOM   17786 C  CA  . LEU F  2 226 ? 33.956  -57.892 -17.638  1.00 194.66 ? 336  LEU F CA  1 
ATOM   17787 C  C   . LEU F  2 226 ? 34.666  -58.728 -16.580  1.00 192.06 ? 336  LEU F C   1 
ATOM   17788 O  O   . LEU F  2 226 ? 34.128  -59.740 -16.113  1.00 187.14 ? 336  LEU F O   1 
ATOM   17789 C  CB  . LEU F  2 226 ? 32.716  -57.238 -17.025  1.00 185.75 ? 336  LEU F CB  1 
ATOM   17790 C  CG  . LEU F  2 226 ? 32.754  -55.730 -16.765  1.00 184.57 ? 336  LEU F CG  1 
ATOM   17791 C  CD1 . LEU F  2 226 ? 34.075  -55.300 -16.144  1.00 183.38 ? 336  LEU F CD1 1 
ATOM   17792 C  CD2 . LEU F  2 226 ? 32.482  -54.968 -18.044  1.00 185.03 ? 336  LEU F CD2 1 
ATOM   17793 N  N   . GLN F  2 227 ? 35.856  -58.285 -16.182  1.00 193.30 ? 337  GLN F N   1 
ATOM   17794 C  CA  . GLN F  2 227 ? 36.619  -58.937 -15.131  1.00 200.96 ? 337  GLN F CA  1 
ATOM   17795 C  C   . GLN F  2 227 ? 37.182  -57.876 -14.198  1.00 206.52 ? 337  GLN F C   1 
ATOM   17796 O  O   . GLN F  2 227 ? 37.097  -56.674 -14.468  1.00 214.68 ? 337  GLN F O   1 
ATOM   17797 C  CB  . GLN F  2 227 ? 37.751  -59.793 -15.712  1.00 204.15 ? 337  GLN F CB  1 
ATOM   17798 C  CG  . GLN F  2 227 ? 37.285  -61.026 -16.467  1.00 205.72 ? 337  GLN F CG  1 
ATOM   17799 C  CD  . GLN F  2 227 ? 38.443  -61.895 -16.920  1.00 197.89 ? 337  GLN F CD  1 
ATOM   17800 O  OE1 . GLN F  2 227 ? 39.604  -61.505 -16.806  1.00 199.55 ? 337  GLN F OE1 1 
ATOM   17801 N  NE2 . GLN F  2 227 ? 38.133  -63.086 -17.422  1.00 194.37 ? 337  GLN F NE2 1 
ATOM   17802 N  N   . LYS F  2 228 ? 37.756  -58.335 -13.083  1.00 217.21 ? 338  LYS F N   1 
ATOM   17803 C  CA  . LYS F  2 228 ? 38.435  -57.421 -12.170  1.00 223.39 ? 338  LYS F CA  1 
ATOM   17804 C  C   . LYS F  2 228 ? 39.571  -56.701 -12.884  1.00 235.70 ? 338  LYS F C   1 
ATOM   17805 O  O   . LYS F  2 228 ? 39.732  -55.482 -12.757  1.00 242.08 ? 338  LYS F O   1 
ATOM   17806 C  CB  . LYS F  2 228 ? 38.964  -58.186 -10.958  1.00 207.06 ? 338  LYS F CB  1 
ATOM   17807 C  CG  . LYS F  2 228 ? 37.901  -58.786 -10.062  1.00 196.70 ? 338  LYS F CG  1 
ATOM   17808 C  CD  . LYS F  2 228 ? 38.569  -59.499 -8.895   1.00 197.12 ? 338  LYS F CD  1 
ATOM   17809 C  CE  . LYS F  2 228 ? 37.561  -60.124 -7.949   1.00 203.88 ? 338  LYS F CE  1 
ATOM   17810 N  NZ  . LYS F  2 228 ? 38.240  -60.828 -6.820   1.00 203.62 ? 338  LYS F NZ  1 
ATOM   17811 N  N   . ASP F  2 229 ? 40.367  -57.444 -13.650  1.00 230.14 ? 339  ASP F N   1 
ATOM   17812 C  CA  . ASP F  2 229 ? 41.356  -56.846 -14.542  1.00 215.28 ? 339  ASP F CA  1 
ATOM   17813 C  C   . ASP F  2 229 ? 40.639  -56.532 -15.843  1.00 212.32 ? 339  ASP F C   1 
ATOM   17814 O  O   . ASP F  2 229 ? 40.564  -57.355 -16.758  1.00 210.50 ? 339  ASP F O   1 
ATOM   17815 C  CB  . ASP F  2 229 ? 42.540  -57.774 -14.760  1.00 222.03 ? 339  ASP F CB  1 
ATOM   17816 C  CG  . ASP F  2 229 ? 43.398  -57.913 -13.528  1.00 233.45 ? 339  ASP F CG  1 
ATOM   17817 O  OD1 . ASP F  2 229 ? 43.507  -56.930 -12.763  1.00 235.02 ? 339  ASP F OD1 1 
ATOM   17818 O  OD2 . ASP F  2 229 ? 43.967  -59.004 -13.327  1.00 239.03 ? 339  ASP F OD2 1 
ATOM   17819 N  N   . SER F  2 230 ? 40.063  -55.336 -15.905  1.00 201.65 ? 340  SER F N   1 
ATOM   17820 C  CA  . SER F  2 230 ? 39.283  -54.905 -17.050  1.00 214.98 ? 340  SER F CA  1 
ATOM   17821 C  C   . SER F  2 230 ? 40.144  -54.483 -18.230  1.00 230.27 ? 340  SER F C   1 
ATOM   17822 O  O   . SER F  2 230 ? 39.611  -53.917 -19.198  1.00 238.70 ? 340  SER F O   1 
ATOM   17823 C  CB  . SER F  2 230 ? 38.367  -53.757 -16.654  1.00 223.56 ? 340  SER F CB  1 
ATOM   17824 O  OG  . SER F  2 230 ? 39.128  -52.705 -16.084  1.00 228.74 ? 340  SER F OG  1 
ATOM   17825 N  N   . GLY F  2 231 ? 41.441  -54.799 -18.216  1.00 222.67 ? 341  GLY F N   1 
ATOM   17826 C  CA  . GLY F  2 231 ? 42.227  -54.565 -19.395  1.00 206.58 ? 341  GLY F CA  1 
ATOM   17827 C  C   . GLY F  2 231 ? 41.826  -55.447 -20.551  1.00 182.55 ? 341  GLY F C   1 
ATOM   17828 O  O   . GLY F  2 231 ? 42.312  -55.224 -21.660  1.00 175.29 ? 341  GLY F O   1 
ATOM   17829 N  N   . ASN F  2 232 ? 40.995  -56.472 -20.333  1.00 200.68 ? 342  ASN F N   1 
ATOM   17830 C  CA  . ASN F  2 232 ? 40.592  -57.263 -21.493  1.00 196.79 ? 342  ASN F CA  1 
ATOM   17831 C  C   . ASN F  2 232 ? 39.839  -56.407 -22.485  1.00 199.39 ? 342  ASN F C   1 
ATOM   17832 O  O   . ASN F  2 232 ? 40.150  -56.426 -23.682  1.00 193.50 ? 342  ASN F O   1 
ATOM   17833 C  CB  . ASN F  2 232 ? 39.726  -58.443 -21.104  1.00 164.79 ? 342  ASN F CB  1 
ATOM   17834 C  CG  . ASN F  2 232 ? 39.741  -59.667 -22.181  1.00 178.75 ? 342  ASN F CG  1 
ATOM   17835 O  OD1 . ASN F  2 232 ? 40.714  -59.932 -23.033  1.00 199.26 ? 342  ASN F OD1 1 
ATOM   17836 N  ND2 . ASN F  2 232 ? 38.656  -60.482 -22.040  1.00 169.85 ? 342  ASN F ND2 1 
ATOM   17837 N  N   . ILE F  2 233 ? 38.887  -55.603 -22.002  1.00 204.40 ? 343  ILE F N   1 
ATOM   17838 C  CA  . ILE F  2 233 ? 38.100  -54.817 -22.938  1.00 203.44 ? 343  ILE F CA  1 
ATOM   17839 C  C   . ILE F  2 233 ? 39.007  -53.850 -23.674  1.00 192.29 ? 343  ILE F C   1 
ATOM   17840 O  O   . ILE F  2 233 ? 38.756  -53.496 -24.836  1.00 193.71 ? 343  ILE F O   1 
ATOM   17841 C  CB  . ILE F  2 233 ? 36.955  -54.105 -22.196  1.00 209.55 ? 343  ILE F CB  1 
ATOM   17842 C  CG1 . ILE F  2 233 ? 36.311  -55.113 -21.251  1.00 219.27 ? 343  ILE F CG1 1 
ATOM   17843 C  CG2 . ILE F  2 233 ? 35.929  -53.569 -23.193  1.00 205.65 ? 343  ILE F CG2 1 
ATOM   17844 C  CD1 . ILE F  2 233 ? 35.231  -54.569 -20.410  1.00 230.31 ? 343  ILE F CD1 1 
ATOM   17845 N  N   . LEU F  2 234 ? 40.103  -53.456 -23.036  1.00 179.22 ? 344  LEU F N   1 
ATOM   17846 C  CA  . LEU F  2 234 ? 41.089  -52.625 -23.701  1.00 174.38 ? 344  LEU F CA  1 
ATOM   17847 C  C   . LEU F  2 234 ? 41.742  -53.372 -24.857  1.00 170.40 ? 344  LEU F C   1 
ATOM   17848 O  O   . LEU F  2 234 ? 42.044  -52.767 -25.892  1.00 167.25 ? 344  LEU F O   1 
ATOM   17849 C  CB  . LEU F  2 234 ? 42.141  -52.182 -22.681  1.00 187.46 ? 344  LEU F CB  1 
ATOM   17850 C  CG  . LEU F  2 234 ? 41.623  -51.392 -21.471  1.00 185.77 ? 344  LEU F CG  1 
ATOM   17851 C  CD1 . LEU F  2 234 ? 42.772  -50.877 -20.609  1.00 183.70 ? 344  LEU F CD1 1 
ATOM   17852 C  CD2 . LEU F  2 234 ? 40.716  -50.252 -21.900  1.00 186.94 ? 344  LEU F CD2 1 
ATOM   17853 N  N   . GLN F  2 235 ? 41.924  -54.690 -24.723  1.00 174.28 ? 345  GLN F N   1 
ATOM   17854 C  CA  . GLN F  2 235 ? 42.506  -55.464 -25.815  1.00 187.13 ? 345  GLN F CA  1 
ATOM   17855 C  C   . GLN F  2 235 ? 41.632  -55.416 -27.061  1.00 194.89 ? 345  GLN F C   1 
ATOM   17856 O  O   . GLN F  2 235 ? 42.150  -55.500 -28.180  1.00 208.36 ? 345  GLN F O   1 
ATOM   17857 C  CB  . GLN F  2 235 ? 42.739  -56.912 -25.377  1.00 197.40 ? 345  GLN F CB  1 
ATOM   17858 C  CG  . GLN F  2 235 ? 43.924  -57.089 -24.442  1.00 193.52 ? 345  GLN F CG  1 
ATOM   17859 C  CD  . GLN F  2 235 ? 44.221  -58.545 -24.140  1.00 189.41 ? 345  GLN F CD  1 
ATOM   17860 O  OE1 . GLN F  2 235 ? 43.618  -59.449 -24.721  1.00 187.26 ? 345  GLN F OE1 1 
ATOM   17861 N  NE2 . GLN F  2 235 ? 45.149  -58.779 -23.220  1.00 187.38 ? 345  GLN F NE2 1 
ATOM   17862 N  N   . LEU F  2 236 ? 40.314  -55.270 -26.890  1.00 180.63 ? 346  LEU F N   1 
ATOM   17863 C  CA  . LEU F  2 236 ? 39.431  -55.075 -28.037  1.00 183.55 ? 346  LEU F CA  1 
ATOM   17864 C  C   . LEU F  2 236 ? 39.803  -53.812 -28.791  1.00 191.59 ? 346  LEU F C   1 
ATOM   17865 O  O   . LEU F  2 236 ? 40.029  -53.832 -30.008  1.00 195.51 ? 346  LEU F O   1 
ATOM   17866 C  CB  . LEU F  2 236 ? 37.982  -54.957 -27.573  1.00 180.82 ? 346  LEU F CB  1 
ATOM   17867 C  CG  . LEU F  2 236 ? 37.137  -56.113 -27.053  1.00 188.56 ? 346  LEU F CG  1 
ATOM   17868 C  CD1 . LEU F  2 236 ? 35.893  -55.551 -26.403  1.00 200.17 ? 346  LEU F CD1 1 
ATOM   17869 C  CD2 . LEU F  2 236 ? 36.728  -57.050 -28.164  1.00 198.09 ? 346  LEU F CD2 1 
ATOM   17870 N  N   . ILE F  2 237 ? 39.871  -52.696 -28.067  1.00 180.89 ? 347  ILE F N   1 
ATOM   17871 C  CA  . ILE F  2 237 ? 40.016  -51.397 -28.704  1.00 166.50 ? 347  ILE F CA  1 
ATOM   17872 C  C   . ILE F  2 237 ? 41.356  -51.312 -29.416  1.00 166.84 ? 347  ILE F C   1 
ATOM   17873 O  O   . ILE F  2 237 ? 41.450  -50.801 -30.538  1.00 167.87 ? 347  ILE F O   1 
ATOM   17874 C  CB  . ILE F  2 237 ? 39.838  -50.290 -27.651  1.00 166.22 ? 347  ILE F CB  1 
ATOM   17875 C  CG1 . ILE F  2 237 ? 38.673  -50.642 -26.722  1.00 169.05 ? 347  ILE F CG1 1 
ATOM   17876 C  CG2 . ILE F  2 237 ? 39.545  -48.970 -28.328  1.00 182.73 ? 347  ILE F CG2 1 
ATOM   17877 C  CD1 . ILE F  2 237 ? 38.425  -49.633 -25.619  1.00 170.95 ? 347  ILE F CD1 1 
ATOM   17878 N  N   . ILE F  2 238 ? 42.411  -51.839 -28.786  1.00 187.08 ? 348  ILE F N   1 
ATOM   17879 C  CA  . ILE F  2 238 ? 43.731  -51.835 -29.408  1.00 193.71 ? 348  ILE F CA  1 
ATOM   17880 C  C   . ILE F  2 238 ? 43.723  -52.679 -30.675  1.00 204.24 ? 348  ILE F C   1 
ATOM   17881 O  O   . ILE F  2 238 ? 44.280  -52.285 -31.707  1.00 209.59 ? 348  ILE F O   1 
ATOM   17882 C  CB  . ILE F  2 238 ? 44.787  -52.330 -28.405  1.00 181.15 ? 348  ILE F CB  1 
ATOM   17883 C  CG1 . ILE F  2 238 ? 44.794  -51.437 -27.165  1.00 187.25 ? 348  ILE F CG1 1 
ATOM   17884 C  CG2 . ILE F  2 238 ? 46.160  -52.379 -29.054  1.00 172.46 ? 348  ILE F CG2 1 
ATOM   17885 C  CD1 . ILE F  2 238 ? 45.810  -51.843 -26.128  1.00 191.64 ? 348  ILE F CD1 1 
ATOM   17886 N  N   . SER F  2 239 ? 43.070  -53.839 -30.625  1.00 209.86 ? 349  SER F N   1 
ATOM   17887 C  CA  . SER F  2 239 ? 42.917  -54.691 -31.795  1.00 214.62 ? 349  SER F CA  1 
ATOM   17888 C  C   . SER F  2 239 ? 41.757  -54.253 -32.672  1.00 224.32 ? 349  SER F C   1 
ATOM   17889 O  O   . SER F  2 239 ? 41.420  -54.946 -33.637  1.00 231.42 ? 349  SER F O   1 
ATOM   17890 C  CB  . SER F  2 239 ? 42.737  -56.151 -31.368  1.00 209.17 ? 349  SER F CB  1 
ATOM   17891 O  OG  . SER F  2 239 ? 41.654  -56.291 -30.464  1.00 218.60 ? 349  SER F OG  1 
ATOM   17892 N  N   . ALA F  2 240 ? 41.142  -53.118 -32.353  1.00 205.29 ? 350  ALA F N   1 
ATOM   17893 C  CA  . ALA F  2 240 ? 40.169  -52.492 -33.226  1.00 212.57 ? 350  ALA F CA  1 
ATOM   17894 C  C   . ALA F  2 240 ? 40.744  -51.276 -33.930  1.00 213.33 ? 350  ALA F C   1 
ATOM   17895 O  O   . ALA F  2 240 ? 40.114  -50.753 -34.855  1.00 233.28 ? 350  ALA F O   1 
ATOM   17896 C  CB  . ALA F  2 240 ? 38.914  -52.091 -32.435  1.00 209.63 ? 350  ALA F CB  1 
ATOM   17897 N  N   . TYR F  2 241 ? 41.940  -50.847 -33.547  1.00 202.25 ? 351  TYR F N   1 
ATOM   17898 C  CA  . TYR F  2 241 ? 42.640  -49.763 -34.212  1.00 209.75 ? 351  TYR F CA  1 
ATOM   17899 C  C   . TYR F  2 241 ? 43.400  -50.259 -35.429  1.00 215.35 ? 351  TYR F C   1 
ATOM   17900 O  O   . TYR F  2 241 ? 44.185  -49.511 -36.017  1.00 229.23 ? 351  TYR F O   1 
ATOM   17901 C  CB  . TYR F  2 241 ? 43.590  -49.078 -33.220  1.00 215.53 ? 351  TYR F CB  1 
ATOM   17902 C  CG  . TYR F  2 241 ? 44.053  -47.687 -33.611  1.00 230.86 ? 351  TYR F CG  1 
ATOM   17903 C  CD1 . TYR F  2 241 ? 43.183  -46.604 -33.562  1.00 227.74 ? 351  TYR F CD1 1 
ATOM   17904 C  CD2 . TYR F  2 241 ? 45.371  -47.450 -33.988  1.00 245.01 ? 351  TYR F CD2 1 
ATOM   17905 C  CE1 . TYR F  2 241 ? 43.605  -45.333 -33.905  1.00 234.07 ? 351  TYR F CE1 1 
ATOM   17906 C  CE2 . TYR F  2 241 ? 45.801  -46.180 -34.331  1.00 247.19 ? 351  TYR F CE2 1 
ATOM   17907 C  CZ  . TYR F  2 241 ? 44.913  -45.128 -34.286  1.00 241.49 ? 351  TYR F CZ  1 
ATOM   17908 O  OH  . TYR F  2 241 ? 45.335  -43.863 -34.625  1.00 244.26 ? 351  TYR F OH  1 
ATOM   17909 N  N   . GLU F  2 242 ? 43.162  -51.514 -35.809  1.00 217.98 ? 352  GLU F N   1 
ATOM   17910 C  CA  . GLU F  2 242 ? 43.809  -52.086 -36.981  1.00 240.10 ? 352  GLU F CA  1 
ATOM   17911 C  C   . GLU F  2 242 ? 43.420  -51.334 -38.247  1.00 248.00 ? 352  GLU F C   1 
ATOM   17912 O  O   . GLU F  2 242 ? 44.250  -51.142 -39.144  1.00 260.99 ? 352  GLU F O   1 
ATOM   17913 C  CB  . GLU F  2 242 ? 43.431  -53.562 -37.095  1.00 248.02 ? 352  GLU F CB  1 
ATOM   17914 C  CG  . GLU F  2 242 ? 43.809  -54.389 -35.875  1.00 239.82 ? 352  GLU F CG  1 
ATOM   17915 C  CD  . GLU F  2 242 ? 43.229  -55.793 -35.919  1.00 250.79 ? 352  GLU F CD  1 
ATOM   17916 O  OE1 . GLU F  2 242 ? 42.411  -56.071 -36.821  1.00 266.45 ? 352  GLU F OE1 1 
ATOM   17917 O  OE2 . GLU F  2 242 ? 43.582  -56.614 -35.047  1.00 244.35 ? 352  GLU F OE2 1 
ATOM   17918 N  N   . GLU F  2 243 ? 42.161  -50.899 -38.333  1.00 228.67 ? 353  GLU F N   1 
ATOM   17919 C  CA  . GLU F  2 243 ? 41.641  -50.171 -39.486  1.00 231.67 ? 353  GLU F CA  1 
ATOM   17920 C  C   . GLU F  2 243 ? 41.828  -50.960 -40.778  1.00 249.49 ? 353  GLU F C   1 
ATOM   17921 O  O   . GLU F  2 243 ? 41.235  -52.032 -40.943  1.00 253.10 ? 353  GLU F O   1 
ATOM   17922 C  CB  . GLU F  2 243 ? 42.307  -48.798 -39.596  1.00 225.44 ? 353  GLU F CB  1 
ATOM   17923 C  CG  . GLU F  2 243 ? 42.202  -47.967 -38.338  1.00 219.81 ? 353  GLU F CG  1 
ATOM   17924 C  CD  . GLU F  2 243 ? 42.675  -46.547 -38.547  1.00 238.77 ? 353  GLU F CD  1 
ATOM   17925 O  OE1 . GLU F  2 243 ? 43.645  -46.138 -37.875  1.00 251.93 ? 353  GLU F OE1 1 
ATOM   17926 O  OE2 . GLU F  2 243 ? 42.090  -45.848 -39.399  1.00 252.63 ? 353  GLU F OE2 1 
ATOM   17927 N  N   . LEU F  2 244 ? 42.652  -50.441 -41.689  1.00 271.01 ? 354  LEU F N   1 
ATOM   17928 C  CA  . LEU F  2 244 ? 42.915  -51.064 -42.992  1.00 273.36 ? 354  LEU F CA  1 
ATOM   17929 C  C   . LEU F  2 244 ? 41.628  -51.309 -43.784  1.00 274.59 ? 354  LEU F C   1 
ATOM   17930 O  O   . LEU F  2 244 ? 41.596  -52.127 -44.707  1.00 270.20 ? 354  LEU F O   1 
ATOM   17931 C  CB  . LEU F  2 244 ? 43.684  -52.378 -42.817  1.00 262.38 ? 354  LEU F CB  1 
ATOM   17932 C  CG  . LEU F  2 244 ? 45.098  -52.275 -42.239  1.00 244.93 ? 354  LEU F CG  1 
ATOM   17933 C  CD1 . LEU F  2 244 ? 45.740  -53.649 -42.137  1.00 232.90 ? 354  LEU F CD1 1 
ATOM   17934 C  CD2 . LEU F  2 244 ? 45.958  -51.340 -43.077  1.00 249.77 ? 354  LEU F CD2 1 
ATOM   17935 N  N   . GLU G  3 12  ? 58.880  -33.955 54.220   1.00 281.97 ? 10   GLU G N   1 
ATOM   17936 C  CA  . GLU G  3 12  ? 57.769  -34.367 55.069   1.00 280.75 ? 10   GLU G CA  1 
ATOM   17937 C  C   . GLU G  3 12  ? 56.618  -33.370 54.986   1.00 270.55 ? 10   GLU G C   1 
ATOM   17938 O  O   . GLU G  3 12  ? 55.494  -33.673 55.381   1.00 269.88 ? 10   GLU G O   1 
ATOM   17939 C  CB  . GLU G  3 12  ? 58.229  -34.524 56.523   1.00 289.50 ? 10   GLU G CB  1 
ATOM   17940 C  CG  . GLU G  3 12  ? 59.132  -35.723 56.778   1.00 283.66 ? 10   GLU G CG  1 
ATOM   17941 C  CD  . GLU G  3 12  ? 58.364  -37.028 56.854   1.00 275.10 ? 10   GLU G CD  1 
ATOM   17942 O  OE1 . GLU G  3 12  ? 57.129  -36.985 57.036   1.00 267.92 ? 10   GLU G OE1 1 
ATOM   17943 O  OE2 . GLU G  3 12  ? 58.997  -38.097 56.731   1.00 280.88 ? 10   GLU G OE2 1 
ATOM   17944 N  N   . LEU G  3 13  ? 56.905  -32.172 54.472   1.00 254.72 ? 11   LEU G N   1 
ATOM   17945 C  CA  . LEU G  3 13  ? 55.880  -31.143 54.351   1.00 242.14 ? 11   LEU G CA  1 
ATOM   17946 C  C   . LEU G  3 13  ? 54.853  -31.465 53.276   1.00 239.76 ? 11   LEU G C   1 
ATOM   17947 O  O   . LEU G  3 13  ? 53.723  -30.970 53.353   1.00 239.23 ? 11   LEU G O   1 
ATOM   17948 C  CB  . LEU G  3 13  ? 56.527  -29.789 54.051   1.00 242.79 ? 11   LEU G CB  1 
ATOM   17949 C  CG  . LEU G  3 13  ? 57.585  -29.317 55.049   1.00 253.30 ? 11   LEU G CG  1 
ATOM   17950 C  CD1 . LEU G  3 13  ? 58.138  -27.957 54.644   1.00 259.12 ? 11   LEU G CD1 1 
ATOM   17951 C  CD2 . LEU G  3 13  ? 57.010  -29.276 56.459   1.00 258.34 ? 11   LEU G CD2 1 
ATOM   17952 N  N   . VAL G  3 14  ? 55.220  -32.282 52.283   1.00 244.66 ? 12   VAL G N   1 
ATOM   17953 C  CA  . VAL G  3 14  ? 54.287  -32.631 51.216   1.00 244.00 ? 12   VAL G CA  1 
ATOM   17954 C  C   . VAL G  3 14  ? 53.144  -33.480 51.760   1.00 250.86 ? 12   VAL G C   1 
ATOM   17955 O  O   . VAL G  3 14  ? 51.982  -33.305 51.373   1.00 245.35 ? 12   VAL G O   1 
ATOM   17956 C  CB  . VAL G  3 14  ? 55.029  -33.348 50.073   1.00 239.50 ? 12   VAL G CB  1 
ATOM   17957 C  CG1 . VAL G  3 14  ? 54.053  -33.765 48.981   1.00 237.73 ? 12   VAL G CG1 1 
ATOM   17958 C  CG2 . VAL G  3 14  ? 56.124  -32.461 49.503   1.00 240.28 ? 12   VAL G CG2 1 
ATOM   17959 N  N   . LYS G  3 15  ? 53.453  -34.407 52.669   1.00 262.26 ? 13   LYS G N   1 
ATOM   17960 C  CA  . LYS G  3 15  ? 52.450  -35.342 53.167   1.00 255.22 ? 13   LYS G CA  1 
ATOM   17961 C  C   . LYS G  3 15  ? 51.482  -34.699 54.155   1.00 257.38 ? 13   LYS G C   1 
ATOM   17962 O  O   . LYS G  3 15  ? 50.339  -35.154 54.273   1.00 252.61 ? 13   LYS G O   1 
ATOM   17963 C  CB  . LYS G  3 15  ? 53.143  -36.541 53.816   1.00 255.17 ? 13   LYS G CB  1 
ATOM   17964 C  CG  . LYS G  3 15  ? 54.152  -37.220 52.905   1.00 253.87 ? 13   LYS G CG  1 
ATOM   17965 C  CD  . LYS G  3 15  ? 54.863  -38.368 53.593   1.00 242.98 ? 13   LYS G CD  1 
ATOM   17966 C  CE  . LYS G  3 15  ? 55.786  -39.076 52.619   1.00 235.02 ? 13   LYS G CE  1 
ATOM   17967 N  NZ  . LYS G  3 15  ? 56.449  -40.246 53.242   1.00 231.41 ? 13   LYS G NZ  1 
ATOM   17968 N  N   . ARG G  3 16  ? 51.905  -33.643 54.860   1.00 265.18 ? 14   ARG G N   1 
ATOM   17969 C  CA  . ARG G  3 16  ? 51.081  -33.065 55.921   1.00 264.42 ? 14   ARG G CA  1 
ATOM   17970 C  C   . ARG G  3 16  ? 49.909  -32.243 55.391   1.00 258.27 ? 14   ARG G C   1 
ATOM   17971 O  O   . ARG G  3 16  ? 48.924  -32.059 56.114   1.00 254.94 ? 14   ARG G O   1 
ATOM   17972 C  CB  . ARG G  3 16  ? 51.944  -32.198 56.843   1.00 268.88 ? 14   ARG G CB  1 
ATOM   17973 C  CG  . ARG G  3 16  ? 52.940  -32.974 57.702   1.00 270.18 ? 14   ARG G CG  1 
ATOM   17974 C  CD  . ARG G  3 16  ? 52.229  -33.930 58.647   1.00 257.40 ? 14   ARG G CD  1 
ATOM   17975 N  NE  . ARG G  3 16  ? 51.217  -33.254 59.452   1.00 249.90 ? 14   ARG G NE  1 
ATOM   17976 C  CZ  . ARG G  3 16  ? 50.436  -33.867 60.334   1.00 246.84 ? 14   ARG G CZ  1 
ATOM   17977 N  NH1 . ARG G  3 16  ? 50.551  -35.174 60.528   1.00 241.38 ? 14   ARG G NH1 1 
ATOM   17978 N  NH2 . ARG G  3 16  ? 49.540  -33.175 61.024   1.00 254.60 ? 14   ARG G NH2 1 
ATOM   17979 N  N   . LYS G  3 17  ? 49.988  -31.742 54.156   1.00 265.10 ? 15   LYS G N   1 
ATOM   17980 C  CA  . LYS G  3 17  ? 48.889  -30.959 53.596   1.00 265.37 ? 15   LYS G CA  1 
ATOM   17981 C  C   . LYS G  3 17  ? 47.690  -31.824 53.213   1.00 264.43 ? 15   LYS G C   1 
ATOM   17982 O  O   . LYS G  3 17  ? 46.545  -31.393 53.387   1.00 265.86 ? 15   LYS G O   1 
ATOM   17983 C  CB  . LYS G  3 17  ? 49.374  -30.168 52.383   1.00 264.54 ? 15   LYS G CB  1 
ATOM   17984 C  CG  . LYS G  3 17  ? 48.280  -29.396 51.664   1.00 257.49 ? 15   LYS G CG  1 
ATOM   17985 C  CD  . LYS G  3 17  ? 48.854  -28.406 50.673   1.00 256.50 ? 15   LYS G CD  1 
ATOM   17986 C  CE  . LYS G  3 17  ? 49.597  -27.292 51.388   1.00 262.37 ? 15   LYS G CE  1 
ATOM   17987 N  NZ  . LYS G  3 17  ? 50.094  -26.261 50.437   1.00 259.05 ? 15   LYS G NZ  1 
ATOM   17988 N  N   . ARG G  3 18  ? 47.927  -33.040 52.706   1.00 264.04 ? 16   ARG G N   1 
ATOM   17989 C  CA  . ARG G  3 18  ? 46.827  -33.920 52.317   1.00 262.20 ? 16   ARG G CA  1 
ATOM   17990 C  C   . ARG G  3 18  ? 46.018  -34.391 53.520   1.00 256.27 ? 16   ARG G C   1 
ATOM   17991 O  O   . ARG G  3 18  ? 44.804  -34.600 53.402   1.00 252.09 ? 16   ARG G O   1 
ATOM   17992 C  CB  . ARG G  3 18  ? 47.361  -35.133 51.553   1.00 263.90 ? 16   ARG G CB  1 
ATOM   17993 C  CG  . ARG G  3 18  ? 46.281  -36.108 51.092   1.00 260.32 ? 16   ARG G CG  1 
ATOM   17994 C  CD  . ARG G  3 18  ? 46.874  -37.353 50.454   1.00 259.58 ? 16   ARG G CD  1 
ATOM   17995 N  NE  . ARG G  3 18  ? 45.869  -38.117 49.721   1.00 251.62 ? 16   ARG G NE  1 
ATOM   17996 C  CZ  . ARG G  3 18  ? 45.068  -39.021 50.273   1.00 254.25 ? 16   ARG G CZ  1 
ATOM   17997 N  NH1 . ARG G  3 18  ? 45.152  -39.278 51.570   1.00 278.65 ? 16   ARG G NH1 1 
ATOM   17998 N  NH2 . ARG G  3 18  ? 44.183  -39.668 49.529   1.00 239.20 ? 16   ARG G NH2 1 
ATOM   17999 N  N   . ILE G  3 19  ? 46.666  -34.573 54.674   1.00 259.38 ? 17   ILE G N   1 
ATOM   18000 C  CA  . ILE G  3 19  ? 45.964  -35.084 55.850   1.00 266.32 ? 17   ILE G CA  1 
ATOM   18001 C  C   . ILE G  3 19  ? 44.858  -34.124 56.271   1.00 267.91 ? 17   ILE G C   1 
ATOM   18002 O  O   . ILE G  3 19  ? 43.740  -34.545 56.597   1.00 269.98 ? 17   ILE G O   1 
ATOM   18003 C  CB  . ILE G  3 19  ? 46.959  -35.346 56.996   1.00 284.38 ? 17   ILE G CB  1 
ATOM   18004 C  CG1 . ILE G  3 19  ? 48.004  -36.384 56.570   1.00 282.86 ? 17   ILE G CG1 1 
ATOM   18005 C  CG2 . ILE G  3 19  ? 46.229  -35.810 58.250   1.00 287.55 ? 17   ILE G CG2 1 
ATOM   18006 C  CD1 . ILE G  3 19  ? 49.017  -36.729 57.653   1.00 284.03 ? 17   ILE G CD1 1 
ATOM   18007 N  N   . GLU G  3 20  ? 45.146  -32.818 56.265   1.00 262.60 ? 18   GLU G N   1 
ATOM   18008 C  CA  . GLU G  3 20  ? 44.135  -31.834 56.633   1.00 254.87 ? 18   GLU G CA  1 
ATOM   18009 C  C   . GLU G  3 20  ? 43.018  -31.742 55.605   1.00 262.17 ? 18   GLU G C   1 
ATOM   18010 O  O   . GLU G  3 20  ? 41.929  -31.255 55.933   1.00 262.28 ? 18   GLU G O   1 
ATOM   18011 C  CB  . GLU G  3 20  ? 44.781  -30.463 56.835   1.00 240.39 ? 18   GLU G CB  1 
ATOM   18012 C  CG  . GLU G  3 20  ? 45.572  -30.359 58.126   1.00 239.46 ? 18   GLU G CG  1 
ATOM   18013 C  CD  . GLU G  3 20  ? 44.715  -30.618 59.354   1.00 238.31 ? 18   GLU G CD  1 
ATOM   18014 O  OE1 . GLU G  3 20  ? 43.514  -30.275 59.328   1.00 236.31 ? 18   GLU G OE1 1 
ATOM   18015 O  OE2 . GLU G  3 20  ? 45.239  -31.170 60.344   1.00 242.30 ? 18   GLU G OE2 1 
ATOM   18016 N  N   . ALA G  3 21  ? 43.263  -32.192 54.372   1.00 267.17 ? 19   ALA G N   1 
ATOM   18017 C  CA  . ALA G  3 21  ? 42.187  -32.317 53.398   1.00 260.37 ? 19   ALA G CA  1 
ATOM   18018 C  C   . ALA G  3 21  ? 41.379  -33.588 53.618   1.00 251.29 ? 19   ALA G C   1 
ATOM   18019 O  O   . ALA G  3 21  ? 40.178  -33.613 53.322   1.00 243.55 ? 19   ALA G O   1 
ATOM   18020 C  CB  . ALA G  3 21  ? 42.751  -32.288 51.976   1.00 260.24 ? 19   ALA G CB  1 
ATOM   18021 N  N   . ILE G  3 22  ? 42.014  -34.646 54.133   1.00 242.15 ? 20   ILE G N   1 
ATOM   18022 C  CA  . ILE G  3 22  ? 41.279  -35.853 54.495   1.00 238.05 ? 20   ILE G CA  1 
ATOM   18023 C  C   . ILE G  3 22  ? 40.359  -35.578 55.678   1.00 240.20 ? 20   ILE G C   1 
ATOM   18024 O  O   . ILE G  3 22  ? 39.229  -36.078 55.732   1.00 239.63 ? 20   ILE G O   1 
ATOM   18025 C  CB  . ILE G  3 22  ? 42.256  -37.003 54.795   1.00 240.21 ? 20   ILE G CB  1 
ATOM   18026 C  CG1 . ILE G  3 22  ? 42.993  -37.433 53.525   1.00 240.48 ? 20   ILE G CG1 1 
ATOM   18027 C  CG2 . ILE G  3 22  ? 41.518  -38.183 55.396   1.00 239.75 ? 20   ILE G CG2 1 
ATOM   18028 C  CD1 . ILE G  3 22  ? 42.099  -38.083 52.491   1.00 238.50 ? 20   ILE G CD1 1 
ATOM   18029 N  N   . ARG G  3 23  ? 40.831  -34.778 56.641   1.00 254.26 ? 21   ARG G N   1 
ATOM   18030 C  CA  . ARG G  3 23  ? 40.015  -34.426 57.799   1.00 255.66 ? 21   ARG G CA  1 
ATOM   18031 C  C   . ARG G  3 23  ? 38.745  -33.698 57.375   1.00 259.84 ? 21   ARG G C   1 
ATOM   18032 O  O   . ARG G  3 23  ? 37.648  -34.006 57.855   1.00 259.42 ? 21   ARG G O   1 
ATOM   18033 C  CB  . ARG G  3 23  ? 40.826  -33.562 58.765   1.00 247.08 ? 21   ARG G CB  1 
ATOM   18034 C  CG  . ARG G  3 23  ? 39.992  -32.914 59.855   1.00 244.40 ? 21   ARG G CG  1 
ATOM   18035 C  CD  . ARG G  3 23  ? 40.820  -31.967 60.705   1.00 249.21 ? 21   ARG G CD  1 
ATOM   18036 N  NE  . ARG G  3 23  ? 41.876  -32.659 61.438   1.00 242.29 ? 21   ARG G NE  1 
ATOM   18037 C  CZ  . ARG G  3 23  ? 41.741  -33.141 62.670   1.00 243.53 ? 21   ARG G CZ  1 
ATOM   18038 N  NH1 . ARG G  3 23  ? 40.590  -33.011 63.316   1.00 244.05 ? 21   ARG G NH1 1 
ATOM   18039 N  NH2 . ARG G  3 23  ? 42.759  -33.754 63.257   1.00 249.05 ? 21   ARG G NH2 1 
ATOM   18040 N  N   . GLY G  3 24  ? 38.879  -32.721 56.474   1.00 266.98 ? 22   GLY G N   1 
ATOM   18041 C  CA  . GLY G  3 24  ? 37.719  -32.023 55.948   1.00 268.50 ? 22   GLY G CA  1 
ATOM   18042 C  C   . GLY G  3 24  ? 36.895  -32.841 54.975   1.00 253.76 ? 22   GLY G C   1 
ATOM   18043 O  O   . GLY G  3 24  ? 35.739  -32.492 54.715   1.00 244.97 ? 22   GLY G O   1 
ATOM   18044 N  N   . GLN G  3 25  ? 37.462  -33.920 54.432   1.00 257.19 ? 23   GLN G N   1 
ATOM   18045 C  CA  . GLN G  3 25  ? 36.709  -34.795 53.539   1.00 261.45 ? 23   GLN G CA  1 
ATOM   18046 C  C   . GLN G  3 25  ? 35.820  -35.756 54.324   1.00 260.77 ? 23   GLN G C   1 
ATOM   18047 O  O   . GLN G  3 25  ? 34.613  -35.836 54.075   1.00 258.43 ? 23   GLN G O   1 
ATOM   18048 C  CB  . GLN G  3 25  ? 37.667  -35.576 52.633   1.00 265.90 ? 23   GLN G CB  1 
ATOM   18049 C  CG  . GLN G  3 25  ? 36.978  -36.470 51.600   1.00 261.73 ? 23   GLN G CG  1 
ATOM   18050 C  CD  . GLN G  3 25  ? 37.946  -37.397 50.878   1.00 254.59 ? 23   GLN G CD  1 
ATOM   18051 O  OE1 . GLN G  3 25  ? 39.009  -37.736 51.400   1.00 253.14 ? 23   GLN G OE1 1 
ATOM   18052 N  NE2 . GLN G  3 25  ? 37.580  -37.811 49.671   1.00 251.71 ? 23   GLN G NE2 1 
ATOM   18053 N  N   . ILE G  3 26  ? 36.405  -36.489 55.278   1.00 253.25 ? 24   ILE G N   1 
ATOM   18054 C  CA  . ILE G  3 26  ? 35.657  -37.494 56.032   1.00 243.96 ? 24   ILE G CA  1 
ATOM   18055 C  C   . ILE G  3 26  ? 34.461  -36.859 56.730   1.00 246.84 ? 24   ILE G C   1 
ATOM   18056 O  O   . ILE G  3 26  ? 33.341  -37.383 56.683   1.00 241.61 ? 24   ILE G O   1 
ATOM   18057 C  CB  . ILE G  3 26  ? 36.580  -38.203 57.038   1.00 248.07 ? 24   ILE G CB  1 
ATOM   18058 C  CG1 . ILE G  3 26  ? 37.729  -38.901 56.311   1.00 247.93 ? 24   ILE G CG1 1 
ATOM   18059 C  CG2 . ILE G  3 26  ? 35.790  -39.192 57.880   1.00 252.07 ? 24   ILE G CG2 1 
ATOM   18060 C  CD1 . ILE G  3 26  ? 38.697  -39.597 57.238   1.00 252.47 ? 24   ILE G CD1 1 
ATOM   18061 N  N   . LEU G  3 27  ? 34.685  -35.721 57.396   1.00 253.66 ? 25   LEU G N   1 
ATOM   18062 C  CA  . LEU G  3 27  ? 33.588  -35.028 58.061   1.00 257.58 ? 25   LEU G CA  1 
ATOM   18063 C  C   . LEU G  3 27  ? 32.536  -34.560 57.062   1.00 243.45 ? 25   LEU G C   1 
ATOM   18064 O  O   . LEU G  3 27  ? 31.340  -34.569 57.373   1.00 238.75 ? 25   LEU G O   1 
ATOM   18065 C  CB  . LEU G  3 27  ? 34.129  -33.843 58.867   1.00 274.08 ? 25   LEU G CB  1 
ATOM   18066 C  CG  . LEU G  3 27  ? 35.107  -34.161 60.004   1.00 276.30 ? 25   LEU G CG  1 
ATOM   18067 C  CD1 . LEU G  3 27  ? 35.595  -32.886 60.684   1.00 286.06 ? 25   LEU G CD1 1 
ATOM   18068 C  CD2 . LEU G  3 27  ? 34.476  -35.103 61.019   1.00 272.65 ? 25   LEU G CD2 1 
ATOM   18069 N  N   . SER G  3 28  ? 32.954  -34.159 55.857   1.00 244.19 ? 26   SER G N   1 
ATOM   18070 C  CA  . SER G  3 28  ? 31.976  -33.764 54.848   1.00 254.45 ? 26   SER G CA  1 
ATOM   18071 C  C   . SER G  3 28  ? 31.260  -34.974 54.264   1.00 259.99 ? 26   SER G C   1 
ATOM   18072 O  O   . SER G  3 28  ? 30.078  -34.881 53.911   1.00 262.55 ? 26   SER G O   1 
ATOM   18073 C  CB  . SER G  3 28  ? 32.650  -32.951 53.737   1.00 253.13 ? 26   SER G CB  1 
ATOM   18074 O  OG  . SER G  3 28  ? 33.640  -33.703 53.058   1.00 241.71 ? 26   SER G OG  1 
ATOM   18075 N  N   . LYS G  3 29  ? 31.952  -36.114 54.155   1.00 258.54 ? 27   LYS G N   1 
ATOM   18076 C  CA  . LYS G  3 29  ? 31.302  -37.321 53.655   1.00 251.95 ? 27   LYS G CA  1 
ATOM   18077 C  C   . LYS G  3 29  ? 30.240  -37.820 54.624   1.00 257.77 ? 27   LYS G C   1 
ATOM   18078 O  O   . LYS G  3 29  ? 29.203  -38.336 54.195   1.00 255.98 ? 27   LYS G O   1 
ATOM   18079 C  CB  . LYS G  3 29  ? 32.348  -38.406 53.386   1.00 244.61 ? 27   LYS G CB  1 
ATOM   18080 C  CG  . LYS G  3 29  ? 33.337  -38.042 52.280   1.00 253.73 ? 27   LYS G CG  1 
ATOM   18081 C  CD  . LYS G  3 29  ? 34.419  -39.101 52.110   1.00 253.19 ? 27   LYS G CD  1 
ATOM   18082 C  CE  . LYS G  3 29  ? 33.892  -40.332 51.394   1.00 245.89 ? 27   LYS G CE  1 
ATOM   18083 N  NZ  . LYS G  3 29  ? 33.537  -40.028 49.982   1.00 245.08 ? 27   LYS G NZ  1 
ATOM   18084 N  N   . LEU G  3 30  ? 30.472  -37.663 55.925   1.00 258.01 ? 28   LEU G N   1 
ATOM   18085 C  CA  . LEU G  3 30  ? 29.464  -37.970 56.929   1.00 248.67 ? 28   LEU G CA  1 
ATOM   18086 C  C   . LEU G  3 30  ? 28.470  -36.835 57.116   1.00 239.35 ? 28   LEU G C   1 
ATOM   18087 O  O   . LEU G  3 30  ? 27.575  -36.950 57.964   1.00 231.54 ? 28   LEU G O   1 
ATOM   18088 C  CB  . LEU G  3 30  ? 30.137  -38.294 58.266   1.00 244.51 ? 28   LEU G CB  1 
ATOM   18089 C  CG  . LEU G  3 30  ? 31.130  -39.455 58.277   1.00 241.16 ? 28   LEU G CG  1 
ATOM   18090 C  CD1 . LEU G  3 30  ? 31.805  -39.556 59.633   1.00 252.87 ? 28   LEU G CD1 1 
ATOM   18091 C  CD2 . LEU G  3 30  ? 30.433  -40.757 57.933   1.00 238.83 ? 28   LEU G CD2 1 
ATOM   18092 N  N   . ARG G  3 31  ? 28.605  -35.755 56.344   1.00 241.64 ? 29   ARG G N   1 
ATOM   18093 C  CA  . ARG G  3 31  ? 27.792  -34.555 56.511   1.00 244.30 ? 29   ARG G CA  1 
ATOM   18094 C  C   . ARG G  3 31  ? 27.844  -34.069 57.958   1.00 256.36 ? 29   ARG G C   1 
ATOM   18095 O  O   . ARG G  3 31  ? 26.838  -33.653 58.536   1.00 269.26 ? 29   ARG G O   1 
ATOM   18096 C  CB  . ARG G  3 31  ? 26.350  -34.798 56.058   1.00 245.48 ? 29   ARG G CB  1 
ATOM   18097 C  CG  . ARG G  3 31  ? 25.578  -33.536 55.693   1.00 259.95 ? 29   ARG G CG  1 
ATOM   18098 C  CD  . ARG G  3 31  ? 24.122  -33.847 55.368   1.00 269.66 ? 29   ARG G CD  1 
ATOM   18099 N  NE  . ARG G  3 31  ? 23.985  -34.727 54.209   1.00 267.81 ? 29   ARG G NE  1 
ATOM   18100 C  CZ  . ARG G  3 31  ? 23.664  -34.316 52.985   1.00 265.88 ? 29   ARG G CZ  1 
ATOM   18101 N  NH1 . ARG G  3 31  ? 23.438  -33.031 52.748   1.00 261.95 ? 29   ARG G NH1 1 
ATOM   18102 N  NH2 . ARG G  3 31  ? 23.564  -35.194 51.995   1.00 264.85 ? 29   ARG G NH2 1 
ATOM   18103 N  N   . LEU G  3 32  ? 29.037  -34.128 58.549   1.00 256.62 ? 30   LEU G N   1 
ATOM   18104 C  CA  . LEU G  3 32  ? 29.243  -33.831 59.960   1.00 261.14 ? 30   LEU G CA  1 
ATOM   18105 C  C   . LEU G  3 32  ? 30.268  -32.718 60.135   1.00 261.06 ? 30   LEU G C   1 
ATOM   18106 O  O   . LEU G  3 32  ? 31.224  -32.605 59.359   1.00 254.93 ? 30   LEU G O   1 
ATOM   18107 C  CB  . LEU G  3 32  ? 29.702  -35.082 60.723   1.00 248.82 ? 30   LEU G CB  1 
ATOM   18108 C  CG  . LEU G  3 32  ? 28.645  -36.165 60.937   1.00 247.60 ? 30   LEU G CG  1 
ATOM   18109 C  CD1 . LEU G  3 32  ? 29.221  -37.325 61.734   1.00 248.60 ? 30   LEU G CD1 1 
ATOM   18110 C  CD2 . LEU G  3 32  ? 27.431  -35.576 61.636   1.00 266.62 ? 30   LEU G CD2 1 
ATOM   18111 N  N   . ALA G  3 33  ? 30.061  -31.894 61.160   1.00 272.14 ? 31   ALA G N   1 
ATOM   18112 C  CA  . ALA G  3 33  ? 31.035  -30.877 61.534   1.00 270.84 ? 31   ALA G CA  1 
ATOM   18113 C  C   . ALA G  3 33  ? 31.985  -31.367 62.614   1.00 272.63 ? 31   ALA G C   1 
ATOM   18114 O  O   . ALA G  3 33  ? 33.142  -30.931 62.659   1.00 272.13 ? 31   ALA G O   1 
ATOM   18115 C  CB  . ALA G  3 33  ? 30.319  -29.609 62.016   1.00 274.89 ? 31   ALA G CB  1 
ATOM   18116 N  N   . SER G  3 34  ? 31.524  -32.275 63.472   1.00 273.98 ? 32   SER G N   1 
ATOM   18117 C  CA  . SER G  3 34  ? 32.312  -32.783 64.582   1.00 275.36 ? 32   SER G CA  1 
ATOM   18118 C  C   . SER G  3 34  ? 31.958  -34.243 64.829   1.00 272.94 ? 32   SER G C   1 
ATOM   18119 O  O   . SER G  3 34  ? 30.823  -34.661 64.570   1.00 267.84 ? 32   SER G O   1 
ATOM   18120 C  CB  . SER G  3 34  ? 32.079  -31.959 65.858   1.00 275.59 ? 32   SER G CB  1 
ATOM   18121 O  OG  . SER G  3 34  ? 30.699  -31.880 66.173   1.00 267.56 ? 32   SER G OG  1 
ATOM   18122 N  N   . PRO G  3 35  ? 32.910  -35.036 65.319   1.00 270.84 ? 33   PRO G N   1 
ATOM   18123 C  CA  . PRO G  3 35  ? 32.649  -36.450 65.652   1.00 263.16 ? 33   PRO G CA  1 
ATOM   18124 C  C   . PRO G  3 35  ? 31.670  -36.596 66.806   1.00 273.05 ? 33   PRO G C   1 
ATOM   18125 O  O   . PRO G  3 35  ? 31.503  -35.669 67.615   1.00 288.72 ? 33   PRO G O   1 
ATOM   18126 C  CB  . PRO G  3 35  ? 34.044  -36.969 66.041   1.00 256.29 ? 33   PRO G CB  1 
ATOM   18127 C  CG  . PRO G  3 35  ? 34.992  -36.063 65.308   1.00 255.08 ? 33   PRO G CG  1 
ATOM   18128 C  CD  . PRO G  3 35  ? 34.345  -34.715 65.385   1.00 271.57 ? 33   PRO G CD  1 
ATOM   18129 N  N   . PRO G  3 36  ? 31.017  -37.754 66.933   1.00 263.67 ? 34   PRO G N   1 
ATOM   18130 C  CA  . PRO G  3 36  ? 30.083  -37.962 68.049   1.00 271.72 ? 34   PRO G CA  1 
ATOM   18131 C  C   . PRO G  3 36  ? 30.813  -38.063 69.381   1.00 281.17 ? 34   PRO G C   1 
ATOM   18132 O  O   . PRO G  3 36  ? 32.041  -38.130 69.456   1.00 283.64 ? 34   PRO G O   1 
ATOM   18133 C  CB  . PRO G  3 36  ? 29.386  -39.277 67.693   1.00 258.75 ? 34   PRO G CB  1 
ATOM   18134 C  CG  . PRO G  3 36  ? 30.372  -40.000 66.836   1.00 254.36 ? 34   PRO G CG  1 
ATOM   18135 C  CD  . PRO G  3 36  ? 31.093  -38.931 66.050   1.00 256.37 ? 34   PRO G CD  1 
ATOM   18136 N  N   . SER G  3 37  ? 30.023  -38.087 70.451   1.00 283.16 ? 35   SER G N   1 
ATOM   18137 C  CA  . SER G  3 37  ? 30.560  -38.001 71.808   1.00 281.85 ? 35   SER G CA  1 
ATOM   18138 C  C   . SER G  3 37  ? 30.720  -39.366 72.477   1.00 284.66 ? 35   SER G C   1 
ATOM   18139 O  O   . SER G  3 37  ? 31.538  -39.522 73.390   1.00 294.19 ? 35   SER G O   1 
ATOM   18140 C  CB  . SER G  3 37  ? 29.668  -37.099 72.668   1.00 284.81 ? 35   SER G CB  1 
ATOM   18141 O  OG  . SER G  3 37  ? 29.685  -35.763 72.196   1.00 291.83 ? 35   SER G OG  1 
ATOM   18142 N  N   . GLU G  3 40  ? 31.261  -46.180 73.803   1.00 238.05 ? 38   GLU G N   1 
ATOM   18143 C  CA  . GLU G  3 40  ? 31.786  -46.776 75.033   1.00 233.19 ? 38   GLU G CA  1 
ATOM   18144 C  C   . GLU G  3 40  ? 31.218  -48.205 75.072   1.00 234.86 ? 38   GLU G C   1 
ATOM   18145 O  O   . GLU G  3 40  ? 30.160  -48.446 74.475   1.00 230.50 ? 38   GLU G O   1 
ATOM   18146 C  CB  . GLU G  3 40  ? 31.418  -45.881 76.276   1.00 222.86 ? 38   GLU G CB  1 
ATOM   18147 C  CG  . GLU G  3 40  ? 31.271  -46.554 77.744   1.00 226.36 ? 38   GLU G CG  1 
ATOM   18148 C  CD  . GLU G  3 40  ? 29.774  -47.027 78.181   1.00 225.58 ? 38   GLU G CD  1 
ATOM   18149 O  OE1 . GLU G  3 40  ? 28.863  -47.239 77.286   1.00 220.82 ? 38   GLU G OE1 1 
ATOM   18150 O  OE2 . GLU G  3 40  ? 29.547  -47.220 79.438   1.00 230.07 ? 38   GLU G OE2 1 
ATOM   18151 N  N   . VAL G  3 41  ? 31.929  -49.137 75.735   1.00 247.78 ? 39   VAL G N   1 
ATOM   18152 C  CA  . VAL G  3 41  ? 31.718  -50.627 75.731   1.00 241.96 ? 39   VAL G CA  1 
ATOM   18153 C  C   . VAL G  3 41  ? 31.928  -51.270 74.297   1.00 244.57 ? 39   VAL G C   1 
ATOM   18154 O  O   . VAL G  3 41  ? 31.738  -50.614 73.272   1.00 236.78 ? 39   VAL G O   1 
ATOM   18155 C  CB  . VAL G  3 41  ? 30.326  -50.998 76.419   1.00 229.76 ? 39   VAL G CB  1 
ATOM   18156 C  CG1 . VAL G  3 41  ? 30.020  -52.539 76.429   1.00 228.48 ? 39   VAL G CG1 1 
ATOM   18157 C  CG2 . VAL G  3 41  ? 30.240  -50.404 77.860   1.00 228.56 ? 39   VAL G CG2 1 
ATOM   18158 N  N   . PRO G  3 42  ? 32.498  -52.491 74.229   1.00 269.24 ? 40   PRO G N   1 
ATOM   18159 C  CA  . PRO G  3 42  ? 33.044  -53.301 75.325   1.00 272.16 ? 40   PRO G CA  1 
ATOM   18160 C  C   . PRO G  3 42  ? 34.556  -53.221 75.559   1.00 283.93 ? 40   PRO G C   1 
ATOM   18161 O  O   . PRO G  3 42  ? 35.310  -53.008 74.610   1.00 287.88 ? 40   PRO G O   1 
ATOM   18162 C  CB  . PRO G  3 42  ? 32.646  -54.724 74.911   1.00 258.69 ? 40   PRO G CB  1 
ATOM   18163 C  CG  . PRO G  3 42  ? 32.363  -54.670 73.433   1.00 255.06 ? 40   PRO G CG  1 
ATOM   18164 C  CD  . PRO G  3 42  ? 32.496  -53.252 72.966   1.00 260.96 ? 40   PRO G CD  1 
ATOM   18165 N  N   . PRO G  3 43  ? 34.994  -53.420 76.808   1.00 290.63 ? 41   PRO G N   1 
ATOM   18166 C  CA  . PRO G  3 43  ? 36.442  -53.436 77.068   1.00 285.74 ? 41   PRO G CA  1 
ATOM   18167 C  C   . PRO G  3 43  ? 37.146  -54.576 76.366   1.00 275.30 ? 41   PRO G C   1 
ATOM   18168 O  O   . PRO G  3 43  ? 38.373  -54.528 76.194   1.00 274.21 ? 41   PRO G O   1 
ATOM   18169 C  CB  . PRO G  3 43  ? 36.530  -53.564 78.595   1.00 287.05 ? 41   PRO G CB  1 
ATOM   18170 C  CG  . PRO G  3 43  ? 35.254  -54.217 78.991   1.00 287.70 ? 41   PRO G CG  1 
ATOM   18171 C  CD  . PRO G  3 43  ? 34.211  -53.712 78.024   1.00 290.50 ? 41   PRO G CD  1 
ATOM   18172 N  N   . GLY G  3 44  ? 36.400  -55.597 75.950   1.00 341.29 ? 42   GLY G N   1 
ATOM   18173 C  CA  . GLY G  3 44  ? 36.905  -56.643 75.096   1.00 308.69 ? 42   GLY G CA  1 
ATOM   18174 C  C   . GLY G  3 44  ? 36.485  -56.426 73.654   1.00 295.35 ? 42   GLY G C   1 
ATOM   18175 O  O   . GLY G  3 44  ? 36.185  -55.302 73.235   1.00 285.48 ? 42   GLY G O   1 
ATOM   18176 N  N   . PRO G  3 45  ? 36.460  -57.499 72.862   1.00 312.97 ? 43   PRO G N   1 
ATOM   18177 C  CA  . PRO G  3 45  ? 36.132  -57.356 71.434   1.00 294.16 ? 43   PRO G CA  1 
ATOM   18178 C  C   . PRO G  3 45  ? 34.659  -57.030 71.228   1.00 295.47 ? 43   PRO G C   1 
ATOM   18179 O  O   . PRO G  3 45  ? 33.779  -57.657 71.822   1.00 293.40 ? 43   PRO G O   1 
ATOM   18180 C  CB  . PRO G  3 45  ? 36.496  -58.725 70.843   1.00 286.12 ? 43   PRO G CB  1 
ATOM   18181 C  CG  . PRO G  3 45  ? 36.476  -59.664 72.001   1.00 311.81 ? 43   PRO G CG  1 
ATOM   18182 C  CD  . PRO G  3 45  ? 36.885  -58.866 73.204   1.00 324.62 ? 43   PRO G CD  1 
ATOM   18183 N  N   . LEU G  3 46  ? 34.400  -56.045 70.364   1.00 299.01 ? 44   LEU G N   1 
ATOM   18184 C  CA  . LEU G  3 46  ? 33.045  -55.587 70.091   1.00 306.33 ? 44   LEU G CA  1 
ATOM   18185 C  C   . LEU G  3 46  ? 32.232  -56.702 69.419   1.00 313.79 ? 44   LEU G C   1 
ATOM   18186 O  O   . LEU G  3 46  ? 32.799  -57.692 68.944   1.00 312.13 ? 44   LEU G O   1 
ATOM   18187 C  CB  . LEU G  3 46  ? 33.094  -54.320 69.236   1.00 282.46 ? 44   LEU G CB  1 
ATOM   18188 C  CG  . LEU G  3 46  ? 33.946  -54.358 67.973   1.00 257.41 ? 44   LEU G CG  1 
ATOM   18189 C  CD1 . LEU G  3 46  ? 33.122  -54.817 66.785   1.00 249.76 ? 44   LEU G CD1 1 
ATOM   18190 C  CD2 . LEU G  3 46  ? 34.552  -52.993 67.719   1.00 257.08 ? 44   LEU G CD2 1 
ATOM   18191 N  N   . PRO G  3 47  ? 30.896  -56.565 69.376   1.00 304.23 ? 45   PRO G N   1 
ATOM   18192 C  CA  . PRO G  3 47  ? 30.048  -57.682 68.930   1.00 284.76 ? 45   PRO G CA  1 
ATOM   18193 C  C   . PRO G  3 47  ? 30.395  -58.145 67.526   1.00 247.47 ? 45   PRO G C   1 
ATOM   18194 O  O   . PRO G  3 47  ? 30.635  -57.340 66.625   1.00 244.57 ? 45   PRO G O   1 
ATOM   18195 C  CB  . PRO G  3 47  ? 28.635  -57.098 68.988   1.00 275.77 ? 45   PRO G CB  1 
ATOM   18196 C  CG  . PRO G  3 47  ? 28.836  -55.624 68.903   1.00 270.27 ? 45   PRO G CG  1 
ATOM   18197 C  CD  . PRO G  3 47  ? 30.076  -55.383 69.694   1.00 296.99 ? 45   PRO G CD  1 
ATOM   18198 N  N   . GLU G  3 48  ? 30.410  -59.467 67.352   1.00 244.16 ? 46   GLU G N   1 
ATOM   18199 C  CA  . GLU G  3 48  ? 30.719  -60.091 66.076   1.00 246.12 ? 46   GLU G CA  1 
ATOM   18200 C  C   . GLU G  3 48  ? 29.557  -60.041 65.097   1.00 247.24 ? 46   GLU G C   1 
ATOM   18201 O  O   . GLU G  3 48  ? 29.677  -60.581 63.990   1.00 245.32 ? 46   GLU G O   1 
ATOM   18202 C  CB  . GLU G  3 48  ? 31.155  -61.543 66.296   1.00 243.81 ? 46   GLU G CB  1 
ATOM   18203 C  CG  . GLU G  3 48  ? 32.464  -61.672 67.049   1.00 243.13 ? 46   GLU G CG  1 
ATOM   18204 C  CD  . GLU G  3 48  ? 33.018  -63.079 67.017   1.00 245.77 ? 46   GLU G CD  1 
ATOM   18205 O  OE1 . GLU G  3 48  ? 32.264  -64.008 66.662   1.00 244.55 ? 46   GLU G OE1 1 
ATOM   18206 O  OE2 . GLU G  3 48  ? 34.210  -63.254 67.342   1.00 249.40 ? 46   GLU G OE2 1 
ATOM   18207 N  N   . ALA G  3 49  ? 28.437  -59.421 65.474   1.00 241.00 ? 47   ALA G N   1 
ATOM   18208 C  CA  . ALA G  3 49  ? 27.364  -59.207 64.511   1.00 240.96 ? 47   ALA G CA  1 
ATOM   18209 C  C   . ALA G  3 49  ? 27.751  -58.138 63.499   1.00 244.57 ? 47   ALA G C   1 
ATOM   18210 O  O   . ALA G  3 49  ? 27.430  -58.256 62.311   1.00 228.22 ? 47   ALA G O   1 
ATOM   18211 C  CB  . ALA G  3 49  ? 26.075  -58.821 65.235   1.00 237.96 ? 47   ALA G CB  1 
ATOM   18212 N  N   . VAL G  3 50  ? 28.439  -57.087 63.952   1.00 261.17 ? 48   VAL G N   1 
ATOM   18213 C  CA  . VAL G  3 50  ? 28.950  -56.081 63.029   1.00 242.43 ? 48   VAL G CA  1 
ATOM   18214 C  C   . VAL G  3 50  ? 30.318  -56.468 62.484   1.00 239.37 ? 48   VAL G C   1 
ATOM   18215 O  O   . VAL G  3 50  ? 30.732  -55.939 61.444   1.00 249.86 ? 48   VAL G O   1 
ATOM   18216 C  CB  . VAL G  3 50  ? 29.020  -54.699 63.697   1.00 247.79 ? 48   VAL G CB  1 
ATOM   18217 C  CG1 . VAL G  3 50  ? 27.655  -54.308 64.237   1.00 259.26 ? 48   VAL G CG1 1 
ATOM   18218 C  CG2 . VAL G  3 50  ? 30.071  -54.686 64.799   1.00 262.87 ? 48   VAL G CG2 1 
ATOM   18219 N  N   . LEU G  3 51  ? 31.036  -57.372 63.159   1.00 238.83 ? 49   LEU G N   1 
ATOM   18220 C  CA  . LEU G  3 51  ? 32.270  -57.900 62.590   1.00 229.30 ? 49   LEU G CA  1 
ATOM   18221 C  C   . LEU G  3 51  ? 31.983  -58.846 61.435   1.00 239.90 ? 49   LEU G C   1 
ATOM   18222 O  O   . LEU G  3 51  ? 32.824  -59.000 60.540   1.00 245.15 ? 49   LEU G O   1 
ATOM   18223 C  CB  . LEU G  3 51  ? 33.092  -58.613 63.665   1.00 239.24 ? 49   LEU G CB  1 
ATOM   18224 C  CG  . LEU G  3 51  ? 33.740  -57.720 64.722   1.00 261.66 ? 49   LEU G CG  1 
ATOM   18225 C  CD1 . LEU G  3 51  ? 34.534  -58.552 65.720   1.00 278.14 ? 49   LEU G CD1 1 
ATOM   18226 C  CD2 . LEU G  3 51  ? 34.623  -56.672 64.065   1.00 241.06 ? 49   LEU G CD2 1 
ATOM   18227 N  N   . ALA G  3 52  ? 30.811  -59.489 61.439   1.00 251.75 ? 50   ALA G N   1 
ATOM   18228 C  CA  . ALA G  3 52  ? 30.397  -60.278 60.285   1.00 245.82 ? 50   ALA G CA  1 
ATOM   18229 C  C   . ALA G  3 52  ? 30.076  -59.379 59.099   1.00 238.99 ? 50   ALA G C   1 
ATOM   18230 O  O   . ALA G  3 52  ? 30.329  -59.749 57.947   1.00 241.15 ? 50   ALA G O   1 
ATOM   18231 C  CB  . ALA G  3 52  ? 29.190  -61.149 60.645   1.00 246.38 ? 50   ALA G CB  1 
ATOM   18232 N  N   . LEU G  3 53  ? 29.515  -58.195 59.363   1.00 235.00 ? 51   LEU G N   1 
ATOM   18233 C  CA  . LEU G  3 53  ? 29.341  -57.205 58.307   1.00 231.93 ? 51   LEU G CA  1 
ATOM   18234 C  C   . LEU G  3 53  ? 30.683  -56.670 57.829   1.00 228.57 ? 51   LEU G C   1 
ATOM   18235 O  O   . LEU G  3 53  ? 30.896  -56.502 56.623   1.00 234.82 ? 51   LEU G O   1 
ATOM   18236 C  CB  . LEU G  3 53  ? 28.463  -56.054 58.800   1.00 236.09 ? 51   LEU G CB  1 
ATOM   18237 C  CG  . LEU G  3 53  ? 26.949  -56.167 58.638   1.00 230.71 ? 51   LEU G CG  1 
ATOM   18238 C  CD1 . LEU G  3 53  ? 26.381  -57.226 59.559   1.00 237.19 ? 51   LEU G CD1 1 
ATOM   18239 C  CD2 . LEU G  3 53  ? 26.301  -54.822 58.905   1.00 235.05 ? 51   LEU G CD2 1 
ATOM   18240 N  N   . TYR G  3 54  ? 31.600  -56.397 58.758   1.00 221.14 ? 52   TYR G N   1 
ATOM   18241 C  CA  . TYR G  3 54  ? 32.885  -55.823 58.377   1.00 222.71 ? 52   TYR G CA  1 
ATOM   18242 C  C   . TYR G  3 54  ? 33.745  -56.832 57.628   1.00 224.16 ? 52   TYR G C   1 
ATOM   18243 O  O   . TYR G  3 54  ? 34.491  -56.461 56.715   1.00 224.39 ? 52   TYR G O   1 
ATOM   18244 C  CB  . TYR G  3 54  ? 33.612  -55.317 59.618   1.00 250.49 ? 52   TYR G CB  1 
ATOM   18245 C  CG  . TYR G  3 54  ? 34.941  -54.664 59.331   1.00 258.68 ? 52   TYR G CG  1 
ATOM   18246 C  CD1 . TYR G  3 54  ? 35.007  -53.403 58.756   1.00 252.09 ? 52   TYR G CD1 1 
ATOM   18247 C  CD2 . TYR G  3 54  ? 36.131  -55.303 59.653   1.00 273.76 ? 52   TYR G CD2 1 
ATOM   18248 C  CE1 . TYR G  3 54  ? 36.223  -52.801 58.500   1.00 264.55 ? 52   TYR G CE1 1 
ATOM   18249 C  CE2 . TYR G  3 54  ? 37.350  -54.708 59.403   1.00 275.23 ? 52   TYR G CE2 1 
ATOM   18250 C  CZ  . TYR G  3 54  ? 37.391  -53.458 58.826   1.00 272.09 ? 52   TYR G CZ  1 
ATOM   18251 O  OH  . TYR G  3 54  ? 38.606  -52.865 58.574   1.00 273.77 ? 52   TYR G OH  1 
ATOM   18252 N  N   . ASN G  3 55  ? 33.662  -58.113 58.002   1.00 220.51 ? 53   ASN G N   1 
ATOM   18253 C  CA  . ASN G  3 55  ? 34.370  -59.151 57.263   1.00 224.08 ? 53   ASN G CA  1 
ATOM   18254 C  C   . ASN G  3 55  ? 33.722  -59.437 55.913   1.00 235.46 ? 53   ASN G C   1 
ATOM   18255 O  O   . ASN G  3 55  ? 34.392  -59.965 55.019   1.00 232.25 ? 53   ASN G O   1 
ATOM   18256 C  CB  . ASN G  3 55  ? 34.446  -60.431 58.098   1.00 225.02 ? 53   ASN G CB  1 
ATOM   18257 C  CG  . ASN G  3 55  ? 35.559  -60.389 59.129   1.00 251.40 ? 53   ASN G CG  1 
ATOM   18258 O  OD1 . ASN G  3 55  ? 36.087  -59.321 59.442   1.00 241.63 ? 53   ASN G OD1 1 
ATOM   18259 N  ND2 . ASN G  3 55  ? 35.915  -61.556 59.667   1.00 332.47 ? 53   ASN G ND2 1 
ATOM   18260 N  N   . SER G  3 56  ? 32.440  -59.096 55.743   1.00 249.19 ? 54   SER G N   1 
ATOM   18261 C  CA  . SER G  3 56  ? 31.765  -59.282 54.463   1.00 235.58 ? 54   SER G CA  1 
ATOM   18262 C  C   . SER G  3 56  ? 31.936  -58.093 53.530   1.00 219.03 ? 54   SER G C   1 
ATOM   18263 O  O   . SER G  3 56  ? 31.700  -58.231 52.325   1.00 213.70 ? 54   SER G O   1 
ATOM   18264 C  CB  . SER G  3 56  ? 30.271  -59.535 54.680   1.00 230.42 ? 54   SER G CB  1 
ATOM   18265 O  OG  . SER G  3 56  ? 30.049  -60.669 55.500   1.00 237.97 ? 54   SER G OG  1 
ATOM   18266 N  N   . THR G  3 57  ? 32.327  -56.930 54.053   1.00 211.18 ? 55   THR G N   1 
ATOM   18267 C  CA  . THR G  3 57  ? 32.522  -55.768 53.195   1.00 209.87 ? 55   THR G CA  1 
ATOM   18268 C  C   . THR G  3 57  ? 33.930  -55.713 52.612   1.00 225.10 ? 55   THR G C   1 
ATOM   18269 O  O   . THR G  3 57  ? 34.107  -55.223 51.490   1.00 237.90 ? 55   THR G O   1 
ATOM   18270 C  CB  . THR G  3 57  ? 32.223  -54.484 53.969   1.00 209.82 ? 55   THR G CB  1 
ATOM   18271 O  OG1 . THR G  3 57  ? 31.008  -54.638 54.710   1.00 221.68 ? 55   THR G OG1 1 
ATOM   18272 C  CG2 . THR G  3 57  ? 32.059  -53.321 53.009   1.00 205.33 ? 55   THR G CG2 1 
ATOM   18273 N  N   . ARG G  3 58  ? 34.936  -56.210 53.339   1.00 239.55 ? 56   ARG G N   1 
ATOM   18274 C  CA  . ARG G  3 58  ? 36.312  -56.228 52.848   1.00 244.10 ? 56   ARG G CA  1 
ATOM   18275 C  C   . ARG G  3 58  ? 36.596  -57.378 51.893   1.00 251.37 ? 56   ARG G C   1 
ATOM   18276 O  O   . ARG G  3 58  ? 37.654  -57.382 51.253   1.00 257.26 ? 56   ARG G O   1 
ATOM   18277 C  CB  . ARG G  3 58  ? 37.298  -56.316 54.015   1.00 241.30 ? 56   ARG G CB  1 
ATOM   18278 C  CG  . ARG G  3 58  ? 37.221  -55.159 54.984   1.00 235.66 ? 56   ARG G CG  1 
ATOM   18279 C  CD  . ARG G  3 58  ? 38.437  -55.114 55.894   1.00 235.44 ? 56   ARG G CD  1 
ATOM   18280 N  NE  . ARG G  3 58  ? 38.480  -56.219 56.847   1.00 237.62 ? 56   ARG G NE  1 
ATOM   18281 C  CZ  . ARG G  3 58  ? 39.237  -57.301 56.704   1.00 244.54 ? 56   ARG G CZ  1 
ATOM   18282 N  NH1 . ARG G  3 58  ? 40.015  -57.428 55.639   1.00 247.95 ? 56   ARG G NH1 1 
ATOM   18283 N  NH2 . ARG G  3 58  ? 39.219  -58.253 57.627   1.00 250.91 ? 56   ARG G NH2 1 
ATOM   18284 N  N   . ASP G  3 59  ? 35.685  -58.346 51.788   1.00 244.47 ? 57   ASP G N   1 
ATOM   18285 C  CA  . ASP G  3 59  ? 35.888  -59.577 51.023   1.00 238.09 ? 57   ASP G CA  1 
ATOM   18286 C  C   . ASP G  3 59  ? 35.419  -59.347 49.589   1.00 240.67 ? 57   ASP G C   1 
ATOM   18287 O  O   . ASP G  3 59  ? 34.261  -59.598 49.242   1.00 244.04 ? 57   ASP G O   1 
ATOM   18288 C  CB  . ASP G  3 59  ? 35.142  -60.723 51.698   1.00 231.45 ? 57   ASP G CB  1 
ATOM   18289 C  CG  . ASP G  3 59  ? 35.439  -62.082 51.083   1.00 230.92 ? 57   ASP G CG  1 
ATOM   18290 O  OD1 . ASP G  3 59  ? 36.077  -62.150 50.011   1.00 237.26 ? 57   ASP G OD1 1 
ATOM   18291 O  OD2 . ASP G  3 59  ? 35.013  -63.093 51.675   1.00 232.57 ? 57   ASP G OD2 1 
ATOM   18292 N  N   . ARG G  3 60  ? 36.327  -58.888 48.731   1.00 238.57 ? 58   ARG G N   1 
ATOM   18293 C  CA  . ARG G  3 60  ? 36.006  -58.633 47.325   1.00 235.30 ? 58   ARG G CA  1 
ATOM   18294 C  C   . ARG G  3 60  ? 36.751  -59.635 46.430   1.00 245.67 ? 58   ARG G C   1 
ATOM   18295 O  O   . ARG G  3 60  ? 37.913  -59.436 46.069   1.00 256.05 ? 58   ARG G O   1 
ATOM   18296 C  CB  . ARG G  3 60  ? 36.314  -57.166 46.948   1.00 234.24 ? 58   ARG G CB  1 
ATOM   18297 C  CG  . ARG G  3 60  ? 37.701  -56.619 47.313   1.00 242.63 ? 58   ARG G CG  1 
ATOM   18298 C  CD  . ARG G  3 60  ? 38.588  -56.500 46.070   1.00 247.88 ? 58   ARG G CD  1 
ATOM   18299 N  NE  . ARG G  3 60  ? 39.574  -55.424 46.143   1.00 245.14 ? 58   ARG G NE  1 
ATOM   18300 C  CZ  . ARG G  3 60  ? 40.564  -55.270 45.269   1.00 239.62 ? 58   ARG G CZ  1 
ATOM   18301 N  NH1 . ARG G  3 60  ? 40.704  -56.130 44.269   1.00 238.96 ? 58   ARG G NH1 1 
ATOM   18302 N  NH2 . ARG G  3 60  ? 41.418  -54.263 45.396   1.00 237.95 ? 58   ARG G NH2 1 
ATOM   18303 N  N   . VAL G  3 61  ? 36.065  -60.720 46.066   1.00 227.41 ? 59   VAL G N   1 
ATOM   18304 C  CA  . VAL G  3 61  ? 36.544  -61.635 45.030   1.00 222.45 ? 59   VAL G CA  1 
ATOM   18305 C  C   . VAL G  3 61  ? 35.666  -61.438 43.799   1.00 219.91 ? 59   VAL G C   1 
ATOM   18306 O  O   . VAL G  3 61  ? 36.080  -60.801 42.822   1.00 218.38 ? 59   VAL G O   1 
ATOM   18307 C  CB  . VAL G  3 61  ? 36.534  -63.108 45.494   1.00 217.91 ? 59   VAL G CB  1 
ATOM   18308 C  CG1 . VAL G  3 61  ? 37.110  -64.027 44.410   1.00 218.55 ? 59   VAL G CG1 1 
ATOM   18309 C  CG2 . VAL G  3 61  ? 37.315  -63.267 46.788   1.00 222.66 ? 59   VAL G CG2 1 
ATOM   18310 N  N   . ALA G  3 62  ? 34.444  -61.971 43.853   1.00 212.11 ? 60   ALA G N   1 
ATOM   18311 C  CA  . ALA G  3 62  ? 33.443  -61.841 42.788   1.00 197.86 ? 60   ALA G CA  1 
ATOM   18312 C  C   . ALA G  3 62  ? 33.889  -62.502 41.491   1.00 197.10 ? 60   ALA G C   1 
ATOM   18313 O  O   . ALA G  3 62  ? 33.055  -62.890 40.672   1.00 195.84 ? 60   ALA G O   1 
ATOM   18314 C  CB  . ALA G  3 62  ? 33.102  -60.371 42.542   1.00 194.66 ? 60   ALA G CB  1 
ATOM   18315 N  N   . ALA G  3 74  ? 29.308  -36.901 41.484   1.00 206.13 ? 72   ALA G N   1 
ATOM   18316 C  CA  . ALA G  3 74  ? 28.179  -37.756 41.829   1.00 200.99 ? 72   ALA G CA  1 
ATOM   18317 C  C   . ALA G  3 74  ? 28.033  -37.889 43.346   1.00 216.27 ? 72   ALA G C   1 
ATOM   18318 O  O   . ALA G  3 74  ? 28.135  -36.899 44.071   1.00 220.00 ? 72   ALA G O   1 
ATOM   18319 C  CB  . ALA G  3 74  ? 28.334  -39.123 41.187   1.00 196.15 ? 72   ALA G CB  1 
ATOM   18320 N  N   . ASP G  3 75  ? 27.799  -39.113 43.822   1.00 235.65 ? 73   ASP G N   1 
ATOM   18321 C  CA  . ASP G  3 75  ? 27.531  -39.369 45.240   1.00 232.54 ? 73   ASP G CA  1 
ATOM   18322 C  C   . ASP G  3 75  ? 28.846  -39.583 45.975   1.00 232.63 ? 73   ASP G C   1 
ATOM   18323 O  O   . ASP G  3 75  ? 29.402  -40.684 45.972   1.00 215.30 ? 73   ASP G O   1 
ATOM   18324 C  CB  . ASP G  3 75  ? 26.615  -40.573 45.408   1.00 218.15 ? 73   ASP G CB  1 
ATOM   18325 C  CG  . ASP G  3 75  ? 25.242  -40.333 44.841   1.00 212.45 ? 73   ASP G CG  1 
ATOM   18326 O  OD1 . ASP G  3 75  ? 25.048  -40.594 43.635   1.00 218.05 ? 73   ASP G OD1 1 
ATOM   18327 O  OD2 . ASP G  3 75  ? 24.360  -39.879 45.599   1.00 209.93 ? 73   ASP G OD2 1 
ATOM   18328 N  N   . TYR G  3 76  ? 29.334  -38.528 46.624   1.00 237.11 ? 74   TYR G N   1 
ATOM   18329 C  CA  . TYR G  3 76  ? 30.549  -38.606 47.418   1.00 238.17 ? 74   TYR G CA  1 
ATOM   18330 C  C   . TYR G  3 76  ? 30.282  -38.892 48.888   1.00 229.77 ? 74   TYR G C   1 
ATOM   18331 O  O   . TYR G  3 76  ? 31.229  -39.193 49.623   1.00 235.54 ? 74   TYR G O   1 
ATOM   18332 C  CB  . TYR G  3 76  ? 31.350  -37.303 47.298   1.00 244.92 ? 74   TYR G CB  1 
ATOM   18333 C  CG  . TYR G  3 76  ? 32.116  -37.163 46.001   1.00 252.51 ? 74   TYR G CG  1 
ATOM   18334 C  CD1 . TYR G  3 76  ? 33.343  -37.792 45.826   1.00 252.62 ? 74   TYR G CD1 1 
ATOM   18335 C  CD2 . TYR G  3 76  ? 31.620  -36.395 44.957   1.00 253.14 ? 74   TYR G CD2 1 
ATOM   18336 C  CE1 . TYR G  3 76  ? 34.049  -37.666 44.646   1.00 244.47 ? 74   TYR G CE1 1 
ATOM   18337 C  CE2 . TYR G  3 76  ? 32.318  -36.262 43.773   1.00 245.85 ? 74   TYR G CE2 1 
ATOM   18338 C  CZ  . TYR G  3 76  ? 33.531  -36.899 43.623   1.00 242.25 ? 74   TYR G CZ  1 
ATOM   18339 O  OH  . TYR G  3 76  ? 34.226  -36.767 42.446   1.00 238.76 ? 74   TYR G OH  1 
ATOM   18340 N  N   . TYR G  3 77  ? 29.031  -38.816 49.337   1.00 229.46 ? 75   TYR G N   1 
ATOM   18341 C  CA  . TYR G  3 77  ? 28.730  -39.009 50.747   1.00 241.68 ? 75   TYR G CA  1 
ATOM   18342 C  C   . TYR G  3 77  ? 28.806  -40.494 51.115   1.00 252.34 ? 75   TYR G C   1 
ATOM   18343 O  O   . TYR G  3 77  ? 29.033  -41.370 50.272   1.00 257.07 ? 75   TYR G O   1 
ATOM   18344 C  CB  . TYR G  3 77  ? 27.358  -38.427 51.081   1.00 234.36 ? 75   TYR G CB  1 
ATOM   18345 C  CG  . TYR G  3 77  ? 27.274  -36.921 50.949   1.00 235.32 ? 75   TYR G CG  1 
ATOM   18346 C  CD1 . TYR G  3 77  ? 27.571  -36.091 52.023   1.00 235.71 ? 75   TYR G CD1 1 
ATOM   18347 C  CD2 . TYR G  3 77  ? 26.891  -36.328 49.751   1.00 243.76 ? 75   TYR G CD2 1 
ATOM   18348 C  CE1 . TYR G  3 77  ? 27.493  -34.714 51.908   1.00 240.67 ? 75   TYR G CE1 1 
ATOM   18349 C  CE2 . TYR G  3 77  ? 26.810  -34.951 49.626   1.00 246.68 ? 75   TYR G CE2 1 
ATOM   18350 C  CZ  . TYR G  3 77  ? 27.112  -34.149 50.708   1.00 240.08 ? 75   TYR G CZ  1 
ATOM   18351 O  OH  . TYR G  3 77  ? 27.035  -32.778 50.594   1.00 239.01 ? 75   TYR G OH  1 
ATOM   18352 N  N   . ALA G  3 78  ? 28.606  -40.777 52.401   1.00 251.06 ? 76   ALA G N   1 
ATOM   18353 C  CA  . ALA G  3 78  ? 28.764  -42.116 52.953   1.00 239.70 ? 76   ALA G CA  1 
ATOM   18354 C  C   . ALA G  3 78  ? 27.467  -42.914 52.863   1.00 231.51 ? 76   ALA G C   1 
ATOM   18355 O  O   . ALA G  3 78  ? 26.366  -42.363 52.777   1.00 234.58 ? 76   ALA G O   1 
ATOM   18356 C  CB  . ALA G  3 78  ? 29.222  -42.048 54.409   1.00 242.62 ? 76   ALA G CB  1 
ATOM   18357 N  N   . LYS G  3 79  ? 27.614  -44.237 52.898   1.00 215.99 ? 77   LYS G N   1 
ATOM   18358 C  CA  . LYS G  3 79  ? 26.490  -45.158 52.817   1.00 208.79 ? 77   LYS G CA  1 
ATOM   18359 C  C   . LYS G  3 79  ? 26.534  -46.100 54.011   1.00 208.29 ? 77   LYS G C   1 
ATOM   18360 O  O   . LYS G  3 79  ? 27.576  -46.700 54.290   1.00 210.17 ? 77   LYS G O   1 
ATOM   18361 C  CB  . LYS G  3 79  ? 26.524  -45.955 51.507   1.00 203.20 ? 77   LYS G CB  1 
ATOM   18362 C  CG  . LYS G  3 79  ? 26.790  -45.106 50.272   1.00 202.39 ? 77   LYS G CG  1 
ATOM   18363 C  CD  . LYS G  3 79  ? 25.673  -44.101 50.027   1.00 214.25 ? 77   LYS G CD  1 
ATOM   18364 C  CE  . LYS G  3 79  ? 25.945  -43.270 48.777   1.00 215.98 ? 77   LYS G CE  1 
ATOM   18365 N  NZ  . LYS G  3 79  ? 24.886  -42.255 48.510   1.00 226.19 ? 77   LYS G NZ  1 
ATOM   18366 N  N   . GLU G  3 80  ? 25.410  -46.225 54.716   1.00 209.18 ? 78   GLU G N   1 
ATOM   18367 C  CA  . GLU G  3 80  ? 25.325  -47.105 55.876   1.00 215.83 ? 78   GLU G CA  1 
ATOM   18368 C  C   . GLU G  3 80  ? 25.045  -48.531 55.416   1.00 229.93 ? 78   GLU G C   1 
ATOM   18369 O  O   . GLU G  3 80  ? 24.012  -48.797 54.790   1.00 233.14 ? 78   GLU G O   1 
ATOM   18370 C  CB  . GLU G  3 80  ? 24.239  -46.627 56.835   1.00 219.82 ? 78   GLU G CB  1 
ATOM   18371 C  CG  . GLU G  3 80  ? 24.073  -47.503 58.063   1.00 223.29 ? 78   GLU G CG  1 
ATOM   18372 C  CD  . GLU G  3 80  ? 23.072  -46.929 59.036   1.00 227.50 ? 78   GLU G CD  1 
ATOM   18373 O  OE1 . GLU G  3 80  ? 22.720  -45.741 58.884   1.00 226.36 ? 78   GLU G OE1 1 
ATOM   18374 O  OE2 . GLU G  3 80  ? 22.633  -47.660 59.947   1.00 225.52 ? 78   GLU G OE2 1 
ATOM   18375 N  N   . VAL G  3 81  ? 25.953  -49.448 55.737   1.00 246.26 ? 79   VAL G N   1 
ATOM   18376 C  CA  . VAL G  3 81  ? 25.899  -50.812 55.221   1.00 247.28 ? 79   VAL G CA  1 
ATOM   18377 C  C   . VAL G  3 81  ? 25.220  -51.712 56.247   1.00 241.03 ? 79   VAL G C   1 
ATOM   18378 O  O   . VAL G  3 81  ? 25.640  -51.779 57.407   1.00 234.95 ? 79   VAL G O   1 
ATOM   18379 C  CB  . VAL G  3 81  ? 27.302  -51.329 54.876   1.00 250.30 ? 79   VAL G CB  1 
ATOM   18380 C  CG1 . VAL G  3 81  ? 27.236  -52.780 54.434   1.00 240.72 ? 79   VAL G CG1 1 
ATOM   18381 C  CG2 . VAL G  3 81  ? 27.932  -50.468 53.793   1.00 247.36 ? 79   VAL G CG2 1 
ATOM   18382 N  N   . THR G  3 82  ? 24.176  -52.416 55.811   1.00 236.45 ? 80   THR G N   1 
ATOM   18383 C  CA  . THR G  3 82  ? 23.474  -53.394 56.628   1.00 237.36 ? 80   THR G CA  1 
ATOM   18384 C  C   . THR G  3 82  ? 23.183  -54.621 55.772   1.00 234.07 ? 80   THR G C   1 
ATOM   18385 O  O   . THR G  3 82  ? 23.117  -54.539 54.544   1.00 242.20 ? 80   THR G O   1 
ATOM   18386 C  CB  . THR G  3 82  ? 22.167  -52.824 57.201   1.00 233.72 ? 80   THR G CB  1 
ATOM   18387 O  OG1 . THR G  3 82  ? 21.395  -52.235 56.145   1.00 218.51 ? 80   THR G OG1 1 
ATOM   18388 C  CG2 . THR G  3 82  ? 22.457  -51.772 58.269   1.00 230.90 ? 80   THR G CG2 1 
ATOM   18389 N  N   . ARG G  3 83  ? 23.007  -55.769 56.427   1.00 228.82 ? 81   ARG G N   1 
ATOM   18390 C  CA  . ARG G  3 83  ? 22.772  -57.022 55.722   1.00 217.46 ? 81   ARG G CA  1 
ATOM   18391 C  C   . ARG G  3 83  ? 21.577  -57.755 56.325   1.00 221.79 ? 81   ARG G C   1 
ATOM   18392 O  O   . ARG G  3 83  ? 21.150  -57.476 57.450   1.00 233.34 ? 81   ARG G O   1 
ATOM   18393 C  CB  . ARG G  3 83  ? 24.015  -57.926 55.751   1.00 211.80 ? 81   ARG G CB  1 
ATOM   18394 C  CG  . ARG G  3 83  ? 24.208  -58.672 57.057   1.00 217.77 ? 81   ARG G CG  1 
ATOM   18395 C  CD  . ARG G  3 83  ? 25.308  -59.723 56.974   1.00 217.99 ? 81   ARG G CD  1 
ATOM   18396 N  NE  . ARG G  3 83  ? 25.329  -60.555 58.176   1.00 245.08 ? 81   ARG G NE  1 
ATOM   18397 C  CZ  . ARG G  3 83  ? 26.150  -61.582 58.372   1.00 242.32 ? 81   ARG G CZ  1 
ATOM   18398 N  NH1 . ARG G  3 83  ? 27.033  -61.918 57.441   1.00 229.96 ? 81   ARG G NH1 1 
ATOM   18399 N  NH2 . ARG G  3 83  ? 26.085  -62.274 59.504   1.00 249.40 ? 81   ARG G NH2 1 
ATOM   18400 N  N   . VAL G  3 84  ? 21.036  -58.704 55.557   1.00 200.45 ? 82   VAL G N   1 
ATOM   18401 C  CA  . VAL G  3 84  ? 19.904  -59.528 55.979   1.00 199.44 ? 82   VAL G CA  1 
ATOM   18402 C  C   . VAL G  3 84  ? 20.106  -60.947 55.463   1.00 201.02 ? 82   VAL G C   1 
ATOM   18403 O  O   . VAL G  3 84  ? 20.331  -61.151 54.266   1.00 200.20 ? 82   VAL G O   1 
ATOM   18404 C  CB  . VAL G  3 84  ? 18.556  -58.968 55.478   1.00 198.34 ? 82   VAL G CB  1 
ATOM   18405 C  CG1 . VAL G  3 84  ? 18.072  -57.847 56.380   1.00 206.96 ? 82   VAL G CG1 1 
ATOM   18406 C  CG2 . VAL G  3 84  ? 18.682  -58.479 54.048   1.00 195.96 ? 82   VAL G CG2 1 
ATOM   18407 N  N   . LEU G  3 85  ? 20.010  -61.928 56.357   1.00 217.54 ? 83   LEU G N   1 
ATOM   18408 C  CA  . LEU G  3 85  ? 20.178  -63.320 55.967   1.00 223.66 ? 83   LEU G CA  1 
ATOM   18409 C  C   . LEU G  3 85  ? 18.905  -63.850 55.302   1.00 230.05 ? 83   LEU G C   1 
ATOM   18410 O  O   . LEU G  3 85  ? 17.861  -63.193 55.280   1.00 230.25 ? 83   LEU G O   1 
ATOM   18411 C  CB  . LEU G  3 85  ? 20.542  -64.175 57.178   1.00 231.20 ? 83   LEU G CB  1 
ATOM   18412 C  CG  . LEU G  3 85  ? 21.849  -63.823 57.891   1.00 235.33 ? 83   LEU G CG  1 
ATOM   18413 C  CD1 . LEU G  3 85  ? 21.982  -64.612 59.184   1.00 251.81 ? 83   LEU G CD1 1 
ATOM   18414 C  CD2 . LEU G  3 85  ? 23.036  -64.083 56.981   1.00 223.79 ? 83   LEU G CD2 1 
ATOM   18415 N  N   . MET G  3 86  ? 19.001  -65.062 54.752   1.00 236.95 ? 84   MET G N   1 
ATOM   18416 C  CA  . MET G  3 86  ? 17.884  -65.668 54.044   1.00 232.10 ? 84   MET G CA  1 
ATOM   18417 C  C   . MET G  3 86  ? 17.087  -66.575 54.980   1.00 229.77 ? 84   MET G C   1 
ATOM   18418 O  O   . MET G  3 86  ? 17.408  -66.738 56.159   1.00 230.55 ? 84   MET G O   1 
ATOM   18419 C  CB  . MET G  3 86  ? 18.370  -66.449 52.822   1.00 228.15 ? 84   MET G CB  1 
ATOM   18420 C  CG  . MET G  3 86  ? 19.077  -67.754 53.146   1.00 237.82 ? 84   MET G CG  1 
ATOM   18421 S  SD  . MET G  3 86  ? 19.275  -68.814 51.700   1.00 234.45 ? 84   MET G SD  1 
ATOM   18422 C  CE  . MET G  3 86  ? 20.020  -70.270 52.437   1.00 256.00 ? 84   MET G CE  1 
ATOM   18423 N  N   . VAL G  3 87  ? 16.026  -67.178 54.440   1.00 250.62 ? 85   VAL G N   1 
ATOM   18424 C  CA  . VAL G  3 87  ? 15.142  -68.058 55.198   1.00 275.76 ? 85   VAL G CA  1 
ATOM   18425 C  C   . VAL G  3 87  ? 15.647  -69.489 55.087   1.00 283.01 ? 85   VAL G C   1 
ATOM   18426 O  O   . VAL G  3 87  ? 16.160  -69.906 54.042   1.00 282.99 ? 85   VAL G O   1 
ATOM   18427 C  CB  . VAL G  3 87  ? 13.690  -67.939 54.697   1.00 283.63 ? 85   VAL G CB  1 
ATOM   18428 C  CG1 . VAL G  3 87  ? 12.749  -68.768 55.566   1.00 295.71 ? 85   VAL G CG1 1 
ATOM   18429 C  CG2 . VAL G  3 87  ? 13.251  -66.488 54.680   1.00 279.59 ? 85   VAL G CG2 1 
ATOM   18430 N  N   . GLU G  3 88  ? 15.491  -70.252 56.167   1.00 287.47 ? 86   GLU G N   1 
ATOM   18431 C  CA  . GLU G  3 88  ? 15.906  -71.646 56.185   1.00 283.28 ? 86   GLU G CA  1 
ATOM   18432 C  C   . GLU G  3 88  ? 15.034  -72.468 55.236   1.00 291.99 ? 86   GLU G C   1 
ATOM   18433 O  O   . GLU G  3 88  ? 14.117  -71.961 54.585   1.00 299.26 ? 86   GLU G O   1 
ATOM   18434 C  CB  . GLU G  3 88  ? 15.822  -72.197 57.605   1.00 280.67 ? 86   GLU G CB  1 
ATOM   18435 C  CG  . GLU G  3 88  ? 16.320  -71.228 58.658   1.00 277.31 ? 86   GLU G CG  1 
ATOM   18436 C  CD  . GLU G  3 88  ? 15.880  -71.604 60.055   1.00 291.29 ? 86   GLU G CD  1 
ATOM   18437 O  OE1 . GLU G  3 88  ? 15.185  -72.630 60.203   1.00 298.06 ? 86   GLU G OE1 1 
ATOM   18438 O  OE2 . GLU G  3 88  ? 16.226  -70.871 61.004   1.00 296.52 ? 86   GLU G OE2 1 
ATOM   18439 N  N   . THR G  3 89  ? 15.321  -73.768 55.164   1.00 287.54 ? 87   THR G N   1 
ATOM   18440 C  CA  . THR G  3 89  ? 14.477  -74.670 54.387   1.00 285.00 ? 87   THR G CA  1 
ATOM   18441 C  C   . THR G  3 89  ? 13.125  -74.912 55.044   1.00 279.99 ? 87   THR G C   1 
ATOM   18442 O  O   . THR G  3 89  ? 12.301  -75.647 54.487   1.00 273.60 ? 87   THR G O   1 
ATOM   18443 C  CB  . THR G  3 89  ? 15.191  -76.001 54.162   1.00 281.58 ? 87   THR G CB  1 
ATOM   18444 O  OG1 . THR G  3 89  ? 15.672  -76.505 55.415   1.00 278.42 ? 87   THR G OG1 1 
ATOM   18445 C  CG2 . THR G  3 89  ? 16.358  -75.813 53.201   1.00 263.37 ? 87   THR G CG2 1 
ATOM   18446 N  N   . HIS G  3 90  ? 12.886  -74.320 56.206   1.00 274.65 ? 88   HIS G N   1 
ATOM   18447 C  CA  . HIS G  3 90  ? 11.591  -74.365 56.865   1.00 280.72 ? 88   HIS G CA  1 
ATOM   18448 C  C   . HIS G  3 90  ? 10.775  -73.156 56.405   1.00 274.55 ? 88   HIS G C   1 
ATOM   18449 O  O   . HIS G  3 90  ? 11.046  -72.587 55.347   1.00 270.23 ? 88   HIS G O   1 
ATOM   18450 C  CB  . HIS G  3 90  ? 11.782  -74.410 58.383   1.00 298.03 ? 88   HIS G CB  1 
ATOM   18451 C  CG  . HIS G  3 90  ? 12.771  -75.438 58.834   1.00 305.74 ? 88   HIS G CG  1 
ATOM   18452 N  ND1 . HIS G  3 90  ? 14.120  -75.339 58.570   1.00 294.39 ? 88   HIS G ND1 1 
ATOM   18453 C  CD2 . HIS G  3 90  ? 12.606  -76.588 59.528   1.00 317.01 ? 88   HIS G CD2 1 
ATOM   18454 C  CE1 . HIS G  3 90  ? 14.745  -76.383 59.083   1.00 305.94 ? 88   HIS G CE1 1 
ATOM   18455 N  NE2 . HIS G  3 90  ? 13.849  -77.156 59.670   1.00 317.15 ? 88   HIS G NE2 1 
ATOM   18456 N  N   . ASN G  3 91  ? 9.771   -72.757 57.187   1.00 282.09 ? 89   ASN G N   1 
ATOM   18457 C  CA  . ASN G  3 91  ? 9.002   -71.531 56.941   1.00 278.69 ? 89   ASN G CA  1 
ATOM   18458 C  C   . ASN G  3 91  ? 8.433   -71.468 55.522   1.00 277.52 ? 89   ASN G C   1 
ATOM   18459 O  O   . ASN G  3 91  ? 8.530   -70.441 54.847   1.00 277.99 ? 89   ASN G O   1 
ATOM   18460 C  CB  . ASN G  3 91  ? 9.844   -70.289 57.238   1.00 262.88 ? 89   ASN G CB  1 
ATOM   18461 C  CG  . ASN G  3 91  ? 10.087  -70.095 58.720   1.00 289.14 ? 89   ASN G CG  1 
ATOM   18462 O  OD1 . ASN G  3 91  ? 9.305   -70.549 59.555   1.00 317.49 ? 89   ASN G OD1 1 
ATOM   18463 N  ND2 . ASN G  3 91  ? 11.173  -69.411 59.056   1.00 274.56 ? 89   ASN G ND2 1 
ATOM   18464 N  N   . GLU G  3 92  ? 7.843   -72.575 55.065   1.00 276.33 ? 90   GLU G N   1 
ATOM   18465 C  CA  . GLU G  3 92  ? 7.069   -72.675 53.825   1.00 276.39 ? 90   GLU G CA  1 
ATOM   18466 C  C   . GLU G  3 92  ? 7.905   -72.525 52.553   1.00 265.05 ? 90   GLU G C   1 
ATOM   18467 O  O   . GLU G  3 92  ? 7.345   -72.276 51.474   1.00 251.93 ? 90   GLU G O   1 
ATOM   18468 C  CB  . GLU G  3 92  ? 5.925   -71.654 53.801   1.00 273.60 ? 90   GLU G CB  1 
ATOM   18469 C  CG  . GLU G  3 92  ? 4.959   -71.782 54.972   1.00 259.43 ? 90   GLU G CG  1 
ATOM   18470 C  CD  . GLU G  3 92  ? 3.964   -70.641 55.029   1.00 253.64 ? 90   GLU G CD  1 
ATOM   18471 O  OE1 . GLU G  3 92  ? 4.171   -69.637 54.316   1.00 264.78 ? 90   GLU G OE1 1 
ATOM   18472 O  OE2 . GLU G  3 92  ? 2.976   -70.749 55.784   1.00 248.54 ? 90   GLU G OE2 1 
ATOM   18473 N  N   . ILE G  3 93  ? 9.231   -72.679 52.633   1.00 258.48 ? 91   ILE G N   1 
ATOM   18474 C  CA  . ILE G  3 93  ? 10.074  -72.635 51.439   1.00 247.07 ? 91   ILE G CA  1 
ATOM   18475 C  C   . ILE G  3 93  ? 10.067  -73.956 50.687   1.00 252.13 ? 91   ILE G C   1 
ATOM   18476 O  O   . ILE G  3 93  ? 10.675  -74.060 49.612   1.00 249.97 ? 91   ILE G O   1 
ATOM   18477 C  CB  . ILE G  3 93  ? 11.501  -72.224 51.858   1.00 245.45 ? 91   ILE G CB  1 
ATOM   18478 C  CG1 . ILE G  3 93  ? 11.448  -71.025 52.802   1.00 244.71 ? 91   ILE G CG1 1 
ATOM   18479 C  CG2 . ILE G  3 93  ? 12.350  -71.852 50.659   1.00 242.20 ? 91   ILE G CG2 1 
ATOM   18480 C  CD1 . ILE G  3 93  ? 10.676  -69.845 52.255   1.00 240.13 ? 91   ILE G CD1 1 
ATOM   18481 N  N   . TYR G  3 94  ? 9.362   -74.962 51.204   1.00 259.58 ? 92   TYR G N   1 
ATOM   18482 C  CA  . TYR G  3 94  ? 9.463   -76.333 50.729   1.00 255.90 ? 92   TYR G CA  1 
ATOM   18483 C  C   . TYR G  3 94  ? 8.231   -76.833 49.991   1.00 258.10 ? 92   TYR G C   1 
ATOM   18484 O  O   . TYR G  3 94  ? 8.356   -77.719 49.141   1.00 256.74 ? 92   TYR G O   1 
ATOM   18485 C  CB  . TYR G  3 94  ? 9.747   -77.272 51.910   1.00 252.02 ? 92   TYR G CB  1 
ATOM   18486 C  CG  . TYR G  3 94  ? 8.810   -77.065 53.086   1.00 253.32 ? 92   TYR G CG  1 
ATOM   18487 C  CD1 . TYR G  3 94  ? 9.088   -76.121 54.068   1.00 246.69 ? 92   TYR G CD1 1 
ATOM   18488 C  CD2 . TYR G  3 94  ? 7.646   -77.816 53.212   1.00 267.31 ? 92   TYR G CD2 1 
ATOM   18489 C  CE1 . TYR G  3 94  ? 8.231   -75.930 55.140   1.00 258.40 ? 92   TYR G CE1 1 
ATOM   18490 C  CE2 . TYR G  3 94  ? 6.786   -77.634 54.279   1.00 268.86 ? 92   TYR G CE2 1 
ATOM   18491 C  CZ  . TYR G  3 94  ? 7.082   -76.692 55.239   1.00 264.62 ? 92   TYR G CZ  1 
ATOM   18492 O  OH  . TYR G  3 94  ? 6.222   -76.515 56.298   1.00 259.91 ? 92   TYR G OH  1 
ATOM   18493 N  N   . ASP G  3 95  ? 7.045   -76.296 50.290   1.00 262.75 ? 93   ASP G N   1 
ATOM   18494 C  CA  . ASP G  3 95  ? 5.829   -76.766 49.639   1.00 263.11 ? 93   ASP G CA  1 
ATOM   18495 C  C   . ASP G  3 95  ? 5.730   -76.332 48.185   1.00 257.88 ? 93   ASP G C   1 
ATOM   18496 O  O   . ASP G  3 95  ? 4.782   -76.734 47.498   1.00 262.09 ? 93   ASP G O   1 
ATOM   18497 C  CB  . ASP G  3 95  ? 4.602   -76.273 50.416   1.00 263.88 ? 93   ASP G CB  1 
ATOM   18498 C  CG  . ASP G  3 95  ? 3.348   -77.068 50.091   1.00 271.41 ? 93   ASP G CG  1 
ATOM   18499 O  OD1 . ASP G  3 95  ? 3.469   -78.163 49.501   1.00 273.76 ? 93   ASP G OD1 1 
ATOM   18500 O  OD2 . ASP G  3 95  ? 2.241   -76.604 50.439   1.00 279.91 ? 93   ASP G OD2 1 
ATOM   18501 N  N   . LYS G  3 96  ? 6.678   -75.539 47.695   1.00 243.60 ? 94   LYS G N   1 
ATOM   18502 C  CA  . LYS G  3 96  ? 6.663   -75.063 46.321   1.00 245.77 ? 94   LYS G CA  1 
ATOM   18503 C  C   . LYS G  3 96  ? 7.788   -75.622 45.466   1.00 257.32 ? 94   LYS G C   1 
ATOM   18504 O  O   . LYS G  3 96  ? 7.582   -75.844 44.271   1.00 259.46 ? 94   LYS G O   1 
ATOM   18505 C  CB  . LYS G  3 96  ? 6.739   -73.530 46.292   1.00 241.55 ? 94   LYS G CB  1 
ATOM   18506 C  CG  . LYS G  3 96  ? 5.599   -72.827 47.004   1.00 241.00 ? 94   LYS G CG  1 
ATOM   18507 C  CD  . LYS G  3 96  ? 4.320   -72.906 46.200   1.00 244.30 ? 94   LYS G CD  1 
ATOM   18508 C  CE  . LYS G  3 96  ? 3.327   -71.864 46.677   1.00 243.90 ? 94   LYS G CE  1 
ATOM   18509 N  NZ  . LYS G  3 96  ? 3.006   -72.019 48.124   1.00 249.37 ? 94   LYS G NZ  1 
ATOM   18510 N  N   . PHE G  3 97  ? 8.962   -75.862 46.042   1.00 260.10 ? 95   PHE G N   1 
ATOM   18511 C  CA  . PHE G  3 97  ? 10.127  -76.223 45.243   1.00 256.49 ? 95   PHE G CA  1 
ATOM   18512 C  C   . PHE G  3 97  ? 10.738  -77.532 45.715   1.00 262.37 ? 95   PHE G C   1 
ATOM   18513 O  O   . PHE G  3 97  ? 10.162  -78.593 45.488   1.00 280.74 ? 95   PHE G O   1 
ATOM   18514 C  CB  . PHE G  3 97  ? 11.157  -75.101 45.299   1.00 249.10 ? 95   PHE G CB  1 
ATOM   18515 C  CG  . PHE G  3 97  ? 10.555  -73.735 45.215   1.00 255.68 ? 95   PHE G CG  1 
ATOM   18516 C  CD1 . PHE G  3 97  ? 10.250  -73.181 43.985   1.00 248.83 ? 95   PHE G CD1 1 
ATOM   18517 C  CD2 . PHE G  3 97  ? 10.261  -73.021 46.364   1.00 261.53 ? 95   PHE G CD2 1 
ATOM   18518 C  CE1 . PHE G  3 97  ? 9.679   -71.937 43.898   1.00 244.92 ? 95   PHE G CE1 1 
ATOM   18519 C  CE2 . PHE G  3 97  ? 9.685   -71.772 46.280   1.00 256.40 ? 95   PHE G CE2 1 
ATOM   18520 C  CZ  . PHE G  3 97  ? 9.395   -71.229 45.042   1.00 245.83 ? 95   PHE G CZ  1 
ATOM   18521 N  N   . LYS G  3 98  ? 11.920  -77.442 46.330   1.00 257.71 ? 96   LYS G N   1 
ATOM   18522 C  CA  . LYS G  3 98  ? 12.559  -78.511 47.095   1.00 266.10 ? 96   LYS G CA  1 
ATOM   18523 C  C   . LYS G  3 98  ? 13.340  -79.513 46.245   1.00 280.76 ? 96   LYS G C   1 
ATOM   18524 O  O   . LYS G  3 98  ? 14.463  -79.871 46.613   1.00 284.19 ? 96   LYS G O   1 
ATOM   18525 C  CB  . LYS G  3 98  ? 11.520  -79.238 47.959   1.00 273.98 ? 96   LYS G CB  1 
ATOM   18526 C  CG  . LYS G  3 98  ? 12.015  -80.519 48.623   1.00 267.41 ? 96   LYS G CG  1 
ATOM   18527 C  CD  . LYS G  3 98  ? 10.867  -81.252 49.309   1.00 265.42 ? 96   LYS G CD  1 
ATOM   18528 C  CE  . LYS G  3 98  ? 11.287  -82.634 49.803   1.00 276.69 ? 96   LYS G CE  1 
ATOM   18529 N  NZ  . LYS G  3 98  ? 10.169  -83.403 50.432   1.00 289.89 ? 96   LYS G NZ  1 
ATOM   18530 N  N   . GLN G  3 99  ? 12.796  -79.962 45.105   1.00 295.89 ? 97   GLN G N   1 
ATOM   18531 C  CA  . GLN G  3 99  ? 13.332  -81.151 44.440   1.00 303.42 ? 97   GLN G CA  1 
ATOM   18532 C  C   . GLN G  3 99  ? 14.061  -80.902 43.123   1.00 293.80 ? 97   GLN G C   1 
ATOM   18533 O  O   . GLN G  3 99  ? 14.729  -81.822 42.634   1.00 291.28 ? 97   GLN G O   1 
ATOM   18534 C  CB  . GLN G  3 99  ? 12.215  -82.171 44.167   1.00 310.87 ? 97   GLN G CB  1 
ATOM   18535 C  CG  . GLN G  3 99  ? 11.125  -82.233 45.218   1.00 313.24 ? 97   GLN G CG  1 
ATOM   18536 C  CD  . GLN G  3 99  ? 9.887   -81.464 44.805   1.00 306.47 ? 97   GLN G CD  1 
ATOM   18537 O  OE1 . GLN G  3 99  ? 9.874   -80.798 43.767   1.00 310.26 ? 97   GLN G OE1 1 
ATOM   18538 N  NE2 . GLN G  3 99  ? 8.838   -81.551 45.614   1.00 301.59 ? 97   GLN G NE2 1 
ATOM   18539 N  N   . SER G  3 100 ? 13.936  -79.724 42.512   1.00 283.95 ? 98   SER G N   1 
ATOM   18540 C  CA  . SER G  3 100 ? 14.669  -79.503 41.270   1.00 278.42 ? 98   SER G CA  1 
ATOM   18541 C  C   . SER G  3 100 ? 16.161  -79.543 41.569   1.00 275.06 ? 98   SER G C   1 
ATOM   18542 O  O   . SER G  3 100 ? 16.754  -78.533 41.964   1.00 266.84 ? 98   SER G O   1 
ATOM   18543 C  CB  . SER G  3 100 ? 14.264  -78.184 40.610   1.00 269.38 ? 98   SER G CB  1 
ATOM   18544 O  OG  . SER G  3 100 ? 14.492  -77.092 41.474   1.00 269.08 ? 98   SER G OG  1 
ATOM   18545 N  N   . THR G  3 101 ? 16.769  -80.721 41.397   1.00 280.66 ? 99   THR G N   1 
ATOM   18546 C  CA  . THR G  3 101 ? 18.143  -80.949 41.829   1.00 274.09 ? 99   THR G CA  1 
ATOM   18547 C  C   . THR G  3 101 ? 19.151  -80.071 41.104   1.00 268.20 ? 99   THR G C   1 
ATOM   18548 O  O   . THR G  3 101 ? 20.296  -79.985 41.556   1.00 260.96 ? 99   THR G O   1 
ATOM   18549 C  CB  . THR G  3 101 ? 18.529  -82.417 41.630   1.00 275.11 ? 99   THR G CB  1 
ATOM   18550 O  OG1 . THR G  3 101 ? 18.532  -82.726 40.231   1.00 274.40 ? 99   THR G OG1 1 
ATOM   18551 C  CG2 . THR G  3 101 ? 17.548  -83.330 42.343   1.00 277.96 ? 99   THR G CG2 1 
ATOM   18552 N  N   . HIS G  3 102 ? 18.763  -79.428 40.000   1.00 271.82 ? 100  HIS G N   1 
ATOM   18553 C  CA  . HIS G  3 102 ? 19.652  -78.575 39.219   1.00 270.75 ? 100  HIS G CA  1 
ATOM   18554 C  C   . HIS G  3 102 ? 19.418  -77.090 39.479   1.00 268.41 ? 100  HIS G C   1 
ATOM   18555 O  O   . HIS G  3 102 ? 19.676  -76.262 38.598   1.00 255.55 ? 100  HIS G O   1 
ATOM   18556 C  CB  . HIS G  3 102 ? 19.495  -78.867 37.727   1.00 267.29 ? 100  HIS G CB  1 
ATOM   18557 C  CG  . HIS G  3 102 ? 19.852  -80.267 37.341   1.00 275.33 ? 100  HIS G CG  1 
ATOM   18558 N  ND1 . HIS G  3 102 ? 21.119  -80.625 36.931   1.00 274.29 ? 100  HIS G ND1 1 
ATOM   18559 C  CD2 . HIS G  3 102 ? 19.108  -81.397 37.297   1.00 285.31 ? 100  HIS G CD2 1 
ATOM   18560 C  CE1 . HIS G  3 102 ? 21.140  -81.917 36.653   1.00 285.93 ? 100  HIS G CE1 1 
ATOM   18561 N  NE2 . HIS G  3 102 ? 19.933  -82.409 36.866   1.00 291.04 ? 100  HIS G NE2 1 
ATOM   18562 N  N   . SER G  3 103 ? 18.934  -76.732 40.667   1.00 277.62 ? 101  SER G N   1 
ATOM   18563 C  CA  . SER G  3 103 ? 18.638  -75.335 40.962   1.00 261.66 ? 101  SER G CA  1 
ATOM   18564 C  C   . SER G  3 103 ? 18.637  -75.116 42.469   1.00 260.71 ? 101  SER G C   1 
ATOM   18565 O  O   . SER G  3 103 ? 18.568  -76.064 43.256   1.00 260.36 ? 101  SER G O   1 
ATOM   18566 C  CB  . SER G  3 103 ? 17.296  -74.910 40.354   1.00 252.96 ? 101  SER G CB  1 
ATOM   18567 O  OG  . SER G  3 103 ? 17.286  -75.101 38.950   1.00 247.59 ? 101  SER G OG  1 
ATOM   18568 N  N   . ILE G  3 104 ? 18.718  -73.844 42.855   1.00 257.99 ? 102  ILE G N   1 
ATOM   18569 C  CA  . ILE G  3 104 ? 18.670  -73.420 44.252   1.00 258.54 ? 102  ILE G CA  1 
ATOM   18570 C  C   . ILE G  3 104 ? 17.743  -72.216 44.351   1.00 257.45 ? 102  ILE G C   1 
ATOM   18571 O  O   . ILE G  3 104 ? 17.857  -71.274 43.560   1.00 246.85 ? 102  ILE G O   1 
ATOM   18572 C  CB  . ILE G  3 104 ? 20.070  -73.074 44.798   1.00 248.74 ? 102  ILE G CB  1 
ATOM   18573 C  CG1 . ILE G  3 104 ? 20.798  -74.339 45.254   1.00 256.92 ? 102  ILE G CG1 1 
ATOM   18574 C  CG2 . ILE G  3 104 ? 19.977  -72.076 45.938   1.00 246.71 ? 102  ILE G CG2 1 
ATOM   18575 C  CD1 . ILE G  3 104 ? 22.106  -74.075 45.974   1.00 254.74 ? 102  ILE G CD1 1 
ATOM   18576 N  N   . TYR G  3 105 ? 16.825  -72.242 45.315   1.00 272.30 ? 103  TYR G N   1 
ATOM   18577 C  CA  . TYR G  3 105 ? 15.865  -71.163 45.508   1.00 265.88 ? 103  TYR G CA  1 
ATOM   18578 C  C   . TYR G  3 105 ? 16.129  -70.461 46.832   1.00 262.12 ? 103  TYR G C   1 
ATOM   18579 O  O   . TYR G  3 105 ? 16.392  -71.111 47.848   1.00 269.82 ? 103  TYR G O   1 
ATOM   18580 C  CB  . TYR G  3 105 ? 14.427  -71.686 45.473   1.00 272.62 ? 103  TYR G CB  1 
ATOM   18581 C  CG  . TYR G  3 105 ? 14.150  -72.577 44.290   1.00 281.46 ? 103  TYR G CG  1 
ATOM   18582 C  CD1 . TYR G  3 105 ? 13.746  -72.046 43.072   1.00 275.14 ? 103  TYR G CD1 1 
ATOM   18583 C  CD2 . TYR G  3 105 ? 14.307  -73.952 44.387   1.00 291.68 ? 103  TYR G CD2 1 
ATOM   18584 C  CE1 . TYR G  3 105 ? 13.499  -72.864 41.983   1.00 278.61 ? 103  TYR G CE1 1 
ATOM   18585 C  CE2 . TYR G  3 105 ? 14.063  -74.775 43.311   1.00 292.56 ? 103  TYR G CE2 1 
ATOM   18586 C  CZ  . TYR G  3 105 ? 13.659  -74.229 42.110   1.00 288.11 ? 103  TYR G CZ  1 
ATOM   18587 O  OH  . TYR G  3 105 ? 13.417  -75.057 41.036   1.00 293.98 ? 103  TYR G OH  1 
ATOM   18588 N  N   . MET G  3 106 ? 16.054  -69.132 46.816   1.00 263.65 ? 104  MET G N   1 
ATOM   18589 C  CA  . MET G  3 106 ? 16.341  -68.313 47.983   1.00 266.84 ? 104  MET G CA  1 
ATOM   18590 C  C   . MET G  3 106 ? 15.194  -67.341 48.207   1.00 262.78 ? 104  MET G C   1 
ATOM   18591 O  O   . MET G  3 106 ? 14.671  -66.761 47.252   1.00 266.85 ? 104  MET G O   1 
ATOM   18592 C  CB  . MET G  3 106 ? 17.658  -67.550 47.806   1.00 271.19 ? 104  MET G CB  1 
ATOM   18593 C  CG  . MET G  3 106 ? 18.845  -68.441 47.472   1.00 271.87 ? 104  MET G CG  1 
ATOM   18594 S  SD  . MET G  3 106 ? 20.286  -67.514 46.914   1.00 273.33 ? 104  MET G SD  1 
ATOM   18595 C  CE  . MET G  3 106 ? 19.661  -66.774 45.407   1.00 252.34 ? 104  MET G CE  1 
ATOM   18596 N  N   . PHE G  3 107 ? 14.805  -67.158 49.467   1.00 260.32 ? 105  PHE G N   1 
ATOM   18597 C  CA  . PHE G  3 107 ? 13.650  -66.335 49.795   1.00 271.91 ? 105  PHE G CA  1 
ATOM   18598 C  C   . PHE G  3 107 ? 13.966  -65.398 50.956   1.00 279.67 ? 105  PHE G C   1 
ATOM   18599 O  O   . PHE G  3 107 ? 14.788  -65.709 51.824   1.00 272.30 ? 105  PHE G O   1 
ATOM   18600 C  CB  . PHE G  3 107 ? 12.431  -67.214 50.125   1.00 281.92 ? 105  PHE G CB  1 
ATOM   18601 C  CG  . PHE G  3 107 ? 11.672  -67.678 48.908   1.00 274.10 ? 105  PHE G CG  1 
ATOM   18602 C  CD1 . PHE G  3 107 ? 12.178  -68.677 48.089   1.00 259.75 ? 105  PHE G CD1 1 
ATOM   18603 C  CD2 . PHE G  3 107 ? 10.448  -67.113 48.588   1.00 276.19 ? 105  PHE G CD2 1 
ATOM   18604 C  CE1 . PHE G  3 107 ? 11.481  -69.093 46.974   1.00 256.40 ? 105  PHE G CE1 1 
ATOM   18605 C  CE2 . PHE G  3 107 ? 9.746   -67.529 47.476   1.00 272.85 ? 105  PHE G CE2 1 
ATOM   18606 C  CZ  . PHE G  3 107 ? 10.263  -68.516 46.669   1.00 266.62 ? 105  PHE G CZ  1 
ATOM   18607 N  N   . PHE G  3 108 ? 13.299  -64.239 50.956   1.00 289.60 ? 106  PHE G N   1 
ATOM   18608 C  CA  . PHE G  3 108 ? 13.491  -63.209 51.972   1.00 283.59 ? 106  PHE G CA  1 
ATOM   18609 C  C   . PHE G  3 108 ? 12.136  -62.659 52.413   1.00 271.22 ? 106  PHE G C   1 
ATOM   18610 O  O   . PHE G  3 108 ? 11.113  -62.861 51.753   1.00 276.56 ? 106  PHE G O   1 
ATOM   18611 C  CB  . PHE G  3 108 ? 14.376  -62.064 51.456   1.00 273.17 ? 106  PHE G CB  1 
ATOM   18612 C  CG  . PHE G  3 108 ? 15.761  -62.493 51.046   1.00 265.62 ? 106  PHE G CG  1 
ATOM   18613 C  CD1 . PHE G  3 108 ? 16.791  -62.529 51.973   1.00 276.75 ? 106  PHE G CD1 1 
ATOM   18614 C  CD2 . PHE G  3 108 ? 16.035  -62.844 49.732   1.00 249.37 ? 106  PHE G CD2 1 
ATOM   18615 C  CE1 . PHE G  3 108 ? 18.065  -62.916 51.602   1.00 274.28 ? 106  PHE G CE1 1 
ATOM   18616 C  CE2 . PHE G  3 108 ? 17.308  -63.232 49.354   1.00 247.42 ? 106  PHE G CE2 1 
ATOM   18617 C  CZ  . PHE G  3 108 ? 18.325  -63.268 50.291   1.00 259.64 ? 106  PHE G CZ  1 
ATOM   18618 N  N   . GLN G  3 109 ? 12.140  -61.948 53.540   1.00 234.81 ? 107  GLN G N   1 
ATOM   18619 C  CA  . GLN G  3 109 ? 10.941  -61.323 54.087   1.00 219.90 ? 107  GLN G CA  1 
ATOM   18620 C  C   . GLN G  3 109 ? 11.015  -59.814 53.907   1.00 223.21 ? 107  GLN G C   1 
ATOM   18621 O  O   . GLN G  3 109 ? 12.019  -59.191 54.270   1.00 231.66 ? 107  GLN G O   1 
ATOM   18622 C  CB  . GLN G  3 109 ? 10.769  -61.659 55.569   1.00 218.26 ? 107  GLN G CB  1 
ATOM   18623 C  CG  . GLN G  3 109 ? 10.467  -63.116 55.841   1.00 221.64 ? 107  GLN G CG  1 
ATOM   18624 C  CD  . GLN G  3 109 ? 10.353  -63.417 57.321   1.00 224.79 ? 107  GLN G CD  1 
ATOM   18625 O  OE1 . GLN G  3 109 ? 10.623  -62.563 58.167   1.00 228.37 ? 107  GLN G OE1 1 
ATOM   18626 N  NE2 . GLN G  3 109 ? 9.951   -64.639 57.643   1.00 227.22 ? 107  GLN G NE2 1 
ATOM   18627 N  N   . THR G  3 110 ? 9.947   -59.228 53.364   1.00 225.83 ? 108  THR G N   1 
ATOM   18628 C  CA  . THR G  3 110 ? 9.918   -57.786 53.148   1.00 224.02 ? 108  THR G CA  1 
ATOM   18629 C  C   . THR G  3 110 ? 9.720   -57.013 54.441   1.00 223.14 ? 108  THR G C   1 
ATOM   18630 O  O   . THR G  3 110 ? 10.067  -55.828 54.501   1.00 219.11 ? 108  THR G O   1 
ATOM   18631 C  CB  . THR G  3 110 ? 8.808   -57.413 52.162   1.00 226.69 ? 108  THR G CB  1 
ATOM   18632 O  OG1 . THR G  3 110 ? 8.783   -58.362 51.089   1.00 231.70 ? 108  THR G OG1 1 
ATOM   18633 C  CG2 . THR G  3 110 ? 9.033   -56.012 51.587   1.00 215.38 ? 108  THR G CG2 1 
ATOM   18634 N  N   . SER G  3 111 ? 9.174   -57.659 55.473   1.00 220.16 ? 109  SER G N   1 
ATOM   18635 C  CA  . SER G  3 111 ? 8.957   -56.981 56.743   1.00 219.84 ? 109  SER G CA  1 
ATOM   18636 C  C   . SER G  3 111 ? 10.267  -56.556 57.397   1.00 214.08 ? 109  SER G C   1 
ATOM   18637 O  O   . SER G  3 111 ? 10.264  -55.645 58.233   1.00 208.53 ? 109  SER G O   1 
ATOM   18638 C  CB  . SER G  3 111 ? 8.151   -57.887 57.676   1.00 219.71 ? 109  SER G CB  1 
ATOM   18639 O  OG  . SER G  3 111 ? 6.940   -58.302 57.060   1.00 209.29 ? 109  SER G OG  1 
ATOM   18640 N  N   . GLU G  3 112 ? 11.387  -57.181 57.025   1.00 212.98 ? 110  GLU G N   1 
ATOM   18641 C  CA  . GLU G  3 112 ? 12.700  -56.800 57.529   1.00 207.25 ? 110  GLU G CA  1 
ATOM   18642 C  C   . GLU G  3 112 ? 13.503  -55.974 56.534   1.00 198.57 ? 110  GLU G C   1 
ATOM   18643 O  O   . GLU G  3 112 ? 14.462  -55.304 56.937   1.00 197.28 ? 110  GLU G O   1 
ATOM   18644 C  CB  . GLU G  3 112 ? 13.505  -58.051 57.905   1.00 204.51 ? 110  GLU G CB  1 
ATOM   18645 C  CG  . GLU G  3 112 ? 12.759  -59.011 58.817   1.00 226.50 ? 110  GLU G CG  1 
ATOM   18646 C  CD  . GLU G  3 112 ? 13.573  -60.238 59.178   1.00 224.28 ? 110  GLU G CD  1 
ATOM   18647 O  OE1 . GLU G  3 112 ? 14.761  -60.300 58.792   1.00 204.65 ? 110  GLU G OE1 1 
ATOM   18648 O  OE2 . GLU G  3 112 ? 13.023  -61.140 59.849   1.00 224.47 ? 110  GLU G OE2 1 
ATOM   18649 N  N   . LEU G  3 113 ? 13.139  -56.012 55.253   1.00 203.72 ? 111  LEU G N   1 
ATOM   18650 C  CA  . LEU G  3 113 ? 13.849  -55.217 54.260   1.00 203.01 ? 111  LEU G CA  1 
ATOM   18651 C  C   . LEU G  3 113 ? 13.505  -53.742 54.397   1.00 200.08 ? 111  LEU G C   1 
ATOM   18652 O  O   . LEU G  3 113 ? 14.398  -52.890 54.450   1.00 198.90 ? 111  LEU G O   1 
ATOM   18653 C  CB  . LEU G  3 113 ? 13.519  -55.719 52.857   1.00 206.66 ? 111  LEU G CB  1 
ATOM   18654 C  CG  . LEU G  3 113 ? 14.235  -57.008 52.455   1.00 201.87 ? 111  LEU G CG  1 
ATOM   18655 C  CD1 . LEU G  3 113 ? 13.795  -57.447 51.072   1.00 201.22 ? 111  LEU G CD1 1 
ATOM   18656 C  CD2 . LEU G  3 113 ? 15.740  -56.809 52.508   1.00 198.17 ? 111  LEU G CD2 1 
ATOM   18657 N  N   . ARG G  3 114 ? 12.213  -53.420 54.467   1.00 212.31 ? 112  ARG G N   1 
ATOM   18658 C  CA  . ARG G  3 114 ? 11.769  -52.042 54.607   1.00 226.26 ? 112  ARG G CA  1 
ATOM   18659 C  C   . ARG G  3 114 ? 11.982  -51.488 56.015   1.00 254.92 ? 112  ARG G C   1 
ATOM   18660 O  O   . ARG G  3 114 ? 11.415  -50.441 56.353   1.00 275.32 ? 112  ARG G O   1 
ATOM   18661 C  CB  . ARG G  3 114 ? 10.298  -51.921 54.196   1.00 221.45 ? 112  ARG G CB  1 
ATOM   18662 C  CG  . ARG G  3 114 ? 10.069  -52.166 52.714   1.00 214.19 ? 112  ARG G CG  1 
ATOM   18663 C  CD  . ARG G  3 114 ? 8.652   -51.832 52.297   1.00 217.29 ? 112  ARG G CD  1 
ATOM   18664 N  NE  . ARG G  3 114 ? 7.692   -52.815 52.784   1.00 233.49 ? 112  ARG G NE  1 
ATOM   18665 C  CZ  . ARG G  3 114 ? 6.378   -52.721 52.612   1.00 258.80 ? 112  ARG G CZ  1 
ATOM   18666 N  NH1 . ARG G  3 114 ? 5.863   -51.685 51.964   1.00 255.69 ? 112  ARG G NH1 1 
ATOM   18667 N  NH2 . ARG G  3 114 ? 5.576   -53.663 53.092   1.00 273.22 ? 112  ARG G NH2 1 
ATOM   18668 N  N   . GLU G  3 115 ? 12.782  -52.163 56.838   1.00 256.59 ? 113  GLU G N   1 
ATOM   18669 C  CA  . GLU G  3 115 ? 13.177  -51.640 58.137   1.00 244.96 ? 113  GLU G CA  1 
ATOM   18670 C  C   . GLU G  3 115 ? 14.623  -51.167 58.160   1.00 251.85 ? 113  GLU G C   1 
ATOM   18671 O  O   . GLU G  3 115 ? 14.937  -50.203 58.868   1.00 260.32 ? 113  GLU G O   1 
ATOM   18672 C  CB  . GLU G  3 115 ? 12.969  -52.704 59.223   1.00 222.93 ? 113  GLU G CB  1 
ATOM   18673 C  CG  . GLU G  3 115 ? 12.981  -52.159 60.639   1.00 228.59 ? 113  GLU G CG  1 
ATOM   18674 C  CD  . GLU G  3 115 ? 12.812  -53.253 61.672   1.00 256.90 ? 113  GLU G CD  1 
ATOM   18675 O  OE1 . GLU G  3 115 ? 12.802  -54.437 61.273   1.00 251.56 ? 113  GLU G OE1 1 
ATOM   18676 O  OE2 . GLU G  3 115 ? 12.690  -52.937 62.877   1.00 288.75 ? 113  GLU G OE2 1 
ATOM   18677 N  N   . ALA G  3 116 ? 15.501  -51.816 57.392   1.00 239.12 ? 114  ALA G N   1 
ATOM   18678 C  CA  . ALA G  3 116 ? 16.867  -51.330 57.244   1.00 237.19 ? 114  ALA G CA  1 
ATOM   18679 C  C   . ALA G  3 116 ? 16.928  -50.130 56.307   1.00 235.99 ? 114  ALA G C   1 
ATOM   18680 O  O   . ALA G  3 116 ? 17.691  -49.188 56.548   1.00 237.34 ? 114  ALA G O   1 
ATOM   18681 C  CB  . ALA G  3 116 ? 17.771  -52.452 56.732   1.00 226.12 ? 114  ALA G CB  1 
ATOM   18682 N  N   . VAL G  3 117 ? 16.132  -50.146 55.243   1.00 243.09 ? 115  VAL G N   1 
ATOM   18683 C  CA  . VAL G  3 117 ? 16.056  -49.032 54.298   1.00 247.82 ? 115  VAL G CA  1 
ATOM   18684 C  C   . VAL G  3 117 ? 14.602  -48.586 54.194   1.00 252.85 ? 115  VAL G C   1 
ATOM   18685 O  O   . VAL G  3 117 ? 13.831  -49.176 53.420   1.00 258.54 ? 115  VAL G O   1 
ATOM   18686 C  CB  . VAL G  3 117 ? 16.618  -49.427 52.921   1.00 234.19 ? 115  VAL G CB  1 
ATOM   18687 C  CG1 . VAL G  3 117 ? 16.637  -48.229 51.984   1.00 225.98 ? 115  VAL G CG1 1 
ATOM   18688 C  CG2 . VAL G  3 117 ? 18.009  -50.027 53.057   1.00 226.32 ? 115  VAL G CG2 1 
ATOM   18689 N  N   . PRO G  3 118 ? 14.181  -47.564 54.945   1.00 248.42 ? 116  PRO G N   1 
ATOM   18690 C  CA  . PRO G  3 118 ? 12.755  -47.177 54.907   1.00 247.10 ? 116  PRO G CA  1 
ATOM   18691 C  C   . PRO G  3 118 ? 12.301  -46.690 53.545   1.00 243.21 ? 116  PRO G C   1 
ATOM   18692 O  O   . PRO G  3 118 ? 11.317  -47.204 52.994   1.00 233.31 ? 116  PRO G O   1 
ATOM   18693 C  CB  . PRO G  3 118 ? 12.669  -46.072 55.973   1.00 256.04 ? 116  PRO G CB  1 
ATOM   18694 C  CG  . PRO G  3 118 ? 13.868  -46.289 56.857   1.00 255.66 ? 116  PRO G CG  1 
ATOM   18695 C  CD  . PRO G  3 118 ? 14.941  -46.806 55.952   1.00 244.55 ? 116  PRO G CD  1 
ATOM   18696 N  N   . GLU G  3 119 ? 12.998  -45.711 52.976   1.00 258.44 ? 117  GLU G N   1 
ATOM   18697 C  CA  . GLU G  3 119 ? 12.577  -45.149 51.701   1.00 261.88 ? 117  GLU G CA  1 
ATOM   18698 C  C   . GLU G  3 119 ? 13.358  -45.781 50.559   1.00 243.17 ? 117  GLU G C   1 
ATOM   18699 O  O   . GLU G  3 119 ? 14.592  -45.882 50.643   1.00 229.82 ? 117  GLU G O   1 
ATOM   18700 C  CB  . GLU G  3 119 ? 12.783  -43.637 51.701   1.00 272.84 ? 117  GLU G CB  1 
ATOM   18701 C  CG  . GLU G  3 119 ? 12.209  -42.923 50.495   1.00 273.37 ? 117  GLU G CG  1 
ATOM   18702 C  CD  . GLU G  3 119 ? 12.227  -41.416 50.655   1.00 273.26 ? 117  GLU G CD  1 
ATOM   18703 O  OE1 . GLU G  3 119 ? 12.682  -40.929 51.715   1.00 261.39 ? 117  GLU G OE1 1 
ATOM   18704 O  OE2 . GLU G  3 119 ? 11.782  -40.720 49.719   1.00 283.05 ? 117  GLU G OE2 1 
ATOM   18705 N  N   . PRO G  3 120 ? 12.689  -46.210 49.484   1.00 239.27 ? 118  PRO G N   1 
ATOM   18706 C  CA  . PRO G  3 120 ? 13.419  -46.810 48.352   1.00 240.84 ? 118  PRO G CA  1 
ATOM   18707 C  C   . PRO G  3 120 ? 14.425  -45.872 47.706   1.00 257.07 ? 118  PRO G C   1 
ATOM   18708 O  O   . PRO G  3 120 ? 15.320  -46.344 46.990   1.00 258.34 ? 118  PRO G O   1 
ATOM   18709 C  CB  . PRO G  3 120 ? 12.297  -47.188 47.372   1.00 232.85 ? 118  PRO G CB  1 
ATOM   18710 C  CG  . PRO G  3 120 ? 11.070  -47.292 48.215   1.00 235.98 ? 118  PRO G CG  1 
ATOM   18711 C  CD  . PRO G  3 120 ? 11.233  -46.239 49.273   1.00 244.74 ? 118  PRO G CD  1 
ATOM   18712 N  N   . VAL G  3 121 ? 14.309  -44.560 47.931   1.00 253.01 ? 119  VAL G N   1 
ATOM   18713 C  CA  . VAL G  3 121 ? 15.259  -43.624 47.342   1.00 236.81 ? 119  VAL G CA  1 
ATOM   18714 C  C   . VAL G  3 121 ? 16.583  -43.660 48.093   1.00 228.04 ? 119  VAL G C   1 
ATOM   18715 O  O   . VAL G  3 121 ? 17.644  -43.408 47.509   1.00 222.60 ? 119  VAL G O   1 
ATOM   18716 C  CB  . VAL G  3 121 ? 14.662  -42.204 47.309   1.00 227.38 ? 119  VAL G CB  1 
ATOM   18717 C  CG1 . VAL G  3 121 ? 15.461  -41.323 46.366   1.00 234.73 ? 119  VAL G CG1 1 
ATOM   18718 C  CG2 . VAL G  3 121 ? 13.200  -42.245 46.889   1.00 221.30 ? 119  VAL G CG2 1 
ATOM   18719 N  N   . LEU G  3 122 ? 16.551  -43.984 49.388   1.00 221.95 ? 120  LEU G N   1 
ATOM   18720 C  CA  . LEU G  3 122 ? 17.774  -44.072 50.175   1.00 220.06 ? 120  LEU G CA  1 
ATOM   18721 C  C   . LEU G  3 122 ? 18.692  -45.192 49.705   1.00 217.21 ? 120  LEU G C   1 
ATOM   18722 O  O   . LEU G  3 122 ? 19.899  -45.133 49.958   1.00 216.84 ? 120  LEU G O   1 
ATOM   18723 C  CB  . LEU G  3 122 ? 17.431  -44.278 51.648   1.00 228.80 ? 120  LEU G CB  1 
ATOM   18724 C  CG  . LEU G  3 122 ? 16.505  -43.238 52.271   1.00 236.86 ? 120  LEU G CG  1 
ATOM   18725 C  CD1 . LEU G  3 122 ? 16.180  -43.622 53.702   1.00 232.45 ? 120  LEU G CD1 1 
ATOM   18726 C  CD2 . LEU G  3 122 ? 17.132  -41.852 52.215   1.00 247.75 ? 120  LEU G CD2 1 
ATOM   18727 N  N   . LEU G  3 123 ? 18.152  -46.203 49.030   1.00 219.65 ? 121  LEU G N   1 
ATOM   18728 C  CA  . LEU G  3 123 ? 18.963  -47.328 48.586   1.00 227.25 ? 121  LEU G CA  1 
ATOM   18729 C  C   . LEU G  3 123 ? 19.887  -46.896 47.450   1.00 228.30 ? 121  LEU G C   1 
ATOM   18730 O  O   . LEU G  3 123 ? 19.441  -46.310 46.456   1.00 209.93 ? 121  LEU G O   1 
ATOM   18731 C  CB  . LEU G  3 123 ? 18.059  -48.481 48.141   1.00 230.18 ? 121  LEU G CB  1 
ATOM   18732 C  CG  . LEU G  3 123 ? 18.574  -49.927 48.158   1.00 232.90 ? 121  LEU G CG  1 
ATOM   18733 C  CD1 . LEU G  3 123 ? 19.477  -50.221 46.965   1.00 236.35 ? 121  LEU G CD1 1 
ATOM   18734 C  CD2 . LEU G  3 123 ? 19.292  -50.235 49.465   1.00 228.20 ? 121  LEU G CD2 1 
ATOM   18735 N  N   . SER G  3 124 ? 21.179  -47.192 47.599   1.00 235.40 ? 122  SER G N   1 
ATOM   18736 C  CA  . SER G  3 124 ? 22.180  -46.869 46.591   1.00 222.80 ? 122  SER G CA  1 
ATOM   18737 C  C   . SER G  3 124 ? 22.724  -48.115 45.903   1.00 225.83 ? 122  SER G C   1 
ATOM   18738 O  O   . SER G  3 124 ? 22.678  -48.211 44.673   1.00 230.42 ? 122  SER G O   1 
ATOM   18739 C  CB  . SER G  3 124 ? 23.324  -46.064 47.227   1.00 216.46 ? 122  SER G CB  1 
ATOM   18740 O  OG  . SER G  3 124 ? 23.970  -46.807 48.247   1.00 219.56 ? 122  SER G OG  1 
ATOM   18741 N  N   . ARG G  3 125 ? 23.238  -49.082 46.663   1.00 223.28 ? 123  ARG G N   1 
ATOM   18742 C  CA  . ARG G  3 125 ? 23.815  -50.295 46.094   1.00 209.11 ? 123  ARG G CA  1 
ATOM   18743 C  C   . ARG G  3 125 ? 23.326  -51.500 46.883   1.00 213.99 ? 123  ARG G C   1 
ATOM   18744 O  O   . ARG G  3 125 ? 23.408  -51.513 48.115   1.00 231.19 ? 123  ARG G O   1 
ATOM   18745 C  CB  . ARG G  3 125 ? 25.349  -50.237 46.102   1.00 197.87 ? 123  ARG G CB  1 
ATOM   18746 C  CG  . ARG G  3 125 ? 26.027  -51.488 45.556   1.00 198.23 ? 123  ARG G CG  1 
ATOM   18747 C  CD  . ARG G  3 125 ? 27.545  -51.339 45.490   1.00 205.56 ? 123  ARG G CD  1 
ATOM   18748 N  NE  . ARG G  3 125 ? 28.185  -52.499 44.867   1.00 216.54 ? 123  ARG G NE  1 
ATOM   18749 C  CZ  . ARG G  3 125 ? 28.514  -52.578 43.579   1.00 216.79 ? 123  ARG G CZ  1 
ATOM   18750 N  NH1 . ARG G  3 125 ? 28.269  -51.562 42.762   1.00 221.68 ? 123  ARG G NH1 1 
ATOM   18751 N  NH2 . ARG G  3 125 ? 29.091  -53.675 43.105   1.00 209.47 ? 123  ARG G NH2 1 
ATOM   18752 N  N   . ALA G  3 126 ? 22.819  -52.508 46.174   1.00 202.50 ? 124  ALA G N   1 
ATOM   18753 C  CA  . ALA G  3 126 ? 22.291  -53.719 46.805   1.00 207.05 ? 124  ALA G CA  1 
ATOM   18754 C  C   . ALA G  3 126 ? 22.795  -54.925 46.017   1.00 202.66 ? 124  ALA G C   1 
ATOM   18755 O  O   . ALA G  3 126 ? 22.213  -55.289 44.990   1.00 201.22 ? 124  ALA G O   1 
ATOM   18756 C  CB  . ALA G  3 126 ? 20.769  -53.691 46.864   1.00 211.27 ? 124  ALA G CB  1 
ATOM   18757 N  N   . GLU G  3 127 ? 23.867  -55.546 46.503   1.00 190.88 ? 125  GLU G N   1 
ATOM   18758 C  CA  . GLU G  3 127 ? 24.496  -56.679 45.834   1.00 190.20 ? 125  GLU G CA  1 
ATOM   18759 C  C   . GLU G  3 127 ? 24.242  -57.956 46.626   1.00 188.75 ? 125  GLU G C   1 
ATOM   18760 O  O   . GLU G  3 127 ? 24.437  -57.987 47.845   1.00 192.20 ? 125  GLU G O   1 
ATOM   18761 C  CB  . GLU G  3 127 ? 25.999  -56.441 45.653   1.00 194.16 ? 125  GLU G CB  1 
ATOM   18762 C  CG  . GLU G  3 127 ? 26.719  -55.877 46.872   1.00 197.70 ? 125  GLU G CG  1 
ATOM   18763 C  CD  . GLU G  3 127 ? 28.168  -55.523 46.578   1.00 193.06 ? 125  GLU G CD  1 
ATOM   18764 O  OE1 . GLU G  3 127 ? 28.691  -55.979 45.540   1.00 188.93 ? 125  GLU G OE1 1 
ATOM   18765 O  OE2 . GLU G  3 127 ? 28.782  -54.786 47.378   1.00 202.74 ? 125  GLU G OE2 1 
ATOM   18766 N  N   . LEU G  3 128 ? 23.802  -59.003 45.929   1.00 189.69 ? 126  LEU G N   1 
ATOM   18767 C  CA  . LEU G  3 128 ? 23.487  -60.289 46.543   1.00 195.40 ? 126  LEU G CA  1 
ATOM   18768 C  C   . LEU G  3 128 ? 24.729  -61.176 46.536   1.00 209.09 ? 126  LEU G C   1 
ATOM   18769 O  O   . LEU G  3 128 ? 25.249  -61.508 45.465   1.00 210.81 ? 126  LEU G O   1 
ATOM   18770 C  CB  . LEU G  3 128 ? 22.337  -60.963 45.794   1.00 191.59 ? 126  LEU G CB  1 
ATOM   18771 C  CG  . LEU G  3 128 ? 21.929  -62.374 46.224   1.00 197.87 ? 126  LEU G CG  1 
ATOM   18772 C  CD1 . LEU G  3 128 ? 21.450  -62.375 47.668   1.00 225.17 ? 126  LEU G CD1 1 
ATOM   18773 C  CD2 . LEU G  3 128 ? 20.859  -62.942 45.299   1.00 198.20 ? 126  LEU G CD2 1 
ATOM   18774 N  N   . ARG G  3 129 ? 25.195  -61.573 47.721   1.00 225.75 ? 127  ARG G N   1 
ATOM   18775 C  CA  . ARG G  3 129 ? 26.429  -62.337 47.869   1.00 220.22 ? 127  ARG G CA  1 
ATOM   18776 C  C   . ARG G  3 129 ? 26.140  -63.746 48.379   1.00 211.81 ? 127  ARG G C   1 
ATOM   18777 O  O   . ARG G  3 129 ? 25.303  -63.934 49.266   1.00 219.58 ? 127  ARG G O   1 
ATOM   18778 C  CB  . ARG G  3 129 ? 27.392  -61.623 48.825   1.00 223.22 ? 127  ARG G CB  1 
ATOM   18779 C  CG  . ARG G  3 129 ? 27.740  -60.203 48.399   1.00 213.57 ? 127  ARG G CG  1 
ATOM   18780 C  CD  . ARG G  3 129 ? 28.950  -59.676 49.149   1.00 218.63 ? 127  ARG G CD  1 
ATOM   18781 N  NE  . ARG G  3 129 ? 29.380  -58.381 48.632   1.00 219.78 ? 127  ARG G NE  1 
ATOM   18782 C  CZ  . ARG G  3 129 ? 30.490  -57.757 49.013   1.00 228.46 ? 127  ARG G CZ  1 
ATOM   18783 N  NH1 . ARG G  3 129 ? 31.286  -58.312 49.916   1.00 222.45 ? 127  ARG G NH1 1 
ATOM   18784 N  NH2 . ARG G  3 129 ? 30.805  -56.580 48.490   1.00 239.96 ? 127  ARG G NH2 1 
ATOM   18785 N  N   . LEU G  3 130 ? 26.841  -64.739 47.825   1.00 193.61 ? 128  LEU G N   1 
ATOM   18786 C  CA  . LEU G  3 130 ? 26.623  -66.128 48.219   1.00 196.28 ? 128  LEU G CA  1 
ATOM   18787 C  C   . LEU G  3 130 ? 27.898  -66.761 48.771   1.00 209.49 ? 128  LEU G C   1 
ATOM   18788 O  O   . LEU G  3 130 ? 28.812  -66.052 49.207   1.00 214.07 ? 128  LEU G O   1 
ATOM   18789 C  CB  . LEU G  3 130 ? 26.102  -66.945 47.036   1.00 197.71 ? 128  LEU G CB  1 
ATOM   18790 C  CG  . LEU G  3 130 ? 25.011  -66.312 46.175   1.00 195.99 ? 128  LEU G CG  1 
ATOM   18791 C  CD1 . LEU G  3 130 ? 24.561  -67.297 45.118   1.00 201.65 ? 128  LEU G CD1 1 
ATOM   18792 C  CD2 . LEU G  3 130 ? 23.831  -65.864 47.019   1.00 195.26 ? 128  LEU G CD2 1 
ATOM   18793 N  N   . LEU G  3 131 ? 27.974  -68.090 48.774   1.00 211.96 ? 129  LEU G N   1 
ATOM   18794 C  CA  . LEU G  3 131 ? 29.184  -68.769 49.226   1.00 207.77 ? 129  LEU G CA  1 
ATOM   18795 C  C   . LEU G  3 131 ? 29.372  -70.061 48.442   1.00 210.28 ? 129  LEU G C   1 
ATOM   18796 O  O   . LEU G  3 131 ? 28.526  -70.959 48.501   1.00 211.28 ? 129  LEU G O   1 
ATOM   18797 C  CB  . LEU G  3 131 ? 29.122  -69.042 50.730   1.00 213.69 ? 129  LEU G CB  1 
ATOM   18798 C  CG  . LEU G  3 131 ? 30.403  -69.527 51.413   1.00 224.06 ? 129  LEU G CG  1 
ATOM   18799 C  CD1 . LEU G  3 131 ? 30.464  -71.048 51.475   1.00 237.64 ? 129  LEU G CD1 1 
ATOM   18800 C  CD2 . LEU G  3 131 ? 31.640  -68.973 50.713   1.00 214.72 ? 129  LEU G CD2 1 
ATOM   18801 N  N   . ARG G  3 132 ? 30.493  -70.157 47.734   1.00 212.54 ? 130  ARG G N   1 
ATOM   18802 C  CA  . ARG G  3 132 ? 30.813  -71.308 46.903   1.00 214.90 ? 130  ARG G CA  1 
ATOM   18803 C  C   . ARG G  3 132 ? 31.569  -72.364 47.704   1.00 224.59 ? 130  ARG G C   1 
ATOM   18804 O  O   . ARG G  3 132 ? 32.363  -72.046 48.593   1.00 237.53 ? 130  ARG G O   1 
ATOM   18805 C  CB  . ARG G  3 132 ? 31.643  -70.864 45.694   1.00 216.43 ? 130  ARG G CB  1 
ATOM   18806 C  CG  . ARG G  3 132 ? 32.437  -71.956 44.982   1.00 226.57 ? 130  ARG G CG  1 
ATOM   18807 C  CD  . ARG G  3 132 ? 33.484  -71.342 44.057   1.00 220.22 ? 130  ARG G CD  1 
ATOM   18808 N  NE  . ARG G  3 132 ? 34.358  -72.340 43.443   1.00 240.60 ? 130  ARG G NE  1 
ATOM   18809 C  CZ  . ARG G  3 132 ? 34.314  -72.689 42.160   1.00 245.90 ? 130  ARG G CZ  1 
ATOM   18810 N  NH1 . ARG G  3 132 ? 35.151  -73.607 41.691   1.00 244.90 ? 130  ARG G NH1 1 
ATOM   18811 N  NH2 . ARG G  3 132 ? 33.434  -72.121 41.347   1.00 243.41 ? 130  ARG G NH2 1 
ATOM   18812 N  N   . LEU G  3 133 ? 31.306  -73.632 47.386   1.00 228.46 ? 131  LEU G N   1 
ATOM   18813 C  CA  . LEU G  3 133 ? 32.008  -74.752 48.004   1.00 243.25 ? 131  LEU G CA  1 
ATOM   18814 C  C   . LEU G  3 133 ? 32.815  -75.562 47.002   1.00 246.08 ? 131  LEU G C   1 
ATOM   18815 O  O   . LEU G  3 133 ? 34.019  -75.770 47.207   1.00 241.85 ? 131  LEU G O   1 
ATOM   18816 C  CB  . LEU G  3 133 ? 31.015  -75.676 48.735   1.00 257.80 ? 131  LEU G CB  1 
ATOM   18817 C  CG  . LEU G  3 133 ? 30.456  -75.247 50.097   1.00 260.11 ? 131  LEU G CG  1 
ATOM   18818 C  CD1 . LEU G  3 133 ? 29.415  -74.147 49.960   1.00 255.84 ? 131  LEU G CD1 1 
ATOM   18819 C  CD2 . LEU G  3 133 ? 29.877  -76.445 50.837   1.00 260.73 ? 131  LEU G CD2 1 
ATOM   18820 N  N   . LYS G  3 134 ? 32.185  -76.026 45.922   1.00 255.49 ? 132  LYS G N   1 
ATOM   18821 C  CA  . LYS G  3 134 ? 32.856  -76.892 44.959   1.00 263.56 ? 132  LYS G CA  1 
ATOM   18822 C  C   . LYS G  3 134 ? 34.034  -76.171 44.317   1.00 252.43 ? 132  LYS G C   1 
ATOM   18823 O  O   . LYS G  3 134 ? 33.933  -75.007 43.925   1.00 247.71 ? 132  LYS G O   1 
ATOM   18824 C  CB  . LYS G  3 134 ? 31.871  -77.343 43.880   1.00 261.55 ? 132  LYS G CB  1 
ATOM   18825 C  CG  . LYS G  3 134 ? 32.158  -78.709 43.275   1.00 263.60 ? 132  LYS G CG  1 
ATOM   18826 C  CD  . LYS G  3 134 ? 30.975  -79.177 42.438   1.00 256.87 ? 132  LYS G CD  1 
ATOM   18827 C  CE  . LYS G  3 134 ? 31.124  -80.627 42.018   1.00 265.55 ? 132  LYS G CE  1 
ATOM   18828 N  NZ  . LYS G  3 134 ? 29.933  -81.107 41.264   1.00 264.21 ? 132  LYS G NZ  1 
ATOM   18829 N  N   . LEU G  3 135 ? 35.157  -76.875 44.203   1.00 250.50 ? 133  LEU G N   1 
ATOM   18830 C  CA  . LEU G  3 135 ? 36.382  -76.284 43.693   1.00 241.04 ? 133  LEU G CA  1 
ATOM   18831 C  C   . LEU G  3 135 ? 36.856  -76.881 42.377   1.00 236.91 ? 133  LEU G C   1 
ATOM   18832 O  O   . LEU G  3 135 ? 37.733  -76.291 41.736   1.00 228.44 ? 133  LEU G O   1 
ATOM   18833 C  CB  . LEU G  3 135 ? 37.504  -76.402 44.740   1.00 246.92 ? 133  LEU G CB  1 
ATOM   18834 C  CG  . LEU G  3 135 ? 37.951  -77.775 45.255   1.00 248.05 ? 133  LEU G CG  1 
ATOM   18835 C  CD1 . LEU G  3 135 ? 39.142  -78.299 44.464   1.00 246.59 ? 133  LEU G CD1 1 
ATOM   18836 C  CD2 . LEU G  3 135 ? 38.287  -77.701 46.737   1.00 241.86 ? 133  LEU G CD2 1 
ATOM   18837 N  N   . LYS G  3 136 ? 36.305  -78.014 41.951   1.00 252.90 ? 134  LYS G N   1 
ATOM   18838 C  CA  . LYS G  3 136 ? 36.753  -78.704 40.750   1.00 250.86 ? 134  LYS G CA  1 
ATOM   18839 C  C   . LYS G  3 136 ? 35.824  -78.414 39.575   1.00 242.36 ? 134  LYS G C   1 
ATOM   18840 O  O   . LYS G  3 136 ? 34.641  -78.108 39.752   1.00 234.02 ? 134  LYS G O   1 
ATOM   18841 C  CB  . LYS G  3 136 ? 36.834  -80.213 40.990   1.00 246.90 ? 134  LYS G CB  1 
ATOM   18842 C  CG  . LYS G  3 136 ? 37.833  -80.611 42.062   1.00 239.74 ? 134  LYS G CG  1 
ATOM   18843 C  CD  . LYS G  3 136 ? 37.803  -82.101 42.327   1.00 242.34 ? 134  LYS G CD  1 
ATOM   18844 C  CE  . LYS G  3 136 ? 38.780  -82.462 43.431   1.00 252.94 ? 134  LYS G CE  1 
ATOM   18845 N  NZ  . LYS G  3 136 ? 38.782  -83.920 43.731   1.00 265.30 ? 134  LYS G NZ  1 
ATOM   18846 N  N   . VAL G  3 137 ? 36.384  -78.519 38.365   1.00 242.40 ? 135  VAL G N   1 
ATOM   18847 C  CA  . VAL G  3 137 ? 35.691  -78.255 37.103   1.00 243.63 ? 135  VAL G CA  1 
ATOM   18848 C  C   . VAL G  3 137 ? 35.063  -76.861 37.138   1.00 253.54 ? 135  VAL G C   1 
ATOM   18849 O  O   . VAL G  3 137 ? 35.423  -76.027 37.976   1.00 255.77 ? 135  VAL G O   1 
ATOM   18850 C  CB  . VAL G  3 137 ? 34.645  -79.350 36.797   1.00 246.60 ? 135  VAL G CB  1 
ATOM   18851 C  CG1 . VAL G  3 137 ? 34.383  -79.457 35.298   1.00 246.38 ? 135  VAL G CG1 1 
ATOM   18852 C  CG2 . VAL G  3 137 ? 35.108  -80.701 37.323   1.00 259.46 ? 135  VAL G CG2 1 
ATOM   18853 N  N   . GLU G  3 138 ? 34.128  -76.595 36.226   1.00 263.58 ? 136  GLU G N   1 
ATOM   18854 C  CA  . GLU G  3 138 ? 33.508  -75.284 36.091   1.00 255.28 ? 136  GLU G CA  1 
ATOM   18855 C  C   . GLU G  3 138 ? 32.041  -75.474 35.735   1.00 249.95 ? 136  GLU G C   1 
ATOM   18856 O  O   . GLU G  3 138 ? 31.637  -76.529 35.237   1.00 255.87 ? 136  GLU G O   1 
ATOM   18857 C  CB  . GLU G  3 138 ? 34.209  -74.441 35.017   1.00 247.42 ? 136  GLU G CB  1 
ATOM   18858 C  CG  . GLU G  3 138 ? 33.899  -74.905 33.601   1.00 251.49 ? 136  GLU G CG  1 
ATOM   18859 C  CD  . GLU G  3 138 ? 34.888  -74.396 32.573   1.00 249.17 ? 136  GLU G CD  1 
ATOM   18860 O  OE1 . GLU G  3 138 ? 35.844  -73.691 32.957   1.00 244.77 ? 136  GLU G OE1 1 
ATOM   18861 O  OE2 . GLU G  3 138 ? 34.710  -74.710 31.376   1.00 252.28 ? 136  GLU G OE2 1 
ATOM   18862 N  N   . GLN G  3 139 ? 31.241  -74.439 35.990   1.00 230.59 ? 137  GLN G N   1 
ATOM   18863 C  CA  . GLN G  3 139 ? 29.821  -74.485 35.670   1.00 236.28 ? 137  GLN G CA  1 
ATOM   18864 C  C   . GLN G  3 139 ? 29.348  -73.109 35.217   1.00 237.33 ? 137  GLN G C   1 
ATOM   18865 O  O   . GLN G  3 139 ? 29.997  -72.089 35.464   1.00 233.07 ? 137  GLN G O   1 
ATOM   18866 C  CB  . GLN G  3 139 ? 28.987  -74.983 36.860   1.00 240.63 ? 137  GLN G CB  1 
ATOM   18867 C  CG  . GLN G  3 139 ? 28.951  -76.507 37.010   1.00 255.55 ? 137  GLN G CG  1 
ATOM   18868 C  CD  . GLN G  3 139 ? 29.724  -77.008 38.219   1.00 259.79 ? 137  GLN G CD  1 
ATOM   18869 O  OE1 . GLN G  3 139 ? 30.609  -76.324 38.733   1.00 263.22 ? 137  GLN G OE1 1 
ATOM   18870 N  NE2 . GLN G  3 139 ? 29.387  -78.209 38.682   1.00 253.73 ? 137  GLN G NE2 1 
ATOM   18871 N  N   . HIS G  3 140 ? 28.200  -73.100 34.537   1.00 237.84 ? 138  HIS G N   1 
ATOM   18872 C  CA  . HIS G  3 140 ? 27.602  -71.899 33.963   1.00 221.51 ? 138  HIS G CA  1 
ATOM   18873 C  C   . HIS G  3 140 ? 26.280  -71.629 34.665   1.00 213.59 ? 138  HIS G C   1 
ATOM   18874 O  O   . HIS G  3 140 ? 25.445  -72.532 34.787   1.00 220.57 ? 138  HIS G O   1 
ATOM   18875 C  CB  . HIS G  3 140 ? 27.386  -72.067 32.455   1.00 223.07 ? 138  HIS G CB  1 
ATOM   18876 C  CG  . HIS G  3 140 ? 27.015  -70.802 31.749   1.00 211.99 ? 138  HIS G CG  1 
ATOM   18877 N  ND1 . HIS G  3 140 ? 27.915  -69.780 31.535   1.00 206.96 ? 138  HIS G ND1 1 
ATOM   18878 C  CD2 . HIS G  3 140 ? 25.846  -70.395 31.201   1.00 210.11 ? 138  HIS G CD2 1 
ATOM   18879 C  CE1 . HIS G  3 140 ? 27.315  -68.797 30.888   1.00 204.43 ? 138  HIS G CE1 1 
ATOM   18880 N  NE2 . HIS G  3 140 ? 26.059  -69.145 30.674   1.00 207.42 ? 138  HIS G NE2 1 
ATOM   18881 N  N   . VAL G  3 141 ? 26.081  -70.391 35.110   1.00 193.00 ? 139  VAL G N   1 
ATOM   18882 C  CA  . VAL G  3 141 ? 25.006  -70.056 36.036   1.00 194.49 ? 139  VAL G CA  1 
ATOM   18883 C  C   . VAL G  3 141 ? 24.134  -68.961 35.434   1.00 196.64 ? 139  VAL G C   1 
ATOM   18884 O  O   . VAL G  3 141 ? 24.649  -67.970 34.904   1.00 212.09 ? 139  VAL G O   1 
ATOM   18885 C  CB  . VAL G  3 141 ? 25.572  -69.618 37.398   1.00 192.62 ? 139  VAL G CB  1 
ATOM   18886 C  CG1 . VAL G  3 141 ? 24.458  -69.144 38.306   1.00 194.77 ? 139  VAL G CG1 1 
ATOM   18887 C  CG2 . VAL G  3 141 ? 26.341  -70.761 38.035   1.00 203.66 ? 139  VAL G CG2 1 
ATOM   18888 N  N   . GLU G  3 142 ? 22.816  -69.133 35.535   1.00 192.72 ? 140  GLU G N   1 
ATOM   18889 C  CA  . GLU G  3 142 ? 21.848  -68.105 35.177   1.00 193.31 ? 140  GLU G CA  1 
ATOM   18890 C  C   . GLU G  3 142 ? 21.037  -67.726 36.408   1.00 193.23 ? 140  GLU G C   1 
ATOM   18891 O  O   . GLU G  3 142 ? 20.723  -68.579 37.244   1.00 194.05 ? 140  GLU G O   1 
ATOM   18892 C  CB  . GLU G  3 142 ? 20.907  -68.577 34.064   1.00 201.82 ? 140  GLU G CB  1 
ATOM   18893 C  CG  . GLU G  3 142 ? 21.603  -68.969 32.774   1.00 212.06 ? 140  GLU G CG  1 
ATOM   18894 C  CD  . GLU G  3 142 ? 20.634  -69.505 31.740   1.00 225.00 ? 140  GLU G CD  1 
ATOM   18895 O  OE1 . GLU G  3 142 ? 19.408  -69.424 31.973   1.00 225.47 ? 140  GLU G OE1 1 
ATOM   18896 O  OE2 . GLU G  3 142 ? 21.098  -70.012 30.696   1.00 234.14 ? 140  GLU G OE2 1 
ATOM   18897 N  N   . LEU G  3 143 ? 20.695  -66.446 36.513   1.00 186.57 ? 141  LEU G N   1 
ATOM   18898 C  CA  . LEU G  3 143 ? 19.980  -65.909 37.661   1.00 183.87 ? 141  LEU G CA  1 
ATOM   18899 C  C   . LEU G  3 143 ? 18.607  -65.409 37.232   1.00 191.19 ? 141  LEU G C   1 
ATOM   18900 O  O   . LEU G  3 143 ? 18.454  -64.845 36.145   1.00 212.04 ? 141  LEU G O   1 
ATOM   18901 C  CB  . LEU G  3 143 ? 20.775  -64.774 38.304   1.00 177.96 ? 141  LEU G CB  1 
ATOM   18902 C  CG  . LEU G  3 143 ? 20.178  -64.192 39.579   1.00 174.30 ? 141  LEU G CG  1 
ATOM   18903 C  CD1 . LEU G  3 143 ? 20.091  -65.270 40.643   1.00 179.22 ? 141  LEU G CD1 1 
ATOM   18904 C  CD2 . LEU G  3 143 ? 21.011  -63.016 40.053   1.00 168.38 ? 141  LEU G CD2 1 
ATOM   18905 N  N   . TYR G  3 144 ? 17.608  -65.614 38.087   1.00 199.37 ? 142  TYR G N   1 
ATOM   18906 C  CA  . TYR G  3 144 ? 16.237  -65.243 37.770   1.00 204.71 ? 142  TYR G CA  1 
ATOM   18907 C  C   . TYR G  3 144 ? 15.626  -64.470 38.931   1.00 204.28 ? 142  TYR G C   1 
ATOM   18908 O  O   . TYR G  3 144 ? 16.198  -64.379 40.020   1.00 200.68 ? 142  TYR G O   1 
ATOM   18909 C  CB  . TYR G  3 144 ? 15.387  -66.479 37.444   1.00 223.17 ? 142  TYR G CB  1 
ATOM   18910 C  CG  . TYR G  3 144 ? 15.764  -67.174 36.152   1.00 236.02 ? 142  TYR G CG  1 
ATOM   18911 C  CD1 . TYR G  3 144 ? 15.174  -66.811 34.948   1.00 234.52 ? 142  TYR G CD1 1 
ATOM   18912 C  CD2 . TYR G  3 144 ? 16.702  -68.200 36.137   1.00 238.40 ? 142  TYR G CD2 1 
ATOM   18913 C  CE1 . TYR G  3 144 ? 15.511  -67.444 33.764   1.00 226.26 ? 142  TYR G CE1 1 
ATOM   18914 C  CE2 . TYR G  3 144 ? 17.045  -68.840 34.956   1.00 229.00 ? 142  TYR G CE2 1 
ATOM   18915 C  CZ  . TYR G  3 144 ? 16.446  -68.457 33.775   1.00 217.34 ? 142  TYR G CZ  1 
ATOM   18916 O  OH  . TYR G  3 144 ? 16.780  -69.089 32.599   1.00 213.77 ? 142  TYR G OH  1 
ATOM   18917 N  N   . GLN G  3 145 ? 14.445  -63.907 38.687   1.00 218.63 ? 143  GLN G N   1 
ATOM   18918 C  CA  . GLN G  3 145 ? 13.712  -63.140 39.683   1.00 224.68 ? 143  GLN G CA  1 
ATOM   18919 C  C   . GLN G  3 145 ? 12.310  -63.716 39.850   1.00 226.51 ? 143  GLN G C   1 
ATOM   18920 O  O   . GLN G  3 145 ? 11.755  -64.311 38.923   1.00 233.54 ? 143  GLN G O   1 
ATOM   18921 C  CB  . GLN G  3 145 ? 13.635  -61.659 39.288   1.00 224.13 ? 143  GLN G CB  1 
ATOM   18922 C  CG  . GLN G  3 145 ? 13.042  -60.749 40.351   1.00 227.90 ? 143  GLN G CG  1 
ATOM   18923 C  CD  . GLN G  3 145 ? 12.804  -59.345 39.840   1.00 231.42 ? 143  GLN G CD  1 
ATOM   18924 O  OE1 . GLN G  3 145 ? 13.311  -58.962 38.783   1.00 238.45 ? 143  GLN G OE1 1 
ATOM   18925 N  NE2 . GLN G  3 145 ? 12.023  -58.568 40.584   1.00 226.70 ? 143  GLN G NE2 1 
ATOM   18926 N  N   . LYS G  3 146 ? 11.740  -63.538 41.042   1.00 219.82 ? 144  LYS G N   1 
ATOM   18927 C  CA  . LYS G  3 146 ? 10.435  -64.109 41.359   1.00 223.14 ? 144  LYS G CA  1 
ATOM   18928 C  C   . LYS G  3 146 ? 9.323   -63.213 40.824   1.00 226.64 ? 144  LYS G C   1 
ATOM   18929 O  O   . LYS G  3 146 ? 9.230   -62.037 41.194   1.00 220.77 ? 144  LYS G O   1 
ATOM   18930 C  CB  . LYS G  3 146 ? 10.289  -64.296 42.867   1.00 222.80 ? 144  LYS G CB  1 
ATOM   18931 C  CG  . LYS G  3 146 ? 8.993   -64.970 43.290   1.00 222.91 ? 144  LYS G CG  1 
ATOM   18932 C  CD  . LYS G  3 146 ? 8.885   -65.042 44.805   1.00 220.21 ? 144  LYS G CD  1 
ATOM   18933 C  CE  . LYS G  3 146 ? 7.560   -65.649 45.236   1.00 223.04 ? 144  LYS G CE  1 
ATOM   18934 N  NZ  . LYS G  3 146 ? 7.322   -65.571 46.706   1.00 221.59 ? 144  LYS G NZ  1 
ATOM   18935 N  N   . TYR G  3 147 ? 8.474   -63.776 39.964   1.00 238.51 ? 145  TYR G N   1 
ATOM   18936 C  CA  . TYR G  3 147 ? 7.323   -63.074 39.407   1.00 242.57 ? 145  TYR G CA  1 
ATOM   18937 C  C   . TYR G  3 147 ? 6.085   -63.951 39.526   1.00 252.25 ? 145  TYR G C   1 
ATOM   18938 O  O   . TYR G  3 147 ? 6.128   -65.139 39.189   1.00 256.40 ? 145  TYR G O   1 
ATOM   18939 C  CB  . TYR G  3 147 ? 7.558   -62.691 37.942   1.00 235.86 ? 145  TYR G CB  1 
ATOM   18940 C  CG  . TYR G  3 147 ? 8.374   -61.433 37.769   1.00 232.81 ? 145  TYR G CG  1 
ATOM   18941 C  CD1 . TYR G  3 147 ? 7.762   -60.187 37.738   1.00 228.29 ? 145  TYR G CD1 1 
ATOM   18942 C  CD2 . TYR G  3 147 ? 9.755   -61.490 37.644   1.00 243.64 ? 145  TYR G CD2 1 
ATOM   18943 C  CE1 . TYR G  3 147 ? 8.503   -59.030 37.585   1.00 229.23 ? 145  TYR G CE1 1 
ATOM   18944 C  CE2 . TYR G  3 147 ? 10.506  -60.338 37.489   1.00 242.63 ? 145  TYR G CE2 1 
ATOM   18945 C  CZ  . TYR G  3 147 ? 9.875   -59.111 37.460   1.00 235.07 ? 145  TYR G CZ  1 
ATOM   18946 O  OH  . TYR G  3 147 ? 10.616  -57.961 37.306   1.00 232.27 ? 145  TYR G OH  1 
ATOM   18947 N  N   . SER G  3 148 ? 4.985   -63.365 40.009   1.00 251.23 ? 146  SER G N   1 
ATOM   18948 C  CA  . SER G  3 148 ? 3.699   -64.048 40.158   1.00 245.81 ? 146  SER G CA  1 
ATOM   18949 C  C   . SER G  3 148 ? 3.785   -65.262 41.080   1.00 251.28 ? 146  SER G C   1 
ATOM   18950 O  O   . SER G  3 148 ? 2.899   -66.125 41.056   1.00 254.09 ? 146  SER G O   1 
ATOM   18951 C  CB  . SER G  3 148 ? 3.127   -64.457 38.795   1.00 240.98 ? 146  SER G CB  1 
ATOM   18952 O  OG  . SER G  3 148 ? 1.826   -65.003 38.923   1.00 244.28 ? 146  SER G OG  1 
ATOM   18953 N  N   . GLN G  3 149 ? 4.843   -65.347 41.886   1.00 250.52 ? 147  GLN G N   1 
ATOM   18954 C  CA  . GLN G  3 149 ? 5.108   -66.442 42.817   1.00 242.80 ? 147  GLN G CA  1 
ATOM   18955 C  C   . GLN G  3 149 ? 5.187   -67.804 42.131   1.00 237.65 ? 147  GLN G C   1 
ATOM   18956 O  O   . GLN G  3 149 ? 5.142   -68.839 42.810   1.00 238.14 ? 147  GLN G O   1 
ATOM   18957 C  CB  . GLN G  3 149 ? 4.069   -66.477 43.945   1.00 254.91 ? 147  GLN G CB  1 
ATOM   18958 C  CG  . GLN G  3 149 ? 4.008   -65.190 44.759   1.00 255.38 ? 147  GLN G CG  1 
ATOM   18959 C  CD  . GLN G  3 149 ? 3.049   -65.277 45.929   1.00 267.82 ? 147  GLN G CD  1 
ATOM   18960 O  OE1 . GLN G  3 149 ? 2.631   -66.364 46.327   1.00 272.80 ? 147  GLN G OE1 1 
ATOM   18961 N  NE2 . GLN G  3 149 ? 2.692   -64.125 46.486   1.00 270.49 ? 147  GLN G NE2 1 
ATOM   18962 N  N   . ASN G  3 150 ? 5.318   -67.830 40.804   1.00 233.79 ? 148  ASN G N   1 
ATOM   18963 C  CA  . ASN G  3 150 ? 5.406   -69.073 40.049   1.00 237.76 ? 148  ASN G CA  1 
ATOM   18964 C  C   . ASN G  3 150 ? 6.331   -68.901 38.851   1.00 232.07 ? 148  ASN G C   1 
ATOM   18965 O  O   . ASN G  3 150 ? 7.102   -69.807 38.516   1.00 232.20 ? 148  ASN G O   1 
ATOM   18966 C  CB  . ASN G  3 150 ? 4.017   -69.522 39.586   1.00 248.73 ? 148  ASN G CB  1 
ATOM   18967 C  CG  . ASN G  3 150 ? 4.062   -70.784 38.738   1.00 256.50 ? 148  ASN G CG  1 
ATOM   18968 O  OD1 . ASN G  3 150 ? 4.939   -71.629 38.909   1.00 265.74 ? 148  ASN G OD1 1 
ATOM   18969 N  ND2 . ASN G  3 150 ? 3.113   -70.914 37.816   1.00 254.70 ? 148  ASN G ND2 1 
ATOM   18970 N  N   . SER G  3 151 ? 6.263   -67.744 38.203   1.00 221.50 ? 149  SER G N   1 
ATOM   18971 C  CA  . SER G  3 151 ? 7.062   -67.475 37.019   1.00 219.47 ? 149  SER G CA  1 
ATOM   18972 C  C   . SER G  3 151 ? 8.387   -66.825 37.397   1.00 215.91 ? 149  SER G C   1 
ATOM   18973 O  O   . SER G  3 151 ? 8.490   -66.098 38.389   1.00 212.88 ? 149  SER G O   1 
ATOM   18974 C  CB  . SER G  3 151 ? 6.301   -66.572 36.048   1.00 221.17 ? 149  SER G CB  1 
ATOM   18975 O  OG  . SER G  3 151 ? 7.124   -66.202 34.957   1.00 229.19 ? 149  SER G OG  1 
ATOM   18976 N  N   . TRP G  3 152 ? 9.411   -67.098 36.593   1.00 232.78 ? 150  TRP G N   1 
ATOM   18977 C  CA  . TRP G  3 152 ? 10.746  -66.569 36.826   1.00 234.83 ? 150  TRP G CA  1 
ATOM   18978 C  C   . TRP G  3 152 ? 11.231  -65.850 35.579   1.00 235.04 ? 150  TRP G C   1 
ATOM   18979 O  O   . TRP G  3 152 ? 11.075  -66.349 34.459   1.00 242.69 ? 150  TRP G O   1 
ATOM   18980 C  CB  . TRP G  3 152 ? 11.730  -67.679 37.208   1.00 239.32 ? 150  TRP G CB  1 
ATOM   18981 C  CG  . TRP G  3 152 ? 11.247  -68.537 38.338   1.00 253.04 ? 150  TRP G CG  1 
ATOM   18982 C  CD1 . TRP G  3 152 ? 10.601  -69.734 38.237   1.00 264.26 ? 150  TRP G CD1 1 
ATOM   18983 C  CD2 . TRP G  3 152 ? 11.365  -68.261 39.741   1.00 251.73 ? 150  TRP G CD2 1 
ATOM   18984 N  NE1 . TRP G  3 152 ? 10.313  -70.224 39.488   1.00 268.41 ? 150  TRP G NE1 1 
ATOM   18985 C  CE2 . TRP G  3 152 ? 10.771  -69.339 40.429   1.00 260.51 ? 150  TRP G CE2 1 
ATOM   18986 C  CE3 . TRP G  3 152 ? 11.916  -67.211 40.481   1.00 238.00 ? 150  TRP G CE3 1 
ATOM   18987 C  CZ2 . TRP G  3 152 ? 10.712  -69.397 41.821   1.00 252.05 ? 150  TRP G CZ2 1 
ATOM   18988 C  CZ3 . TRP G  3 152 ? 11.858  -67.272 41.865   1.00 235.42 ? 150  TRP G CZ3 1 
ATOM   18989 C  CH2 . TRP G  3 152 ? 11.259  -68.356 42.519   1.00 240.04 ? 150  TRP G CH2 1 
ATOM   18990 N  N   . ARG G  3 153 ? 11.821  -64.677 35.775   1.00 205.47 ? 151  ARG G N   1 
ATOM   18991 C  CA  . ARG G  3 153 ? 12.310  -63.871 34.671   1.00 206.01 ? 151  ARG G CA  1 
ATOM   18992 C  C   . ARG G  3 153 ? 13.814  -63.675 34.791   1.00 202.53 ? 151  ARG G C   1 
ATOM   18993 O  O   . ARG G  3 153 ? 14.350  -63.515 35.893   1.00 198.19 ? 151  ARG G O   1 
ATOM   18994 C  CB  . ARG G  3 153 ? 11.588  -62.523 34.605   1.00 208.23 ? 151  ARG G CB  1 
ATOM   18995 C  CG  . ARG G  3 153 ? 10.141  -62.641 34.128   1.00 213.36 ? 151  ARG G CG  1 
ATOM   18996 C  CD  . ARG G  3 153 ? 10.022  -63.537 32.892   1.00 213.10 ? 151  ARG G CD  1 
ATOM   18997 N  NE  . ARG G  3 153 ? 10.630  -62.941 31.704   1.00 212.75 ? 151  ARG G NE  1 
ATOM   18998 C  CZ  . ARG G  3 153 ? 9.962   -62.241 30.792   1.00 213.27 ? 151  ARG G CZ  1 
ATOM   18999 N  NH1 . ARG G  3 153 ? 8.658   -62.048 30.928   1.00 220.29 ? 151  ARG G NH1 1 
ATOM   19000 N  NH2 . ARG G  3 153 ? 10.596  -61.733 29.742   1.00 212.08 ? 151  ARG G NH2 1 
ATOM   19001 N  N   . TYR G  3 154 ? 14.475  -63.694 33.638   1.00 212.44 ? 152  TYR G N   1 
ATOM   19002 C  CA  . TYR G  3 154 ? 15.925  -63.643 33.558   1.00 205.07 ? 152  TYR G CA  1 
ATOM   19003 C  C   . TYR G  3 154 ? 16.464  -62.347 34.156   1.00 195.20 ? 152  TYR G C   1 
ATOM   19004 O  O   . TYR G  3 154 ? 15.803  -61.304 34.146   1.00 191.64 ? 152  TYR G O   1 
ATOM   19005 C  CB  . TYR G  3 154 ? 16.351  -63.772 32.095   1.00 205.83 ? 152  TYR G CB  1 
ATOM   19006 C  CG  . TYR G  3 154 ? 17.827  -63.957 31.874   1.00 200.61 ? 152  TYR G CG  1 
ATOM   19007 C  CD1 . TYR G  3 154 ? 18.397  -65.222 31.907   1.00 202.17 ? 152  TYR G CD1 1 
ATOM   19008 C  CD2 . TYR G  3 154 ? 18.649  -62.871 31.610   1.00 195.88 ? 152  TYR G CD2 1 
ATOM   19009 C  CE1 . TYR G  3 154 ? 19.742  -65.398 31.696   1.00 202.91 ? 152  TYR G CE1 1 
ATOM   19010 C  CE2 . TYR G  3 154 ? 19.995  -63.037 31.399   1.00 196.25 ? 152  TYR G CE2 1 
ATOM   19011 C  CZ  . TYR G  3 154 ? 20.535  -64.303 31.443   1.00 207.08 ? 152  TYR G CZ  1 
ATOM   19012 O  OH  . TYR G  3 154 ? 21.878  -64.480 31.232   1.00 219.69 ? 152  TYR G OH  1 
ATOM   19013 N  N   . LEU G  3 155 ? 17.684  -62.424 34.688   1.00 191.36 ? 153  LEU G N   1 
ATOM   19014 C  CA  . LEU G  3 155 ? 18.350  -61.259 35.254   1.00 183.41 ? 153  LEU G CA  1 
ATOM   19015 C  C   . LEU G  3 155 ? 19.740  -61.093 34.657   1.00 180.52 ? 153  LEU G C   1 
ATOM   19016 O  O   . LEU G  3 155 ? 19.907  -60.390 33.655   1.00 187.06 ? 153  LEU G O   1 
ATOM   19017 C  CB  . LEU G  3 155 ? 18.438  -61.372 36.775   1.00 179.09 ? 153  LEU G CB  1 
ATOM   19018 C  CG  . LEU G  3 155 ? 17.097  -61.345 37.504   1.00 179.90 ? 153  LEU G CG  1 
ATOM   19019 C  CD1 . LEU G  3 155 ? 17.320  -61.396 38.999   1.00 177.65 ? 153  LEU G CD1 1 
ATOM   19020 C  CD2 . LEU G  3 155 ? 16.316  -60.104 37.114   1.00 177.98 ? 153  LEU G CD2 1 
ATOM   19021 N  N   . SER G  3 156 ? 20.742  -61.738 35.252   1.00 178.57 ? 154  SER G N   1 
ATOM   19022 C  CA  . SER G  3 156 ? 22.125  -61.604 34.813   1.00 176.26 ? 154  SER G CA  1 
ATOM   19023 C  C   . SER G  3 156 ? 22.749  -62.987 34.635   1.00 187.83 ? 154  SER G C   1 
ATOM   19024 O  O   . SER G  3 156 ? 22.103  -64.018 34.847   1.00 192.21 ? 154  SER G O   1 
ATOM   19025 C  CB  . SER G  3 156 ? 22.935  -60.759 35.802   1.00 169.01 ? 154  SER G CB  1 
ATOM   19026 O  OG  . SER G  3 156 ? 22.960  -61.349 37.087   1.00 169.52 ? 154  SER G OG  1 
ATOM   19027 N  N   . ASN G  3 157 ? 24.024  -63.004 34.238   1.00 199.08 ? 155  ASN G N   1 
ATOM   19028 C  CA  . ASN G  3 157 ? 24.745  -64.238 33.954   1.00 204.70 ? 155  ASN G CA  1 
ATOM   19029 C  C   . ASN G  3 157 ? 26.208  -64.084 34.354   1.00 196.46 ? 155  ASN G C   1 
ATOM   19030 O  O   . ASN G  3 157 ? 26.761  -62.980 34.328   1.00 187.33 ? 155  ASN G O   1 
ATOM   19031 C  CB  . ASN G  3 157 ? 24.638  -64.610 32.467   1.00 219.50 ? 155  ASN G CB  1 
ATOM   19032 C  CG  . ASN G  3 157 ? 25.278  -65.948 32.143   1.00 232.31 ? 155  ASN G CG  1 
ATOM   19033 O  OD1 . ASN G  3 157 ? 26.453  -66.013 31.779   1.00 233.88 ? 155  ASN G OD1 1 
ATOM   19034 N  ND2 . ASN G  3 157 ? 24.503  -67.021 32.262   1.00 239.42 ? 155  ASN G ND2 1 
ATOM   19035 N  N   . ARG G  3 158 ? 26.834  -65.206 34.720   1.00 195.27 ? 156  ARG G N   1 
ATOM   19036 C  CA  . ARG G  3 158 ? 28.230  -65.197 35.143   1.00 192.45 ? 156  ARG G CA  1 
ATOM   19037 C  C   . ARG G  3 158 ? 28.808  -66.603 35.048   1.00 193.67 ? 156  ARG G C   1 
ATOM   19038 O  O   . ARG G  3 158 ? 28.209  -67.559 35.551   1.00 196.23 ? 156  ARG G O   1 
ATOM   19039 C  CB  . ARG G  3 158 ? 28.361  -64.669 36.573   1.00 192.20 ? 156  ARG G CB  1 
ATOM   19040 C  CG  . ARG G  3 158 ? 29.784  -64.389 37.010   1.00 191.89 ? 156  ARG G CG  1 
ATOM   19041 C  CD  . ARG G  3 158 ? 29.778  -63.488 38.229   1.00 195.65 ? 156  ARG G CD  1 
ATOM   19042 N  NE  . ARG G  3 158 ? 28.963  -62.297 38.000   1.00 196.81 ? 156  ARG G NE  1 
ATOM   19043 C  CZ  . ARG G  3 158 ? 28.735  -61.359 38.913   1.00 192.38 ? 156  ARG G CZ  1 
ATOM   19044 N  NH1 . ARG G  3 158 ? 29.263  -61.473 40.123   1.00 189.01 ? 156  ARG G NH1 1 
ATOM   19045 N  NH2 . ARG G  3 158 ? 27.981  -60.308 38.616   1.00 184.74 ? 156  ARG G NH2 1 
ATOM   19046 N  N   . LEU G  3 159 ? 29.968  -66.721 34.413   1.00 197.31 ? 157  LEU G N   1 
ATOM   19047 C  CA  . LEU G  3 159 ? 30.684  -67.985 34.346   1.00 199.91 ? 157  LEU G CA  1 
ATOM   19048 C  C   . LEU G  3 159 ? 31.596  -68.119 35.560   1.00 199.51 ? 157  LEU G C   1 
ATOM   19049 O  O   . LEU G  3 159 ? 32.059  -67.123 36.126   1.00 197.52 ? 157  LEU G O   1 
ATOM   19050 C  CB  . LEU G  3 159 ? 31.500  -68.087 33.053   1.00 210.68 ? 157  LEU G CB  1 
ATOM   19051 C  CG  . LEU G  3 159 ? 30.783  -68.178 31.696   1.00 204.47 ? 157  LEU G CG  1 
ATOM   19052 C  CD1 . LEU G  3 159 ? 30.278  -66.823 31.204   1.00 200.15 ? 157  LEU G CD1 1 
ATOM   19053 C  CD2 . LEU G  3 159 ? 31.697  -68.812 30.659   1.00 206.76 ? 157  LEU G CD2 1 
ATOM   19054 N  N   . LEU G  3 160 ? 31.851  -69.362 35.961   1.00 196.55 ? 158  LEU G N   1 
ATOM   19055 C  CA  . LEU G  3 160 ? 32.588  -69.655 37.184   1.00 201.13 ? 158  LEU G CA  1 
ATOM   19056 C  C   . LEU G  3 160 ? 33.868  -70.423 36.870   1.00 217.50 ? 158  LEU G C   1 
ATOM   19057 O  O   . LEU G  3 160 ? 33.900  -71.246 35.948   1.00 224.07 ? 158  LEU G O   1 
ATOM   19058 C  CB  . LEU G  3 160 ? 31.719  -70.451 38.165   1.00 197.81 ? 158  LEU G CB  1 
ATOM   19059 C  CG  . LEU G  3 160 ? 30.714  -69.671 39.023   1.00 195.99 ? 158  LEU G CG  1 
ATOM   19060 C  CD1 . LEU G  3 160 ? 29.567  -69.087 38.206   1.00 195.20 ? 158  LEU G CD1 1 
ATOM   19061 C  CD2 . LEU G  3 160 ? 30.182  -70.556 40.135   1.00 198.00 ? 158  LEU G CD2 1 
ATOM   19062 N  N   . ALA G  3 161 ? 34.928  -70.158 37.663   1.00 210.33 ? 159  ALA G N   1 
ATOM   19063 C  CA  . ALA G  3 161 ? 36.270  -70.695 37.476   1.00 203.73 ? 159  ALA G CA  1 
ATOM   19064 C  C   . ALA G  3 161 ? 36.659  -71.645 38.611   1.00 206.68 ? 159  ALA G C   1 
ATOM   19065 O  O   . ALA G  3 161 ? 36.330  -71.399 39.776   1.00 210.05 ? 159  ALA G O   1 
ATOM   19066 C  CB  . ALA G  3 161 ? 37.299  -69.561 37.396   1.00 202.07 ? 159  ALA G CB  1 
ATOM   19067 N  N   . PRO G  3 162 ? 37.378  -72.738 38.301   1.00 214.99 ? 160  PRO G N   1 
ATOM   19068 C  CA  . PRO G  3 162 ? 37.750  -73.710 39.341   1.00 218.99 ? 160  PRO G CA  1 
ATOM   19069 C  C   . PRO G  3 162 ? 38.801  -73.194 40.310   1.00 219.64 ? 160  PRO G C   1 
ATOM   19070 O  O   . PRO G  3 162 ? 40.000  -73.413 40.109   1.00 229.28 ? 160  PRO G O   1 
ATOM   19071 C  CB  . PRO G  3 162 ? 38.287  -74.898 38.530   1.00 230.60 ? 160  PRO G CB  1 
ATOM   19072 C  CG  . PRO G  3 162 ? 38.749  -74.301 37.245   1.00 229.38 ? 160  PRO G CG  1 
ATOM   19073 C  CD  . PRO G  3 162 ? 37.812  -73.162 36.959   1.00 223.27 ? 160  PRO G CD  1 
ATOM   19074 N  N   . SER G  3 163 ? 38.369  -72.518 41.369   1.00 212.70 ? 161  SER G N   1 
ATOM   19075 C  CA  . SER G  3 163 ? 39.285  -72.035 42.391   1.00 214.29 ? 161  SER G CA  1 
ATOM   19076 C  C   . SER G  3 163 ? 39.419  -73.076 43.493   1.00 217.55 ? 161  SER G C   1 
ATOM   19077 O  O   . SER G  3 163 ? 38.416  -73.589 43.997   1.00 216.82 ? 161  SER G O   1 
ATOM   19078 C  CB  . SER G  3 163 ? 38.803  -70.707 42.971   1.00 212.89 ? 161  SER G CB  1 
ATOM   19079 O  OG  . SER G  3 163 ? 39.580  -70.340 44.098   1.00 214.77 ? 161  SER G OG  1 
ATOM   19080 N  N   . ASP G  3 164 ? 40.666  -73.373 43.869   1.00 241.82 ? 162  ASP G N   1 
ATOM   19081 C  CA  . ASP G  3 164 ? 40.944  -74.427 44.840   1.00 254.89 ? 162  ASP G CA  1 
ATOM   19082 C  C   . ASP G  3 164 ? 40.400  -74.110 46.228   1.00 249.04 ? 162  ASP G C   1 
ATOM   19083 O  O   . ASP G  3 164 ? 40.231  -75.030 47.037   1.00 254.09 ? 162  ASP G O   1 
ATOM   19084 C  CB  . ASP G  3 164 ? 42.452  -74.675 44.932   1.00 266.37 ? 162  ASP G CB  1 
ATOM   19085 C  CG  . ASP G  3 164 ? 43.078  -74.991 43.588   1.00 265.06 ? 162  ASP G CG  1 
ATOM   19086 O  OD1 . ASP G  3 164 ? 42.841  -76.103 43.070   1.00 272.55 ? 162  ASP G OD1 1 
ATOM   19087 O  OD2 . ASP G  3 164 ? 43.819  -74.135 43.056   1.00 256.11 ? 162  ASP G OD2 1 
ATOM   19088 N  N   . SER G  3 165 ? 40.138  -72.847 46.525   1.00 234.56 ? 163  SER G N   1 
ATOM   19089 C  CA  . SER G  3 165 ? 39.662  -72.423 47.828   1.00 241.92 ? 163  SER G CA  1 
ATOM   19090 C  C   . SER G  3 165 ? 38.212  -71.966 47.743   1.00 239.81 ? 163  SER G C   1 
ATOM   19091 O  O   . SER G  3 165 ? 37.714  -71.646 46.659   1.00 227.75 ? 163  SER G O   1 
ATOM   19092 C  CB  . SER G  3 165 ? 40.539  -71.285 48.377   1.00 241.55 ? 163  SER G CB  1 
ATOM   19093 O  OG  . SER G  3 165 ? 40.491  -70.141 47.543   1.00 236.79 ? 163  SER G OG  1 
ATOM   19094 N  N   . PRO G  3 166 ? 37.490  -71.951 48.866   1.00 248.54 ? 164  PRO G N   1 
ATOM   19095 C  CA  . PRO G  3 166 ? 36.121  -71.417 48.849   1.00 238.83 ? 164  PRO G CA  1 
ATOM   19096 C  C   . PRO G  3 166 ? 36.125  -69.950 48.452   1.00 230.51 ? 164  PRO G C   1 
ATOM   19097 O  O   . PRO G  3 166 ? 36.831  -69.131 49.044   1.00 231.21 ? 164  PRO G O   1 
ATOM   19098 C  CB  . PRO G  3 166 ? 35.644  -71.614 50.294   1.00 240.93 ? 164  PRO G CB  1 
ATOM   19099 C  CG  . PRO G  3 166 ? 36.899  -71.723 51.101   1.00 246.24 ? 164  PRO G CG  1 
ATOM   19100 C  CD  . PRO G  3 166 ? 37.863  -72.440 50.205   1.00 256.20 ? 164  PRO G CD  1 
ATOM   19101 N  N   . GLU G  3 167 ? 35.337  -69.621 47.435   1.00 221.44 ? 165  GLU G N   1 
ATOM   19102 C  CA  . GLU G  3 167 ? 35.306  -68.270 46.901   1.00 217.06 ? 165  GLU G CA  1 
ATOM   19103 C  C   . GLU G  3 167 ? 33.957  -67.619 47.165   1.00 217.47 ? 165  GLU G C   1 
ATOM   19104 O  O   . GLU G  3 167 ? 32.927  -68.290 47.264   1.00 228.52 ? 165  GLU G O   1 
ATOM   19105 C  CB  . GLU G  3 167 ? 35.606  -68.260 45.403   1.00 214.90 ? 165  GLU G CB  1 
ATOM   19106 C  CG  . GLU G  3 167 ? 37.009  -68.721 45.079   1.00 222.60 ? 165  GLU G CG  1 
ATOM   19107 C  CD  . GLU G  3 167 ? 38.080  -67.743 45.526   1.00 221.22 ? 165  GLU G CD  1 
ATOM   19108 O  OE1 . GLU G  3 167 ? 38.647  -67.046 44.660   1.00 215.83 ? 165  GLU G OE1 1 
ATOM   19109 O  OE2 . GLU G  3 167 ? 38.358  -67.670 46.742   1.00 230.43 ? 165  GLU G OE2 1 
ATOM   19110 N  N   . TRP G  3 168 ? 33.983  -66.297 47.282   1.00 210.99 ? 166  TRP G N   1 
ATOM   19111 C  CA  . TRP G  3 168 ? 32.804  -65.503 47.594   1.00 215.84 ? 166  TRP G CA  1 
ATOM   19112 C  C   . TRP G  3 168 ? 32.491  -64.629 46.386   1.00 217.60 ? 166  TRP G C   1 
ATOM   19113 O  O   . TRP G  3 168 ? 33.333  -63.832 45.961   1.00 219.95 ? 166  TRP G O   1 
ATOM   19114 C  CB  . TRP G  3 168 ? 33.047  -64.658 48.847   1.00 212.44 ? 166  TRP G CB  1 
ATOM   19115 C  CG  . TRP G  3 168 ? 31.823  -64.380 49.688   1.00 206.25 ? 166  TRP G CG  1 
ATOM   19116 C  CD1 . TRP G  3 168 ? 30.776  -63.567 49.367   1.00 205.12 ? 166  TRP G CD1 1 
ATOM   19117 C  CD2 . TRP G  3 168 ? 31.544  -64.889 51.001   1.00 202.80 ? 166  TRP G CD2 1 
ATOM   19118 N  NE1 . TRP G  3 168 ? 29.856  -63.550 50.389   1.00 202.88 ? 166  TRP G NE1 1 
ATOM   19119 C  CE2 . TRP G  3 168 ? 30.305  -64.353 51.404   1.00 199.73 ? 166  TRP G CE2 1 
ATOM   19120 C  CE3 . TRP G  3 168 ? 32.219  -65.750 51.870   1.00 215.07 ? 166  TRP G CE3 1 
ATOM   19121 C  CZ2 . TRP G  3 168 ? 29.728  -64.650 52.636   1.00 200.06 ? 166  TRP G CZ2 1 
ATOM   19122 C  CZ3 . TRP G  3 168 ? 31.643  -66.045 53.093   1.00 224.84 ? 166  TRP G CZ3 1 
ATOM   19123 C  CH2 . TRP G  3 168 ? 30.410  -65.496 53.464   1.00 214.30 ? 166  TRP G CH2 1 
ATOM   19124 N  N   . LEU G  3 169 ? 31.295  -64.794 45.825   1.00 222.91 ? 167  LEU G N   1 
ATOM   19125 C  CA  . LEU G  3 169 ? 30.844  -64.032 44.668   1.00 218.65 ? 167  LEU G CA  1 
ATOM   19126 C  C   . LEU G  3 169 ? 29.749  -63.053 45.080   1.00 214.90 ? 167  LEU G C   1 
ATOM   19127 O  O   . LEU G  3 169 ? 29.329  -63.000 46.238   1.00 219.73 ? 167  LEU G O   1 
ATOM   19128 C  CB  . LEU G  3 169 ? 30.349  -64.962 43.560   1.00 226.59 ? 167  LEU G CB  1 
ATOM   19129 C  CG  . LEU G  3 169 ? 31.366  -65.363 42.490   1.00 237.95 ? 167  LEU G CG  1 
ATOM   19130 C  CD1 . LEU G  3 169 ? 32.452  -66.250 43.083   1.00 246.78 ? 167  LEU G CD1 1 
ATOM   19131 C  CD2 . LEU G  3 169 ? 30.677  -66.046 41.314   1.00 243.04 ? 167  LEU G CD2 1 
ATOM   19132 N  N   . SER G  3 170 ? 29.278  -62.276 44.105   1.00 216.77 ? 168  SER G N   1 
ATOM   19133 C  CA  . SER G  3 170 ? 28.266  -61.264 44.372   1.00 221.12 ? 168  SER G CA  1 
ATOM   19134 C  C   . SER G  3 170 ? 27.567  -60.889 43.072   1.00 215.05 ? 168  SER G C   1 
ATOM   19135 O  O   . SER G  3 170 ? 28.206  -60.797 42.020   1.00 221.44 ? 168  SER G O   1 
ATOM   19136 C  CB  . SER G  3 170 ? 28.884  -60.020 45.022   1.00 220.01 ? 168  SER G CB  1 
ATOM   19137 O  OG  . SER G  3 170 ? 29.857  -59.432 44.178   1.00 232.36 ? 168  SER G OG  1 
ATOM   19138 N  N   . PHE G  3 171 ? 26.256  -60.668 43.157   1.00 192.61 ? 169  PHE G N   1 
ATOM   19139 C  CA  . PHE G  3 171 ? 25.444  -60.282 42.009   1.00 181.23 ? 169  PHE G CA  1 
ATOM   19140 C  C   . PHE G  3 171 ? 24.695  -59.000 42.336   1.00 176.57 ? 169  PHE G C   1 
ATOM   19141 O  O   . PHE G  3 171 ? 23.913  -58.958 43.291   1.00 189.15 ? 169  PHE G O   1 
ATOM   19142 C  CB  . PHE G  3 171 ? 24.469  -61.393 41.621   1.00 184.88 ? 169  PHE G CB  1 
ATOM   19143 C  CG  . PHE G  3 171 ? 25.110  -62.518 40.868   1.00 191.49 ? 169  PHE G CG  1 
ATOM   19144 C  CD1 . PHE G  3 171 ? 25.232  -62.464 39.490   1.00 194.68 ? 169  PHE G CD1 1 
ATOM   19145 C  CD2 . PHE G  3 171 ? 25.599  -63.627 41.537   1.00 193.64 ? 169  PHE G CD2 1 
ATOM   19146 C  CE1 . PHE G  3 171 ? 25.824  -63.498 38.793   1.00 194.65 ? 169  PHE G CE1 1 
ATOM   19147 C  CE2 . PHE G  3 171 ? 26.192  -64.664 40.846   1.00 195.25 ? 169  PHE G CE2 1 
ATOM   19148 C  CZ  . PHE G  3 171 ? 26.305  -64.600 39.472   1.00 196.29 ? 169  PHE G CZ  1 
ATOM   19149 N  N   . ASP G  3 172 ? 24.927  -57.968 41.536   1.00 187.89 ? 170  ASP G N   1 
ATOM   19150 C  CA  . ASP G  3 172 ? 24.337  -56.651 41.755   1.00 183.56 ? 170  ASP G CA  1 
ATOM   19151 C  C   . ASP G  3 172 ? 22.855  -56.700 41.398   1.00 186.64 ? 170  ASP G C   1 
ATOM   19152 O  O   . ASP G  3 172 ? 22.487  -56.676 40.222   1.00 200.96 ? 170  ASP G O   1 
ATOM   19153 C  CB  . ASP G  3 172 ? 25.081  -55.618 40.916   1.00 194.32 ? 170  ASP G CB  1 
ATOM   19154 C  CG  . ASP G  3 172 ? 24.840  -54.195 41.382   1.00 204.51 ? 170  ASP G CG  1 
ATOM   19155 O  OD1 . ASP G  3 172 ? 23.745  -53.911 41.913   1.00 209.84 ? 170  ASP G OD1 1 
ATOM   19156 O  OD2 . ASP G  3 172 ? 25.752  -53.356 41.212   1.00 206.39 ? 170  ASP G OD2 1 
ATOM   19157 N  N   . VAL G  3 173 ? 21.992  -56.765 42.413   1.00 194.58 ? 171  VAL G N   1 
ATOM   19158 C  CA  . VAL G  3 173 ? 20.548  -56.783 42.192   1.00 201.61 ? 171  VAL G CA  1 
ATOM   19159 C  C   . VAL G  3 173 ? 19.922  -55.512 42.750   1.00 199.81 ? 171  VAL G C   1 
ATOM   19160 O  O   . VAL G  3 173 ? 18.808  -55.539 43.285   1.00 194.28 ? 171  VAL G O   1 
ATOM   19161 C  CB  . VAL G  3 173 ? 19.898  -58.028 42.821   1.00 220.67 ? 171  VAL G CB  1 
ATOM   19162 C  CG1 . VAL G  3 173 ? 20.268  -59.277 42.038   1.00 235.23 ? 171  VAL G CG1 1 
ATOM   19163 C  CG2 . VAL G  3 173 ? 20.309  -58.161 44.280   1.00 220.29 ? 171  VAL G CG2 1 
ATOM   19164 N  N   . THR G  3 174 ? 20.631  -54.389 42.619   1.00 211.21 ? 172  THR G N   1 
ATOM   19165 C  CA  . THR G  3 174 ? 20.140  -53.128 43.166   1.00 212.50 ? 172  THR G CA  1 
ATOM   19166 C  C   . THR G  3 174 ? 18.818  -52.726 42.523   1.00 204.88 ? 172  THR G C   1 
ATOM   19167 O  O   . THR G  3 174 ? 17.870  -52.339 43.217   1.00 202.09 ? 172  THR G O   1 
ATOM   19168 C  CB  . THR G  3 174 ? 21.188  -52.035 42.975   1.00 221.87 ? 172  THR G CB  1 
ATOM   19169 O  OG1 . THR G  3 174 ? 22.375  -52.381 43.700   1.00 236.89 ? 172  THR G OG1 1 
ATOM   19170 C  CG2 . THR G  3 174 ? 20.665  -50.698 43.479   1.00 218.51 ? 172  THR G CG2 1 
ATOM   19171 N  N   . GLY G  3 175 ? 18.736  -52.817 41.192   1.00 206.90 ? 173  GLY G N   1 
ATOM   19172 C  CA  . GLY G  3 175 ? 17.501  -52.474 40.506   1.00 213.22 ? 173  GLY G CA  1 
ATOM   19173 C  C   . GLY G  3 175 ? 16.326  -53.333 40.929   1.00 219.03 ? 173  GLY G C   1 
ATOM   19174 O  O   . GLY G  3 175 ? 15.173  -52.897 40.849   1.00 228.82 ? 173  GLY G O   1 
ATOM   19175 N  N   . VAL G  3 176 ? 16.595  -54.555 41.392   1.00 212.77 ? 174  VAL G N   1 
ATOM   19176 C  CA  . VAL G  3 176 ? 15.527  -55.432 41.860   1.00 222.53 ? 174  VAL G CA  1 
ATOM   19177 C  C   . VAL G  3 176 ? 15.088  -55.040 43.264   1.00 222.89 ? 174  VAL G C   1 
ATOM   19178 O  O   . VAL G  3 176 ? 13.889  -54.946 43.553   1.00 226.94 ? 174  VAL G O   1 
ATOM   19179 C  CB  . VAL G  3 176 ? 15.980  -56.902 41.804   1.00 219.81 ? 174  VAL G CB  1 
ATOM   19180 C  CG1 . VAL G  3 176 ? 14.900  -57.808 42.373   1.00 220.38 ? 174  VAL G CG1 1 
ATOM   19181 C  CG2 . VAL G  3 176 ? 16.319  -57.301 40.379   1.00 216.84 ? 174  VAL G CG2 1 
ATOM   19182 N  N   . VAL G  3 177 ? 16.053  -54.807 44.155   1.00 209.53 ? 175  VAL G N   1 
ATOM   19183 C  CA  . VAL G  3 177 ? 15.730  -54.485 45.541   1.00 198.02 ? 175  VAL G CA  1 
ATOM   19184 C  C   . VAL G  3 177 ? 14.998  -53.151 45.628   1.00 199.11 ? 175  VAL G C   1 
ATOM   19185 O  O   . VAL G  3 177 ? 14.109  -52.972 46.468   1.00 200.55 ? 175  VAL G O   1 
ATOM   19186 C  CB  . VAL G  3 177 ? 17.010  -54.493 46.395   1.00 195.61 ? 175  VAL G CB  1 
ATOM   19187 C  CG1 . VAL G  3 177 ? 16.687  -54.163 47.836   1.00 196.32 ? 175  VAL G CG1 1 
ATOM   19188 C  CG2 . VAL G  3 177 ? 17.699  -55.844 46.303   1.00 196.86 ? 175  VAL G CG2 1 
ATOM   19189 N  N   . ARG G  3 178 ? 15.348  -52.201 44.754   1.00 204.46 ? 176  ARG G N   1 
ATOM   19190 C  CA  . ARG G  3 178 ? 14.725  -50.880 44.803   1.00 209.61 ? 176  ARG G CA  1 
ATOM   19191 C  C   . ARG G  3 178 ? 13.228  -50.957 44.532   1.00 224.31 ? 176  ARG G C   1 
ATOM   19192 O  O   . ARG G  3 178 ? 12.436  -50.256 45.174   1.00 238.41 ? 176  ARG G O   1 
ATOM   19193 C  CB  . ARG G  3 178 ? 15.395  -49.944 43.798   1.00 202.75 ? 176  ARG G CB  1 
ATOM   19194 C  CG  . ARG G  3 178 ? 14.694  -48.602 43.642   1.00 208.08 ? 176  ARG G CG  1 
ATOM   19195 C  CD  . ARG G  3 178 ? 15.496  -47.646 42.776   1.00 215.25 ? 176  ARG G CD  1 
ATOM   19196 N  NE  . ARG G  3 178 ? 16.686  -47.148 43.464   1.00 225.17 ? 176  ARG G NE  1 
ATOM   19197 C  CZ  . ARG G  3 178 ? 17.919  -47.605 43.264   1.00 230.12 ? 176  ARG G CZ  1 
ATOM   19198 N  NH1 . ARG G  3 178 ? 18.139  -48.578 42.388   1.00 230.70 ? 176  ARG G NH1 1 
ATOM   19199 N  NH2 . ARG G  3 178 ? 18.936  -47.084 43.940   1.00 222.01 ? 176  ARG G NH2 1 
ATOM   19200 N  N   . GLN G  3 179 ? 12.818  -51.801 43.582   1.00 225.70 ? 177  GLN G N   1 
ATOM   19201 C  CA  . GLN G  3 179 ? 11.397  -51.919 43.273   1.00 224.26 ? 177  GLN G CA  1 
ATOM   19202 C  C   . GLN G  3 179 ? 10.646  -52.687 44.351   1.00 228.04 ? 177  GLN G C   1 
ATOM   19203 O  O   . GLN G  3 179 ? 9.440   -52.486 44.523   1.00 233.20 ? 177  GLN G O   1 
ATOM   19204 C  CB  . GLN G  3 179 ? 11.207  -52.598 41.920   1.00 223.73 ? 177  GLN G CB  1 
ATOM   19205 C  CG  . GLN G  3 179 ? 11.874  -51.875 40.771   1.00 237.10 ? 177  GLN G CG  1 
ATOM   19206 C  CD  . GLN G  3 179 ? 11.757  -52.637 39.472   1.00 250.10 ? 177  GLN G CD  1 
ATOM   19207 O  OE1 . GLN G  3 179 ? 11.123  -53.691 39.413   1.00 250.56 ? 177  GLN G OE1 1 
ATOM   19208 N  NE2 . GLN G  3 179 ? 12.373  -52.110 38.419   1.00 253.67 ? 177  GLN G NE2 1 
ATOM   19209 N  N   . TRP G  3 180 ? 11.333  -53.565 45.082   1.00 225.80 ? 178  TRP G N   1 
ATOM   19210 C  CA  . TRP G  3 180 ? 10.674  -54.372 46.100   1.00 224.84 ? 178  TRP G CA  1 
ATOM   19211 C  C   . TRP G  3 180 ? 10.361  -53.588 47.365   1.00 218.89 ? 178  TRP G C   1 
ATOM   19212 O  O   . TRP G  3 180 ? 9.437   -53.963 48.096   1.00 220.27 ? 178  TRP G O   1 
ATOM   19213 C  CB  . TRP G  3 180 ? 11.539  -55.583 46.446   1.00 225.70 ? 178  TRP G CB  1 
ATOM   19214 C  CG  . TRP G  3 180 ? 11.522  -56.647 45.396   1.00 228.48 ? 178  TRP G CG  1 
ATOM   19215 C  CD1 . TRP G  3 180 ? 10.865  -56.611 44.199   1.00 233.86 ? 178  TRP G CD1 1 
ATOM   19216 C  CD2 . TRP G  3 180 ? 12.183  -57.914 45.452   1.00 226.82 ? 178  TRP G CD2 1 
ATOM   19217 N  NE1 . TRP G  3 180 ? 11.081  -57.779 43.506   1.00 228.72 ? 178  TRP G NE1 1 
ATOM   19218 C  CE2 . TRP G  3 180 ? 11.887  -58.595 44.254   1.00 229.79 ? 178  TRP G CE2 1 
ATOM   19219 C  CE3 . TRP G  3 180 ? 12.999  -58.541 46.399   1.00 227.52 ? 178  TRP G CE3 1 
ATOM   19220 C  CZ2 . TRP G  3 180 ? 12.377  -59.870 43.980   1.00 232.38 ? 178  TRP G CZ2 1 
ATOM   19221 C  CZ3 . TRP G  3 180 ? 13.484  -59.805 46.124   1.00 228.95 ? 178  TRP G CZ3 1 
ATOM   19222 C  CH2 . TRP G  3 180 ? 13.172  -60.456 44.925   1.00 231.38 ? 178  TRP G CH2 1 
ATOM   19223 N  N   . LEU G  3 181 ? 11.109  -52.520 47.644   1.00 209.31 ? 179  LEU G N   1 
ATOM   19224 C  CA  . LEU G  3 181 ? 10.817  -51.682 48.798   1.00 208.25 ? 179  LEU G CA  1 
ATOM   19225 C  C   . LEU G  3 181 ? 9.639   -50.755 48.555   1.00 210.81 ? 179  LEU G C   1 
ATOM   19226 O  O   . LEU G  3 181 ? 9.056   -50.248 49.520   1.00 227.47 ? 179  LEU G O   1 
ATOM   19227 C  CB  . LEU G  3 181 ? 12.050  -50.862 49.186   1.00 208.19 ? 179  LEU G CB  1 
ATOM   19228 C  CG  . LEU G  3 181 ? 13.039  -51.479 50.180   1.00 217.82 ? 179  LEU G CG  1 
ATOM   19229 C  CD1 . LEU G  3 181 ? 13.469  -52.875 49.756   1.00 222.81 ? 179  LEU G CD1 1 
ATOM   19230 C  CD2 . LEU G  3 181 ? 14.253  -50.577 50.339   1.00 211.90 ? 179  LEU G CD2 1 
ATOM   19231 N  N   . SER G  3 182 ? 9.278   -50.520 47.291   1.00 207.81 ? 180  SER G N   1 
ATOM   19232 C  CA  . SER G  3 182 ? 8.092   -49.736 46.976   1.00 221.55 ? 180  SER G CA  1 
ATOM   19233 C  C   . SER G  3 182 ? 6.817   -50.567 47.025   1.00 238.80 ? 180  SER G C   1 
ATOM   19234 O  O   . SER G  3 182 ? 5.727   -50.000 47.167   1.00 257.86 ? 180  SER G O   1 
ATOM   19235 C  CB  . SER G  3 182 ? 8.237   -49.088 45.596   1.00 212.00 ? 180  SER G CB  1 
ATOM   19236 O  OG  . SER G  3 182 ? 8.333   -50.065 44.575   1.00 213.02 ? 180  SER G OG  1 
ATOM   19237 N  N   . ARG G  3 183 ? 6.927   -51.889 46.932   1.00 233.15 ? 181  ARG G N   1 
ATOM   19238 C  CA  . ARG G  3 183 ? 5.769   -52.769 46.958   1.00 230.56 ? 181  ARG G CA  1 
ATOM   19239 C  C   . ARG G  3 183 ? 5.489   -53.254 48.377   1.00 229.75 ? 181  ARG G C   1 
ATOM   19240 O  O   . ARG G  3 183 ? 6.400   -53.430 49.191   1.00 220.18 ? 181  ARG G O   1 
ATOM   19241 C  CB  . ARG G  3 183 ? 5.982   -53.971 46.038   1.00 228.41 ? 181  ARG G CB  1 
ATOM   19242 C  CG  . ARG G  3 183 ? 6.462   -53.600 44.647   1.00 240.54 ? 181  ARG G CG  1 
ATOM   19243 C  CD  . ARG G  3 183 ? 6.814   -54.832 43.829   1.00 253.96 ? 181  ARG G CD  1 
ATOM   19244 N  NE  . ARG G  3 183 ? 7.570   -54.496 42.623   1.00 239.46 ? 181  ARG G NE  1 
ATOM   19245 C  CZ  . ARG G  3 183 ? 7.018   -54.178 41.456   1.00 234.51 ? 181  ARG G CZ  1 
ATOM   19246 N  NH1 . ARG G  3 183 ? 5.698   -54.147 41.330   1.00 252.64 ? 181  ARG G NH1 1 
ATOM   19247 N  NH2 . ARG G  3 183 ? 7.786   -53.891 40.414   1.00 226.65 ? 181  ARG G NH2 1 
ATOM   19248 N  N   . GLY G  3 184 ? 4.209   -53.465 48.666   1.00 249.61 ? 182  GLY G N   1 
ATOM   19249 C  CA  . GLY G  3 184 ? 3.775   -54.020 49.929   1.00 263.54 ? 182  GLY G CA  1 
ATOM   19250 C  C   . GLY G  3 184 ? 3.793   -55.530 49.986   1.00 267.36 ? 182  GLY G C   1 
ATOM   19251 O  O   . GLY G  3 184 ? 3.294   -56.112 50.956   1.00 263.63 ? 182  GLY G O   1 
ATOM   19252 N  N   . GLY G  3 185 ? 4.344   -56.183 48.966   1.00 263.18 ? 183  GLY G N   1 
ATOM   19253 C  CA  . GLY G  3 185 ? 4.445   -57.627 48.952   1.00 261.36 ? 183  GLY G CA  1 
ATOM   19254 C  C   . GLY G  3 185 ? 5.400   -58.125 50.013   1.00 251.44 ? 183  GLY G C   1 
ATOM   19255 O  O   . GLY G  3 185 ? 6.616   -57.959 49.888   1.00 250.05 ? 183  GLY G O   1 
ATOM   19256 N  N   . GLU G  3 186 ? 4.862   -58.732 51.068   1.00 243.94 ? 184  GLU G N   1 
ATOM   19257 C  CA  . GLU G  3 186 ? 5.673   -59.171 52.194   1.00 240.22 ? 184  GLU G CA  1 
ATOM   19258 C  C   . GLU G  3 186 ? 6.399   -60.490 51.936   1.00 241.53 ? 184  GLU G C   1 
ATOM   19259 O  O   . GLU G  3 186 ? 6.987   -61.044 52.873   1.00 248.58 ? 184  GLU G O   1 
ATOM   19260 C  CB  . GLU G  3 186 ? 4.807   -59.290 53.455   1.00 247.92 ? 184  GLU G CB  1 
ATOM   19261 C  CG  . GLU G  3 186 ? 4.211   -57.967 53.942   1.00 235.59 ? 184  GLU G CG  1 
ATOM   19262 C  CD  . GLU G  3 186 ? 3.632   -58.060 55.349   1.00 232.43 ? 184  GLU G CD  1 
ATOM   19263 O  OE1 . GLU G  3 186 ? 3.863   -59.084 56.028   1.00 233.22 ? 184  GLU G OE1 1 
ATOM   19264 O  OE2 . GLU G  3 186 ? 2.948   -57.106 55.778   1.00 232.91 ? 184  GLU G OE2 1 
ATOM   19265 N  N   . ILE G  3 187 ? 6.379   -61.008 50.707   1.00 233.69 ? 185  ILE G N   1 
ATOM   19266 C  CA  . ILE G  3 187 ? 7.102   -62.232 50.369   1.00 229.69 ? 185  ILE G CA  1 
ATOM   19267 C  C   . ILE G  3 187 ? 7.663   -62.092 48.958   1.00 241.91 ? 185  ILE G C   1 
ATOM   19268 O  O   . ILE G  3 187 ? 6.910   -61.855 48.005   1.00 238.80 ? 185  ILE G O   1 
ATOM   19269 C  CB  . ILE G  3 187 ? 6.217   -63.488 50.484   1.00 222.33 ? 185  ILE G CB  1 
ATOM   19270 C  CG1 . ILE G  3 187 ? 6.974   -64.721 49.986   1.00 222.97 ? 185  ILE G CG1 1 
ATOM   19271 C  CG2 . ILE G  3 187 ? 4.898   -63.308 49.740   1.00 225.24 ? 185  ILE G CG2 1 
ATOM   19272 C  CD1 . ILE G  3 187 ? 8.207   -65.047 50.799   1.00 220.60 ? 185  ILE G CD1 1 
ATOM   19273 N  N   . GLU G  3 188 ? 8.983   -62.222 48.827   1.00 255.57 ? 186  GLU G N   1 
ATOM   19274 C  CA  . GLU G  3 188 ? 9.685   -62.153 47.544   1.00 258.85 ? 186  GLU G CA  1 
ATOM   19275 C  C   . GLU G  3 188 ? 10.799  -63.199 47.557   1.00 263.52 ? 186  GLU G C   1 
ATOM   19276 O  O   . GLU G  3 188 ? 10.912  -63.993 48.495   1.00 276.85 ? 186  GLU G O   1 
ATOM   19277 C  CB  . GLU G  3 188 ? 10.233  -60.741 47.290   1.00 251.04 ? 186  GLU G CB  1 
ATOM   19278 C  CG  . GLU G  3 188 ? 9.174   -59.656 47.148   1.00 249.91 ? 186  GLU G CG  1 
ATOM   19279 C  CD  . GLU G  3 188 ? 8.395   -59.750 45.847   1.00 251.30 ? 186  GLU G CD  1 
ATOM   19280 O  OE1 . GLU G  3 188 ? 8.797   -60.526 44.951   1.00 259.07 ? 186  GLU G OE1 1 
ATOM   19281 O  OE2 . GLU G  3 188 ? 7.378   -59.036 45.722   1.00 242.81 ? 186  GLU G OE2 1 
ATOM   19282 N  N   . GLY G  3 189 ? 11.632  -63.205 46.520   1.00 253.61 ? 187  GLY G N   1 
ATOM   19283 C  CA  . GLY G  3 189 ? 12.735  -64.146 46.473   1.00 257.60 ? 187  GLY G CA  1 
ATOM   19284 C  C   . GLY G  3 189 ? 13.425  -64.155 45.123   1.00 253.68 ? 187  GLY G C   1 
ATOM   19285 O  O   . GLY G  3 189 ? 13.052  -63.428 44.197   1.00 246.00 ? 187  GLY G O   1 
ATOM   19286 N  N   . PHE G  3 190 ? 14.451  -65.010 45.032   1.00 262.97 ? 188  PHE G N   1 
ATOM   19287 C  CA  . PHE G  3 190 ? 15.264  -65.187 43.832   1.00 248.34 ? 188  PHE G CA  1 
ATOM   19288 C  C   . PHE G  3 190 ? 15.345  -66.666 43.467   1.00 253.27 ? 188  PHE G C   1 
ATOM   19289 O  O   . PHE G  3 190 ? 14.892  -67.545 44.206   1.00 269.88 ? 188  PHE G O   1 
ATOM   19290 C  CB  . PHE G  3 190 ? 16.682  -64.631 44.019   1.00 237.59 ? 188  PHE G CB  1 
ATOM   19291 C  CG  . PHE G  3 190 ? 16.735  -63.148 44.228   1.00 239.20 ? 188  PHE G CG  1 
ATOM   19292 C  CD1 . PHE G  3 190 ? 16.838  -62.285 43.149   1.00 231.83 ? 188  PHE G CD1 1 
ATOM   19293 C  CD2 . PHE G  3 190 ? 16.693  -62.615 45.505   1.00 258.51 ? 188  PHE G CD2 1 
ATOM   19294 C  CE1 . PHE G  3 190 ? 16.892  -60.916 43.340   1.00 233.87 ? 188  PHE G CE1 1 
ATOM   19295 C  CE2 . PHE G  3 190 ? 16.747  -61.249 45.704   1.00 265.28 ? 188  PHE G CE2 1 
ATOM   19296 C  CZ  . PHE G  3 190 ? 16.847  -60.398 44.619   1.00 249.74 ? 188  PHE G CZ  1 
ATOM   19297 N  N   . ARG G  3 191 ? 15.951  -66.939 42.311   1.00 223.20 ? 189  ARG G N   1 
ATOM   19298 C  CA  . ARG G  3 191 ? 16.144  -68.307 41.848   1.00 220.45 ? 189  ARG G CA  1 
ATOM   19299 C  C   . ARG G  3 191 ? 17.475  -68.391 41.121   1.00 220.06 ? 189  ARG G C   1 
ATOM   19300 O  O   . ARG G  3 191 ? 17.808  -67.503 40.330   1.00 223.88 ? 189  ARG G O   1 
ATOM   19301 C  CB  . ARG G  3 191 ? 15.011  -68.749 40.917   1.00 226.74 ? 189  ARG G CB  1 
ATOM   19302 C  CG  . ARG G  3 191 ? 15.309  -70.029 40.148   1.00 226.35 ? 189  ARG G CG  1 
ATOM   19303 C  CD  . ARG G  3 191 ? 14.409  -70.176 38.929   1.00 226.31 ? 189  ARG G CD  1 
ATOM   19304 N  NE  . ARG G  3 191 ? 14.890  -71.219 38.027   1.00 222.55 ? 189  ARG G NE  1 
ATOM   19305 C  CZ  . ARG G  3 191 ? 14.364  -71.484 36.835   1.00 224.88 ? 189  ARG G CZ  1 
ATOM   19306 N  NH1 . ARG G  3 191 ? 13.331  -70.784 36.388   1.00 226.70 ? 189  ARG G NH1 1 
ATOM   19307 N  NH2 . ARG G  3 191 ? 14.875  -72.450 36.087   1.00 225.53 ? 189  ARG G NH2 1 
ATOM   19308 N  N   . LEU G  3 192 ? 18.228  -69.456 41.382   1.00 224.90 ? 190  LEU G N   1 
ATOM   19309 C  CA  . LEU G  3 192 ? 19.527  -69.662 40.748   1.00 227.25 ? 190  LEU G CA  1 
ATOM   19310 C  C   . LEU G  3 192 ? 19.564  -71.062 40.139   1.00 236.06 ? 190  LEU G C   1 
ATOM   19311 O  O   . LEU G  3 192 ? 19.823  -72.044 40.841   1.00 246.96 ? 190  LEU G O   1 
ATOM   19312 C  CB  . LEU G  3 192 ? 20.656  -69.461 41.751   1.00 221.34 ? 190  LEU G CB  1 
ATOM   19313 C  CG  . LEU G  3 192 ? 22.057  -69.324 41.159   1.00 218.57 ? 190  LEU G CG  1 
ATOM   19314 C  CD1 . LEU G  3 192 ? 22.860  -68.321 41.962   1.00 224.80 ? 190  LEU G CD1 1 
ATOM   19315 C  CD2 . LEU G  3 192 ? 22.761  -70.664 41.137   1.00 219.59 ? 190  LEU G CD2 1 
ATOM   19316 N  N   . SER G  3 193 ? 19.314  -71.152 38.838   1.00 227.63 ? 191  SER G N   1 
ATOM   19317 C  CA  . SER G  3 193 ? 19.431  -72.400 38.106   1.00 225.07 ? 191  SER G CA  1 
ATOM   19318 C  C   . SER G  3 193 ? 20.730  -72.383 37.297   1.00 211.81 ? 191  SER G C   1 
ATOM   19319 O  O   . SER G  3 193 ? 21.626  -71.572 37.555   1.00 209.23 ? 191  SER G O   1 
ATOM   19320 C  CB  . SER G  3 193 ? 18.186  -72.605 37.235   1.00 232.24 ? 191  SER G CB  1 
ATOM   19321 O  OG  . SER G  3 193 ? 18.037  -71.555 36.298   1.00 232.27 ? 191  SER G OG  1 
ATOM   19322 N  N   . ALA G  3 194 ? 20.843  -73.269 36.317   1.00 205.44 ? 192  ALA G N   1 
ATOM   19323 C  CA  . ALA G  3 194 ? 22.042  -73.363 35.498   1.00 203.87 ? 192  ALA G CA  1 
ATOM   19324 C  C   . ALA G  3 194 ? 21.699  -73.061 34.040   1.00 209.22 ? 192  ALA G C   1 
ATOM   19325 O  O   . ALA G  3 194 ? 20.619  -72.557 33.722   1.00 231.71 ? 192  ALA G O   1 
ATOM   19326 C  CB  . ALA G  3 194 ? 22.690  -74.738 35.649   1.00 204.42 ? 192  ALA G CB  1 
ATOM   19327 N  N   . HIS G  3 195 ? 22.635  -73.374 33.152   1.00 205.02 ? 193  HIS G N   1 
ATOM   19328 C  CA  . HIS G  3 195 ? 22.456  -73.087 31.738   1.00 204.34 ? 193  HIS G CA  1 
ATOM   19329 C  C   . HIS G  3 195 ? 21.392  -73.997 31.126   1.00 207.12 ? 193  HIS G C   1 
ATOM   19330 O  O   . HIS G  3 195 ? 21.246  -75.165 31.501   1.00 208.83 ? 193  HIS G O   1 
ATOM   19331 C  CB  . HIS G  3 195 ? 23.784  -73.249 31.001   1.00 209.42 ? 193  HIS G CB  1 
ATOM   19332 C  CG  . HIS G  3 195 ? 23.720  -72.915 29.543   1.00 220.20 ? 193  HIS G CG  1 
ATOM   19333 N  ND1 . HIS G  3 195 ? 23.260  -71.704 29.073   1.00 219.56 ? 193  HIS G ND1 1 
ATOM   19334 C  CD2 . HIS G  3 195 ? 24.070  -73.634 28.451   1.00 229.88 ? 193  HIS G CD2 1 
ATOM   19335 C  CE1 . HIS G  3 195 ? 23.324  -71.693 27.754   1.00 224.23 ? 193  HIS G CE1 1 
ATOM   19336 N  NE2 . HIS G  3 195 ? 23.812  -72.853 27.351   1.00 231.05 ? 193  HIS G NE2 1 
ATOM   19337 N  N   . CYS G  3 196 ? 20.634  -73.435 30.180   1.00 207.89 ? 194  CYS G N   1 
ATOM   19338 C  CA  . CYS G  3 196 ? 19.624  -74.159 29.410   1.00 214.25 ? 194  CYS G CA  1 
ATOM   19339 C  C   . CYS G  3 196 ? 20.028  -74.106 27.939   1.00 213.31 ? 194  CYS G C   1 
ATOM   19340 O  O   . CYS G  3 196 ? 20.039  -73.030 27.332   1.00 206.69 ? 194  CYS G O   1 
ATOM   19341 C  CB  . CYS G  3 196 ? 18.229  -73.561 29.608   1.00 219.39 ? 194  CYS G CB  1 
ATOM   19342 S  SG  . CYS G  3 196 ? 17.803  -72.875 31.241   1.00 238.19 ? 194  CYS G SG  1 
ATOM   19343 N  N   . SER G  3 197 ? 20.358  -75.263 27.362   1.00 229.20 ? 195  SER G N   1 
ATOM   19344 C  CA  . SER G  3 197 ? 20.812  -75.354 25.976   1.00 220.56 ? 195  SER G CA  1 
ATOM   19345 C  C   . SER G  3 197 ? 19.623  -75.710 25.086   1.00 239.50 ? 195  SER G C   1 
ATOM   19346 O  O   . SER G  3 197 ? 19.106  -76.831 25.146   1.00 254.28 ? 195  SER G O   1 
ATOM   19347 C  CB  . SER G  3 197 ? 21.927  -76.389 25.841   1.00 216.68 ? 195  SER G CB  1 
ATOM   19348 O  OG  . SER G  3 197 ? 21.476  -77.672 26.244   1.00 225.57 ? 195  SER G OG  1 
ATOM   19349 N  N   . CYS G  3 198 ? 19.185  -74.753 24.270   1.00 235.02 ? 196  CYS G N   1 
ATOM   19350 C  CA  . CYS G  3 198 ? 18.107  -74.995 23.310   1.00 237.04 ? 196  CYS G CA  1 
ATOM   19351 C  C   . CYS G  3 198 ? 18.461  -74.385 21.958   1.00 227.65 ? 196  CYS G C   1 
ATOM   19352 O  O   . CYS G  3 198 ? 19.516  -73.770 21.803   1.00 219.29 ? 196  CYS G O   1 
ATOM   19353 C  CB  . CYS G  3 198 ? 16.774  -74.422 23.808   1.00 239.98 ? 196  CYS G CB  1 
ATOM   19354 S  SG  . CYS G  3 198 ? 16.662  -72.617 23.731   1.00 233.97 ? 196  CYS G SG  1 
ATOM   19355 N  N   . ASP G  3 208 ? 17.940  -80.728 28.745   1.00 252.70 ? 206  ASP G N   1 
ATOM   19356 C  CA  . ASP G  3 208 ? 19.310  -80.842 29.229   1.00 255.45 ? 206  ASP G CA  1 
ATOM   19357 C  C   . ASP G  3 208 ? 19.520  -79.909 30.420   1.00 247.80 ? 206  ASP G C   1 
ATOM   19358 O  O   . ASP G  3 208 ? 19.572  -78.688 30.270   1.00 242.09 ? 206  ASP G O   1 
ATOM   19359 C  CB  . ASP G  3 208 ? 20.307  -80.524 28.110   1.00 262.05 ? 206  ASP G CB  1 
ATOM   19360 C  CG  . ASP G  3 208 ? 21.508  -81.464 28.103   1.00 268.31 ? 206  ASP G CG  1 
ATOM   19361 O  OD1 . ASP G  3 208 ? 21.854  -82.012 29.172   1.00 270.16 ? 206  ASP G OD1 1 
ATOM   19362 O  OD2 . ASP G  3 208 ? 22.111  -81.652 27.024   1.00 265.01 ? 206  ASP G OD2 1 
ATOM   19363 N  N   . ILE G  3 209 ? 19.633  -80.500 31.607   1.00 260.44 ? 207  ILE G N   1 
ATOM   19364 C  CA  . ILE G  3 209 ? 19.832  -79.769 32.853   1.00 261.36 ? 207  ILE G CA  1 
ATOM   19365 C  C   . ILE G  3 209 ? 21.237  -80.047 33.367   1.00 275.73 ? 207  ILE G C   1 
ATOM   19366 O  O   . ILE G  3 209 ? 21.713  -81.188 33.316   1.00 285.36 ? 207  ILE G O   1 
ATOM   19367 C  CB  . ILE G  3 209 ? 18.780  -80.160 33.908   1.00 262.73 ? 207  ILE G CB  1 
ATOM   19368 C  CG1 . ILE G  3 209 ? 17.931  -81.324 33.397   1.00 269.07 ? 207  ILE G CG1 1 
ATOM   19369 C  CG2 . ILE G  3 209 ? 17.911  -78.967 34.256   1.00 257.58 ? 207  ILE G CG2 1 
ATOM   19370 C  CD1 . ILE G  3 209 ? 17.248  -82.106 34.492   1.00 268.33 ? 207  ILE G CD1 1 
ATOM   19371 N  N   . ASN G  3 210 ? 21.895  -79.009 33.869   1.00 272.52 ? 208  ASN G N   1 
ATOM   19372 C  CA  . ASN G  3 210 ? 23.257  -79.135 34.379   1.00 275.38 ? 208  ASN G CA  1 
ATOM   19373 C  C   . ASN G  3 210 ? 23.379  -78.275 35.633   1.00 276.85 ? 208  ASN G C   1 
ATOM   19374 O  O   . ASN G  3 210 ? 22.380  -77.877 36.245   1.00 272.02 ? 208  ASN G O   1 
ATOM   19375 C  CB  . ASN G  3 210 ? 24.282  -78.739 33.304   1.00 262.28 ? 208  ASN G CB  1 
ATOM   19376 C  CG  . ASN G  3 210 ? 24.027  -79.417 31.971   1.00 253.24 ? 208  ASN G CG  1 
ATOM   19377 O  OD1 . ASN G  3 210 ? 24.234  -80.623 31.823   1.00 260.05 ? 208  ASN G OD1 1 
ATOM   19378 N  ND2 . ASN G  3 210 ? 23.588  -78.639 30.987   1.00 247.07 ? 208  ASN G ND2 1 
ATOM   19379 N  N   . GLY G  3 211 ? 24.620  -77.987 36.026   1.00 277.49 ? 209  GLY G N   1 
ATOM   19380 C  CA  . GLY G  3 211 ? 24.901  -77.086 37.125   1.00 265.33 ? 209  GLY G CA  1 
ATOM   19381 C  C   . GLY G  3 211 ? 25.026  -77.771 38.467   1.00 258.17 ? 209  GLY G C   1 
ATOM   19382 O  O   . GLY G  3 211 ? 26.130  -77.935 38.996   1.00 253.61 ? 209  GLY G O   1 
ATOM   19383 N  N   . PHE G  3 212 ? 23.895  -78.172 39.031   1.00 271.37 ? 210  PHE G N   1 
ATOM   19384 C  CA  . PHE G  3 212 ? 23.852  -78.815 40.341   1.00 283.84 ? 210  PHE G CA  1 
ATOM   19385 C  C   . PHE G  3 212 ? 23.682  -80.309 40.101   1.00 286.58 ? 210  PHE G C   1 
ATOM   19386 O  O   . PHE G  3 212 ? 22.569  -80.789 39.872   1.00 285.43 ? 210  PHE G O   1 
ATOM   19387 C  CB  . PHE G  3 212 ? 22.716  -78.259 41.194   1.00 295.02 ? 210  PHE G CB  1 
ATOM   19388 C  CG  . PHE G  3 212 ? 22.744  -76.767 41.366   1.00 294.45 ? 210  PHE G CG  1 
ATOM   19389 C  CD1 . PHE G  3 212 ? 22.386  -75.925 40.323   1.00 288.11 ? 210  PHE G CD1 1 
ATOM   19390 C  CD2 . PHE G  3 212 ? 23.092  -76.206 42.581   1.00 292.15 ? 210  PHE G CD2 1 
ATOM   19391 C  CE1 . PHE G  3 212 ? 22.404  -74.557 40.481   1.00 279.26 ? 210  PHE G CE1 1 
ATOM   19392 C  CE2 . PHE G  3 212 ? 23.114  -74.837 42.743   1.00 282.26 ? 210  PHE G CE2 1 
ATOM   19393 C  CZ  . PHE G  3 212 ? 22.766  -74.014 41.694   1.00 277.11 ? 210  PHE G CZ  1 
ATOM   19394 N  N   . THR G  3 213 ? 24.791  -81.047 40.148   1.00 301.08 ? 211  THR G N   1 
ATOM   19395 C  CA  . THR G  3 213 ? 24.753  -82.475 39.868   1.00 311.26 ? 211  THR G CA  1 
ATOM   19396 C  C   . THR G  3 213 ? 24.375  -83.306 41.085   1.00 320.45 ? 211  THR G C   1 
ATOM   19397 O  O   . THR G  3 213 ? 24.169  -84.517 40.948   1.00 322.31 ? 211  THR G O   1 
ATOM   19398 C  CB  . THR G  3 213 ? 26.106  -82.941 39.325   1.00 304.52 ? 211  THR G CB  1 
ATOM   19399 O  OG1 . THR G  3 213 ? 27.114  -82.757 40.326   1.00 302.29 ? 211  THR G OG1 1 
ATOM   19400 C  CG2 . THR G  3 213 ? 26.474  -82.140 38.088   1.00 290.47 ? 211  THR G CG2 1 
ATOM   19401 N  N   . THR G  3 214 ? 24.272  -82.695 42.259   1.00 318.70 ? 212  THR G N   1 
ATOM   19402 C  CA  . THR G  3 214 ? 23.868  -83.389 43.471   1.00 317.91 ? 212  THR G CA  1 
ATOM   19403 C  C   . THR G  3 214 ? 22.433  -83.024 43.834   1.00 312.23 ? 212  THR G C   1 
ATOM   19404 O  O   . THR G  3 214 ? 21.975  -81.904 43.589   1.00 302.26 ? 212  THR G O   1 
ATOM   19405 C  CB  . THR G  3 214 ? 24.802  -83.043 44.634   1.00 313.02 ? 212  THR G CB  1 
ATOM   19406 O  OG1 . THR G  3 214 ? 26.158  -83.019 44.171   1.00 317.31 ? 212  THR G OG1 1 
ATOM   19407 C  CG2 . THR G  3 214 ? 24.678  -84.080 45.749   1.00 311.32 ? 212  THR G CG2 1 
ATOM   19408 N  N   . GLY G  3 215 ? 21.727  -83.990 44.429   1.00 313.01 ? 213  GLY G N   1 
ATOM   19409 C  CA  . GLY G  3 215 ? 20.365  -83.815 44.885   1.00 313.23 ? 213  GLY G CA  1 
ATOM   19410 C  C   . GLY G  3 215 ? 20.187  -83.340 46.311   1.00 316.90 ? 213  GLY G C   1 
ATOM   19411 O  O   . GLY G  3 215 ? 19.047  -83.107 46.727   1.00 316.40 ? 213  GLY G O   1 
ATOM   19412 N  N   . ARG G  3 216 ? 21.270  -83.190 47.081   1.00 312.89 ? 214  ARG G N   1 
ATOM   19413 C  CA  . ARG G  3 216 ? 21.145  -82.661 48.435   1.00 304.42 ? 214  ARG G CA  1 
ATOM   19414 C  C   . ARG G  3 216 ? 20.937  -81.155 48.444   1.00 299.53 ? 214  ARG G C   1 
ATOM   19415 O  O   . ARG G  3 216 ? 20.478  -80.611 49.456   1.00 291.15 ? 214  ARG G O   1 
ATOM   19416 C  CB  . ARG G  3 216 ? 22.387  -83.000 49.262   1.00 295.25 ? 214  ARG G CB  1 
ATOM   19417 C  CG  . ARG G  3 216 ? 22.761  -84.467 49.267   1.00 292.62 ? 214  ARG G CG  1 
ATOM   19418 C  CD  . ARG G  3 216 ? 23.993  -84.709 50.123   1.00 286.25 ? 214  ARG G CD  1 
ATOM   19419 N  NE  . ARG G  3 216 ? 24.245  -86.131 50.332   1.00 287.12 ? 214  ARG G NE  1 
ATOM   19420 C  CZ  . ARG G  3 216 ? 25.197  -86.607 51.125   1.00 285.15 ? 214  ARG G CZ  1 
ATOM   19421 N  NH1 . ARG G  3 216 ? 25.988  -85.773 51.786   1.00 284.18 ? 214  ARG G NH1 1 
ATOM   19422 N  NH2 . ARG G  3 216 ? 25.358  -87.916 51.260   1.00 291.81 ? 214  ARG G NH2 1 
ATOM   19423 N  N   . ARG G  3 217 ? 21.292  -80.478 47.346   1.00 303.22 ? 215  ARG G N   1 
ATOM   19424 C  CA  . ARG G  3 217 ? 21.209  -79.029 47.176   1.00 290.31 ? 215  ARG G CA  1 
ATOM   19425 C  C   . ARG G  3 217 ? 22.199  -78.298 48.077   1.00 287.17 ? 215  ARG G C   1 
ATOM   19426 O  O   . ARG G  3 217 ? 22.413  -77.090 47.917   1.00 271.88 ? 215  ARG G O   1 
ATOM   19427 C  CB  . ARG G  3 217 ? 19.783  -78.525 47.427   1.00 285.05 ? 215  ARG G CB  1 
ATOM   19428 C  CG  . ARG G  3 217 ? 19.444  -77.244 46.694   1.00 262.21 ? 215  ARG G CG  1 
ATOM   19429 C  CD  . ARG G  3 217 ? 18.434  -76.409 47.466   1.00 258.44 ? 215  ARG G CD  1 
ATOM   19430 N  NE  . ARG G  3 217 ? 17.215  -77.153 47.773   1.00 265.83 ? 215  ARG G NE  1 
ATOM   19431 C  CZ  . ARG G  3 217 ? 16.195  -76.662 48.470   1.00 263.86 ? 215  ARG G CZ  1 
ATOM   19432 N  NH1 . ARG G  3 217 ? 16.240  -75.423 48.936   1.00 260.71 ? 215  ARG G NH1 1 
ATOM   19433 N  NH2 . ARG G  3 217 ? 15.127  -77.411 48.703   1.00 262.17 ? 215  ARG G NH2 1 
ATOM   19434 N  N   . GLY G  3 218 ? 22.819  -79.017 49.013   1.00 288.58 ? 216  GLY G N   1 
ATOM   19435 C  CA  . GLY G  3 218 ? 23.784  -78.463 49.938   1.00 277.88 ? 216  GLY G CA  1 
ATOM   19436 C  C   . GLY G  3 218 ? 25.224  -78.820 49.651   1.00 275.59 ? 216  GLY G C   1 
ATOM   19437 O  O   . GLY G  3 218 ? 26.104  -78.481 50.448   1.00 261.86 ? 216  GLY G O   1 
ATOM   19438 N  N   . ASP G  3 219 ? 25.493  -79.500 48.535   1.00 283.46 ? 217  ASP G N   1 
ATOM   19439 C  CA  . ASP G  3 219 ? 26.865  -79.829 48.166   1.00 275.92 ? 217  ASP G CA  1 
ATOM   19440 C  C   . ASP G  3 219 ? 27.540  -78.678 47.428   1.00 259.58 ? 217  ASP G C   1 
ATOM   19441 O  O   . ASP G  3 219 ? 28.730  -78.422 47.633   1.00 254.96 ? 217  ASP G O   1 
ATOM   19442 C  CB  . ASP G  3 219 ? 26.888  -81.095 47.308   1.00 272.31 ? 217  ASP G CB  1 
ATOM   19443 C  CG  . ASP G  3 219 ? 28.283  -81.452 46.833   1.00 264.93 ? 217  ASP G CG  1 
ATOM   19444 O  OD1 . ASP G  3 219 ? 28.712  -80.926 45.784   1.00 256.22 ? 217  ASP G OD1 1 
ATOM   19445 O  OD2 . ASP G  3 219 ? 28.951  -82.259 47.511   1.00 270.14 ? 217  ASP G OD2 1 
ATOM   19446 N  N   . LEU G  3 220 ? 26.797  -77.977 46.566   1.00 241.79 ? 218  LEU G N   1 
ATOM   19447 C  CA  . LEU G  3 220 ? 27.372  -76.901 45.768   1.00 233.42 ? 218  LEU G CA  1 
ATOM   19448 C  C   . LEU G  3 220 ? 27.347  -75.558 46.485   1.00 229.95 ? 218  LEU G C   1 
ATOM   19449 O  O   . LEU G  3 220 ? 28.167  -74.685 46.174   1.00 222.26 ? 218  LEU G O   1 
ATOM   19450 C  CB  . LEU G  3 220 ? 26.628  -76.781 44.435   1.00 232.69 ? 218  LEU G CB  1 
ATOM   19451 C  CG  . LEU G  3 220 ? 27.265  -75.910 43.348   1.00 224.74 ? 218  LEU G CG  1 
ATOM   19452 C  CD1 . LEU G  3 220 ? 28.650  -76.405 43.023   1.00 225.31 ? 218  LEU G CD1 1 
ATOM   19453 C  CD2 . LEU G  3 220 ? 26.424  -75.892 42.089   1.00 225.29 ? 218  LEU G CD2 1 
ATOM   19454 N  N   . ALA G  3 221 ? 26.431  -75.368 47.429   1.00 239.66 ? 219  ALA G N   1 
ATOM   19455 C  CA  . ALA G  3 221 ? 26.318  -74.101 48.130   1.00 234.00 ? 219  ALA G CA  1 
ATOM   19456 C  C   . ALA G  3 221 ? 25.887  -74.370 49.564   1.00 249.18 ? 219  ALA G C   1 
ATOM   19457 O  O   . ALA G  3 221 ? 25.458  -75.473 49.911   1.00 267.85 ? 219  ALA G O   1 
ATOM   19458 C  CB  . ALA G  3 221 ? 25.336  -73.163 47.427   1.00 228.35 ? 219  ALA G CB  1 
ATOM   19459 N  N   . THR G  3 222 ? 25.996  -73.339 50.399   1.00 250.55 ? 220  THR G N   1 
ATOM   19460 C  CA  . THR G  3 222 ? 25.709  -73.455 51.825   1.00 259.43 ? 220  THR G CA  1 
ATOM   19461 C  C   . THR G  3 222 ? 24.202  -73.353 52.060   1.00 259.74 ? 220  THR G C   1 
ATOM   19462 O  O   . THR G  3 222 ? 23.602  -72.292 51.858   1.00 242.78 ? 220  THR G O   1 
ATOM   19463 C  CB  . THR G  3 222 ? 26.461  -72.385 52.612   1.00 254.94 ? 220  THR G CB  1 
ATOM   19464 O  OG1 . THR G  3 222 ? 25.994  -72.372 53.967   1.00 267.35 ? 220  THR G OG1 1 
ATOM   19465 C  CG2 . THR G  3 222 ? 26.266  -71.006 51.977   1.00 239.53 ? 220  THR G CG2 1 
ATOM   19466 N  N   . ILE G  3 223 ? 23.595  -74.458 52.494   1.00 280.85 ? 221  ILE G N   1 
ATOM   19467 C  CA  . ILE G  3 223 ? 22.180  -74.525 52.849   1.00 284.25 ? 221  ILE G CA  1 
ATOM   19468 C  C   . ILE G  3 223 ? 22.071  -74.763 54.349   1.00 286.78 ? 221  ILE G C   1 
ATOM   19469 O  O   . ILE G  3 223 ? 22.928  -75.421 54.951   1.00 287.41 ? 221  ILE G O   1 
ATOM   19470 C  CB  . ILE G  3 223 ? 21.446  -75.645 52.079   1.00 287.79 ? 221  ILE G CB  1 
ATOM   19471 C  CG1 . ILE G  3 223 ? 21.739  -75.553 50.584   1.00 273.05 ? 221  ILE G CG1 1 
ATOM   19472 C  CG2 . ILE G  3 223 ? 19.944  -75.585 52.324   1.00 292.16 ? 221  ILE G CG2 1 
ATOM   19473 C  CD1 . ILE G  3 223 ? 21.220  -74.297 49.942   1.00 261.28 ? 221  ILE G CD1 1 
ATOM   19474 N  N   . HIS G  3 224 ? 21.016  -74.209 54.958   1.00 290.97 ? 222  HIS G N   1 
ATOM   19475 C  CA  . HIS G  3 224 ? 20.638  -74.447 56.353   1.00 304.85 ? 222  HIS G CA  1 
ATOM   19476 C  C   . HIS G  3 224 ? 21.779  -74.306 57.362   1.00 313.29 ? 222  HIS G C   1 
ATOM   19477 O  O   . HIS G  3 224 ? 21.619  -74.671 58.531   1.00 320.53 ? 222  HIS G O   1 
ATOM   19478 C  CB  . HIS G  3 224 ? 19.998  -75.837 56.507   1.00 312.98 ? 222  HIS G CB  1 
ATOM   19479 C  CG  . HIS G  3 224 ? 20.930  -76.977 56.226   1.00 314.12 ? 222  HIS G CG  1 
ATOM   19480 N  ND1 . HIS G  3 224 ? 21.948  -77.340 57.082   1.00 319.31 ? 222  HIS G ND1 1 
ATOM   19481 C  CD2 . HIS G  3 224 ? 21.002  -77.828 55.175   1.00 307.73 ? 222  HIS G CD2 1 
ATOM   19482 C  CE1 . HIS G  3 224 ? 22.605  -78.366 56.573   1.00 317.88 ? 222  HIS G CE1 1 
ATOM   19483 N  NE2 . HIS G  3 224 ? 22.051  -78.682 55.416   1.00 313.42 ? 222  HIS G NE2 1 
ATOM   19484 N  N   . GLY G  3 225 ? 22.928  -73.779 56.941   1.00 299.49 ? 223  GLY G N   1 
ATOM   19485 C  CA  . GLY G  3 225 ? 24.045  -73.546 57.825   1.00 298.44 ? 223  GLY G CA  1 
ATOM   19486 C  C   . GLY G  3 225 ? 24.324  -72.062 58.006   1.00 283.61 ? 223  GLY G C   1 
ATOM   19487 O  O   . GLY G  3 225 ? 23.680  -71.197 57.419   1.00 269.65 ? 223  GLY G O   1 
ATOM   19488 N  N   . MET G  3 226 ? 25.310  -71.780 58.855   1.00 274.81 ? 224  MET G N   1 
ATOM   19489 C  CA  . MET G  3 226 ? 25.770  -70.410 59.006   1.00 265.42 ? 224  MET G CA  1 
ATOM   19490 C  C   . MET G  3 226 ? 26.559  -69.991 57.767   1.00 269.24 ? 224  MET G C   1 
ATOM   19491 O  O   . MET G  3 226 ? 26.856  -70.802 56.885   1.00 269.26 ? 224  MET G O   1 
ATOM   19492 C  CB  . MET G  3 226 ? 26.623  -70.264 60.262   1.00 270.81 ? 224  MET G CB  1 
ATOM   19493 C  CG  . MET G  3 226 ? 27.791  -71.222 60.315   1.00 280.54 ? 224  MET G CG  1 
ATOM   19494 S  SD  . MET G  3 226 ? 28.787  -70.966 61.788   1.00 307.12 ? 224  MET G SD  1 
ATOM   19495 C  CE  . MET G  3 226 ? 29.353  -69.290 61.506   1.00 285.62 ? 224  MET G CE  1 
ATOM   19496 N  N   . ASN G  3 227 ? 26.902  -68.701 57.708   1.00 287.21 ? 225  ASN G N   1 
ATOM   19497 C  CA  . ASN G  3 227 ? 27.532  -68.083 56.538   1.00 284.54 ? 225  ASN G CA  1 
ATOM   19498 C  C   . ASN G  3 227 ? 26.685  -68.260 55.281   1.00 274.90 ? 225  ASN G C   1 
ATOM   19499 O  O   . ASN G  3 227 ? 27.211  -68.255 54.161   1.00 263.01 ? 225  ASN G O   1 
ATOM   19500 C  CB  . ASN G  3 227 ? 28.949  -68.624 56.307   1.00 287.21 ? 225  ASN G CB  1 
ATOM   19501 C  CG  . ASN G  3 227 ? 29.864  -68.394 57.494   1.00 298.13 ? 225  ASN G CG  1 
ATOM   19502 O  OD1 . ASN G  3 227 ? 29.637  -67.495 58.305   1.00 303.47 ? 225  ASN G OD1 1 
ATOM   19503 N  ND2 . ASN G  3 227 ? 30.908  -69.206 57.601   1.00 300.83 ? 225  ASN G ND2 1 
ATOM   19504 N  N   . ARG G  3 228 ? 25.375  -68.418 55.465   1.00 277.56 ? 226  ARG G N   1 
ATOM   19505 C  CA  . ARG G  3 228 ? 24.461  -68.671 54.371   1.00 265.97 ? 226  ARG G CA  1 
ATOM   19506 C  C   . ARG G  3 228 ? 24.263  -67.402 53.548   1.00 258.58 ? 226  ARG G C   1 
ATOM   19507 O  O   . ARG G  3 228 ? 24.588  -66.302 54.002   1.00 264.88 ? 226  ARG G O   1 
ATOM   19508 C  CB  . ARG G  3 228 ? 23.125  -69.171 54.916   1.00 259.44 ? 226  ARG G CB  1 
ATOM   19509 C  CG  . ARG G  3 228 ? 22.463  -68.214 55.882   1.00 245.94 ? 226  ARG G CG  1 
ATOM   19510 C  CD  . ARG G  3 228 ? 21.155  -68.770 56.397   1.00 246.39 ? 226  ARG G CD  1 
ATOM   19511 N  NE  . ARG G  3 228 ? 20.530  -67.861 57.350   1.00 254.11 ? 226  ARG G NE  1 
ATOM   19512 C  CZ  . ARG G  3 228 ? 19.405  -68.127 58.001   1.00 267.53 ? 226  ARG G CZ  1 
ATOM   19513 N  NH1 . ARG G  3 228 ? 18.782  -69.279 57.797   1.00 263.92 ? 226  ARG G NH1 1 
ATOM   19514 N  NH2 . ARG G  3 228 ? 18.901  -67.245 58.855   1.00 277.47 ? 226  ARG G NH2 1 
ATOM   19515 N  N   . PRO G  3 229 ? 23.747  -67.536 52.327   1.00 244.14 ? 227  PRO G N   1 
ATOM   19516 C  CA  . PRO G  3 229 ? 23.602  -66.369 51.447   1.00 244.85 ? 227  PRO G CA  1 
ATOM   19517 C  C   . PRO G  3 229 ? 22.823  -65.231 52.099   1.00 237.36 ? 227  PRO G C   1 
ATOM   19518 O  O   . PRO G  3 229 ? 21.770  -65.436 52.708   1.00 230.54 ? 227  PRO G O   1 
ATOM   19519 C  CB  . PRO G  3 229 ? 22.866  -66.944 50.236   1.00 248.77 ? 227  PRO G CB  1 
ATOM   19520 C  CG  . PRO G  3 229 ? 23.326  -68.370 50.181   1.00 245.89 ? 227  PRO G CG  1 
ATOM   19521 C  CD  . PRO G  3 229 ? 23.516  -68.802 51.609   1.00 239.31 ? 227  PRO G CD  1 
ATOM   19522 N  N   . PHE G  3 230 ? 23.365  -64.018 51.978   1.00 228.11 ? 228  PHE G N   1 
ATOM   19523 C  CA  . PHE G  3 230 ? 22.767  -62.821 52.549   1.00 224.91 ? 228  PHE G CA  1 
ATOM   19524 C  C   . PHE G  3 230 ? 22.824  -61.701 51.517   1.00 206.03 ? 228  PHE G C   1 
ATOM   19525 O  O   . PHE G  3 230 ? 23.668  -61.701 50.621   1.00 205.05 ? 228  PHE G O   1 
ATOM   19526 C  CB  . PHE G  3 230 ? 23.479  -62.389 53.842   1.00 234.47 ? 228  PHE G CB  1 
ATOM   19527 C  CG  . PHE G  3 230 ? 24.861  -61.834 53.624   1.00 235.37 ? 228  PHE G CG  1 
ATOM   19528 C  CD1 . PHE G  3 230 ? 25.943  -62.679 53.437   1.00 242.66 ? 228  PHE G CD1 1 
ATOM   19529 C  CD2 . PHE G  3 230 ? 25.079  -60.466 53.613   1.00 229.84 ? 228  PHE G CD2 1 
ATOM   19530 C  CE1 . PHE G  3 230 ? 27.214  -62.169 53.236   1.00 241.90 ? 228  PHE G CE1 1 
ATOM   19531 C  CE2 . PHE G  3 230 ? 26.345  -59.950 53.417   1.00 230.10 ? 228  PHE G CE2 1 
ATOM   19532 C  CZ  . PHE G  3 230 ? 27.413  -60.803 53.226   1.00 234.44 ? 228  PHE G CZ  1 
ATOM   19533 N  N   . LEU G  3 231 ? 21.911  -60.737 51.657   1.00 193.68 ? 229  LEU G N   1 
ATOM   19534 C  CA  . LEU G  3 231 ? 21.798  -59.606 50.741   1.00 190.27 ? 229  LEU G CA  1 
ATOM   19535 C  C   . LEU G  3 231 ? 22.450  -58.378 51.370   1.00 188.43 ? 229  LEU G C   1 
ATOM   19536 O  O   . LEU G  3 231 ? 21.884  -57.766 52.281   1.00 189.45 ? 229  LEU G O   1 
ATOM   19537 C  CB  . LEU G  3 231 ? 20.335  -59.328 50.407   1.00 189.98 ? 229  LEU G CB  1 
ATOM   19538 C  CG  . LEU G  3 231 ? 20.059  -58.164 49.456   1.00 194.20 ? 229  LEU G CG  1 
ATOM   19539 C  CD1 . LEU G  3 231 ? 20.731  -58.396 48.117   1.00 201.91 ? 229  LEU G CD1 1 
ATOM   19540 C  CD2 . LEU G  3 231 ? 18.569  -57.968 49.269   1.00 198.57 ? 229  LEU G CD2 1 
ATOM   19541 N  N   . LEU G  3 232 ? 23.628  -58.007 50.873   1.00 193.35 ? 230  LEU G N   1 
ATOM   19542 C  CA  . LEU G  3 232 ? 24.348  -56.851 51.393   1.00 192.79 ? 230  LEU G CA  1 
ATOM   19543 C  C   . LEU G  3 232 ? 23.749  -55.562 50.839   1.00 189.56 ? 230  LEU G C   1 
ATOM   19544 O  O   . LEU G  3 232 ? 23.607  -55.403 49.623   1.00 187.64 ? 230  LEU G O   1 
ATOM   19545 C  CB  . LEU G  3 232 ? 25.829  -56.945 51.031   1.00 197.02 ? 230  LEU G CB  1 
ATOM   19546 C  CG  . LEU G  3 232 ? 26.781  -55.947 51.695   1.00 200.08 ? 230  LEU G CG  1 
ATOM   19547 C  CD1 . LEU G  3 232 ? 26.806  -56.165 53.198   1.00 219.21 ? 230  LEU G CD1 1 
ATOM   19548 C  CD2 . LEU G  3 232 ? 28.179  -56.070 51.111   1.00 196.93 ? 230  LEU G CD2 1 
ATOM   19549 N  N   . LEU G  3 233 ? 23.402  -54.638 51.732   1.00 215.07 ? 231  LEU G N   1 
ATOM   19550 C  CA  . LEU G  3 233 ? 22.751  -53.389 51.358   1.00 230.03 ? 231  LEU G CA  1 
ATOM   19551 C  C   . LEU G  3 233 ? 23.639  -52.206 51.726   1.00 241.35 ? 231  LEU G C   1 
ATOM   19552 O  O   . LEU G  3 233 ? 24.333  -52.232 52.747   1.00 255.19 ? 231  LEU G O   1 
ATOM   19553 C  CB  . LEU G  3 233 ? 21.383  -53.254 52.046   1.00 244.26 ? 231  LEU G CB  1 
ATOM   19554 C  CG  . LEU G  3 233 ? 20.358  -54.377 51.841   1.00 238.15 ? 231  LEU G CG  1 
ATOM   19555 C  CD1 . LEU G  3 233 ? 19.136  -54.159 52.731   1.00 234.04 ? 231  LEU G CD1 1 
ATOM   19556 C  CD2 . LEU G  3 233 ? 19.948  -54.484 50.379   1.00 229.12 ? 231  LEU G CD2 1 
ATOM   19557 N  N   . MET G  3 234 ? 23.619  -51.168 50.887   1.00 225.03 ? 232  MET G N   1 
ATOM   19558 C  CA  . MET G  3 234 ? 24.371  -49.933 51.135   1.00 211.64 ? 232  MET G CA  1 
ATOM   19559 C  C   . MET G  3 234 ? 23.448  -48.767 50.792   1.00 207.17 ? 232  MET G C   1 
ATOM   19560 O  O   . MET G  3 234 ? 23.247  -48.458 49.614   1.00 204.25 ? 232  MET G O   1 
ATOM   19561 C  CB  . MET G  3 234 ? 25.656  -49.881 50.316   1.00 206.79 ? 232  MET G CB  1 
ATOM   19562 C  CG  . MET G  3 234 ? 26.579  -51.080 50.506   1.00 209.70 ? 232  MET G CG  1 
ATOM   19563 S  SD  . MET G  3 234 ? 27.999  -51.064 49.395   1.00 214.12 ? 232  MET G SD  1 
ATOM   19564 C  CE  . MET G  3 234 ? 28.780  -52.616 49.826   1.00 216.92 ? 232  MET G CE  1 
ATOM   19565 N  N   . ALA G  3 235 ? 22.888  -48.124 51.814   1.00 217.41 ? 233  ALA G N   1 
ATOM   19566 C  CA  . ALA G  3 235 ? 21.911  -47.063 51.623   1.00 214.47 ? 233  ALA G CA  1 
ATOM   19567 C  C   . ALA G  3 235 ? 22.354  -45.812 52.369   1.00 222.82 ? 233  ALA G C   1 
ATOM   19568 O  O   . ALA G  3 235 ? 23.310  -45.827 53.147   1.00 242.06 ? 233  ALA G O   1 
ATOM   19569 C  CB  . ALA G  3 235 ? 20.516  -47.498 52.091   1.00 215.90 ? 233  ALA G CB  1 
ATOM   19570 N  N   . THR G  3 236 ? 21.635  -44.708 52.124   1.00 220.91 ? 234  THR G N   1 
ATOM   19571 C  CA  . THR G  3 236 ? 21.942  -43.428 52.760   1.00 228.56 ? 234  THR G CA  1 
ATOM   19572 C  C   . THR G  3 236 ? 20.963  -43.151 53.890   1.00 250.65 ? 234  THR G C   1 
ATOM   19573 O  O   . THR G  3 236 ? 19.744  -43.217 53.674   1.00 262.43 ? 234  THR G O   1 
ATOM   19574 C  CB  . THR G  3 236 ? 21.886  -42.295 51.741   1.00 208.63 ? 234  THR G CB  1 
ATOM   19575 O  OG1 . THR G  3 236 ? 22.928  -42.465 50.775   1.00 204.73 ? 234  THR G OG1 1 
ATOM   19576 C  CG2 . THR G  3 236 ? 22.061  -40.950 52.424   1.00 211.30 ? 234  THR G CG2 1 
ATOM   19577 N  N   . PRO G  3 237 ? 21.449  -42.833 55.091   1.00 234.70 ? 235  PRO G N   1 
ATOM   19578 C  CA  . PRO G  3 237 ? 20.541  -42.584 56.217   1.00 229.10 ? 235  PRO G CA  1 
ATOM   19579 C  C   . PRO G  3 237 ? 19.608  -41.410 55.953   1.00 228.85 ? 235  PRO G C   1 
ATOM   19580 O  O   . PRO G  3 237 ? 19.868  -40.546 55.110   1.00 225.61 ? 235  PRO G O   1 
ATOM   19581 C  CB  . PRO G  3 237 ? 21.495  -42.285 57.380   1.00 229.75 ? 235  PRO G CB  1 
ATOM   19582 C  CG  . PRO G  3 237 ? 22.776  -42.954 56.994   1.00 222.27 ? 235  PRO G CG  1 
ATOM   19583 C  CD  . PRO G  3 237 ? 22.861  -42.795 55.506   1.00 221.62 ? 235  PRO G CD  1 
ATOM   19584 N  N   . LEU G  3 238 ? 18.493  -41.395 56.692   1.00 229.52 ? 236  LEU G N   1 
ATOM   19585 C  CA  . LEU G  3 238 ? 17.555  -40.282 56.597   1.00 227.94 ? 236  LEU G CA  1 
ATOM   19586 C  C   . LEU G  3 238 ? 18.169  -38.999 57.133   1.00 231.93 ? 236  LEU G C   1 
ATOM   19587 O  O   . LEU G  3 238 ? 17.757  -37.901 56.741   1.00 240.73 ? 236  LEU G O   1 
ATOM   19588 C  CB  . LEU G  3 238 ? 16.267  -40.604 57.365   1.00 226.25 ? 236  LEU G CB  1 
ATOM   19589 C  CG  . LEU G  3 238 ? 15.412  -41.804 56.939   1.00 216.07 ? 236  LEU G CG  1 
ATOM   19590 C  CD1 . LEU G  3 238 ? 15.907  -43.105 57.561   1.00 210.10 ? 236  LEU G CD1 1 
ATOM   19591 C  CD2 . LEU G  3 238 ? 13.954  -41.558 57.286   1.00 207.44 ? 236  LEU G CD2 1 
ATOM   19592 N  N   . GLU G  3 239 ? 19.150  -39.123 58.032   1.00 218.95 ? 237  GLU G N   1 
ATOM   19593 C  CA  . GLU G  3 239 ? 19.837  -37.959 58.576   1.00 213.76 ? 237  GLU G CA  1 
ATOM   19594 C  C   . GLU G  3 239 ? 20.578  -37.182 57.494   1.00 215.81 ? 237  GLU G C   1 
ATOM   19595 O  O   . GLU G  3 239 ? 20.762  -35.965 57.618   1.00 210.02 ? 237  GLU G O   1 
ATOM   19596 C  CB  . GLU G  3 239 ? 20.803  -38.413 59.671   1.00 214.79 ? 237  GLU G CB  1 
ATOM   19597 C  CG  . GLU G  3 239 ? 20.152  -39.292 60.730   1.00 217.43 ? 237  GLU G CG  1 
ATOM   19598 C  CD  . GLU G  3 239 ? 21.112  -40.315 61.299   1.00 216.36 ? 237  GLU G CD  1 
ATOM   19599 O  OE1 . GLU G  3 239 ? 22.237  -40.424 60.770   1.00 218.25 ? 237  GLU G OE1 1 
ATOM   19600 O  OE2 . GLU G  3 239 ? 20.744  -41.011 62.268   1.00 216.95 ? 237  GLU G OE2 1 
ATOM   19601 N  N   . ARG G  3 240 ? 21.002  -37.863 56.428   1.00 231.41 ? 238  ARG G N   1 
ATOM   19602 C  CA  . ARG G  3 240 ? 21.703  -37.198 55.335   1.00 229.14 ? 238  ARG G CA  1 
ATOM   19603 C  C   . ARG G  3 240 ? 20.721  -36.546 54.366   1.00 219.00 ? 238  ARG G C   1 
ATOM   19604 O  O   . ARG G  3 240 ? 20.781  -35.335 54.128   1.00 225.22 ? 238  ARG G O   1 
ATOM   19605 C  CB  . ARG G  3 240 ? 22.595  -38.199 54.595   1.00 213.31 ? 238  ARG G CB  1 
ATOM   19606 C  CG  . ARG G  3 240 ? 23.440  -39.089 55.492   1.00 212.97 ? 238  ARG G CG  1 
ATOM   19607 C  CD  . ARG G  3 240 ? 24.517  -38.298 56.209   1.00 227.94 ? 238  ARG G CD  1 
ATOM   19608 N  NE  . ARG G  3 240 ? 25.334  -39.156 57.060   1.00 237.63 ? 238  ARG G NE  1 
ATOM   19609 C  CZ  . ARG G  3 240 ? 25.130  -39.333 58.362   1.00 251.05 ? 238  ARG G CZ  1 
ATOM   19610 N  NH1 . ARG G  3 240 ? 24.134  -38.706 58.975   1.00 244.31 ? 238  ARG G NH1 1 
ATOM   19611 N  NH2 . ARG G  3 240 ? 25.926  -40.136 59.054   1.00 259.70 ? 238  ARG G NH2 1 
ATOM   19612 N  N   . ALA G  3 241 ? 19.808  -37.343 53.798   1.00 202.80 ? 239  ALA G N   1 
ATOM   19613 C  CA  . ALA G  3 241 ? 18.903  -36.839 52.767   1.00 202.33 ? 239  ALA G CA  1 
ATOM   19614 C  C   . ALA G  3 241 ? 18.072  -35.672 53.280   1.00 207.86 ? 239  ALA G C   1 
ATOM   19615 O  O   . ALA G  3 241 ? 17.936  -34.647 52.603   1.00 222.22 ? 239  ALA G O   1 
ATOM   19616 C  CB  . ALA G  3 241 ? 17.997  -37.965 52.273   1.00 199.22 ? 239  ALA G CB  1 
ATOM   19617 N  N   . GLN G  3 242 ? 17.509  -35.807 54.475   1.00 203.28 ? 240  GLN G N   1 
ATOM   19618 C  CA  . GLN G  3 242 ? 16.728  -34.730 55.070   1.00 205.87 ? 240  GLN G CA  1 
ATOM   19619 C  C   . GLN G  3 242 ? 17.627  -33.592 55.536   1.00 210.39 ? 240  GLN G C   1 
ATOM   19620 O  O   . GLN G  3 242 ? 17.444  -32.445 55.137   1.00 213.93 ? 240  GLN G O   1 
ATOM   19621 C  CB  . GLN G  3 242 ? 15.900  -35.256 56.240   1.00 218.40 ? 240  GLN G CB  1 
ATOM   19622 C  CG  . GLN G  3 242 ? 14.947  -36.372 55.866   1.00 211.29 ? 240  GLN G CG  1 
ATOM   19623 C  CD  . GLN G  3 242 ? 14.183  -36.902 57.061   1.00 212.76 ? 240  GLN G CD  1 
ATOM   19624 O  OE1 . GLN G  3 242 ? 14.300  -36.378 58.171   1.00 219.92 ? 240  GLN G OE1 1 
ATOM   19625 N  NE2 . GLN G  3 242 ? 13.397  -37.950 56.843   1.00 209.54 ? 240  GLN G NE2 1 
ATOM   19626 N  N   . ALA G  3 252 ? 28.165  -34.897 38.874   1.00 232.57 ? 250  ALA G N   1 
ATOM   19627 C  CA  . ALA G  3 252 ? 29.040  -34.565 37.755   1.00 238.68 ? 250  ALA G CA  1 
ATOM   19628 C  C   . ALA G  3 252 ? 28.270  -34.572 36.435   1.00 235.44 ? 250  ALA G C   1 
ATOM   19629 O  O   . ALA G  3 252 ? 28.232  -35.583 35.735   1.00 219.99 ? 250  ALA G O   1 
ATOM   19630 C  CB  . ALA G  3 252 ? 30.217  -35.533 37.693   1.00 231.84 ? 250  ALA G CB  1 
ATOM   19631 N  N   . LEU G  3 253 ? 27.648  -33.441 36.111   1.00 233.88 ? 251  LEU G N   1 
ATOM   19632 C  CA  . LEU G  3 253 ? 26.876  -33.317 34.884   1.00 216.99 ? 251  LEU G CA  1 
ATOM   19633 C  C   . LEU G  3 253 ? 27.789  -33.027 33.696   1.00 201.46 ? 251  LEU G C   1 
ATOM   19634 O  O   . LEU G  3 253 ? 28.879  -32.463 33.841   1.00 175.86 ? 251  LEU G O   1 
ATOM   19635 C  CB  . LEU G  3 253 ? 25.827  -32.215 35.029   1.00 193.31 ? 251  LEU G CB  1 
ATOM   19636 C  CG  . LEU G  3 253 ? 24.882  -32.395 36.220   1.00 192.70 ? 251  LEU G CG  1 
ATOM   19637 C  CD1 . LEU G  3 253 ? 23.877  -31.259 36.290   1.00 193.35 ? 251  LEU G CD1 1 
ATOM   19638 C  CD2 . LEU G  3 253 ? 24.178  -33.745 36.163   1.00 201.05 ? 251  LEU G CD2 1 
ATOM   19639 N  N   . ASP G  3 254 ? 27.322  -33.408 32.505   1.00 212.53 ? 252  ASP G N   1 
ATOM   19640 C  CA  . ASP G  3 254 ? 28.132  -33.319 31.293   1.00 209.95 ? 252  ASP G CA  1 
ATOM   19641 C  C   . ASP G  3 254 ? 27.749  -32.145 30.397   1.00 203.03 ? 252  ASP G C   1 
ATOM   19642 O  O   . ASP G  3 254 ? 27.480  -31.039 30.879   1.00 179.24 ? 252  ASP G O   1 
ATOM   19643 C  CB  . ASP G  3 254 ? 28.036  -34.626 30.494   1.00 221.22 ? 252  ASP G CB  1 
ATOM   19644 C  CG  . ASP G  3 254 ? 26.599  -35.105 30.310   1.00 215.85 ? 252  ASP G CG  1 
ATOM   19645 O  OD1 . ASP G  3 254 ? 25.661  -34.328 30.585   1.00 228.83 ? 252  ASP G OD1 1 
ATOM   19646 O  OD2 . ASP G  3 254 ? 26.409  -36.261 29.874   1.00 202.15 ? 252  ASP G OD2 1 
ATOM   19647 N  N   . THR G  3 255 ? 27.723  -32.390 29.081   1.00 192.94 ? 253  THR G N   1 
ATOM   19648 C  CA  . THR G  3 255 ? 27.422  -31.341 28.116   1.00 171.59 ? 253  THR G CA  1 
ATOM   19649 C  C   . THR G  3 255 ? 25.973  -30.880 28.195   1.00 173.72 ? 253  THR G C   1 
ATOM   19650 O  O   . THR G  3 255 ? 25.674  -29.742 27.815   1.00 161.97 ? 253  THR G O   1 
ATOM   19651 C  CB  . THR G  3 255 ? 27.737  -31.836 26.700   1.00 158.20 ? 253  THR G CB  1 
ATOM   19652 O  OG1 . THR G  3 255 ? 26.880  -32.936 26.371   1.00 161.31 ? 253  THR G OG1 1 
ATOM   19653 C  CG2 . THR G  3 255 ? 29.179  -32.304 26.609   1.00 156.11 ? 253  THR G CG2 1 
ATOM   19654 N  N   . ASN G  3 256 ? 25.075  -31.715 28.722   1.00 200.46 ? 254  ASN G N   1 
ATOM   19655 C  CA  . ASN G  3 256 ? 23.663  -31.363 28.797   1.00 196.85 ? 254  ASN G CA  1 
ATOM   19656 C  C   . ASN G  3 256 ? 23.385  -30.291 29.834   1.00 192.46 ? 254  ASN G C   1 
ATOM   19657 O  O   . ASN G  3 256 ? 22.257  -29.795 29.902   1.00 193.07 ? 254  ASN G O   1 
ATOM   19658 C  CB  . ASN G  3 256 ? 22.832  -32.604 29.121   1.00 219.79 ? 254  ASN G CB  1 
ATOM   19659 C  CG  . ASN G  3 256 ? 22.983  -33.691 28.083   1.00 214.82 ? 254  ASN G CG  1 
ATOM   19660 O  OD1 . ASN G  3 256 ? 23.172  -33.412 26.899   1.00 219.43 ? 254  ASN G OD1 1 
ATOM   19661 N  ND2 . ASN G  3 256 ? 22.921  -34.943 28.524   1.00 205.58 ? 254  ASN G ND2 1 
ATOM   19662 N  N   . TYR G  3 257 ? 24.383  -29.919 30.626   1.00 186.12 ? 255  TYR G N   1 
ATOM   19663 C  CA  . TYR G  3 257 ? 24.238  -28.903 31.656   1.00 201.61 ? 255  TYR G CA  1 
ATOM   19664 C  C   . TYR G  3 257 ? 25.326  -27.868 31.455   1.00 197.01 ? 255  TYR G C   1 
ATOM   19665 O  O   . TYR G  3 257 ? 25.150  -26.689 31.783   1.00 185.24 ? 255  TYR G O   1 
ATOM   19666 C  CB  . TYR G  3 257 ? 24.337  -29.516 33.053   1.00 219.55 ? 255  TYR G CB  1 
ATOM   19667 C  CG  . TYR G  3 257 ? 24.605  -28.509 34.156   1.00 221.97 ? 255  TYR G CG  1 
ATOM   19668 C  CD1 . TYR G  3 257 ? 23.584  -27.724 34.676   1.00 217.84 ? 255  TYR G CD1 1 
ATOM   19669 C  CD2 . TYR G  3 257 ? 25.884  -28.347 34.676   1.00 217.17 ? 255  TYR G CD2 1 
ATOM   19670 C  CE1 . TYR G  3 257 ? 23.830  -26.806 35.685   1.00 227.25 ? 255  TYR G CE1 1 
ATOM   19671 C  CE2 . TYR G  3 257 ? 26.140  -27.432 35.681   1.00 207.16 ? 255  TYR G CE2 1 
ATOM   19672 C  CZ  . TYR G  3 257 ? 25.111  -26.665 36.182   1.00 224.99 ? 255  TYR G CZ  1 
ATOM   19673 O  OH  . TYR G  3 257 ? 25.362  -25.755 37.184   1.00 238.86 ? 255  TYR G OH  1 
ATOM   19674 N  N   . CYS G  3 258 ? 26.463  -28.316 30.924   1.00 188.48 ? 256  CYS G N   1 
ATOM   19675 C  CA  . CYS G  3 258 ? 27.617  -27.449 30.763   1.00 185.14 ? 256  CYS G CA  1 
ATOM   19676 C  C   . CYS G  3 258 ? 27.516  -26.552 29.544   1.00 176.22 ? 256  CYS G C   1 
ATOM   19677 O  O   . CYS G  3 258 ? 28.248  -25.560 29.456   1.00 160.25 ? 256  CYS G O   1 
ATOM   19678 C  CB  . CYS G  3 258 ? 28.892  -28.294 30.666   1.00 176.55 ? 256  CYS G CB  1 
ATOM   19679 S  SG  . CYS G  3 258 ? 29.785  -28.264 32.207   1.00 184.52 ? 256  CYS G SG  1 
ATOM   19680 N  N   . PHE G  3 259 ? 26.627  -26.870 28.611   1.00 180.85 ? 257  PHE G N   1 
ATOM   19681 C  CA  . PHE G  3 259 ? 26.445  -26.067 27.415   1.00 181.37 ? 257  PHE G CA  1 
ATOM   19682 C  C   . PHE G  3 259 ? 25.209  -25.187 27.487   1.00 191.00 ? 257  PHE G C   1 
ATOM   19683 O  O   . PHE G  3 259 ? 25.123  -24.198 26.750   1.00 187.37 ? 257  PHE G O   1 
ATOM   19684 C  CB  . PHE G  3 259 ? 26.374  -26.981 26.186   1.00 171.88 ? 257  PHE G CB  1 
ATOM   19685 C  CG  . PHE G  3 259 ? 27.706  -27.562 25.781   1.00 173.49 ? 257  PHE G CG  1 
ATOM   19686 C  CD1 . PHE G  3 259 ? 28.453  -28.318 26.674   1.00 170.82 ? 257  PHE G CD1 1 
ATOM   19687 C  CD2 . PHE G  3 259 ? 28.191  -27.386 24.497   1.00 193.08 ? 257  PHE G CD2 1 
ATOM   19688 C  CE1 . PHE G  3 259 ? 29.670  -28.858 26.303   1.00 153.84 ? 257  PHE G CE1 1 
ATOM   19689 C  CE2 . PHE G  3 259 ? 29.403  -27.933 24.120   1.00 181.39 ? 257  PHE G CE2 1 
ATOM   19690 C  CZ  . PHE G  3 259 ? 30.142  -28.668 25.023   1.00 165.40 ? 257  PHE G CZ  1 
ATOM   19691 N  N   . SER G  3 260 ? 24.248  -25.538 28.338   1.00 205.86 ? 258  SER G N   1 
ATOM   19692 C  CA  . SER G  3 260 ? 23.036  -24.758 28.526   1.00 211.48 ? 258  SER G CA  1 
ATOM   19693 C  C   . SER G  3 260 ? 23.154  -23.741 29.653   1.00 213.93 ? 258  SER G C   1 
ATOM   19694 O  O   . SER G  3 260 ? 22.277  -22.880 29.779   1.00 222.18 ? 258  SER G O   1 
ATOM   19695 C  CB  . SER G  3 260 ? 21.843  -25.680 28.801   1.00 218.29 ? 258  SER G CB  1 
ATOM   19696 O  OG  . SER G  3 260 ? 22.061  -26.469 29.958   1.00 222.36 ? 258  SER G OG  1 
ATOM   19697 N  N   . SER G  3 261 ? 24.205  -23.817 30.472   1.00 215.01 ? 259  SER G N   1 
ATOM   19698 C  CA  . SER G  3 261 ? 24.387  -22.910 31.595   1.00 213.31 ? 259  SER G CA  1 
ATOM   19699 C  C   . SER G  3 261 ? 25.805  -22.350 31.602   1.00 210.39 ? 259  SER G C   1 
ATOM   19700 O  O   . SER G  3 261 ? 26.730  -22.919 31.014   1.00 205.70 ? 259  SER G O   1 
ATOM   19701 C  CB  . SER G  3 261 ? 24.097  -23.602 32.935   1.00 216.52 ? 259  SER G CB  1 
ATOM   19702 O  OG  . SER G  3 261 ? 24.965  -24.704 33.145   1.00 224.88 ? 259  SER G OG  1 
ATOM   19703 N  N   . THR G  3 262 ? 25.960  -21.215 32.289   1.00 218.92 ? 260  THR G N   1 
ATOM   19704 C  CA  . THR G  3 262 ? 27.245  -20.529 32.432   1.00 230.37 ? 260  THR G CA  1 
ATOM   19705 C  C   . THR G  3 262 ? 27.811  -20.844 33.814   1.00 228.01 ? 260  THR G C   1 
ATOM   19706 O  O   . THR G  3 262 ? 27.469  -20.189 34.802   1.00 230.01 ? 260  THR G O   1 
ATOM   19707 C  CB  . THR G  3 262 ? 27.083  -19.025 32.235   1.00 230.11 ? 260  THR G CB  1 
ATOM   19708 O  OG1 . THR G  3 262 ? 26.489  -18.765 30.958   1.00 224.01 ? 260  THR G OG1 1 
ATOM   19709 C  CG2 . THR G  3 262 ? 28.437  -18.323 32.321   1.00 227.59 ? 260  THR G CG2 1 
ATOM   19710 N  N   . GLU G  3 263 ? 28.683  -21.846 33.880   1.00 201.91 ? 261  GLU G N   1 
ATOM   19711 C  CA  . GLU G  3 263 ? 29.272  -22.272 35.141   1.00 190.57 ? 261  GLU G CA  1 
ATOM   19712 C  C   . GLU G  3 263 ? 30.532  -21.467 35.443   1.00 181.56 ? 261  GLU G C   1 
ATOM   19713 O  O   . GLU G  3 263 ? 31.311  -21.141 34.542   1.00 170.70 ? 261  GLU G O   1 
ATOM   19714 C  CB  . GLU G  3 263 ? 29.595  -23.768 35.100   1.00 191.44 ? 261  GLU G CB  1 
ATOM   19715 C  CG  . GLU G  3 263 ? 29.976  -24.378 36.443   1.00 211.28 ? 261  GLU G CG  1 
ATOM   19716 C  CD  . GLU G  3 263 ? 28.801  -24.470 37.405   1.00 229.44 ? 261  GLU G CD  1 
ATOM   19717 O  OE1 . GLU G  3 263 ? 27.653  -24.607 36.933   1.00 227.91 ? 261  GLU G OE1 1 
ATOM   19718 O  OE2 . GLU G  3 263 ? 29.024  -24.402 38.632   1.00 243.68 ? 261  GLU G OE2 1 
ATOM   19719 N  N   . LYS G  3 264 ? 30.718  -21.134 36.717   1.00 182.80 ? 262  LYS G N   1 
ATOM   19720 C  CA  . LYS G  3 264 ? 31.970  -20.562 37.187   1.00 176.20 ? 262  LYS G CA  1 
ATOM   19721 C  C   . LYS G  3 264 ? 32.941  -21.629 37.686   1.00 178.82 ? 262  LYS G C   1 
ATOM   19722 O  O   . LYS G  3 264 ? 34.130  -21.337 37.851   1.00 180.07 ? 262  LYS G O   1 
ATOM   19723 C  CB  . LYS G  3 264 ? 31.683  -19.531 38.290   1.00 187.56 ? 262  LYS G CB  1 
ATOM   19724 C  CG  . LYS G  3 264 ? 32.884  -18.725 38.755   1.00 200.84 ? 262  LYS G CG  1 
ATOM   19725 C  CD  . LYS G  3 264 ? 33.636  -18.123 37.585   1.00 205.22 ? 262  LYS G CD  1 
ATOM   19726 C  CE  . LYS G  3 264 ? 34.867  -17.367 38.057   1.00 206.40 ? 262  LYS G CE  1 
ATOM   19727 N  NZ  . LYS G  3 264 ? 35.676  -16.847 36.921   1.00 196.44 ? 262  LYS G NZ  1 
ATOM   19728 N  N   . ASN G  3 265 ? 32.471  -22.857 37.902   1.00 195.42 ? 263  ASN G N   1 
ATOM   19729 C  CA  . ASN G  3 265 ? 33.273  -23.969 38.385   1.00 184.86 ? 263  ASN G CA  1 
ATOM   19730 C  C   . ASN G  3 265 ? 33.745  -24.856 37.231   1.00 162.70 ? 263  ASN G C   1 
ATOM   19731 O  O   . ASN G  3 265 ? 33.675  -24.490 36.052   1.00 156.86 ? 263  ASN G O   1 
ATOM   19732 C  CB  . ASN G  3 265 ? 32.469  -24.772 39.408   1.00 203.42 ? 263  ASN G CB  1 
ATOM   19733 C  CG  . ASN G  3 265 ? 32.351  -24.059 40.741   1.00 207.28 ? 263  ASN G CG  1 
ATOM   19734 O  OD1 . ASN G  3 265 ? 33.344  -23.578 41.292   1.00 213.44 ? 263  ASN G OD1 1 
ATOM   19735 N  ND2 . ASN G  3 265 ? 31.130  -23.963 41.253   1.00 197.35 ? 263  ASN G ND2 1 
ATOM   19736 N  N   . CYS G  3 266 ? 34.228  -26.050 37.582   1.00 165.09 ? 264  CYS G N   1 
ATOM   19737 C  CA  . CYS G  3 266 ? 34.776  -27.017 36.636   1.00 165.59 ? 264  CYS G CA  1 
ATOM   19738 C  C   . CYS G  3 266 ? 33.720  -27.530 35.667   1.00 169.22 ? 264  CYS G C   1 
ATOM   19739 O  O   . CYS G  3 266 ? 33.024  -28.513 35.948   1.00 184.38 ? 264  CYS G O   1 
ATOM   19740 C  CB  . CYS G  3 266 ? 35.409  -28.185 37.388   1.00 182.72 ? 264  CYS G CB  1 
ATOM   19741 S  SG  . CYS G  3 266 ? 35.990  -29.537 36.342   1.00 188.55 ? 264  CYS G SG  1 
ATOM   19742 N  N   . CYS G  3 267 ? 33.582  -26.851 34.535   1.00 151.58 ? 265  CYS G N   1 
ATOM   19743 C  CA  . CYS G  3 267 ? 32.627  -27.201 33.497   1.00 163.58 ? 265  CYS G CA  1 
ATOM   19744 C  C   . CYS G  3 267 ? 33.367  -27.511 32.195   1.00 135.63 ? 265  CYS G C   1 
ATOM   19745 O  O   . CYS G  3 267 ? 34.442  -26.962 31.934   1.00 134.55 ? 265  CYS G O   1 
ATOM   19746 C  CB  . CYS G  3 267 ? 31.638  -26.046 33.320   1.00 188.76 ? 265  CYS G CB  1 
ATOM   19747 S  SG  . CYS G  3 267 ? 30.243  -26.289 32.229   1.00 240.93 ? 265  CYS G SG  1 
ATOM   19748 N  N   . VAL G  3 268 ? 32.804  -28.403 31.379   1.00 145.30 ? 266  VAL G N   1 
ATOM   19749 C  CA  . VAL G  3 268 ? 33.397  -28.722 30.081   1.00 141.26 ? 266  VAL G CA  1 
ATOM   19750 C  C   . VAL G  3 268 ? 32.997  -27.654 29.068   1.00 137.61 ? 266  VAL G C   1 
ATOM   19751 O  O   . VAL G  3 268 ? 31.812  -27.474 28.770   1.00 137.69 ? 266  VAL G O   1 
ATOM   19752 C  CB  . VAL G  3 268 ? 32.988  -30.122 29.600   1.00 148.92 ? 266  VAL G CB  1 
ATOM   19753 C  CG1 . VAL G  3 268 ? 31.512  -30.386 29.838   1.00 152.10 ? 266  VAL G CG1 1 
ATOM   19754 C  CG2 . VAL G  3 268 ? 33.340  -30.299 28.125   1.00 150.70 ? 266  VAL G CG2 1 
ATOM   19755 N  N   . ARG G  3 269 ? 33.988  -26.965 28.513   1.00 132.18 ? 267  ARG G N   1 
ATOM   19756 C  CA  . ARG G  3 269 ? 33.745  -25.872 27.586   1.00 128.03 ? 267  ARG G CA  1 
ATOM   19757 C  C   . ARG G  3 269 ? 33.774  -26.383 26.151   1.00 157.85 ? 267  ARG G C   1 
ATOM   19758 O  O   . ARG G  3 269 ? 34.457  -27.359 25.833   1.00 184.30 ? 267  ARG G O   1 
ATOM   19759 C  CB  . ARG G  3 269 ? 34.787  -24.769 27.771   1.00 127.92 ? 267  ARG G CB  1 
ATOM   19760 C  CG  . ARG G  3 269 ? 34.933  -24.292 29.208   1.00 130.19 ? 267  ARG G CG  1 
ATOM   19761 C  CD  . ARG G  3 269 ? 33.602  -23.809 29.774   1.00 132.13 ? 267  ARG G CD  1 
ATOM   19762 N  NE  . ARG G  3 269 ? 33.677  -23.567 31.213   1.00 134.79 ? 267  ARG G NE  1 
ATOM   19763 C  CZ  . ARG G  3 269 ? 32.644  -23.213 31.972   1.00 137.28 ? 267  ARG G CZ  1 
ATOM   19764 N  NH1 . ARG G  3 269 ? 31.442  -23.063 31.434   1.00 137.46 ? 267  ARG G NH1 1 
ATOM   19765 N  NH2 . ARG G  3 269 ? 32.814  -23.018 33.273   1.00 139.93 ? 267  ARG G NH2 1 
ATOM   19766 N  N   . GLN G  3 270 ? 33.022  -25.712 25.283   1.00 151.23 ? 268  GLN G N   1 
ATOM   19767 C  CA  . GLN G  3 270 ? 32.921  -26.127 23.891   1.00 124.10 ? 268  GLN G CA  1 
ATOM   19768 C  C   . GLN G  3 270 ? 34.164  -25.731 23.106   1.00 122.61 ? 268  GLN G C   1 
ATOM   19769 O  O   . GLN G  3 270 ? 34.713  -24.640 23.281   1.00 122.54 ? 268  GLN G O   1 
ATOM   19770 C  CB  . GLN G  3 270 ? 31.684  -25.515 23.235   1.00 134.12 ? 268  GLN G CB  1 
ATOM   19771 C  CG  . GLN G  3 270 ? 31.439  -25.992 21.809   1.00 154.20 ? 268  GLN G CG  1 
ATOM   19772 C  CD  . GLN G  3 270 ? 30.270  -25.288 21.150   1.00 167.69 ? 268  GLN G CD  1 
ATOM   19773 O  OE1 . GLN G  3 270 ? 29.607  -24.445 21.765   1.00 185.92 ? 268  GLN G OE1 1 
ATOM   19774 N  NE2 . GLN G  3 270 ? 30.000  -25.642 19.894   1.00 141.41 ? 268  GLN G NE2 1 
ATOM   19775 N  N   . LEU G  3 271 ? 34.613  -26.637 22.241   1.00 151.35 ? 269  LEU G N   1 
ATOM   19776 C  CA  . LEU G  3 271 ? 35.764  -26.356 21.388   1.00 146.82 ? 269  LEU G CA  1 
ATOM   19777 C  C   . LEU G  3 271 ? 35.696  -27.268 20.167   1.00 140.83 ? 269  LEU G C   1 
ATOM   19778 O  O   . LEU G  3 271 ? 35.845  -28.489 20.288   1.00 125.58 ? 269  LEU G O   1 
ATOM   19779 C  CB  . LEU G  3 271 ? 37.066  -26.540 22.150   1.00 125.10 ? 269  LEU G CB  1 
ATOM   19780 C  CG  . LEU G  3 271 ? 38.322  -26.321 21.311   1.00 123.03 ? 269  LEU G CG  1 
ATOM   19781 C  CD1 . LEU G  3 271 ? 38.341  -24.909 20.747   1.00 128.00 ? 269  LEU G CD1 1 
ATOM   19782 C  CD2 . LEU G  3 271 ? 39.559  -26.603 22.136   1.00 124.89 ? 269  LEU G CD2 1 
ATOM   19783 N  N   . TYR G  3 272 ? 35.443  -26.674 19.009   1.00 132.18 ? 270  TYR G N   1 
ATOM   19784 C  CA  . TYR G  3 272 ? 35.445  -27.373 17.734   1.00 119.44 ? 270  TYR G CA  1 
ATOM   19785 C  C   . TYR G  3 272 ? 36.805  -27.182 17.081   1.00 120.56 ? 270  TYR G C   1 
ATOM   19786 O  O   . TYR G  3 272 ? 37.229  -26.046 16.846   1.00 150.34 ? 270  TYR G O   1 
ATOM   19787 C  CB  . TYR G  3 272 ? 34.335  -26.839 16.835   1.00 143.20 ? 270  TYR G CB  1 
ATOM   19788 C  CG  . TYR G  3 272 ? 34.350  -27.392 15.438   1.00 149.66 ? 270  TYR G CG  1 
ATOM   19789 C  CD1 . TYR G  3 272 ? 33.850  -28.657 15.164   1.00 126.75 ? 270  TYR G CD1 1 
ATOM   19790 C  CD2 . TYR G  3 272 ? 34.861  -26.644 14.388   1.00 162.27 ? 270  TYR G CD2 1 
ATOM   19791 C  CE1 . TYR G  3 272 ? 33.854  -29.155 13.887   1.00 124.64 ? 270  TYR G CE1 1 
ATOM   19792 C  CE2 . TYR G  3 272 ? 34.873  -27.137 13.109   1.00 157.40 ? 270  TYR G CE2 1 
ATOM   19793 C  CZ  . TYR G  3 272 ? 34.369  -28.392 12.864   1.00 139.96 ? 270  TYR G CZ  1 
ATOM   19794 O  OH  . TYR G  3 272 ? 34.382  -28.881 11.581   1.00 167.04 ? 270  TYR G OH  1 
ATOM   19795 N  N   . ILE G  3 273 ? 37.481  -28.284 16.780   1.00 119.75 ? 271  ILE G N   1 
ATOM   19796 C  CA  . ILE G  3 273 ? 38.838  -28.252 16.251   1.00 124.52 ? 271  ILE G CA  1 
ATOM   19797 C  C   . ILE G  3 273 ? 38.783  -28.567 14.765   1.00 124.00 ? 271  ILE G C   1 
ATOM   19798 O  O   . ILE G  3 273 ? 38.364  -29.660 14.371   1.00 129.45 ? 271  ILE G O   1 
ATOM   19799 C  CB  . ILE G  3 273 ? 39.753  -29.232 16.999   1.00 134.24 ? 271  ILE G CB  1 
ATOM   19800 C  CG1 . ILE G  3 273 ? 39.878  -28.809 18.462   1.00 130.68 ? 271  ILE G CG1 1 
ATOM   19801 C  CG2 . ILE G  3 273 ? 41.121  -29.324 16.336   1.00 132.57 ? 271  ILE G CG2 1 
ATOM   19802 C  CD1 . ILE G  3 273 ? 40.848  -29.644 19.242   1.00 122.71 ? 271  ILE G CD1 1 
ATOM   19803 N  N   . ASP G  3 274 ? 39.202  -27.611 13.942   1.00 119.52 ? 272  ASP G N   1 
ATOM   19804 C  CA  . ASP G  3 274 ? 39.292  -27.805 12.506   1.00 122.48 ? 272  ASP G CA  1 
ATOM   19805 C  C   . ASP G  3 274 ? 40.721  -28.159 12.125   1.00 126.17 ? 272  ASP G C   1 
ATOM   19806 O  O   . ASP G  3 274 ? 41.678  -27.629 12.693   1.00 132.55 ? 272  ASP G O   1 
ATOM   19807 C  CB  . ASP G  3 274 ? 38.851  -26.556 11.743   1.00 123.44 ? 272  ASP G CB  1 
ATOM   19808 C  CG  . ASP G  3 274 ? 38.569  -26.839 10.272   1.00 130.95 ? 272  ASP G CG  1 
ATOM   19809 O  OD1 . ASP G  3 274 ? 39.255  -27.700 9.679    1.00 135.43 ? 272  ASP G OD1 1 
ATOM   19810 O  OD2 . ASP G  3 274 ? 37.664  -26.197 9.700    1.00 141.21 ? 272  ASP G OD2 1 
ATOM   19811 N  N   . PHE G  3 275 ? 40.858  -29.053 11.151   1.00 126.64 ? 273  PHE G N   1 
ATOM   19812 C  CA  . PHE G  3 275 ? 42.180  -29.471 10.714   1.00 131.61 ? 273  PHE G CA  1 
ATOM   19813 C  C   . PHE G  3 275 ? 42.798  -28.464 9.763    1.00 141.85 ? 273  PHE G C   1 
ATOM   19814 O  O   . PHE G  3 275 ? 44.002  -28.200 9.829    1.00 148.57 ? 273  PHE G O   1 
ATOM   19815 C  CB  . PHE G  3 275 ? 42.087  -30.834 10.056   1.00 134.80 ? 273  PHE G CB  1 
ATOM   19816 C  CG  . PHE G  3 275 ? 41.610  -31.892 10.978   1.00 129.40 ? 273  PHE G CG  1 
ATOM   19817 C  CD1 . PHE G  3 275 ? 42.501  -32.585 11.771   1.00 138.71 ? 273  PHE G CD1 1 
ATOM   19818 C  CD2 . PHE G  3 275 ? 40.265  -32.181 11.071   1.00 127.42 ? 273  PHE G CD2 1 
ATOM   19819 C  CE1 . PHE G  3 275 ? 42.057  -33.559 12.630   1.00 144.04 ? 273  PHE G CE1 1 
ATOM   19820 C  CE2 . PHE G  3 275 ? 39.814  -33.152 11.925   1.00 128.50 ? 273  PHE G CE2 1 
ATOM   19821 C  CZ  . PHE G  3 275 ? 40.709  -33.844 12.707   1.00 140.19 ? 273  PHE G CZ  1 
ATOM   19822 N  N   . ARG G  3 276 ? 41.995  -27.909 8.863    1.00 152.20 ? 274  ARG G N   1 
ATOM   19823 C  CA  . ARG G  3 276 ? 42.509  -26.935 7.912    1.00 155.14 ? 274  ARG G CA  1 
ATOM   19824 C  C   . ARG G  3 276 ? 42.699  -25.563 8.552    1.00 151.03 ? 274  ARG G C   1 
ATOM   19825 O  O   . ARG G  3 276 ? 43.617  -24.826 8.171    1.00 142.76 ? 274  ARG G O   1 
ATOM   19826 C  CB  . ARG G  3 276 ? 41.551  -26.833 6.719    1.00 171.34 ? 274  ARG G CB  1 
ATOM   19827 C  CG  . ARG G  3 276 ? 41.507  -28.064 5.821    1.00 166.76 ? 274  ARG G CG  1 
ATOM   19828 C  CD  . ARG G  3 276 ? 42.678  -28.096 4.848    1.00 173.28 ? 274  ARG G CD  1 
ATOM   19829 N  NE  . ARG G  3 276 ? 42.525  -27.122 3.766    1.00 178.93 ? 274  ARG G NE  1 
ATOM   19830 C  CZ  . ARG G  3 276 ? 43.119  -25.930 3.729    1.00 189.49 ? 274  ARG G CZ  1 
ATOM   19831 N  NH1 . ARG G  3 276 ? 43.919  -25.547 4.718    1.00 208.60 ? 274  ARG G NH1 1 
ATOM   19832 N  NH2 . ARG G  3 276 ? 42.915  -25.120 2.698    1.00 168.83 ? 274  ARG G NH2 1 
ATOM   19833 N  N   . LYS G  3 277 ? 41.873  -25.222 9.541    1.00 153.73 ? 275  LYS G N   1 
ATOM   19834 C  CA  . LYS G  3 277 ? 41.821  -23.886 10.125   1.00 146.54 ? 275  LYS G CA  1 
ATOM   19835 C  C   . LYS G  3 277 ? 42.647  -23.744 11.394   1.00 137.23 ? 275  LYS G C   1 
ATOM   19836 O  O   . LYS G  3 277 ? 43.351  -22.745 11.563   1.00 130.21 ? 275  LYS G O   1 
ATOM   19837 C  CB  . LYS G  3 277 ? 40.365  -23.513 10.424   1.00 159.35 ? 275  LYS G CB  1 
ATOM   19838 C  CG  . LYS G  3 277 ? 40.166  -22.121 11.001   1.00 169.51 ? 275  LYS G CG  1 
ATOM   19839 C  CD  . LYS G  3 277 ? 40.513  -21.033 9.997    1.00 171.73 ? 275  LYS G CD  1 
ATOM   19840 C  CE  . LYS G  3 277 ? 40.247  -19.654 10.582   1.00 155.70 ? 275  LYS G CE  1 
ATOM   19841 N  NZ  . LYS G  3 277 ? 41.045  -19.437 11.826   1.00 125.97 ? 275  LYS G NZ  1 
ATOM   19842 N  N   . ASP G  3 278 ? 42.575  -24.717 12.294   1.00 122.00 ? 276  ASP G N   1 
ATOM   19843 C  CA  . ASP G  3 278 ? 43.237  -24.633 13.586   1.00 119.61 ? 276  ASP G CA  1 
ATOM   19844 C  C   . ASP G  3 278 ? 44.494  -25.488 13.657   1.00 122.83 ? 276  ASP G C   1 
ATOM   19845 O  O   . ASP G  3 278 ? 45.185  -25.471 14.680   1.00 121.74 ? 276  ASP G O   1 
ATOM   19846 C  CB  . ASP G  3 278 ? 42.254  -25.037 14.689   1.00 123.81 ? 276  ASP G CB  1 
ATOM   19847 C  CG  . ASP G  3 278 ? 41.001  -24.195 14.668   1.00 154.47 ? 276  ASP G CG  1 
ATOM   19848 O  OD1 . ASP G  3 278 ? 41.101  -23.008 14.280   1.00 165.52 ? 276  ASP G OD1 1 
ATOM   19849 O  OD2 . ASP G  3 278 ? 39.922  -24.723 15.013   1.00 164.04 ? 276  ASP G OD2 1 
ATOM   19850 N  N   . LEU G  3 279 ? 44.797  -26.235 12.597   1.00 144.68 ? 277  LEU G N   1 
ATOM   19851 C  CA  . LEU G  3 279 ? 45.969  -27.097 12.532   1.00 148.44 ? 277  LEU G CA  1 
ATOM   19852 C  C   . LEU G  3 279 ? 46.733  -27.004 11.217   1.00 154.70 ? 277  LEU G C   1 
ATOM   19853 O  O   . LEU G  3 279 ? 47.958  -27.178 11.222   1.00 156.64 ? 277  LEU G O   1 
ATOM   19854 C  CB  . LEU G  3 279 ? 45.577  -28.557 12.782   1.00 156.94 ? 277  LEU G CB  1 
ATOM   19855 C  CG  . LEU G  3 279 ? 45.218  -28.929 14.221   1.00 154.71 ? 277  LEU G CG  1 
ATOM   19856 C  CD1 . LEU G  3 279 ? 44.827  -30.394 14.313   1.00 152.92 ? 277  LEU G CD1 1 
ATOM   19857 C  CD2 . LEU G  3 279 ? 46.361  -28.600 15.184   1.00 150.10 ? 277  LEU G CD2 1 
ATOM   19858 N  N   . GLY G  3 280 ? 46.068  -26.737 10.099   1.00 162.73 ? 278  GLY G N   1 
ATOM   19859 C  CA  . GLY G  3 280 ? 46.717  -26.712 8.807    1.00 174.55 ? 278  GLY G CA  1 
ATOM   19860 C  C   . GLY G  3 280 ? 47.047  -28.099 8.301    1.00 195.00 ? 278  GLY G C   1 
ATOM   19861 O  O   . GLY G  3 280 ? 48.120  -28.306 7.717    1.00 208.66 ? 278  GLY G O   1 
ATOM   19862 N  N   . TRP G  3 281 ? 46.136  -29.055 8.487    1.00 201.84 ? 279  TRP G N   1 
ATOM   19863 C  CA  . TRP G  3 281 ? 46.348  -30.442 8.080    1.00 199.16 ? 279  TRP G CA  1 
ATOM   19864 C  C   . TRP G  3 281 ? 45.333  -30.806 7.003    1.00 197.25 ? 279  TRP G C   1 
ATOM   19865 O  O   . TRP G  3 281 ? 44.142  -30.967 7.292    1.00 200.03 ? 279  TRP G O   1 
ATOM   19866 C  CB  . TRP G  3 281 ? 46.236  -31.389 9.275    1.00 193.02 ? 279  TRP G CB  1 
ATOM   19867 C  CG  . TRP G  3 281 ? 47.344  -31.242 10.280   1.00 188.11 ? 279  TRP G CG  1 
ATOM   19868 C  CD1 . TRP G  3 281 ? 48.383  -30.351 10.241   1.00 190.41 ? 279  TRP G CD1 1 
ATOM   19869 C  CD2 . TRP G  3 281 ? 47.531  -32.022 11.468   1.00 180.76 ? 279  TRP G CD2 1 
ATOM   19870 N  NE1 . TRP G  3 281 ? 49.194  -30.524 11.336   1.00 189.79 ? 279  TRP G NE1 1 
ATOM   19871 C  CE2 . TRP G  3 281 ? 48.694  -31.545 12.103   1.00 184.57 ? 279  TRP G CE2 1 
ATOM   19872 C  CE3 . TRP G  3 281 ? 46.824  -33.077 12.058   1.00 172.85 ? 279  TRP G CE3 1 
ATOM   19873 C  CZ2 . TRP G  3 281 ? 49.168  -32.087 13.297   1.00 172.48 ? 279  TRP G CZ2 1 
ATOM   19874 C  CZ3 . TRP G  3 281 ? 47.297  -33.614 13.248   1.00 167.08 ? 279  TRP G CZ3 1 
ATOM   19875 C  CH2 . TRP G  3 281 ? 48.456  -33.116 13.854   1.00 170.92 ? 279  TRP G CH2 1 
ATOM   19876 N  N   . LYS G  3 282 ? 45.808  -30.936 5.768    1.00 203.53 ? 280  LYS G N   1 
ATOM   19877 C  CA  . LYS G  3 282 ? 44.983  -31.346 4.644    1.00 204.53 ? 280  LYS G CA  1 
ATOM   19878 C  C   . LYS G  3 282 ? 45.206  -32.809 4.290    1.00 218.21 ? 280  LYS G C   1 
ATOM   19879 O  O   . LYS G  3 282 ? 44.732  -33.272 3.248    1.00 239.32 ? 280  LYS G O   1 
ATOM   19880 C  CB  . LYS G  3 282 ? 45.261  -30.449 3.432    1.00 205.62 ? 280  LYS G CB  1 
ATOM   19881 C  CG  . LYS G  3 282 ? 44.124  -30.401 2.414    1.00 218.51 ? 280  LYS G CG  1 
ATOM   19882 C  CD  . LYS G  3 282 ? 44.353  -29.324 1.371    1.00 212.18 ? 280  LYS G CD  1 
ATOM   19883 C  CE  . LYS G  3 282 ? 45.627  -29.585 0.591    1.00 198.68 ? 280  LYS G CE  1 
ATOM   19884 N  NZ  . LYS G  3 282 ? 45.838  -28.547 -0.451   1.00 194.36 ? 280  LYS G NZ  1 
ATOM   19885 N  N   . TRP G  3 283 ? 45.920  -33.544 5.137    1.00 210.35 ? 281  TRP G N   1 
ATOM   19886 C  CA  . TRP G  3 283 ? 46.200  -34.954 4.917    1.00 199.17 ? 281  TRP G CA  1 
ATOM   19887 C  C   . TRP G  3 283 ? 45.180  -35.867 5.582    1.00 188.04 ? 281  TRP G C   1 
ATOM   19888 O  O   . TRP G  3 283 ? 45.265  -37.091 5.427    1.00 179.57 ? 281  TRP G O   1 
ATOM   19889 C  CB  . TRP G  3 283 ? 47.607  -35.288 5.425    1.00 201.91 ? 281  TRP G CB  1 
ATOM   19890 C  CG  . TRP G  3 283 ? 47.788  -35.053 6.894    1.00 200.04 ? 281  TRP G CG  1 
ATOM   19891 C  CD1 . TRP G  3 283 ? 48.074  -33.868 7.509    1.00 201.11 ? 281  TRP G CD1 1 
ATOM   19892 C  CD2 . TRP G  3 283 ? 47.692  -36.033 7.934    1.00 190.17 ? 281  TRP G CD2 1 
ATOM   19893 N  NE1 . TRP G  3 283 ? 48.166  -34.051 8.869    1.00 201.20 ? 281  TRP G NE1 1 
ATOM   19894 C  CE2 . TRP G  3 283 ? 47.935  -35.371 9.155    1.00 194.89 ? 281  TRP G CE2 1 
ATOM   19895 C  CE3 . TRP G  3 283 ? 47.426  -37.405 7.951    1.00 181.23 ? 281  TRP G CE3 1 
ATOM   19896 C  CZ2 . TRP G  3 283 ? 47.917  -36.037 10.380   1.00 179.70 ? 281  TRP G CZ2 1 
ATOM   19897 C  CZ3 . TRP G  3 283 ? 47.410  -38.064 9.165    1.00 178.24 ? 281  TRP G CZ3 1 
ATOM   19898 C  CH2 . TRP G  3 283 ? 47.654  -37.380 10.363   1.00 177.24 ? 281  TRP G CH2 1 
ATOM   19899 N  N   . ILE G  3 284 ? 44.205  -35.304 6.290    1.00 183.66 ? 282  ILE G N   1 
ATOM   19900 C  CA  . ILE G  3 284 ? 43.147  -36.065 6.943    1.00 173.99 ? 282  ILE G CA  1 
ATOM   19901 C  C   . ILE G  3 284 ? 41.861  -35.805 6.177    1.00 179.05 ? 282  ILE G C   1 
ATOM   19902 O  O   . ILE G  3 284 ? 41.315  -34.695 6.217    1.00 183.71 ? 282  ILE G O   1 
ATOM   19903 C  CB  . ILE G  3 284 ? 42.997  -35.680 8.419    1.00 152.92 ? 282  ILE G CB  1 
ATOM   19904 C  CG1 . ILE G  3 284 ? 44.281  -36.007 9.178    1.00 153.76 ? 282  ILE G CG1 1 
ATOM   19905 C  CG2 . ILE G  3 284 ? 41.797  -36.382 9.034    1.00 145.88 ? 282  ILE G CG2 1 
ATOM   19906 C  CD1 . ILE G  3 284 ? 44.207  -35.694 10.649   1.00 147.31 ? 282  ILE G CD1 1 
ATOM   19907 N  N   . HIS G  3 285 ? 41.362  -36.839 5.498    1.00 155.08 ? 283  HIS G N   1 
ATOM   19908 C  CA  . HIS G  3 285 ? 40.168  -36.670 4.680    1.00 153.93 ? 283  HIS G CA  1 
ATOM   19909 C  C   . HIS G  3 285 ? 38.930  -36.553 5.556    1.00 142.22 ? 283  HIS G C   1 
ATOM   19910 O  O   . HIS G  3 285 ? 38.153  -35.600 5.427    1.00 139.39 ? 283  HIS G O   1 
ATOM   19911 C  CB  . HIS G  3 285 ? 40.031  -37.836 3.698    1.00 202.05 ? 283  HIS G CB  1 
ATOM   19912 C  CG  . HIS G  3 285 ? 41.109  -37.887 2.659    1.00 212.54 ? 283  HIS G CG  1 
ATOM   19913 N  ND1 . HIS G  3 285 ? 42.450  -37.930 2.978    1.00 210.45 ? 283  HIS G ND1 1 
ATOM   19914 C  CD2 . HIS G  3 285 ? 41.044  -37.923 1.305    1.00 205.25 ? 283  HIS G CD2 1 
ATOM   19915 C  CE1 . HIS G  3 285 ? 43.164  -37.976 1.867    1.00 206.90 ? 283  HIS G CE1 1 
ATOM   19916 N  NE2 . HIS G  3 285 ? 42.336  -37.975 0.838    1.00 208.20 ? 283  HIS G NE2 1 
ATOM   19917 N  N   . GLU G  3 286 ? 38.731  -37.512 6.452    1.00 144.87 ? 284  GLU G N   1 
ATOM   19918 C  CA  . GLU G  3 286 ? 37.583  -37.496 7.346    1.00 144.69 ? 284  GLU G CA  1 
ATOM   19919 C  C   . GLU G  3 286 ? 37.986  -37.822 8.780    1.00 162.63 ? 284  GLU G C   1 
ATOM   19920 O  O   . GLU G  3 286 ? 38.724  -38.781 9.015    1.00 171.11 ? 284  GLU G O   1 
ATOM   19921 C  CB  . GLU G  3 286 ? 36.523  -38.483 6.862    1.00 145.66 ? 284  GLU G CB  1 
ATOM   19922 C  CG  . GLU G  3 286 ? 35.935  -38.139 5.503    1.00 159.64 ? 284  GLU G CG  1 
ATOM   19923 C  CD  . GLU G  3 286 ? 35.107  -36.874 5.529    1.00 144.78 ? 284  GLU G CD  1 
ATOM   19924 O  OE1 . GLU G  3 286 ? 34.608  -36.526 6.619    1.00 143.64 ? 284  GLU G OE1 1 
ATOM   19925 O  OE2 . GLU G  3 286 ? 34.962  -36.228 4.468    1.00 144.01 ? 284  GLU G OE2 1 
ATOM   19926 N  N   . PRO G  3 287 ? 37.505  -37.019 9.742    1.00 160.01 ? 285  PRO G N   1 
ATOM   19927 C  CA  . PRO G  3 287 ? 36.691  -35.835 9.466    1.00 134.92 ? 285  PRO G CA  1 
ATOM   19928 C  C   . PRO G  3 287 ? 37.560  -34.624 9.168    1.00 132.59 ? 285  PRO G C   1 
ATOM   19929 O  O   . PRO G  3 287 ? 38.785  -34.732 9.208    1.00 137.03 ? 285  PRO G O   1 
ATOM   19930 C  CB  . PRO G  3 287 ? 35.915  -35.641 10.765   1.00 133.21 ? 285  PRO G CB  1 
ATOM   19931 C  CG  . PRO G  3 287 ? 36.856  -36.133 11.813   1.00 133.86 ? 285  PRO G CG  1 
ATOM   19932 C  CD  . PRO G  3 287 ? 37.624  -37.275 11.189   1.00 145.50 ? 285  PRO G CD  1 
ATOM   19933 N  N   . LYS G  3 288 ? 36.931  -33.492 8.857    1.00 134.97 ? 286  LYS G N   1 
ATOM   19934 C  CA  . LYS G  3 288 ? 37.628  -32.234 8.622    1.00 156.51 ? 286  LYS G CA  1 
ATOM   19935 C  C   . LYS G  3 288 ? 37.355  -31.244 9.752    1.00 155.13 ? 286  LYS G C   1 
ATOM   19936 O  O   . LYS G  3 288 ? 37.382  -30.026 9.551    1.00 131.57 ? 286  LYS G O   1 
ATOM   19937 C  CB  . LYS G  3 288 ? 37.234  -31.649 7.265    1.00 160.22 ? 286  LYS G CB  1 
ATOM   19938 C  CG  . LYS G  3 288 ? 37.580  -32.554 6.070    1.00 154.17 ? 286  LYS G CG  1 
ATOM   19939 C  CD  . LYS G  3 288 ? 36.960  -32.065 4.758    1.00 147.07 ? 286  LYS G CD  1 
ATOM   19940 C  CE  . LYS G  3 288 ? 37.219  -33.045 3.618    1.00 149.43 ? 286  LYS G CE  1 
ATOM   19941 N  NZ  . LYS G  3 288 ? 36.563  -32.609 2.353    1.00 151.38 ? 286  LYS G NZ  1 
ATOM   19942 N  N   . GLY G  3 289 ? 37.110  -31.768 10.952   1.00 163.65 ? 287  GLY G N   1 
ATOM   19943 C  CA  . GLY G  3 289 ? 36.778  -30.973 12.114   1.00 137.65 ? 287  GLY G CA  1 
ATOM   19944 C  C   . GLY G  3 289 ? 35.908  -31.745 13.085   1.00 138.52 ? 287  GLY G C   1 
ATOM   19945 O  O   . GLY G  3 289 ? 35.086  -32.566 12.663   1.00 132.91 ? 287  GLY G O   1 
ATOM   19946 N  N   . TYR G  3 290 ? 36.094  -31.527 14.385   1.00 144.62 ? 288  TYR G N   1 
ATOM   19947 C  CA  . TYR G  3 290 ? 35.311  -32.247 15.382   1.00 139.12 ? 288  TYR G CA  1 
ATOM   19948 C  C   . TYR G  3 290 ? 35.300  -31.448 16.683   1.00 123.30 ? 288  TYR G C   1 
ATOM   19949 O  O   . TYR G  3 290 ? 36.018  -30.457 16.834   1.00 121.98 ? 288  TYR G O   1 
ATOM   19950 C  CB  . TYR G  3 290 ? 35.860  -33.663 15.575   1.00 126.88 ? 288  TYR G CB  1 
ATOM   19951 C  CG  . TYR G  3 290 ? 37.134  -33.711 16.369   1.00 127.02 ? 288  TYR G CG  1 
ATOM   19952 C  CD1 . TYR G  3 290 ? 38.310  -33.175 15.863   1.00 126.43 ? 288  TYR G CD1 1 
ATOM   19953 C  CD2 . TYR G  3 290 ? 37.166  -34.309 17.615   1.00 128.09 ? 288  TYR G CD2 1 
ATOM   19954 C  CE1 . TYR G  3 290 ? 39.475  -33.215 16.585   1.00 126.92 ? 288  TYR G CE1 1 
ATOM   19955 C  CE2 . TYR G  3 290 ? 38.325  -34.360 18.341   1.00 128.55 ? 288  TYR G CE2 1 
ATOM   19956 C  CZ  . TYR G  3 290 ? 39.477  -33.811 17.823   1.00 127.99 ? 288  TYR G CZ  1 
ATOM   19957 O  OH  . TYR G  3 290 ? 40.638  -33.859 18.550   1.00 128.80 ? 288  TYR G OH  1 
ATOM   19958 N  N   . HIS G  3 291 ? 34.452  -31.885 17.620   1.00 126.88 ? 289  HIS G N   1 
ATOM   19959 C  CA  . HIS G  3 291 ? 34.283  -31.227 18.921   1.00 126.33 ? 289  HIS G CA  1 
ATOM   19960 C  C   . HIS G  3 291 ? 35.105  -31.970 19.965   1.00 127.44 ? 289  HIS G C   1 
ATOM   19961 O  O   . HIS G  3 291 ? 34.622  -32.892 20.623   1.00 129.06 ? 289  HIS G O   1 
ATOM   19962 C  CB  . HIS G  3 291 ? 32.819  -31.179 19.329   1.00 131.02 ? 289  HIS G CB  1 
ATOM   19963 C  CG  . HIS G  3 291 ? 31.999  -30.242 18.509   1.00 144.55 ? 289  HIS G CG  1 
ATOM   19964 N  ND1 . HIS G  3 291 ? 31.771  -30.439 17.165   1.00 143.80 ? 289  HIS G ND1 1 
ATOM   19965 C  CD2 . HIS G  3 291 ? 31.339  -29.108 18.841   1.00 150.05 ? 289  HIS G CD2 1 
ATOM   19966 C  CE1 . HIS G  3 291 ? 31.012  -29.464 16.701   1.00 143.58 ? 289  HIS G CE1 1 
ATOM   19967 N  NE2 . HIS G  3 291 ? 30.735  -28.643 17.698   1.00 159.53 ? 289  HIS G NE2 1 
ATOM   19968 N  N   . ALA G  3 292 ? 36.350  -31.539 20.144   1.00 124.08 ? 290  ALA G N   1 
ATOM   19969 C  CA  . ALA G  3 292 ? 37.188  -32.148 21.167   1.00 125.38 ? 290  ALA G CA  1 
ATOM   19970 C  C   . ALA G  3 292 ? 36.860  -31.603 22.547   1.00 125.39 ? 290  ALA G C   1 
ATOM   19971 O  O   . ALA G  3 292 ? 36.860  -32.354 23.528   1.00 142.42 ? 290  ALA G O   1 
ATOM   19972 C  CB  . ALA G  3 292 ? 38.660  -31.912 20.844   1.00 125.23 ? 290  ALA G CB  1 
ATOM   19973 N  N   . ASN G  3 293 ? 36.594  -30.299 22.637   1.00 162.08 ? 291  ASN G N   1 
ATOM   19974 C  CA  . ASN G  3 293 ? 36.266  -29.615 23.884   1.00 147.17 ? 291  ASN G CA  1 
ATOM   19975 C  C   . ASN G  3 293 ? 37.413  -29.704 24.884   1.00 145.00 ? 291  ASN G C   1 
ATOM   19976 O  O   . ASN G  3 293 ? 38.491  -30.216 24.562   1.00 166.76 ? 291  ASN G O   1 
ATOM   19977 C  CB  . ASN G  3 293 ? 34.976  -30.171 24.497   1.00 125.60 ? 291  ASN G CB  1 
ATOM   19978 C  CG  . ASN G  3 293 ? 33.778  -30.001 23.583   1.00 125.07 ? 291  ASN G CG  1 
ATOM   19979 O  OD1 . ASN G  3 293 ? 33.839  -29.289 22.582   1.00 123.72 ? 291  ASN G OD1 1 
ATOM   19980 N  ND2 . ASN G  3 293 ? 32.675  -30.648 23.932   1.00 126.43 ? 291  ASN G ND2 1 
ATOM   19981 N  N   . PHE G  3 294 ? 37.193  -29.189 26.090   1.00 134.79 ? 292  PHE G N   1 
ATOM   19982 C  CA  . PHE G  3 294 ? 38.204  -29.207 27.138   1.00 146.05 ? 292  PHE G CA  1 
ATOM   19983 C  C   . PHE G  3 294 ? 37.526  -28.924 28.473   1.00 156.29 ? 292  PHE G C   1 
ATOM   19984 O  O   . PHE G  3 294 ? 36.356  -28.536 28.528   1.00 141.90 ? 292  PHE G O   1 
ATOM   19985 C  CB  . PHE G  3 294 ? 39.315  -28.194 26.851   1.00 145.19 ? 292  PHE G CB  1 
ATOM   19986 C  CG  . PHE G  3 294 ? 38.827  -26.779 26.745   1.00 141.14 ? 292  PHE G CG  1 
ATOM   19987 C  CD1 . PHE G  3 294 ? 38.326  -26.294 25.548   1.00 141.65 ? 292  PHE G CD1 1 
ATOM   19988 C  CD2 . PHE G  3 294 ? 38.864  -25.933 27.844   1.00 140.80 ? 292  PHE G CD2 1 
ATOM   19989 C  CE1 . PHE G  3 294 ? 37.877  -24.991 25.445   1.00 152.64 ? 292  PHE G CE1 1 
ATOM   19990 C  CE2 . PHE G  3 294 ? 38.414  -24.626 27.749   1.00 142.66 ? 292  PHE G CE2 1 
ATOM   19991 C  CZ  . PHE G  3 294 ? 37.923  -24.155 26.545   1.00 151.19 ? 292  PHE G CZ  1 
ATOM   19992 N  N   . CYS G  3 295 ? 38.278  -29.127 29.555   1.00 176.04 ? 293  CYS G N   1 
ATOM   19993 C  CA  . CYS G  3 295 ? 37.808  -28.855 30.912   1.00 161.81 ? 293  CYS G CA  1 
ATOM   19994 C  C   . CYS G  3 295 ? 38.521  -27.621 31.451   1.00 164.18 ? 293  CYS G C   1 
ATOM   19995 O  O   . CYS G  3 295 ? 39.755  -27.584 31.499   1.00 149.12 ? 293  CYS G O   1 
ATOM   19996 C  CB  . CYS G  3 295 ? 38.047  -30.043 31.845   1.00 147.11 ? 293  CYS G CB  1 
ATOM   19997 S  SG  . CYS G  3 295 ? 37.302  -31.602 31.323   1.00 165.58 ? 293  CYS G SG  1 
ATOM   19998 N  N   . LEU G  3 296 ? 37.744  -26.610 31.836   1.00 169.46 ? 294  LEU G N   1 
ATOM   19999 C  CA  . LEU G  3 296 ? 38.278  -25.396 32.438   1.00 169.67 ? 294  LEU G CA  1 
ATOM   20000 C  C   . LEU G  3 296 ? 37.401  -25.011 33.621   1.00 156.42 ? 294  LEU G C   1 
ATOM   20001 O  O   . LEU G  3 296 ? 36.177  -24.922 33.483   1.00 148.08 ? 294  LEU G O   1 
ATOM   20002 C  CB  . LEU G  3 296 ? 38.344  -24.257 31.411   1.00 156.92 ? 294  LEU G CB  1 
ATOM   20003 C  CG  . LEU G  3 296 ? 39.364  -23.130 31.622   1.00 145.57 ? 294  LEU G CG  1 
ATOM   20004 C  CD1 . LEU G  3 296 ? 38.880  -22.083 32.623   1.00 149.02 ? 294  LEU G CD1 1 
ATOM   20005 C  CD2 . LEU G  3 296 ? 40.705  -23.707 32.053   1.00 151.41 ? 294  LEU G CD2 1 
ATOM   20006 N  N   . GLY G  3 297 ? 38.022  -24.784 34.779   1.00 154.92 ? 295  GLY G N   1 
ATOM   20007 C  CA  . GLY G  3 297 ? 37.288  -24.391 35.960   1.00 170.29 ? 295  GLY G CA  1 
ATOM   20008 C  C   . GLY G  3 297 ? 37.968  -24.759 37.266   1.00 186.90 ? 295  GLY G C   1 
ATOM   20009 O  O   . GLY G  3 297 ? 38.788  -25.680 37.331   1.00 190.05 ? 295  GLY G O   1 
ATOM   20010 N  N   . PRO G  3 298 ? 37.642  -24.031 38.333   1.00 175.54 ? 296  PRO G N   1 
ATOM   20011 C  CA  . PRO G  3 298 ? 38.224  -24.323 39.647   1.00 175.89 ? 296  PRO G CA  1 
ATOM   20012 C  C   . PRO G  3 298 ? 37.456  -25.406 40.395   1.00 176.47 ? 296  PRO G C   1 
ATOM   20013 O  O   . PRO G  3 298 ? 36.282  -25.674 40.134   1.00 175.98 ? 296  PRO G O   1 
ATOM   20014 C  CB  . PRO G  3 298 ? 38.119  -22.977 40.374   1.00 173.31 ? 296  PRO G CB  1 
ATOM   20015 C  CG  . PRO G  3 298 ? 36.900  -22.354 39.793   1.00 166.51 ? 296  PRO G CG  1 
ATOM   20016 C  CD  . PRO G  3 298 ? 36.839  -22.797 38.348   1.00 158.61 ? 296  PRO G CD  1 
ATOM   20017 N  N   . CYS G  3 299 ? 38.150  -26.022 41.355   1.00 169.79 ? 297  CYS G N   1 
ATOM   20018 C  CA  . CYS G  3 299 ? 37.571  -27.075 42.190   1.00 178.43 ? 297  CYS G CA  1 
ATOM   20019 C  C   . CYS G  3 299 ? 37.973  -26.846 43.642   1.00 196.46 ? 297  CYS G C   1 
ATOM   20020 O  O   . CYS G  3 299 ? 39.004  -27.355 44.100   1.00 205.88 ? 297  CYS G O   1 
ATOM   20021 C  CB  . CYS G  3 299 ? 38.022  -28.465 41.737   1.00 188.77 ? 297  CYS G CB  1 
ATOM   20022 S  SG  . CYS G  3 299 ? 37.648  -28.882 40.017   1.00 222.55 ? 297  CYS G SG  1 
ATOM   20023 N  N   . PRO G  3 300 ? 37.188  -26.075 44.396   1.00 197.77 ? 298  PRO G N   1 
ATOM   20024 C  CA  . PRO G  3 300 ? 37.499  -25.835 45.807   1.00 196.50 ? 298  PRO G CA  1 
ATOM   20025 C  C   . PRO G  3 300 ? 36.784  -26.821 46.727   1.00 210.79 ? 298  PRO G C   1 
ATOM   20026 O  O   . PRO G  3 300 ? 35.971  -27.644 46.299   1.00 224.20 ? 298  PRO G O   1 
ATOM   20027 C  CB  . PRO G  3 300 ? 36.985  -24.404 46.033   1.00 191.75 ? 298  PRO G CB  1 
ATOM   20028 C  CG  . PRO G  3 300 ? 35.924  -24.185 44.963   1.00 178.24 ? 298  PRO G CG  1 
ATOM   20029 C  CD  . PRO G  3 300 ? 35.976  -25.348 43.985   1.00 183.31 ? 298  PRO G CD  1 
ATOM   20030 N  N   . TYR G  3 301 ? 37.102  -26.717 48.015   1.00 211.87 ? 299  TYR G N   1 
ATOM   20031 C  CA  . TYR G  3 301 ? 36.513  -27.597 49.026   1.00 225.75 ? 299  TYR G CA  1 
ATOM   20032 C  C   . TYR G  3 301 ? 35.073  -27.194 49.339   1.00 223.98 ? 299  TYR G C   1 
ATOM   20033 O  O   . TYR G  3 301 ? 34.595  -27.363 50.464   1.00 226.97 ? 299  TYR G O   1 
ATOM   20034 C  CB  . TYR G  3 301 ? 37.352  -27.591 50.310   1.00 240.74 ? 299  TYR G CB  1 
ATOM   20035 C  CG  . TYR G  3 301 ? 38.834  -27.806 50.085   1.00 243.09 ? 299  TYR G CG  1 
ATOM   20036 C  CD1 . TYR G  3 301 ? 39.341  -29.077 49.850   1.00 238.34 ? 299  TYR G CD1 1 
ATOM   20037 C  CD2 . TYR G  3 301 ? 39.725  -26.741 50.116   1.00 241.76 ? 299  TYR G CD2 1 
ATOM   20038 C  CE1 . TYR G  3 301 ? 40.692  -29.282 49.646   1.00 231.82 ? 299  TYR G CE1 1 
ATOM   20039 C  CE2 . TYR G  3 301 ? 41.080  -26.937 49.913   1.00 238.94 ? 299  TYR G CE2 1 
ATOM   20040 C  CZ  . TYR G  3 301 ? 41.556  -28.211 49.679   1.00 231.63 ? 299  TYR G CZ  1 
ATOM   20041 O  OH  . TYR G  3 301 ? 42.901  -28.417 49.477   1.00 229.34 ? 299  TYR G OH  1 
ATOM   20042 N  N   . ALA G  3 326 ? 46.206  -30.163 45.222   1.00 242.74 ? 324  ALA G N   1 
ATOM   20043 C  CA  . ALA G  3 326 ? 45.484  -29.157 44.451   1.00 242.81 ? 324  ALA G CA  1 
ATOM   20044 C  C   . ALA G  3 326 ? 44.491  -29.813 43.490   1.00 247.77 ? 324  ALA G C   1 
ATOM   20045 O  O   . ALA G  3 326 ? 44.890  -30.383 42.475   1.00 257.43 ? 324  ALA G O   1 
ATOM   20046 C  CB  . ALA G  3 326 ? 46.462  -28.275 43.691   1.00 238.39 ? 324  ALA G CB  1 
ATOM   20047 N  N   . PRO G  3 327 ? 43.206  -29.761 43.837   1.00 238.92 ? 325  PRO G N   1 
ATOM   20048 C  CA  . PRO G  3 327 ? 42.167  -30.363 42.981   1.00 229.77 ? 325  PRO G CA  1 
ATOM   20049 C  C   . PRO G  3 327 ? 42.069  -29.679 41.623   1.00 221.97 ? 325  PRO G C   1 
ATOM   20050 O  O   . PRO G  3 327 ? 41.890  -28.462 41.533   1.00 221.00 ? 325  PRO G O   1 
ATOM   20051 C  CB  . PRO G  3 327 ? 40.885  -30.177 43.803   1.00 231.77 ? 325  PRO G CB  1 
ATOM   20052 C  CG  . PRO G  3 327 ? 41.358  -29.994 45.217   1.00 241.44 ? 325  PRO G CG  1 
ATOM   20053 C  CD  . PRO G  3 327 ? 42.654  -29.253 45.104   1.00 244.39 ? 325  PRO G CD  1 
ATOM   20054 N  N   . CYS G  3 328 ? 42.195  -30.470 40.559   1.00 213.43 ? 326  CYS G N   1 
ATOM   20055 C  CA  . CYS G  3 328 ? 42.152  -29.967 39.192   1.00 198.49 ? 326  CYS G CA  1 
ATOM   20056 C  C   . CYS G  3 328 ? 40.857  -30.372 38.496   1.00 188.46 ? 326  CYS G C   1 
ATOM   20057 O  O   . CYS G  3 328 ? 40.164  -31.313 38.901   1.00 188.28 ? 326  CYS G O   1 
ATOM   20058 C  CB  . CYS G  3 328 ? 43.348  -30.459 38.368   1.00 209.97 ? 326  CYS G CB  1 
ATOM   20059 S  SG  . CYS G  3 328 ? 44.966  -29.807 38.856   1.00 223.31 ? 326  CYS G SG  1 
ATOM   20060 N  N   . CYS G  3 329 ? 40.526  -29.610 37.453   1.00 169.51 ? 327  CYS G N   1 
ATOM   20061 C  CA  . CYS G  3 329 ? 39.374  -29.866 36.587   1.00 170.66 ? 327  CYS G CA  1 
ATOM   20062 C  C   . CYS G  3 329 ? 39.785  -30.819 35.465   1.00 178.03 ? 327  CYS G C   1 
ATOM   20063 O  O   . CYS G  3 329 ? 40.208  -30.401 34.383   1.00 169.89 ? 327  CYS G O   1 
ATOM   20064 C  CB  . CYS G  3 329 ? 38.834  -28.551 36.044   1.00 177.52 ? 327  CYS G CB  1 
ATOM   20065 S  SG  . CYS G  3 329 ? 37.321  -28.667 35.079   1.00 197.94 ? 327  CYS G SG  1 
ATOM   20066 N  N   . VAL G  3 330 ? 39.665  -32.120 35.721   1.00 180.57 ? 328  VAL G N   1 
ATOM   20067 C  CA  . VAL G  3 330 ? 40.070  -33.140 34.751   1.00 149.08 ? 328  VAL G CA  1 
ATOM   20068 C  C   . VAL G  3 330 ? 38.834  -33.786 34.133   1.00 146.73 ? 328  VAL G C   1 
ATOM   20069 O  O   . VAL G  3 330 ? 37.793  -33.893 34.798   1.00 149.31 ? 328  VAL G O   1 
ATOM   20070 C  CB  . VAL G  3 330 ? 40.974  -34.201 35.402   1.00 153.64 ? 328  VAL G CB  1 
ATOM   20071 C  CG1 . VAL G  3 330 ? 42.284  -33.580 35.866   1.00 156.82 ? 328  VAL G CG1 1 
ATOM   20072 C  CG2 . VAL G  3 330 ? 40.261  -34.874 36.567   1.00 160.18 ? 328  VAL G CG2 1 
ATOM   20073 N  N   . PRO G  3 331 ? 38.901  -34.234 32.880   1.00 147.60 ? 329  PRO G N   1 
ATOM   20074 C  CA  . PRO G  3 331 ? 37.745  -34.903 32.271   1.00 146.06 ? 329  PRO G CA  1 
ATOM   20075 C  C   . PRO G  3 331 ? 37.474  -36.262 32.897   1.00 171.41 ? 329  PRO G C   1 
ATOM   20076 O  O   . PRO G  3 331 ? 38.397  -37.002 33.247   1.00 203.67 ? 329  PRO G O   1 
ATOM   20077 C  CB  . PRO G  3 331 ? 38.151  -35.040 30.800   1.00 141.44 ? 329  PRO G CB  1 
ATOM   20078 C  CG  . PRO G  3 331 ? 39.643  -35.011 30.816   1.00 156.57 ? 329  PRO G CG  1 
ATOM   20079 C  CD  . PRO G  3 331 ? 40.005  -34.058 31.920   1.00 144.64 ? 329  PRO G CD  1 
ATOM   20080 N  N   . GLN G  3 332 ? 36.189  -36.583 33.041   1.00 168.11 ? 330  GLN G N   1 
ATOM   20081 C  CA  . GLN G  3 332 ? 35.765  -37.866 33.589   1.00 154.34 ? 330  GLN G CA  1 
ATOM   20082 C  C   . GLN G  3 332 ? 35.420  -38.881 32.509   1.00 163.69 ? 330  GLN G C   1 
ATOM   20083 O  O   . GLN G  3 332 ? 35.813  -40.048 32.616   1.00 196.06 ? 330  GLN G O   1 
ATOM   20084 C  CB  . GLN G  3 332 ? 34.560  -37.682 34.520   1.00 160.41 ? 330  GLN G CB  1 
ATOM   20085 C  CG  . GLN G  3 332 ? 34.086  -38.969 35.193   1.00 165.39 ? 330  GLN G CG  1 
ATOM   20086 C  CD  . GLN G  3 332 ? 32.970  -38.735 36.198   1.00 169.98 ? 330  GLN G CD  1 
ATOM   20087 O  OE1 . GLN G  3 332 ? 32.440  -37.629 36.306   1.00 167.94 ? 330  GLN G OE1 1 
ATOM   20088 N  NE2 . GLN G  3 332 ? 32.615  -39.776 36.946   1.00 174.77 ? 330  GLN G NE2 1 
ATOM   20089 N  N   . ALA G  3 333 ? 34.697  -38.465 31.473   1.00 160.19 ? 331  ALA G N   1 
ATOM   20090 C  CA  . ALA G  3 333 ? 34.316  -39.335 30.368   1.00 163.61 ? 331  ALA G CA  1 
ATOM   20091 C  C   . ALA G  3 333 ? 34.871  -38.784 29.062   1.00 143.28 ? 331  ALA G C   1 
ATOM   20092 O  O   . ALA G  3 333 ? 34.709  -37.596 28.765   1.00 140.46 ? 331  ALA G O   1 
ATOM   20093 C  CB  . ALA G  3 333 ? 32.793  -39.481 30.281   1.00 175.03 ? 331  ALA G CB  1 
ATOM   20094 N  N   . LEU G  3 334 ? 35.540  -39.640 28.296   1.00 161.31 ? 332  LEU G N   1 
ATOM   20095 C  CA  . LEU G  3 334 ? 36.075  -39.261 26.998   1.00 164.05 ? 332  LEU G CA  1 
ATOM   20096 C  C   . LEU G  3 334 ? 35.611  -40.249 25.935   1.00 166.84 ? 332  LEU G C   1 
ATOM   20097 O  O   . LEU G  3 334 ? 35.291  -41.405 26.229   1.00 148.85 ? 332  LEU G O   1 
ATOM   20098 C  CB  . LEU G  3 334 ? 37.605  -39.172 27.021   1.00 155.21 ? 332  LEU G CB  1 
ATOM   20099 C  CG  . LEU G  3 334 ? 38.201  -37.990 27.790   1.00 143.78 ? 332  LEU G CG  1 
ATOM   20100 C  CD1 . LEU G  3 334 ? 38.283  -38.281 29.282   1.00 148.21 ? 332  LEU G CD1 1 
ATOM   20101 C  CD2 . LEU G  3 334 ? 39.571  -37.661 27.228   1.00 142.64 ? 332  LEU G CD2 1 
ATOM   20102 N  N   . GLU G  3 335 ? 35.585  -39.782 24.688   1.00 154.79 ? 333  GLU G N   1 
ATOM   20103 C  CA  . GLU G  3 335 ? 35.067  -40.559 23.575   1.00 143.56 ? 333  GLU G CA  1 
ATOM   20104 C  C   . GLU G  3 335 ? 36.095  -40.656 22.453   1.00 143.59 ? 333  GLU G C   1 
ATOM   20105 O  O   . GLU G  3 335 ? 36.790  -39.676 22.158   1.00 140.99 ? 333  GLU G O   1 
ATOM   20106 C  CB  . GLU G  3 335 ? 33.763  -39.922 23.052   1.00 171.56 ? 333  GLU G CB  1 
ATOM   20107 C  CG  . GLU G  3 335 ? 32.631  -39.866 24.091   1.00 178.69 ? 333  GLU G CG  1 
ATOM   20108 C  CD  . GLU G  3 335 ? 31.340  -39.247 23.560   1.00 153.07 ? 333  GLU G CD  1 
ATOM   20109 O  OE1 . GLU G  3 335 ? 31.249  -38.971 22.344   1.00 139.69 ? 333  GLU G OE1 1 
ATOM   20110 O  OE2 . GLU G  3 335 ? 30.406  -39.051 24.367   1.00 141.32 ? 333  GLU G OE2 1 
ATOM   20111 N  N   . PRO G  3 336 ? 36.229  -41.825 21.826   1.00 152.90 ? 334  PRO G N   1 
ATOM   20112 C  CA  . PRO G  3 336 ? 37.204  -41.984 20.741   1.00 155.87 ? 334  PRO G CA  1 
ATOM   20113 C  C   . PRO G  3 336 ? 36.757  -41.294 19.458   1.00 165.87 ? 334  PRO G C   1 
ATOM   20114 O  O   . PRO G  3 336 ? 35.595  -40.920 19.293   1.00 169.00 ? 334  PRO G O   1 
ATOM   20115 C  CB  . PRO G  3 336 ? 37.270  -43.503 20.553   1.00 153.85 ? 334  PRO G CB  1 
ATOM   20116 C  CG  . PRO G  3 336 ? 35.943  -43.985 20.988   1.00 154.96 ? 334  PRO G CG  1 
ATOM   20117 C  CD  . PRO G  3 336 ? 35.536  -43.089 22.130   1.00 163.64 ? 334  PRO G CD  1 
ATOM   20118 N  N   . LEU G  3 337 ? 37.705  -41.134 18.532   1.00 169.85 ? 335  LEU G N   1 
ATOM   20119 C  CA  . LEU G  3 337 ? 37.442  -40.465 17.254   1.00 146.39 ? 335  LEU G CA  1 
ATOM   20120 C  C   . LEU G  3 337 ? 37.999  -41.274 16.089   1.00 146.58 ? 335  LEU G C   1 
ATOM   20121 O  O   . LEU G  3 337 ? 39.229  -41.478 16.011   1.00 148.08 ? 335  LEU G O   1 
ATOM   20122 C  CB  . LEU G  3 337 ? 38.032  -39.052 17.236   1.00 139.55 ? 335  LEU G CB  1 
ATOM   20123 C  CG  . LEU G  3 337 ? 37.935  -38.344 15.879   1.00 137.92 ? 335  LEU G CG  1 
ATOM   20124 C  CD1 . LEU G  3 337 ? 36.481  -38.068 15.526   1.00 136.77 ? 335  LEU G CD1 1 
ATOM   20125 C  CD2 . LEU G  3 337 ? 38.749  -37.060 15.853   1.00 134.99 ? 335  LEU G CD2 1 
ATOM   20126 N  N   . PRO G  3 338 ? 37.157  -41.734 15.162   1.00 148.08 ? 336  PRO G N   1 
ATOM   20127 C  CA  . PRO G  3 338 ? 37.664  -42.397 13.957   1.00 163.72 ? 336  PRO G CA  1 
ATOM   20128 C  C   . PRO G  3 338 ? 38.141  -41.393 12.917   1.00 159.40 ? 336  PRO G C   1 
ATOM   20129 O  O   . PRO G  3 338 ? 37.493  -40.375 12.661   1.00 145.40 ? 336  PRO G O   1 
ATOM   20130 C  CB  . PRO G  3 338 ? 36.444  -43.179 13.454   1.00 178.34 ? 336  PRO G CB  1 
ATOM   20131 C  CG  . PRO G  3 338 ? 35.275  -42.382 13.924   1.00 150.30 ? 336  PRO G CG  1 
ATOM   20132 C  CD  . PRO G  3 338 ? 35.685  -41.786 15.247   1.00 147.65 ? 336  PRO G CD  1 
ATOM   20133 N  N   . ILE G  3 339 ? 39.290  -41.694 12.303   1.00 173.85 ? 337  ILE G N   1 
ATOM   20134 C  CA  . ILE G  3 339 ? 39.886  -40.827 11.295   1.00 152.03 ? 337  ILE G CA  1 
ATOM   20135 C  C   . ILE G  3 339 ? 40.156  -41.635 10.036   1.00 174.10 ? 337  ILE G C   1 
ATOM   20136 O  O   . ILE G  3 339 ? 40.213  -42.867 10.058   1.00 181.14 ? 337  ILE G O   1 
ATOM   20137 C  CB  . ILE G  3 339 ? 41.190  -40.162 11.778   1.00 148.14 ? 337  ILE G CB  1 
ATOM   20138 C  CG1 . ILE G  3 339 ? 42.274  -41.212 12.022   1.00 157.60 ? 337  ILE G CG1 1 
ATOM   20139 C  CG2 . ILE G  3 339 ? 40.933  -39.377 13.048   1.00 144.42 ? 337  ILE G CG2 1 
ATOM   20140 C  CD1 . ILE G  3 339 ? 43.602  -40.620 12.443   1.00 152.53 ? 337  ILE G CD1 1 
ATOM   20141 N  N   . VAL G  3 340 ? 40.319  -40.917 8.926    1.00 183.14 ? 338  VAL G N   1 
ATOM   20142 C  CA  . VAL G  3 340 ? 40.633  -41.515 7.633    1.00 182.16 ? 338  VAL G CA  1 
ATOM   20143 C  C   . VAL G  3 340 ? 41.783  -40.735 7.011    1.00 177.34 ? 338  VAL G C   1 
ATOM   20144 O  O   . VAL G  3 340 ? 41.652  -39.534 6.746    1.00 174.08 ? 338  VAL G O   1 
ATOM   20145 C  CB  . VAL G  3 340 ? 39.420  -41.532 6.692    1.00 166.02 ? 338  VAL G CB  1 
ATOM   20146 C  CG1 . VAL G  3 340 ? 39.840  -42.028 5.321    1.00 162.02 ? 338  VAL G CG1 1 
ATOM   20147 C  CG2 . VAL G  3 340 ? 38.319  -42.411 7.269    1.00 172.48 ? 338  VAL G CG2 1 
ATOM   20148 N  N   . TYR G  3 341 ? 42.912  -41.410 6.797    1.00 174.17 ? 339  TYR G N   1 
ATOM   20149 C  CA  . TYR G  3 341 ? 44.072  -40.808 6.158    1.00 177.84 ? 339  TYR G CA  1 
ATOM   20150 C  C   . TYR G  3 341 ? 44.730  -41.836 5.252    1.00 198.23 ? 339  TYR G C   1 
ATOM   20151 O  O   . TYR G  3 341 ? 44.484  -43.039 5.359    1.00 221.44 ? 339  TYR G O   1 
ATOM   20152 C  CB  . TYR G  3 341 ? 45.078  -40.271 7.187    1.00 176.68 ? 339  TYR G CB  1 
ATOM   20153 C  CG  . TYR G  3 341 ? 45.790  -41.330 8.007    1.00 187.49 ? 339  TYR G CG  1 
ATOM   20154 C  CD1 . TYR G  3 341 ? 45.188  -41.889 9.126    1.00 179.52 ? 339  TYR G CD1 1 
ATOM   20155 C  CD2 . TYR G  3 341 ? 47.077  -41.750 7.678    1.00 211.03 ? 339  TYR G CD2 1 
ATOM   20156 C  CE1 . TYR G  3 341 ? 45.836  -42.847 9.886    1.00 183.47 ? 339  TYR G CE1 1 
ATOM   20157 C  CE2 . TYR G  3 341 ? 47.734  -42.709 8.434    1.00 210.18 ? 339  TYR G CE2 1 
ATOM   20158 C  CZ  . TYR G  3 341 ? 47.107  -43.253 9.536    1.00 196.60 ? 339  TYR G CZ  1 
ATOM   20159 O  OH  . TYR G  3 341 ? 47.753  -44.204 10.292   1.00 203.01 ? 339  TYR G OH  1 
ATOM   20160 N  N   . TYR G  3 342 ? 45.574  -41.348 4.351    1.00 202.10 ? 340  TYR G N   1 
ATOM   20161 C  CA  . TYR G  3 342 ? 46.278  -42.205 3.411    1.00 223.76 ? 340  TYR G CA  1 
ATOM   20162 C  C   . TYR G  3 342 ? 47.733  -42.396 3.832    1.00 209.28 ? 340  TYR G C   1 
ATOM   20163 O  O   . TYR G  3 342 ? 48.318  -41.573 4.541    1.00 198.49 ? 340  TYR G O   1 
ATOM   20164 C  CB  . TYR G  3 342 ? 46.213  -41.623 1.996    1.00 233.35 ? 340  TYR G CB  1 
ATOM   20165 C  CG  . TYR G  3 342 ? 44.915  -41.889 1.260    1.00 224.21 ? 340  TYR G CG  1 
ATOM   20166 C  CD1 . TYR G  3 342 ? 43.740  -41.241 1.624    1.00 214.02 ? 340  TYR G CD1 1 
ATOM   20167 C  CD2 . TYR G  3 342 ? 44.872  -42.771 0.187    1.00 203.98 ? 340  TYR G CD2 1 
ATOM   20168 C  CE1 . TYR G  3 342 ? 42.553  -41.476 0.949    1.00 209.00 ? 340  TYR G CE1 1 
ATOM   20169 C  CE2 . TYR G  3 342 ? 43.689  -43.008 -0.498   1.00 207.46 ? 340  TYR G CE2 1 
ATOM   20170 C  CZ  . TYR G  3 342 ? 42.532  -42.360 -0.111   1.00 204.02 ? 340  TYR G CZ  1 
ATOM   20171 O  OH  . TYR G  3 342 ? 41.351  -42.595 -0.785   1.00 195.59 ? 340  TYR G OH  1 
ATOM   20172 N  N   . VAL G  3 343 ? 48.319  -43.495 3.362    1.00 220.68 ? 341  VAL G N   1 
ATOM   20173 C  CA  . VAL G  3 343 ? 49.726  -43.814 3.588    1.00 237.11 ? 341  VAL G CA  1 
ATOM   20174 C  C   . VAL G  3 343 ? 50.319  -44.112 2.217    1.00 250.53 ? 341  VAL G C   1 
ATOM   20175 O  O   . VAL G  3 343 ? 50.201  -45.234 1.713    1.00 243.06 ? 341  VAL G O   1 
ATOM   20176 C  CB  . VAL G  3 343 ? 49.919  -44.997 4.544    1.00 237.24 ? 341  VAL G CB  1 
ATOM   20177 C  CG1 . VAL G  3 343 ? 51.399  -45.289 4.735    1.00 242.11 ? 341  VAL G CG1 1 
ATOM   20178 C  CG2 . VAL G  3 343 ? 49.258  -44.720 5.883    1.00 214.91 ? 341  VAL G CG2 1 
ATOM   20179 N  N   . GLY G  3 344 ? 50.957  -43.113 1.611    1.00 244.66 ? 342  GLY G N   1 
ATOM   20180 C  CA  . GLY G  3 344 ? 51.437  -43.256 0.255    1.00 239.89 ? 342  GLY G CA  1 
ATOM   20181 C  C   . GLY G  3 344 ? 50.288  -43.462 -0.705   1.00 227.88 ? 342  GLY G C   1 
ATOM   20182 O  O   . GLY G  3 344 ? 49.674  -42.499 -1.171   1.00 218.90 ? 342  GLY G O   1 
ATOM   20183 N  N   . ARG G  3 345 ? 49.991  -44.720 -1.011   1.00 226.38 ? 343  ARG G N   1 
ATOM   20184 C  CA  . ARG G  3 345 ? 48.853  -45.068 -1.845   1.00 221.87 ? 343  ARG G CA  1 
ATOM   20185 C  C   . ARG G  3 345 ? 47.809  -45.871 -1.083   1.00 209.22 ? 343  ARG G C   1 
ATOM   20186 O  O   . ARG G  3 345 ? 46.755  -46.184 -1.649   1.00 208.72 ? 343  ARG G O   1 
ATOM   20187 C  CB  . ARG G  3 345 ? 49.314  -45.858 -3.082   1.00 253.73 ? 343  ARG G CB  1 
ATOM   20188 C  CG  . ARG G  3 345 ? 50.547  -45.290 -3.783   1.00 254.71 ? 343  ARG G CG  1 
ATOM   20189 C  CD  . ARG G  3 345 ? 50.913  -46.085 -5.037   1.00 251.02 ? 343  ARG G CD  1 
ATOM   20190 N  NE  . ARG G  3 345 ? 52.230  -45.718 -5.559   1.00 239.12 ? 343  ARG G NE  1 
ATOM   20191 C  CZ  . ARG G  3 345 ? 53.361  -46.361 -5.274   1.00 240.85 ? 343  ARG G CZ  1 
ATOM   20192 N  NH1 . ARG G  3 345 ? 53.344  -47.414 -4.470   1.00 240.62 ? 343  ARG G NH1 1 
ATOM   20193 N  NH2 . ARG G  3 345 ? 54.510  -45.951 -5.794   1.00 246.80 ? 343  ARG G NH2 1 
ATOM   20194 N  N   . LYS G  3 346 ? 48.060  -46.194 0.186    1.00 204.74 ? 344  LYS G N   1 
ATOM   20195 C  CA  . LYS G  3 346 ? 47.184  -47.064 0.966    1.00 207.52 ? 344  LYS G CA  1 
ATOM   20196 C  C   . LYS G  3 346 ? 46.367  -46.255 1.964    1.00 224.59 ? 344  LYS G C   1 
ATOM   20197 O  O   . LYS G  3 346 ? 46.938  -45.692 2.911    1.00 232.94 ? 344  LYS G O   1 
ATOM   20198 C  CB  . LYS G  3 346 ? 48.008  -48.132 1.691    1.00 211.21 ? 344  LYS G CB  1 
ATOM   20199 C  CG  . LYS G  3 346 ? 49.021  -48.841 0.795    1.00 234.30 ? 344  LYS G CG  1 
ATOM   20200 C  CD  . LYS G  3 346 ? 49.762  -49.959 1.520    1.00 238.09 ? 344  LYS G CD  1 
ATOM   20201 C  CE  . LYS G  3 346 ? 50.841  -50.586 0.632    1.00 242.97 ? 344  LYS G CE  1 
ATOM   20202 N  NZ  . LYS G  3 346 ? 50.296  -51.354 -0.532   1.00 253.19 ? 344  LYS G NZ  1 
ATOM   20203 N  N   . PRO G  3 347 ? 45.044  -46.169 1.799    1.00 221.13 ? 345  PRO G N   1 
ATOM   20204 C  CA  . PRO G  3 347 ? 44.205  -45.465 2.781    1.00 186.05 ? 345  PRO G CA  1 
ATOM   20205 C  C   . PRO G  3 347 ? 43.939  -46.335 4.002    1.00 187.31 ? 345  PRO G C   1 
ATOM   20206 O  O   . PRO G  3 347 ? 43.535  -47.494 3.881    1.00 212.34 ? 345  PRO G O   1 
ATOM   20207 C  CB  . PRO G  3 347 ? 42.911  -45.185 2.009    1.00 184.34 ? 345  PRO G CB  1 
ATOM   20208 C  CG  . PRO G  3 347 ? 42.829  -46.281 1.026    1.00 212.20 ? 345  PRO G CG  1 
ATOM   20209 C  CD  . PRO G  3 347 ? 44.252  -46.666 0.659    1.00 236.96 ? 345  PRO G CD  1 
ATOM   20210 N  N   . LYS G  3 348 ? 44.165  -45.769 5.184    1.00 188.31 ? 346  LYS G N   1 
ATOM   20211 C  CA  . LYS G  3 348 ? 43.970  -46.476 6.443    1.00 198.07 ? 346  LYS G CA  1 
ATOM   20212 C  C   . LYS G  3 348 ? 42.909  -45.759 7.268    1.00 198.39 ? 346  LYS G C   1 
ATOM   20213 O  O   . LYS G  3 348 ? 43.051  -44.569 7.574    1.00 183.22 ? 346  LYS G O   1 
ATOM   20214 C  CB  . LYS G  3 348 ? 45.284  -46.583 7.220    1.00 190.57 ? 346  LYS G CB  1 
ATOM   20215 C  CG  . LYS G  3 348 ? 46.360  -47.387 6.506    1.00 199.92 ? 346  LYS G CG  1 
ATOM   20216 C  CD  . LYS G  3 348 ? 47.599  -47.560 7.372    1.00 201.95 ? 346  LYS G CD  1 
ATOM   20217 C  CE  . LYS G  3 348 ? 48.660  -48.392 6.666    1.00 215.48 ? 346  LYS G CE  1 
ATOM   20218 N  NZ  . LYS G  3 348 ? 48.156  -49.755 6.321    1.00 223.38 ? 346  LYS G NZ  1 
ATOM   20219 N  N   . VAL G  3 349 ? 41.840  -46.475 7.603    1.00 194.53 ? 347  VAL G N   1 
ATOM   20220 C  CA  . VAL G  3 349 ? 40.800  -45.965 8.487    1.00 176.91 ? 347  VAL G CA  1 
ATOM   20221 C  C   . VAL G  3 349 ? 41.154  -46.390 9.908    1.00 177.31 ? 347  VAL G C   1 
ATOM   20222 O  O   . VAL G  3 349 ? 41.031  -47.566 10.260   1.00 182.08 ? 347  VAL G O   1 
ATOM   20223 C  CB  . VAL G  3 349 ? 39.415  -46.481 8.081    1.00 178.32 ? 347  VAL G CB  1 
ATOM   20224 C  CG1 . VAL G  3 349 ? 38.337  -45.869 8.965    1.00 178.50 ? 347  VAL G CG1 1 
ATOM   20225 C  CG2 . VAL G  3 349 ? 39.154  -46.185 6.615    1.00 187.58 ? 347  VAL G CG2 1 
ATOM   20226 N  N   . GLU G  3 350 ? 41.589  -45.434 10.729   1.00 169.59 ? 348  GLU G N   1 
ATOM   20227 C  CA  . GLU G  3 350 ? 42.013  -45.709 12.093   1.00 170.96 ? 348  GLU G CA  1 
ATOM   20228 C  C   . GLU G  3 350 ? 41.175  -44.911 13.084   1.00 164.51 ? 348  GLU G C   1 
ATOM   20229 O  O   . GLU G  3 350 ? 40.550  -43.908 12.732   1.00 160.15 ? 348  GLU G O   1 
ATOM   20230 C  CB  . GLU G  3 350 ? 43.499  -45.390 12.290   1.00 176.98 ? 348  GLU G CB  1 
ATOM   20231 C  CG  . GLU G  3 350 ? 44.408  -46.176 11.365   1.00 189.93 ? 348  GLU G CG  1 
ATOM   20232 C  CD  . GLU G  3 350 ? 45.865  -46.097 11.765   1.00 192.79 ? 348  GLU G CD  1 
ATOM   20233 O  OE1 . GLU G  3 350 ? 46.687  -46.809 11.149   1.00 207.15 ? 348  GLU G OE1 1 
ATOM   20234 O  OE2 . GLU G  3 350 ? 46.184  -45.341 12.704   1.00 185.00 ? 348  GLU G OE2 1 
ATOM   20235 N  N   . GLN G  3 351 ? 41.185  -45.362 14.341   1.00 165.33 ? 349  GLN G N   1 
ATOM   20236 C  CA  . GLN G  3 351 ? 40.383  -44.759 15.402   1.00 161.30 ? 349  GLN G CA  1 
ATOM   20237 C  C   . GLN G  3 351 ? 41.276  -44.425 16.588   1.00 165.49 ? 349  GLN G C   1 
ATOM   20238 O  O   . GLN G  3 351 ? 41.916  -45.314 17.163   1.00 164.22 ? 349  GLN G O   1 
ATOM   20239 C  CB  . GLN G  3 351 ? 39.240  -45.684 15.837   1.00 163.68 ? 349  GLN G CB  1 
ATOM   20240 C  CG  . GLN G  3 351 ? 38.309  -45.072 16.880   1.00 162.08 ? 349  GLN G CG  1 
ATOM   20241 C  CD  . GLN G  3 351 ? 37.212  -46.026 17.328   1.00 165.03 ? 349  GLN G CD  1 
ATOM   20242 O  OE1 . GLN G  3 351 ? 37.310  -47.239 17.137   1.00 167.95 ? 349  GLN G OE1 1 
ATOM   20243 N  NE2 . GLN G  3 351 ? 36.151  -45.477 17.915   1.00 167.27 ? 349  GLN G NE2 1 
ATOM   20244 N  N   . LEU G  3 352 ? 41.318  -43.143 16.945   1.00 183.82 ? 350  LEU G N   1 
ATOM   20245 C  CA  . LEU G  3 352 ? 42.079  -42.690 18.098   1.00 169.73 ? 350  LEU G CA  1 
ATOM   20246 C  C   . LEU G  3 352 ? 41.264  -42.881 19.370   1.00 161.71 ? 350  LEU G C   1 
ATOM   20247 O  O   . LEU G  3 352 ? 40.043  -42.707 19.373   1.00 153.15 ? 350  LEU G O   1 
ATOM   20248 C  CB  . LEU G  3 352 ? 42.470  -41.220 17.939   1.00 158.51 ? 350  LEU G CB  1 
ATOM   20249 C  CG  . LEU G  3 352 ? 43.336  -40.852 16.730   1.00 167.21 ? 350  LEU G CG  1 
ATOM   20250 C  CD1 . LEU G  3 352 ? 43.624  -39.366 16.706   1.00 163.12 ? 350  LEU G CD1 1 
ATOM   20251 C  CD2 . LEU G  3 352 ? 44.636  -41.640 16.733   1.00 195.56 ? 350  LEU G CD2 1 
ATOM   20252 N  N   . SER G  3 353 ? 41.949  -43.233 20.455   1.00 180.39 ? 351  SER G N   1 
ATOM   20253 C  CA  . SER G  3 353 ? 41.297  -43.495 21.731   1.00 188.65 ? 351  SER G CA  1 
ATOM   20254 C  C   . SER G  3 353 ? 41.305  -42.252 22.620   1.00 173.67 ? 351  SER G C   1 
ATOM   20255 O  O   . SER G  3 353 ? 42.353  -41.628 22.817   1.00 157.55 ? 351  SER G O   1 
ATOM   20256 C  CB  . SER G  3 353 ? 41.977  -44.675 22.433   1.00 214.96 ? 351  SER G CB  1 
ATOM   20257 O  OG  . SER G  3 353 ? 43.370  -44.459 22.584   1.00 225.80 ? 351  SER G OG  1 
ATOM   20258 N  N   . ASN G  3 354 ? 40.129  -41.913 23.164   1.00 179.37 ? 352  ASN G N   1 
ATOM   20259 C  CA  . ASN G  3 354 ? 39.916  -40.786 24.073   1.00 173.45 ? 352  ASN G CA  1 
ATOM   20260 C  C   . ASN G  3 354 ? 40.320  -39.435 23.484   1.00 174.22 ? 352  ASN G C   1 
ATOM   20261 O  O   . ASN G  3 354 ? 41.429  -38.950 23.729   1.00 175.16 ? 352  ASN G O   1 
ATOM   20262 C  CB  . ASN G  3 354 ? 40.665  -41.013 25.391   1.00 172.17 ? 352  ASN G CB  1 
ATOM   20263 C  CG  . ASN G  3 354 ? 40.138  -42.209 26.163   1.00 187.23 ? 352  ASN G CG  1 
ATOM   20264 O  OD1 . ASN G  3 354 ? 39.198  -42.088 26.948   1.00 202.77 ? 352  ASN G OD1 1 
ATOM   20265 N  ND2 . ASN G  3 354 ? 40.756  -43.368 25.959   1.00 203.83 ? 352  ASN G ND2 1 
ATOM   20266 N  N   . MET G  3 355 ? 39.396  -38.784 22.774   1.00 159.51 ? 353  MET G N   1 
ATOM   20267 C  CA  . MET G  3 355 ? 39.670  -37.493 22.151   1.00 151.37 ? 353  MET G CA  1 
ATOM   20268 C  C   . MET G  3 355 ? 38.604  -36.472 22.531   1.00 134.43 ? 353  MET G C   1 
ATOM   20269 O  O   . MET G  3 355 ? 38.922  -35.354 22.951   1.00 132.48 ? 353  MET G O   1 
ATOM   20270 C  CB  . MET G  3 355 ? 39.728  -37.637 20.624   1.00 170.39 ? 353  MET G CB  1 
ATOM   20271 C  CG  . MET G  3 355 ? 40.866  -38.503 20.087   1.00 170.55 ? 353  MET G CG  1 
ATOM   20272 S  SD  . MET G  3 355 ? 42.514  -37.853 20.430   1.00 229.11 ? 353  MET G SD  1 
ATOM   20273 C  CE  . MET G  3 355 ? 42.466  -36.290 19.560   1.00 198.79 ? 353  MET G CE  1 
ATOM   20274 N  N   . ILE G  3 356 ? 37.339  -36.856 22.392   1.00 134.55 ? 354  ILE G N   1 
ATOM   20275 C  CA  . ILE G  3 356 ? 36.218  -35.969 22.684   1.00 132.62 ? 354  ILE G CA  1 
ATOM   20276 C  C   . ILE G  3 356 ? 35.954  -35.983 24.184   1.00 133.48 ? 354  ILE G C   1 
ATOM   20277 O  O   . ILE G  3 356 ? 35.599  -37.020 24.753   1.00 146.15 ? 354  ILE G O   1 
ATOM   20278 C  CB  . ILE G  3 356 ? 34.964  -36.391 21.904   1.00 133.08 ? 354  ILE G CB  1 
ATOM   20279 C  CG1 . ILE G  3 356 ? 35.151  -36.177 20.398   1.00 132.14 ? 354  ILE G CG1 1 
ATOM   20280 C  CG2 . ILE G  3 356 ? 33.743  -35.644 22.415   1.00 132.02 ? 354  ILE G CG2 1 
ATOM   20281 C  CD1 . ILE G  3 356 ? 35.719  -37.377 19.661   1.00 134.67 ? 354  ILE G CD1 1 
ATOM   20282 N  N   . VAL G  3 357 ? 36.093  -34.828 24.824   1.00 131.65 ? 355  VAL G N   1 
ATOM   20283 C  CA  . VAL G  3 357 ? 35.858  -34.720 26.260   1.00 132.67 ? 355  VAL G CA  1 
ATOM   20284 C  C   . VAL G  3 357 ? 34.371  -34.521 26.518   1.00 133.45 ? 355  VAL G C   1 
ATOM   20285 O  O   . VAL G  3 357 ? 33.799  -33.488 26.153   1.00 146.76 ? 355  VAL G O   1 
ATOM   20286 C  CB  . VAL G  3 357 ? 36.671  -33.572 26.864   1.00 131.53 ? 355  VAL G CB  1 
ATOM   20287 C  CG1 . VAL G  3 357 ? 36.251  -33.344 28.299   1.00 132.78 ? 355  VAL G CG1 1 
ATOM   20288 C  CG2 . VAL G  3 357 ? 38.149  -33.885 26.779   1.00 132.13 ? 355  VAL G CG2 1 
ATOM   20289 N  N   . ARG G  3 358 ? 33.751  -35.491 27.187   1.00 136.24 ? 356  ARG G N   1 
ATOM   20290 C  CA  . ARG G  3 358 ? 32.317  -35.420 27.494   1.00 135.87 ? 356  ARG G CA  1 
ATOM   20291 C  C   . ARG G  3 358 ? 32.111  -34.783 28.864   1.00 137.63 ? 356  ARG G C   1 
ATOM   20292 O  O   . ARG G  3 358 ? 31.603  -33.663 28.966   1.00 138.02 ? 356  ARG G O   1 
ATOM   20293 C  CB  . ARG G  3 358 ? 31.683  -36.813 27.426   1.00 154.85 ? 356  ARG G CB  1 
ATOM   20294 C  CG  . ARG G  3 358 ? 30.166  -36.830 27.622   1.00 162.40 ? 356  ARG G CG  1 
ATOM   20295 C  CD  . ARG G  3 358 ? 29.454  -36.094 26.497   1.00 158.08 ? 356  ARG G CD  1 
ATOM   20296 N  NE  . ARG G  3 358 ? 29.560  -36.791 25.219   1.00 170.85 ? 356  ARG G NE  1 
ATOM   20297 C  CZ  . ARG G  3 358 ? 28.986  -36.371 24.096   1.00 162.49 ? 356  ARG G CZ  1 
ATOM   20298 N  NH1 . ARG G  3 358 ? 28.276  -35.251 24.098   1.00 135.49 ? 356  ARG G NH1 1 
ATOM   20299 N  NH2 . ARG G  3 358 ? 29.128  -37.062 22.972   1.00 167.47 ? 356  ARG G NH2 1 
ATOM   20300 N  N   . SER G  3 359 ? 32.510  -35.483 29.919   1.00 138.73 ? 357  SER G N   1 
ATOM   20301 C  CA  . SER G  3 359 ? 32.328  -35.024 31.286   1.00 140.04 ? 357  SER G CA  1 
ATOM   20302 C  C   . SER G  3 359 ? 33.647  -34.526 31.852   1.00 139.64 ? 357  SER G C   1 
ATOM   20303 O  O   . SER G  3 359 ? 34.722  -34.758 31.296   1.00 138.82 ? 357  SER G O   1 
ATOM   20304 C  CB  . SER G  3 359 ? 31.776  -36.146 32.175   1.00 143.30 ? 357  SER G CB  1 
ATOM   20305 O  OG  . SER G  3 359 ? 30.578  -36.680 31.647   1.00 144.10 ? 357  SER G OG  1 
ATOM   20306 N  N   . CYS G  3 360 ? 33.545  -33.835 32.983   1.00 150.71 ? 358  CYS G N   1 
ATOM   20307 C  CA  . CYS G  3 360 ? 34.703  -33.342 33.712   1.00 154.89 ? 358  CYS G CA  1 
ATOM   20308 C  C   . CYS G  3 360 ? 34.454  -33.537 35.196   1.00 170.37 ? 358  CYS G C   1 
ATOM   20309 O  O   . CYS G  3 360 ? 33.343  -33.304 35.680   1.00 180.64 ? 358  CYS G O   1 
ATOM   20310 C  CB  . CYS G  3 360 ? 34.987  -31.859 33.432   1.00 148.57 ? 358  CYS G CB  1 
ATOM   20311 S  SG  . CYS G  3 360 ? 35.300  -31.446 31.692   1.00 149.95 ? 358  CYS G SG  1 
ATOM   20312 N  N   . LYS G  3 361 ? 35.491  -33.963 35.908   1.00 179.36 ? 359  LYS G N   1 
ATOM   20313 C  CA  . LYS G  3 361 ? 35.452  -34.204 37.342   1.00 194.47 ? 359  LYS G CA  1 
ATOM   20314 C  C   . LYS G  3 361 ? 36.554  -33.404 38.036   1.00 206.30 ? 359  LYS G C   1 
ATOM   20315 O  O   . LYS G  3 361 ? 37.376  -32.746 37.393   1.00 210.52 ? 359  LYS G O   1 
ATOM   20316 C  CB  . LYS G  3 361 ? 35.586  -35.707 37.641   1.00 178.37 ? 359  LYS G CB  1 
ATOM   20317 C  CG  . LYS G  3 361 ? 36.893  -36.335 37.158   1.00 177.30 ? 359  LYS G CG  1 
ATOM   20318 C  CD  . LYS G  3 361 ? 37.002  -37.812 37.549   1.00 189.10 ? 359  LYS G CD  1 
ATOM   20319 C  CE  . LYS G  3 361 ? 38.299  -38.442 37.027   1.00 188.07 ? 359  LYS G CE  1 
ATOM   20320 N  NZ  . LYS G  3 361 ? 38.459  -39.888 37.382   1.00 177.17 ? 359  LYS G NZ  1 
ATOM   20321 N  N   . CYS G  3 362 ? 36.560  -33.457 39.369   1.00 198.27 ? 360  CYS G N   1 
ATOM   20322 C  CA  . CYS G  3 362 ? 37.586  -32.819 40.189   1.00 185.02 ? 360  CYS G CA  1 
ATOM   20323 C  C   . CYS G  3 362 ? 38.212  -33.860 41.100   1.00 197.18 ? 360  CYS G C   1 
ATOM   20324 O  O   . CYS G  3 362 ? 37.533  -34.425 41.963   1.00 216.25 ? 360  CYS G O   1 
ATOM   20325 C  CB  . CYS G  3 362 ? 37.014  -31.678 41.024   1.00 193.74 ? 360  CYS G CB  1 
ATOM   20326 S  SG  . CYS G  3 362 ? 36.272  -30.384 40.053   1.00 228.38 ? 360  CYS G SG  1 
ATOM   20327 N  N   . SER G  3 363 ? 39.499  -34.112 40.912   1.00 195.49 ? 361  SER G N   1 
ATOM   20328 C  CA  . SER G  3 363 ? 40.190  -35.075 41.754   1.00 218.95 ? 361  SER G CA  1 
ATOM   20329 C  C   . SER G  3 363 ? 41.627  -34.629 41.970   1.00 227.11 ? 361  SER G C   1 
ATOM   20330 O  O   . SER G  3 363 ? 42.066  -33.631 41.397   1.00 216.31 ? 361  SER G O   1 
ATOM   20331 C  CB  . SER G  3 363 ? 40.136  -36.478 41.140   1.00 234.22 ? 361  SER G CB  1 
ATOM   20332 O  OG  . SER G  3 363 ? 40.666  -36.492 39.828   1.00 247.64 ? 361  SER G OG  1 
ATOM   20333 O  OXT . SER G  3 363 ? 42.371  -35.241 42.736   1.00 242.10 ? 361  SER G OXT 1 
ATOM   20334 N  N   . LYS H  3 7   ? 45.029  -17.874 38.321   1.00 207.00 ? 5    LYS H N   1 
ATOM   20335 C  CA  . LYS H  3 7   ? 44.334  -16.953 39.212   1.00 214.44 ? 5    LYS H CA  1 
ATOM   20336 C  C   . LYS H  3 7   ? 44.607  -15.519 38.777   1.00 233.07 ? 5    LYS H C   1 
ATOM   20337 O  O   . LYS H  3 7   ? 44.642  -14.603 39.601   1.00 246.88 ? 5    LYS H O   1 
ATOM   20338 C  CB  . LYS H  3 7   ? 44.773  -17.165 40.667   1.00 198.65 ? 5    LYS H CB  1 
ATOM   20339 C  CG  . LYS H  3 7   ? 43.745  -16.737 41.711   1.00 196.34 ? 5    LYS H CG  1 
ATOM   20340 C  CD  . LYS H  3 7   ? 44.382  -16.585 43.080   1.00 208.26 ? 5    LYS H CD  1 
ATOM   20341 C  CE  . LYS H  3 7   ? 45.437  -15.493 43.070   1.00 205.64 ? 5    LYS H CE  1 
ATOM   20342 N  NZ  . LYS H  3 7   ? 46.113  -15.357 44.386   1.00 211.84 ? 5    LYS H NZ  1 
ATOM   20343 N  N   . THR H  3 8   ? 44.814  -15.323 37.473   1.00 212.57 ? 6    THR H N   1 
ATOM   20344 C  CA  . THR H  3 8   ? 45.135  -13.996 36.941   1.00 202.86 ? 6    THR H CA  1 
ATOM   20345 C  C   . THR H  3 8   ? 44.424  -13.829 35.598   1.00 187.26 ? 6    THR H C   1 
ATOM   20346 O  O   . THR H  3 8   ? 44.995  -14.110 34.541   1.00 174.16 ? 6    THR H O   1 
ATOM   20347 C  CB  . THR H  3 8   ? 46.640  -13.802 36.812   1.00 202.18 ? 6    THR H CB  1 
ATOM   20348 O  OG1 . THR H  3 8   ? 47.302  -14.402 37.933   1.00 228.52 ? 6    THR H OG1 1 
ATOM   20349 C  CG2 . THR H  3 8   ? 46.975  -12.319 36.787   1.00 182.85 ? 6    THR H CG2 1 
ATOM   20350 N  N   . ILE H  3 9   ? 43.168  -13.385 35.659   1.00 199.49 ? 7    ILE H N   1 
ATOM   20351 C  CA  . ILE H  3 9   ? 42.384  -12.922 34.514   1.00 208.58 ? 7    ILE H CA  1 
ATOM   20352 C  C   . ILE H  3 9   ? 42.006  -14.037 33.537   1.00 218.84 ? 7    ILE H C   1 
ATOM   20353 O  O   . ILE H  3 9   ? 40.835  -14.150 33.155   1.00 215.89 ? 7    ILE H O   1 
ATOM   20354 C  CB  . ILE H  3 9   ? 43.108  -11.778 33.771   1.00 186.89 ? 7    ILE H CB  1 
ATOM   20355 C  CG1 . ILE H  3 9   ? 43.099  -10.483 34.593   1.00 176.12 ? 7    ILE H CG1 1 
ATOM   20356 C  CG2 . ILE H  3 9   ? 42.456  -11.516 32.438   1.00 187.58 ? 7    ILE H CG2 1 
ATOM   20357 C  CD1 . ILE H  3 9   ? 44.136  -10.400 35.679   1.00 182.41 ? 7    ILE H CD1 1 
ATOM   20358 N  N   . ASP H  3 10  ? 42.984  -14.829 33.083   1.00 200.40 ? 8    ASP H N   1 
ATOM   20359 C  CA  . ASP H  3 10  ? 42.753  -15.963 32.182   1.00 171.42 ? 8    ASP H CA  1 
ATOM   20360 C  C   . ASP H  3 10  ? 42.427  -15.488 30.767   1.00 170.33 ? 8    ASP H C   1 
ATOM   20361 O  O   . ASP H  3 10  ? 41.912  -14.380 30.574   1.00 162.23 ? 8    ASP H O   1 
ATOM   20362 C  CB  . ASP H  3 10  ? 41.676  -16.917 32.716   1.00 167.93 ? 8    ASP H CB  1 
ATOM   20363 C  CG  . ASP H  3 10  ? 42.134  -17.662 33.955   1.00 181.28 ? 8    ASP H CG  1 
ATOM   20364 O  OD1 . ASP H  3 10  ? 43.368  -17.737 34.158   1.00 198.41 ? 8    ASP H OD1 1 
ATOM   20365 O  OD2 . ASP H  3 10  ? 41.275  -18.174 34.711   1.00 180.91 ? 8    ASP H OD2 1 
ATOM   20366 N  N   . MET H  3 11  ? 42.715  -16.321 29.773   1.00 194.78 ? 9    MET H N   1 
ATOM   20367 C  CA  . MET H  3 11  ? 42.544  -15.966 28.369   1.00 175.27 ? 9    MET H CA  1 
ATOM   20368 C  C   . MET H  3 11  ? 41.660  -16.973 27.641   1.00 153.14 ? 9    MET H C   1 
ATOM   20369 O  O   . MET H  3 11  ? 41.202  -17.973 28.199   1.00 150.62 ? 9    MET H O   1 
ATOM   20370 C  CB  . MET H  3 11  ? 43.892  -15.907 27.650   1.00 198.53 ? 9    MET H CB  1 
ATOM   20371 C  CG  . MET H  3 11  ? 44.859  -14.871 28.158   1.00 230.74 ? 9    MET H CG  1 
ATOM   20372 S  SD  . MET H  3 11  ? 46.521  -15.196 27.542   1.00 278.57 ? 9    MET H SD  1 
ATOM   20373 C  CE  . MET H  3 11  ? 47.021  -16.540 28.614   1.00 243.50 ? 9    MET H CE  1 
ATOM   20374 N  N   . GLU H  3 12  ? 41.460  -16.692 26.354   1.00 178.13 ? 10   GLU H N   1 
ATOM   20375 C  CA  . GLU H  3 12  ? 40.860  -17.620 25.407   1.00 181.88 ? 10   GLU H CA  1 
ATOM   20376 C  C   . GLU H  3 12  ? 41.940  -18.434 24.722   1.00 157.54 ? 10   GLU H C   1 
ATOM   20377 O  O   . GLU H  3 12  ? 41.641  -19.279 23.873   1.00 152.22 ? 10   GLU H O   1 
ATOM   20378 C  CB  . GLU H  3 12  ? 40.041  -16.866 24.348   1.00 220.11 ? 10   GLU H CB  1 
ATOM   20379 C  CG  . GLU H  3 12  ? 38.958  -17.706 23.675   1.00 198.93 ? 10   GLU H CG  1 
ATOM   20380 C  CD  . GLU H  3 12  ? 38.382  -17.049 22.434   1.00 184.85 ? 10   GLU H CD  1 
ATOM   20381 O  OE1 . GLU H  3 12  ? 39.116  -16.960 21.427   1.00 182.19 ? 10   GLU H OE1 1 
ATOM   20382 O  OE2 . GLU H  3 12  ? 37.217  -16.598 22.472   1.00 168.19 ? 10   GLU H OE2 1 
ATOM   20383 N  N   . LEU H  3 13  ? 43.198  -18.151 25.065   1.00 169.69 ? 11   LEU H N   1 
ATOM   20384 C  CA  . LEU H  3 13  ? 44.343  -18.911 24.593   1.00 179.51 ? 11   LEU H CA  1 
ATOM   20385 C  C   . LEU H  3 13  ? 44.373  -20.300 25.205   1.00 184.84 ? 11   LEU H C   1 
ATOM   20386 O  O   . LEU H  3 13  ? 45.104  -21.172 24.719   1.00 201.66 ? 11   LEU H O   1 
ATOM   20387 C  CB  . LEU H  3 13  ? 45.628  -18.141 24.920   1.00 182.74 ? 11   LEU H CB  1 
ATOM   20388 C  CG  . LEU H  3 13  ? 47.002  -18.809 24.936   1.00 166.87 ? 11   LEU H CG  1 
ATOM   20389 C  CD1 . LEU H  3 13  ? 47.370  -19.350 23.566   1.00 164.25 ? 11   LEU H CD1 1 
ATOM   20390 C  CD2 . LEU H  3 13  ? 48.025  -17.805 25.401   1.00 177.12 ? 11   LEU H CD2 1 
ATOM   20391 N  N   . VAL H  3 14  ? 43.594  -20.518 26.263   1.00 159.34 ? 12   VAL H N   1 
ATOM   20392 C  CA  . VAL H  3 14  ? 43.477  -21.851 26.837   1.00 146.77 ? 12   VAL H CA  1 
ATOM   20393 C  C   . VAL H  3 14  ? 43.014  -22.837 25.772   1.00 155.56 ? 12   VAL H C   1 
ATOM   20394 O  O   . VAL H  3 14  ? 43.446  -23.997 25.742   1.00 171.54 ? 12   VAL H O   1 
ATOM   20395 C  CB  . VAL H  3 14  ? 42.525  -21.819 28.044   1.00 147.45 ? 12   VAL H CB  1 
ATOM   20396 C  CG1 . VAL H  3 14  ? 42.404  -23.202 28.677   1.00 147.97 ? 12   VAL H CG1 1 
ATOM   20397 C  CG2 . VAL H  3 14  ? 42.996  -20.781 29.058   1.00 160.60 ? 12   VAL H CG2 1 
ATOM   20398 N  N   . LYS H  3 15  ? 42.141  -22.380 24.868   1.00 153.60 ? 13   LYS H N   1 
ATOM   20399 C  CA  . LYS H  3 15  ? 41.683  -23.229 23.775   1.00 135.33 ? 13   LYS H CA  1 
ATOM   20400 C  C   . LYS H  3 15  ? 42.824  -23.563 22.824   1.00 136.72 ? 13   LYS H C   1 
ATOM   20401 O  O   . LYS H  3 15  ? 42.923  -24.695 22.337   1.00 145.57 ? 13   LYS H O   1 
ATOM   20402 C  CB  . LYS H  3 15  ? 40.542  -22.542 23.023   1.00 132.97 ? 13   LYS H CB  1 
ATOM   20403 C  CG  . LYS H  3 15  ? 39.344  -22.150 23.884   1.00 131.92 ? 13   LYS H CG  1 
ATOM   20404 C  CD  . LYS H  3 15  ? 38.267  -21.480 23.045   1.00 130.08 ? 13   LYS H CD  1 
ATOM   20405 C  CE  . LYS H  3 15  ? 37.045  -21.133 23.871   1.00 129.56 ? 13   LYS H CE  1 
ATOM   20406 N  NZ  . LYS H  3 15  ? 35.989  -20.522 23.023   1.00 128.97 ? 13   LYS H NZ  1 
ATOM   20407 N  N   . ARG H  3 16  ? 43.723  -22.606 22.589   1.00 135.26 ? 14   ARG H N   1 
ATOM   20408 C  CA  . ARG H  3 16  ? 44.859  -22.857 21.712   1.00 137.07 ? 14   ARG H CA  1 
ATOM   20409 C  C   . ARG H  3 16  ? 45.883  -23.769 22.367   1.00 139.09 ? 14   ARG H C   1 
ATOM   20410 O  O   . ARG H  3 16  ? 46.647  -24.436 21.658   1.00 140.45 ? 14   ARG H O   1 
ATOM   20411 C  CB  . ARG H  3 16  ? 45.511  -21.532 21.308   1.00 148.62 ? 14   ARG H CB  1 
ATOM   20412 C  CG  . ARG H  3 16  ? 44.708  -20.704 20.314   1.00 151.72 ? 14   ARG H CG  1 
ATOM   20413 C  CD  . ARG H  3 16  ? 44.489  -21.497 19.037   1.00 179.64 ? 14   ARG H CD  1 
ATOM   20414 N  NE  . ARG H  3 16  ? 45.745  -22.065 18.553   1.00 178.11 ? 14   ARG H NE  1 
ATOM   20415 C  CZ  . ARG H  3 16  ? 45.869  -22.781 17.441   1.00 155.50 ? 14   ARG H CZ  1 
ATOM   20416 N  NH1 . ARG H  3 16  ? 44.813  -23.017 16.677   1.00 146.01 ? 14   ARG H NH1 1 
ATOM   20417 N  NH2 . ARG H  3 16  ? 47.054  -23.258 17.091   1.00 157.89 ? 14   ARG H NH2 1 
ATOM   20418 N  N   . LYS H  3 17  ? 45.905  -23.808 23.704   1.00 152.75 ? 15   LYS H N   1 
ATOM   20419 C  CA  . LYS H  3 17  ? 46.769  -24.729 24.432   1.00 161.48 ? 15   LYS H CA  1 
ATOM   20420 C  C   . LYS H  3 17  ? 46.284  -26.158 24.260   1.00 156.77 ? 15   LYS H C   1 
ATOM   20421 O  O   . LYS H  3 17  ? 47.089  -27.097 24.264   1.00 150.95 ? 15   LYS H O   1 
ATOM   20422 C  CB  . LYS H  3 17  ? 46.806  -24.346 25.916   1.00 161.05 ? 15   LYS H CB  1 
ATOM   20423 C  CG  . LYS H  3 17  ? 47.710  -23.153 26.260   1.00 172.61 ? 15   LYS H CG  1 
ATOM   20424 C  CD  . LYS H  3 17  ? 47.698  -22.856 27.765   1.00 186.69 ? 15   LYS H CD  1 
ATOM   20425 C  CE  . LYS H  3 17  ? 48.658  -21.731 28.136   1.00 166.79 ? 15   LYS H CE  1 
ATOM   20426 N  NZ  . LYS H  3 17  ? 48.562  -21.362 29.576   1.00 166.74 ? 15   LYS H NZ  1 
ATOM   20427 N  N   . ARG H  3 18  ? 44.966  -26.328 24.145   1.00 144.31 ? 16   ARG H N   1 
ATOM   20428 C  CA  . ARG H  3 18  ? 44.384  -27.622 23.816   1.00 145.17 ? 16   ARG H CA  1 
ATOM   20429 C  C   . ARG H  3 18  ? 44.701  -28.011 22.377   1.00 154.39 ? 16   ARG H C   1 
ATOM   20430 O  O   . ARG H  3 18  ? 44.996  -29.178 22.094   1.00 149.76 ? 16   ARG H O   1 
ATOM   20431 C  CB  . ARG H  3 18  ? 42.873  -27.578 24.038   1.00 136.27 ? 16   ARG H CB  1 
ATOM   20432 C  CG  . ARG H  3 18  ? 42.104  -28.774 23.495   1.00 165.19 ? 16   ARG H CG  1 
ATOM   20433 C  CD  . ARG H  3 18  ? 42.151  -29.963 24.437   1.00 165.04 ? 16   ARG H CD  1 
ATOM   20434 N  NE  . ARG H  3 18  ? 41.528  -31.144 23.847   1.00 154.96 ? 16   ARG H NE  1 
ATOM   20435 C  CZ  . ARG H  3 18  ? 41.367  -32.298 24.483   1.00 159.91 ? 16   ARG H CZ  1 
ATOM   20436 N  NH1 . ARG H  3 18  ? 41.777  -32.429 25.737   1.00 199.66 ? 16   ARG H NH1 1 
ATOM   20437 N  NH2 . ARG H  3 18  ? 40.788  -33.318 23.867   1.00 152.26 ? 16   ARG H NH2 1 
ATOM   20438 N  N   . ILE H  3 19  ? 44.628  -27.047 21.454   1.00 152.82 ? 17   ILE H N   1 
ATOM   20439 C  CA  . ILE H  3 19  ? 44.866  -27.331 20.040   1.00 145.23 ? 17   ILE H CA  1 
ATOM   20440 C  C   . ILE H  3 19  ? 46.299  -27.790 19.810   1.00 148.05 ? 17   ILE H C   1 
ATOM   20441 O  O   . ILE H  3 19  ? 46.547  -28.761 19.085   1.00 137.19 ? 17   ILE H O   1 
ATOM   20442 C  CB  . ILE H  3 19  ? 44.522  -26.097 19.185   1.00 131.65 ? 17   ILE H CB  1 
ATOM   20443 C  CG1 . ILE H  3 19  ? 43.030  -25.783 19.297   1.00 128.35 ? 17   ILE H CG1 1 
ATOM   20444 C  CG2 . ILE H  3 19  ? 44.943  -26.309 17.743   1.00 134.03 ? 17   ILE H CG2 1 
ATOM   20445 C  CD1 . ILE H  3 19  ? 42.588  -24.621 18.450   1.00 141.02 ? 17   ILE H CD1 1 
ATOM   20446 N  N   . GLU H  3 20  ? 47.267  -27.106 20.424   1.00 175.09 ? 18   GLU H N   1 
ATOM   20447 C  CA  . GLU H  3 20  ? 48.658  -27.507 20.261   1.00 178.64 ? 18   GLU H CA  1 
ATOM   20448 C  C   . GLU H  3 20  ? 48.978  -28.791 21.015   1.00 164.83 ? 18   GLU H C   1 
ATOM   20449 O  O   . GLU H  3 20  ? 49.963  -29.460 20.685   1.00 147.78 ? 18   GLU H O   1 
ATOM   20450 C  CB  . GLU H  3 20  ? 49.574  -26.368 20.717   1.00 179.13 ? 18   GLU H CB  1 
ATOM   20451 C  CG  . GLU H  3 20  ? 49.599  -25.175 19.765   1.00 163.12 ? 18   GLU H CG  1 
ATOM   20452 C  CD  . GLU H  3 20  ? 50.119  -25.537 18.390   1.00 174.61 ? 18   GLU H CD  1 
ATOM   20453 O  OE1 . GLU H  3 20  ? 51.018  -26.399 18.307   1.00 185.34 ? 18   GLU H OE1 1 
ATOM   20454 O  OE2 . GLU H  3 20  ? 49.630  -24.962 17.395   1.00 176.28 ? 18   GLU H OE2 1 
ATOM   20455 N  N   . ALA H  3 21  ? 48.158  -29.154 22.004   1.00 170.35 ? 19   ALA H N   1 
ATOM   20456 C  CA  . ALA H  3 21  ? 48.302  -30.443 22.670   1.00 179.19 ? 19   ALA H CA  1 
ATOM   20457 C  C   . ALA H  3 21  ? 47.616  -31.550 21.886   1.00 181.26 ? 19   ALA H C   1 
ATOM   20458 O  O   . ALA H  3 21  ? 48.038  -32.709 21.956   1.00 177.23 ? 19   ALA H O   1 
ATOM   20459 C  CB  . ALA H  3 21  ? 47.736  -30.375 24.090   1.00 181.95 ? 19   ALA H CB  1 
ATOM   20460 N  N   . ILE H  3 22  ? 46.557  -31.208 21.150   1.00 187.40 ? 20   ILE H N   1 
ATOM   20461 C  CA  . ILE H  3 22  ? 45.922  -32.166 20.254   1.00 175.40 ? 20   ILE H CA  1 
ATOM   20462 C  C   . ILE H  3 22  ? 46.847  -32.479 19.082   1.00 153.20 ? 20   ILE H C   1 
ATOM   20463 O  O   . ILE H  3 22  ? 46.985  -33.638 18.670   1.00 144.46 ? 20   ILE H O   1 
ATOM   20464 C  CB  . ILE H  3 22  ? 44.562  -31.615 19.780   1.00 147.58 ? 20   ILE H CB  1 
ATOM   20465 C  CG1 . ILE H  3 22  ? 43.546  -31.583 20.927   1.00 132.30 ? 20   ILE H CG1 1 
ATOM   20466 C  CG2 . ILE H  3 22  ? 44.015  -32.427 18.625   1.00 168.23 ? 20   ILE H CG2 1 
ATOM   20467 C  CD1 . ILE H  3 22  ? 43.154  -32.933 21.448   1.00 133.45 ? 20   ILE H CD1 1 
ATOM   20468 N  N   . ARG H  3 23  ? 47.510  -31.450 18.546   1.00 161.05 ? 21   ARG H N   1 
ATOM   20469 C  CA  . ARG H  3 23  ? 48.422  -31.627 17.418   1.00 149.70 ? 21   ARG H CA  1 
ATOM   20470 C  C   . ARG H  3 23  ? 49.504  -32.652 17.731   1.00 153.13 ? 21   ARG H C   1 
ATOM   20471 O  O   . ARG H  3 23  ? 49.709  -33.606 16.972   1.00 160.30 ? 21   ARG H O   1 
ATOM   20472 C  CB  . ARG H  3 23  ? 49.039  -30.279 17.054   1.00 158.11 ? 21   ARG H CB  1 
ATOM   20473 C  CG  . ARG H  3 23  ? 50.142  -30.345 16.026   1.00 163.67 ? 21   ARG H CG  1 
ATOM   20474 C  CD  . ARG H  3 23  ? 50.794  -28.987 15.852   1.00 168.17 ? 21   ARG H CD  1 
ATOM   20475 N  NE  . ARG H  3 23  ? 49.881  -27.976 15.320   1.00 162.65 ? 21   ARG H NE  1 
ATOM   20476 C  CZ  . ARG H  3 23  ? 49.753  -27.692 14.029   1.00 165.34 ? 21   ARG H CZ  1 
ATOM   20477 N  NH1 . ARG H  3 23  ? 50.472  -28.350 13.131   1.00 171.28 ? 21   ARG H NH1 1 
ATOM   20478 N  NH2 . ARG H  3 23  ? 48.912  -26.750 13.635   1.00 163.38 ? 21   ARG H NH2 1 
ATOM   20479 N  N   . GLY H  3 24  ? 50.191  -32.489 18.864   1.00 174.49 ? 22   GLY H N   1 
ATOM   20480 C  CA  . GLY H  3 24  ? 51.210  -33.451 19.243   1.00 194.30 ? 22   GLY H CA  1 
ATOM   20481 C  C   . GLY H  3 24  ? 50.646  -34.780 19.688   1.00 183.34 ? 22   GLY H C   1 
ATOM   20482 O  O   . GLY H  3 24  ? 51.366  -35.785 19.681   1.00 158.90 ? 22   GLY H O   1 
ATOM   20483 N  N   . GLN H  3 25  ? 49.364  -34.808 20.055   1.00 168.04 ? 23   GLN H N   1 
ATOM   20484 C  CA  . GLN H  3 25  ? 48.733  -36.042 20.500   1.00 160.75 ? 23   GLN H CA  1 
ATOM   20485 C  C   . GLN H  3 25  ? 48.433  -36.946 19.316   1.00 155.47 ? 23   GLN H C   1 
ATOM   20486 O  O   . GLN H  3 25  ? 48.819  -38.120 19.306   1.00 157.39 ? 23   GLN H O   1 
ATOM   20487 C  CB  . GLN H  3 25  ? 47.450  -35.728 21.274   1.00 149.70 ? 23   GLN H CB  1 
ATOM   20488 C  CG  . GLN H  3 25  ? 46.799  -36.932 21.935   1.00 162.08 ? 23   GLN H CG  1 
ATOM   20489 C  CD  . GLN H  3 25  ? 45.421  -36.612 22.483   1.00 154.10 ? 23   GLN H CD  1 
ATOM   20490 O  OE1 . GLN H  3 25  ? 44.775  -35.664 22.044   1.00 143.44 ? 23   GLN H OE1 1 
ATOM   20491 N  NE2 . GLN H  3 25  ? 44.973  -37.391 23.460   1.00 180.08 ? 23   GLN H NE2 1 
ATOM   20492 N  N   . ILE H  3 26  ? 47.740  -36.409 18.310   1.00 146.46 ? 24   ILE H N   1 
ATOM   20493 C  CA  . ILE H  3 26  ? 47.391  -37.195 17.131   1.00 149.83 ? 24   ILE H CA  1 
ATOM   20494 C  C   . ILE H  3 26  ? 48.640  -37.790 16.502   1.00 166.93 ? 24   ILE H C   1 
ATOM   20495 O  O   . ILE H  3 26  ? 48.663  -38.968 16.127   1.00 189.82 ? 24   ILE H O   1 
ATOM   20496 C  CB  . ILE H  3 26  ? 46.618  -36.324 16.127   1.00 145.57 ? 24   ILE H CB  1 
ATOM   20497 C  CG1 . ILE H  3 26  ? 45.363  -35.760 16.791   1.00 140.94 ? 24   ILE H CG1 1 
ATOM   20498 C  CG2 . ILE H  3 26  ? 46.278  -37.129 14.875   1.00 166.57 ? 24   ILE H CG2 1 
ATOM   20499 C  CD1 . ILE H  3 26  ? 44.548  -34.875 15.888   1.00 139.21 ? 24   ILE H CD1 1 
ATOM   20500 N  N   . LEU H  3 27  ? 49.700  -36.992 16.382   1.00 167.79 ? 25   LEU H N   1 
ATOM   20501 C  CA  . LEU H  3 27  ? 50.922  -37.497 15.770   1.00 182.66 ? 25   LEU H CA  1 
ATOM   20502 C  C   . LEU H  3 27  ? 51.563  -38.599 16.606   1.00 191.20 ? 25   LEU H C   1 
ATOM   20503 O  O   . LEU H  3 27  ? 52.159  -39.528 16.050   1.00 210.03 ? 25   LEU H O   1 
ATOM   20504 C  CB  . LEU H  3 27  ? 51.904  -36.348 15.545   1.00 191.29 ? 25   LEU H CB  1 
ATOM   20505 C  CG  . LEU H  3 27  ? 51.444  -35.267 14.564   1.00 186.52 ? 25   LEU H CG  1 
ATOM   20506 C  CD1 . LEU H  3 27  ? 52.517  -34.204 14.425   1.00 210.67 ? 25   LEU H CD1 1 
ATOM   20507 C  CD2 . LEU H  3 27  ? 51.105  -35.866 13.208   1.00 175.94 ? 25   LEU H CD2 1 
ATOM   20508 N  N   . SER H  3 28  ? 51.436  -38.532 17.933   1.00 176.09 ? 26   SER H N   1 
ATOM   20509 C  CA  . SER H  3 28  ? 52.049  -39.552 18.777   1.00 188.41 ? 26   SER H CA  1 
ATOM   20510 C  C   . SER H  3 28  ? 51.252  -40.851 18.781   1.00 188.20 ? 26   SER H C   1 
ATOM   20511 O  O   . SER H  3 28  ? 51.844  -41.935 18.846   1.00 194.12 ? 26   SER H O   1 
ATOM   20512 C  CB  . SER H  3 28  ? 52.209  -39.026 20.203   1.00 182.34 ? 26   SER H CB  1 
ATOM   20513 O  OG  . SER H  3 28  ? 50.948  -38.761 20.789   1.00 167.25 ? 26   SER H OG  1 
ATOM   20514 N  N   . LYS H  3 29  ? 49.922  -40.768 18.696   1.00 183.90 ? 27   LYS H N   1 
ATOM   20515 C  CA  . LYS H  3 29  ? 49.115  -41.982 18.667   1.00 180.88 ? 27   LYS H CA  1 
ATOM   20516 C  C   . LYS H  3 29  ? 49.286  -42.726 17.355   1.00 185.25 ? 27   LYS H C   1 
ATOM   20517 O  O   . LYS H  3 29  ? 49.208  -43.959 17.326   1.00 195.52 ? 27   LYS H O   1 
ATOM   20518 C  CB  . LYS H  3 29  ? 47.646  -41.641 18.894   1.00 177.43 ? 27   LYS H CB  1 
ATOM   20519 C  CG  . LYS H  3 29  ? 47.355  -41.126 20.283   1.00 174.26 ? 27   LYS H CG  1 
ATOM   20520 C  CD  . LYS H  3 29  ? 45.892  -40.819 20.440   1.00 164.81 ? 27   LYS H CD  1 
ATOM   20521 C  CE  . LYS H  3 29  ? 45.573  -40.491 21.873   1.00 161.33 ? 27   LYS H CE  1 
ATOM   20522 N  NZ  . LYS H  3 29  ? 44.119  -40.293 22.048   1.00 158.74 ? 27   LYS H NZ  1 
ATOM   20523 N  N   . LEU H  3 30  ? 49.538  -42.003 16.273   1.00 194.31 ? 28   LEU H N   1 
ATOM   20524 C  CA  . LEU H  3 30  ? 49.827  -42.614 14.989   1.00 190.28 ? 28   LEU H CA  1 
ATOM   20525 C  C   . LEU H  3 30  ? 51.291  -42.987 14.865   1.00 193.95 ? 28   LEU H C   1 
ATOM   20526 O  O   . LEU H  3 30  ? 51.700  -43.504 13.818   1.00 214.19 ? 28   LEU H O   1 
ATOM   20527 C  CB  . LEU H  3 30  ? 49.431  -41.669 13.847   1.00 186.68 ? 28   LEU H CB  1 
ATOM   20528 C  CG  . LEU H  3 30  ? 47.955  -41.274 13.764   1.00 191.97 ? 28   LEU H CG  1 
ATOM   20529 C  CD1 . LEU H  3 30  ? 47.725  -40.239 12.675   1.00 209.03 ? 28   LEU H CD1 1 
ATOM   20530 C  CD2 . LEU H  3 30  ? 47.083  -42.488 13.521   1.00 186.85 ? 28   LEU H CD2 1 
ATOM   20531 N  N   . ARG H  3 31  ? 52.079  -42.728 15.912   1.00 187.20 ? 29   ARG H N   1 
ATOM   20532 C  CA  . ARG H  3 31  ? 53.515  -42.984 15.913   1.00 206.46 ? 29   ARG H CA  1 
ATOM   20533 C  C   . ARG H  3 31  ? 54.187  -42.266 14.745   1.00 217.09 ? 29   ARG H C   1 
ATOM   20534 O  O   . ARG H  3 31  ? 55.062  -42.813 14.068   1.00 252.25 ? 29   ARG H O   1 
ATOM   20535 C  CB  . ARG H  3 31  ? 53.809  -44.488 15.889   1.00 215.29 ? 29   ARG H CB  1 
ATOM   20536 C  CG  . ARG H  3 31  ? 55.180  -44.880 16.420   1.00 221.64 ? 29   ARG H CG  1 
ATOM   20537 C  CD  . ARG H  3 31  ? 55.441  -46.363 16.203   1.00 237.95 ? 29   ARG H CD  1 
ATOM   20538 N  NE  . ARG H  3 31  ? 54.549  -47.194 17.006   1.00 245.82 ? 29   ARG H NE  1 
ATOM   20539 C  CZ  . ARG H  3 31  ? 54.895  -47.764 18.156   1.00 251.67 ? 29   ARG H CZ  1 
ATOM   20540 N  NH1 . ARG H  3 31  ? 56.120  -47.601 18.638   1.00 252.27 ? 29   ARG H NH1 1 
ATOM   20541 N  NH2 . ARG H  3 31  ? 54.018  -48.503 18.821   1.00 256.60 ? 29   ARG H NH2 1 
ATOM   20542 N  N   . LEU H  3 32  ? 53.769  -41.027 14.506   1.00 193.01 ? 30   LEU H N   1 
ATOM   20543 C  CA  . LEU H  3 32  ? 54.282  -40.221 13.411   1.00 186.14 ? 30   LEU H CA  1 
ATOM   20544 C  C   . LEU H  3 32  ? 54.988  -38.991 13.962   1.00 195.41 ? 30   LEU H C   1 
ATOM   20545 O  O   . LEU H  3 32  ? 54.598  -38.439 14.995   1.00 212.51 ? 30   LEU H O   1 
ATOM   20546 C  CB  . LEU H  3 32  ? 53.155  -39.791 12.462   1.00 184.02 ? 30   LEU H CB  1 
ATOM   20547 C  CG  . LEU H  3 32  ? 52.521  -40.891 11.607   1.00 187.41 ? 30   LEU H CG  1 
ATOM   20548 C  CD1 . LEU H  3 32  ? 51.417  -40.334 10.716   1.00 182.01 ? 30   LEU H CD1 1 
ATOM   20549 C  CD2 . LEU H  3 32  ? 53.580  -41.599 10.771   1.00 226.57 ? 30   LEU H CD2 1 
ATOM   20550 N  N   . ALA H  3 33  ? 56.043  -38.573 13.268   1.00 203.32 ? 31   ALA H N   1 
ATOM   20551 C  CA  . ALA H  3 33  ? 56.753  -37.348 13.611   1.00 212.96 ? 31   ALA H CA  1 
ATOM   20552 C  C   . ALA H  3 33  ? 56.279  -36.151 12.805   1.00 201.70 ? 31   ALA H C   1 
ATOM   20553 O  O   . ALA H  3 33  ? 56.251  -35.031 13.329   1.00 187.75 ? 31   ALA H O   1 
ATOM   20554 C  CB  . ALA H  3 33  ? 58.262  -37.535 13.406   1.00 221.08 ? 31   ALA H CB  1 
ATOM   20555 N  N   . SER H  3 34  ? 55.878  -36.376 11.557   1.00 217.81 ? 32   SER H N   1 
ATOM   20556 C  CA  . SER H  3 34  ? 55.413  -35.338 10.654   1.00 218.66 ? 32   SER H CA  1 
ATOM   20557 C  C   . SER H  3 34  ? 54.305  -35.917 9.789    1.00 219.45 ? 32   SER H C   1 
ATOM   20558 O  O   . SER H  3 34  ? 54.269  -37.133 9.566    1.00 223.80 ? 32   SER H O   1 
ATOM   20559 C  CB  . SER H  3 34  ? 56.556  -34.806 9.772    1.00 235.98 ? 32   SER H CB  1 
ATOM   20560 O  OG  . SER H  3 34  ? 57.123  -35.834 8.974    1.00 250.37 ? 32   SER H OG  1 
ATOM   20561 N  N   . PRO H  3 35  ? 53.375  -35.089 9.322    1.00 207.79 ? 33   PRO H N   1 
ATOM   20562 C  CA  . PRO H  3 35  ? 52.292  -35.576 8.444    1.00 215.98 ? 33   PRO H CA  1 
ATOM   20563 C  C   . PRO H  3 35  ? 52.840  -36.196 7.170    1.00 228.65 ? 33   PRO H C   1 
ATOM   20564 O  O   . PRO H  3 35  ? 53.843  -35.718 6.619    1.00 243.21 ? 33   PRO H O   1 
ATOM   20565 C  CB  . PRO H  3 35  ? 51.490  -34.301 8.146    1.00 200.77 ? 33   PRO H CB  1 
ATOM   20566 C  CG  . PRO H  3 35  ? 51.748  -33.419 9.322    1.00 190.57 ? 33   PRO H CG  1 
ATOM   20567 C  CD  . PRO H  3 35  ? 53.170  -33.688 9.729    1.00 192.46 ? 33   PRO H CD  1 
ATOM   20568 N  N   . PRO H  3 36  ? 52.210  -37.262 6.672    1.00 222.34 ? 34   PRO H N   1 
ATOM   20569 C  CA  . PRO H  3 36  ? 52.720  -37.945 5.475    1.00 229.50 ? 34   PRO H CA  1 
ATOM   20570 C  C   . PRO H  3 36  ? 52.518  -37.116 4.215    1.00 239.18 ? 34   PRO H C   1 
ATOM   20571 O  O   . PRO H  3 36  ? 51.891  -36.054 4.217    1.00 233.48 ? 34   PRO H O   1 
ATOM   20572 C  CB  . PRO H  3 36  ? 51.897  -39.236 5.425    1.00 221.04 ? 34   PRO H CB  1 
ATOM   20573 C  CG  . PRO H  3 36  ? 50.625  -38.885 6.102    1.00 212.39 ? 34   PRO H CG  1 
ATOM   20574 C  CD  . PRO H  3 36  ? 50.977  -37.887 7.179    1.00 214.81 ? 34   PRO H CD  1 
ATOM   20575 N  N   . SER H  3 37  ? 53.058  -37.639 3.114    1.00 247.10 ? 35   SER H N   1 
ATOM   20576 C  CA  . SER H  3 37  ? 53.003  -36.955 1.831    1.00 238.97 ? 35   SER H CA  1 
ATOM   20577 C  C   . SER H  3 37  ? 51.687  -37.263 1.136    1.00 235.06 ? 35   SER H C   1 
ATOM   20578 O  O   . SER H  3 37  ? 51.251  -38.416 1.080    1.00 238.47 ? 35   SER H O   1 
ATOM   20579 C  CB  . SER H  3 37  ? 54.170  -37.380 0.933    1.00 231.22 ? 35   SER H CB  1 
ATOM   20580 O  OG  . SER H  3 37  ? 54.062  -38.743 0.552    1.00 228.40 ? 35   SER H OG  1 
ATOM   20581 N  N   . GLN H  3 38  ? 51.089  -36.228 0.553    1.00 236.80 ? 36   GLN H N   1 
ATOM   20582 C  CA  . GLN H  3 38  ? 49.787  -36.333 -0.089   1.00 240.31 ? 36   GLN H CA  1 
ATOM   20583 C  C   . GLN H  3 38  ? 49.894  -36.056 -1.584   1.00 245.60 ? 36   GLN H C   1 
ATOM   20584 O  O   . GLN H  3 38  ? 48.880  -35.881 -2.267   1.00 245.82 ? 36   GLN H O   1 
ATOM   20585 C  CB  . GLN H  3 38  ? 48.798  -35.380 0.591    1.00 242.31 ? 36   GLN H CB  1 
ATOM   20586 C  CG  . GLN H  3 38  ? 47.319  -35.657 0.336    1.00 250.49 ? 36   GLN H CG  1 
ATOM   20587 C  CD  . GLN H  3 38  ? 46.428  -34.605 0.968    1.00 246.01 ? 36   GLN H CD  1 
ATOM   20588 O  OE1 . GLN H  3 38  ? 46.918  -33.644 1.561    1.00 242.30 ? 36   GLN H OE1 1 
ATOM   20589 N  NE2 . GLN H  3 38  ? 45.116  -34.789 0.863    1.00 238.82 ? 36   GLN H NE2 1 
ATOM   20590 N  N   . GLY H  3 39  ? 51.116  -36.062 -2.104   1.00 239.26 ? 37   GLY H N   1 
ATOM   20591 C  CA  . GLY H  3 39  ? 51.364  -35.926 -3.516   1.00 238.76 ? 37   GLY H CA  1 
ATOM   20592 C  C   . GLY H  3 39  ? 51.465  -37.311 -4.113   1.00 248.50 ? 37   GLY H C   1 
ATOM   20593 O  O   . GLY H  3 39  ? 51.547  -37.456 -5.337   1.00 251.41 ? 37   GLY H O   1 
ATOM   20594 N  N   . GLU H  3 40  ? 51.438  -38.330 -3.229   1.00 254.95 ? 38   GLU H N   1 
ATOM   20595 C  CA  . GLU H  3 40  ? 51.370  -39.753 -3.569   1.00 252.26 ? 38   GLU H CA  1 
ATOM   20596 C  C   . GLU H  3 40  ? 49.939  -40.240 -3.443   1.00 242.44 ? 38   GLU H C   1 
ATOM   20597 O  O   . GLU H  3 40  ? 49.651  -41.417 -3.684   1.00 237.01 ? 38   GLU H O   1 
ATOM   20598 C  CB  . GLU H  3 40  ? 52.288  -40.614 -2.644   1.00 243.66 ? 38   GLU H CB  1 
ATOM   20599 C  CG  . GLU H  3 40  ? 52.720  -42.114 -3.228   1.00 228.84 ? 38   GLU H CG  1 
ATOM   20600 C  CD  . GLU H  3 40  ? 53.665  -43.110 -2.316   1.00 229.36 ? 38   GLU H CD  1 
ATOM   20601 O  OE1 . GLU H  3 40  ? 54.143  -42.804 -1.160   1.00 237.88 ? 38   GLU H OE1 1 
ATOM   20602 O  OE2 . GLU H  3 40  ? 53.926  -44.256 -2.790   1.00 234.66 ? 38   GLU H OE2 1 
ATOM   20603 N  N   . VAL H  3 41  ? 49.015  -39.329 -3.179   1.00 235.98 ? 39   VAL H N   1 
ATOM   20604 C  CA  . VAL H  3 41  ? 47.636  -39.716 -2.951   1.00 243.86 ? 39   VAL H CA  1 
ATOM   20605 C  C   . VAL H  3 41  ? 46.846  -39.062 -4.076   1.00 248.39 ? 39   VAL H C   1 
ATOM   20606 O  O   . VAL H  3 41  ? 47.127  -37.911 -4.444   1.00 238.62 ? 39   VAL H O   1 
ATOM   20607 C  CB  . VAL H  3 41  ? 47.176  -39.289 -1.548   1.00 243.68 ? 39   VAL H CB  1 
ATOM   20608 C  CG1 . VAL H  3 41  ? 45.741  -39.700 -1.286   1.00 240.01 ? 39   VAL H CG1 1 
ATOM   20609 C  CG2 . VAL H  3 41  ? 48.106  -39.868 -0.482   1.00 251.36 ? 39   VAL H CG2 1 
ATOM   20610 N  N   . PRO H  3 42  ? 45.884  -39.754 -4.678   1.00 260.36 ? 40   PRO H N   1 
ATOM   20611 C  CA  . PRO H  3 42  ? 45.141  -39.150 -5.768   1.00 253.08 ? 40   PRO H CA  1 
ATOM   20612 C  C   . PRO H  3 42  ? 43.939  -38.395 -5.237   1.00 248.99 ? 40   PRO H C   1 
ATOM   20613 O  O   . PRO H  3 42  ? 43.116  -38.955 -4.497   1.00 239.74 ? 40   PRO H O   1 
ATOM   20614 C  CB  . PRO H  3 42  ? 44.717  -40.354 -6.623   1.00 250.76 ? 40   PRO H CB  1 
ATOM   20615 C  CG  . PRO H  3 42  ? 44.799  -41.555 -5.707   1.00 250.62 ? 40   PRO H CG  1 
ATOM   20616 C  CD  . PRO H  3 42  ? 45.487  -41.154 -4.434   1.00 262.04 ? 40   PRO H CD  1 
ATOM   20617 N  N   . PRO H  3 43  ? 43.813  -37.115 -5.586   1.00 269.83 ? 41   PRO H N   1 
ATOM   20618 C  CA  . PRO H  3 43  ? 42.647  -36.342 -5.143   1.00 271.44 ? 41   PRO H CA  1 
ATOM   20619 C  C   . PRO H  3 43  ? 41.415  -36.724 -5.946   1.00 264.64 ? 41   PRO H C   1 
ATOM   20620 O  O   . PRO H  3 43  ? 41.463  -36.822 -7.176   1.00 267.40 ? 41   PRO H O   1 
ATOM   20621 C  CB  . PRO H  3 43  ? 43.064  -34.888 -5.400   1.00 276.26 ? 41   PRO H CB  1 
ATOM   20622 C  CG  . PRO H  3 43  ? 44.049  -34.978 -6.503   1.00 283.05 ? 41   PRO H CG  1 
ATOM   20623 C  CD  . PRO H  3 43  ? 44.790  -36.278 -6.305   1.00 278.32 ? 41   PRO H CD  1 
ATOM   20624 N  N   . GLY H  3 44  ? 40.313  -36.961 -5.241   1.00 279.33 ? 42   GLY H N   1 
ATOM   20625 C  CA  . GLY H  3 44  ? 39.054  -37.226 -5.892   1.00 273.21 ? 42   GLY H CA  1 
ATOM   20626 C  C   . GLY H  3 44  ? 38.402  -38.520 -5.450   1.00 264.09 ? 42   GLY H C   1 
ATOM   20627 O  O   . GLY H  3 44  ? 37.313  -38.513 -4.866   1.00 250.07 ? 42   GLY H O   1 
ATOM   20628 N  N   . PRO H  3 45  ? 39.053  -39.658 -5.704   1.00 259.49 ? 43   PRO H N   1 
ATOM   20629 C  CA  . PRO H  3 45  ? 38.419  -40.944 -5.380   1.00 240.30 ? 43   PRO H CA  1 
ATOM   20630 C  C   . PRO H  3 45  ? 38.290  -41.110 -3.874   1.00 222.14 ? 43   PRO H C   1 
ATOM   20631 O  O   . PRO H  3 45  ? 39.277  -41.070 -3.135   1.00 216.55 ? 43   PRO H O   1 
ATOM   20632 C  CB  . PRO H  3 45  ? 39.369  -41.979 -5.991   1.00 243.27 ? 43   PRO H CB  1 
ATOM   20633 C  CG  . PRO H  3 45  ? 40.675  -41.290 -6.085   1.00 245.79 ? 43   PRO H CG  1 
ATOM   20634 C  CD  . PRO H  3 45  ? 40.370  -39.847 -6.338   1.00 257.06 ? 43   PRO H CD  1 
ATOM   20635 N  N   . LEU H  3 46  ? 37.050  -41.283 -3.430   1.00 224.45 ? 44   LEU H N   1 
ATOM   20636 C  CA  . LEU H  3 46  ? 36.720  -41.562 -2.036   1.00 231.54 ? 44   LEU H CA  1 
ATOM   20637 C  C   . LEU H  3 46  ? 35.780  -42.758 -2.062   1.00 222.55 ? 44   LEU H C   1 
ATOM   20638 O  O   . LEU H  3 46  ? 34.557  -42.583 -2.210   1.00 224.61 ? 44   LEU H O   1 
ATOM   20639 C  CB  . LEU H  3 46  ? 36.068  -40.348 -1.387   1.00 230.03 ? 44   LEU H CB  1 
ATOM   20640 C  CG  . LEU H  3 46  ? 36.986  -39.142 -1.230   1.00 226.29 ? 44   LEU H CG  1 
ATOM   20641 C  CD1 . LEU H  3 46  ? 36.205  -37.838 -1.166   1.00 213.75 ? 44   LEU H CD1 1 
ATOM   20642 C  CD2 . LEU H  3 46  ? 37.782  -39.351 0.039    1.00 222.56 ? 44   LEU H CD2 1 
ATOM   20643 N  N   . PRO H  3 47  ? 36.297  -43.974 -1.885   1.00 200.40 ? 45   PRO H N   1 
ATOM   20644 C  CA  . PRO H  3 47  ? 35.455  -45.161 -2.074   1.00 204.28 ? 45   PRO H CA  1 
ATOM   20645 C  C   . PRO H  3 47  ? 34.345  -45.251 -1.041   1.00 210.36 ? 45   PRO H C   1 
ATOM   20646 O  O   . PRO H  3 47  ? 34.525  -44.887 0.123    1.00 216.14 ? 45   PRO H O   1 
ATOM   20647 C  CB  . PRO H  3 47  ? 36.444  -46.326 -1.931   1.00 194.33 ? 45   PRO H CB  1 
ATOM   20648 C  CG  . PRO H  3 47  ? 37.553  -45.772 -1.115   1.00 187.48 ? 45   PRO H CG  1 
ATOM   20649 C  CD  . PRO H  3 47  ? 37.681  -44.334 -1.534   1.00 188.93 ? 45   PRO H CD  1 
ATOM   20650 N  N   . GLU H  3 48  ? 33.186  -45.733 -1.487   1.00 219.45 ? 46   GLU H N   1 
ATOM   20651 C  CA  . GLU H  3 48  ? 32.081  -45.979 -0.573   1.00 219.30 ? 46   GLU H CA  1 
ATOM   20652 C  C   . GLU H  3 48  ? 32.290  -47.238 0.257    1.00 213.28 ? 46   GLU H C   1 
ATOM   20653 O  O   . GLU H  3 48  ? 31.450  -47.548 1.108    1.00 209.37 ? 46   GLU H O   1 
ATOM   20654 C  CB  . GLU H  3 48  ? 30.755  -46.067 -1.348   1.00 213.31 ? 46   GLU H CB  1 
ATOM   20655 C  CG  . GLU H  3 48  ? 30.312  -44.749 -1.977   1.00 205.37 ? 46   GLU H CG  1 
ATOM   20656 C  CD  . GLU H  3 48  ? 28.880  -44.782 -2.471   1.00 208.93 ? 46   GLU H CD  1 
ATOM   20657 O  OE1 . GLU H  3 48  ? 28.306  -45.887 -2.582   1.00 213.11 ? 46   GLU H OE1 1 
ATOM   20658 O  OE2 . GLU H  3 48  ? 28.331  -43.694 -2.750   1.00 209.39 ? 46   GLU H OE2 1 
ATOM   20659 N  N   . ALA H  3 49  ? 33.388  -47.966 0.032    1.00 205.17 ? 47   ALA H N   1 
ATOM   20660 C  CA  . ALA H  3 49  ? 33.718  -49.113 0.869    1.00 191.04 ? 47   ALA H CA  1 
ATOM   20661 C  C   . ALA H  3 49  ? 34.315  -48.665 2.197    1.00 191.28 ? 47   ALA H C   1 
ATOM   20662 O  O   . ALA H  3 49  ? 34.062  -49.285 3.235    1.00 190.66 ? 47   ALA H O   1 
ATOM   20663 C  CB  . ALA H  3 49  ? 34.675  -50.056 0.139    1.00 191.84 ? 47   ALA H CB  1 
ATOM   20664 N  N   . VAL H  3 50  ? 35.124  -47.603 2.180    1.00 186.25 ? 48   VAL H N   1 
ATOM   20665 C  CA  . VAL H  3 50  ? 35.663  -47.066 3.424    1.00 184.54 ? 48   VAL H CA  1 
ATOM   20666 C  C   . VAL H  3 50  ? 34.670  -46.132 4.101    1.00 186.84 ? 48   VAL H C   1 
ATOM   20667 O  O   . VAL H  3 50  ? 34.790  -45.880 5.307    1.00 187.24 ? 48   VAL H O   1 
ATOM   20668 C  CB  . VAL H  3 50  ? 37.005  -46.353 3.183    1.00 186.05 ? 48   VAL H CB  1 
ATOM   20669 C  CG1 . VAL H  3 50  ? 37.994  -47.288 2.494    1.00 183.82 ? 48   VAL H CG1 1 
ATOM   20670 C  CG2 . VAL H  3 50  ? 36.809  -45.085 2.370    1.00 193.15 ? 48   VAL H CG2 1 
ATOM   20671 N  N   . LEU H  3 51  ? 33.677  -45.630 3.359    1.00 194.39 ? 49   LEU H N   1 
ATOM   20672 C  CA  . LEU H  3 51  ? 32.632  -44.815 3.968    1.00 203.87 ? 49   LEU H CA  1 
ATOM   20673 C  C   . LEU H  3 51  ? 31.677  -45.660 4.798    1.00 209.75 ? 49   LEU H C   1 
ATOM   20674 O  O   . LEU H  3 51  ? 31.097  -45.160 5.765    1.00 221.01 ? 49   LEU H O   1 
ATOM   20675 C  CB  . LEU H  3 51  ? 31.863  -44.045 2.891    1.00 224.29 ? 49   LEU H CB  1 
ATOM   20676 C  CG  . LEU H  3 51  ? 32.584  -42.883 2.198    1.00 241.91 ? 49   LEU H CG  1 
ATOM   20677 C  CD1 . LEU H  3 51  ? 31.651  -42.156 1.236    1.00 253.85 ? 49   LEU H CD1 1 
ATOM   20678 C  CD2 . LEU H  3 51  ? 33.151  -41.912 3.224    1.00 235.65 ? 49   LEU H CD2 1 
ATOM   20679 N  N   . ALA H  3 52  ? 31.493  -46.933 4.436    1.00 194.55 ? 50   ALA H N   1 
ATOM   20680 C  CA  . ALA H  3 52  ? 30.705  -47.827 5.276    1.00 185.42 ? 50   ALA H CA  1 
ATOM   20681 C  C   . ALA H  3 52  ? 31.462  -48.194 6.545    1.00 181.16 ? 50   ALA H C   1 
ATOM   20682 O  O   . ALA H  3 52  ? 30.841  -48.448 7.584    1.00 178.78 ? 50   ALA H O   1 
ATOM   20683 C  CB  . ALA H  3 52  ? 30.309  -49.082 4.497    1.00 186.92 ? 50   ALA H CB  1 
ATOM   20684 N  N   . LEU H  3 53  ? 32.796  -48.245 6.474    1.00 180.61 ? 51   LEU H N   1 
ATOM   20685 C  CA  . LEU H  3 53  ? 33.599  -48.447 7.675    1.00 177.34 ? 51   LEU H CA  1 
ATOM   20686 C  C   . LEU H  3 53  ? 33.464  -47.263 8.617    1.00 180.64 ? 51   LEU H C   1 
ATOM   20687 O  O   . LEU H  3 53  ? 33.209  -47.432 9.815    1.00 184.36 ? 51   LEU H O   1 
ATOM   20688 C  CB  . LEU H  3 53  ? 35.068  -48.651 7.304    1.00 176.29 ? 51   LEU H CB  1 
ATOM   20689 C  CG  . LEU H  3 53  ? 35.607  -50.072 7.169    1.00 182.40 ? 51   LEU H CG  1 
ATOM   20690 C  CD1 . LEU H  3 53  ? 36.987  -50.038 6.535    1.00 206.35 ? 51   LEU H CD1 1 
ATOM   20691 C  CD2 . LEU H  3 53  ? 35.663  -50.741 8.532    1.00 163.26 ? 51   LEU H CD2 1 
ATOM   20692 N  N   . TYR H  3 54  ? 33.619  -46.049 8.084    1.00 166.72 ? 52   TYR H N   1 
ATOM   20693 C  CA  . TYR H  3 54  ? 33.530  -44.853 8.910    1.00 171.20 ? 52   TYR H CA  1 
ATOM   20694 C  C   . TYR H  3 54  ? 32.120  -44.660 9.458    1.00 192.72 ? 52   TYR H C   1 
ATOM   20695 O  O   . TYR H  3 54  ? 31.951  -44.152 10.574   1.00 194.84 ? 52   TYR H O   1 
ATOM   20696 C  CB  . TYR H  3 54  ? 33.971  -43.637 8.093    1.00 167.64 ? 52   TYR H CB  1 
ATOM   20697 C  CG  . TYR H  3 54  ? 34.095  -42.340 8.867    1.00 170.13 ? 52   TYR H CG  1 
ATOM   20698 C  CD1 . TYR H  3 54  ? 35.166  -42.117 9.727    1.00 176.01 ? 52   TYR H CD1 1 
ATOM   20699 C  CD2 . TYR H  3 54  ? 33.147  -41.333 8.731    1.00 162.91 ? 52   TYR H CD2 1 
ATOM   20700 C  CE1 . TYR H  3 54  ? 35.283  -40.928 10.431   1.00 171.36 ? 52   TYR H CE1 1 
ATOM   20701 C  CE2 . TYR H  3 54  ? 33.258  -40.144 9.431    1.00 159.89 ? 52   TYR H CE2 1 
ATOM   20702 C  CZ  . TYR H  3 54  ? 34.326  -39.948 10.278   1.00 157.96 ? 52   TYR H CZ  1 
ATOM   20703 O  OH  . TYR H  3 54  ? 34.441  -38.770 10.974   1.00 155.91 ? 52   TYR H OH  1 
ATOM   20704 N  N   . ASN H  3 55  ? 31.100  -45.077 8.699    1.00 203.61 ? 53   ASN H N   1 
ATOM   20705 C  CA  . ASN H  3 55  ? 29.718  -44.946 9.148    1.00 212.76 ? 53   ASN H CA  1 
ATOM   20706 C  C   . ASN H  3 55  ? 29.375  -45.960 10.227   1.00 214.51 ? 53   ASN H C   1 
ATOM   20707 O  O   . ASN H  3 55  ? 28.485  -45.701 11.045   1.00 209.63 ? 53   ASN H O   1 
ATOM   20708 C  CB  . ASN H  3 55  ? 28.768  -45.102 7.956    1.00 212.64 ? 53   ASN H CB  1 
ATOM   20709 C  CG  . ASN H  3 55  ? 28.777  -43.891 7.031    1.00 212.57 ? 53   ASN H CG  1 
ATOM   20710 O  OD1 . ASN H  3 55  ? 29.523  -42.933 7.247    1.00 185.13 ? 53   ASN H OD1 1 
ATOM   20711 N  ND2 . ASN H  3 55  ? 27.968  -43.942 5.983    1.00 260.90 ? 53   ASN H ND2 1 
ATOM   20712 N  N   . SER H  3 56  ? 30.072  -47.094 10.258   1.00 209.90 ? 54   SER H N   1 
ATOM   20713 C  CA  . SER H  3 56  ? 29.841  -48.099 11.282   1.00 192.17 ? 54   SER H CA  1 
ATOM   20714 C  C   . SER H  3 56  ? 30.629  -47.814 12.552   1.00 190.88 ? 54   SER H C   1 
ATOM   20715 O  O   . SER H  3 56  ? 30.231  -48.272 13.629   1.00 196.80 ? 54   SER H O   1 
ATOM   20716 C  CB  . SER H  3 56  ? 30.199  -49.489 10.741   1.00 177.12 ? 54   SER H CB  1 
ATOM   20717 O  OG  . SER H  3 56  ? 31.537  -49.524 10.274   1.00 167.10 ? 54   SER H OG  1 
ATOM   20718 N  N   . THR H  3 57  ? 31.712  -47.036 12.456   1.00 181.91 ? 55   THR H N   1 
ATOM   20719 C  CA  . THR H  3 57  ? 32.486  -46.666 13.635   1.00 168.83 ? 55   THR H CA  1 
ATOM   20720 C  C   . THR H  3 57  ? 31.863  -45.490 14.359   1.00 165.95 ? 55   THR H C   1 
ATOM   20721 O  O   . THR H  3 57  ? 32.011  -45.371 15.580   1.00 173.50 ? 55   THR H O   1 
ATOM   20722 C  CB  . THR H  3 57  ? 33.930  -46.327 13.267   1.00 173.63 ? 55   THR H CB  1 
ATOM   20723 O  OG1 . THR H  3 57  ? 33.944  -45.318 12.251   1.00 190.80 ? 55   THR H OG1 1 
ATOM   20724 C  CG2 . THR H  3 57  ? 34.651  -47.562 12.771   1.00 170.74 ? 55   THR H CG2 1 
ATOM   20725 N  N   . ARG H  3 58  ? 31.199  -44.593 13.632   1.00 164.98 ? 56   ARG H N   1 
ATOM   20726 C  CA  . ARG H  3 58  ? 30.509  -43.521 14.322   1.00 163.68 ? 56   ARG H CA  1 
ATOM   20727 C  C   . ARG H  3 58  ? 29.249  -44.040 14.992   1.00 173.18 ? 56   ARG H C   1 
ATOM   20728 O  O   . ARG H  3 58  ? 28.711  -43.376 15.884   1.00 194.53 ? 56   ARG H O   1 
ATOM   20729 C  CB  . ARG H  3 58  ? 30.175  -42.391 13.347   1.00 175.91 ? 56   ARG H CB  1 
ATOM   20730 C  CG  . ARG H  3 58  ? 31.389  -41.710 12.738   1.00 172.71 ? 56   ARG H CG  1 
ATOM   20731 C  CD  . ARG H  3 58  ? 31.010  -40.341 12.209   1.00 175.81 ? 56   ARG H CD  1 
ATOM   20732 N  NE  . ARG H  3 58  ? 30.039  -40.433 11.126   1.00 179.03 ? 56   ARG H NE  1 
ATOM   20733 C  CZ  . ARG H  3 58  ? 29.160  -39.482 10.830   1.00 181.36 ? 56   ARG H CZ  1 
ATOM   20734 N  NH1 . ARG H  3 58  ? 29.123  -38.361 11.540   1.00 180.45 ? 56   ARG H NH1 1 
ATOM   20735 N  NH2 . ARG H  3 58  ? 28.313  -39.652 9.824    1.00 185.40 ? 56   ARG H NH2 1 
ATOM   20736 N  N   . ASP H  3 59  ? 28.781  -45.217 14.588   1.00 182.12 ? 57   ASP H N   1 
ATOM   20737 C  CA  . ASP H  3 59  ? 27.619  -45.856 15.196   1.00 201.36 ? 57   ASP H CA  1 
ATOM   20738 C  C   . ASP H  3 59  ? 28.086  -46.578 16.453   1.00 197.81 ? 57   ASP H C   1 
ATOM   20739 O  O   . ASP H  3 59  ? 28.606  -47.696 16.384   1.00 200.54 ? 57   ASP H O   1 
ATOM   20740 C  CB  . ASP H  3 59  ? 26.958  -46.823 14.224   1.00 214.78 ? 57   ASP H CB  1 
ATOM   20741 C  CG  . ASP H  3 59  ? 25.597  -47.288 14.705   1.00 236.35 ? 57   ASP H CG  1 
ATOM   20742 O  OD1 . ASP H  3 59  ? 25.283  -47.108 15.905   1.00 226.45 ? 57   ASP H OD1 1 
ATOM   20743 O  OD2 . ASP H  3 59  ? 24.845  -47.850 13.883   1.00 256.82 ? 57   ASP H OD2 1 
ATOM   20744 N  N   . ARG H  3 60  ? 27.890  -45.956 17.613   1.00 196.84 ? 58   ARG H N   1 
ATOM   20745 C  CA  . ARG H  3 60  ? 28.314  -46.543 18.883   1.00 198.72 ? 58   ARG H CA  1 
ATOM   20746 C  C   . ARG H  3 60  ? 27.119  -47.267 19.487   1.00 216.06 ? 58   ARG H C   1 
ATOM   20747 O  O   . ARG H  3 60  ? 26.289  -46.675 20.176   1.00 224.05 ? 58   ARG H O   1 
ATOM   20748 C  CB  . ARG H  3 60  ? 28.873  -45.481 19.814   1.00 185.24 ? 58   ARG H CB  1 
ATOM   20749 C  CG  . ARG H  3 60  ? 30.129  -44.851 19.274   1.00 176.89 ? 58   ARG H CG  1 
ATOM   20750 C  CD  . ARG H  3 60  ? 30.572  -43.688 20.115   1.00 193.07 ? 58   ARG H CD  1 
ATOM   20751 N  NE  . ARG H  3 60  ? 31.687  -42.995 19.485   1.00 212.88 ? 58   ARG H NE  1 
ATOM   20752 C  CZ  . ARG H  3 60  ? 32.189  -41.849 19.925   1.00 227.42 ? 58   ARG H CZ  1 
ATOM   20753 N  NH1 . ARG H  3 60  ? 31.667  -41.271 20.999   1.00 231.59 ? 58   ARG H NH1 1 
ATOM   20754 N  NH2 . ARG H  3 60  ? 33.208  -41.282 19.292   1.00 229.92 ? 58   ARG H NH2 1 
ATOM   20755 N  N   . VAL H  3 61  ? 27.038  -48.567 19.218   1.00 196.18 ? 59   VAL H N   1 
ATOM   20756 C  CA  . VAL H  3 61  ? 25.981  -49.381 19.792   1.00 191.10 ? 59   VAL H CA  1 
ATOM   20757 C  C   . VAL H  3 61  ? 26.200  -49.507 21.293   1.00 204.05 ? 59   VAL H C   1 
ATOM   20758 O  O   . VAL H  3 61  ? 27.315  -49.783 21.755   1.00 197.42 ? 59   VAL H O   1 
ATOM   20759 C  CB  . VAL H  3 61  ? 25.939  -50.759 19.123   1.00 167.40 ? 59   VAL H CB  1 
ATOM   20760 C  CG1 . VAL H  3 61  ? 24.757  -51.534 19.656   1.00 159.08 ? 59   VAL H CG1 1 
ATOM   20761 C  CG2 . VAL H  3 61  ? 25.888  -50.606 17.614   1.00 158.99 ? 59   VAL H CG2 1 
ATOM   20762 N  N   . ALA H  3 62  ? 25.136  -49.305 22.062   1.00 219.56 ? 60   ALA H N   1 
ATOM   20763 C  CA  . ALA H  3 62  ? 25.236  -49.462 23.500   1.00 207.85 ? 60   ALA H CA  1 
ATOM   20764 C  C   . ALA H  3 62  ? 25.452  -50.930 23.856   1.00 202.98 ? 60   ALA H C   1 
ATOM   20765 O  O   . ALA H  3 62  ? 25.042  -51.843 23.130   1.00 166.14 ? 60   ALA H O   1 
ATOM   20766 C  CB  . ALA H  3 62  ? 23.982  -48.917 24.189   1.00 192.34 ? 60   ALA H CB  1 
ATOM   20767 N  N   . GLY H  3 63  ? 26.136  -51.148 24.974   1.00 197.38 ? 61   GLY H N   1 
ATOM   20768 C  CA  . GLY H  3 63  ? 26.431  -52.488 25.439   1.00 178.05 ? 61   GLY H CA  1 
ATOM   20769 C  C   . GLY H  3 63  ? 26.563  -52.568 26.945   1.00 149.84 ? 61   GLY H C   1 
ATOM   20770 O  O   . GLY H  3 63  ? 25.857  -53.338 27.594   1.00 149.78 ? 61   GLY H O   1 
ATOM   20771 N  N   . PRO H  3 72  ? 46.731  -50.177 28.866   1.00 177.59 ? 70   PRO H N   1 
ATOM   20772 C  CA  . PRO H  3 72  ? 48.177  -50.033 29.060   1.00 193.68 ? 70   PRO H CA  1 
ATOM   20773 C  C   . PRO H  3 72  ? 48.852  -49.224 27.957   1.00 204.79 ? 70   PRO H C   1 
ATOM   20774 O  O   . PRO H  3 72  ? 48.243  -48.317 27.386   1.00 182.03 ? 70   PRO H O   1 
ATOM   20775 C  CB  . PRO H  3 72  ? 48.675  -51.482 29.055   1.00 187.36 ? 70   PRO H CB  1 
ATOM   20776 C  CG  . PRO H  3 72  ? 47.510  -52.271 29.531   1.00 183.60 ? 70   PRO H CG  1 
ATOM   20777 C  CD  . PRO H  3 72  ? 46.297  -51.580 28.977   1.00 176.54 ? 70   PRO H CD  1 
ATOM   20778 N  N   . GLU H  3 73  ? 50.114  -49.557 27.669   1.00 242.98 ? 71   GLU H N   1 
ATOM   20779 C  CA  . GLU H  3 73  ? 50.854  -48.830 26.645   1.00 248.16 ? 71   GLU H CA  1 
ATOM   20780 C  C   . GLU H  3 73  ? 50.339  -49.145 25.248   1.00 238.72 ? 71   GLU H C   1 
ATOM   20781 O  O   . GLU H  3 73  ? 50.483  -48.322 24.338   1.00 243.01 ? 71   GLU H O   1 
ATOM   20782 C  CB  . GLU H  3 73  ? 52.349  -49.145 26.740   1.00 245.35 ? 71   GLU H CB  1 
ATOM   20783 C  CG  . GLU H  3 73  ? 53.066  -48.455 27.894   1.00 252.67 ? 71   GLU H CG  1 
ATOM   20784 C  CD  . GLU H  3 73  ? 52.763  -49.087 29.241   1.00 261.22 ? 71   GLU H CD  1 
ATOM   20785 O  OE1 . GLU H  3 73  ? 52.266  -50.234 29.263   1.00 265.59 ? 71   GLU H OE1 1 
ATOM   20786 O  OE2 . GLU H  3 73  ? 53.020  -48.438 30.278   1.00 258.88 ? 71   GLU H OE2 1 
ATOM   20787 N  N   . ALA H  3 74  ? 49.738  -50.320 25.053   1.00 216.86 ? 72   ALA H N   1 
ATOM   20788 C  CA  . ALA H  3 74  ? 49.247  -50.671 23.729   1.00 203.84 ? 72   ALA H CA  1 
ATOM   20789 C  C   . ALA H  3 74  ? 47.843  -50.144 23.472   1.00 195.41 ? 72   ALA H C   1 
ATOM   20790 O  O   . ALA H  3 74  ? 47.408  -50.115 22.314   1.00 192.46 ? 72   ALA H O   1 
ATOM   20791 C  CB  . ALA H  3 74  ? 49.277  -52.191 23.545   1.00 209.70 ? 72   ALA H CB  1 
ATOM   20792 N  N   . ASP H  3 75  ? 47.135  -49.721 24.515   1.00 204.27 ? 73   ASP H N   1 
ATOM   20793 C  CA  . ASP H  3 75  ? 45.766  -49.246 24.388   1.00 211.94 ? 73   ASP H CA  1 
ATOM   20794 C  C   . ASP H  3 75  ? 45.673  -47.748 24.113   1.00 195.84 ? 73   ASP H C   1 
ATOM   20795 O  O   . ASP H  3 75  ? 44.580  -47.251 23.819   1.00 190.65 ? 73   ASP H O   1 
ATOM   20796 C  CB  . ASP H  3 75  ? 44.985  -49.596 25.661   1.00 221.75 ? 73   ASP H CB  1 
ATOM   20797 C  CG  . ASP H  3 75  ? 43.492  -49.433 25.491   1.00 222.09 ? 73   ASP H CG  1 
ATOM   20798 O  OD1 . ASP H  3 75  ? 42.999  -49.643 24.361   1.00 220.71 ? 73   ASP H OD1 1 
ATOM   20799 O  OD2 . ASP H  3 75  ? 42.813  -49.107 26.488   1.00 224.13 ? 73   ASP H OD2 1 
ATOM   20800 N  N   . TYR H  3 76  ? 46.785  -47.019 24.187   1.00 177.28 ? 74   TYR H N   1 
ATOM   20801 C  CA  . TYR H  3 76  ? 46.778  -45.581 23.952   1.00 177.38 ? 74   TYR H CA  1 
ATOM   20802 C  C   . TYR H  3 76  ? 47.031  -45.213 22.496   1.00 183.38 ? 74   TYR H C   1 
ATOM   20803 O  O   . TYR H  3 76  ? 46.600  -44.141 22.055   1.00 183.94 ? 74   TYR H O   1 
ATOM   20804 C  CB  . TYR H  3 76  ? 47.826  -44.909 24.851   1.00 181.79 ? 74   TYR H CB  1 
ATOM   20805 C  CG  . TYR H  3 76  ? 48.291  -43.539 24.398   1.00 192.66 ? 74   TYR H CG  1 
ATOM   20806 C  CD1 . TYR H  3 76  ? 47.553  -42.400 24.697   1.00 194.71 ? 74   TYR H CD1 1 
ATOM   20807 C  CD2 . TYR H  3 76  ? 49.480  -43.385 23.693   1.00 188.61 ? 74   TYR H CD2 1 
ATOM   20808 C  CE1 . TYR H  3 76  ? 47.981  -41.150 24.299   1.00 189.44 ? 74   TYR H CE1 1 
ATOM   20809 C  CE2 . TYR H  3 76  ? 49.914  -42.139 23.290   1.00 188.48 ? 74   TYR H CE2 1 
ATOM   20810 C  CZ  . TYR H  3 76  ? 49.161  -41.028 23.595   1.00 186.25 ? 74   TYR H CZ  1 
ATOM   20811 O  OH  . TYR H  3 76  ? 49.596  -39.789 23.194   1.00 185.50 ? 74   TYR H OH  1 
ATOM   20812 N  N   . TYR H  3 77  ? 47.700  -46.075 21.740   1.00 186.06 ? 75   TYR H N   1 
ATOM   20813 C  CA  . TYR H  3 77  ? 47.986  -45.792 20.345   1.00 188.02 ? 75   TYR H CA  1 
ATOM   20814 C  C   . TYR H  3 77  ? 46.746  -46.048 19.486   1.00 178.19 ? 75   TYR H C   1 
ATOM   20815 O  O   . TYR H  3 77  ? 45.697  -46.493 19.963   1.00 164.59 ? 75   TYR H O   1 
ATOM   20816 C  CB  . TYR H  3 77  ? 49.193  -46.609 19.888   1.00 194.46 ? 75   TYR H CB  1 
ATOM   20817 C  CG  . TYR H  3 77  ? 50.487  -46.177 20.552   1.00 199.62 ? 75   TYR H CG  1 
ATOM   20818 C  CD1 . TYR H  3 77  ? 51.279  -45.175 20.003   1.00 212.95 ? 75   TYR H CD1 1 
ATOM   20819 C  CD2 . TYR H  3 77  ? 50.899  -46.754 21.744   1.00 191.19 ? 75   TYR H CD2 1 
ATOM   20820 C  CE1 . TYR H  3 77  ? 52.458  -44.779 20.617   1.00 217.10 ? 75   TYR H CE1 1 
ATOM   20821 C  CE2 . TYR H  3 77  ? 52.070  -46.363 22.364   1.00 192.31 ? 75   TYR H CE2 1 
ATOM   20822 C  CZ  . TYR H  3 77  ? 52.846  -45.377 21.801   1.00 200.22 ? 75   TYR H CZ  1 
ATOM   20823 O  OH  . TYR H  3 77  ? 54.012  -44.994 22.426   1.00 198.22 ? 75   TYR H OH  1 
ATOM   20824 N  N   . ALA H  3 78  ? 46.868  -45.745 18.196   1.00 187.40 ? 76   ALA H N   1 
ATOM   20825 C  CA  . ALA H  3 78  ? 45.755  -45.851 17.267   1.00 192.84 ? 76   ALA H CA  1 
ATOM   20826 C  C   . ALA H  3 78  ? 45.559  -47.292 16.809   1.00 199.74 ? 76   ALA H C   1 
ATOM   20827 O  O   . ALA H  3 78  ? 46.486  -48.108 16.809   1.00 220.03 ? 76   ALA H O   1 
ATOM   20828 C  CB  . ALA H  3 78  ? 45.984  -44.952 16.053   1.00 201.88 ? 76   ALA H CB  1 
ATOM   20829 N  N   . LYS H  3 79  ? 44.331  -47.596 16.394   1.00 183.28 ? 77   LYS H N   1 
ATOM   20830 C  CA  . LYS H  3 79  ? 43.963  -48.926 15.929   1.00 177.93 ? 77   LYS H CA  1 
ATOM   20831 C  C   . LYS H  3 79  ? 43.371  -48.832 14.529   1.00 186.95 ? 77   LYS H C   1 
ATOM   20832 O  O   . LYS H  3 79  ? 42.424  -48.071 14.302   1.00 189.33 ? 77   LYS H O   1 
ATOM   20833 C  CB  . LYS H  3 79  ? 42.967  -49.583 16.890   1.00 164.03 ? 77   LYS H CB  1 
ATOM   20834 C  CG  . LYS H  3 79  ? 43.380  -49.502 18.353   1.00 172.84 ? 77   LYS H CG  1 
ATOM   20835 C  CD  . LYS H  3 79  ? 44.665  -50.273 18.608   1.00 179.06 ? 77   LYS H CD  1 
ATOM   20836 C  CE  . LYS H  3 79  ? 45.068  -50.210 20.070   1.00 170.00 ? 77   LYS H CE  1 
ATOM   20837 N  NZ  . LYS H  3 79  ? 46.344  -50.939 20.315   1.00 171.45 ? 77   LYS H NZ  1 
ATOM   20838 N  N   . GLU H  3 80  ? 43.919  -49.619 13.601   1.00 195.93 ? 78   GLU H N   1 
ATOM   20839 C  CA  . GLU H  3 80  ? 43.456  -49.635 12.215   1.00 187.40 ? 78   GLU H CA  1 
ATOM   20840 C  C   . GLU H  3 80  ? 42.152  -50.417 12.138   1.00 176.96 ? 78   GLU H C   1 
ATOM   20841 O  O   . GLU H  3 80  ? 42.131  -51.631 12.360   1.00 168.74 ? 78   GLU H O   1 
ATOM   20842 C  CB  . GLU H  3 80  ? 44.517  -50.248 11.305   1.00 193.79 ? 78   GLU H CB  1 
ATOM   20843 C  CG  . GLU H  3 80  ? 44.102  -50.325 9.841    1.00 211.66 ? 78   GLU H CG  1 
ATOM   20844 C  CD  . GLU H  3 80  ? 45.206  -50.845 8.938    1.00 218.08 ? 78   GLU H CD  1 
ATOM   20845 O  OE1 . GLU H  3 80  ? 46.372  -50.893 9.388    1.00 218.05 ? 78   GLU H OE1 1 
ATOM   20846 O  OE2 . GLU H  3 80  ? 44.906  -51.207 7.779    1.00 221.36 ? 78   GLU H OE2 1 
ATOM   20847 N  N   . VAL H  3 81  ? 41.067  -49.729 11.806   1.00 164.69 ? 79   VAL H N   1 
ATOM   20848 C  CA  . VAL H  3 81  ? 39.738  -50.327 11.789   1.00 165.87 ? 79   VAL H CA  1 
ATOM   20849 C  C   . VAL H  3 81  ? 39.428  -50.859 10.395   1.00 163.99 ? 79   VAL H C   1 
ATOM   20850 O  O   . VAL H  3 81  ? 39.433  -50.108 9.414    1.00 175.87 ? 79   VAL H O   1 
ATOM   20851 C  CB  . VAL H  3 81  ? 38.672  -49.322 12.240   1.00 186.55 ? 79   VAL H CB  1 
ATOM   20852 C  CG1 . VAL H  3 81  ? 37.293  -49.951 12.149   1.00 202.01 ? 79   VAL H CG1 1 
ATOM   20853 C  CG2 . VAL H  3 81  ? 38.959  -48.860 13.660   1.00 182.11 ? 79   VAL H CG2 1 
ATOM   20854 N  N   . THR H  3 82  ? 39.148  -52.155 10.317   1.00 150.97 ? 80   THR H N   1 
ATOM   20855 C  CA  . THR H  3 82  ? 38.716  -52.814 9.096    1.00 150.32 ? 80   THR H CA  1 
ATOM   20856 C  C   . THR H  3 82  ? 37.537  -53.719 9.419    1.00 145.41 ? 80   THR H C   1 
ATOM   20857 O  O   . THR H  3 82  ? 37.380  -54.167 10.555   1.00 151.92 ? 80   THR H O   1 
ATOM   20858 C  CB  . THR H  3 82  ? 39.853  -53.632 8.474    1.00 149.78 ? 80   THR H CB  1 
ATOM   20859 O  OG1 . THR H  3 82  ? 40.439  -54.474 9.477    1.00 145.03 ? 80   THR H OG1 1 
ATOM   20860 C  CG2 . THR H  3 82  ? 40.923  -52.714 7.892    1.00 161.37 ? 80   THR H CG2 1 
ATOM   20861 N  N   . ARG H  3 83  ? 36.703  -53.987 8.420    1.00 153.07 ? 81   ARG H N   1 
ATOM   20862 C  CA  . ARG H  3 83  ? 35.546  -54.847 8.614    1.00 149.45 ? 81   ARG H CA  1 
ATOM   20863 C  C   . ARG H  3 83  ? 35.528  -55.927 7.544    1.00 149.85 ? 81   ARG H C   1 
ATOM   20864 O  O   . ARG H  3 83  ? 36.186  -55.815 6.508    1.00 152.96 ? 81   ARG H O   1 
ATOM   20865 C  CB  . ARG H  3 83  ? 34.234  -54.057 8.578    1.00 153.76 ? 81   ARG H CB  1 
ATOM   20866 C  CG  . ARG H  3 83  ? 33.734  -53.747 7.184    1.00 166.22 ? 81   ARG H CG  1 
ATOM   20867 C  CD  . ARG H  3 83  ? 32.354  -53.112 7.219    1.00 169.44 ? 81   ARG H CD  1 
ATOM   20868 N  NE  . ARG H  3 83  ? 31.767  -53.012 5.886    1.00 193.04 ? 81   ARG H NE  1 
ATOM   20869 C  CZ  . ARG H  3 83  ? 30.554  -52.526 5.631    1.00 199.54 ? 81   ARG H CZ  1 
ATOM   20870 N  NH1 . ARG H  3 83  ? 29.791  -52.082 6.625    1.00 207.44 ? 81   ARG H NH1 1 
ATOM   20871 N  NH2 . ARG H  3 83  ? 30.109  -52.477 4.381    1.00 189.77 ? 81   ARG H NH2 1 
ATOM   20872 N  N   . VAL H  3 84  ? 34.768  -56.985 7.809    1.00 131.47 ? 82   VAL H N   1 
ATOM   20873 C  CA  . VAL H  3 84  ? 34.598  -58.085 6.866    1.00 133.70 ? 82   VAL H CA  1 
ATOM   20874 C  C   . VAL H  3 84  ? 33.147  -58.534 6.912    1.00 133.31 ? 82   VAL H C   1 
ATOM   20875 O  O   . VAL H  3 84  ? 32.611  -58.821 7.988    1.00 131.52 ? 82   VAL H O   1 
ATOM   20876 C  CB  . VAL H  3 84  ? 35.541  -59.268 7.166    1.00 134.61 ? 82   VAL H CB  1 
ATOM   20877 C  CG1 . VAL H  3 84  ? 36.934  -59.016 6.588    1.00 136.39 ? 82   VAL H CG1 1 
ATOM   20878 C  CG2 . VAL H  3 84  ? 35.626  -59.501 8.650    1.00 132.34 ? 82   VAL H CG2 1 
ATOM   20879 N  N   . LEU H  3 85  ? 32.510  -58.578 5.748    1.00 144.10 ? 83   LEU H N   1 
ATOM   20880 C  CA  . LEU H  3 85  ? 31.144  -59.055 5.632    1.00 149.57 ? 83   LEU H CA  1 
ATOM   20881 C  C   . LEU H  3 85  ? 31.114  -60.579 5.738    1.00 142.37 ? 83   LEU H C   1 
ATOM   20882 O  O   . LEU H  3 85  ? 32.144  -61.255 5.671    1.00 140.68 ? 83   LEU H O   1 
ATOM   20883 C  CB  . LEU H  3 85  ? 30.535  -58.596 4.309    1.00 164.03 ? 83   LEU H CB  1 
ATOM   20884 C  CG  . LEU H  3 85  ? 30.439  -57.085 4.098    1.00 153.89 ? 83   LEU H CG  1 
ATOM   20885 C  CD1 . LEU H  3 85  ? 29.987  -56.783 2.685    1.00 182.83 ? 83   LEU H CD1 1 
ATOM   20886 C  CD2 . LEU H  3 85  ? 29.492  -56.464 5.102    1.00 154.27 ? 83   LEU H CD2 1 
ATOM   20887 N  N   . MET H  3 86  ? 29.911  -61.125 5.882    1.00 147.46 ? 84   MET H N   1 
ATOM   20888 C  CA  . MET H  3 86  ? 29.755  -62.556 6.073    1.00 146.21 ? 84   MET H CA  1 
ATOM   20889 C  C   . MET H  3 86  ? 29.530  -63.270 4.746    1.00 162.72 ? 84   MET H C   1 
ATOM   20890 O  O   . MET H  3 86  ? 29.436  -62.661 3.680    1.00 187.05 ? 84   MET H O   1 
ATOM   20891 C  CB  . MET H  3 86  ? 28.606  -62.847 7.032    1.00 145.83 ? 84   MET H CB  1 
ATOM   20892 C  CG  . MET H  3 86  ? 27.244  -62.493 6.502    1.00 149.86 ? 84   MET H CG  1 
ATOM   20893 S  SD  . MET H  3 86  ? 25.985  -63.245 7.540    1.00 150.26 ? 84   MET H SD  1 
ATOM   20894 C  CE  . MET H  3 86  ? 24.512  -62.756 6.659    1.00 158.36 ? 84   MET H CE  1 
ATOM   20895 N  N   . VAL H  3 87  ? 29.438  -64.583 4.821    1.00 178.24 ? 85   VAL H N   1 
ATOM   20896 C  CA  . VAL H  3 87  ? 29.145  -65.411 3.661    1.00 166.80 ? 85   VAL H CA  1 
ATOM   20897 C  C   . VAL H  3 87  ? 27.636  -65.479 3.497    1.00 167.05 ? 85   VAL H C   1 
ATOM   20898 O  O   . VAL H  3 87  ? 26.891  -65.589 4.477    1.00 167.84 ? 85   VAL H O   1 
ATOM   20899 C  CB  . VAL H  3 87  ? 29.768  -66.810 3.812    1.00 159.55 ? 85   VAL H CB  1 
ATOM   20900 C  CG1 . VAL H  3 87  ? 29.567  -67.609 2.544    1.00 181.07 ? 85   VAL H CG1 1 
ATOM   20901 C  CG2 . VAL H  3 87  ? 31.251  -66.689 4.130    1.00 154.48 ? 85   VAL H CG2 1 
ATOM   20902 N  N   . GLU H  3 88  ? 27.183  -65.395 2.253    1.00 182.78 ? 86   GLU H N   1 
ATOM   20903 C  CA  . GLU H  3 88  ? 25.763  -65.397 1.952    1.00 197.97 ? 86   GLU H CA  1 
ATOM   20904 C  C   . GLU H  3 88  ? 25.152  -66.772 2.231    1.00 219.81 ? 86   GLU H C   1 
ATOM   20905 O  O   . GLU H  3 88  ? 25.853  -67.761 2.459    1.00 235.64 ? 86   GLU H O   1 
ATOM   20906 C  CB  . GLU H  3 88  ? 25.554  -65.003 0.495    1.00 221.66 ? 86   GLU H CB  1 
ATOM   20907 C  CG  . GLU H  3 88  ? 26.411  -63.819 0.083    1.00 216.67 ? 86   GLU H CG  1 
ATOM   20908 C  CD  . GLU H  3 88  ? 26.611  -63.727 -1.418   1.00 208.64 ? 86   GLU H CD  1 
ATOM   20909 O  OE1 . GLU H  3 88  ? 26.024  -64.548 -2.154   1.00 198.36 ? 86   GLU H OE1 1 
ATOM   20910 O  OE2 . GLU H  3 88  ? 27.376  -62.845 -1.864   1.00 202.42 ? 86   GLU H OE2 1 
ATOM   20911 N  N   . THR H  3 89  ? 23.820  -66.838 2.185    1.00 206.90 ? 87   THR H N   1 
ATOM   20912 C  CA  . THR H  3 89  ? 23.151  -68.126 2.329    1.00 202.38 ? 87   THR H CA  1 
ATOM   20913 C  C   . THR H  3 89  ? 23.148  -68.929 1.042    1.00 198.26 ? 87   THR H C   1 
ATOM   20914 O  O   . THR H  3 89  ? 22.541  -70.006 1.002    1.00 199.47 ? 87   THR H O   1 
ATOM   20915 C  CB  . THR H  3 89  ? 21.709  -67.948 2.804    1.00 201.47 ? 87   THR H CB  1 
ATOM   20916 O  OG1 . THR H  3 89  ? 21.100  -66.854 2.106    1.00 202.41 ? 87   THR H OG1 1 
ATOM   20917 C  CG2 . THR H  3 89  ? 21.653  -67.744 4.310    1.00 196.07 ? 87   THR H CG2 1 
ATOM   20918 N  N   . HIS H  3 90  ? 23.812  -68.442 0.003    1.00 209.48 ? 88   HIS H N   1 
ATOM   20919 C  CA  . HIS H  3 90  ? 23.852  -69.146 -1.265   1.00 224.74 ? 88   HIS H CA  1 
ATOM   20920 C  C   . HIS H  3 90  ? 24.962  -70.180 -1.291   1.00 228.33 ? 88   HIS H C   1 
ATOM   20921 O  O   . HIS H  3 90  ? 25.045  -70.958 -2.248   1.00 242.74 ? 88   HIS H O   1 
ATOM   20922 C  CB  . HIS H  3 90  ? 24.050  -68.145 -2.414   1.00 230.39 ? 88   HIS H CB  1 
ATOM   20923 C  CG  . HIS H  3 90  ? 23.084  -66.999 -2.395   1.00 234.77 ? 88   HIS H CG  1 
ATOM   20924 N  ND1 . HIS H  3 90  ? 23.128  -66.005 -1.440   1.00 225.75 ? 88   HIS H ND1 1 
ATOM   20925 C  CD2 . HIS H  3 90  ? 22.064  -66.676 -3.226   1.00 238.40 ? 88   HIS H CD2 1 
ATOM   20926 C  CE1 . HIS H  3 90  ? 22.168  -65.128 -1.674   1.00 219.37 ? 88   HIS H CE1 1 
ATOM   20927 N  NE2 . HIS H  3 90  ? 21.509  -65.511 -2.753   1.00 236.31 ? 88   HIS H NE2 1 
ATOM   20928 N  N   . ASN H  3 91  ? 25.796  -70.211 -0.251   1.00 211.57 ? 89   ASN H N   1 
ATOM   20929 C  CA  . ASN H  3 91  ? 26.901  -71.151 -0.139   1.00 205.63 ? 89   ASN H CA  1 
ATOM   20930 C  C   . ASN H  3 91  ? 27.020  -71.660 1.291    1.00 198.95 ? 89   ASN H C   1 
ATOM   20931 O  O   . ASN H  3 91  ? 27.007  -70.869 2.238    1.00 191.71 ? 89   ASN H O   1 
ATOM   20932 C  CB  . ASN H  3 91  ? 28.214  -70.496 -0.578   1.00 203.29 ? 89   ASN H CB  1 
ATOM   20933 C  CG  . ASN H  3 91  ? 28.279  -70.267 -2.076   1.00 240.67 ? 89   ASN H CG  1 
ATOM   20934 O  OD1 . ASN H  3 91  ? 27.707  -71.029 -2.858   1.00 256.29 ? 89   ASN H OD1 1 
ATOM   20935 N  ND2 . ASN H  3 91  ? 28.961  -69.202 -2.484   1.00 251.16 ? 89   ASN H ND2 1 
ATOM   20936 N  N   . GLU H  3 92  ? 27.112  -72.981 1.441    1.00 200.22 ? 90   GLU H N   1 
ATOM   20937 C  CA  . GLU H  3 92  ? 27.340  -73.658 2.717    1.00 194.97 ? 90   GLU H CA  1 
ATOM   20938 C  C   . GLU H  3 92  ? 26.339  -73.406 3.842    1.00 176.94 ? 90   GLU H C   1 
ATOM   20939 O  O   . GLU H  3 92  ? 26.234  -74.234 4.753    1.00 177.63 ? 90   GLU H O   1 
ATOM   20940 C  CB  . GLU H  3 92  ? 28.723  -73.274 3.243    1.00 199.30 ? 90   GLU H CB  1 
ATOM   20941 C  CG  . GLU H  3 92  ? 29.865  -73.626 2.328    1.00 205.85 ? 90   GLU H CG  1 
ATOM   20942 C  CD  . GLU H  3 92  ? 31.174  -73.099 2.855    1.00 204.35 ? 90   GLU H CD  1 
ATOM   20943 O  OE1 . GLU H  3 92  ? 31.145  -72.376 3.875    1.00 215.91 ? 90   GLU H OE1 1 
ATOM   20944 O  OE2 . GLU H  3 92  ? 32.224  -73.392 2.246    1.00 183.17 ? 90   GLU H OE2 1 
ATOM   20945 N  N   . ILE H  3 93  ? 25.595  -72.295 3.823    1.00 182.60 ? 91   ILE H N   1 
ATOM   20946 C  CA  . ILE H  3 93  ? 24.716  -72.014 4.960    1.00 209.61 ? 91   ILE H CA  1 
ATOM   20947 C  C   . ILE H  3 93  ? 23.386  -72.739 4.819    1.00 211.86 ? 91   ILE H C   1 
ATOM   20948 O  O   . ILE H  3 93  ? 22.626  -72.829 5.797    1.00 223.26 ? 91   ILE H O   1 
ATOM   20949 C  CB  . ILE H  3 93  ? 24.498  -70.496 5.165    1.00 215.13 ? 91   ILE H CB  1 
ATOM   20950 C  CG1 . ILE H  3 93  ? 25.829  -69.741 5.134    1.00 201.34 ? 91   ILE H CG1 1 
ATOM   20951 C  CG2 . ILE H  3 93  ? 23.808  -70.189 6.501    1.00 190.77 ? 91   ILE H CG2 1 
ATOM   20952 C  CD1 . ILE H  3 93  ? 25.734  -68.307 5.641    1.00 175.23 ? 91   ILE H CD1 1 
ATOM   20953 N  N   . TYR H  3 94  ? 23.110  -73.325 3.658    1.00 213.81 ? 92   TYR H N   1 
ATOM   20954 C  CA  . TYR H  3 94  ? 21.896  -74.096 3.455    1.00 222.26 ? 92   TYR H CA  1 
ATOM   20955 C  C   . TYR H  3 94  ? 22.179  -75.584 3.368    1.00 237.74 ? 92   TYR H C   1 
ATOM   20956 O  O   . TYR H  3 94  ? 21.235  -76.381 3.381    1.00 249.58 ? 92   TYR H O   1 
ATOM   20957 C  CB  . TYR H  3 94  ? 21.156  -73.630 2.187    1.00 237.41 ? 92   TYR H CB  1 
ATOM   20958 C  CG  . TYR H  3 94  ? 21.826  -73.998 0.875    1.00 258.89 ? 92   TYR H CG  1 
ATOM   20959 C  CD1 . TYR H  3 94  ? 22.871  -73.236 0.369    1.00 259.52 ? 92   TYR H CD1 1 
ATOM   20960 C  CD2 . TYR H  3 94  ? 21.384  -75.086 0.122    1.00 260.42 ? 92   TYR H CD2 1 
ATOM   20961 C  CE1 . TYR H  3 94  ? 23.479  -73.562 -0.833   1.00 261.95 ? 92   TYR H CE1 1 
ATOM   20962 C  CE2 . TYR H  3 94  ? 21.985  -75.418 -1.082   1.00 253.02 ? 92   TYR H CE2 1 
ATOM   20963 C  CZ  . TYR H  3 94  ? 23.031  -74.653 -1.554   1.00 253.88 ? 92   TYR H CZ  1 
ATOM   20964 O  OH  . TYR H  3 94  ? 23.627  -74.982 -2.749   1.00 244.80 ? 92   TYR H OH  1 
ATOM   20965 N  N   . ASP H  3 95  ? 23.453  -75.975 3.293    1.00 247.13 ? 93   ASP H N   1 
ATOM   20966 C  CA  . ASP H  3 95  ? 23.800  -77.367 3.047    1.00 263.19 ? 93   ASP H CA  1 
ATOM   20967 C  C   . ASP H  3 95  ? 23.562  -78.255 4.260    1.00 253.97 ? 93   ASP H C   1 
ATOM   20968 O  O   . ASP H  3 95  ? 23.488  -79.478 4.102    1.00 262.20 ? 93   ASP H O   1 
ATOM   20969 C  CB  . ASP H  3 95  ? 25.262  -77.481 2.603    1.00 264.64 ? 93   ASP H CB  1 
ATOM   20970 C  CG  . ASP H  3 95  ? 25.573  -76.652 1.366    1.00 246.46 ? 93   ASP H CG  1 
ATOM   20971 O  OD1 . ASP H  3 95  ? 24.626  -76.097 0.769    1.00 265.49 ? 93   ASP H OD1 1 
ATOM   20972 O  OD2 . ASP H  3 95  ? 26.761  -76.563 0.988    1.00 203.04 ? 93   ASP H OD2 1 
ATOM   20973 N  N   . LYS H  3 96  ? 23.441  -77.687 5.457    1.00 221.97 ? 94   LYS H N   1 
ATOM   20974 C  CA  . LYS H  3 96  ? 23.284  -78.502 6.655    1.00 223.37 ? 94   LYS H CA  1 
ATOM   20975 C  C   . LYS H  3 96  ? 22.006  -78.217 7.429    1.00 230.93 ? 94   LYS H C   1 
ATOM   20976 O  O   . LYS H  3 96  ? 21.333  -79.157 7.866    1.00 250.69 ? 94   LYS H O   1 
ATOM   20977 C  CB  . LYS H  3 96  ? 24.496  -78.308 7.581    1.00 214.00 ? 94   LYS H CB  1 
ATOM   20978 C  CG  . LYS H  3 96  ? 24.435  -79.120 8.863    1.00 212.26 ? 94   LYS H CG  1 
ATOM   20979 C  CD  . LYS H  3 96  ? 25.676  -78.907 9.716    1.00 205.85 ? 94   LYS H CD  1 
ATOM   20980 C  CE  . LYS H  3 96  ? 25.525  -79.550 11.088   1.00 199.39 ? 94   LYS H CE  1 
ATOM   20981 N  NZ  . LYS H  3 96  ? 25.213  -81.003 10.986   1.00 201.75 ? 94   LYS H NZ  1 
ATOM   20982 N  N   . PHE H  3 97  ? 21.653  -76.963 7.615    1.00 225.45 ? 95   PHE H N   1 
ATOM   20983 C  CA  . PHE H  3 97  ? 20.539  -76.617 8.491    1.00 229.05 ? 95   PHE H CA  1 
ATOM   20984 C  C   . PHE H  3 97  ? 19.553  -75.643 7.868    1.00 229.67 ? 95   PHE H C   1 
ATOM   20985 O  O   . PHE H  3 97  ? 18.351  -75.755 8.130    1.00 228.87 ? 95   PHE H O   1 
ATOM   20986 C  CB  . PHE H  3 97  ? 21.090  -76.031 9.796    1.00 227.72 ? 95   PHE H CB  1 
ATOM   20987 C  CG  . PHE H  3 97  ? 22.445  -75.405 9.644    1.00 225.15 ? 95   PHE H CG  1 
ATOM   20988 C  CD1 . PHE H  3 97  ? 22.602  -74.214 8.954    1.00 217.43 ? 95   PHE H CD1 1 
ATOM   20989 C  CD2 . PHE H  3 97  ? 23.566  -76.014 10.185   1.00 217.41 ? 95   PHE H CD2 1 
ATOM   20990 C  CE1 . PHE H  3 97  ? 23.852  -73.644 8.808    1.00 212.11 ? 95   PHE H CE1 1 
ATOM   20991 C  CE2 . PHE H  3 97  ? 24.818  -75.447 10.043   1.00 201.86 ? 95   PHE H CE2 1 
ATOM   20992 C  CZ  . PHE H  3 97  ? 24.960  -74.262 9.353    1.00 203.88 ? 95   PHE H CZ  1 
ATOM   20993 N  N   . LYS H  3 98  ? 20.036  -74.682 7.074    1.00 229.42 ? 96   LYS H N   1 
ATOM   20994 C  CA  . LYS H  3 98  ? 19.239  -73.586 6.531    1.00 225.52 ? 96   LYS H CA  1 
ATOM   20995 C  C   . LYS H  3 98  ? 18.770  -72.684 7.664    1.00 215.85 ? 96   LYS H C   1 
ATOM   20996 O  O   . LYS H  3 98  ? 19.490  -72.496 8.650    1.00 205.12 ? 96   LYS H O   1 
ATOM   20997 C  CB  . LYS H  3 98  ? 18.052  -74.096 5.704    1.00 218.10 ? 96   LYS H CB  1 
ATOM   20998 C  CG  . LYS H  3 98  ? 18.448  -74.856 4.445    1.00 217.74 ? 96   LYS H CG  1 
ATOM   20999 C  CD  . LYS H  3 98  ? 17.276  -75.011 3.488    1.00 214.56 ? 96   LYS H CD  1 
ATOM   21000 C  CE  . LYS H  3 98  ? 16.255  -76.006 4.010    1.00 218.92 ? 96   LYS H CE  1 
ATOM   21001 N  NZ  . LYS H  3 98  ? 16.785  -77.401 4.032    1.00 218.44 ? 96   LYS H NZ  1 
ATOM   21002 N  N   . GLN H  3 99  ? 17.584  -72.101 7.521    1.00 228.22 ? 97   GLN H N   1 
ATOM   21003 C  CA  . GLN H  3 99  ? 17.042  -71.160 8.492    1.00 233.22 ? 97   GLN H CA  1 
ATOM   21004 C  C   . GLN H  3 99  ? 15.756  -71.721 9.083    1.00 240.25 ? 97   GLN H C   1 
ATOM   21005 O  O   . GLN H  3 99  ? 14.937  -72.307 8.367    1.00 239.47 ? 97   GLN H O   1 
ATOM   21006 C  CB  . GLN H  3 99  ? 16.785  -69.788 7.848    1.00 232.78 ? 97   GLN H CB  1 
ATOM   21007 C  CG  . GLN H  3 99  ? 16.265  -68.717 8.800    1.00 234.13 ? 97   GLN H CG  1 
ATOM   21008 C  CD  . GLN H  3 99  ? 14.749  -68.656 8.839    1.00 240.86 ? 97   GLN H CD  1 
ATOM   21009 O  OE1 . GLN H  3 99  ? 14.138  -68.718 9.907    1.00 239.16 ? 97   GLN H OE1 1 
ATOM   21010 N  NE2 . GLN H  3 99  ? 14.133  -68.537 7.668    1.00 243.90 ? 97   GLN H NE2 1 
ATOM   21011 N  N   . SER H  3 100 ? 15.584  -71.543 10.393   1.00 234.54 ? 98   SER H N   1 
ATOM   21012 C  CA  . SER H  3 100 ? 14.379  -71.999 11.069   1.00 233.65 ? 98   SER H CA  1 
ATOM   21013 C  C   . SER H  3 100 ? 14.065  -71.075 12.237   1.00 229.57 ? 98   SER H C   1 
ATOM   21014 O  O   . SER H  3 100 ? 14.895  -70.271 12.670   1.00 222.06 ? 98   SER H O   1 
ATOM   21015 C  CB  . SER H  3 100 ? 14.521  -73.445 11.557   1.00 231.52 ? 98   SER H CB  1 
ATOM   21016 O  OG  . SER H  3 100 ? 14.692  -74.335 10.469   1.00 228.35 ? 98   SER H OG  1 
ATOM   21017 N  N   . THR H  3 101 ? 12.843  -71.212 12.754   1.00 229.86 ? 99   THR H N   1 
ATOM   21018 C  CA  . THR H  3 101 ? 12.387  -70.400 13.874   1.00 221.46 ? 99   THR H CA  1 
ATOM   21019 C  C   . THR H  3 101 ? 13.176  -70.669 15.143   1.00 215.72 ? 99   THR H C   1 
ATOM   21020 O  O   . THR H  3 101 ? 13.000  -69.947 16.130   1.00 222.18 ? 99   THR H O   1 
ATOM   21021 C  CB  . THR H  3 101 ? 10.905  -70.661 14.128   1.00 232.92 ? 99   THR H CB  1 
ATOM   21022 O  OG1 . THR H  3 101 ? 10.730  -72.016 14.561   1.00 235.30 ? 99   THR H OG1 1 
ATOM   21023 C  CG2 . THR H  3 101 ? 10.108  -70.442 12.854   1.00 240.45 ? 99   THR H CG2 1 
ATOM   21024 N  N   . HIS H  3 102 ? 14.034  -71.684 15.140   1.00 224.88 ? 100  HIS H N   1 
ATOM   21025 C  CA  . HIS H  3 102 ? 14.771  -72.089 16.327   1.00 233.56 ? 100  HIS H CA  1 
ATOM   21026 C  C   . HIS H  3 102 ? 16.134  -71.418 16.420   1.00 228.55 ? 100  HIS H C   1 
ATOM   21027 O  O   . HIS H  3 102 ? 16.612  -71.160 17.531   1.00 223.56 ? 100  HIS H O   1 
ATOM   21028 C  CB  . HIS H  3 102 ? 14.929  -73.616 16.328   1.00 245.55 ? 100  HIS H CB  1 
ATOM   21029 C  CG  . HIS H  3 102 ? 15.493  -74.177 17.598   1.00 257.45 ? 100  HIS H CG  1 
ATOM   21030 N  ND1 . HIS H  3 102 ? 15.952  -75.474 17.693   1.00 253.89 ? 100  HIS H ND1 1 
ATOM   21031 C  CD2 . HIS H  3 102 ? 15.654  -73.631 18.827   1.00 260.76 ? 100  HIS H CD2 1 
ATOM   21032 C  CE1 . HIS H  3 102 ? 16.385  -75.698 18.920   1.00 254.00 ? 100  HIS H CE1 1 
ATOM   21033 N  NE2 . HIS H  3 102 ? 16.216  -74.596 19.629   1.00 257.86 ? 100  HIS H NE2 1 
ATOM   21034 N  N   . SER H  3 103 ? 16.758  -71.098 15.286   1.00 228.61 ? 101  SER H N   1 
ATOM   21035 C  CA  . SER H  3 103 ? 18.093  -70.513 15.299   1.00 221.90 ? 101  SER H CA  1 
ATOM   21036 C  C   . SER H  3 103 ? 18.337  -69.732 14.013   1.00 200.64 ? 101  SER H C   1 
ATOM   21037 O  O   . SER H  3 103 ? 17.614  -69.876 13.024   1.00 194.09 ? 101  SER H O   1 
ATOM   21038 C  CB  . SER H  3 103 ? 19.165  -71.593 15.490   1.00 229.90 ? 101  SER H CB  1 
ATOM   21039 O  OG  . SER H  3 103 ? 19.001  -72.649 14.558   1.00 237.87 ? 101  SER H OG  1 
ATOM   21040 N  N   . ILE H  3 104 ? 19.372  -68.893 14.049   1.00 185.16 ? 102  ILE H N   1 
ATOM   21041 C  CA  . ILE H  3 104 ? 19.821  -68.113 12.901   1.00 181.26 ? 102  ILE H CA  1 
ATOM   21042 C  C   . ILE H  3 104 ? 21.337  -68.242 12.799   1.00 183.14 ? 102  ILE H C   1 
ATOM   21043 O  O   . ILE H  3 104 ? 22.046  -68.019 13.787   1.00 173.18 ? 102  ILE H O   1 
ATOM   21044 C  CB  . ILE H  3 104 ? 19.393  -66.637 13.025   1.00 181.72 ? 102  ILE H CB  1 
ATOM   21045 C  CG1 . ILE H  3 104 ? 17.914  -66.483 12.655   1.00 204.42 ? 102  ILE H CG1 1 
ATOM   21046 C  CG2 . ILE H  3 104 ? 20.271  -65.736 12.175   1.00 173.09 ? 102  ILE H CG2 1 
ATOM   21047 C  CD1 . ILE H  3 104 ? 17.398  -65.065 12.746   1.00 212.04 ? 102  ILE H CD1 1 
ATOM   21048 N  N   . TYR H  3 105 ? 21.832  -68.595 11.609   1.00 191.29 ? 103  TYR H N   1 
ATOM   21049 C  CA  . TYR H  3 105 ? 23.245  -68.888 11.396   1.00 179.35 ? 103  TYR H CA  1 
ATOM   21050 C  C   . TYR H  3 105 ? 23.910  -67.843 10.507   1.00 177.69 ? 103  TYR H C   1 
ATOM   21051 O  O   . TYR H  3 105 ? 23.372  -67.462 9.463    1.00 192.45 ? 103  TYR H O   1 
ATOM   21052 C  CB  . TYR H  3 105 ? 23.428  -70.277 10.776   1.00 174.93 ? 103  TYR H CB  1 
ATOM   21053 C  CG  . TYR H  3 105 ? 22.784  -71.390 11.570   1.00 183.87 ? 103  TYR H CG  1 
ATOM   21054 C  CD1 . TYR H  3 105 ? 23.454  -71.987 12.631   1.00 192.81 ? 103  TYR H CD1 1 
ATOM   21055 C  CD2 . TYR H  3 105 ? 21.507  -71.843 11.264   1.00 201.84 ? 103  TYR H CD2 1 
ATOM   21056 C  CE1 . TYR H  3 105 ? 22.872  -73.005 13.366   1.00 211.07 ? 103  TYR H CE1 1 
ATOM   21057 C  CE2 . TYR H  3 105 ? 20.914  -72.863 11.994   1.00 220.51 ? 103  TYR H CE2 1 
ATOM   21058 C  CZ  . TYR H  3 105 ? 21.602  -73.440 13.044   1.00 224.41 ? 103  TYR H CZ  1 
ATOM   21059 O  OH  . TYR H  3 105 ? 21.018  -74.454 13.772   1.00 232.05 ? 103  TYR H OH  1 
ATOM   21060 N  N   . MET H  3 106 ? 25.099  -67.401 10.926   1.00 168.83 ? 104  MET H N   1 
ATOM   21061 C  CA  . MET H  3 106 ? 25.930  -66.460 10.184   1.00 163.70 ? 104  MET H CA  1 
ATOM   21062 C  C   . MET H  3 106 ? 27.316  -67.060 10.010   1.00 161.87 ? 104  MET H C   1 
ATOM   21063 O  O   . MET H  3 106 ? 27.898  -67.572 10.971   1.00 165.59 ? 104  MET H O   1 
ATOM   21064 C  CB  . MET H  3 106 ? 26.045  -65.119 10.916   1.00 164.50 ? 104  MET H CB  1 
ATOM   21065 C  CG  . MET H  3 106 ? 24.720  -64.481 11.296   1.00 168.02 ? 104  MET H CG  1 
ATOM   21066 S  SD  . MET H  3 106 ? 24.957  -63.159 12.498   1.00 154.38 ? 104  MET H SD  1 
ATOM   21067 C  CE  . MET H  3 106 ? 25.536  -64.103 13.903   1.00 164.17 ? 104  MET H CE  1 
ATOM   21068 N  N   . PHE H  3 107 ? 27.866  -66.958 8.801    1.00 168.09 ? 105  PHE H N   1 
ATOM   21069 C  CA  . PHE H  3 107 ? 29.137  -67.593 8.485    1.00 165.73 ? 105  PHE H CA  1 
ATOM   21070 C  C   . PHE H  3 107 ? 30.109  -66.578 7.905    1.00 160.55 ? 105  PHE H C   1 
ATOM   21071 O  O   . PHE H  3 107 ? 29.716  -65.650 7.194    1.00 183.26 ? 105  PHE H O   1 
ATOM   21072 C  CB  . PHE H  3 107 ? 28.960  -68.754 7.496    1.00 186.06 ? 105  PHE H CB  1 
ATOM   21073 C  CG  . PHE H  3 107 ? 28.577  -70.050 8.148    1.00 197.85 ? 105  PHE H CG  1 
ATOM   21074 C  CD1 . PHE H  3 107 ? 27.281  -70.269 8.579    1.00 208.11 ? 105  PHE H CD1 1 
ATOM   21075 C  CD2 . PHE H  3 107 ? 29.514  -71.056 8.321    1.00 199.83 ? 105  PHE H CD2 1 
ATOM   21076 C  CE1 . PHE H  3 107 ? 26.928  -71.465 9.180    1.00 213.18 ? 105  PHE H CE1 1 
ATOM   21077 C  CE2 . PHE H  3 107 ? 29.166  -72.254 8.918    1.00 201.35 ? 105  PHE H CE2 1 
ATOM   21078 C  CZ  . PHE H  3 107 ? 27.873  -72.459 9.348    1.00 203.79 ? 105  PHE H CZ  1 
ATOM   21079 N  N   . PHE H  3 108 ? 31.388  -66.771 8.219    1.00 142.82 ? 106  PHE H N   1 
ATOM   21080 C  CA  . PHE H  3 108 ? 32.469  -65.918 7.749    1.00 141.70 ? 106  PHE H CA  1 
ATOM   21081 C  C   . PHE H  3 108 ? 33.601  -66.798 7.242    1.00 143.88 ? 106  PHE H C   1 
ATOM   21082 O  O   . PHE H  3 108 ? 33.636  -68.006 7.491    1.00 178.29 ? 106  PHE H O   1 
ATOM   21083 C  CB  . PHE H  3 108 ? 32.978  -64.995 8.862    1.00 173.99 ? 106  PHE H CB  1 
ATOM   21084 C  CG  . PHE H  3 108 ? 31.959  -64.001 9.343    1.00 194.51 ? 106  PHE H CG  1 
ATOM   21085 C  CD1 . PHE H  3 108 ? 31.000  -64.363 10.277   1.00 168.55 ? 106  PHE H CD1 1 
ATOM   21086 C  CD2 . PHE H  3 108 ? 31.975  -62.695 8.878    1.00 201.02 ? 106  PHE H CD2 1 
ATOM   21087 C  CE1 . PHE H  3 108 ? 30.067  -63.447 10.722   1.00 146.96 ? 106  PHE H CE1 1 
ATOM   21088 C  CE2 . PHE H  3 108 ? 31.046  -61.772 9.325    1.00 178.98 ? 106  PHE H CE2 1 
ATOM   21089 C  CZ  . PHE H  3 108 ? 30.091  -62.150 10.245   1.00 154.04 ? 106  PHE H CZ  1 
ATOM   21090 N  N   . GLN H  3 109 ? 34.545  -66.187 6.541    1.00 146.10 ? 107  GLN H N   1 
ATOM   21091 C  CA  . GLN H  3 109 ? 35.703  -66.924 6.067    1.00 168.69 ? 107  GLN H CA  1 
ATOM   21092 C  C   . GLN H  3 109 ? 36.856  -66.752 7.055    1.00 166.93 ? 107  GLN H C   1 
ATOM   21093 O  O   . GLN H  3 109 ? 36.652  -66.395 8.219    1.00 183.81 ? 107  GLN H O   1 
ATOM   21094 C  CB  . GLN H  3 109 ? 36.112  -66.449 4.666    1.00 190.16 ? 107  GLN H CB  1 
ATOM   21095 C  CG  . GLN H  3 109 ? 35.100  -66.686 3.570    1.00 200.07 ? 107  GLN H CG  1 
ATOM   21096 C  CD  . GLN H  3 109 ? 35.601  -66.200 2.218    1.00 188.50 ? 107  GLN H CD  1 
ATOM   21097 O  OE1 . GLN H  3 109 ? 36.634  -65.531 2.125    1.00 171.30 ? 107  GLN H OE1 1 
ATOM   21098 N  NE2 . GLN H  3 109 ? 34.866  -66.532 1.164    1.00 193.09 ? 107  GLN H NE2 1 
ATOM   21099 N  N   . THR H  3 110 ? 38.075  -67.009 6.589    1.00 158.56 ? 108  THR H N   1 
ATOM   21100 C  CA  . THR H  3 110 ? 39.299  -66.769 7.348    1.00 155.75 ? 108  THR H CA  1 
ATOM   21101 C  C   . THR H  3 110 ? 40.414  -66.254 6.468    1.00 157.96 ? 108  THR H C   1 
ATOM   21102 O  O   . THR H  3 110 ? 41.352  -65.632 6.979    1.00 157.68 ? 108  THR H O   1 
ATOM   21103 C  CB  . THR H  3 110 ? 39.784  -68.045 8.055    1.00 156.78 ? 108  THR H CB  1 
ATOM   21104 O  OG1 . THR H  3 110 ? 38.665  -68.759 8.599    1.00 160.69 ? 108  THR H OG1 1 
ATOM   21105 C  CG2 . THR H  3 110 ? 40.741  -67.696 9.191    1.00 155.81 ? 108  THR H CG2 1 
ATOM   21106 N  N   . SER H  3 111 ? 40.340  -66.478 5.161    1.00 172.43 ? 109  SER H N   1 
ATOM   21107 C  CA  . SER H  3 111 ? 41.341  -65.961 4.253    1.00 188.16 ? 109  SER H CA  1 
ATOM   21108 C  C   . SER H  3 111 ? 41.299  -64.447 4.181    1.00 175.41 ? 109  SER H C   1 
ATOM   21109 O  O   . SER H  3 111 ? 42.312  -63.827 3.845    1.00 181.07 ? 109  SER H O   1 
ATOM   21110 C  CB  . SER H  3 111 ? 41.123  -66.579 2.876    1.00 228.48 ? 109  SER H CB  1 
ATOM   21111 O  OG  . SER H  3 111 ? 41.139  -67.992 2.976    1.00 246.41 ? 109  SER H OG  1 
ATOM   21112 N  N   . GLU H  3 112 ? 40.155  -63.846 4.505    1.00 164.46 ? 110  GLU H N   1 
ATOM   21113 C  CA  . GLU H  3 112 ? 40.027  -62.401 4.607    1.00 175.05 ? 110  GLU H CA  1 
ATOM   21114 C  C   . GLU H  3 112 ? 40.120  -61.895 6.039    1.00 157.68 ? 110  GLU H C   1 
ATOM   21115 O  O   . GLU H  3 112 ? 40.413  -60.711 6.244    1.00 156.93 ? 110  GLU H O   1 
ATOM   21116 C  CB  . GLU H  3 112 ? 38.689  -61.942 4.011    1.00 181.97 ? 110  GLU H CB  1 
ATOM   21117 C  CG  . GLU H  3 112 ? 37.458  -62.571 4.675    1.00 173.21 ? 110  GLU H CG  1 
ATOM   21118 C  CD  . GLU H  3 112 ? 36.138  -62.181 4.013    1.00 180.58 ? 110  GLU H CD  1 
ATOM   21119 O  OE1 . GLU H  3 112 ? 36.164  -61.467 2.989    1.00 185.46 ? 110  GLU H OE1 1 
ATOM   21120 O  OE2 . GLU H  3 112 ? 35.070  -62.591 4.518    1.00 184.81 ? 110  GLU H OE2 1 
ATOM   21121 N  N   . LEU H  3 113 ? 39.856  -62.757 7.024    1.00 160.31 ? 111  LEU H N   1 
ATOM   21122 C  CA  . LEU H  3 113 ? 40.007  -62.373 8.422    1.00 155.03 ? 111  LEU H CA  1 
ATOM   21123 C  C   . LEU H  3 113 ? 41.478  -62.289 8.799    1.00 159.63 ? 111  LEU H C   1 
ATOM   21124 O  O   . LEU H  3 113 ? 41.925  -61.304 9.399    1.00 164.13 ? 111  LEU H O   1 
ATOM   21125 C  CB  . LEU H  3 113 ? 39.280  -63.374 9.321    1.00 147.00 ? 111  LEU H CB  1 
ATOM   21126 C  CG  . LEU H  3 113 ? 37.773  -63.199 9.534    1.00 143.97 ? 111  LEU H CG  1 
ATOM   21127 C  CD1 . LEU H  3 113 ? 37.541  -61.953 10.349   1.00 142.71 ? 111  LEU H CD1 1 
ATOM   21128 C  CD2 . LEU H  3 113 ? 36.983  -63.128 8.229    1.00 156.28 ? 111  LEU H CD2 1 
ATOM   21129 N  N   . ARG H  3 114 ? 42.248  -63.317 8.445    1.00 161.40 ? 112  ARG H N   1 
ATOM   21130 C  CA  . ARG H  3 114 ? 43.690  -63.329 8.632    1.00 166.94 ? 112  ARG H CA  1 
ATOM   21131 C  C   . ARG H  3 114 ? 44.432  -62.564 7.543    1.00 164.49 ? 112  ARG H C   1 
ATOM   21132 O  O   . ARG H  3 114 ? 45.664  -62.595 7.510    1.00 177.57 ? 112  ARG H O   1 
ATOM   21133 C  CB  . ARG H  3 114 ? 44.189  -64.784 8.718    1.00 172.97 ? 112  ARG H CB  1 
ATOM   21134 C  CG  . ARG H  3 114 ? 43.756  -65.524 10.010   1.00 157.52 ? 112  ARG H CG  1 
ATOM   21135 C  CD  . ARG H  3 114 ? 44.408  -66.902 10.192   1.00 157.14 ? 112  ARG H CD  1 
ATOM   21136 N  NE  . ARG H  3 114 ? 43.874  -67.894 9.266    1.00 162.54 ? 112  ARG H NE  1 
ATOM   21137 C  CZ  . ARG H  3 114 ? 44.476  -68.260 8.139    1.00 191.85 ? 112  ARG H CZ  1 
ATOM   21138 N  NH1 . ARG H  3 114 ? 45.637  -67.716 7.807    1.00 216.50 ? 112  ARG H NH1 1 
ATOM   21139 N  NH2 . ARG H  3 114 ? 43.923  -69.168 7.342    1.00 174.82 ? 112  ARG H NH2 1 
ATOM   21140 N  N   . GLU H  3 115 ? 43.719  -61.857 6.676    1.00 168.91 ? 113  GLU H N   1 
ATOM   21141 C  CA  . GLU H  3 115 ? 44.364  -60.966 5.725    1.00 184.64 ? 113  GLU H CA  1 
ATOM   21142 C  C   . GLU H  3 115 ? 44.247  -59.511 6.160    1.00 182.97 ? 113  GLU H C   1 
ATOM   21143 O  O   . GLU H  3 115 ? 45.190  -58.735 5.976    1.00 182.33 ? 113  GLU H O   1 
ATOM   21144 C  CB  . GLU H  3 115 ? 43.763  -61.144 4.321    1.00 210.52 ? 113  GLU H CB  1 
ATOM   21145 C  CG  . GLU H  3 115 ? 44.693  -60.780 3.148    1.00 214.69 ? 113  GLU H CG  1 
ATOM   21146 C  CD  . GLU H  3 115 ? 44.888  -59.289 2.959    1.00 225.81 ? 113  GLU H CD  1 
ATOM   21147 O  OE1 . GLU H  3 115 ? 43.924  -58.530 3.199    1.00 234.57 ? 113  GLU H OE1 1 
ATOM   21148 O  OE2 . GLU H  3 115 ? 46.004  -58.883 2.557    1.00 226.23 ? 113  GLU H OE2 1 
ATOM   21149 N  N   . ALA H  3 116 ? 43.108  -59.140 6.755    1.00 185.81 ? 114  ALA H N   1 
ATOM   21150 C  CA  . ALA H  3 116 ? 42.954  -57.812 7.344    1.00 198.14 ? 114  ALA H CA  1 
ATOM   21151 C  C   . ALA H  3 116 ? 43.758  -57.686 8.634    1.00 201.53 ? 114  ALA H C   1 
ATOM   21152 O  O   . ALA H  3 116 ? 44.296  -56.613 8.938    1.00 202.03 ? 114  ALA H O   1 
ATOM   21153 C  CB  . ALA H  3 116 ? 41.473  -57.517 7.595    1.00 192.35 ? 114  ALA H CB  1 
ATOM   21154 N  N   . VAL H  3 117 ? 43.826  -58.758 9.417    1.00 192.88 ? 115  VAL H N   1 
ATOM   21155 C  CA  . VAL H  3 117 ? 44.674  -58.819 10.606   1.00 175.61 ? 115  VAL H CA  1 
ATOM   21156 C  C   . VAL H  3 117 ? 45.584  -60.032 10.449   1.00 179.12 ? 115  VAL H C   1 
ATOM   21157 O  O   . VAL H  3 117 ? 45.202  -61.145 10.839   1.00 181.36 ? 115  VAL H O   1 
ATOM   21158 C  CB  . VAL H  3 117 ? 43.844  -58.901 11.896   1.00 155.61 ? 115  VAL H CB  1 
ATOM   21159 C  CG1 . VAL H  3 117 ? 44.753  -58.847 13.120   1.00 154.36 ? 115  VAL H CG1 1 
ATOM   21160 C  CG2 . VAL H  3 117 ? 42.820  -57.775 11.950   1.00 152.85 ? 115  VAL H CG2 1 
ATOM   21161 N  N   . PRO H  3 118 ? 46.780  -59.867 9.872    1.00 162.69 ? 116  PRO H N   1 
ATOM   21162 C  CA  . PRO H  3 118 ? 47.661  -61.019 9.625    1.00 164.17 ? 116  PRO H CA  1 
ATOM   21163 C  C   . PRO H  3 118 ? 48.027  -61.805 10.874   1.00 163.38 ? 116  PRO H C   1 
ATOM   21164 O  O   . PRO H  3 118 ? 47.832  -63.023 10.931   1.00 167.75 ? 116  PRO H O   1 
ATOM   21165 C  CB  . PRO H  3 118 ? 48.900  -60.373 8.990    1.00 177.21 ? 116  PRO H CB  1 
ATOM   21166 C  CG  . PRO H  3 118 ? 48.396  -59.100 8.387    1.00 171.37 ? 116  PRO H CG  1 
ATOM   21167 C  CD  . PRO H  3 118 ? 47.344  -58.616 9.341    1.00 166.87 ? 116  PRO H CD  1 
ATOM   21168 N  N   . GLU H  3 119 ? 48.581  -61.126 11.870   1.00 171.27 ? 117  GLU H N   1 
ATOM   21169 C  CA  . GLU H  3 119 ? 49.019  -61.826 13.070   1.00 184.34 ? 117  GLU H CA  1 
ATOM   21170 C  C   . GLU H  3 119 ? 47.946  -61.745 14.147   1.00 174.73 ? 117  GLU H C   1 
ATOM   21171 O  O   . GLU H  3 119 ? 47.416  -60.651 14.409   1.00 161.67 ? 117  GLU H O   1 
ATOM   21172 C  CB  . GLU H  3 119 ? 50.329  -61.231 13.583   1.00 199.27 ? 117  GLU H CB  1 
ATOM   21173 C  CG  . GLU H  3 119 ? 51.017  -62.072 14.644   1.00 206.70 ? 117  GLU H CG  1 
ATOM   21174 C  CD  . GLU H  3 119 ? 52.436  -61.616 14.934   1.00 207.13 ? 117  GLU H CD  1 
ATOM   21175 O  OE1 . GLU H  3 119 ? 52.886  -60.625 14.320   1.00 207.43 ? 117  GLU H OE1 1 
ATOM   21176 O  OE2 . GLU H  3 119 ? 53.105  -62.255 15.774   1.00 206.73 ? 117  GLU H OE2 1 
ATOM   21177 N  N   . PRO H  3 120 ? 47.592  -62.873 14.774   1.00 170.70 ? 118  PRO H N   1 
ATOM   21178 C  CA  . PRO H  3 120 ? 46.500  -62.859 15.762   1.00 183.47 ? 118  PRO H CA  1 
ATOM   21179 C  C   . PRO H  3 120 ? 46.740  -61.917 16.922   1.00 183.42 ? 118  PRO H C   1 
ATOM   21180 O  O   . PRO H  3 120 ? 45.776  -61.516 17.588   1.00 179.25 ? 118  PRO H O   1 
ATOM   21181 C  CB  . PRO H  3 120 ? 46.447  -64.318 16.241   1.00 173.50 ? 118  PRO H CB  1 
ATOM   21182 C  CG  . PRO H  3 120 ? 47.074  -65.105 15.149   1.00 166.96 ? 118  PRO H CG  1 
ATOM   21183 C  CD  . PRO H  3 120 ? 48.145  -64.223 14.581   1.00 169.78 ? 118  PRO H CD  1 
ATOM   21184 N  N   . VAL H  3 121 ? 47.992  -61.539 17.186   1.00 174.89 ? 119  VAL H N   1 
ATOM   21185 C  CA  . VAL H  3 121 ? 48.279  -60.678 18.326   1.00 161.52 ? 119  VAL H CA  1 
ATOM   21186 C  C   . VAL H  3 121 ? 47.879  -59.242 18.041   1.00 159.22 ? 119  VAL H C   1 
ATOM   21187 O  O   . VAL H  3 121 ? 47.611  -58.480 18.978   1.00 159.22 ? 119  VAL H O   1 
ATOM   21188 C  CB  . VAL H  3 121 ? 49.769  -60.755 18.704   1.00 173.16 ? 119  VAL H CB  1 
ATOM   21189 C  CG1 . VAL H  3 121 ? 50.002  -60.160 20.085   1.00 173.71 ? 119  VAL H CG1 1 
ATOM   21190 C  CG2 . VAL H  3 121 ? 50.264  -62.197 18.640   1.00 180.08 ? 119  VAL H CG2 1 
ATOM   21191 N  N   . LEU H  3 122 ? 47.824  -58.859 16.766   1.00 161.69 ? 120  LEU H N   1 
ATOM   21192 C  CA  . LEU H  3 122 ? 47.495  -57.486 16.410   1.00 178.83 ? 120  LEU H CA  1 
ATOM   21193 C  C   . LEU H  3 122 ? 46.062  -57.143 16.784   1.00 187.94 ? 120  LEU H C   1 
ATOM   21194 O  O   . LEU H  3 122 ? 45.744  -55.968 17.009   1.00 179.60 ? 120  LEU H O   1 
ATOM   21195 C  CB  . LEU H  3 122 ? 47.707  -57.274 14.911   1.00 170.30 ? 120  LEU H CB  1 
ATOM   21196 C  CG  . LEU H  3 122 ? 49.095  -57.587 14.345   1.00 177.68 ? 120  LEU H CG  1 
ATOM   21197 C  CD1 . LEU H  3 122 ? 49.103  -57.438 12.834   1.00 179.32 ? 120  LEU H CD1 1 
ATOM   21198 C  CD2 . LEU H  3 122 ? 50.152  -56.691 14.972   1.00 185.74 ? 120  LEU H CD2 1 
ATOM   21199 N  N   . LEU H  3 123 ? 45.196  -58.150 16.873   1.00 195.13 ? 121  LEU H N   1 
ATOM   21200 C  CA  . LEU H  3 123 ? 43.782  -57.920 17.134   1.00 178.34 ? 121  LEU H CA  1 
ATOM   21201 C  C   . LEU H  3 123 ? 43.585  -57.322 18.521   1.00 157.83 ? 121  LEU H C   1 
ATOM   21202 O  O   . LEU H  3 123 ? 44.097  -57.846 19.516   1.00 155.68 ? 121  LEU H O   1 
ATOM   21203 C  CB  . LEU H  3 123 ? 43.008  -59.232 16.998   1.00 181.64 ? 121  LEU H CB  1 
ATOM   21204 C  CG  . LEU H  3 123 ? 41.512  -59.175 16.666   1.00 188.22 ? 121  LEU H CG  1 
ATOM   21205 C  CD1 . LEU H  3 123 ? 40.666  -58.886 17.898   1.00 182.70 ? 121  LEU H CD1 1 
ATOM   21206 C  CD2 . LEU H  3 123 ? 41.240  -58.147 15.574   1.00 201.06 ? 121  LEU H CD2 1 
ATOM   21207 N  N   . SER H  3 124 ? 42.854  -56.209 18.579   1.00 151.64 ? 122  SER H N   1 
ATOM   21208 C  CA  . SER H  3 124 ? 42.543  -55.534 19.832   1.00 160.19 ? 122  SER H CA  1 
ATOM   21209 C  C   . SER H  3 124 ? 41.081  -55.705 20.224   1.00 167.55 ? 122  SER H C   1 
ATOM   21210 O  O   . SER H  3 124 ? 40.788  -56.212 21.309   1.00 175.02 ? 122  SER H O   1 
ATOM   21211 C  CB  . SER H  3 124 ? 42.902  -54.046 19.742   1.00 142.36 ? 122  SER H CB  1 
ATOM   21212 O  OG  . SER H  3 124 ? 42.608  -53.388 20.959   1.00 139.12 ? 122  SER H OG  1 
ATOM   21213 N  N   . ARG H  3 125 ? 40.148  -55.272 19.376   1.00 176.46 ? 123  ARG H N   1 
ATOM   21214 C  CA  . ARG H  3 125 ? 38.721  -55.431 19.640   1.00 178.12 ? 123  ARG H CA  1 
ATOM   21215 C  C   . ARG H  3 125 ? 38.012  -55.881 18.371   1.00 167.60 ? 123  ARG H C   1 
ATOM   21216 O  O   . ARG H  3 125 ? 38.206  -55.288 17.305   1.00 179.93 ? 123  ARG H O   1 
ATOM   21217 C  CB  . ARG H  3 125 ? 38.101  -54.127 20.154   1.00 186.52 ? 123  ARG H CB  1 
ATOM   21218 C  CG  . ARG H  3 125 ? 36.612  -54.224 20.449   1.00 187.32 ? 123  ARG H CG  1 
ATOM   21219 C  CD  . ARG H  3 125 ? 36.103  -52.968 21.140   1.00 190.32 ? 123  ARG H CD  1 
ATOM   21220 N  NE  . ARG H  3 125 ? 34.697  -53.084 21.517   1.00 197.39 ? 123  ARG H NE  1 
ATOM   21221 C  CZ  . ARG H  3 125 ? 34.052  -52.208 22.281   1.00 200.34 ? 123  ARG H CZ  1 
ATOM   21222 N  NH1 . ARG H  3 125 ? 34.686  -51.145 22.761   1.00 199.13 ? 123  ARG H NH1 1 
ATOM   21223 N  NH2 . ARG H  3 125 ? 32.772  -52.401 22.571   1.00 208.95 ? 123  ARG H NH2 1 
ATOM   21224 N  N   . ALA H  3 126 ? 37.199  -56.930 18.484   1.00 147.26 ? 124  ALA H N   1 
ATOM   21225 C  CA  . ALA H  3 126 ? 36.456  -57.475 17.348   1.00 146.93 ? 124  ALA H CA  1 
ATOM   21226 C  C   . ALA H  3 126 ? 35.001  -57.671 17.763   1.00 130.70 ? 124  ALA H C   1 
ATOM   21227 O  O   . ALA H  3 126 ? 34.671  -58.655 18.428   1.00 130.63 ? 124  ALA H O   1 
ATOM   21228 C  CB  . ALA H  3 126 ? 37.076  -58.778 16.861   1.00 162.98 ? 124  ALA H CB  1 
ATOM   21229 N  N   . GLU H  3 127 ? 34.135  -56.732 17.387   1.00 133.13 ? 125  GLU H N   1 
ATOM   21230 C  CA  . GLU H  3 127 ? 32.716  -56.788 17.713   1.00 133.59 ? 125  GLU H CA  1 
ATOM   21231 C  C   . GLU H  3 127 ? 31.909  -57.131 16.467   1.00 135.80 ? 125  GLU H C   1 
ATOM   21232 O  O   . GLU H  3 127 ? 32.078  -56.502 15.418   1.00 156.63 ? 125  GLU H O   1 
ATOM   21233 C  CB  . GLU H  3 127 ? 32.228  -55.467 18.314   1.00 150.56 ? 125  GLU H CB  1 
ATOM   21234 C  CG  . GLU H  3 127 ? 32.704  -54.226 17.584   1.00 147.75 ? 125  GLU H CG  1 
ATOM   21235 C  CD  . GLU H  3 127 ? 32.311  -52.947 18.293   1.00 165.28 ? 125  GLU H CD  1 
ATOM   21236 O  OE1 . GLU H  3 127 ? 31.454  -53.010 19.199   1.00 169.23 ? 125  GLU H OE1 1 
ATOM   21237 O  OE2 . GLU H  3 127 ? 32.863  -51.880 17.949   1.00 179.64 ? 125  GLU H OE2 1 
ATOM   21238 N  N   . LEU H  3 128 ? 31.029  -58.123 16.588   1.00 123.48 ? 126  LEU H N   1 
ATOM   21239 C  CA  . LEU H  3 128 ? 30.160  -58.541 15.493   1.00 124.40 ? 126  LEU H CA  1 
ATOM   21240 C  C   . LEU H  3 128 ? 28.880  -57.713 15.520   1.00 126.15 ? 126  LEU H C   1 
ATOM   21241 O  O   . LEU H  3 128 ? 28.145  -57.731 16.514   1.00 142.58 ? 126  LEU H O   1 
ATOM   21242 C  CB  . LEU H  3 128 ? 29.843  -60.033 15.594   1.00 124.93 ? 126  LEU H CB  1 
ATOM   21243 C  CG  . LEU H  3 128 ? 28.851  -60.596 14.571   1.00 138.01 ? 126  LEU H CG  1 
ATOM   21244 C  CD1 . LEU H  3 128 ? 29.386  -60.430 13.162   1.00 166.23 ? 126  LEU H CD1 1 
ATOM   21245 C  CD2 . LEU H  3 128 ? 28.530  -62.062 14.850   1.00 132.36 ? 126  LEU H CD2 1 
ATOM   21246 N  N   . ARG H  3 129 ? 28.614  -56.990 14.434   1.00 141.30 ? 127  ARG H N   1 
ATOM   21247 C  CA  . ARG H  3 129 ? 27.482  -56.077 14.358   1.00 145.70 ? 127  ARG H CA  1 
ATOM   21248 C  C   . ARG H  3 129 ? 26.428  -56.578 13.377   1.00 157.41 ? 127  ARG H C   1 
ATOM   21249 O  O   . ARG H  3 129 ? 26.754  -57.056 12.285   1.00 171.42 ? 127  ARG H O   1 
ATOM   21250 C  CB  . ARG H  3 129 ? 27.949  -54.675 13.965   1.00 145.24 ? 127  ARG H CB  1 
ATOM   21251 C  CG  . ARG H  3 129 ? 29.001  -54.121 14.904   1.00 142.02 ? 127  ARG H CG  1 
ATOM   21252 C  CD  . ARG H  3 129 ? 29.073  -52.614 14.826   1.00 145.10 ? 127  ARG H CD  1 
ATOM   21253 N  NE  . ARG H  3 129 ? 29.953  -52.058 15.849   1.00 142.49 ? 127  ARG H NE  1 
ATOM   21254 C  CZ  . ARG H  3 129 ? 30.091  -50.757 16.088   1.00 153.34 ? 127  ARG H CZ  1 
ATOM   21255 N  NH1 . ARG H  3 129 ? 29.398  -49.874 15.383   1.00 173.94 ? 127  ARG H NH1 1 
ATOM   21256 N  NH2 . ARG H  3 129 ? 30.913  -50.338 17.041   1.00 150.81 ? 127  ARG H NH2 1 
ATOM   21257 N  N   . LEU H  3 130 ? 25.159  -56.455 13.779   1.00 157.35 ? 128  LEU H N   1 
ATOM   21258 C  CA  . LEU H  3 130 ? 24.023  -56.903 12.979   1.00 162.83 ? 128  LEU H CA  1 
ATOM   21259 C  C   . LEU H  3 130 ? 23.077  -55.743 12.686   1.00 179.63 ? 128  LEU H C   1 
ATOM   21260 O  O   . LEU H  3 130 ? 23.441  -54.575 12.854   1.00 198.05 ? 128  LEU H O   1 
ATOM   21261 C  CB  . LEU H  3 130 ? 23.260  -58.012 13.700   1.00 156.79 ? 128  LEU H CB  1 
ATOM   21262 C  CG  . LEU H  3 130 ? 24.062  -59.137 14.348   1.00 148.70 ? 128  LEU H CG  1 
ATOM   21263 C  CD1 . LEU H  3 130 ? 23.129  -60.219 14.843   1.00 150.30 ? 128  LEU H CD1 1 
ATOM   21264 C  CD2 . LEU H  3 130 ? 25.065  -59.712 13.387   1.00 154.95 ? 128  LEU H CD2 1 
ATOM   21265 N  N   . LEU H  3 131 ? 21.853  -56.058 12.268   1.00 168.59 ? 129  LEU H N   1 
ATOM   21266 C  CA  . LEU H  3 131 ? 20.832  -55.050 12.001   1.00 167.26 ? 129  LEU H CA  1 
ATOM   21267 C  C   . LEU H  3 131 ? 19.478  -55.560 12.464   1.00 190.13 ? 129  LEU H C   1 
ATOM   21268 O  O   . LEU H  3 131 ? 18.968  -56.544 11.920   1.00 207.92 ? 129  LEU H O   1 
ATOM   21269 C  CB  . LEU H  3 131 ? 20.783  -54.705 10.514   1.00 176.40 ? 129  LEU H CB  1 
ATOM   21270 C  CG  . LEU H  3 131 ? 19.781  -53.623 10.111   1.00 182.58 ? 129  LEU H CG  1 
ATOM   21271 C  CD1 . LEU H  3 131 ? 19.810  -52.444 11.069   1.00 175.39 ? 129  LEU H CD1 1 
ATOM   21272 C  CD2 . LEU H  3 131 ? 20.045  -53.173 8.682    1.00 209.29 ? 129  LEU H CD2 1 
ATOM   21273 N  N   . ARG H  3 132 ? 18.886  -54.881 13.441   1.00 200.51 ? 130  ARG H N   1 
ATOM   21274 C  CA  . ARG H  3 132 ? 17.582  -55.265 13.961   1.00 193.17 ? 130  ARG H CA  1 
ATOM   21275 C  C   . ARG H  3 132 ? 16.469  -54.668 13.112   1.00 196.58 ? 130  ARG H C   1 
ATOM   21276 O  O   . ARG H  3 132 ? 16.653  -53.668 12.414   1.00 214.54 ? 130  ARG H O   1 
ATOM   21277 C  CB  . ARG H  3 132 ? 17.395  -54.796 15.407   1.00 188.79 ? 130  ARG H CB  1 
ATOM   21278 C  CG  . ARG H  3 132 ? 18.128  -55.589 16.470   1.00 186.94 ? 130  ARG H CG  1 
ATOM   21279 C  CD  . ARG H  3 132 ? 17.687  -55.110 17.859   1.00 221.23 ? 130  ARG H CD  1 
ATOM   21280 N  NE  . ARG H  3 132 ? 18.397  -55.777 18.950   1.00 239.57 ? 130  ARG H NE  1 
ATOM   21281 C  CZ  . ARG H  3 132 ? 18.225  -55.501 20.242   1.00 231.80 ? 130  ARG H CZ  1 
ATOM   21282 N  NH1 . ARG H  3 132 ? 17.361  -54.564 20.616   1.00 216.15 ? 130  ARG H NH1 1 
ATOM   21283 N  NH2 . ARG H  3 132 ? 18.919  -56.159 21.164   1.00 224.88 ? 130  ARG H NH2 1 
ATOM   21284 N  N   . LEU H  3 133 ? 15.314  -55.309 13.166   1.00 179.94 ? 131  LEU H N   1 
ATOM   21285 C  CA  . LEU H  3 133 ? 14.082  -54.750 12.643   1.00 187.79 ? 131  LEU H CA  1 
ATOM   21286 C  C   . LEU H  3 133 ? 13.155  -54.488 13.819   1.00 187.56 ? 131  LEU H C   1 
ATOM   21287 O  O   . LEU H  3 133 ? 13.450  -54.868 14.955   1.00 185.26 ? 131  LEU H O   1 
ATOM   21288 C  CB  . LEU H  3 133 ? 13.439  -55.699 11.628   1.00 193.89 ? 131  LEU H CB  1 
ATOM   21289 C  CG  . LEU H  3 133 ? 14.206  -55.778 10.311   1.00 204.54 ? 131  LEU H CG  1 
ATOM   21290 C  CD1 . LEU H  3 133 ? 13.516  -56.715 9.337    1.00 220.04 ? 131  LEU H CD1 1 
ATOM   21291 C  CD2 . LEU H  3 133 ? 14.362  -54.390 9.711    1.00 199.91 ? 131  LEU H CD2 1 
ATOM   21292 N  N   . LYS H  3 134 ? 12.046  -53.807 13.555   1.00 189.34 ? 132  LYS H N   1 
ATOM   21293 C  CA  . LYS H  3 134 ? 11.115  -53.521 14.637   1.00 199.99 ? 132  LYS H CA  1 
ATOM   21294 C  C   . LYS H  3 134 ? 10.588  -54.831 15.220   1.00 218.38 ? 132  LYS H C   1 
ATOM   21295 O  O   . LYS H  3 134 ? 10.102  -55.702 14.490   1.00 233.21 ? 132  LYS H O   1 
ATOM   21296 C  CB  . LYS H  3 134 ? 9.969   -52.635 14.136   1.00 217.41 ? 132  LYS H CB  1 
ATOM   21297 C  CG  . LYS H  3 134 ? 9.147   -53.212 12.983   1.00 220.05 ? 132  LYS H CG  1 
ATOM   21298 C  CD  . LYS H  3 134 ? 7.976   -52.300 12.627   1.00 228.04 ? 132  LYS H CD  1 
ATOM   21299 C  CE  . LYS H  3 134 ? 7.140   -52.866 11.485   1.00 219.15 ? 132  LYS H CE  1 
ATOM   21300 N  NZ  . LYS H  3 134 ? 5.971   -51.997 11.168   1.00 219.05 ? 132  LYS H NZ  1 
ATOM   21301 N  N   . LEU H  3 135 ? 10.721  -54.989 16.539   1.00 226.51 ? 133  LEU H N   1 
ATOM   21302 C  CA  . LEU H  3 135 ? 10.311  -56.213 17.212   1.00 233.92 ? 133  LEU H CA  1 
ATOM   21303 C  C   . LEU H  3 135 ? 9.336   -55.954 18.352   1.00 237.06 ? 133  LEU H C   1 
ATOM   21304 O  O   . LEU H  3 135 ? 8.793   -56.913 18.917   1.00 238.30 ? 133  LEU H O   1 
ATOM   21305 C  CB  . LEU H  3 135 ? 11.536  -56.977 17.739   1.00 226.24 ? 133  LEU H CB  1 
ATOM   21306 C  CG  . LEU H  3 135 ? 11.325  -58.474 17.965   1.00 221.17 ? 133  LEU H CG  1 
ATOM   21307 C  CD1 . LEU H  3 135 ? 10.719  -59.115 16.724   1.00 204.69 ? 133  LEU H CD1 1 
ATOM   21308 C  CD2 . LEU H  3 135 ? 12.631  -59.147 18.329   1.00 227.31 ? 133  LEU H CD2 1 
ATOM   21309 N  N   . LYS H  3 136 ? 9.120   -54.695 18.711   1.00 224.87 ? 134  LYS H N   1 
ATOM   21310 C  CA  . LYS H  3 136 ? 8.189   -54.268 19.762   1.00 219.04 ? 134  LYS H CA  1 
ATOM   21311 C  C   . LYS H  3 136 ? 8.579   -54.942 21.082   1.00 218.29 ? 134  LYS H C   1 
ATOM   21312 O  O   . LYS H  3 136 ? 9.779   -55.101 21.367   1.00 212.57 ? 134  LYS H O   1 
ATOM   21313 C  CB  . LYS H  3 136 ? 6.761   -54.524 19.326   1.00 225.26 ? 134  LYS H CB  1 
ATOM   21314 C  CG  . LYS H  3 136 ? 6.320   -53.762 18.082   1.00 236.54 ? 134  LYS H CG  1 
ATOM   21315 C  CD  . LYS H  3 136 ? 4.894   -54.128 17.688   1.00 251.06 ? 134  LYS H CD  1 
ATOM   21316 C  CE  . LYS H  3 136 ? 4.436   -53.391 16.433   1.00 253.97 ? 134  LYS H CE  1 
ATOM   21317 N  NZ  . LYS H  3 136 ? 3.037   -53.766 16.074   1.00 263.56 ? 134  LYS H NZ  1 
ATOM   21318 N  N   . VAL H  3 137 ? 7.587   -55.407 21.840   1.00 237.60 ? 135  VAL H N   1 
ATOM   21319 C  CA  . VAL H  3 137 ? 7.631   -55.589 23.290   1.00 265.30 ? 135  VAL H CA  1 
ATOM   21320 C  C   . VAL H  3 137 ? 8.933   -56.193 23.812   1.00 264.83 ? 135  VAL H C   1 
ATOM   21321 O  O   . VAL H  3 137 ? 9.799   -55.470 24.320   1.00 273.03 ? 135  VAL H O   1 
ATOM   21322 C  CB  . VAL H  3 137 ? 6.424   -56.426 23.749   1.00 262.01 ? 135  VAL H CB  1 
ATOM   21323 C  CG1 . VAL H  3 137 ? 6.186   -56.227 25.242   1.00 243.78 ? 135  VAL H CG1 1 
ATOM   21324 C  CG2 . VAL H  3 137 ? 5.177   -56.053 22.950   1.00 250.08 ? 135  VAL H CG2 1 
ATOM   21325 N  N   . GLU H  3 138 ? 9.094   -57.508 23.693   1.00 237.34 ? 136  GLU H N   1 
ATOM   21326 C  CA  . GLU H  3 138 ? 10.177  -58.168 24.405   1.00 219.01 ? 136  GLU H CA  1 
ATOM   21327 C  C   . GLU H  3 138 ? 10.745  -59.315 23.588   1.00 203.91 ? 136  GLU H C   1 
ATOM   21328 O  O   . GLU H  3 138 ? 10.016  -60.003 22.870   1.00 210.01 ? 136  GLU H O   1 
ATOM   21329 C  CB  . GLU H  3 138 ? 9.705   -58.706 25.765   1.00 221.03 ? 136  GLU H CB  1 
ATOM   21330 C  CG  . GLU H  3 138 ? 9.494   -57.655 26.843   1.00 207.51 ? 136  GLU H CG  1 
ATOM   21331 C  CD  . GLU H  3 138 ? 8.835   -58.223 28.091   1.00 204.93 ? 136  GLU H CD  1 
ATOM   21332 O  OE1 . GLU H  3 138 ? 7.609   -58.465 28.070   1.00 208.76 ? 136  GLU H OE1 1 
ATOM   21333 O  OE2 . GLU H  3 138 ? 9.547   -58.440 29.093   1.00 204.74 ? 136  GLU H OE2 1 
ATOM   21334 N  N   . GLN H  3 139 ? 12.061  -59.478 23.671   1.00 192.63 ? 137  GLN H N   1 
ATOM   21335 C  CA  . GLN H  3 139 ? 12.697  -60.711 23.240   1.00 193.08 ? 137  GLN H CA  1 
ATOM   21336 C  C   . GLN H  3 139 ? 14.009  -60.872 23.997   1.00 188.58 ? 137  GLN H C   1 
ATOM   21337 O  O   . GLN H  3 139 ? 14.594  -59.898 24.477   1.00 183.94 ? 137  GLN H O   1 
ATOM   21338 C  CB  . GLN H  3 139 ? 12.920  -60.730 21.723   1.00 198.61 ? 137  GLN H CB  1 
ATOM   21339 C  CG  . GLN H  3 139 ? 13.083  -62.120 21.105   1.00 206.63 ? 137  GLN H CG  1 
ATOM   21340 C  CD  . GLN H  3 139 ? 11.852  -63.008 21.222   1.00 216.46 ? 137  GLN H CD  1 
ATOM   21341 O  OE1 . GLN H  3 139 ? 11.961  -64.235 21.174   1.00 219.61 ? 137  GLN H OE1 1 
ATOM   21342 N  NE2 . GLN H  3 139 ? 10.677  -62.397 21.343   1.00 221.28 ? 137  GLN H NE2 1 
ATOM   21343 N  N   . HIS H  3 140 ? 14.459  -62.122 24.111   1.00 188.01 ? 138  HIS H N   1 
ATOM   21344 C  CA  . HIS H  3 140 ? 15.735  -62.451 24.738   1.00 194.68 ? 138  HIS H CA  1 
ATOM   21345 C  C   . HIS H  3 140 ? 16.553  -63.327 23.801   1.00 204.51 ? 138  HIS H C   1 
ATOM   21346 O  O   . HIS H  3 140 ? 16.037  -64.303 23.247   1.00 212.75 ? 138  HIS H O   1 
ATOM   21347 C  CB  . HIS H  3 140 ? 15.535  -63.160 26.075   1.00 194.89 ? 138  HIS H CB  1 
ATOM   21348 C  CG  . HIS H  3 140 ? 16.797  -63.314 26.865   1.00 193.34 ? 138  HIS H CG  1 
ATOM   21349 N  ND1 . HIS H  3 140 ? 16.883  -64.123 27.976   1.00 208.39 ? 138  HIS H ND1 1 
ATOM   21350 C  CD2 . HIS H  3 140 ? 18.021  -62.756 26.711   1.00 180.04 ? 138  HIS H CD2 1 
ATOM   21351 C  CE1 . HIS H  3 140 ? 18.108  -64.067 28.467   1.00 194.60 ? 138  HIS H CE1 1 
ATOM   21352 N  NE2 . HIS H  3 140 ? 18.818  -63.243 27.719   1.00 181.76 ? 138  HIS H NE2 1 
ATOM   21353 N  N   . VAL H  3 141 ? 17.829  -62.984 23.633   1.00 201.83 ? 139  VAL H N   1 
ATOM   21354 C  CA  . VAL H  3 141 ? 18.704  -63.617 22.652   1.00 196.36 ? 139  VAL H CA  1 
ATOM   21355 C  C   . VAL H  3 141 ? 19.958  -64.139 23.347   1.00 202.38 ? 139  VAL H C   1 
ATOM   21356 O  O   . VAL H  3 141 ? 20.542  -63.446 24.189   1.00 205.18 ? 139  VAL H O   1 
ATOM   21357 C  CB  . VAL H  3 141 ? 19.064  -62.637 21.523   1.00 197.00 ? 139  VAL H CB  1 
ATOM   21358 C  CG1 . VAL H  3 141 ? 20.005  -63.290 20.530   1.00 205.92 ? 139  VAL H CG1 1 
ATOM   21359 C  CG2 . VAL H  3 141 ? 17.801  -62.154 20.830   1.00 196.92 ? 139  VAL H CG2 1 
ATOM   21360 N  N   . GLU H  3 142 ? 20.349  -65.373 23.015   1.00 202.36 ? 140  GLU H N   1 
ATOM   21361 C  CA  . GLU H  3 142 ? 21.615  -65.962 23.438   1.00 192.37 ? 140  GLU H CA  1 
ATOM   21362 C  C   . GLU H  3 142 ? 22.488  -66.235 22.220   1.00 190.20 ? 140  GLU H C   1 
ATOM   21363 O  O   . GLU H  3 142 ? 21.995  -66.689 21.184   1.00 193.97 ? 140  GLU H O   1 
ATOM   21364 C  CB  . GLU H  3 142 ? 21.389  -67.262 24.209   1.00 188.47 ? 140  GLU H CB  1 
ATOM   21365 C  CG  . GLU H  3 142 ? 20.539  -67.095 25.446   1.00 209.44 ? 140  GLU H CG  1 
ATOM   21366 C  CD  . GLU H  3 142 ? 20.312  -68.404 26.159   1.00 211.69 ? 140  GLU H CD  1 
ATOM   21367 O  OE1 . GLU H  3 142 ? 20.915  -69.413 25.736   1.00 205.28 ? 140  GLU H OE1 1 
ATOM   21368 O  OE2 . GLU H  3 142 ? 19.528  -68.426 27.133   1.00 218.28 ? 140  GLU H OE2 1 
ATOM   21369 N  N   . LEU H  3 143 ? 23.789  -65.984 22.356   1.00 187.55 ? 141  LEU H N   1 
ATOM   21370 C  CA  . LEU H  3 143 ? 24.736  -66.135 21.259   1.00 180.77 ? 141  LEU H CA  1 
ATOM   21371 C  C   . LEU H  3 143 ? 25.672  -67.307 21.517   1.00 191.02 ? 141  LEU H C   1 
ATOM   21372 O  O   . LEU H  3 143 ? 26.051  -67.574 22.663   1.00 201.83 ? 141  LEU H O   1 
ATOM   21373 C  CB  . LEU H  3 143 ? 25.552  -64.855 21.050   1.00 172.56 ? 141  LEU H CB  1 
ATOM   21374 C  CG  . LEU H  3 143 ? 26.489  -64.827 19.836   1.00 149.87 ? 141  LEU H CG  1 
ATOM   21375 C  CD1 . LEU H  3 143 ? 25.722  -64.990 18.530   1.00 144.52 ? 141  LEU H CD1 1 
ATOM   21376 C  CD2 . LEU H  3 143 ? 27.309  -63.544 19.819   1.00 147.90 ? 141  LEU H CD2 1 
ATOM   21377 N  N   . TYR H  3 144 ? 26.037  -68.009 20.443   1.00 177.42 ? 142  TYR H N   1 
ATOM   21378 C  CA  . TYR H  3 144 ? 26.883  -69.188 20.533   1.00 173.72 ? 142  TYR H CA  1 
ATOM   21379 C  C   . TYR H  3 144 ? 28.045  -69.089 19.549   1.00 147.23 ? 142  TYR H C   1 
ATOM   21380 O  O   . TYR H  3 144 ? 28.059  -68.266 18.629   1.00 142.84 ? 142  TYR H O   1 
ATOM   21381 C  CB  . TYR H  3 144 ? 26.075  -70.472 20.283   1.00 179.54 ? 142  TYR H CB  1 
ATOM   21382 C  CG  . TYR H  3 144 ? 25.046  -70.768 21.355   1.00 174.54 ? 142  TYR H CG  1 
ATOM   21383 C  CD1 . TYR H  3 144 ? 25.378  -71.512 22.482   1.00 176.32 ? 142  TYR H CD1 1 
ATOM   21384 C  CD2 . TYR H  3 144 ? 23.743  -70.301 21.241   1.00 179.72 ? 142  TYR H CD2 1 
ATOM   21385 C  CE1 . TYR H  3 144 ? 24.439  -71.781 23.464   1.00 190.25 ? 142  TYR H CE1 1 
ATOM   21386 C  CE2 . TYR H  3 144 ? 22.801  -70.564 22.217   1.00 193.19 ? 142  TYR H CE2 1 
ATOM   21387 C  CZ  . TYR H  3 144 ? 23.152  -71.304 23.325   1.00 203.93 ? 142  TYR H CZ  1 
ATOM   21388 O  OH  . TYR H  3 144 ? 22.208  -71.564 24.292   1.00 223.22 ? 142  TYR H OH  1 
ATOM   21389 N  N   . GLN H  3 145 ? 29.021  -69.964 19.759   1.00 174.55 ? 143  GLN H N   1 
ATOM   21390 C  CA  . GLN H  3 145 ? 30.220  -70.061 18.945   1.00 172.96 ? 143  GLN H CA  1 
ATOM   21391 C  C   . GLN H  3 145 ? 30.339  -71.481 18.414   1.00 192.54 ? 143  GLN H C   1 
ATOM   21392 O  O   . GLN H  3 145 ? 29.877  -72.439 19.045   1.00 208.16 ? 143  GLN H O   1 
ATOM   21393 C  CB  . GLN H  3 145 ? 31.465  -69.703 19.763   1.00 171.88 ? 143  GLN H CB  1 
ATOM   21394 C  CG  . GLN H  3 145 ? 32.773  -69.656 18.985   1.00 178.29 ? 143  GLN H CG  1 
ATOM   21395 C  CD  . GLN H  3 145 ? 33.981  -69.538 19.901   1.00 172.65 ? 143  GLN H CD  1 
ATOM   21396 O  OE1 . GLN H  3 145 ? 33.843  -69.237 21.087   1.00 182.41 ? 143  GLN H OE1 1 
ATOM   21397 N  NE2 . GLN H  3 145 ? 35.171  -69.783 19.356   1.00 164.01 ? 143  GLN H NE2 1 
ATOM   21398 N  N   . LYS H  3 146 ? 30.955  -71.614 17.245   1.00 184.40 ? 144  LYS H N   1 
ATOM   21399 C  CA  . LYS H  3 146 ? 31.161  -72.930 16.651   1.00 186.51 ? 144  LYS H CA  1 
ATOM   21400 C  C   . LYS H  3 146 ? 32.417  -73.567 17.236   1.00 191.91 ? 144  LYS H C   1 
ATOM   21401 O  O   . LYS H  3 146 ? 33.516  -73.011 17.123   1.00 184.48 ? 144  LYS H O   1 
ATOM   21402 C  CB  . LYS H  3 146 ? 31.267  -72.827 15.131   1.00 194.29 ? 144  LYS H CB  1 
ATOM   21403 C  CG  . LYS H  3 146 ? 31.373  -74.164 14.415   1.00 202.99 ? 144  LYS H CG  1 
ATOM   21404 C  CD  . LYS H  3 146 ? 31.508  -73.978 12.910   1.00 205.43 ? 144  LYS H CD  1 
ATOM   21405 C  CE  . LYS H  3 146 ? 32.758  -73.190 12.526   1.00 197.14 ? 144  LYS H CE  1 
ATOM   21406 N  NZ  . LYS H  3 146 ? 34.004  -73.924 12.891   1.00 184.41 ? 144  LYS H NZ  1 
ATOM   21407 N  N   . TYR H  3 147 ? 32.252  -74.727 17.868   1.00 198.31 ? 145  TYR H N   1 
ATOM   21408 C  CA  . TYR H  3 147 ? 33.353  -75.498 18.439   1.00 195.28 ? 145  TYR H CA  1 
ATOM   21409 C  C   . TYR H  3 147 ? 33.560  -76.728 17.595   1.00 202.08 ? 145  TYR H C   1 
ATOM   21410 O  O   . TYR H  3 147 ? 32.605  -77.477 17.339   1.00 206.24 ? 145  TYR H O   1 
ATOM   21411 C  CB  . TYR H  3 147 ? 33.078  -75.935 19.870   1.00 199.89 ? 145  TYR H CB  1 
ATOM   21412 C  CG  . TYR H  3 147 ? 33.695  -75.006 20.847   1.00 229.13 ? 145  TYR H CG  1 
ATOM   21413 C  CD1 . TYR H  3 147 ? 34.913  -75.287 21.436   1.00 234.36 ? 145  TYR H CD1 1 
ATOM   21414 C  CD2 . TYR H  3 147 ? 33.132  -73.770 21.058   1.00 255.45 ? 145  TYR H CD2 1 
ATOM   21415 C  CE1 . TYR H  3 147 ? 35.488  -74.405 22.306   1.00 244.01 ? 145  TYR H CE1 1 
ATOM   21416 C  CE2 . TYR H  3 147 ? 33.695  -72.861 21.882   1.00 257.99 ? 145  TYR H CE2 1 
ATOM   21417 C  CZ  . TYR H  3 147 ? 34.867  -73.176 22.530   1.00 249.64 ? 145  TYR H CZ  1 
ATOM   21418 O  OH  . TYR H  3 147 ? 35.379  -72.230 23.377   1.00 235.15 ? 145  TYR H OH  1 
ATOM   21419 N  N   . SER H  3 148 ? 34.807  -76.932 17.187   1.00 237.90 ? 146  SER H N   1 
ATOM   21420 C  CA  . SER H  3 148 ? 35.140  -77.999 16.276   1.00 253.67 ? 146  SER H CA  1 
ATOM   21421 C  C   . SER H  3 148 ? 34.234  -77.768 15.075   1.00 252.11 ? 146  SER H C   1 
ATOM   21422 O  O   . SER H  3 148 ? 34.257  -76.666 14.505   1.00 237.07 ? 146  SER H O   1 
ATOM   21423 C  CB  . SER H  3 148 ? 34.956  -79.319 17.028   1.00 238.43 ? 146  SER H CB  1 
ATOM   21424 O  OG  . SER H  3 148 ? 35.285  -79.133 18.413   1.00 229.69 ? 146  SER H OG  1 
ATOM   21425 N  N   . GLN H  3 149 ? 33.381  -78.713 14.709   1.00 251.20 ? 147  GLN H N   1 
ATOM   21426 C  CA  . GLN H  3 149 ? 32.340  -78.431 13.733   1.00 246.14 ? 147  GLN H CA  1 
ATOM   21427 C  C   . GLN H  3 149 ? 30.950  -78.703 14.303   1.00 242.29 ? 147  GLN H C   1 
ATOM   21428 O  O   . GLN H  3 149 ? 29.969  -77.974 14.024   1.00 253.78 ? 147  GLN H O   1 
ATOM   21429 C  CB  . GLN H  3 149 ? 32.516  -79.329 12.506   1.00 241.01 ? 147  GLN H CB  1 
ATOM   21430 C  CG  . GLN H  3 149 ? 32.986  -78.698 11.199   1.00 244.00 ? 147  GLN H CG  1 
ATOM   21431 C  CD  . GLN H  3 149 ? 34.423  -79.077 10.820   1.00 251.31 ? 147  GLN H CD  1 
ATOM   21432 O  OE1 . GLN H  3 149 ? 34.660  -79.985 10.017   1.00 259.10 ? 147  GLN H OE1 1 
ATOM   21433 N  NE2 . GLN H  3 149 ? 35.385  -78.365 11.393   1.00 241.30 ? 147  GLN H NE2 1 
ATOM   21434 N  N   . ASN H  3 150 ? 30.867  -79.781 15.111   1.00 235.01 ? 148  ASN H N   1 
ATOM   21435 C  CA  . ASN H  3 150 ? 29.613  -80.288 15.675   1.00 237.03 ? 148  ASN H CA  1 
ATOM   21436 C  C   . ASN H  3 150 ? 29.064  -79.380 16.798   1.00 237.86 ? 148  ASN H C   1 
ATOM   21437 O  O   . ASN H  3 150 ? 27.904  -78.939 16.723   1.00 226.68 ? 148  ASN H O   1 
ATOM   21438 C  CB  . ASN H  3 150 ? 29.852  -81.711 16.243   1.00 239.35 ? 148  ASN H CB  1 
ATOM   21439 C  CG  . ASN H  3 150 ? 30.074  -82.955 15.125   1.00 236.79 ? 148  ASN H CG  1 
ATOM   21440 O  OD1 . ASN H  3 150 ? 29.380  -83.085 14.025   1.00 225.93 ? 148  ASN H OD1 1 
ATOM   21441 N  ND2 . ASN H  3 150 ? 31.024  -83.863 15.486   1.00 241.01 ? 148  ASN H ND2 1 
ATOM   21442 N  N   . SER H  3 151 ? 29.909  -78.973 17.763   1.00 234.43 ? 149  SER H N   1 
ATOM   21443 C  CA  . SER H  3 151 ? 29.429  -78.366 19.002   1.00 229.18 ? 149  SER H CA  1 
ATOM   21444 C  C   . SER H  3 151 ? 29.355  -76.831 19.014   1.00 211.58 ? 149  SER H C   1 
ATOM   21445 O  O   . SER H  3 151 ? 30.073  -76.127 18.295   1.00 200.25 ? 149  SER H O   1 
ATOM   21446 C  CB  . SER H  3 151 ? 30.304  -78.841 20.179   1.00 230.89 ? 149  SER H CB  1 
ATOM   21447 O  OG  . SER H  3 151 ? 30.420  -80.254 20.184   1.00 239.03 ? 149  SER H OG  1 
ATOM   21448 N  N   . TRP H  3 152 ? 28.418  -76.331 19.830   1.00 195.80 ? 150  TRP H N   1 
ATOM   21449 C  CA  . TRP H  3 152 ? 28.166  -74.913 20.050   1.00 187.25 ? 150  TRP H CA  1 
ATOM   21450 C  C   . TRP H  3 152 ? 28.271  -74.607 21.545   1.00 194.42 ? 150  TRP H C   1 
ATOM   21451 O  O   . TRP H  3 152 ? 27.731  -75.358 22.361   1.00 217.34 ? 150  TRP H O   1 
ATOM   21452 C  CB  . TRP H  3 152 ? 26.766  -74.528 19.566   1.00 188.86 ? 150  TRP H CB  1 
ATOM   21453 C  CG  . TRP H  3 152 ? 26.448  -74.962 18.174   1.00 200.52 ? 150  TRP H CG  1 
ATOM   21454 C  CD1 . TRP H  3 152 ? 25.826  -76.119 17.792   1.00 209.66 ? 150  TRP H CD1 1 
ATOM   21455 C  CD2 . TRP H  3 152 ? 26.738  -74.245 16.973   1.00 197.20 ? 150  TRP H CD2 1 
ATOM   21456 N  NE1 . TRP H  3 152 ? 25.693  -76.152 16.424   1.00 197.35 ? 150  TRP H NE1 1 
ATOM   21457 C  CE2 . TRP H  3 152 ? 26.249  -75.015 15.898   1.00 193.82 ? 150  TRP H CE2 1 
ATOM   21458 C  CE3 . TRP H  3 152 ? 27.361  -73.024 16.702   1.00 188.30 ? 150  TRP H CE3 1 
ATOM   21459 C  CZ2 . TRP H  3 152 ? 26.363  -74.603 14.574   1.00 184.10 ? 150  TRP H CZ2 1 
ATOM   21460 C  CZ3 . TRP H  3 152 ? 27.474  -72.616 15.385   1.00 184.70 ? 150  TRP H CZ3 1 
ATOM   21461 C  CH2 . TRP H  3 152 ? 26.977  -73.405 14.338   1.00 179.07 ? 150  TRP H CH2 1 
ATOM   21462 N  N   . ARG H  3 153 ? 28.977  -73.527 21.911   1.00 167.17 ? 151  ARG H N   1 
ATOM   21463 C  CA  . ARG H  3 153 ? 29.113  -73.070 23.292   1.00 169.62 ? 151  ARG H CA  1 
ATOM   21464 C  C   . ARG H  3 153 ? 28.616  -71.634 23.467   1.00 168.23 ? 151  ARG H C   1 
ATOM   21465 O  O   . ARG H  3 153 ? 28.837  -70.755 22.619   1.00 163.21 ? 151  ARG H O   1 
ATOM   21466 C  CB  . ARG H  3 153 ? 30.535  -73.153 23.785   1.00 167.35 ? 151  ARG H CB  1 
ATOM   21467 C  CG  . ARG H  3 153 ? 30.725  -72.678 25.249   1.00 170.80 ? 151  ARG H CG  1 
ATOM   21468 C  CD  . ARG H  3 153 ? 32.211  -72.627 25.526   1.00 187.78 ? 151  ARG H CD  1 
ATOM   21469 N  NE  . ARG H  3 153 ? 32.736  -72.025 26.753   1.00 208.84 ? 151  ARG H NE  1 
ATOM   21470 C  CZ  . ARG H  3 153 ? 33.138  -70.753 26.847   1.00 205.06 ? 151  ARG H CZ  1 
ATOM   21471 N  NH1 . ARG H  3 153 ? 33.075  -69.945 25.803   1.00 212.45 ? 151  ARG H NH1 1 
ATOM   21472 N  NH2 . ARG H  3 153 ? 33.665  -70.299 27.980   1.00 187.54 ? 151  ARG H NH2 1 
ATOM   21473 N  N   . TYR H  3 154 ? 28.017  -71.408 24.628   1.00 166.96 ? 152  TYR H N   1 
ATOM   21474 C  CA  . TYR H  3 154 ? 27.468  -70.128 25.021   1.00 166.84 ? 152  TYR H CA  1 
ATOM   21475 C  C   . TYR H  3 154 ? 28.523  -69.029 24.959   1.00 160.70 ? 152  TYR H C   1 
ATOM   21476 O  O   . TYR H  3 154 ? 29.723  -69.280 25.101   1.00 159.43 ? 152  TYR H O   1 
ATOM   21477 C  CB  . TYR H  3 154 ? 26.927  -70.257 26.434   1.00 189.48 ? 152  TYR H CB  1 
ATOM   21478 C  CG  . TYR H  3 154 ? 26.267  -69.016 26.910   1.00 210.15 ? 152  TYR H CG  1 
ATOM   21479 C  CD1 . TYR H  3 154 ? 24.953  -68.766 26.580   1.00 206.22 ? 152  TYR H CD1 1 
ATOM   21480 C  CD2 . TYR H  3 154 ? 26.943  -68.101 27.702   1.00 221.53 ? 152  TYR H CD2 1 
ATOM   21481 C  CE1 . TYR H  3 154 ? 24.329  -67.643 26.993   1.00 203.39 ? 152  TYR H CE1 1 
ATOM   21482 C  CE2 . TYR H  3 154 ? 26.325  -66.970 28.131   1.00 212.58 ? 152  TYR H CE2 1 
ATOM   21483 C  CZ  . TYR H  3 154 ? 25.016  -66.744 27.773   1.00 203.14 ? 152  TYR H CZ  1 
ATOM   21484 O  OH  . TYR H  3 154 ? 24.399  -65.604 28.206   1.00 190.29 ? 152  TYR H OH  1 
ATOM   21485 N  N   . LEU H  3 155 ? 28.058  -67.804 24.708   1.00 161.28 ? 153  LEU H N   1 
ATOM   21486 C  CA  . LEU H  3 155 ? 28.900  -66.612 24.690   1.00 155.48 ? 153  LEU H CA  1 
ATOM   21487 C  C   . LEU H  3 155 ? 28.296  -65.555 25.604   1.00 165.34 ? 153  LEU H C   1 
ATOM   21488 O  O   . LEU H  3 155 ? 28.642  -65.475 26.788   1.00 175.69 ? 153  LEU H O   1 
ATOM   21489 C  CB  . LEU H  3 155 ? 29.061  -66.070 23.266   1.00 147.97 ? 153  LEU H CB  1 
ATOM   21490 C  CG  . LEU H  3 155 ? 29.844  -66.967 22.304   1.00 145.96 ? 153  LEU H CG  1 
ATOM   21491 C  CD1 . LEU H  3 155 ? 30.003  -66.296 20.952   1.00 146.18 ? 153  LEU H CD1 1 
ATOM   21492 C  CD2 . LEU H  3 155 ? 31.200  -67.324 22.889   1.00 146.69 ? 153  LEU H CD2 1 
ATOM   21493 N  N   . SER H  3 156 ? 27.370  -64.758 25.076   1.00 157.98 ? 154  SER H N   1 
ATOM   21494 C  CA  . SER H  3 156 ? 26.727  -63.706 25.848   1.00 153.07 ? 154  SER H CA  1 
ATOM   21495 C  C   . SER H  3 156 ? 25.221  -63.761 25.632   1.00 154.88 ? 154  SER H C   1 
ATOM   21496 O  O   . SER H  3 156 ? 24.701  -64.592 24.882   1.00 156.86 ? 154  SER H O   1 
ATOM   21497 C  CB  . SER H  3 156 ? 27.271  -62.322 25.476   1.00 146.62 ? 154  SER H CB  1 
ATOM   21498 O  OG  . SER H  3 156 ? 26.958  -61.991 24.138   1.00 140.88 ? 154  SER H OG  1 
ATOM   21499 N  N   . ASN H  3 157 ? 24.521  -62.869 26.326   1.00 161.61 ? 155  ASN H N   1 
ATOM   21500 C  CA  . ASN H  3 157 ? 23.077  -62.733 26.223   1.00 163.30 ? 155  ASN H CA  1 
ATOM   21501 C  C   . ASN H  3 157 ? 22.720  -61.256 26.263   1.00 158.55 ? 155  ASN H C   1 
ATOM   21502 O  O   . ASN H  3 157 ? 23.500  -60.425 26.735   1.00 155.55 ? 155  ASN H O   1 
ATOM   21503 C  CB  . ASN H  3 157 ? 22.357  -63.471 27.352   1.00 182.87 ? 155  ASN H CB  1 
ATOM   21504 C  CG  . ASN H  3 157 ? 22.726  -62.929 28.716   1.00 204.66 ? 155  ASN H CG  1 
ATOM   21505 O  OD1 . ASN H  3 157 ? 22.112  -61.982 29.212   1.00 205.35 ? 155  ASN H OD1 1 
ATOM   21506 N  ND2 . ASN H  3 157 ? 23.751  -63.517 29.324   1.00 219.41 ? 155  ASN H ND2 1 
ATOM   21507 N  N   . ARG H  3 158 ? 21.532  -60.929 25.755   1.00 167.97 ? 156  ARG H N   1 
ATOM   21508 C  CA  . ARG H  3 158 ? 21.102  -59.536 25.738   1.00 182.46 ? 156  ARG H CA  1 
ATOM   21509 C  C   . ARG H  3 158 ? 19.584  -59.467 25.646   1.00 189.44 ? 156  ARG H C   1 
ATOM   21510 O  O   . ARG H  3 158 ? 18.976  -60.170 24.832   1.00 181.33 ? 156  ARG H O   1 
ATOM   21511 C  CB  . ARG H  3 158 ? 21.756  -58.776 24.574   1.00 193.60 ? 156  ARG H CB  1 
ATOM   21512 C  CG  . ARG H  3 158 ? 21.584  -57.264 24.651   1.00 204.76 ? 156  ARG H CG  1 
ATOM   21513 C  CD  . ARG H  3 158 ? 22.614  -56.514 23.796   1.00 214.69 ? 156  ARG H CD  1 
ATOM   21514 N  NE  . ARG H  3 158 ? 23.994  -56.889 24.113   1.00 215.54 ? 156  ARG H NE  1 
ATOM   21515 C  CZ  . ARG H  3 158 ? 25.071  -56.416 23.486   1.00 167.77 ? 156  ARG H CZ  1 
ATOM   21516 N  NH1 . ARG H  3 158 ? 24.943  -55.530 22.507   1.00 146.18 ? 156  ARG H NH1 1 
ATOM   21517 N  NH2 . ARG H  3 158 ? 26.282  -56.823 23.846   1.00 154.03 ? 156  ARG H NH2 1 
ATOM   21518 N  N   . LEU H  3 159 ? 18.979  -58.641 26.499   1.00 201.99 ? 157  LEU H N   1 
ATOM   21519 C  CA  . LEU H  3 159 ? 17.548  -58.379 26.445   1.00 197.78 ? 157  LEU H CA  1 
ATOM   21520 C  C   . LEU H  3 159 ? 17.259  -57.292 25.411   1.00 196.68 ? 157  LEU H C   1 
ATOM   21521 O  O   . LEU H  3 159 ? 18.117  -56.460 25.100   1.00 179.37 ? 157  LEU H O   1 
ATOM   21522 C  CB  . LEU H  3 159 ? 17.026  -57.966 27.824   1.00 198.25 ? 157  LEU H CB  1 
ATOM   21523 C  CG  . LEU H  3 159 ? 15.517  -58.048 28.091   1.00 221.85 ? 157  LEU H CG  1 
ATOM   21524 C  CD1 . LEU H  3 159 ? 15.030  -59.494 28.052   1.00 222.71 ? 157  LEU H CD1 1 
ATOM   21525 C  CD2 . LEU H  3 159 ? 15.157  -57.390 29.423   1.00 223.28 ? 157  LEU H CD2 1 
ATOM   21526 N  N   . LEU H  3 160 ? 16.049  -57.325 24.855   1.00 204.27 ? 158  LEU H N   1 
ATOM   21527 C  CA  . LEU H  3 160 ? 15.666  -56.456 23.749   1.00 198.50 ? 158  LEU H CA  1 
ATOM   21528 C  C   . LEU H  3 160 ? 14.599  -55.454 24.174   1.00 201.66 ? 158  LEU H C   1 
ATOM   21529 O  O   . LEU H  3 160 ? 13.699  -55.779 24.956   1.00 213.24 ? 158  LEU H O   1 
ATOM   21530 C  CB  . LEU H  3 160 ? 15.158  -57.278 22.562   1.00 194.20 ? 158  LEU H CB  1 
ATOM   21531 C  CG  . LEU H  3 160 ? 16.223  -57.895 21.648   1.00 183.34 ? 158  LEU H CG  1 
ATOM   21532 C  CD1 . LEU H  3 160 ? 17.026  -58.977 22.352   1.00 179.70 ? 158  LEU H CD1 1 
ATOM   21533 C  CD2 . LEU H  3 160 ? 15.590  -58.445 20.382   1.00 189.46 ? 158  LEU H CD2 1 
ATOM   21534 N  N   . ALA H  3 161 ? 14.691  -54.236 23.620   1.00 192.04 ? 159  ALA H N   1 
ATOM   21535 C  CA  . ALA H  3 161 ? 13.831  -53.102 23.908   1.00 192.35 ? 159  ALA H CA  1 
ATOM   21536 C  C   . ALA H  3 161 ? 12.907  -52.801 22.729   1.00 208.32 ? 159  ALA H C   1 
ATOM   21537 O  O   . ALA H  3 161 ? 13.285  -53.001 21.569   1.00 218.10 ? 159  ALA H O   1 
ATOM   21538 C  CB  . ALA H  3 161 ? 14.671  -51.858 24.222   1.00 187.28 ? 159  ALA H CB  1 
ATOM   21539 N  N   . PRO H  3 162 ? 11.686  -52.302 22.991   1.00 223.85 ? 160  PRO H N   1 
ATOM   21540 C  CA  . PRO H  3 162 ? 10.733  -52.057 21.897   1.00 227.87 ? 160  PRO H CA  1 
ATOM   21541 C  C   . PRO H  3 162 ? 11.138  -50.912 20.985   1.00 227.85 ? 160  PRO H C   1 
ATOM   21542 O  O   . PRO H  3 162 ? 10.611  -49.800 21.105   1.00 237.40 ? 160  PRO H O   1 
ATOM   21543 C  CB  . PRO H  3 162 ? 9.426   -51.734 22.635   1.00 228.92 ? 160  PRO H CB  1 
ATOM   21544 C  CG  . PRO H  3 162 ? 9.863   -51.225 23.963   1.00 225.88 ? 160  PRO H CG  1 
ATOM   21545 C  CD  . PRO H  3 162 ? 11.096  -52.011 24.309   1.00 231.38 ? 160  PRO H CD  1 
ATOM   21546 N  N   . SER H  3 163 ? 12.060  -51.168 20.064   1.00 208.32 ? 161  SER H N   1 
ATOM   21547 C  CA  . SER H  3 163 ? 12.445  -50.174 19.073   1.00 203.91 ? 161  SER H CA  1 
ATOM   21548 C  C   . SER H  3 163 ? 11.490  -50.264 17.890   1.00 206.90 ? 161  SER H C   1 
ATOM   21549 O  O   . SER H  3 163 ? 11.369  -51.322 17.262   1.00 216.84 ? 161  SER H O   1 
ATOM   21550 C  CB  . SER H  3 163 ? 13.889  -50.384 18.623   1.00 199.68 ? 161  SER H CB  1 
ATOM   21551 O  OG  . SER H  3 163 ? 14.212  -49.522 17.547   1.00 207.44 ? 161  SER H OG  1 
ATOM   21552 N  N   . ASP H  3 164 ? 10.814  -49.156 17.590   1.00 200.61 ? 162  ASP H N   1 
ATOM   21553 C  CA  . ASP H  3 164 ? 9.928   -49.095 16.438   1.00 201.93 ? 162  ASP H CA  1 
ATOM   21554 C  C   . ASP H  3 164 ? 10.691  -48.936 15.133   1.00 210.29 ? 162  ASP H C   1 
ATOM   21555 O  O   . ASP H  3 164 ? 10.105  -49.119 14.061   1.00 228.33 ? 162  ASP H O   1 
ATOM   21556 C  CB  . ASP H  3 164 ? 8.924   -47.951 16.604   1.00 204.45 ? 162  ASP H CB  1 
ATOM   21557 C  CG  . ASP H  3 164 ? 8.118   -48.064 17.883   1.00 209.10 ? 162  ASP H CG  1 
ATOM   21558 O  OD1 . ASP H  3 164 ? 7.242   -48.953 17.965   1.00 211.79 ? 162  ASP H OD1 1 
ATOM   21559 O  OD2 . ASP H  3 164 ? 8.369   -47.269 18.813   1.00 207.34 ? 162  ASP H OD2 1 
ATOM   21560 N  N   . SER H  3 165 ? 11.970  -48.605 15.201   1.00 205.56 ? 163  SER H N   1 
ATOM   21561 C  CA  . SER H  3 165 ? 12.822  -48.349 14.058   1.00 209.10 ? 163  SER H CA  1 
ATOM   21562 C  C   . SER H  3 165 ? 13.913  -49.411 13.953   1.00 200.38 ? 163  SER H C   1 
ATOM   21563 O  O   . SER H  3 165 ? 14.204  -50.115 14.925   1.00 191.57 ? 163  SER H O   1 
ATOM   21564 C  CB  . SER H  3 165 ? 13.456  -46.956 14.181   1.00 220.29 ? 163  SER H CB  1 
ATOM   21565 O  OG  . SER H  3 165 ? 14.264  -46.874 15.341   1.00 230.34 ? 163  SER H OG  1 
ATOM   21566 N  N   . PRO H  3 166 ? 14.512  -49.581 12.775   1.00 197.15 ? 164  PRO H N   1 
ATOM   21567 C  CA  . PRO H  3 166 ? 15.622  -50.537 12.647   1.00 198.49 ? 164  PRO H CA  1 
ATOM   21568 C  C   . PRO H  3 166 ? 16.793  -50.149 13.540   1.00 192.30 ? 164  PRO H C   1 
ATOM   21569 O  O   . PRO H  3 166 ? 17.212  -48.991 13.577   1.00 179.04 ? 164  PRO H O   1 
ATOM   21570 C  CB  . PRO H  3 166 ? 15.989  -50.461 11.159   1.00 195.60 ? 164  PRO H CB  1 
ATOM   21571 C  CG  . PRO H  3 166 ? 15.406  -49.172 10.672   1.00 198.81 ? 164  PRO H CG  1 
ATOM   21572 C  CD  . PRO H  3 166 ? 14.160  -48.975 11.479   1.00 198.51 ? 164  PRO H CD  1 
ATOM   21573 N  N   . GLU H  3 167 ? 17.300  -51.127 14.288   1.00 211.76 ? 165  GLU H N   1 
ATOM   21574 C  CA  . GLU H  3 167 ? 18.369  -50.911 15.252   1.00 202.40 ? 165  GLU H CA  1 
ATOM   21575 C  C   . GLU H  3 167 ? 19.615  -51.706 14.861   1.00 208.00 ? 165  GLU H C   1 
ATOM   21576 O  O   . GLU H  3 167 ? 19.528  -52.766 14.236   1.00 212.74 ? 165  GLU H O   1 
ATOM   21577 C  CB  . GLU H  3 167 ? 17.909  -51.295 16.662   1.00 193.08 ? 165  GLU H CB  1 
ATOM   21578 C  CG  . GLU H  3 167 ? 18.717  -50.667 17.778   1.00 191.76 ? 165  GLU H CG  1 
ATOM   21579 C  CD  . GLU H  3 167 ? 18.152  -50.996 19.145   1.00 200.53 ? 165  GLU H CD  1 
ATOM   21580 O  OE1 . GLU H  3 167 ? 17.080  -51.639 19.209   1.00 191.37 ? 165  GLU H OE1 1 
ATOM   21581 O  OE2 . GLU H  3 167 ? 18.791  -50.630 20.154   1.00 202.81 ? 165  GLU H OE2 1 
ATOM   21582 N  N   . TRP H  3 168 ? 20.780  -51.184 15.242   1.00 188.48 ? 166  TRP H N   1 
ATOM   21583 C  CA  . TRP H  3 168 ? 22.079  -51.771 14.919   1.00 157.85 ? 166  TRP H CA  1 
ATOM   21584 C  C   . TRP H  3 168 ? 22.765  -52.213 16.204   1.00 147.90 ? 166  TRP H C   1 
ATOM   21585 O  O   . TRP H  3 168 ? 22.969  -51.397 17.109   1.00 178.83 ? 166  TRP H O   1 
ATOM   21586 C  CB  . TRP H  3 168 ? 22.945  -50.760 14.168   1.00 163.71 ? 166  TRP H CB  1 
ATOM   21587 C  CG  . TRP H  3 168 ? 24.046  -51.353 13.364   1.00 164.50 ? 166  TRP H CG  1 
ATOM   21588 C  CD1 . TRP H  3 168 ? 25.245  -51.803 13.827   1.00 187.62 ? 166  TRP H CD1 1 
ATOM   21589 C  CD2 . TRP H  3 168 ? 24.058  -51.559 11.949   1.00 161.99 ? 166  TRP H CD2 1 
ATOM   21590 N  NE1 . TRP H  3 168 ? 26.006  -52.276 12.786   1.00 194.35 ? 166  TRP H NE1 1 
ATOM   21591 C  CE2 . TRP H  3 168 ? 25.297  -52.139 11.622   1.00 179.85 ? 166  TRP H CE2 1 
ATOM   21592 C  CE3 . TRP H  3 168 ? 23.140  -51.309 10.927   1.00 169.81 ? 166  TRP H CE3 1 
ATOM   21593 C  CZ2 . TRP H  3 168 ? 25.642  -52.477 10.315   1.00 180.99 ? 166  TRP H CZ2 1 
ATOM   21594 C  CZ3 . TRP H  3 168 ? 23.484  -51.645 9.630    1.00 185.26 ? 166  TRP H CZ3 1 
ATOM   21595 C  CH2 . TRP H  3 168 ? 24.724  -52.223 9.336    1.00 181.58 ? 166  TRP H CH2 1 
ATOM   21596 N  N   . LEU H  3 169 ? 23.106  -53.498 16.296   1.00 145.50 ? 167  LEU H N   1 
ATOM   21597 C  CA  . LEU H  3 169 ? 23.715  -54.047 17.502   1.00 144.62 ? 167  LEU H CA  1 
ATOM   21598 C  C   . LEU H  3 169 ? 25.187  -54.387 17.275   1.00 154.32 ? 167  LEU H C   1 
ATOM   21599 O  O   . LEU H  3 169 ? 25.735  -54.198 16.188   1.00 181.57 ? 167  LEU H O   1 
ATOM   21600 C  CB  . LEU H  3 169 ? 22.935  -55.264 17.998   1.00 142.26 ? 167  LEU H CB  1 
ATOM   21601 C  CG  . LEU H  3 169 ? 21.957  -54.893 19.117   1.00 187.37 ? 167  LEU H CG  1 
ATOM   21602 C  CD1 . LEU H  3 169 ? 22.719  -54.487 20.375   1.00 181.01 ? 167  LEU H CD1 1 
ATOM   21603 C  CD2 . LEU H  3 169 ? 21.025  -53.766 18.691   1.00 216.95 ? 167  LEU H CD2 1 
ATOM   21604 N  N   . SER H  3 170 ? 25.835  -54.872 18.336   1.00 140.85 ? 168  SER H N   1 
ATOM   21605 C  CA  . SER H  3 170 ? 27.246  -55.235 18.286   1.00 137.01 ? 168  SER H CA  1 
ATOM   21606 C  C   . SER H  3 170 ? 27.570  -56.139 19.467   1.00 136.36 ? 168  SER H C   1 
ATOM   21607 O  O   . SER H  3 170 ? 27.129  -55.880 20.590   1.00 170.92 ? 168  SER H O   1 
ATOM   21608 C  CB  . SER H  3 170 ? 28.153  -53.996 18.305   1.00 136.35 ? 168  SER H CB  1 
ATOM   21609 O  OG  . SER H  3 170 ? 28.040  -53.287 19.522   1.00 152.70 ? 168  SER H OG  1 
ATOM   21610 N  N   . PHE H  3 171 ? 28.347  -57.192 19.208   1.00 129.59 ? 169  PHE H N   1 
ATOM   21611 C  CA  . PHE H  3 171 ? 28.746  -58.153 20.233   1.00 131.06 ? 169  PHE H CA  1 
ATOM   21612 C  C   . PHE H  3 171 ? 30.257  -58.321 20.254   1.00 143.54 ? 169  PHE H C   1 
ATOM   21613 O  O   . PHE H  3 171 ? 30.852  -58.734 19.254   1.00 156.93 ? 169  PHE H O   1 
ATOM   21614 C  CB  . PHE H  3 171 ? 28.067  -59.504 20.009   1.00 148.00 ? 169  PHE H CB  1 
ATOM   21615 C  CG  . PHE H  3 171 ? 26.654  -59.549 20.495   1.00 165.20 ? 169  PHE H CG  1 
ATOM   21616 C  CD1 . PHE H  3 171 ? 26.376  -59.902 21.809   1.00 155.33 ? 169  PHE H CD1 1 
ATOM   21617 C  CD2 . PHE H  3 171 ? 25.605  -59.218 19.654   1.00 167.69 ? 169  PHE H CD2 1 
ATOM   21618 C  CE1 . PHE H  3 171 ? 25.076  -59.940 22.274   1.00 140.65 ? 169  PHE H CE1 1 
ATOM   21619 C  CE2 . PHE H  3 171 ? 24.301  -59.252 20.112   1.00 181.41 ? 169  PHE H CE2 1 
ATOM   21620 C  CZ  . PHE H  3 171 ? 24.037  -59.614 21.426   1.00 160.51 ? 169  PHE H CZ  1 
ATOM   21621 N  N   . ASP H  3 172 ? 30.869  -58.031 21.401   1.00 152.30 ? 170  ASP H N   1 
ATOM   21622 C  CA  . ASP H  3 172 ? 32.316  -58.165 21.572   1.00 147.32 ? 170  ASP H CA  1 
ATOM   21623 C  C   . ASP H  3 172 ? 32.710  -59.637 21.580   1.00 137.74 ? 170  ASP H C   1 
ATOM   21624 O  O   . ASP H  3 172 ? 32.639  -60.314 22.608   1.00 137.92 ? 170  ASP H O   1 
ATOM   21625 C  CB  . ASP H  3 172 ? 32.777  -57.488 22.854   1.00 143.63 ? 170  ASP H CB  1 
ATOM   21626 C  CG  . ASP H  3 172 ? 34.273  -57.288 22.883   1.00 133.95 ? 170  ASP H CG  1 
ATOM   21627 O  OD1 . ASP H  3 172 ? 34.997  -58.245 23.234   1.00 136.13 ? 170  ASP H OD1 1 
ATOM   21628 O  OD2 . ASP H  3 172 ? 34.725  -56.178 22.539   1.00 132.85 ? 170  ASP H OD2 1 
ATOM   21629 N  N   . VAL H  3 173 ? 33.160  -60.129 20.431   1.00 155.95 ? 171  VAL H N   1 
ATOM   21630 C  CA  . VAL H  3 173 ? 33.612  -61.508 20.297   1.00 179.39 ? 171  VAL H CA  1 
ATOM   21631 C  C   . VAL H  3 173 ? 35.120  -61.525 20.056   1.00 182.13 ? 171  VAL H C   1 
ATOM   21632 O  O   . VAL H  3 173 ? 35.631  -62.337 19.274   1.00 178.99 ? 171  VAL H O   1 
ATOM   21633 C  CB  . VAL H  3 173 ? 32.846  -62.224 19.169   1.00 172.14 ? 171  VAL H CB  1 
ATOM   21634 C  CG1 . VAL H  3 173 ? 31.405  -62.472 19.593   1.00 154.78 ? 171  VAL H CG1 1 
ATOM   21635 C  CG2 . VAL H  3 173 ? 32.889  -61.400 17.889   1.00 159.38 ? 171  VAL H CG2 1 
ATOM   21636 N  N   . THR H  3 174 ? 35.838  -60.619 20.727   1.00 172.51 ? 172  THR H N   1 
ATOM   21637 C  CA  . THR H  3 174 ? 37.282  -60.508 20.537   1.00 142.38 ? 172  THR H CA  1 
ATOM   21638 C  C   . THR H  3 174 ? 37.994  -61.811 20.884   1.00 139.32 ? 172  THR H C   1 
ATOM   21639 O  O   . THR H  3 174 ? 38.830  -62.297 20.113   1.00 139.48 ? 172  THR H O   1 
ATOM   21640 C  CB  . THR H  3 174 ? 37.828  -59.357 21.382   1.00 159.21 ? 172  THR H CB  1 
ATOM   21641 O  OG1 . THR H  3 174 ? 37.242  -58.123 20.949   1.00 163.75 ? 172  THR H OG1 1 
ATOM   21642 C  CG2 . THR H  3 174 ? 39.341  -59.272 21.254   1.00 168.03 ? 172  THR H CG2 1 
ATOM   21643 N  N   . GLY H  3 175 ? 37.659  -62.403 22.037   1.00 156.49 ? 173  GLY H N   1 
ATOM   21644 C  CA  . GLY H  3 175 ? 38.295  -63.650 22.434   1.00 166.52 ? 173  GLY H CA  1 
ATOM   21645 C  C   . GLY H  3 175 ? 38.058  -64.777 21.450   1.00 159.98 ? 173  GLY H C   1 
ATOM   21646 O  O   . GLY H  3 175 ? 38.866  -65.705 21.355   1.00 152.79 ? 173  GLY H O   1 
ATOM   21647 N  N   . VAL H  3 176 ? 36.960  -64.707 20.700   1.00 162.77 ? 174  VAL H N   1 
ATOM   21648 C  CA  . VAL H  3 176 ? 36.652  -65.727 19.704   1.00 153.10 ? 174  VAL H CA  1 
ATOM   21649 C  C   . VAL H  3 176 ? 37.490  -65.523 18.453   1.00 145.88 ? 174  VAL H C   1 
ATOM   21650 O  O   . VAL H  3 176 ? 38.082  -66.469 17.923   1.00 147.20 ? 174  VAL H O   1 
ATOM   21651 C  CB  . VAL H  3 176 ? 35.150  -65.705 19.375   1.00 154.40 ? 174  VAL H CB  1 
ATOM   21652 C  CG1 . VAL H  3 176 ? 34.851  -66.645 18.224   1.00 150.31 ? 174  VAL H CG1 1 
ATOM   21653 C  CG2 . VAL H  3 176 ? 34.331  -66.069 20.601   1.00 176.05 ? 174  VAL H CG2 1 
ATOM   21654 N  N   . VAL H  3 177 ? 37.538  -64.284 17.959   1.00 140.87 ? 175  VAL H N   1 
ATOM   21655 C  CA  . VAL H  3 177 ? 38.248  -63.991 16.717   1.00 139.40 ? 175  VAL H CA  1 
ATOM   21656 C  C   . VAL H  3 177 ? 39.741  -64.232 16.881   1.00 141.20 ? 175  VAL H C   1 
ATOM   21657 O  O   . VAL H  3 177 ? 40.414  -64.699 15.955   1.00 142.16 ? 175  VAL H O   1 
ATOM   21658 C  CB  . VAL H  3 177 ? 37.954  -62.547 16.274   1.00 149.10 ? 175  VAL H CB  1 
ATOM   21659 C  CG1 . VAL H  3 177 ? 38.650  -62.245 14.961   1.00 138.50 ? 175  VAL H CG1 1 
ATOM   21660 C  CG2 . VAL H  3 177 ? 36.459  -62.327 16.164   1.00 163.36 ? 175  VAL H CG2 1 
ATOM   21661 N  N   . ARG H  3 178 ? 40.289  -63.900 18.051   1.00 153.71 ? 176  ARG H N   1 
ATOM   21662 C  CA  . ARG H  3 178 ? 41.707  -64.143 18.292   1.00 159.17 ? 176  ARG H CA  1 
ATOM   21663 C  C   . ARG H  3 178 ? 42.030  -65.627 18.182   1.00 165.69 ? 176  ARG H C   1 
ATOM   21664 O  O   . ARG H  3 178 ? 43.058  -66.007 17.606   1.00 153.05 ? 176  ARG H O   1 
ATOM   21665 C  CB  . ARG H  3 178 ? 42.105  -63.605 19.665   1.00 160.64 ? 176  ARG H CB  1 
ATOM   21666 C  CG  . ARG H  3 178 ? 43.519  -63.958 20.090   1.00 156.16 ? 176  ARG H CG  1 
ATOM   21667 C  CD  . ARG H  3 178 ? 43.903  -63.236 21.367   1.00 158.17 ? 176  ARG H CD  1 
ATOM   21668 N  NE  . ARG H  3 178 ? 44.080  -61.803 21.149   1.00 172.36 ? 176  ARG H NE  1 
ATOM   21669 C  CZ  . ARG H  3 178 ? 43.176  -60.875 21.453   1.00 179.36 ? 176  ARG H CZ  1 
ATOM   21670 N  NH1 . ARG H  3 178 ? 42.016  -61.219 22.001   1.00 189.33 ? 176  ARG H NH1 1 
ATOM   21671 N  NH2 . ARG H  3 178 ? 43.436  -59.597 21.214   1.00 166.24 ? 176  ARG H NH2 1 
ATOM   21672 N  N   . GLN H  3 179 ? 41.154  -66.484 18.720   1.00 183.00 ? 177  GLN H N   1 
ATOM   21673 C  CA  . GLN H  3 179 ? 41.365  -67.924 18.618   1.00 188.19 ? 177  GLN H CA  1 
ATOM   21674 C  C   . GLN H  3 179 ? 41.191  -68.396 17.187   1.00 167.78 ? 177  GLN H C   1 
ATOM   21675 O  O   . GLN H  3 179 ? 41.816  -69.381 16.774   1.00 179.30 ? 177  GLN H O   1 
ATOM   21676 C  CB  . GLN H  3 179 ? 40.391  -68.672 19.532   1.00 199.82 ? 177  GLN H CB  1 
ATOM   21677 C  CG  . GLN H  3 179 ? 40.544  -68.377 21.013   1.00 206.70 ? 177  GLN H CG  1 
ATOM   21678 C  CD  . GLN H  3 179 ? 39.504  -69.090 21.853   1.00 193.48 ? 177  GLN H CD  1 
ATOM   21679 O  OE1 . GLN H  3 179 ? 38.713  -69.883 21.341   1.00 182.53 ? 177  GLN H OE1 1 
ATOM   21680 N  NE2 . GLN H  3 179 ? 39.493  -68.803 23.150   1.00 192.50 ? 177  GLN H NE2 1 
ATOM   21681 N  N   . TRP H  3 180 ? 40.353  -67.705 16.421   1.00 157.85 ? 178  TRP H N   1 
ATOM   21682 C  CA  . TRP H  3 180 ? 40.150  -68.055 15.027   1.00 157.58 ? 178  TRP H CA  1 
ATOM   21683 C  C   . TRP H  3 180 ? 41.320  -67.628 14.163   1.00 157.78 ? 178  TRP H C   1 
ATOM   21684 O  O   . TRP H  3 180 ? 41.556  -68.240 13.116   1.00 180.31 ? 178  TRP H O   1 
ATOM   21685 C  CB  . TRP H  3 180 ? 38.861  -67.415 14.512   1.00 169.42 ? 178  TRP H CB  1 
ATOM   21686 C  CG  . TRP H  3 180 ? 37.621  -68.100 14.980   1.00 181.86 ? 178  TRP H CG  1 
ATOM   21687 C  CD1 . TRP H  3 180 ? 37.543  -69.194 15.794   1.00 200.35 ? 178  TRP H CD1 1 
ATOM   21688 C  CD2 . TRP H  3 180 ? 36.274  -67.731 14.672   1.00 171.05 ? 178  TRP H CD2 1 
ATOM   21689 N  NE1 . TRP H  3 180 ? 36.227  -69.533 16.003   1.00 203.30 ? 178  TRP H NE1 1 
ATOM   21690 C  CE2 . TRP H  3 180 ? 35.429  -68.649 15.326   1.00 188.57 ? 178  TRP H CE2 1 
ATOM   21691 C  CE3 . TRP H  3 180 ? 35.701  -66.714 13.903   1.00 155.28 ? 178  TRP H CE3 1 
ATOM   21692 C  CZ2 . TRP H  3 180 ? 34.043  -68.580 15.233   1.00 193.94 ? 178  TRP H CZ2 1 
ATOM   21693 C  CZ3 . TRP H  3 180 ? 34.327  -66.646 13.813   1.00 159.93 ? 178  TRP H CZ3 1 
ATOM   21694 C  CH2 . TRP H  3 180 ? 33.512  -67.573 14.473   1.00 186.48 ? 178  TRP H CH2 1 
ATOM   21695 N  N   . LEU H  3 181 ? 42.069  -66.614 14.591   1.00 151.73 ? 179  LEU H N   1 
ATOM   21696 C  CA  . LEU H  3 181 ? 43.232  -66.171 13.839   1.00 166.82 ? 179  LEU H CA  1 
ATOM   21697 C  C   . LEU H  3 181 ? 44.449  -67.037 14.123   1.00 199.26 ? 179  LEU H C   1 
ATOM   21698 O  O   . LEU H  3 181 ? 45.382  -67.064 13.310   1.00 212.88 ? 179  LEU H O   1 
ATOM   21699 C  CB  . LEU H  3 181 ? 43.532  -64.700 14.161   1.00 161.98 ? 179  LEU H CB  1 
ATOM   21700 C  CG  . LEU H  3 181 ? 42.950  -63.615 13.246   1.00 160.47 ? 179  LEU H CG  1 
ATOM   21701 C  CD1 . LEU H  3 181 ? 41.448  -63.751 13.104   1.00 149.09 ? 179  LEU H CD1 1 
ATOM   21702 C  CD2 . LEU H  3 181 ? 43.297  -62.231 13.774   1.00 172.58 ? 179  LEU H CD2 1 
ATOM   21703 N  N   . SER H  3 182 ? 44.440  -67.769 15.242   1.00 210.99 ? 180  SER H N   1 
ATOM   21704 C  CA  . SER H  3 182 ? 45.547  -68.647 15.599   1.00 215.97 ? 180  SER H CA  1 
ATOM   21705 C  C   . SER H  3 182 ? 45.474  -69.983 14.876   1.00 196.74 ? 180  SER H C   1 
ATOM   21706 O  O   . SER H  3 182 ? 46.518  -70.555 14.539   1.00 206.81 ? 180  SER H O   1 
ATOM   21707 C  CB  . SER H  3 182 ? 45.564  -68.878 17.114   1.00 223.77 ? 180  SER H CB  1 
ATOM   21708 O  OG  . SER H  3 182 ? 44.406  -69.586 17.535   1.00 231.88 ? 180  SER H OG  1 
ATOM   21709 N  N   . ARG H  3 183 ? 44.271  -70.484 14.621   1.00 182.38 ? 181  ARG H N   1 
ATOM   21710 C  CA  . ARG H  3 183 ? 44.096  -71.706 13.860   1.00 190.00 ? 181  ARG H CA  1 
ATOM   21711 C  C   . ARG H  3 183 ? 43.973  -71.374 12.382   1.00 216.91 ? 181  ARG H C   1 
ATOM   21712 O  O   . ARG H  3 183 ? 43.465  -70.314 11.998   1.00 200.18 ? 181  ARG H O   1 
ATOM   21713 C  CB  . ARG H  3 183 ? 42.853  -72.468 14.321   1.00 180.17 ? 181  ARG H CB  1 
ATOM   21714 C  CG  . ARG H  3 183 ? 42.840  -72.798 15.794   1.00 182.68 ? 181  ARG H CG  1 
ATOM   21715 C  CD  . ARG H  3 183 ? 41.603  -73.596 16.174   1.00 207.02 ? 181  ARG H CD  1 
ATOM   21716 N  NE  . ARG H  3 183 ? 41.457  -73.689 17.622   1.00 218.36 ? 181  ARG H NE  1 
ATOM   21717 C  CZ  . ARG H  3 183 ? 40.690  -72.881 18.343   1.00 221.52 ? 181  ARG H CZ  1 
ATOM   21718 N  NH1 . ARG H  3 183 ? 39.997  -71.926 17.742   1.00 222.62 ? 181  ARG H NH1 1 
ATOM   21719 N  NH2 . ARG H  3 183 ? 40.614  -73.031 19.660   1.00 211.34 ? 181  ARG H NH2 1 
ATOM   21720 N  N   . GLY H  3 184 ? 44.431  -72.300 11.552   1.00 260.15 ? 182  GLY H N   1 
ATOM   21721 C  CA  . GLY H  3 184 ? 44.274  -72.128 10.128   1.00 262.35 ? 182  GLY H CA  1 
ATOM   21722 C  C   . GLY H  3 184 ? 42.930  -72.640 9.653    1.00 259.49 ? 182  GLY H C   1 
ATOM   21723 O  O   . GLY H  3 184 ? 42.812  -73.091 8.511    1.00 246.57 ? 182  GLY H O   1 
ATOM   21724 N  N   . GLY H  3 185 ? 41.923  -72.619 10.530   1.00 259.52 ? 183  GLY H N   1 
ATOM   21725 C  CA  . GLY H  3 185 ? 40.579  -73.016 10.156   1.00 248.45 ? 183  GLY H CA  1 
ATOM   21726 C  C   . GLY H  3 185 ? 39.979  -72.127 9.086    1.00 229.50 ? 183  GLY H C   1 
ATOM   21727 O  O   . GLY H  3 185 ? 39.624  -70.980 9.370    1.00 188.06 ? 183  GLY H O   1 
ATOM   21728 N  N   . GLU H  3 186 ? 39.827  -72.660 7.866    1.00 244.41 ? 184  GLU H N   1 
ATOM   21729 C  CA  . GLU H  3 186 ? 39.438  -71.899 6.680    1.00 222.23 ? 184  GLU H CA  1 
ATOM   21730 C  C   . GLU H  3 186 ? 37.958  -71.511 6.671    1.00 203.69 ? 184  GLU H C   1 
ATOM   21731 O  O   . GLU H  3 186 ? 37.530  -70.731 5.807    1.00 183.45 ? 184  GLU H O   1 
ATOM   21732 C  CB  . GLU H  3 186 ? 39.816  -72.716 5.432    1.00 221.29 ? 184  GLU H CB  1 
ATOM   21733 C  CG  . GLU H  3 186 ? 39.583  -72.085 4.047    1.00 239.39 ? 184  GLU H CG  1 
ATOM   21734 C  CD  . GLU H  3 186 ? 38.229  -72.428 3.444    1.00 245.13 ? 184  GLU H CD  1 
ATOM   21735 O  OE1 . GLU H  3 186 ? 37.641  -73.462 3.835    1.00 236.67 ? 184  GLU H OE1 1 
ATOM   21736 O  OE2 . GLU H  3 186 ? 37.771  -71.676 2.555    1.00 253.69 ? 184  GLU H OE2 1 
ATOM   21737 N  N   . ILE H  3 187 ? 37.183  -71.969 7.647    1.00 198.20 ? 185  ILE H N   1 
ATOM   21738 C  CA  . ILE H  3 187 ? 35.756  -71.676 7.702    1.00 177.05 ? 185  ILE H CA  1 
ATOM   21739 C  C   . ILE H  3 187 ? 35.331  -71.593 9.160    1.00 174.61 ? 185  ILE H C   1 
ATOM   21740 O  O   . ILE H  3 187 ? 35.655  -72.468 9.968    1.00 176.08 ? 185  ILE H O   1 
ATOM   21741 C  CB  . ILE H  3 187 ? 34.926  -72.728 6.943    1.00 182.27 ? 185  ILE H CB  1 
ATOM   21742 C  CG1 . ILE H  3 187 ? 33.430  -72.426 7.082    1.00 173.06 ? 185  ILE H CG1 1 
ATOM   21743 C  CG2 . ILE H  3 187 ? 35.280  -74.143 7.413    1.00 186.62 ? 185  ILE H CG2 1 
ATOM   21744 C  CD1 . ILE H  3 187 ? 33.015  -71.097 6.496    1.00 172.28 ? 185  ILE H CD1 1 
ATOM   21745 N  N   . GLU H  3 188 ? 34.633  -70.512 9.495    1.00 172.92 ? 186  GLU H N   1 
ATOM   21746 C  CA  . GLU H  3 188 ? 34.100  -70.288 10.829   1.00 163.20 ? 186  GLU H CA  1 
ATOM   21747 C  C   . GLU H  3 188 ? 32.675  -69.768 10.692   1.00 168.04 ? 186  GLU H C   1 
ATOM   21748 O  O   . GLU H  3 188 ? 32.136  -69.657 9.586    1.00 186.06 ? 186  GLU H O   1 
ATOM   21749 C  CB  . GLU H  3 188 ? 34.982  -69.314 11.617   1.00 165.82 ? 186  GLU H CB  1 
ATOM   21750 C  CG  . GLU H  3 188 ? 36.399  -69.818 11.863   1.00 189.66 ? 186  GLU H CG  1 
ATOM   21751 C  CD  . GLU H  3 188 ? 36.471  -70.910 12.918   1.00 210.11 ? 186  GLU H CD  1 
ATOM   21752 O  OE1 . GLU H  3 188 ? 35.443  -71.176 13.579   1.00 219.94 ? 186  GLU H OE1 1 
ATOM   21753 O  OE2 . GLU H  3 188 ? 37.557  -71.512 13.078   1.00 211.05 ? 186  GLU H OE2 1 
ATOM   21754 N  N   . GLY H  3 189 ? 32.059  -69.445 11.821   1.00 162.96 ? 187  GLY H N   1 
ATOM   21755 C  CA  . GLY H  3 189 ? 30.713  -68.907 11.797   1.00 163.82 ? 187  GLY H CA  1 
ATOM   21756 C  C   . GLY H  3 189 ? 30.142  -68.820 13.192   1.00 164.07 ? 187  GLY H C   1 
ATOM   21757 O  O   . GLY H  3 189 ? 30.739  -69.280 14.171   1.00 164.22 ? 187  GLY H O   1 
ATOM   21758 N  N   . PHE H  3 190 ? 28.951  -68.226 13.265   1.00 146.90 ? 188  PHE H N   1 
ATOM   21759 C  CA  . PHE H  3 190 ? 28.241  -68.036 14.521   1.00 143.11 ? 188  PHE H CA  1 
ATOM   21760 C  C   . PHE H  3 190 ? 26.842  -68.628 14.424   1.00 167.62 ? 188  PHE H C   1 
ATOM   21761 O  O   . PHE H  3 190 ? 26.396  -69.074 13.364   1.00 199.57 ? 188  PHE H O   1 
ATOM   21762 C  CB  . PHE H  3 190 ? 28.142  -66.552 14.897   1.00 140.05 ? 188  PHE H CB  1 
ATOM   21763 C  CG  . PHE H  3 190 ? 29.465  -65.905 15.204   1.00 136.32 ? 188  PHE H CG  1 
ATOM   21764 C  CD1 . PHE H  3 190 ? 29.976  -65.912 16.492   1.00 136.57 ? 188  PHE H CD1 1 
ATOM   21765 C  CD2 . PHE H  3 190 ? 30.192  -65.276 14.203   1.00 134.32 ? 188  PHE H CD2 1 
ATOM   21766 C  CE1 . PHE H  3 190 ? 31.189  -65.308 16.773   1.00 133.90 ? 188  PHE H CE1 1 
ATOM   21767 C  CE2 . PHE H  3 190 ? 31.404  -64.673 14.481   1.00 131.86 ? 188  PHE H CE2 1 
ATOM   21768 C  CZ  . PHE H  3 190 ? 31.902  -64.689 15.765   1.00 131.28 ? 188  PHE H CZ  1 
ATOM   21769 N  N   . ARG H  3 191 ? 26.142  -68.605 15.554   1.00 164.30 ? 189  ARG H N   1 
ATOM   21770 C  CA  . ARG H  3 191 ? 24.773  -69.086 15.643   1.00 159.91 ? 189  ARG H CA  1 
ATOM   21771 C  C   . ARG H  3 191 ? 23.998  -68.165 16.569   1.00 160.66 ? 189  ARG H C   1 
ATOM   21772 O  O   . ARG H  3 191 ? 24.502  -67.771 17.623   1.00 159.42 ? 189  ARG H O   1 
ATOM   21773 C  CB  . ARG H  3 191 ? 24.713  -70.527 16.166   1.00 166.21 ? 189  ARG H CB  1 
ATOM   21774 C  CG  . ARG H  3 191 ? 23.309  -71.011 16.484   1.00 174.11 ? 189  ARG H CG  1 
ATOM   21775 C  CD  . ARG H  3 191 ? 23.336  -72.187 17.444   1.00 184.13 ? 189  ARG H CD  1 
ATOM   21776 N  NE  . ARG H  3 191 ? 21.999  -72.529 17.921   1.00 196.00 ? 189  ARG H NE  1 
ATOM   21777 C  CZ  . ARG H  3 191 ? 21.746  -73.449 18.847   1.00 207.52 ? 189  ARG H CZ  1 
ATOM   21778 N  NH1 . ARG H  3 191 ? 22.743  -74.121 19.409   1.00 204.69 ? 189  ARG H NH1 1 
ATOM   21779 N  NH2 . ARG H  3 191 ? 20.497  -73.690 19.221   1.00 216.42 ? 189  ARG H NH2 1 
ATOM   21780 N  N   . LEU H  3 192 ? 22.781  -67.816 16.173   1.00 157.85 ? 190  LEU H N   1 
ATOM   21781 C  CA  . LEU H  3 192 ? 21.935  -66.928 16.966   1.00 173.67 ? 190  LEU H CA  1 
ATOM   21782 C  C   . LEU H  3 192 ? 20.596  -67.614 17.238   1.00 203.71 ? 190  LEU H C   1 
ATOM   21783 O  O   . LEU H  3 192 ? 19.722  -67.652 16.366   1.00 217.72 ? 190  LEU H O   1 
ATOM   21784 C  CB  . LEU H  3 192 ? 21.749  -65.588 16.262   1.00 163.34 ? 190  LEU H CB  1 
ATOM   21785 C  CG  . LEU H  3 192 ? 21.169  -64.453 17.109   1.00 157.07 ? 190  LEU H CG  1 
ATOM   21786 C  CD1 . LEU H  3 192 ? 21.806  -63.135 16.725   1.00 149.19 ? 190  LEU H CD1 1 
ATOM   21787 C  CD2 . LEU H  3 192 ? 19.659  -64.375 16.951   1.00 168.51 ? 190  LEU H CD2 1 
ATOM   21788 N  N   . SER H  3 193 ? 20.448  -68.184 18.437   1.00 201.79 ? 191  SER H N   1 
ATOM   21789 C  CA  . SER H  3 193 ? 19.170  -68.681 18.924   1.00 202.67 ? 191  SER H CA  1 
ATOM   21790 C  C   . SER H  3 193 ? 18.627  -67.701 19.961   1.00 201.85 ? 191  SER H C   1 
ATOM   21791 O  O   . SER H  3 193 ? 19.129  -66.583 20.112   1.00 197.40 ? 191  SER H O   1 
ATOM   21792 C  CB  . SER H  3 193 ? 19.313  -70.091 19.499   1.00 208.61 ? 191  SER H CB  1 
ATOM   21793 O  OG  . SER H  3 193 ? 20.212  -70.115 20.594   1.00 218.48 ? 191  SER H OG  1 
ATOM   21794 N  N   . ALA H  3 194 ? 17.615  -68.123 20.708   1.00 205.42 ? 192  ALA H N   1 
ATOM   21795 C  CA  . ALA H  3 194 ? 16.996  -67.257 21.700   1.00 207.85 ? 192  ALA H CA  1 
ATOM   21796 C  C   . ALA H  3 194 ? 17.128  -67.863 23.098   1.00 204.80 ? 192  ALA H C   1 
ATOM   21797 O  O   . ALA H  3 194 ? 17.869  -68.826 23.322   1.00 199.12 ? 192  ALA H O   1 
ATOM   21798 C  CB  . ALA H  3 194 ? 15.534  -66.992 21.336   1.00 213.17 ? 192  ALA H CB  1 
ATOM   21799 N  N   . HIS H  3 195 ? 16.390  -67.279 24.041   1.00 198.28 ? 193  HIS H N   1 
ATOM   21800 C  CA  . HIS H  3 195 ? 16.429  -67.715 25.428   1.00 189.43 ? 193  HIS H CA  1 
ATOM   21801 C  C   . HIS H  3 195 ? 15.755  -69.069 25.612   1.00 199.32 ? 193  HIS H C   1 
ATOM   21802 O  O   . HIS H  3 195 ? 14.803  -69.425 24.911   1.00 205.14 ? 193  HIS H O   1 
ATOM   21803 C  CB  . HIS H  3 195 ? 15.755  -66.687 26.327   1.00 188.47 ? 193  HIS H CB  1 
ATOM   21804 C  CG  . HIS H  3 195 ? 15.809  -67.037 27.781   1.00 209.91 ? 193  HIS H CG  1 
ATOM   21805 N  ND1 . HIS H  3 195 ? 16.991  -67.295 28.441   1.00 208.20 ? 193  HIS H ND1 1 
ATOM   21806 C  CD2 . HIS H  3 195 ? 14.825  -67.186 28.701   1.00 231.15 ? 193  HIS H CD2 1 
ATOM   21807 C  CE1 . HIS H  3 195 ? 16.734  -67.580 29.705   1.00 225.30 ? 193  HIS H CE1 1 
ATOM   21808 N  NE2 . HIS H  3 195 ? 15.427  -67.522 29.889   1.00 231.88 ? 193  HIS H NE2 1 
ATOM   21809 N  N   . CYS H  3 196 ? 16.256  -69.820 26.585   1.00 188.00 ? 194  CYS H N   1 
ATOM   21810 C  CA  . CYS H  3 196 ? 15.735  -71.137 26.922   1.00 196.58 ? 194  CYS H CA  1 
ATOM   21811 C  C   . CYS H  3 196 ? 15.233  -71.097 28.357   1.00 196.79 ? 194  CYS H C   1 
ATOM   21812 O  O   . CYS H  3 196 ? 16.028  -70.982 29.295   1.00 194.47 ? 194  CYS H O   1 
ATOM   21813 C  CB  . CYS H  3 196 ? 16.807  -72.208 26.743   1.00 201.94 ? 194  CYS H CB  1 
ATOM   21814 S  SG  . CYS H  3 196 ? 17.839  -72.014 25.269   1.00 217.06 ? 194  CYS H SG  1 
ATOM   21815 N  N   . SER H  3 197 ? 13.918  -71.194 28.524   1.00 210.59 ? 195  SER H N   1 
ATOM   21816 C  CA  . SER H  3 197 ? 13.301  -71.255 29.844   1.00 224.90 ? 195  SER H CA  1 
ATOM   21817 C  C   . SER H  3 197 ? 13.254  -72.721 30.249   1.00 227.00 ? 195  SER H C   1 
ATOM   21818 O  O   . SER H  3 197 ? 12.514  -73.506 29.650   1.00 220.04 ? 195  SER H O   1 
ATOM   21819 C  CB  . SER H  3 197 ? 11.899  -70.643 29.820   1.00 227.02 ? 195  SER H CB  1 
ATOM   21820 O  OG  . SER H  3 197 ? 11.307  -70.620 31.112   1.00 226.87 ? 195  SER H OG  1 
ATOM   21821 N  N   . CYS H  3 198 ? 14.049  -73.093 31.253   1.00 239.67 ? 196  CYS H N   1 
ATOM   21822 C  CA  . CYS H  3 198 ? 14.233  -74.485 31.645   1.00 240.96 ? 196  CYS H CA  1 
ATOM   21823 C  C   . CYS H  3 198 ? 13.952  -74.626 33.139   1.00 245.00 ? 196  CYS H C   1 
ATOM   21824 O  O   . CYS H  3 198 ? 13.567  -73.663 33.806   1.00 244.93 ? 196  CYS H O   1 
ATOM   21825 C  CB  . CYS H  3 198 ? 15.638  -74.986 31.272   1.00 244.40 ? 196  CYS H CB  1 
ATOM   21826 S  SG  . CYS H  3 198 ? 17.025  -74.432 32.301   1.00 256.55 ? 196  CYS H SG  1 
ATOM   21827 N  N   . ASP H  3 199 ? 14.162  -75.850 33.651   1.00 248.95 ? 197  ASP H N   1 
ATOM   21828 C  CA  . ASP H  3 199 ? 13.597  -76.388 34.896   1.00 257.11 ? 197  ASP H CA  1 
ATOM   21829 C  C   . ASP H  3 199 ? 12.165  -76.833 34.602   1.00 264.72 ? 197  ASP H C   1 
ATOM   21830 O  O   . ASP H  3 199 ? 11.691  -77.837 35.145   1.00 261.35 ? 197  ASP H O   1 
ATOM   21831 C  CB  . ASP H  3 199 ? 13.652  -75.388 36.062   1.00 253.43 ? 197  ASP H CB  1 
ATOM   21832 C  CG  . ASP H  3 199 ? 13.787  -76.072 37.424   1.00 253.36 ? 197  ASP H CG  1 
ATOM   21833 O  OD1 . ASP H  3 199 ? 14.237  -77.235 37.469   1.00 246.08 ? 197  ASP H OD1 1 
ATOM   21834 O  OD2 . ASP H  3 199 ? 13.452  -75.442 38.452   1.00 261.70 ? 197  ASP H OD2 1 
ATOM   21835 N  N   . SER H  3 200 ? 11.469  -76.065 33.761   1.00 265.91 ? 198  SER H N   1 
ATOM   21836 C  CA  . SER H  3 200 ? 10.406  -76.552 32.891   1.00 270.41 ? 198  SER H CA  1 
ATOM   21837 C  C   . SER H  3 200 ? 10.719  -76.037 31.495   1.00 257.53 ? 198  SER H C   1 
ATOM   21838 O  O   . SER H  3 200 ? 11.202  -74.914 31.335   1.00 246.91 ? 198  SER H O   1 
ATOM   21839 C  CB  . SER H  3 200 ? 9.003   -76.086 33.318   1.00 266.69 ? 198  SER H CB  1 
ATOM   21840 O  OG  . SER H  3 200 ? 8.908   -75.887 34.716   1.00 274.77 ? 198  SER H OG  1 
ATOM   21841 N  N   . ARG H  3 201 ? 10.440  -76.856 30.487   1.00 259.18 ? 199  ARG H N   1 
ATOM   21842 C  CA  . ARG H  3 201 ? 11.049  -76.696 29.171   1.00 250.25 ? 199  ARG H CA  1 
ATOM   21843 C  C   . ARG H  3 201 ? 10.212  -75.797 28.267   1.00 244.03 ? 199  ARG H C   1 
ATOM   21844 O  O   . ARG H  3 201 ? 9.029   -76.069 28.031   1.00 254.16 ? 199  ARG H O   1 
ATOM   21845 C  CB  . ARG H  3 201 ? 11.267  -78.059 28.519   1.00 261.30 ? 199  ARG H CB  1 
ATOM   21846 C  CG  . ARG H  3 201 ? 12.321  -78.898 29.225   1.00 263.03 ? 199  ARG H CG  1 
ATOM   21847 C  CD  . ARG H  3 201 ? 13.048  -79.804 28.243   1.00 270.10 ? 199  ARG H CD  1 
ATOM   21848 N  NE  . ARG H  3 201 ? 13.926  -80.756 28.918   1.00 268.81 ? 199  ARG H NE  1 
ATOM   21849 C  CZ  . ARG H  3 201 ? 14.749  -81.593 28.292   1.00 264.13 ? 199  ARG H CZ  1 
ATOM   21850 N  NH1 . ARG H  3 201 ? 14.816  -81.596 26.966   1.00 256.38 ? 199  ARG H NH1 1 
ATOM   21851 N  NH2 . ARG H  3 201 ? 15.507  -82.427 28.992   1.00 263.28 ? 199  ARG H NH2 1 
ATOM   21852 N  N   . ASP H  3 202 ? 10.847  -74.746 27.749   1.00 220.60 ? 200  ASP H N   1 
ATOM   21853 C  CA  . ASP H  3 202 ? 10.267  -73.841 26.767   1.00 218.39 ? 200  ASP H CA  1 
ATOM   21854 C  C   . ASP H  3 202 ? 11.382  -73.360 25.845   1.00 217.36 ? 200  ASP H C   1 
ATOM   21855 O  O   . ASP H  3 202 ? 12.553  -73.326 26.231   1.00 225.00 ? 200  ASP H O   1 
ATOM   21856 C  CB  . ASP H  3 202 ? 9.569   -72.648 27.437   1.00 216.56 ? 200  ASP H CB  1 
ATOM   21857 C  CG  . ASP H  3 202 ? 8.239   -73.019 28.072   1.00 218.04 ? 200  ASP H CG  1 
ATOM   21858 O  OD1 . ASP H  3 202 ? 7.525   -73.881 27.518   1.00 227.86 ? 200  ASP H OD1 1 
ATOM   21859 O  OD2 . ASP H  3 202 ? 7.902   -72.432 29.122   1.00 213.13 ? 200  ASP H OD2 1 
ATOM   21860 N  N   . ASN H  3 203 ? 11.008  -72.972 24.624   1.00 213.83 ? 201  ASN H N   1 
ATOM   21861 C  CA  . ASN H  3 203 ? 11.967  -72.554 23.602   1.00 206.19 ? 201  ASN H CA  1 
ATOM   21862 C  C   . ASN H  3 203 ? 11.215  -71.897 22.450   1.00 205.22 ? 201  ASN H C   1 
ATOM   21863 O  O   . ASN H  3 203 ? 10.014  -72.124 22.282   1.00 214.55 ? 201  ASN H O   1 
ATOM   21864 C  CB  . ASN H  3 203 ? 12.776  -73.745 23.085   1.00 209.15 ? 201  ASN H CB  1 
ATOM   21865 C  CG  . ASN H  3 203 ? 11.893  -74.812 22.467   1.00 215.14 ? 201  ASN H CG  1 
ATOM   21866 O  OD1 . ASN H  3 203 ? 10.721  -74.941 22.823   1.00 221.24 ? 201  ASN H OD1 1 
ATOM   21867 N  ND2 . ASN H  3 203 ? 12.445  -75.575 21.531   1.00 215.08 ? 201  ASN H ND2 1 
ATOM   21868 N  N   . THR H  3 204 ? 11.942  -71.057 21.682   1.00 212.30 ? 202  THR H N   1 
ATOM   21869 C  CA  . THR H  3 204 ? 11.600  -70.444 20.383   1.00 207.99 ? 202  THR H CA  1 
ATOM   21870 C  C   . THR H  3 204 ? 12.370  -69.144 20.160   1.00 209.52 ? 202  THR H C   1 
ATOM   21871 O  O   . THR H  3 204 ? 12.863  -68.539 21.116   1.00 220.83 ? 202  THR H O   1 
ATOM   21872 C  CB  . THR H  3 204 ? 10.104  -70.137 20.189   1.00 212.28 ? 202  THR H CB  1 
ATOM   21873 O  OG1 . THR H  3 204 ? 9.496   -69.729 21.425   1.00 214.20 ? 202  THR H OG1 1 
ATOM   21874 C  CG2 . THR H  3 204 ? 9.352   -71.312 19.532   1.00 221.21 ? 202  THR H CG2 1 
ATOM   21875 N  N   . LEU H  3 205 ? 12.468  -68.705 18.898   1.00 210.24 ? 203  LEU H N   1 
ATOM   21876 C  CA  . LEU H  3 205 ? 13.122  -67.455 18.517   1.00 202.44 ? 203  LEU H CA  1 
ATOM   21877 C  C   . LEU H  3 205 ? 12.184  -66.615 17.661   1.00 203.47 ? 203  LEU H C   1 
ATOM   21878 O  O   . LEU H  3 205 ? 11.555  -67.135 16.734   1.00 209.22 ? 203  LEU H O   1 
ATOM   21879 C  CB  . LEU H  3 205 ? 14.423  -67.709 17.753   1.00 196.85 ? 203  LEU H CB  1 
ATOM   21880 C  CG  . LEU H  3 205 ? 15.049  -66.481 17.090   1.00 186.13 ? 203  LEU H CG  1 
ATOM   21881 C  CD1 . LEU H  3 205 ? 15.444  -65.439 18.116   1.00 181.08 ? 203  LEU H CD1 1 
ATOM   21882 C  CD2 . LEU H  3 205 ? 16.246  -66.900 16.263   1.00 183.48 ? 203  LEU H CD2 1 
ATOM   21883 N  N   . GLN H  3 206 ? 12.097  -65.314 17.969   1.00 206.21 ? 204  GLN H N   1 
ATOM   21884 C  CA  . GLN H  3 206 ? 11.201  -64.409 17.259   1.00 209.92 ? 204  GLN H CA  1 
ATOM   21885 C  C   . GLN H  3 206 ? 11.888  -63.166 16.698   1.00 214.08 ? 204  GLN H C   1 
ATOM   21886 O  O   . GLN H  3 206 ? 11.192  -62.228 16.292   1.00 212.74 ? 204  GLN H O   1 
ATOM   21887 C  CB  . GLN H  3 206 ? 10.062  -63.972 18.186   1.00 217.63 ? 204  GLN H CB  1 
ATOM   21888 C  CG  . GLN H  3 206 ? 9.405   -65.113 18.943   1.00 235.33 ? 204  GLN H CG  1 
ATOM   21889 C  CD  . GLN H  3 206 ? 8.479   -64.624 20.042   1.00 252.04 ? 204  GLN H CD  1 
ATOM   21890 O  OE1 . GLN H  3 206 ? 8.505   -63.450 20.414   1.00 254.94 ? 204  GLN H OE1 1 
ATOM   21891 N  NE2 . GLN H  3 206 ? 7.661   -65.527 20.574   1.00 251.45 ? 204  GLN H NE2 1 
ATOM   21892 N  N   . VAL H  3 207 ? 13.218  -63.117 16.674   1.00 212.76 ? 205  VAL H N   1 
ATOM   21893 C  CA  . VAL H  3 207 ? 13.931  -61.905 16.268   1.00 202.79 ? 205  VAL H CA  1 
ATOM   21894 C  C   . VAL H  3 207 ? 14.017  -61.815 14.750   1.00 213.41 ? 205  VAL H C   1 
ATOM   21895 O  O   . VAL H  3 207 ? 14.331  -62.799 14.067   1.00 215.28 ? 205  VAL H O   1 
ATOM   21896 C  CB  . VAL H  3 207 ? 15.327  -61.855 16.901   1.00 181.56 ? 205  VAL H CB  1 
ATOM   21897 C  CG1 . VAL H  3 207 ? 16.099  -60.653 16.378   1.00 176.54 ? 205  VAL H CG1 1 
ATOM   21898 C  CG2 . VAL H  3 207 ? 15.211  -61.780 18.398   1.00 181.09 ? 205  VAL H CG2 1 
ATOM   21899 N  N   . ASP H  3 208 ? 13.749  -60.620 14.220   1.00 210.41 ? 206  ASP H N   1 
ATOM   21900 C  CA  . ASP H  3 208 ? 13.900  -60.321 12.799   1.00 205.39 ? 206  ASP H CA  1 
ATOM   21901 C  C   . ASP H  3 208 ? 15.187  -59.528 12.611   1.00 193.00 ? 206  ASP H C   1 
ATOM   21902 O  O   . ASP H  3 208 ? 15.240  -58.327 12.894   1.00 188.33 ? 206  ASP H O   1 
ATOM   21903 C  CB  . ASP H  3 208 ? 12.690  -59.567 12.265   1.00 218.55 ? 206  ASP H CB  1 
ATOM   21904 C  CG  . ASP H  3 208 ? 11.593  -60.500 11.799   1.00 243.01 ? 206  ASP H CG  1 
ATOM   21905 O  OD1 . ASP H  3 208 ? 11.905  -61.657 11.440   1.00 244.17 ? 206  ASP H OD1 1 
ATOM   21906 O  OD2 . ASP H  3 208 ? 10.420  -60.076 11.789   1.00 256.46 ? 206  ASP H OD2 1 
ATOM   21907 N  N   . ILE H  3 209 ? 16.222  -60.213 12.134   1.00 191.43 ? 207  ILE H N   1 
ATOM   21908 C  CA  . ILE H  3 209 ? 17.502  -59.613 11.780   1.00 191.10 ? 207  ILE H CA  1 
ATOM   21909 C  C   . ILE H  3 209 ? 17.550  -59.500 10.271   1.00 196.01 ? 207  ILE H C   1 
ATOM   21910 O  O   . ILE H  3 209 ? 16.957  -60.317 9.556    1.00 204.35 ? 207  ILE H O   1 
ATOM   21911 C  CB  . ILE H  3 209 ? 18.691  -60.456 12.279   1.00 168.38 ? 207  ILE H CB  1 
ATOM   21912 C  CG1 . ILE H  3 209 ? 18.433  -60.951 13.696   1.00 166.71 ? 207  ILE H CG1 1 
ATOM   21913 C  CG2 . ILE H  3 209 ? 19.993  -59.664 12.179   1.00 163.72 ? 207  ILE H CG2 1 
ATOM   21914 C  CD1 . ILE H  3 209 ? 19.248  -62.157 14.062   1.00 164.85 ? 207  ILE H CD1 1 
ATOM   21915 N  N   . ASN H  3 210 ? 18.206  -58.452 9.777    1.00 178.86 ? 208  ASN H N   1 
ATOM   21916 C  CA  . ASN H  3 210 ? 18.398  -58.329 8.343    1.00 169.28 ? 208  ASN H CA  1 
ATOM   21917 C  C   . ASN H  3 210 ? 19.017  -59.607 7.808    1.00 191.93 ? 208  ASN H C   1 
ATOM   21918 O  O   . ASN H  3 210 ? 20.149  -59.958 8.156    1.00 190.37 ? 208  ASN H O   1 
ATOM   21919 C  CB  . ASN H  3 210 ? 19.283  -57.127 8.022    1.00 165.96 ? 208  ASN H CB  1 
ATOM   21920 C  CG  . ASN H  3 210 ? 18.986  -56.546 6.667    1.00 174.01 ? 208  ASN H CG  1 
ATOM   21921 O  OD1 . ASN H  3 210 ? 17.862  -56.642 6.173    1.00 178.79 ? 208  ASN H OD1 1 
ATOM   21922 N  ND2 . ASN H  3 210 ? 19.996  -55.968 6.039    1.00 193.65 ? 208  ASN H ND2 1 
ATOM   21923 N  N   . GLY H  3 211 ? 18.266  -60.308 6.970    1.00 218.24 ? 209  GLY H N   1 
ATOM   21924 C  CA  . GLY H  3 211 ? 18.707  -61.550 6.384    1.00 216.90 ? 209  GLY H CA  1 
ATOM   21925 C  C   . GLY H  3 211 ? 18.546  -61.514 4.879    1.00 217.49 ? 209  GLY H C   1 
ATOM   21926 O  O   . GLY H  3 211 ? 18.529  -60.456 4.250    1.00 221.46 ? 209  GLY H O   1 
ATOM   21927 N  N   . PHE H  3 212 ? 18.420  -62.711 4.308    1.00 232.24 ? 210  PHE H N   1 
ATOM   21928 C  CA  . PHE H  3 212 ? 18.294  -62.863 2.866    1.00 250.34 ? 210  PHE H CA  1 
ATOM   21929 C  C   . PHE H  3 212 ? 16.855  -63.021 2.408    1.00 252.24 ? 210  PHE H C   1 
ATOM   21930 O  O   . PHE H  3 212 ? 16.551  -62.729 1.245    1.00 246.71 ? 210  PHE H O   1 
ATOM   21931 C  CB  . PHE H  3 212 ? 19.109  -64.079 2.404    1.00 252.97 ? 210  PHE H CB  1 
ATOM   21932 C  CG  . PHE H  3 212 ? 20.539  -64.062 2.879    1.00 252.69 ? 210  PHE H CG  1 
ATOM   21933 C  CD1 . PHE H  3 212 ? 20.860  -64.398 4.190    1.00 244.00 ? 210  PHE H CD1 1 
ATOM   21934 C  CD2 . PHE H  3 212 ? 21.562  -63.707 2.017    1.00 238.35 ? 210  PHE H CD2 1 
ATOM   21935 C  CE1 . PHE H  3 212 ? 22.169  -64.375 4.624    1.00 243.97 ? 210  PHE H CE1 1 
ATOM   21936 C  CE2 . PHE H  3 212 ? 22.870  -63.683 2.447    1.00 222.49 ? 210  PHE H CE2 1 
ATOM   21937 C  CZ  . PHE H  3 212 ? 23.175  -64.021 3.750    1.00 234.07 ? 210  PHE H CZ  1 
ATOM   21938 N  N   . THR H  3 213 ? 15.979  -63.497 3.294    1.00 250.20 ? 211  THR H N   1 
ATOM   21939 C  CA  . THR H  3 213 ? 14.580  -63.784 2.994    1.00 249.12 ? 211  THR H CA  1 
ATOM   21940 C  C   . THR H  3 213 ? 14.463  -64.841 1.900    1.00 246.18 ? 211  THR H C   1 
ATOM   21941 O  O   . THR H  3 213 ? 13.352  -65.254 1.554    1.00 249.47 ? 211  THR H O   1 
ATOM   21942 C  CB  . THR H  3 213 ? 13.829  -62.512 2.591    1.00 244.41 ? 211  THR H CB  1 
ATOM   21943 O  OG1 . THR H  3 213 ? 14.355  -62.024 1.352    1.00 255.11 ? 211  THR H OG1 1 
ATOM   21944 C  CG2 . THR H  3 213 ? 13.981  -61.436 3.656    1.00 232.20 ? 211  THR H CG2 1 
ATOM   21945 N  N   . THR H  3 214 ? 15.602  -65.239 1.323    1.00 246.84 ? 212  THR H N   1 
ATOM   21946 C  CA  . THR H  3 214 ? 15.717  -66.317 0.346    1.00 259.69 ? 212  THR H CA  1 
ATOM   21947 C  C   . THR H  3 214 ? 15.080  -65.970 -0.997   1.00 266.74 ? 212  THR H C   1 
ATOM   21948 O  O   . THR H  3 214 ? 15.608  -66.348 -2.048   1.00 277.58 ? 212  THR H O   1 
ATOM   21949 C  CB  . THR H  3 214 ? 15.110  -67.613 0.897    1.00 265.27 ? 212  THR H CB  1 
ATOM   21950 O  OG1 . THR H  3 214 ? 15.511  -67.788 2.263    1.00 268.36 ? 212  THR H OG1 1 
ATOM   21951 C  CG2 . THR H  3 214 ? 15.574  -68.815 0.083    1.00 256.80 ? 212  THR H CG2 1 
ATOM   21952 N  N   . GLY H  3 215 ? 13.954  -65.257 -0.987   1.00 265.30 ? 213  GLY H N   1 
ATOM   21953 C  CA  . GLY H  3 215 ? 13.167  -65.121 -2.200   1.00 267.42 ? 213  GLY H CA  1 
ATOM   21954 C  C   . GLY H  3 215 ? 13.134  -63.794 -2.939   1.00 271.14 ? 213  GLY H C   1 
ATOM   21955 O  O   . GLY H  3 215 ? 12.442  -63.693 -3.957   1.00 276.48 ? 213  GLY H O   1 
ATOM   21956 N  N   . ARG H  3 216 ? 13.863  -62.778 -2.482   1.00 251.45 ? 214  ARG H N   1 
ATOM   21957 C  CA  . ARG H  3 216 ? 13.873  -61.498 -3.186   1.00 235.76 ? 214  ARG H CA  1 
ATOM   21958 C  C   . ARG H  3 216 ? 14.740  -61.611 -4.435   1.00 218.62 ? 214  ARG H C   1 
ATOM   21959 O  O   . ARG H  3 216 ? 15.928  -61.939 -4.347   1.00 214.92 ? 214  ARG H O   1 
ATOM   21960 C  CB  . ARG H  3 216 ? 14.371  -60.378 -2.276   1.00 222.44 ? 214  ARG H CB  1 
ATOM   21961 C  CG  . ARG H  3 216 ? 13.618  -60.266 -0.963   1.00 225.31 ? 214  ARG H CG  1 
ATOM   21962 C  CD  . ARG H  3 216 ? 12.133  -60.034 -1.164   1.00 232.07 ? 214  ARG H CD  1 
ATOM   21963 N  NE  . ARG H  3 216 ? 11.430  -59.929 0.111    1.00 236.01 ? 214  ARG H NE  1 
ATOM   21964 C  CZ  . ARG H  3 216 ? 10.108  -59.865 0.232    1.00 242.97 ? 214  ARG H CZ  1 
ATOM   21965 N  NH1 . ARG H  3 216 ? 9.339   -59.901 -0.848   1.00 241.95 ? 214  ARG H NH1 1 
ATOM   21966 N  NH2 . ARG H  3 216 ? 9.555   -59.768 1.434    1.00 245.49 ? 214  ARG H NH2 1 
ATOM   21967 N  N   . ARG H  3 217 ? 14.147  -61.343 -5.599   1.00 203.85 ? 215  ARG H N   1 
ATOM   21968 C  CA  . ARG H  3 217 ? 14.862  -61.482 -6.861   1.00 201.06 ? 215  ARG H CA  1 
ATOM   21969 C  C   . ARG H  3 217 ? 14.902  -60.170 -7.634   1.00 204.26 ? 215  ARG H C   1 
ATOM   21970 O  O   . ARG H  3 217 ? 14.710  -59.095 -7.056   1.00 203.05 ? 215  ARG H O   1 
ATOM   21971 C  CB  . ARG H  3 217 ? 14.219  -62.570 -7.720   1.00 202.50 ? 215  ARG H CB  1 
ATOM   21972 C  CG  . ARG H  3 217 ? 14.207  -63.937 -7.076   1.00 202.27 ? 215  ARG H CG  1 
ATOM   21973 C  CD  . ARG H  3 217 ? 13.849  -65.000 -8.092   1.00 203.00 ? 215  ARG H CD  1 
ATOM   21974 N  NE  . ARG H  3 217 ? 12.515  -64.788 -8.638   1.00 207.50 ? 215  ARG H NE  1 
ATOM   21975 C  CZ  . ARG H  3 217 ? 11.420  -65.374 -8.168   1.00 211.55 ? 215  ARG H CZ  1 
ATOM   21976 N  NH1 . ARG H  3 217 ? 11.503  -66.211 -7.143   1.00 211.21 ? 215  ARG H NH1 1 
ATOM   21977 N  NH2 . ARG H  3 217 ? 10.244  -65.125 -8.724   1.00 220.01 ? 215  ARG H NH2 1 
ATOM   21978 N  N   . GLY H  3 218 ? 15.175  -60.252 -8.937   1.00 216.97 ? 216  GLY H N   1 
ATOM   21979 C  CA  . GLY H  3 218 ? 15.164  -59.096 -9.816   1.00 212.17 ? 216  GLY H CA  1 
ATOM   21980 C  C   . GLY H  3 218 ? 16.458  -58.313 -9.917   1.00 206.96 ? 216  GLY H C   1 
ATOM   21981 O  O   . GLY H  3 218 ? 17.548  -58.860 -9.726   1.00 203.80 ? 216  GLY H O   1 
ATOM   21982 N  N   . ASP H  3 219 ? 16.345  -57.017 -10.221  1.00 199.05 ? 217  ASP H N   1 
ATOM   21983 C  CA  . ASP H  3 219 ? 17.527  -56.169 -10.315  1.00 196.27 ? 217  ASP H CA  1 
ATOM   21984 C  C   . ASP H  3 219 ? 17.997  -55.712 -8.945   1.00 196.13 ? 217  ASP H C   1 
ATOM   21985 O  O   . ASP H  3 219 ? 19.202  -55.639 -8.688   1.00 193.29 ? 217  ASP H O   1 
ATOM   21986 C  CB  . ASP H  3 219 ? 17.234  -54.945 -11.180  1.00 217.64 ? 217  ASP H CB  1 
ATOM   21987 C  CG  . ASP H  3 219 ? 18.407  -53.979 -11.240  1.00 226.21 ? 217  ASP H CG  1 
ATOM   21988 O  OD1 . ASP H  3 219 ? 19.565  -54.436 -11.351  1.00 234.94 ? 217  ASP H OD1 1 
ATOM   21989 O  OD2 . ASP H  3 219 ? 18.170  -52.757 -11.137  1.00 221.11 ? 217  ASP H OD2 1 
ATOM   21990 N  N   . LEU H  3 220 ? 17.061  -55.408 -8.055   1.00 198.74 ? 218  LEU H N   1 
ATOM   21991 C  CA  . LEU H  3 220 ? 17.406  -54.924 -6.730   1.00 199.27 ? 218  LEU H CA  1 
ATOM   21992 C  C   . LEU H  3 220 ? 17.847  -56.039 -5.792   1.00 209.68 ? 218  LEU H C   1 
ATOM   21993 O  O   . LEU H  3 220 ? 18.303  -55.744 -4.683   1.00 216.75 ? 218  LEU H O   1 
ATOM   21994 C  CB  . LEU H  3 220 ? 16.224  -54.148 -6.149   1.00 206.08 ? 218  LEU H CB  1 
ATOM   21995 C  CG  . LEU H  3 220 ? 16.470  -53.237 -4.946   1.00 211.24 ? 218  LEU H CG  1 
ATOM   21996 C  CD1 . LEU H  3 220 ? 17.667  -52.350 -5.184   1.00 209.15 ? 218  LEU H CD1 1 
ATOM   21997 C  CD2 . LEU H  3 220 ? 15.241  -52.380 -4.693   1.00 218.72 ? 218  LEU H CD2 1 
ATOM   21998 N  N   . ALA H  3 221 ? 17.721  -57.303 -6.206   1.00 216.20 ? 219  ALA H N   1 
ATOM   21999 C  CA  . ALA H  3 221 ? 18.076  -58.416 -5.329   1.00 210.15 ? 219  ALA H CA  1 
ATOM   22000 C  C   . ALA H  3 221 ? 19.536  -58.354 -4.900   1.00 211.54 ? 219  ALA H C   1 
ATOM   22001 O  O   . ALA H  3 221 ? 19.873  -58.739 -3.774   1.00 209.45 ? 219  ALA H O   1 
ATOM   22002 C  CB  . ALA H  3 221 ? 17.798  -59.745 -6.025   1.00 204.15 ? 219  ALA H CB  1 
ATOM   22003 N  N   . THR H  3 222 ? 20.420  -57.891 -5.788   1.00 219.47 ? 220  THR H N   1 
ATOM   22004 C  CA  . THR H  3 222 ? 21.842  -57.842 -5.460   1.00 211.30 ? 220  THR H CA  1 
ATOM   22005 C  C   . THR H  3 222 ? 22.109  -56.932 -4.265   1.00 203.76 ? 220  THR H C   1 
ATOM   22006 O  O   . THR H  3 222 ? 22.936  -57.255 -3.404   1.00 196.22 ? 220  THR H O   1 
ATOM   22007 C  CB  . THR H  3 222 ? 22.644  -57.385 -6.679   1.00 205.89 ? 220  THR H CB  1 
ATOM   22008 O  OG1 . THR H  3 222 ? 22.086  -56.172 -7.200   1.00 206.03 ? 220  THR H OG1 1 
ATOM   22009 C  CG2 . THR H  3 222 ? 22.617  -58.452 -7.764   1.00 206.15 ? 220  THR H CG2 1 
ATOM   22010 N  N   . ILE H  3 223 ? 21.394  -55.805 -4.172   1.00 199.78 ? 221  ILE H N   1 
ATOM   22011 C  CA  . ILE H  3 223 ? 21.612  -54.895 -3.050   1.00 190.40 ? 221  ILE H CA  1 
ATOM   22012 C  C   . ILE H  3 223 ? 20.960  -55.415 -1.781   1.00 185.19 ? 221  ILE H C   1 
ATOM   22013 O  O   . ILE H  3 223 ? 21.276  -54.934 -0.687   1.00 192.78 ? 221  ILE H O   1 
ATOM   22014 C  CB  . ILE H  3 223 ? 21.094  -53.479 -3.371   1.00 197.35 ? 221  ILE H CB  1 
ATOM   22015 C  CG1 . ILE H  3 223 ? 21.469  -53.077 -4.799   1.00 216.94 ? 221  ILE H CG1 1 
ATOM   22016 C  CG2 . ILE H  3 223 ? 21.671  -52.452 -2.400   1.00 198.28 ? 221  ILE H CG2 1 
ATOM   22017 C  CD1 . ILE H  3 223 ? 21.278  -51.600 -5.091   1.00 222.90 ? 221  ILE H CD1 1 
ATOM   22018 N  N   . HIS H  3 224 ? 20.103  -56.429 -1.887   1.00 186.01 ? 222  HIS H N   1 
ATOM   22019 C  CA  . HIS H  3 224 ? 19.487  -57.024 -0.709   1.00 189.40 ? 222  HIS H CA  1 
ATOM   22020 C  C   . HIS H  3 224 ? 20.461  -57.903 0.065    1.00 181.99 ? 222  HIS H C   1 
ATOM   22021 O  O   . HIS H  3 224 ? 20.059  -58.541 1.045    1.00 180.93 ? 222  HIS H O   1 
ATOM   22022 C  CB  . HIS H  3 224 ? 18.243  -57.833 -1.110   1.00 201.59 ? 222  HIS H CB  1 
ATOM   22023 C  CG  . HIS H  3 224 ? 17.111  -57.752 -0.125   1.00 208.98 ? 222  HIS H CG  1 
ATOM   22024 N  ND1 . HIS H  3 224 ? 17.302  -57.533 1.223    1.00 208.46 ? 222  HIS H ND1 1 
ATOM   22025 C  CD2 . HIS H  3 224 ? 15.772  -57.859 -0.300   1.00 205.84 ? 222  HIS H CD2 1 
ATOM   22026 C  CE1 . HIS H  3 224 ? 16.131  -57.513 1.835    1.00 202.16 ? 222  HIS H CE1 1 
ATOM   22027 N  NE2 . HIS H  3 224 ? 15.187  -57.710 0.934    1.00 205.35 ? 222  HIS H NE2 1 
ATOM   22028 N  N   . GLY H  3 225 ? 21.727  -57.936 -0.338   1.00 181.99 ? 223  GLY H N   1 
ATOM   22029 C  CA  . GLY H  3 225 ? 22.735  -58.649 0.412    1.00 191.06 ? 223  GLY H CA  1 
ATOM   22030 C  C   . GLY H  3 225 ? 23.569  -57.679 1.219    1.00 180.91 ? 223  GLY H C   1 
ATOM   22031 O  O   . GLY H  3 225 ? 24.373  -58.087 2.061    1.00 183.41 ? 223  GLY H O   1 
ATOM   22032 N  N   . MET H  3 226 ? 23.358  -56.383 0.993    1.00 162.10 ? 224  MET H N   1 
ATOM   22033 C  CA  . MET H  3 226 ? 24.035  -55.380 1.794    1.00 161.17 ? 224  MET H CA  1 
ATOM   22034 C  C   . MET H  3 226 ? 23.471  -55.377 3.205    1.00 160.24 ? 224  MET H C   1 
ATOM   22035 O  O   . MET H  3 226 ? 22.495  -56.063 3.515    1.00 160.86 ? 224  MET H O   1 
ATOM   22036 C  CB  . MET H  3 226 ? 23.895  -53.986 1.184    1.00 167.93 ? 224  MET H CB  1 
ATOM   22037 C  CG  . MET H  3 226 ? 25.082  -53.544 0.348    1.00 175.24 ? 224  MET H CG  1 
ATOM   22038 S  SD  . MET H  3 226 ? 24.986  -51.798 -0.095   1.00 172.75 ? 224  MET H SD  1 
ATOM   22039 C  CE  . MET H  3 226 ? 26.615  -51.541 -0.796   1.00 177.78 ? 224  MET H CE  1 
ATOM   22040 N  N   . ASN H  3 227 ? 24.128  -54.615 4.075    1.00 160.98 ? 225  ASN H N   1 
ATOM   22041 C  CA  . ASN H  3 227 ? 23.778  -54.495 5.486    1.00 163.89 ? 225  ASN H CA  1 
ATOM   22042 C  C   . ASN H  3 227 ? 23.759  -55.841 6.193    1.00 154.06 ? 225  ASN H C   1 
ATOM   22043 O  O   . ASN H  3 227 ? 23.259  -55.939 7.321    1.00 150.51 ? 225  ASN H O   1 
ATOM   22044 C  CB  . ASN H  3 227 ? 22.425  -53.793 5.677    1.00 177.75 ? 225  ASN H CB  1 
ATOM   22045 C  CG  . ASN H  3 227 ? 22.426  -52.363 5.175    1.00 187.74 ? 225  ASN H CG  1 
ATOM   22046 O  OD1 . ASN H  3 227 ? 23.480  -51.751 4.994    1.00 203.80 ? 225  ASN H OD1 1 
ATOM   22047 N  ND2 . ASN H  3 227 ? 21.235  -51.822 4.946    1.00 179.26 ? 225  ASN H ND2 1 
ATOM   22048 N  N   . ARG H  3 228 ? 24.297  -56.879 5.566    1.00 173.82 ? 226  ARG H N   1 
ATOM   22049 C  CA  . ARG H  3 228 ? 24.317  -58.177 6.200    1.00 169.37 ? 226  ARG H CA  1 
ATOM   22050 C  C   . ARG H  3 228 ? 25.316  -58.163 7.354    1.00 160.66 ? 226  ARG H C   1 
ATOM   22051 O  O   . ARG H  3 228 ? 26.234  -57.341 7.378    1.00 168.51 ? 226  ARG H O   1 
ATOM   22052 C  CB  . ARG H  3 228 ? 24.669  -59.271 5.189    1.00 161.06 ? 226  ARG H CB  1 
ATOM   22053 C  CG  . ARG H  3 228 ? 26.048  -59.164 4.551    1.00 160.20 ? 226  ARG H CG  1 
ATOM   22054 C  CD  . ARG H  3 228 ? 26.284  -60.333 3.595    1.00 170.66 ? 226  ARG H CD  1 
ATOM   22055 N  NE  . ARG H  3 228 ? 27.562  -60.266 2.884    1.00 193.16 ? 226  ARG H NE  1 
ATOM   22056 C  CZ  . ARG H  3 228 ? 27.706  -59.851 1.627    1.00 181.93 ? 226  ARG H CZ  1 
ATOM   22057 N  NH1 . ARG H  3 228 ? 26.647  -59.466 0.928    1.00 178.77 ? 226  ARG H NH1 1 
ATOM   22058 N  NH2 . ARG H  3 228 ? 28.907  -59.829 1.061    1.00 164.94 ? 226  ARG H NH2 1 
ATOM   22059 N  N   . PRO H  3 229 ? 25.107  -59.010 8.354    1.00 159.43 ? 227  PRO H N   1 
ATOM   22060 C  CA  . PRO H  3 229 ? 26.062  -59.130 9.465    1.00 155.85 ? 227  PRO H CA  1 
ATOM   22061 C  C   . PRO H  3 229 ? 27.531  -59.124 9.067    1.00 154.60 ? 227  PRO H C   1 
ATOM   22062 O  O   . PRO H  3 229 ? 27.962  -59.889 8.200    1.00 178.85 ? 227  PRO H O   1 
ATOM   22063 C  CB  . PRO H  3 229 ? 25.665  -60.469 10.089   1.00 180.98 ? 227  PRO H CB  1 
ATOM   22064 C  CG  . PRO H  3 229 ? 24.178  -60.499 9.903    1.00 184.03 ? 227  PRO H CG  1 
ATOM   22065 C  CD  . PRO H  3 229 ? 23.889  -59.804 8.591    1.00 176.18 ? 227  PRO H CD  1 
ATOM   22066 N  N   . PHE H  3 230 ? 28.301  -58.239 9.693    1.00 143.04 ? 228  PHE H N   1 
ATOM   22067 C  CA  . PHE H  3 230 ? 29.729  -58.127 9.454    1.00 141.03 ? 228  PHE H CA  1 
ATOM   22068 C  C   . PHE H  3 230 ? 30.470  -58.049 10.780   1.00 134.83 ? 228  PHE H C   1 
ATOM   22069 O  O   . PHE H  3 230 ? 29.934  -57.601 11.796   1.00 133.23 ? 228  PHE H O   1 
ATOM   22070 C  CB  . PHE H  3 230 ? 30.065  -56.893 8.618    1.00 159.97 ? 228  PHE H CB  1 
ATOM   22071 C  CG  . PHE H  3 230 ? 29.968  -55.605 9.384    1.00 164.22 ? 228  PHE H CG  1 
ATOM   22072 C  CD1 . PHE H  3 230 ? 28.739  -55.004 9.604    1.00 149.65 ? 228  PHE H CD1 1 
ATOM   22073 C  CD2 . PHE H  3 230 ? 31.105  -54.994 9.884    1.00 171.19 ? 228  PHE H CD2 1 
ATOM   22074 C  CE1 . PHE H  3 230 ? 28.651  -53.821 10.305   1.00 149.60 ? 228  PHE H CE1 1 
ATOM   22075 C  CE2 . PHE H  3 230 ? 31.021  -53.810 10.586   1.00 167.56 ? 228  PHE H CE2 1 
ATOM   22076 C  CZ  . PHE H  3 230 ? 29.792  -53.223 10.796   1.00 155.42 ? 228  PHE H CZ  1 
ATOM   22077 N  N   . LEU H  3 231 ? 31.731  -58.457 10.742   1.00 128.40 ? 229  LEU H N   1 
ATOM   22078 C  CA  . LEU H  3 231 ? 32.605  -58.466 11.910   1.00 126.29 ? 229  LEU H CA  1 
ATOM   22079 C  C   . LEU H  3 231 ? 33.563  -57.280 11.811   1.00 137.71 ? 229  LEU H C   1 
ATOM   22080 O  O   . LEU H  3 231 ? 34.475  -57.270 10.981   1.00 161.21 ? 229  LEU H O   1 
ATOM   22081 C  CB  . LEU H  3 231 ? 33.349  -59.792 11.997   1.00 127.27 ? 229  LEU H CB  1 
ATOM   22082 C  CG  . LEU H  3 231 ? 34.272  -60.005 13.195   1.00 133.82 ? 229  LEU H CG  1 
ATOM   22083 C  CD1 . LEU H  3 231 ? 33.508  -59.870 14.495   1.00 140.44 ? 229  LEU H CD1 1 
ATOM   22084 C  CD2 . LEU H  3 231 ? 34.934  -61.364 13.090   1.00 139.90 ? 229  LEU H CD2 1 
ATOM   22085 N  N   . LEU H  3 232 ? 33.330  -56.261 12.635   1.00 136.71 ? 230  LEU H N   1 
ATOM   22086 C  CA  . LEU H  3 232 ? 34.199  -55.091 12.678   1.00 138.25 ? 230  LEU H CA  1 
ATOM   22087 C  C   . LEU H  3 232 ? 35.469  -55.401 13.469   1.00 135.65 ? 230  LEU H C   1 
ATOM   22088 O  O   . LEU H  3 232 ? 35.404  -55.904 14.593   1.00 133.12 ? 230  LEU H O   1 
ATOM   22089 C  CB  . LEU H  3 232 ? 33.463  -53.907 13.299   1.00 144.16 ? 230  LEU H CB  1 
ATOM   22090 C  CG  . LEU H  3 232 ? 34.143  -52.546 13.165   1.00 154.33 ? 230  LEU H CG  1 
ATOM   22091 C  CD1 . LEU H  3 232 ? 34.275  -52.175 11.698   1.00 161.07 ? 230  LEU H CD1 1 
ATOM   22092 C  CD2 . LEU H  3 232 ? 33.364  -51.486 13.919   1.00 148.71 ? 230  LEU H CD2 1 
ATOM   22093 N  N   . LEU H  3 233 ? 36.622  -55.122 12.876   1.00 141.42 ? 231  LEU H N   1 
ATOM   22094 C  CA  . LEU H  3 233 ? 37.912  -55.421 13.483   1.00 159.13 ? 231  LEU H CA  1 
ATOM   22095 C  C   . LEU H  3 233 ? 38.672  -54.134 13.777   1.00 161.96 ? 231  LEU H C   1 
ATOM   22096 O  O   . LEU H  3 233 ? 38.601  -53.171 13.007   1.00 185.00 ? 231  LEU H O   1 
ATOM   22097 C  CB  . LEU H  3 233 ? 38.748  -56.316 12.563   1.00 176.84 ? 231  LEU H CB  1 
ATOM   22098 C  CG  . LEU H  3 233 ? 38.105  -57.620 12.089   1.00 152.69 ? 231  LEU H CG  1 
ATOM   22099 C  CD1 . LEU H  3 233 ? 38.999  -58.307 11.066   1.00 141.89 ? 231  LEU H CD1 1 
ATOM   22100 C  CD2 . LEU H  3 233 ? 37.831  -58.532 13.275   1.00 135.86 ? 231  LEU H CD2 1 
ATOM   22101 N  N   . MET H  3 234 ? 39.386  -54.109 14.901   1.00 141.95 ? 232  MET H N   1 
ATOM   22102 C  CA  . MET H  3 234 ? 40.229  -52.971 15.272   1.00 145.18 ? 232  MET H CA  1 
ATOM   22103 C  C   . MET H  3 234 ? 41.574  -53.515 15.749   1.00 145.76 ? 232  MET H C   1 
ATOM   22104 O  O   . MET H  3 234 ? 41.682  -54.024 16.867   1.00 143.15 ? 232  MET H O   1 
ATOM   22105 C  CB  . MET H  3 234 ? 39.556  -52.114 16.337   1.00 165.34 ? 232  MET H CB  1 
ATOM   22106 C  CG  . MET H  3 234 ? 38.173  -51.618 15.939   1.00 172.15 ? 232  MET H CG  1 
ATOM   22107 S  SD  . MET H  3 234 ? 37.343  -50.752 17.280   1.00 197.21 ? 232  MET H SD  1 
ATOM   22108 C  CE  . MET H  3 234 ? 35.774  -50.358 16.516   1.00 190.10 ? 232  MET H CE  1 
ATOM   22109 N  N   . ALA H  3 235 ? 42.597  -53.415 14.903   1.00 157.76 ? 233  ALA H N   1 
ATOM   22110 C  CA  . ALA H  3 235 ? 43.901  -54.005 15.173   1.00 176.53 ? 233  ALA H CA  1 
ATOM   22111 C  C   . ALA H  3 235 ? 44.998  -52.955 15.030   1.00 191.86 ? 233  ALA H C   1 
ATOM   22112 O  O   . ALA H  3 235 ? 44.760  -51.823 14.601   1.00 211.82 ? 233  ALA H O   1 
ATOM   22113 C  CB  . ALA H  3 235 ? 44.179  -55.191 14.237   1.00 188.04 ? 233  ALA H CB  1 
ATOM   22114 N  N   . THR H  3 236 ? 46.243  -53.355 15.403   1.00 181.92 ? 234  THR H N   1 
ATOM   22115 C  CA  . THR H  3 236 ? 47.427  -52.503 15.312   1.00 173.05 ? 234  THR H CA  1 
ATOM   22116 C  C   . THR H  3 236 ? 48.225  -52.846 14.064   1.00 177.35 ? 234  THR H C   1 
ATOM   22117 O  O   . THR H  3 236 ? 48.533  -54.028 13.841   1.00 182.00 ? 234  THR H O   1 
ATOM   22118 C  CB  . THR H  3 236 ? 48.309  -52.669 16.545   1.00 170.43 ? 234  THR H CB  1 
ATOM   22119 O  OG1 . THR H  3 236 ? 47.581  -52.285 17.718   1.00 166.85 ? 234  THR H OG1 1 
ATOM   22120 C  CG2 . THR H  3 236 ? 49.562  -51.812 16.422   1.00 178.24 ? 234  THR H CG2 1 
ATOM   22121 N  N   . PRO H  3 237 ? 48.561  -51.860 13.230   1.00 188.02 ? 235  PRO H N   1 
ATOM   22122 C  CA  . PRO H  3 237 ? 49.282  -52.152 11.985   1.00 196.77 ? 235  PRO H CA  1 
ATOM   22123 C  C   . PRO H  3 237 ? 50.609  -52.861 12.223   1.00 202.61 ? 235  PRO H C   1 
ATOM   22124 O  O   . PRO H  3 237 ? 51.244  -52.721 13.272   1.00 203.21 ? 235  PRO H O   1 
ATOM   22125 C  CB  . PRO H  3 237 ? 49.493  -50.765 11.368   1.00 195.10 ? 235  PRO H CB  1 
ATOM   22126 C  CG  . PRO H  3 237 ? 48.380  -49.936 11.932   1.00 196.14 ? 235  PRO H CG  1 
ATOM   22127 C  CD  . PRO H  3 237 ? 48.186  -50.440 13.334   1.00 191.70 ? 235  PRO H CD  1 
ATOM   22128 N  N   . LEU H  3 238 ? 51.015  -53.642 11.216   1.00 195.25 ? 236  LEU H N   1 
ATOM   22129 C  CA  . LEU H  3 238 ? 52.274  -54.379 11.277   1.00 186.80 ? 236  LEU H CA  1 
ATOM   22130 C  C   . LEU H  3 238 ? 53.475  -53.451 11.169   1.00 195.51 ? 236  LEU H C   1 
ATOM   22131 O  O   . LEU H  3 238 ? 54.559  -53.778 11.668   1.00 196.27 ? 236  LEU H O   1 
ATOM   22132 C  CB  . LEU H  3 238 ? 52.329  -55.418 10.152   1.00 182.41 ? 236  LEU H CB  1 
ATOM   22133 C  CG  . LEU H  3 238 ? 51.262  -56.513 10.071   1.00 174.94 ? 236  LEU H CG  1 
ATOM   22134 C  CD1 . LEU H  3 238 ? 50.011  -56.020 9.362    1.00 172.36 ? 236  LEU H CD1 1 
ATOM   22135 C  CD2 . LEU H  3 238 ? 51.818  -57.739 9.367    1.00 189.47 ? 236  LEU H CD2 1 
ATOM   22136 N  N   . GLU H  3 239 ? 53.302  -52.297 10.518   1.00 212.77 ? 237  GLU H N   1 
ATOM   22137 C  CA  . GLU H  3 239 ? 54.411  -51.368 10.344   1.00 221.44 ? 237  GLU H CA  1 
ATOM   22138 C  C   . GLU H  3 239 ? 54.899  -50.837 11.682   1.00 221.29 ? 237  GLU H C   1 
ATOM   22139 O  O   . GLU H  3 239 ? 56.085  -50.522 11.831   1.00 228.86 ? 237  GLU H O   1 
ATOM   22140 C  CB  . GLU H  3 239 ? 53.999  -50.210 9.429    1.00 222.44 ? 237  GLU H CB  1 
ATOM   22141 C  CG  . GLU H  3 239 ? 53.632  -50.611 8.001    1.00 222.73 ? 237  GLU H CG  1 
ATOM   22142 C  CD  . GLU H  3 239 ? 52.251  -51.233 7.899    1.00 232.48 ? 237  GLU H CD  1 
ATOM   22143 O  OE1 . GLU H  3 239 ? 51.500  -51.186 8.896    1.00 241.81 ? 237  GLU H OE1 1 
ATOM   22144 O  OE2 . GLU H  3 239 ? 51.918  -51.769 6.822    1.00 231.16 ? 237  GLU H OE2 1 
ATOM   22145 N  N   . ARG H  3 240 ? 54.009  -50.751 12.672   1.00 206.34 ? 238  ARG H N   1 
ATOM   22146 C  CA  . ARG H  3 240 ? 54.401  -50.236 13.977   1.00 204.19 ? 238  ARG H CA  1 
ATOM   22147 C  C   . ARG H  3 240 ? 55.135  -51.303 14.778   1.00 205.77 ? 238  ARG H C   1 
ATOM   22148 O  O   . ARG H  3 240 ? 56.319  -51.146 15.098   1.00 217.46 ? 238  ARG H O   1 
ATOM   22149 C  CB  . ARG H  3 240 ? 53.168  -49.737 14.734   1.00 203.83 ? 238  ARG H CB  1 
ATOM   22150 C  CG  . ARG H  3 240 ? 52.248  -48.878 13.887   1.00 205.11 ? 238  ARG H CG  1 
ATOM   22151 C  CD  . ARG H  3 240 ? 51.192  -48.187 14.729   1.00 199.34 ? 238  ARG H CD  1 
ATOM   22152 N  NE  . ARG H  3 240 ? 50.113  -47.640 13.911   1.00 195.95 ? 238  ARG H NE  1 
ATOM   22153 C  CZ  . ARG H  3 240 ? 50.197  -46.507 13.221   1.00 202.04 ? 238  ARG H CZ  1 
ATOM   22154 N  NH1 . ARG H  3 240 ? 51.317  -45.798 13.236   1.00 205.12 ? 238  ARG H NH1 1 
ATOM   22155 N  NH2 . ARG H  3 240 ? 49.163  -46.087 12.507   1.00 207.86 ? 238  ARG H NH2 1 
ATOM   22156 N  N   . ALA H  3 241 ? 54.445  -52.403 15.090   1.00 189.56 ? 239  ALA H N   1 
ATOM   22157 C  CA  . ALA H  3 241 ? 55.018  -53.516 15.838   1.00 187.96 ? 239  ALA H CA  1 
ATOM   22158 C  C   . ALA H  3 241 ? 55.769  -53.032 17.072   1.00 191.85 ? 239  ALA H C   1 
ATOM   22159 O  O   . ALA H  3 241 ? 55.365  -52.051 17.705   1.00 191.70 ? 239  ALA H O   1 
ATOM   22160 C  CB  . ALA H  3 241 ? 55.948  -54.339 14.941   1.00 198.41 ? 239  ALA H CB  1 
ATOM   22161 N  N   . GLN H  3 242 ? 56.869  -53.704 17.402   1.00 200.54 ? 240  GLN H N   1 
ATOM   22162 C  CA  . GLN H  3 242 ? 57.710  -53.332 18.538   1.00 204.56 ? 240  GLN H CA  1 
ATOM   22163 C  C   . GLN H  3 242 ? 56.907  -53.242 19.835   1.00 198.63 ? 240  GLN H C   1 
ATOM   22164 O  O   . GLN H  3 242 ? 55.983  -54.022 20.063   1.00 195.86 ? 240  GLN H O   1 
ATOM   22165 C  CB  . GLN H  3 242 ? 58.424  -52.004 18.257   1.00 208.71 ? 240  GLN H CB  1 
ATOM   22166 C  CG  . GLN H  3 242 ? 59.337  -51.538 19.375   1.00 213.80 ? 240  GLN H CG  1 
ATOM   22167 C  CD  . GLN H  3 242 ? 58.616  -50.655 20.371   1.00 215.32 ? 240  GLN H CD  1 
ATOM   22168 O  OE1 . GLN H  3 242 ? 57.545  -50.122 20.080   1.00 204.78 ? 240  GLN H OE1 1 
ATOM   22169 N  NE2 . GLN H  3 242 ? 59.190  -50.510 21.559   1.00 227.52 ? 240  GLN H NE2 1 
ATOM   22170 N  N   . SER H  3 261 ? 58.854  -45.077 38.783   1.00 213.31 ? 259  SER H N   1 
ATOM   22171 C  CA  . SER H  3 261 ? 58.683  -45.646 40.110   1.00 201.73 ? 259  SER H CA  1 
ATOM   22172 C  C   . SER H  3 261 ? 59.612  -44.931 41.091   1.00 207.79 ? 259  SER H C   1 
ATOM   22173 O  O   . SER H  3 261 ? 59.348  -44.910 42.291   1.00 208.23 ? 259  SER H O   1 
ATOM   22174 C  CB  . SER H  3 261 ? 58.968  -47.141 40.091   1.00 198.05 ? 259  SER H CB  1 
ATOM   22175 O  OG  . SER H  3 261 ? 60.308  -47.361 39.694   1.00 211.76 ? 259  SER H OG  1 
ATOM   22176 N  N   . THR H  3 262 ? 60.688  -44.342 40.566   1.00 225.10 ? 260  THR H N   1 
ATOM   22177 C  CA  . THR H  3 262 ? 61.656  -43.558 41.336   1.00 231.10 ? 260  THR H CA  1 
ATOM   22178 C  C   . THR H  3 262 ? 61.357  -42.068 41.260   1.00 230.33 ? 260  THR H C   1 
ATOM   22179 O  O   . THR H  3 262 ? 62.233  -41.252 40.963   1.00 234.50 ? 260  THR H O   1 
ATOM   22180 C  CB  . THR H  3 262 ? 63.079  -43.832 40.847   1.00 237.22 ? 260  THR H CB  1 
ATOM   22181 O  OG1 . THR H  3 262 ? 63.173  -43.512 39.454   1.00 247.79 ? 260  THR H OG1 1 
ATOM   22182 C  CG2 . THR H  3 262 ? 63.452  -45.303 41.062   1.00 225.61 ? 260  THR H CG2 1 
ATOM   22183 N  N   . GLU H  3 263 ? 60.080  -41.706 41.453   1.00 221.12 ? 261  GLU H N   1 
ATOM   22184 C  CA  . GLU H  3 263 ? 59.608  -40.325 41.645   1.00 221.55 ? 261  GLU H CA  1 
ATOM   22185 C  C   . GLU H  3 263 ? 60.308  -39.276 40.768   1.00 224.04 ? 261  GLU H C   1 
ATOM   22186 O  O   . GLU H  3 263 ? 60.525  -38.130 41.173   1.00 225.33 ? 261  GLU H O   1 
ATOM   22187 C  CB  . GLU H  3 263 ? 59.719  -39.944 43.104   1.00 203.53 ? 261  GLU H CB  1 
ATOM   22188 C  CG  . GLU H  3 263 ? 61.131  -39.496 43.494   1.00 208.13 ? 261  GLU H CG  1 
ATOM   22189 C  CD  . GLU H  3 263 ? 61.475  -39.781 44.994   1.00 221.35 ? 261  GLU H CD  1 
ATOM   22190 O  OE1 . GLU H  3 263 ? 60.591  -39.721 45.972   1.00 234.57 ? 261  GLU H OE1 1 
ATOM   22191 O  OE2 . GLU H  3 263 ? 62.696  -40.088 45.172   1.00 221.34 ? 261  GLU H OE2 1 
ATOM   22192 N  N   . LYS H  3 264 ? 60.612  -39.655 39.534   1.00 237.88 ? 262  LYS H N   1 
ATOM   22193 C  CA  . LYS H  3 264 ? 61.023  -38.721 38.497   1.00 243.71 ? 262  LYS H CA  1 
ATOM   22194 C  C   . LYS H  3 264 ? 59.808  -38.117 37.809   1.00 232.06 ? 262  LYS H C   1 
ATOM   22195 O  O   . LYS H  3 264 ? 59.653  -36.894 37.749   1.00 225.76 ? 262  LYS H O   1 
ATOM   22196 C  CB  . LYS H  3 264 ? 61.896  -39.436 37.466   1.00 242.21 ? 262  LYS H CB  1 
ATOM   22197 C  CG  . LYS H  3 264 ? 62.497  -38.511 36.434   1.00 229.18 ? 262  LYS H CG  1 
ATOM   22198 C  CD  . LYS H  3 264 ? 62.902  -39.282 35.192   1.00 223.37 ? 262  LYS H CD  1 
ATOM   22199 C  CE  . LYS H  3 264 ? 63.680  -40.548 35.529   1.00 229.27 ? 262  LYS H CE  1 
ATOM   22200 N  NZ  . LYS H  3 264 ? 64.944  -40.287 36.275   1.00 232.13 ? 262  LYS H NZ  1 
ATOM   22201 N  N   . ASN H  3 265 ? 58.932  -38.969 37.286   1.00 228.72 ? 263  ASN H N   1 
ATOM   22202 C  CA  . ASN H  3 265 ? 57.699  -38.511 36.666   1.00 221.81 ? 263  ASN H CA  1 
ATOM   22203 C  C   . ASN H  3 265 ? 56.559  -38.627 37.673   1.00 232.89 ? 263  ASN H C   1 
ATOM   22204 O  O   . ASN H  3 265 ? 56.778  -38.856 38.865   1.00 251.87 ? 263  ASN H O   1 
ATOM   22205 C  CB  . ASN H  3 265 ? 57.413  -39.295 35.391   1.00 213.03 ? 263  ASN H CB  1 
ATOM   22206 C  CG  . ASN H  3 265 ? 58.381  -38.968 34.289   1.00 204.48 ? 263  ASN H CG  1 
ATOM   22207 O  OD1 . ASN H  3 265 ? 58.650  -37.800 34.008   1.00 208.77 ? 263  ASN H OD1 1 
ATOM   22208 N  ND2 . ASN H  3 265 ? 58.942  -39.998 33.678   1.00 199.37 ? 263  ASN H ND2 1 
ATOM   22209 N  N   . CYS H  3 266 ? 55.326  -38.451 37.200   1.00 225.60 ? 264  CYS H N   1 
ATOM   22210 C  CA  . CYS H  3 266 ? 54.148  -38.519 38.062   1.00 219.70 ? 264  CYS H CA  1 
ATOM   22211 C  C   . CYS H  3 266 ? 53.894  -39.959 38.499   1.00 219.66 ? 264  CYS H C   1 
ATOM   22212 O  O   . CYS H  3 266 ? 53.240  -40.725 37.786   1.00 210.33 ? 264  CYS H O   1 
ATOM   22213 C  CB  . CYS H  3 266 ? 52.942  -37.911 37.328   1.00 214.48 ? 264  CYS H CB  1 
ATOM   22214 S  SG  . CYS H  3 266 ? 51.256  -38.230 37.938   1.00 214.60 ? 264  CYS H SG  1 
ATOM   22215 N  N   . CYS H  3 267 ? 54.435  -40.341 39.658   1.00 228.82 ? 265  CYS H N   1 
ATOM   22216 C  CA  . CYS H  3 267 ? 54.278  -41.681 40.208   1.00 231.17 ? 265  CYS H CA  1 
ATOM   22217 C  C   . CYS H  3 267 ? 53.663  -41.611 41.603   1.00 228.46 ? 265  CYS H C   1 
ATOM   22218 O  O   . CYS H  3 267 ? 53.830  -40.622 42.325   1.00 232.21 ? 265  CYS H O   1 
ATOM   22219 C  CB  . CYS H  3 267 ? 55.622  -42.422 40.265   1.00 243.78 ? 265  CYS H CB  1 
ATOM   22220 S  SG  . CYS H  3 267 ? 56.383  -42.702 38.641   1.00 248.71 ? 265  CYS H SG  1 
ATOM   22221 N  N   . VAL H  3 268 ? 52.953  -42.673 41.977   1.00 225.38 ? 266  VAL H N   1 
ATOM   22222 C  CA  . VAL H  3 268 ? 52.257  -42.723 43.260   1.00 222.94 ? 266  VAL H CA  1 
ATOM   22223 C  C   . VAL H  3 268 ? 53.232  -43.179 44.342   1.00 224.98 ? 266  VAL H C   1 
ATOM   22224 O  O   . VAL H  3 268 ? 53.872  -44.229 44.220   1.00 221.65 ? 266  VAL H O   1 
ATOM   22225 C  CB  . VAL H  3 268 ? 51.026  -43.640 43.186   1.00 219.15 ? 266  VAL H CB  1 
ATOM   22226 C  CG1 . VAL H  3 268 ? 51.345  -44.921 42.424   1.00 217.74 ? 266  VAL H CG1 1 
ATOM   22227 C  CG2 . VAL H  3 268 ? 50.509  -43.953 44.581   1.00 224.43 ? 266  VAL H CG2 1 
ATOM   22228 N  N   . ARG H  3 269 ? 53.346  -42.385 45.407   1.00 238.25 ? 267  ARG H N   1 
ATOM   22229 C  CA  . ARG H  3 269 ? 54.278  -42.642 46.495   1.00 250.83 ? 267  ARG H CA  1 
ATOM   22230 C  C   . ARG H  3 269 ? 53.567  -43.302 47.676   1.00 261.16 ? 267  ARG H C   1 
ATOM   22231 O  O   . ARG H  3 269 ? 52.362  -43.129 47.878   1.00 263.26 ? 267  ARG H O   1 
ATOM   22232 C  CB  . ARG H  3 269 ? 54.948  -41.338 46.948   1.00 248.68 ? 267  ARG H CB  1 
ATOM   22233 C  CG  . ARG H  3 269 ? 55.652  -40.568 45.830   1.00 242.28 ? 267  ARG H CG  1 
ATOM   22234 C  CD  . ARG H  3 269 ? 56.293  -39.285 46.348   1.00 242.25 ? 267  ARG H CD  1 
ATOM   22235 N  NE  . ARG H  3 269 ? 57.307  -39.556 47.364   1.00 241.62 ? 267  ARG H NE  1 
ATOM   22236 C  CZ  . ARG H  3 269 ? 57.969  -38.617 48.033   1.00 239.47 ? 267  ARG H CZ  1 
ATOM   22237 N  NH1 . ARG H  3 269 ? 57.729  -37.334 47.798   1.00 242.61 ? 267  ARG H NH1 1 
ATOM   22238 N  NH2 . ARG H  3 269 ? 58.873  -38.964 48.939   1.00 237.83 ? 267  ARG H NH2 1 
ATOM   22239 N  N   . GLN H  3 270 ? 54.335  -44.061 48.460   1.00 260.37 ? 268  GLN H N   1 
ATOM   22240 C  CA  . GLN H  3 270 ? 53.793  -44.795 49.598   1.00 252.17 ? 268  GLN H CA  1 
ATOM   22241 C  C   . GLN H  3 270 ? 53.552  -43.866 50.784   1.00 256.89 ? 268  GLN H C   1 
ATOM   22242 O  O   . GLN H  3 270 ? 54.341  -42.954 51.049   1.00 259.37 ? 268  GLN H O   1 
ATOM   22243 C  CB  . GLN H  3 270 ? 54.748  -45.923 50.003   1.00 255.46 ? 268  GLN H CB  1 
ATOM   22244 C  CG  . GLN H  3 270 ? 54.268  -46.799 51.163   1.00 264.94 ? 268  GLN H CG  1 
ATOM   22245 C  CD  . GLN H  3 270 ? 55.312  -47.817 51.605   1.00 273.07 ? 268  GLN H CD  1 
ATOM   22246 O  OE1 . GLN H  3 270 ? 56.371  -47.942 50.990   1.00 278.00 ? 268  GLN H OE1 1 
ATOM   22247 N  NE2 . GLN H  3 270 ? 55.017  -48.547 52.678   1.00 266.41 ? 268  GLN H NE2 1 
ATOM   22248 N  N   . LEU H  3 271 ? 52.454  -44.110 51.505   1.00 242.38 ? 269  LEU H N   1 
ATOM   22249 C  CA  . LEU H  3 271 ? 52.114  -43.306 52.680   1.00 244.50 ? 269  LEU H CA  1 
ATOM   22250 C  C   . LEU H  3 271 ? 51.147  -44.101 53.550   1.00 245.17 ? 269  LEU H C   1 
ATOM   22251 O  O   . LEU H  3 271 ? 50.003  -44.336 53.147   1.00 245.92 ? 269  LEU H O   1 
ATOM   22252 C  CB  . LEU H  3 271 ? 51.507  -41.973 52.264   1.00 237.46 ? 269  LEU H CB  1 
ATOM   22253 C  CG  . LEU H  3 271 ? 51.037  -41.074 53.406   1.00 240.06 ? 269  LEU H CG  1 
ATOM   22254 C  CD1 . LEU H  3 271 ? 52.190  -40.761 54.342   1.00 247.82 ? 269  LEU H CD1 1 
ATOM   22255 C  CD2 . LEU H  3 271 ? 50.427  -39.799 52.854   1.00 242.23 ? 269  LEU H CD2 1 
ATOM   22256 N  N   . TYR H  3 272 ? 51.597  -44.502 54.738   1.00 244.97 ? 270  TYR H N   1 
ATOM   22257 C  CA  . TYR H  3 272 ? 50.773  -45.249 55.681   1.00 242.46 ? 270  TYR H CA  1 
ATOM   22258 C  C   . TYR H  3 272 ? 50.246  -44.300 56.749   1.00 248.95 ? 270  TYR H C   1 
ATOM   22259 O  O   . TYR H  3 272 ? 51.028  -43.604 57.408   1.00 259.90 ? 270  TYR H O   1 
ATOM   22260 C  CB  . TYR H  3 272 ? 51.566  -46.389 56.320   1.00 238.36 ? 270  TYR H CB  1 
ATOM   22261 C  CG  . TYR H  3 272 ? 50.834  -47.083 57.446   1.00 235.39 ? 270  TYR H CG  1 
ATOM   22262 C  CD1 . TYR H  3 272 ? 49.817  -47.991 57.185   1.00 228.35 ? 270  TYR H CD1 1 
ATOM   22263 C  CD2 . TYR H  3 272 ? 51.167  -46.835 58.771   1.00 239.34 ? 270  TYR H CD2 1 
ATOM   22264 C  CE1 . TYR H  3 272 ? 49.150  -48.628 58.210   1.00 229.41 ? 270  TYR H CE1 1 
ATOM   22265 C  CE2 . TYR H  3 272 ? 50.507  -47.468 59.802   1.00 239.30 ? 270  TYR H CE2 1 
ATOM   22266 C  CZ  . TYR H  3 272 ? 49.502  -48.362 59.516   1.00 235.56 ? 270  TYR H CZ  1 
ATOM   22267 O  OH  . TYR H  3 272 ? 48.847  -48.992 60.546   1.00 243.61 ? 270  TYR H OH  1 
ATOM   22268 N  N   . ILE H  3 273 ? 48.928  -44.287 56.933   1.00 240.04 ? 271  ILE H N   1 
ATOM   22269 C  CA  . ILE H  3 273 ? 48.270  -43.362 57.849   1.00 236.08 ? 271  ILE H CA  1 
ATOM   22270 C  C   . ILE H  3 273 ? 47.646  -44.157 58.985   1.00 230.16 ? 271  ILE H C   1 
ATOM   22271 O  O   . ILE H  3 273 ? 46.808  -45.039 58.754   1.00 226.31 ? 271  ILE H O   1 
ATOM   22272 C  CB  . ILE H  3 273 ? 47.216  -42.509 57.131   1.00 231.31 ? 271  ILE H CB  1 
ATOM   22273 C  CG1 . ILE H  3 273 ? 47.895  -41.579 56.127   1.00 234.44 ? 271  ILE H CG1 1 
ATOM   22274 C  CG2 . ILE H  3 273 ? 46.403  -41.716 58.142   1.00 232.42 ? 271  ILE H CG2 1 
ATOM   22275 C  CD1 . ILE H  3 273 ? 46.953  -40.597 55.487   1.00 237.43 ? 271  ILE H CD1 1 
ATOM   22276 N  N   . ASP H  3 274 ? 48.045  -43.832 60.210   1.00 251.92 ? 272  ASP H N   1 
ATOM   22277 C  CA  . ASP H  3 274 ? 47.469  -44.410 61.414   1.00 261.29 ? 272  ASP H CA  1 
ATOM   22278 C  C   . ASP H  3 274 ? 46.507  -43.406 62.041   1.00 258.95 ? 272  ASP H C   1 
ATOM   22279 O  O   . ASP H  3 274 ? 46.732  -42.193 61.984   1.00 261.23 ? 272  ASP H O   1 
ATOM   22280 C  CB  . ASP H  3 274 ? 48.570  -44.795 62.410   1.00 269.95 ? 272  ASP H CB  1 
ATOM   22281 C  CG  . ASP H  3 274 ? 48.084  -45.743 63.499   1.00 260.52 ? 272  ASP H CG  1 
ATOM   22282 O  OD1 . ASP H  3 274 ? 46.906  -45.649 63.905   1.00 252.58 ? 272  ASP H OD1 1 
ATOM   22283 O  OD2 . ASP H  3 274 ? 48.890  -46.581 63.958   1.00 256.52 ? 272  ASP H OD2 1 
ATOM   22284 N  N   . PHE H  3 275 ? 45.426  -43.916 62.630   1.00 245.82 ? 273  PHE H N   1 
ATOM   22285 C  CA  . PHE H  3 275 ? 44.428  -43.027 63.213   1.00 239.70 ? 273  PHE H CA  1 
ATOM   22286 C  C   . PHE H  3 275 ? 44.872  -42.495 64.569   1.00 242.82 ? 273  PHE H C   1 
ATOM   22287 O  O   . PHE H  3 275 ? 44.702  -41.304 64.857   1.00 246.16 ? 273  PHE H O   1 
ATOM   22288 C  CB  . PHE H  3 275 ? 43.091  -43.750 63.337   1.00 242.84 ? 273  PHE H CB  1 
ATOM   22289 C  CG  . PHE H  3 275 ? 42.490  -44.128 62.020   1.00 242.14 ? 273  PHE H CG  1 
ATOM   22290 C  CD1 . PHE H  3 275 ? 41.702  -43.228 61.324   1.00 245.47 ? 273  PHE H CD1 1 
ATOM   22291 C  CD2 . PHE H  3 275 ? 42.719  -45.377 61.472   1.00 242.39 ? 273  PHE H CD2 1 
ATOM   22292 C  CE1 . PHE H  3 275 ? 41.149  -43.571 60.109   1.00 243.84 ? 273  PHE H CE1 1 
ATOM   22293 C  CE2 . PHE H  3 275 ? 42.168  -45.726 60.256   1.00 243.12 ? 273  PHE H CE2 1 
ATOM   22294 C  CZ  . PHE H  3 275 ? 41.383  -44.822 59.574   1.00 243.80 ? 273  PHE H CZ  1 
ATOM   22295 N  N   . ARG H  3 276 ? 45.437  -43.360 65.413   1.00 246.42 ? 274  ARG H N   1 
ATOM   22296 C  CA  . ARG H  3 276 ? 45.894  -42.917 66.725   1.00 250.40 ? 274  ARG H CA  1 
ATOM   22297 C  C   . ARG H  3 276 ? 47.169  -42.090 66.625   1.00 261.23 ? 274  ARG H C   1 
ATOM   22298 O  O   . ARG H  3 276 ? 47.429  -41.244 67.490   1.00 268.60 ? 274  ARG H O   1 
ATOM   22299 C  CB  . ARG H  3 276 ? 46.112  -44.127 67.638   1.00 247.37 ? 274  ARG H CB  1 
ATOM   22300 C  CG  . ARG H  3 276 ? 44.842  -44.903 67.957   1.00 238.19 ? 274  ARG H CG  1 
ATOM   22301 C  CD  . ARG H  3 276 ? 44.019  -44.236 69.056   1.00 237.29 ? 274  ARG H CD  1 
ATOM   22302 N  NE  . ARG H  3 276 ? 44.640  -44.376 70.371   1.00 237.38 ? 274  ARG H NE  1 
ATOM   22303 C  CZ  . ARG H  3 276 ? 45.362  -43.429 70.963   1.00 240.00 ? 274  ARG H CZ  1 
ATOM   22304 N  NH1 . ARG H  3 276 ? 45.551  -42.263 70.361   1.00 247.08 ? 274  ARG H NH1 1 
ATOM   22305 N  NH2 . ARG H  3 276 ? 45.892  -43.645 72.159   1.00 240.21 ? 274  ARG H NH2 1 
ATOM   22306 N  N   . LYS H  3 277 ? 47.969  -42.310 65.582   1.00 268.89 ? 275  LYS H N   1 
ATOM   22307 C  CA  . LYS H  3 277 ? 49.265  -41.656 65.461   1.00 279.46 ? 275  LYS H CA  1 
ATOM   22308 C  C   . LYS H  3 277 ? 49.190  -40.373 64.643   1.00 279.57 ? 275  LYS H C   1 
ATOM   22309 O  O   . LYS H  3 277 ? 49.767  -39.353 65.037   1.00 286.04 ? 275  LYS H O   1 
ATOM   22310 C  CB  . LYS H  3 277 ? 50.275  -42.623 64.831   1.00 268.67 ? 275  LYS H CB  1 
ATOM   22311 C  CG  . LYS H  3 277 ? 51.677  -42.059 64.662   1.00 261.34 ? 275  LYS H CG  1 
ATOM   22312 C  CD  . LYS H  3 277 ? 52.339  -41.803 66.005   1.00 261.29 ? 275  LYS H CD  1 
ATOM   22313 C  CE  . LYS H  3 277 ? 53.775  -41.339 65.832   1.00 264.04 ? 275  LYS H CE  1 
ATOM   22314 N  NZ  . LYS H  3 277 ? 53.863  -40.097 65.019   1.00 274.43 ? 275  LYS H NZ  1 
ATOM   22315 N  N   . ASP H  3 278 ? 48.480  -40.397 63.519   1.00 261.77 ? 276  ASP H N   1 
ATOM   22316 C  CA  . ASP H  3 278 ? 48.434  -39.260 62.617   1.00 261.77 ? 276  ASP H CA  1 
ATOM   22317 C  C   . ASP H  3 278 ? 47.137  -38.462 62.718   1.00 267.52 ? 276  ASP H C   1 
ATOM   22318 O  O   . ASP H  3 278 ? 47.005  -37.438 62.046   1.00 279.83 ? 276  ASP H O   1 
ATOM   22319 C  CB  . ASP H  3 278 ? 48.648  -39.732 61.174   1.00 248.03 ? 276  ASP H CB  1 
ATOM   22320 C  CG  . ASP H  3 278 ? 49.964  -40.481 60.991   1.00 243.61 ? 276  ASP H CG  1 
ATOM   22321 O  OD1 . ASP H  3 278 ? 50.953  -40.141 61.674   1.00 245.15 ? 276  ASP H OD1 1 
ATOM   22322 O  OD2 . ASP H  3 278 ? 50.011  -41.413 60.160   1.00 242.90 ? 276  ASP H OD2 1 
ATOM   22323 N  N   . LEU H  3 279 ? 46.183  -38.889 63.543   1.00 259.00 ? 277  LEU H N   1 
ATOM   22324 C  CA  . LEU H  3 279 ? 44.915  -38.172 63.641   1.00 252.57 ? 277  LEU H CA  1 
ATOM   22325 C  C   . LEU H  3 279 ? 44.519  -37.953 65.092   1.00 256.16 ? 277  LEU H C   1 
ATOM   22326 O  O   . LEU H  3 279 ? 43.931  -36.922 65.434   1.00 260.97 ? 277  LEU H O   1 
ATOM   22327 C  CB  . LEU H  3 279 ? 43.804  -38.930 62.915   1.00 250.85 ? 277  LEU H CB  1 
ATOM   22328 C  CG  . LEU H  3 279 ? 43.836  -38.871 61.388   1.00 259.87 ? 277  LEU H CG  1 
ATOM   22329 C  CD1 . LEU H  3 279 ? 42.703  -39.698 60.806   1.00 253.89 ? 277  LEU H CD1 1 
ATOM   22330 C  CD2 . LEU H  3 279 ? 43.755  -37.426 60.917   1.00 265.72 ? 277  LEU H CD2 1 
ATOM   22331 N  N   . GLY H  3 280 ? 44.840  -38.920 65.944   1.00 254.02 ? 278  GLY H N   1 
ATOM   22332 C  CA  . GLY H  3 280 ? 44.453  -38.841 67.340   1.00 255.39 ? 278  GLY H CA  1 
ATOM   22333 C  C   . GLY H  3 280 ? 42.968  -39.023 67.551   1.00 254.73 ? 278  GLY H C   1 
ATOM   22334 O  O   . GLY H  3 280 ? 42.375  -38.326 68.385   1.00 261.38 ? 278  GLY H O   1 
ATOM   22335 N  N   . TRP H  3 281 ? 42.348  -39.934 66.809   1.00 250.36 ? 279  TRP H N   1 
ATOM   22336 C  CA  . TRP H  3 281 ? 40.912  -40.176 66.882   1.00 250.48 ? 279  TRP H CA  1 
ATOM   22337 C  C   . TRP H  3 281 ? 40.682  -41.570 67.454   1.00 239.01 ? 279  TRP H C   1 
ATOM   22338 O  O   . TRP H  3 281 ? 40.920  -42.575 66.776   1.00 239.77 ? 279  TRP H O   1 
ATOM   22339 C  CB  . TRP H  3 281 ? 40.267  -40.026 65.506   1.00 258.38 ? 279  TRP H CB  1 
ATOM   22340 C  CG  . TRP H  3 281 ? 40.227  -38.608 65.012   1.00 261.75 ? 279  TRP H CG  1 
ATOM   22341 C  CD1 . TRP H  3 281 ? 40.723  -37.502 65.643   1.00 263.81 ? 279  TRP H CD1 1 
ATOM   22342 C  CD2 . TRP H  3 281 ? 39.654  -38.143 63.784   1.00 255.88 ? 279  TRP H CD2 1 
ATOM   22343 N  NE1 . TRP H  3 281 ? 40.495  -36.380 64.883   1.00 260.01 ? 279  TRP H NE1 1 
ATOM   22344 C  CE2 . TRP H  3 281 ? 39.839  -36.747 63.737   1.00 254.57 ? 279  TRP H CE2 1 
ATOM   22345 C  CE3 . TRP H  3 281 ? 39.001  -38.773 62.720   1.00 240.34 ? 279  TRP H CE3 1 
ATOM   22346 C  CZ2 . TRP H  3 281 ? 39.396  -35.971 62.670   1.00 247.98 ? 279  TRP H CZ2 1 
ATOM   22347 C  CZ3 . TRP H  3 281 ? 38.563  -38.002 61.661   1.00 236.90 ? 279  TRP H CZ3 1 
ATOM   22348 C  CH2 . TRP H  3 281 ? 38.762  -36.616 61.643   1.00 242.17 ? 279  TRP H CH2 1 
ATOM   22349 N  N   . LYS H  3 282 ? 40.224  -41.630 68.701   1.00 226.87 ? 280  LYS H N   1 
ATOM   22350 C  CA  . LYS H  3 282 ? 39.959  -42.893 69.372   1.00 231.02 ? 280  LYS H CA  1 
ATOM   22351 C  C   . LYS H  3 282 ? 38.490  -43.291 69.302   1.00 249.30 ? 280  LYS H C   1 
ATOM   22352 O  O   . LYS H  3 282 ? 38.081  -44.235 69.985   1.00 267.07 ? 280  LYS H O   1 
ATOM   22353 C  CB  . LYS H  3 282 ? 40.426  -42.824 70.832   1.00 238.45 ? 280  LYS H CB  1 
ATOM   22354 C  CG  . LYS H  3 282 ? 40.791  -44.176 71.447   1.00 227.80 ? 280  LYS H CG  1 
ATOM   22355 C  CD  . LYS H  3 282 ? 41.461  -44.019 72.805   1.00 230.68 ? 280  LYS H CD  1 
ATOM   22356 C  CE  . LYS H  3 282 ? 40.575  -43.270 73.782   1.00 234.54 ? 280  LYS H CE  1 
ATOM   22357 N  NZ  . LYS H  3 282 ? 41.248  -43.100 75.097   1.00 242.96 ? 280  LYS H NZ  1 
ATOM   22358 N  N   . TRP H  3 283 ? 37.688  -42.601 68.493   1.00 252.08 ? 281  TRP H N   1 
ATOM   22359 C  CA  . TRP H  3 283 ? 36.268  -42.909 68.375   1.00 258.11 ? 281  TRP H CA  1 
ATOM   22360 C  C   . TRP H  3 283 ? 35.962  -43.865 67.230   1.00 260.77 ? 281  TRP H C   1 
ATOM   22361 O  O   . TRP H  3 283 ? 34.790  -44.196 67.015   1.00 263.02 ? 281  TRP H O   1 
ATOM   22362 C  CB  . TRP H  3 283 ? 35.454  -41.620 68.206   1.00 254.72 ? 281  TRP H CB  1 
ATOM   22363 C  CG  . TRP H  3 283 ? 35.817  -40.831 66.990   1.00 257.42 ? 281  TRP H CG  1 
ATOM   22364 C  CD1 . TRP H  3 283 ? 36.870  -39.976 66.856   1.00 265.16 ? 281  TRP H CD1 1 
ATOM   22365 C  CD2 . TRP H  3 283 ? 35.124  -40.817 65.734   1.00 263.43 ? 281  TRP H CD2 1 
ATOM   22366 N  NE1 . TRP H  3 283 ? 36.880  -39.432 65.594   1.00 283.31 ? 281  TRP H NE1 1 
ATOM   22367 C  CE2 . TRP H  3 283 ? 35.819  -39.932 64.885   1.00 273.77 ? 281  TRP H CE2 1 
ATOM   22368 C  CE3 . TRP H  3 283 ? 33.986  -41.467 65.244   1.00 252.33 ? 281  TRP H CE3 1 
ATOM   22369 C  CZ2 . TRP H  3 283 ? 35.414  -39.680 63.576   1.00 259.33 ? 281  TRP H CZ2 1 
ATOM   22370 C  CZ3 . TRP H  3 283 ? 33.586  -41.215 63.943   1.00 242.83 ? 281  TRP H CZ3 1 
ATOM   22371 C  CH2 . TRP H  3 283 ? 34.298  -40.330 63.125   1.00 246.32 ? 281  TRP H CH2 1 
ATOM   22372 N  N   . ILE H  3 284 ? 36.976  -44.319 66.501   1.00 263.31 ? 282  ILE H N   1 
ATOM   22373 C  CA  . ILE H  3 284 ? 36.811  -45.268 65.404   1.00 259.44 ? 282  ILE H CA  1 
ATOM   22374 C  C   . ILE H  3 284 ? 37.510  -46.561 65.807   1.00 263.99 ? 282  ILE H C   1 
ATOM   22375 O  O   . ILE H  3 284 ? 38.736  -46.591 65.972   1.00 268.54 ? 282  ILE H O   1 
ATOM   22376 C  CB  . ILE H  3 284 ? 37.365  -44.715 64.085   1.00 251.09 ? 282  ILE H CB  1 
ATOM   22377 C  CG1 . ILE H  3 284 ? 36.597  -43.456 63.676   1.00 245.40 ? 282  ILE H CG1 1 
ATOM   22378 C  CG2 . ILE H  3 284 ? 37.292  -45.768 62.991   1.00 246.58 ? 282  ILE H CG2 1 
ATOM   22379 C  CD1 . ILE H  3 284 ? 37.107  -42.806 62.410   1.00 245.73 ? 282  ILE H CD1 1 
ATOM   22380 N  N   . HIS H  3 285 ? 36.729  -47.634 65.964   1.00 262.40 ? 283  HIS H N   1 
ATOM   22381 C  CA  . HIS H  3 285 ? 37.275  -48.911 66.415   1.00 261.82 ? 283  HIS H CA  1 
ATOM   22382 C  C   . HIS H  3 285 ? 37.962  -49.662 65.279   1.00 261.76 ? 283  HIS H C   1 
ATOM   22383 O  O   . HIS H  3 285 ? 39.122  -50.069 65.406   1.00 262.88 ? 283  HIS H O   1 
ATOM   22384 C  CB  . HIS H  3 285 ? 36.167  -49.772 67.027   1.00 257.81 ? 283  HIS H CB  1 
ATOM   22385 C  CG  . HIS H  3 285 ? 35.587  -49.210 68.286   1.00 255.41 ? 283  HIS H CG  1 
ATOM   22386 N  ND1 . HIS H  3 285 ? 35.057  -47.940 68.359   1.00 251.64 ? 283  HIS H ND1 1 
ATOM   22387 C  CD2 . HIS H  3 285 ? 35.449  -49.748 69.521   1.00 257.11 ? 283  HIS H CD2 1 
ATOM   22388 C  CE1 . HIS H  3 285 ? 34.621  -47.718 69.586   1.00 257.75 ? 283  HIS H CE1 1 
ATOM   22389 N  NE2 . HIS H  3 285 ? 34.847  -48.799 70.310   1.00 263.60 ? 283  HIS H NE2 1 
ATOM   22390 N  N   . GLU H  3 286 ? 37.256  -49.868 64.170   1.00 258.83 ? 284  GLU H N   1 
ATOM   22391 C  CA  . GLU H  3 286 ? 37.804  -50.590 63.025   1.00 251.93 ? 284  GLU H CA  1 
ATOM   22392 C  C   . GLU H  3 286 ? 37.542  -49.835 61.723   1.00 242.67 ? 284  GLU H C   1 
ATOM   22393 O  O   . GLU H  3 286 ? 36.443  -49.324 61.513   1.00 244.29 ? 284  GLU H O   1 
ATOM   22394 C  CB  . GLU H  3 286 ? 37.208  -52.000 62.944   1.00 248.26 ? 284  GLU H CB  1 
ATOM   22395 C  CG  . GLU H  3 286 ? 37.505  -52.882 64.150   1.00 253.31 ? 284  GLU H CG  1 
ATOM   22396 C  CD  . GLU H  3 286 ? 38.967  -53.285 64.240   1.00 251.01 ? 284  GLU H CD  1 
ATOM   22397 O  OE1 . GLU H  3 286 ? 39.654  -53.280 63.197   1.00 240.10 ? 284  GLU H OE1 1 
ATOM   22398 O  OE2 . GLU H  3 286 ? 39.429  -53.608 65.356   1.00 253.96 ? 284  GLU H OE2 1 
ATOM   22399 N  N   . PRO H  3 287 ? 38.558  -49.755 60.846   1.00 234.36 ? 285  PRO H N   1 
ATOM   22400 C  CA  . PRO H  3 287 ? 39.900  -50.303 61.060   1.00 234.86 ? 285  PRO H CA  1 
ATOM   22401 C  C   . PRO H  3 287 ? 40.791  -49.363 61.863   1.00 244.58 ? 285  PRO H C   1 
ATOM   22402 O  O   . PRO H  3 287 ? 40.350  -48.279 62.245   1.00 244.76 ? 285  PRO H O   1 
ATOM   22403 C  CB  . PRO H  3 287 ? 40.430  -50.465 59.637   1.00 232.47 ? 285  PRO H CB  1 
ATOM   22404 C  CG  . PRO H  3 287 ? 39.808  -49.329 58.906   1.00 231.86 ? 285  PRO H CG  1 
ATOM   22405 C  CD  . PRO H  3 287 ? 38.430  -49.146 59.510   1.00 231.39 ? 285  PRO H CD  1 
ATOM   22406 N  N   . LYS H  3 288 ? 42.034  -49.780 62.113   1.00 252.23 ? 286  LYS H N   1 
ATOM   22407 C  CA  . LYS H  3 288 ? 42.990  -49.003 62.889   1.00 252.89 ? 286  LYS H CA  1 
ATOM   22408 C  C   . LYS H  3 288 ? 44.149  -48.503 62.030   1.00 249.61 ? 286  LYS H C   1 
ATOM   22409 O  O   . LYS H  3 288 ? 45.240  -48.237 62.543   1.00 253.28 ? 286  LYS H O   1 
ATOM   22410 C  CB  . LYS H  3 288 ? 43.507  -49.823 64.071   1.00 243.99 ? 286  LYS H CB  1 
ATOM   22411 C  CG  . LYS H  3 288 ? 42.413  -50.304 65.022   1.00 228.41 ? 286  LYS H CG  1 
ATOM   22412 C  CD  . LYS H  3 288 ? 42.949  -51.289 66.048   1.00 226.40 ? 286  LYS H CD  1 
ATOM   22413 C  CE  . LYS H  3 288 ? 41.826  -51.846 66.912   1.00 227.78 ? 286  LYS H CE  1 
ATOM   22414 N  NZ  . LYS H  3 288 ? 42.302  -52.882 67.870   1.00 227.35 ? 286  LYS H NZ  1 
ATOM   22415 N  N   . GLY H  3 289 ? 43.936  -48.378 60.734   1.00 232.00 ? 287  GLY H N   1 
ATOM   22416 C  CA  . GLY H  3 289 ? 44.943  -47.839 59.840   1.00 231.24 ? 287  GLY H CA  1 
ATOM   22417 C  C   . GLY H  3 289 ? 44.790  -48.397 58.437   1.00 231.00 ? 287  GLY H C   1 
ATOM   22418 O  O   . GLY H  3 289 ? 44.361  -49.526 58.211   1.00 229.35 ? 287  GLY H O   1 
ATOM   22419 N  N   . TYR H  3 290 ? 45.154  -47.575 57.456   1.00 242.15 ? 288  TYR H N   1 
ATOM   22420 C  CA  . TYR H  3 290 ? 45.119  -47.978 56.057   1.00 243.51 ? 288  TYR H CA  1 
ATOM   22421 C  C   . TYR H  3 290 ? 46.121  -47.125 55.289   1.00 242.15 ? 288  TYR H C   1 
ATOM   22422 O  O   . TYR H  3 290 ? 46.686  -46.166 55.821   1.00 243.84 ? 288  TYR H O   1 
ATOM   22423 C  CB  . TYR H  3 290 ? 43.706  -47.857 55.472   1.00 240.19 ? 288  TYR H CB  1 
ATOM   22424 C  CG  . TYR H  3 290 ? 43.296  -46.446 55.110   1.00 243.93 ? 288  TYR H CG  1 
ATOM   22425 C  CD1 . TYR H  3 290 ? 43.078  -45.486 56.091   1.00 252.07 ? 288  TYR H CD1 1 
ATOM   22426 C  CD2 . TYR H  3 290 ? 43.110  -46.080 53.785   1.00 246.59 ? 288  TYR H CD2 1 
ATOM   22427 C  CE1 . TYR H  3 290 ? 42.697  -44.194 55.755   1.00 258.81 ? 288  TYR H CE1 1 
ATOM   22428 C  CE2 . TYR H  3 290 ? 42.729  -44.799 53.439   1.00 248.92 ? 288  TYR H CE2 1 
ATOM   22429 C  CZ  . TYR H  3 290 ? 42.523  -43.858 54.424   1.00 253.00 ? 288  TYR H CZ  1 
ATOM   22430 O  OH  . TYR H  3 290 ? 42.143  -42.581 54.069   1.00 251.34 ? 288  TYR H OH  1 
ATOM   22431 N  N   . HIS H  3 291 ? 46.333  -47.490 54.025   1.00 241.74 ? 289  HIS H N   1 
ATOM   22432 C  CA  . HIS H  3 291 ? 47.362  -46.882 53.180   1.00 238.24 ? 289  HIS H CA  1 
ATOM   22433 C  C   . HIS H  3 291 ? 46.714  -45.874 52.232   1.00 239.62 ? 289  HIS H C   1 
ATOM   22434 O  O   . HIS H  3 291 ? 46.326  -46.207 51.112   1.00 235.92 ? 289  HIS H O   1 
ATOM   22435 C  CB  . HIS H  3 291 ? 48.118  -47.952 52.401   1.00 232.30 ? 289  HIS H CB  1 
ATOM   22436 C  CG  . HIS H  3 291 ? 48.989  -48.821 53.250   1.00 237.59 ? 289  HIS H CG  1 
ATOM   22437 N  ND1 . HIS H  3 291 ? 50.330  -48.565 53.439   1.00 243.82 ? 289  HIS H ND1 1 
ATOM   22438 C  CD2 . HIS H  3 291 ? 48.718  -49.947 53.952   1.00 235.65 ? 289  HIS H CD2 1 
ATOM   22439 C  CE1 . HIS H  3 291 ? 50.847  -49.493 54.224   1.00 245.94 ? 289  HIS H CE1 1 
ATOM   22440 N  NE2 . HIS H  3 291 ? 49.890  -50.343 54.550   1.00 238.08 ? 289  HIS H NE2 1 
ATOM   22441 N  N   . ALA H  3 292 ? 46.617  -44.622 52.679   1.00 244.23 ? 290  ALA H N   1 
ATOM   22442 C  CA  . ALA H  3 292 ? 46.088  -43.535 51.854   1.00 252.54 ? 290  ALA H CA  1 
ATOM   22443 C  C   . ALA H  3 292 ? 47.251  -42.869 51.123   1.00 262.67 ? 290  ALA H C   1 
ATOM   22444 O  O   . ALA H  3 292 ? 47.934  -42.002 51.675   1.00 280.13 ? 290  ALA H O   1 
ATOM   22445 C  CB  . ALA H  3 292 ? 45.320  -42.535 52.709   1.00 263.88 ? 290  ALA H CB  1 
ATOM   22446 N  N   . ASN H  3 293 ? 47.470  -43.259 49.872   1.00 255.89 ? 291  ASN H N   1 
ATOM   22447 C  CA  . ASN H  3 293 ? 48.601  -42.750 49.106   1.00 258.95 ? 291  ASN H CA  1 
ATOM   22448 C  C   . ASN H  3 293 ? 48.289  -41.354 48.566   1.00 248.69 ? 291  ASN H C   1 
ATOM   22449 O  O   . ASN H  3 293 ? 47.281  -40.731 48.914   1.00 247.21 ? 291  ASN H O   1 
ATOM   22450 C  CB  . ASN H  3 293 ? 48.960  -43.721 47.988   1.00 262.18 ? 291  ASN H CB  1 
ATOM   22451 C  CG  . ASN H  3 293 ? 49.446  -45.053 48.517   1.00 269.78 ? 291  ASN H CG  1 
ATOM   22452 O  OD1 . ASN H  3 293 ? 49.795  -45.174 49.692   1.00 276.37 ? 291  ASN H OD1 1 
ATOM   22453 N  ND2 . ASN H  3 293 ? 49.480  -46.060 47.653   1.00 266.90 ? 291  ASN H ND2 1 
ATOM   22454 N  N   . PHE H  3 294 ? 49.166  -40.842 47.703   1.00 237.72 ? 292  PHE H N   1 
ATOM   22455 C  CA  . PHE H  3 294 ? 48.969  -39.532 47.095   1.00 236.98 ? 292  PHE H CA  1 
ATOM   22456 C  C   . PHE H  3 294 ? 49.733  -39.482 45.776   1.00 241.74 ? 292  PHE H C   1 
ATOM   22457 O  O   . PHE H  3 294 ? 50.570  -40.340 45.485   1.00 236.86 ? 292  PHE H O   1 
ATOM   22458 C  CB  . PHE H  3 294 ? 49.411  -38.405 48.036   1.00 234.16 ? 292  PHE H CB  1 
ATOM   22459 C  CG  . PHE H  3 294 ? 50.874  -38.433 48.373   1.00 237.50 ? 292  PHE H CG  1 
ATOM   22460 C  CD1 . PHE H  3 294 ? 51.345  -39.230 49.402   1.00 245.81 ? 292  PHE H CD1 1 
ATOM   22461 C  CD2 . PHE H  3 294 ? 51.778  -37.657 47.665   1.00 237.38 ? 292  PHE H CD2 1 
ATOM   22462 C  CE1 . PHE H  3 294 ? 52.689  -39.260 49.714   1.00 258.19 ? 292  PHE H CE1 1 
ATOM   22463 C  CE2 . PHE H  3 294 ? 53.124  -37.682 47.971   1.00 242.52 ? 292  PHE H CE2 1 
ATOM   22464 C  CZ  . PHE H  3 294 ? 53.581  -38.483 48.998   1.00 253.65 ? 292  PHE H CZ  1 
ATOM   22465 N  N   . CYS H  3 295 ? 49.431  -38.457 44.979   1.00 239.47 ? 293  CYS H N   1 
ATOM   22466 C  CA  . CYS H  3 295 ? 50.063  -38.246 43.682   1.00 224.05 ? 293  CYS H CA  1 
ATOM   22467 C  C   . CYS H  3 295 ? 51.003  -37.051 43.771   1.00 225.69 ? 293  CYS H C   1 
ATOM   22468 O  O   . CYS H  3 295 ? 50.575  -35.942 44.110   1.00 229.26 ? 293  CYS H O   1 
ATOM   22469 C  CB  . CYS H  3 295 ? 49.022  -38.018 42.587   1.00 208.60 ? 293  CYS H CB  1 
ATOM   22470 S  SG  . CYS H  3 295 ? 47.821  -39.348 42.374   1.00 203.86 ? 293  CYS H SG  1 
ATOM   22471 N  N   . LEU H  3 296 ? 52.275  -37.276 43.455   1.00 215.66 ? 294  LEU H N   1 
ATOM   22472 C  CA  . LEU H  3 296 ? 53.286  -36.229 43.490   1.00 213.01 ? 294  LEU H CA  1 
ATOM   22473 C  C   . LEU H  3 296 ? 54.102  -36.293 42.209   1.00 211.48 ? 294  LEU H C   1 
ATOM   22474 O  O   . LEU H  3 296 ? 54.634  -37.351 41.860   1.00 218.57 ? 294  LEU H O   1 
ATOM   22475 C  CB  . LEU H  3 296 ? 54.190  -36.381 44.720   1.00 216.84 ? 294  LEU H CB  1 
ATOM   22476 C  CG  . LEU H  3 296 ? 54.955  -35.153 45.222   1.00 214.80 ? 294  LEU H CG  1 
ATOM   22477 C  CD1 . LEU H  3 296 ? 56.221  -34.905 44.414   1.00 213.34 ? 294  LEU H CD1 1 
ATOM   22478 C  CD2 . LEU H  3 296 ? 54.051  -33.933 45.197   1.00 216.87 ? 294  LEU H CD2 1 
ATOM   22479 N  N   . GLY H  3 297 ? 54.199  -35.166 41.515   1.00 215.00 ? 295  GLY H N   1 
ATOM   22480 C  CA  . GLY H  3 297 ? 54.962  -35.096 40.294   1.00 215.58 ? 295  GLY H CA  1 
ATOM   22481 C  C   . GLY H  3 297 ? 54.380  -34.094 39.322   1.00 215.56 ? 295  GLY H C   1 
ATOM   22482 O  O   . GLY H  3 297 ? 53.175  -33.828 39.315   1.00 216.94 ? 295  GLY H O   1 
ATOM   22483 N  N   . PRO H  3 298 ? 55.232  -33.509 38.486   1.00 231.82 ? 296  PRO H N   1 
ATOM   22484 C  CA  . PRO H  3 298 ? 54.761  -32.547 37.488   1.00 236.90 ? 296  PRO H CA  1 
ATOM   22485 C  C   . PRO H  3 298 ? 54.316  -33.224 36.197   1.00 242.45 ? 296  PRO H C   1 
ATOM   22486 O  O   . PRO H  3 298 ? 54.715  -34.346 35.872   1.00 247.70 ? 296  PRO H O   1 
ATOM   22487 C  CB  . PRO H  3 298 ? 56.002  -31.676 37.245   1.00 237.15 ? 296  PRO H CB  1 
ATOM   22488 C  CG  . PRO H  3 298 ? 57.140  -32.626 37.442   1.00 241.42 ? 296  PRO H CG  1 
ATOM   22489 C  CD  . PRO H  3 298 ? 56.703  -33.604 38.513   1.00 239.90 ? 296  PRO H CD  1 
ATOM   22490 N  N   . CYS H  3 299 ? 53.461  -32.507 35.463   1.00 238.84 ? 297  CYS H N   1 
ATOM   22491 C  CA  . CYS H  3 299 ? 52.961  -32.944 34.155   1.00 233.55 ? 297  CYS H CA  1 
ATOM   22492 C  C   . CYS H  3 299 ? 52.990  -31.761 33.195   1.00 227.97 ? 297  CYS H C   1 
ATOM   22493 O  O   . CYS H  3 299 ? 51.988  -31.058 33.019   1.00 230.32 ? 297  CYS H O   1 
ATOM   22494 C  CB  . CYS H  3 299 ? 51.534  -33.500 34.250   1.00 227.82 ? 297  CYS H CB  1 
ATOM   22495 S  SG  . CYS H  3 299 ? 51.143  -34.811 35.468   1.00 222.20 ? 297  CYS H SG  1 
ATOM   22496 N  N   . PRO H  3 300 ? 54.131  -31.506 32.547   1.00 221.17 ? 298  PRO H N   1 
ATOM   22497 C  CA  . PRO H  3 300 ? 54.185  -30.400 31.581   1.00 216.70 ? 298  PRO H CA  1 
ATOM   22498 C  C   . PRO H  3 300 ? 54.043  -30.873 30.144   1.00 207.51 ? 298  PRO H C   1 
ATOM   22499 O  O   . PRO H  3 300 ? 53.932  -32.078 29.893   1.00 202.65 ? 298  PRO H O   1 
ATOM   22500 C  CB  . PRO H  3 300 ? 55.565  -29.788 31.840   1.00 230.42 ? 298  PRO H CB  1 
ATOM   22501 C  CG  . PRO H  3 300 ? 56.393  -30.931 32.444   1.00 234.34 ? 298  PRO H CG  1 
ATOM   22502 C  CD  . PRO H  3 300 ? 55.463  -32.087 32.765   1.00 228.53 ? 298  PRO H CD  1 
ATOM   22503 N  N   . TYR H  3 301 ? 54.048  -29.941 29.191   1.00 201.24 ? 299  TYR H N   1 
ATOM   22504 C  CA  . TYR H  3 301 ? 53.909  -30.322 27.794   1.00 200.79 ? 299  TYR H CA  1 
ATOM   22505 C  C   . TYR H  3 301 ? 54.571  -29.283 26.898   1.00 195.14 ? 299  TYR H C   1 
ATOM   22506 O  O   . TYR H  3 301 ? 54.827  -28.148 27.312   1.00 196.95 ? 299  TYR H O   1 
ATOM   22507 C  CB  . TYR H  3 301 ? 52.434  -30.516 27.417   1.00 209.42 ? 299  TYR H CB  1 
ATOM   22508 C  CG  . TYR H  3 301 ? 51.683  -29.256 27.041   1.00 218.23 ? 299  TYR H CG  1 
ATOM   22509 C  CD1 . TYR H  3 301 ? 51.811  -28.082 27.779   1.00 205.45 ? 299  TYR H CD1 1 
ATOM   22510 C  CD2 . TYR H  3 301 ? 50.832  -29.250 25.946   1.00 224.85 ? 299  TYR H CD2 1 
ATOM   22511 C  CE1 . TYR H  3 301 ? 51.123  -26.941 27.420   1.00 204.75 ? 299  TYR H CE1 1 
ATOM   22512 C  CE2 . TYR H  3 301 ? 50.142  -28.117 25.583   1.00 213.01 ? 299  TYR H CE2 1 
ATOM   22513 C  CZ  . TYR H  3 301 ? 50.287  -26.969 26.321   1.00 205.18 ? 299  TYR H CZ  1 
ATOM   22514 O  OH  . TYR H  3 301 ? 49.589  -25.850 25.944   1.00 211.11 ? 299  TYR H OH  1 
ATOM   22515 N  N   . ILE H  3 302 ? 54.833  -29.695 25.654   1.00 199.63 ? 300  ILE H N   1 
ATOM   22516 C  CA  . ILE H  3 302 ? 55.473  -28.872 24.628   1.00 213.31 ? 300  ILE H CA  1 
ATOM   22517 C  C   . ILE H  3 302 ? 56.723  -28.211 25.202   1.00 223.20 ? 300  ILE H C   1 
ATOM   22518 O  O   . ILE H  3 302 ? 56.781  -26.985 25.362   1.00 209.77 ? 300  ILE H O   1 
ATOM   22519 C  CB  . ILE H  3 302 ? 54.492  -27.836 24.050   1.00 207.81 ? 300  ILE H CB  1 
ATOM   22520 C  CG1 . ILE H  3 302 ? 53.197  -28.527 23.635   1.00 195.06 ? 300  ILE H CG1 1 
ATOM   22521 C  CG2 . ILE H  3 302 ? 55.080  -27.158 22.821   1.00 214.26 ? 300  ILE H CG2 1 
ATOM   22522 C  CD1 . ILE H  3 302 ? 53.405  -29.649 22.646   1.00 182.87 ? 300  ILE H CD1 1 
ATOM   22523 N  N   . TRP H  3 303 ? 57.720  -29.028 25.529   1.00 244.61 ? 301  TRP H N   1 
ATOM   22524 C  CA  . TRP H  3 303 ? 58.993  -28.572 26.065   1.00 241.59 ? 301  TRP H CA  1 
ATOM   22525 C  C   . TRP H  3 303 ? 60.027  -28.504 24.946   1.00 236.96 ? 301  TRP H C   1 
ATOM   22526 O  O   . TRP H  3 303 ? 59.895  -29.161 23.910   1.00 235.33 ? 301  TRP H O   1 
ATOM   22527 C  CB  . TRP H  3 303 ? 59.474  -29.504 27.184   1.00 231.31 ? 301  TRP H CB  1 
ATOM   22528 C  CG  . TRP H  3 303 ? 60.247  -28.803 28.264   1.00 234.40 ? 301  TRP H CG  1 
ATOM   22529 C  CD1 . TRP H  3 303 ? 61.601  -28.812 28.444   1.00 237.53 ? 301  TRP H CD1 1 
ATOM   22530 C  CD2 . TRP H  3 303 ? 59.709  -27.980 29.310   1.00 239.33 ? 301  TRP H CD2 1 
ATOM   22531 N  NE1 . TRP H  3 303 ? 61.938  -28.050 29.538   1.00 244.88 ? 301  TRP H NE1 1 
ATOM   22532 C  CE2 . TRP H  3 303 ? 60.795  -27.528 30.086   1.00 244.81 ? 301  TRP H CE2 1 
ATOM   22533 C  CE3 . TRP H  3 303 ? 58.414  -27.583 29.665   1.00 231.52 ? 301  TRP H CE3 1 
ATOM   22534 C  CZ2 . TRP H  3 303 ? 60.627  -26.699 31.194   1.00 246.54 ? 301  TRP H CZ2 1 
ATOM   22535 C  CZ3 . TRP H  3 303 ? 58.250  -26.760 30.767   1.00 234.23 ? 301  TRP H CZ3 1 
ATOM   22536 C  CH2 . TRP H  3 303 ? 59.351  -26.327 31.517   1.00 242.13 ? 301  TRP H CH2 1 
ATOM   22537 N  N   . SER H  3 304 ? 61.060  -27.690 25.166   1.00 235.69 ? 302  SER H N   1 
ATOM   22538 C  CA  . SER H  3 304 ? 62.095  -27.506 24.158   1.00 230.55 ? 302  SER H CA  1 
ATOM   22539 C  C   . SER H  3 304 ? 62.763  -28.841 23.827   1.00 229.70 ? 302  SER H C   1 
ATOM   22540 O  O   . SER H  3 304 ? 62.685  -29.809 24.589   1.00 222.85 ? 302  SER H O   1 
ATOM   22541 C  CB  . SER H  3 304 ? 63.138  -26.492 24.638   1.00 237.15 ? 302  SER H CB  1 
ATOM   22542 O  OG  . SER H  3 304 ? 62.557  -25.210 24.809   1.00 233.48 ? 302  SER H OG  1 
ATOM   22543 N  N   . LEU H  3 305 ? 63.398  -28.883 22.648   1.00 229.14 ? 303  LEU H N   1 
ATOM   22544 C  CA  . LEU H  3 305 ? 64.075  -30.059 22.096   1.00 227.40 ? 303  LEU H CA  1 
ATOM   22545 C  C   . LEU H  3 305 ? 63.076  -31.103 21.606   1.00 211.23 ? 303  LEU H C   1 
ATOM   22546 O  O   . LEU H  3 305 ? 63.198  -31.603 20.482   1.00 205.44 ? 303  LEU H O   1 
ATOM   22547 C  CB  . LEU H  3 305 ? 65.036  -30.689 23.117   1.00 232.55 ? 303  LEU H CB  1 
ATOM   22548 C  CG  . LEU H  3 305 ? 66.154  -29.818 23.706   1.00 228.92 ? 303  LEU H CG  1 
ATOM   22549 C  CD1 . LEU H  3 305 ? 66.798  -30.486 24.922   1.00 214.43 ? 303  LEU H CD1 1 
ATOM   22550 C  CD2 . LEU H  3 305 ? 67.208  -29.488 22.656   1.00 234.24 ? 303  LEU H CD2 1 
ATOM   22551 N  N   . ASP H  3 306 ? 62.093  -31.433 22.438   1.00 218.73 ? 304  ASP H N   1 
ATOM   22552 C  CA  . ASP H  3 306 ? 61.091  -32.444 22.117   1.00 213.57 ? 304  ASP H CA  1 
ATOM   22553 C  C   . ASP H  3 306 ? 61.741  -33.780 21.772   1.00 216.44 ? 304  ASP H C   1 
ATOM   22554 O  O   . ASP H  3 306 ? 62.660  -34.228 22.459   1.00 216.94 ? 304  ASP H O   1 
ATOM   22555 C  CB  . ASP H  3 306 ? 60.195  -31.973 20.973   1.00 209.30 ? 304  ASP H CB  1 
ATOM   22556 N  N   . VAL H  3 312 ? 57.823  -33.258 24.663   1.00 231.51 ? 310  VAL H N   1 
ATOM   22557 C  CA  . VAL H  3 312 ? 58.432  -34.174 23.708   1.00 222.88 ? 310  VAL H CA  1 
ATOM   22558 C  C   . VAL H  3 312 ? 57.364  -34.935 22.942   1.00 200.92 ? 310  VAL H C   1 
ATOM   22559 O  O   . VAL H  3 312 ? 56.274  -35.177 23.454   1.00 183.43 ? 310  VAL H O   1 
ATOM   22560 C  CB  . VAL H  3 312 ? 59.397  -35.163 24.402   1.00 230.68 ? 310  VAL H CB  1 
ATOM   22561 C  CG1 . VAL H  3 312 ? 60.499  -34.419 25.138   1.00 237.61 ? 310  VAL H CG1 1 
ATOM   22562 C  CG2 . VAL H  3 312 ? 58.637  -36.070 25.356   1.00 225.85 ? 310  VAL H CG2 1 
ATOM   22563 N  N   . LEU H  3 313 ? 57.678  -35.306 21.708   1.00 209.49 ? 311  LEU H N   1 
ATOM   22564 C  CA  . LEU H  3 313 ? 56.837  -36.212 20.944   1.00 204.66 ? 311  LEU H CA  1 
ATOM   22565 C  C   . LEU H  3 313 ? 57.182  -37.665 21.226   1.00 187.89 ? 311  LEU H C   1 
ATOM   22566 O  O   . LEU H  3 313 ? 56.484  -38.565 20.749   1.00 181.23 ? 311  LEU H O   1 
ATOM   22567 C  CB  . LEU H  3 313 ? 56.961  -35.906 19.446   1.00 215.48 ? 311  LEU H CB  1 
ATOM   22568 C  CG  . LEU H  3 313 ? 55.857  -36.388 18.501   1.00 199.20 ? 311  LEU H CG  1 
ATOM   22569 C  CD1 . LEU H  3 313 ? 54.492  -35.897 18.964   1.00 178.56 ? 311  LEU H CD1 1 
ATOM   22570 C  CD2 . LEU H  3 313 ? 56.136  -35.933 17.072   1.00 193.63 ? 311  LEU H CD2 1 
ATOM   22571 N  N   . ALA H  3 314 ? 58.243  -37.908 21.994   1.00 187.80 ? 312  ALA H N   1 
ATOM   22572 C  CA  . ALA H  3 314 ? 58.594  -39.269 22.393   1.00 196.00 ? 312  ALA H CA  1 
ATOM   22573 C  C   . ALA H  3 314 ? 57.709  -39.725 23.550   1.00 209.32 ? 312  ALA H C   1 
ATOM   22574 O  O   . ALA H  3 314 ? 56.803  -40.546 23.371   1.00 195.43 ? 312  ALA H O   1 
ATOM   22575 C  CB  . ALA H  3 314 ? 60.082  -39.338 22.758   1.00 189.69 ? 312  ALA H CB  1 
ATOM   22576 N  N   . LEU H  3 315 ? 57.948  -39.181 24.745   1.00 219.64 ? 313  LEU H N   1 
ATOM   22577 C  CA  . LEU H  3 315 ? 57.164  -39.520 25.932   1.00 206.28 ? 313  LEU H CA  1 
ATOM   22578 C  C   . LEU H  3 315 ? 55.898  -38.669 25.941   1.00 205.63 ? 313  LEU H C   1 
ATOM   22579 O  O   . LEU H  3 315 ? 55.803  -37.626 26.592   1.00 199.21 ? 313  LEU H O   1 
ATOM   22580 C  CB  . LEU H  3 315 ? 57.982  -39.308 27.198   1.00 198.90 ? 313  LEU H CB  1 
ATOM   22581 C  CG  . LEU H  3 315 ? 59.201  -40.213 27.368   1.00 199.69 ? 313  LEU H CG  1 
ATOM   22582 C  CD1 . LEU H  3 315 ? 59.937  -39.860 28.646   1.00 208.02 ? 313  LEU H CD1 1 
ATOM   22583 C  CD2 . LEU H  3 315 ? 58.793  -41.681 27.362   1.00 196.23 ? 313  LEU H CD2 1 
ATOM   22584 N  N   . TYR H  3 316 ? 54.902  -39.125 25.188   1.00 203.75 ? 314  TYR H N   1 
ATOM   22585 C  CA  . TYR H  3 316 ? 53.603  -38.478 25.170   1.00 189.95 ? 314  TYR H CA  1 
ATOM   22586 C  C   . TYR H  3 316 ? 52.522  -39.310 25.843   1.00 185.05 ? 314  TYR H C   1 
ATOM   22587 O  O   . TYR H  3 316 ? 51.434  -38.789 26.105   1.00 183.64 ? 314  TYR H O   1 
ATOM   22588 C  CB  . TYR H  3 316 ? 53.191  -38.159 23.724   1.00 195.57 ? 314  TYR H CB  1 
ATOM   22589 C  CG  . TYR H  3 316 ? 52.557  -36.792 23.572   1.00 213.96 ? 314  TYR H CG  1 
ATOM   22590 C  CD1 . TYR H  3 316 ? 51.185  -36.619 23.721   1.00 227.39 ? 314  TYR H CD1 1 
ATOM   22591 C  CD2 . TYR H  3 316 ? 53.328  -35.673 23.287   1.00 215.92 ? 314  TYR H CD2 1 
ATOM   22592 C  CE1 . TYR H  3 316 ? 50.599  -35.365 23.587   1.00 225.03 ? 314  TYR H CE1 1 
ATOM   22593 C  CE2 . TYR H  3 316 ? 52.753  -34.415 23.151   1.00 223.49 ? 314  TYR H CE2 1 
ATOM   22594 C  CZ  . TYR H  3 316 ? 51.387  -34.267 23.303   1.00 219.81 ? 314  TYR H CZ  1 
ATOM   22595 O  OH  . TYR H  3 316 ? 50.809  -33.022 23.171   1.00 195.67 ? 314  TYR H OH  1 
ATOM   22596 N  N   . ASN H  3 317 ? 52.798  -40.576 26.145   1.00 184.07 ? 315  ASN H N   1 
ATOM   22597 C  CA  . ASN H  3 317 ? 51.801  -41.450 26.745   1.00 180.37 ? 315  ASN H CA  1 
ATOM   22598 C  C   . ASN H  3 317 ? 51.665  -41.246 28.245   1.00 184.27 ? 315  ASN H C   1 
ATOM   22599 O  O   . ASN H  3 317 ? 50.636  -41.622 28.815   1.00 185.13 ? 315  ASN H O   1 
ATOM   22600 C  CB  . ASN H  3 317 ? 52.153  -42.908 26.451   1.00 196.77 ? 315  ASN H CB  1 
ATOM   22601 C  CG  . ASN H  3 317 ? 53.646  -43.158 26.465   1.00 221.13 ? 315  ASN H CG  1 
ATOM   22602 O  OD1 . ASN H  3 317 ? 54.408  -42.404 27.071   1.00 230.06 ? 315  ASN H OD1 1 
ATOM   22603 N  ND2 . ASN H  3 317 ? 54.076  -44.216 25.786   1.00 229.12 ? 315  ASN H ND2 1 
ATOM   22604 N  N   . GLN H  3 318 ? 52.673  -40.675 28.894   1.00 189.80 ? 316  GLN H N   1 
ATOM   22605 C  CA  . GLN H  3 318 ? 52.613  -40.384 30.317   1.00 201.15 ? 316  GLN H CA  1 
ATOM   22606 C  C   . GLN H  3 318 ? 52.615  -38.897 30.633   1.00 217.69 ? 316  GLN H C   1 
ATOM   22607 O  O   . GLN H  3 318 ? 52.042  -38.500 31.651   1.00 217.29 ? 316  GLN H O   1 
ATOM   22608 C  CB  . GLN H  3 318 ? 53.792  -41.044 31.055   1.00 196.67 ? 316  GLN H CB  1 
ATOM   22609 C  CG  . GLN H  3 318 ? 53.761  -42.566 31.065   1.00 191.25 ? 316  GLN H CG  1 
ATOM   22610 C  CD  . GLN H  3 318 ? 54.701  -43.163 32.097   1.00 195.05 ? 316  GLN H CD  1 
ATOM   22611 O  OE1 . GLN H  3 318 ? 55.271  -42.450 32.923   1.00 201.17 ? 316  GLN H OE1 1 
ATOM   22612 N  NE2 . GLN H  3 318 ? 54.863  -44.480 32.057   1.00 198.64 ? 316  GLN H NE2 1 
ATOM   22613 N  N   . HIS H  3 319 ? 53.230  -38.068 29.788   1.00 226.44 ? 317  HIS H N   1 
ATOM   22614 C  CA  . HIS H  3 319 ? 53.335  -36.645 30.087   1.00 231.25 ? 317  HIS H CA  1 
ATOM   22615 C  C   . HIS H  3 319 ? 51.983  -35.953 29.957   1.00 226.30 ? 317  HIS H C   1 
ATOM   22616 O  O   . HIS H  3 319 ? 51.580  -35.183 30.837   1.00 237.22 ? 317  HIS H O   1 
ATOM   22617 C  CB  . HIS H  3 319 ? 54.379  -35.995 29.175   1.00 224.44 ? 317  HIS H CB  1 
ATOM   22618 C  CG  . HIS H  3 319 ? 55.782  -36.458 29.430   1.00 238.49 ? 317  HIS H CG  1 
ATOM   22619 N  ND1 . HIS H  3 319 ? 56.085  -37.498 30.284   1.00 253.24 ? 317  HIS H ND1 1 
ATOM   22620 C  CD2 . HIS H  3 319 ? 56.966  -36.016 28.945   1.00 240.94 ? 317  HIS H CD2 1 
ATOM   22621 C  CE1 . HIS H  3 319 ? 57.394  -37.677 30.314   1.00 250.24 ? 317  HIS H CE1 1 
ATOM   22622 N  NE2 . HIS H  3 319 ? 57.952  -36.791 29.509   1.00 247.80 ? 317  HIS H NE2 1 
ATOM   22623 N  N   . ASN H  3 320 ? 51.254  -36.228 28.879   1.00 201.02 ? 318  ASN H N   1 
ATOM   22624 C  CA  . ASN H  3 320 ? 49.962  -35.584 28.632   1.00 185.30 ? 318  ASN H CA  1 
ATOM   22625 C  C   . ASN H  3 320 ? 49.164  -36.438 27.658   1.00 190.77 ? 318  ASN H C   1 
ATOM   22626 O  O   . ASN H  3 320 ? 49.040  -36.112 26.472   1.00 200.53 ? 318  ASN H O   1 
ATOM   22627 C  CB  . ASN H  3 320 ? 50.153  -34.166 28.082   1.00 173.74 ? 318  ASN H CB  1 
ATOM   22628 C  CG  . ASN H  3 320 ? 48.846  -33.401 27.951   1.00 167.76 ? 318  ASN H CG  1 
ATOM   22629 O  OD1 . ASN H  3 320 ? 47.837  -33.757 28.557   1.00 164.74 ? 318  ASN H OD1 1 
ATOM   22630 N  ND2 . ASN H  3 320 ? 48.869  -32.324 27.175   1.00 167.83 ? 318  ASN H ND2 1 
ATOM   22631 N  N   . PRO H  3 321 ? 48.598  -37.555 28.131   1.00 196.54 ? 319  PRO H N   1 
ATOM   22632 C  CA  . PRO H  3 321 ? 47.751  -38.386 27.260   1.00 185.67 ? 319  PRO H CA  1 
ATOM   22633 C  C   . PRO H  3 321 ? 46.347  -37.843 27.071   1.00 178.03 ? 319  PRO H C   1 
ATOM   22634 O  O   . PRO H  3 321 ? 45.610  -38.353 26.214   1.00 179.21 ? 319  PRO H O   1 
ATOM   22635 C  CB  . PRO H  3 321 ? 47.709  -39.725 28.001   1.00 187.91 ? 319  PRO H CB  1 
ATOM   22636 C  CG  . PRO H  3 321 ? 47.780  -39.320 29.437   1.00 193.41 ? 319  PRO H CG  1 
ATOM   22637 C  CD  . PRO H  3 321 ? 48.717  -38.131 29.481   1.00 201.14 ? 319  PRO H CD  1 
ATOM   22638 N  N   . GLY H  3 322 ? 45.952  -36.844 27.852   1.00 170.45 ? 320  GLY H N   1 
ATOM   22639 C  CA  . GLY H  3 322 ? 44.654  -36.223 27.692   1.00 171.31 ? 320  GLY H CA  1 
ATOM   22640 C  C   . GLY H  3 322 ? 44.684  -35.021 26.773   1.00 159.38 ? 320  GLY H C   1 
ATOM   22641 O  O   . GLY H  3 322 ? 43.635  -34.549 26.323   1.00 154.10 ? 320  GLY H O   1 
ATOM   22642 N  N   . ALA H  3 323 ? 45.891  -34.526 26.487   1.00 162.46 ? 321  ALA H N   1 
ATOM   22643 C  CA  . ALA H  3 323 ? 46.101  -33.344 25.651   1.00 166.57 ? 321  ALA H CA  1 
ATOM   22644 C  C   . ALA H  3 323 ? 45.377  -32.125 26.206   1.00 174.16 ? 321  ALA H C   1 
ATOM   22645 O  O   . ALA H  3 323 ? 44.897  -31.273 25.455   1.00 178.52 ? 321  ALA H O   1 
ATOM   22646 C  CB  . ALA H  3 323 ? 45.682  -33.596 24.201   1.00 180.64 ? 321  ALA H CB  1 
ATOM   22647 N  N   . SER H  3 324 ? 45.293  -32.029 27.527   1.00 184.60 ? 322  SER H N   1 
ATOM   22648 C  CA  . SER H  3 324 ? 44.605  -30.907 28.133   1.00 183.89 ? 322  SER H CA  1 
ATOM   22649 C  C   . SER H  3 324 ? 45.527  -29.690 28.172   1.00 183.53 ? 322  SER H C   1 
ATOM   22650 O  O   . SER H  3 324 ? 46.752  -29.795 28.041   1.00 182.96 ? 322  SER H O   1 
ATOM   22651 C  CB  . SER H  3 324 ? 44.119  -31.273 29.537   1.00 177.45 ? 322  SER H CB  1 
ATOM   22652 O  OG  . SER H  3 324 ? 43.098  -30.397 29.986   1.00 175.52 ? 322  SER H OG  1 
ATOM   22653 N  N   . ALA H  3 325 ? 44.913  -28.516 28.335   1.00 182.65 ? 323  ALA H N   1 
ATOM   22654 C  CA  . ALA H  3 325 ? 45.683  -27.282 28.416   1.00 178.97 ? 323  ALA H CA  1 
ATOM   22655 C  C   . ALA H  3 325 ? 46.604  -27.271 29.630   1.00 199.01 ? 323  ALA H C   1 
ATOM   22656 O  O   . ALA H  3 325 ? 47.676  -26.655 29.593   1.00 197.85 ? 323  ALA H O   1 
ATOM   22657 C  CB  . ALA H  3 325 ? 44.733  -26.083 28.450   1.00 178.21 ? 323  ALA H CB  1 
ATOM   22658 N  N   . ALA H  3 326 ? 46.213  -27.954 30.710   1.00 213.49 ? 324  ALA H N   1 
ATOM   22659 C  CA  . ALA H  3 326 ? 46.999  -28.007 31.941   1.00 202.11 ? 324  ALA H CA  1 
ATOM   22660 C  C   . ALA H  3 326 ? 46.891  -29.398 32.555   1.00 181.17 ? 324  ALA H C   1 
ATOM   22661 O  O   . ALA H  3 326 ? 45.946  -29.676 33.310   1.00 178.92 ? 324  ALA H O   1 
ATOM   22662 C  CB  . ALA H  3 326 ? 46.540  -26.946 32.938   1.00 210.08 ? 324  ALA H CB  1 
ATOM   22663 N  N   . PRO H  3 327 ? 47.835  -30.293 32.262   1.00 187.43 ? 325  PRO H N   1 
ATOM   22664 C  CA  . PRO H  3 327 ? 47.776  -31.646 32.832   1.00 188.78 ? 325  PRO H CA  1 
ATOM   22665 C  C   . PRO H  3 327 ? 48.157  -31.642 34.308   1.00 194.56 ? 325  PRO H C   1 
ATOM   22666 O  O   . PRO H  3 327 ? 49.160  -31.044 34.705   1.00 207.94 ? 325  PRO H O   1 
ATOM   22667 C  CB  . PRO H  3 327 ? 48.793  -32.428 31.989   1.00 197.10 ? 325  PRO H CB  1 
ATOM   22668 C  CG  . PRO H  3 327 ? 49.007  -31.595 30.761   1.00 186.44 ? 325  PRO H CG  1 
ATOM   22669 C  CD  . PRO H  3 327 ? 48.883  -30.185 31.236   1.00 185.93 ? 325  PRO H CD  1 
ATOM   22670 N  N   . CYS H  3 328 ? 47.347  -32.317 35.116   1.00 187.05 ? 326  CYS H N   1 
ATOM   22671 C  CA  . CYS H  3 328 ? 47.599  -32.464 36.540   1.00 193.83 ? 326  CYS H CA  1 
ATOM   22672 C  C   . CYS H  3 328 ? 47.803  -33.929 36.897   1.00 199.67 ? 326  CYS H C   1 
ATOM   22673 O  O   . CYS H  3 328 ? 47.187  -34.821 36.308   1.00 205.39 ? 326  CYS H O   1 
ATOM   22674 C  CB  . CYS H  3 328 ? 46.445  -31.917 37.377   1.00 197.45 ? 326  CYS H CB  1 
ATOM   22675 S  SG  . CYS H  3 328 ? 46.149  -30.161 37.245   1.00 206.39 ? 326  CYS H SG  1 
ATOM   22676 N  N   . CYS H  3 329 ? 48.655  -34.163 37.896   1.00 201.18 ? 327  CYS H N   1 
ATOM   22677 C  CA  . CYS H  3 329 ? 48.951  -35.504 38.398   1.00 207.08 ? 327  CYS H CA  1 
ATOM   22678 C  C   . CYS H  3 329 ? 47.825  -35.909 39.348   1.00 198.68 ? 327  CYS H C   1 
ATOM   22679 O  O   . CYS H  3 329 ? 47.910  -35.772 40.571   1.00 204.79 ? 327  CYS H O   1 
ATOM   22680 C  CB  . CYS H  3 329 ? 50.319  -35.511 39.073   1.00 222.19 ? 327  CYS H CB  1 
ATOM   22681 S  SG  . CYS H  3 329 ? 51.011  -37.100 39.613   1.00 233.34 ? 327  CYS H SG  1 
ATOM   22682 N  N   . VAL H  3 330 ? 46.740  -36.410 38.763   1.00 192.48 ? 328  VAL H N   1 
ATOM   22683 C  CA  . VAL H  3 330 ? 45.518  -36.710 39.510   1.00 192.90 ? 328  VAL H CA  1 
ATOM   22684 C  C   . VAL H  3 330 ? 45.316  -38.218 39.617   1.00 189.53 ? 328  VAL H C   1 
ATOM   22685 O  O   . VAL H  3 330 ? 45.805  -38.969 38.760   1.00 188.17 ? 328  VAL H O   1 
ATOM   22686 C  CB  . VAL H  3 330 ? 44.300  -36.040 38.856   1.00 202.38 ? 328  VAL H CB  1 
ATOM   22687 C  CG1 . VAL H  3 330 ? 44.444  -34.528 38.903   1.00 209.87 ? 328  VAL H CG1 1 
ATOM   22688 C  CG2 . VAL H  3 330 ? 44.142  -36.517 37.420   1.00 197.83 ? 328  VAL H CG2 1 
ATOM   22689 N  N   . PRO H  3 331 ? 44.614  -38.705 40.641   1.00 190.28 ? 329  PRO H N   1 
ATOM   22690 C  CA  . PRO H  3 331 ? 44.348  -40.145 40.725   1.00 184.86 ? 329  PRO H CA  1 
ATOM   22691 C  C   . PRO H  3 331 ? 43.342  -40.588 39.677   1.00 184.57 ? 329  PRO H C   1 
ATOM   22692 O  O   . PRO H  3 331 ? 42.340  -39.913 39.423   1.00 178.84 ? 329  PRO H O   1 
ATOM   22693 C  CB  . PRO H  3 331 ? 43.786  -40.320 42.141   1.00 191.08 ? 329  PRO H CB  1 
ATOM   22694 C  CG  . PRO H  3 331 ? 43.200  -38.998 42.470   1.00 196.66 ? 329  PRO H CG  1 
ATOM   22695 C  CD  . PRO H  3 331 ? 44.108  -37.987 41.823   1.00 198.34 ? 329  PRO H CD  1 
ATOM   22696 N  N   . GLN H  3 332 ? 43.620  -41.741 39.069   1.00 186.66 ? 330  GLN H N   1 
ATOM   22697 C  CA  . GLN H  3 332 ? 42.731  -42.331 38.074   1.00 189.69 ? 330  GLN H CA  1 
ATOM   22698 C  C   . GLN H  3 332 ? 41.808  -43.388 38.661   1.00 178.02 ? 330  GLN H C   1 
ATOM   22699 O  O   . GLN H  3 332 ? 40.607  -43.386 38.368   1.00 188.75 ? 330  GLN H O   1 
ATOM   22700 C  CB  . GLN H  3 332 ? 43.544  -42.944 36.925   1.00 193.95 ? 330  GLN H CB  1 
ATOM   22701 C  CG  . GLN H  3 332 ? 42.693  -43.436 35.754   1.00 193.43 ? 330  GLN H CG  1 
ATOM   22702 C  CD  . GLN H  3 332 ? 43.519  -43.936 34.578   1.00 174.09 ? 330  GLN H CD  1 
ATOM   22703 O  OE1 . GLN H  3 332 ? 44.748  -43.981 34.639   1.00 179.19 ? 330  GLN H OE1 1 
ATOM   22704 N  NE2 . GLN H  3 332 ? 42.841  -44.313 33.496   1.00 153.52 ? 330  GLN H NE2 1 
ATOM   22705 N  N   . ALA H  3 333 ? 42.332  -44.286 39.491   1.00 155.67 ? 331  ALA H N   1 
ATOM   22706 C  CA  . ALA H  3 333 ? 41.552  -45.368 40.073   1.00 153.98 ? 331  ALA H CA  1 
ATOM   22707 C  C   . ALA H  3 333 ? 41.547  -45.236 41.588   1.00 177.63 ? 331  ALA H C   1 
ATOM   22708 O  O   . ALA H  3 333 ? 42.608  -45.097 42.205   1.00 203.58 ? 331  ALA H O   1 
ATOM   22709 C  CB  . ALA H  3 333 ? 42.116  -46.730 39.660   1.00 150.58 ? 331  ALA H CB  1 
ATOM   22710 N  N   . LEU H  3 334 ? 40.355  -45.283 42.185   1.00 178.14 ? 332  LEU H N   1 
ATOM   22711 C  CA  . LEU H  3 334 ? 40.195  -45.174 43.629   1.00 174.83 ? 332  LEU H CA  1 
ATOM   22712 C  C   . LEU H  3 334 ? 39.374  -46.347 44.155   1.00 180.16 ? 332  LEU H C   1 
ATOM   22713 O  O   . LEU H  3 334 ? 38.609  -46.977 43.420   1.00 178.92 ? 332  LEU H O   1 
ATOM   22714 C  CB  . LEU H  3 334 ? 39.531  -43.847 44.027   1.00 178.01 ? 332  LEU H CB  1 
ATOM   22715 C  CG  . LEU H  3 334 ? 40.356  -42.568 43.853   1.00 184.05 ? 332  LEU H CG  1 
ATOM   22716 C  CD1 . LEU H  3 334 ? 40.327  -42.051 42.417   1.00 175.95 ? 332  LEU H CD1 1 
ATOM   22717 C  CD2 . LEU H  3 334 ? 39.882  -41.498 44.824   1.00 195.10 ? 332  LEU H CD2 1 
ATOM   22718 N  N   . GLU H  3 335 ? 39.538  -46.632 45.450   1.00 202.49 ? 333  GLU H N   1 
ATOM   22719 C  CA  . GLU H  3 335 ? 38.871  -47.754 46.098   1.00 209.24 ? 333  GLU H CA  1 
ATOM   22720 C  C   . GLU H  3 335 ? 38.156  -47.300 47.365   1.00 220.88 ? 333  GLU H C   1 
ATOM   22721 O  O   . GLU H  3 335 ? 38.701  -46.500 48.136   1.00 225.62 ? 333  GLU H O   1 
ATOM   22722 C  CB  . GLU H  3 335 ? 39.879  -48.862 46.442   1.00 206.49 ? 333  GLU H CB  1 
ATOM   22723 C  CG  . GLU H  3 335 ? 40.554  -49.473 45.224   1.00 210.31 ? 333  GLU H CG  1 
ATOM   22724 C  CD  . GLU H  3 335 ? 41.509  -50.595 45.580   1.00 216.28 ? 333  GLU H CD  1 
ATOM   22725 O  OE1 . GLU H  3 335 ? 41.533  -51.011 46.757   1.00 211.42 ? 333  GLU H OE1 1 
ATOM   22726 O  OE2 . GLU H  3 335 ? 42.240  -51.062 44.680   1.00 224.98 ? 333  GLU H OE2 1 
ATOM   22727 N  N   . PRO H  3 336 ? 36.943  -47.795 47.610   1.00 223.42 ? 334  PRO H N   1 
ATOM   22728 C  CA  . PRO H  3 336 ? 36.196  -47.383 48.806   1.00 214.01 ? 334  PRO H CA  1 
ATOM   22729 C  C   . PRO H  3 336 ? 36.765  -48.025 50.063   1.00 217.19 ? 334  PRO H C   1 
ATOM   22730 O  O   . PRO H  3 336 ? 37.566  -48.961 50.018   1.00 220.02 ? 334  PRO H O   1 
ATOM   22731 C  CB  . PRO H  3 336 ? 34.775  -47.876 48.521   1.00 213.55 ? 334  PRO H CB  1 
ATOM   22732 C  CG  . PRO H  3 336 ? 34.970  -49.058 47.634   1.00 221.80 ? 334  PRO H CG  1 
ATOM   22733 C  CD  . PRO H  3 336 ? 36.179  -48.745 46.781   1.00 229.87 ? 334  PRO H CD  1 
ATOM   22734 N  N   . LEU H  3 337 ? 36.325  -47.506 51.209   1.00 218.59 ? 335  LEU H N   1 
ATOM   22735 C  CA  . LEU H  3 337 ? 36.824  -47.949 52.508   1.00 229.95 ? 335  LEU H CA  1 
ATOM   22736 C  C   . LEU H  3 337 ? 35.664  -48.157 53.472   1.00 233.95 ? 335  LEU H C   1 
ATOM   22737 O  O   . LEU H  3 337 ? 34.926  -47.193 53.768   1.00 239.45 ? 335  LEU H O   1 
ATOM   22738 C  CB  . LEU H  3 337 ? 37.819  -46.937 53.081   1.00 233.05 ? 335  LEU H CB  1 
ATOM   22739 C  CG  . LEU H  3 337 ? 38.309  -47.258 54.494   1.00 230.88 ? 335  LEU H CG  1 
ATOM   22740 C  CD1 . LEU H  3 337 ? 39.050  -48.586 54.511   1.00 229.71 ? 335  LEU H CD1 1 
ATOM   22741 C  CD2 . LEU H  3 337 ? 39.188  -46.145 55.037   1.00 235.27 ? 335  LEU H CD2 1 
ATOM   22742 N  N   . PRO H  3 338 ? 35.460  -49.368 53.990   1.00 231.33 ? 336  PRO H N   1 
ATOM   22743 C  CA  . PRO H  3 338 ? 34.438  -49.569 55.022   1.00 232.60 ? 336  PRO H CA  1 
ATOM   22744 C  C   . PRO H  3 338 ? 34.957  -49.174 56.398   1.00 243.11 ? 336  PRO H C   1 
ATOM   22745 O  O   . PRO H  3 338 ? 36.137  -49.346 56.714   1.00 249.04 ? 336  PRO H O   1 
ATOM   22746 C  CB  . PRO H  3 338 ? 34.153  -51.073 54.943   1.00 230.64 ? 336  PRO H CB  1 
ATOM   22747 C  CG  . PRO H  3 338 ? 35.440  -51.662 54.467   1.00 228.54 ? 336  PRO H CG  1 
ATOM   22748 C  CD  . PRO H  3 338 ? 36.068  -50.637 53.553   1.00 227.97 ? 336  PRO H CD  1 
ATOM   22749 N  N   . ILE H  3 339 ? 34.055  -48.632 57.222   1.00 246.89 ? 337  ILE H N   1 
ATOM   22750 C  CA  . ILE H  3 339 ? 34.399  -48.137 58.550   1.00 253.37 ? 337  ILE H CA  1 
ATOM   22751 C  C   . ILE H  3 339 ? 33.389  -48.654 59.568   1.00 261.87 ? 337  ILE H C   1 
ATOM   22752 O  O   . ILE H  3 339 ? 32.276  -49.059 59.227   1.00 259.92 ? 337  ILE H O   1 
ATOM   22753 C  CB  . ILE H  3 339 ? 34.462  -46.594 58.601   1.00 253.73 ? 337  ILE H CB  1 
ATOM   22754 C  CG1 . ILE H  3 339 ? 33.093  -45.989 58.276   1.00 247.37 ? 337  ILE H CG1 1 
ATOM   22755 C  CG2 . ILE H  3 339 ? 35.524  -46.072 57.643   1.00 257.03 ? 337  ILE H CG2 1 
ATOM   22756 C  CD1 . ILE H  3 339 ? 33.043  -44.476 58.393   1.00 247.19 ? 337  ILE H CD1 1 
ATOM   22757 N  N   . VAL H  3 340 ? 33.797  -48.627 60.838   1.00 267.11 ? 338  VAL H N   1 
ATOM   22758 C  CA  . VAL H  3 340 ? 32.960  -49.056 61.955   1.00 252.44 ? 338  VAL H CA  1 
ATOM   22759 C  C   . VAL H  3 340 ? 33.104  -48.032 63.074   1.00 242.66 ? 338  VAL H C   1 
ATOM   22760 O  O   . VAL H  3 340 ? 34.209  -47.823 63.589   1.00 242.75 ? 338  VAL H O   1 
ATOM   22761 C  CB  . VAL H  3 340 ? 33.334  -50.462 62.460   1.00 244.26 ? 338  VAL H CB  1 
ATOM   22762 C  CG1 . VAL H  3 340 ? 32.576  -50.788 63.736   1.00 243.80 ? 338  VAL H CG1 1 
ATOM   22763 C  CG2 . VAL H  3 340 ? 33.053  -51.506 61.388   1.00 243.69 ? 338  VAL H CG2 1 
ATOM   22764 N  N   . TYR H  3 341 ? 31.997  -47.394 63.450   1.00 243.76 ? 339  TYR H N   1 
ATOM   22765 C  CA  . TYR H  3 341 ? 32.000  -46.406 64.519   1.00 253.35 ? 339  TYR H CA  1 
ATOM   22766 C  C   . TYR H  3 341 ? 30.717  -46.536 65.329   1.00 263.62 ? 339  TYR H C   1 
ATOM   22767 O  O   . TYR H  3 341 ? 29.727  -47.117 64.877   1.00 258.93 ? 339  TYR H O   1 
ATOM   22768 C  CB  . TYR H  3 341 ? 32.145  -44.976 63.974   1.00 258.57 ? 339  TYR H CB  1 
ATOM   22769 C  CG  . TYR H  3 341 ? 30.938  -44.482 63.210   1.00 258.29 ? 339  TYR H CG  1 
ATOM   22770 C  CD1 . TYR H  3 341 ? 30.737  -44.841 61.883   1.00 247.30 ? 339  TYR H CD1 1 
ATOM   22771 C  CD2 . TYR H  3 341 ? 29.999  -43.651 63.812   1.00 265.22 ? 339  TYR H CD2 1 
ATOM   22772 C  CE1 . TYR H  3 341 ? 29.637  -44.393 61.180   1.00 242.99 ? 339  TYR H CE1 1 
ATOM   22773 C  CE2 . TYR H  3 341 ? 28.895  -43.198 63.115   1.00 263.61 ? 339  TYR H CE2 1 
ATOM   22774 C  CZ  . TYR H  3 341 ? 28.719  -43.573 61.800   1.00 251.76 ? 339  TYR H CZ  1 
ATOM   22775 O  OH  . TYR H  3 341 ? 27.621  -43.125 61.102   1.00 248.94 ? 339  TYR H OH  1 
ATOM   22776 N  N   . TYR H  3 342 ? 30.743  -45.981 66.537   1.00 263.15 ? 340  TYR H N   1 
ATOM   22777 C  CA  . TYR H  3 342 ? 29.603  -46.016 67.440   1.00 257.31 ? 340  TYR H CA  1 
ATOM   22778 C  C   . TYR H  3 342 ? 28.931  -44.650 67.516   1.00 249.96 ? 340  TYR H C   1 
ATOM   22779 O  O   . TYR H  3 342 ? 29.530  -43.614 67.211   1.00 242.49 ? 340  TYR H O   1 
ATOM   22780 C  CB  . TYR H  3 342 ? 30.028  -46.466 68.843   1.00 266.66 ? 340  TYR H CB  1 
ATOM   22781 C  CG  . TYR H  3 342 ? 30.187  -47.965 69.009   1.00 266.30 ? 340  TYR H CG  1 
ATOM   22782 C  CD1 . TYR H  3 342 ? 29.102  -48.764 69.352   1.00 263.15 ? 340  TYR H CD1 1 
ATOM   22783 C  CD2 . TYR H  3 342 ? 31.423  -48.577 68.842   1.00 269.00 ? 340  TYR H CD2 1 
ATOM   22784 C  CE1 . TYR H  3 342 ? 29.242  -50.129 69.514   1.00 261.46 ? 340  TYR H CE1 1 
ATOM   22785 C  CE2 . TYR H  3 342 ? 31.571  -49.943 69.002   1.00 267.44 ? 340  TYR H CE2 1 
ATOM   22786 C  CZ  . TYR H  3 342 ? 30.477  -50.713 69.338   1.00 264.99 ? 340  TYR H CZ  1 
ATOM   22787 O  OH  . TYR H  3 342 ? 30.616  -52.073 69.500   1.00 266.81 ? 340  TYR H OH  1 
ATOM   22788 N  N   . VAL H  3 343 ? 27.666  -44.663 67.930   1.00 241.92 ? 341  VAL H N   1 
ATOM   22789 C  CA  . VAL H  3 343 ? 26.891  -43.439 68.118   1.00 243.63 ? 341  VAL H CA  1 
ATOM   22790 C  C   . VAL H  3 343 ? 26.238  -43.430 69.497   1.00 255.06 ? 341  VAL H C   1 
ATOM   22791 O  O   . VAL H  3 343 ? 26.745  -42.818 70.438   1.00 247.76 ? 341  VAL H O   1 
ATOM   22792 C  CB  . VAL H  3 343 ? 25.822  -43.275 67.022   1.00 225.06 ? 341  VAL H CB  1 
ATOM   22793 C  CG1 . VAL H  3 343 ? 25.053  -41.985 67.230   1.00 226.50 ? 341  VAL H CG1 1 
ATOM   22794 C  CG2 . VAL H  3 343 ? 26.455  -43.298 65.646   1.00 223.30 ? 341  VAL H CG2 1 
ATOM   22795 N  N   . ARG H  3 345 ? 23.726  -45.525 70.968   1.00 229.63 ? 343  ARG H N   1 
ATOM   22796 C  CA  . ARG H  3 345 ? 23.721  -46.930 71.359   1.00 231.49 ? 343  ARG H CA  1 
ATOM   22797 C  C   . ARG H  3 345 ? 23.721  -47.847 70.142   1.00 231.34 ? 343  ARG H C   1 
ATOM   22798 O  O   . ARG H  3 345 ? 23.810  -49.068 70.275   1.00 234.50 ? 343  ARG H O   1 
ATOM   22799 C  CB  . ARG H  3 345 ? 22.508  -47.239 72.240   1.00 232.43 ? 343  ARG H CB  1 
ATOM   22800 C  CG  . ARG H  3 345 ? 21.164  -46.994 71.564   1.00 234.76 ? 343  ARG H CG  1 
ATOM   22801 C  CD  . ARG H  3 345 ? 20.001  -47.302 72.501   1.00 243.45 ? 343  ARG H CD  1 
ATOM   22802 N  NE  . ARG H  3 345 ? 20.082  -46.549 73.751   1.00 248.71 ? 343  ARG H NE  1 
ATOM   22803 C  CZ  . ARG H  3 345 ? 19.529  -45.356 73.944   1.00 256.07 ? 343  ARG H CZ  1 
ATOM   22804 N  NH1 . ARG H  3 345 ? 18.851  -44.770 72.966   1.00 254.71 ? 343  ARG H NH1 1 
ATOM   22805 N  NH2 . ARG H  3 345 ? 19.654  -44.747 75.116   1.00 269.15 ? 343  ARG H NH2 1 
ATOM   22806 N  N   . LYS H  3 346 ? 23.628  -47.250 68.956   1.00 231.82 ? 344  LYS H N   1 
ATOM   22807 C  CA  . LYS H  3 346 ? 23.472  -48.006 67.717   1.00 228.92 ? 344  LYS H CA  1 
ATOM   22808 C  C   . LYS H  3 346 ? 24.769  -48.000 66.918   1.00 236.17 ? 344  LYS H C   1 
ATOM   22809 O  O   . LYS H  3 346 ? 25.167  -46.942 66.402   1.00 228.34 ? 344  LYS H O   1 
ATOM   22810 C  CB  . LYS H  3 346 ? 22.326  -47.428 66.883   1.00 223.42 ? 344  LYS H CB  1 
ATOM   22811 C  CG  . LYS H  3 346 ? 21.003  -47.312 67.646   1.00 235.60 ? 344  LYS H CG  1 
ATOM   22812 C  CD  . LYS H  3 346 ? 19.862  -46.797 66.771   1.00 243.34 ? 344  LYS H CD  1 
ATOM   22813 C  CE  . LYS H  3 346 ? 18.618  -46.481 67.604   1.00 248.30 ? 344  LYS H CE  1 
ATOM   22814 N  NZ  . LYS H  3 346 ? 18.075  -47.675 68.316   1.00 241.58 ? 344  LYS H NZ  1 
ATOM   22815 N  N   . PRO H  3 347 ? 25.458  -49.137 66.788   1.00 245.05 ? 345  PRO H N   1 
ATOM   22816 C  CA  . PRO H  3 347 ? 26.659  -49.190 65.943   1.00 235.62 ? 345  PRO H CA  1 
ATOM   22817 C  C   . PRO H  3 347 ? 26.278  -49.245 64.470   1.00 238.03 ? 345  PRO H C   1 
ATOM   22818 O  O   . PRO H  3 347 ? 25.469  -50.077 64.052   1.00 238.23 ? 345  PRO H O   1 
ATOM   22819 C  CB  . PRO H  3 347 ? 27.352  -50.483 66.391   1.00 229.49 ? 345  PRO H CB  1 
ATOM   22820 C  CG  . PRO H  3 347 ? 26.235  -51.347 66.881   1.00 234.08 ? 345  PRO H CG  1 
ATOM   22821 C  CD  . PRO H  3 347 ? 25.204  -50.416 67.476   1.00 246.87 ? 345  PRO H CD  1 
ATOM   22822 N  N   . LYS H  3 348 ? 26.867  -48.352 63.681   1.00 250.53 ? 346  LYS H N   1 
ATOM   22823 C  CA  . LYS H  3 348 ? 26.540  -48.216 62.268   1.00 246.28 ? 346  LYS H CA  1 
ATOM   22824 C  C   . LYS H  3 348 ? 27.765  -48.551 61.432   1.00 240.10 ? 346  LYS H C   1 
ATOM   22825 O  O   . LYS H  3 348 ? 28.822  -47.933 61.596   1.00 240.22 ? 346  LYS H O   1 
ATOM   22826 C  CB  . LYS H  3 348 ? 26.036  -46.806 61.957   1.00 246.47 ? 346  LYS H CB  1 
ATOM   22827 C  CG  . LYS H  3 348 ? 24.754  -46.446 62.690   1.00 244.10 ? 346  LYS H CG  1 
ATOM   22828 C  CD  . LYS H  3 348 ? 24.216  -45.097 62.247   1.00 239.85 ? 346  LYS H CD  1 
ATOM   22829 C  CE  . LYS H  3 348 ? 22.914  -44.762 62.964   1.00 236.55 ? 346  LYS H CE  1 
ATOM   22830 N  NZ  . LYS H  3 348 ? 21.854  -45.795 62.763   1.00 230.02 ? 346  LYS H NZ  1 
ATOM   22831 N  N   . VAL H  3 349 ? 27.620  -49.527 60.541   1.00 229.18 ? 347  VAL H N   1 
ATOM   22832 C  CA  . VAL H  3 349 ? 28.687  -49.919 59.627   1.00 235.06 ? 347  VAL H CA  1 
ATOM   22833 C  C   . VAL H  3 349 ? 28.466  -49.171 58.317   1.00 230.89 ? 347  VAL H C   1 
ATOM   22834 O  O   . VAL H  3 349 ? 27.475  -49.403 57.621   1.00 229.46 ? 347  VAL H O   1 
ATOM   22835 C  CB  . VAL H  3 349 ? 28.712  -51.435 59.409   1.00 243.34 ? 347  VAL H CB  1 
ATOM   22836 C  CG1 . VAL H  3 349 ? 29.879  -51.818 58.517   1.00 238.11 ? 347  VAL H CG1 1 
ATOM   22837 C  CG2 . VAL H  3 349 ? 28.789  -52.162 60.741   1.00 252.19 ? 347  VAL H CG2 1 
ATOM   22838 N  N   . GLU H  3 350 ? 29.389  -48.273 57.980   1.00 230.70 ? 348  GLU H N   1 
ATOM   22839 C  CA  . GLU H  3 350 ? 29.289  -47.448 56.786   1.00 226.46 ? 348  GLU H CA  1 
ATOM   22840 C  C   . GLU H  3 350 ? 30.526  -47.629 55.916   1.00 227.76 ? 348  GLU H C   1 
ATOM   22841 O  O   . GLU H  3 350 ? 31.575  -48.090 56.375   1.00 234.47 ? 348  GLU H O   1 
ATOM   22842 C  CB  . GLU H  3 350 ? 29.119  -45.964 57.139   1.00 234.59 ? 348  GLU H CB  1 
ATOM   22843 C  CG  . GLU H  3 350 ? 27.905  -45.663 58.006   1.00 240.05 ? 348  GLU H CG  1 
ATOM   22844 C  CD  . GLU H  3 350 ? 27.628  -44.175 58.139   1.00 242.21 ? 348  GLU H CD  1 
ATOM   22845 O  OE1 . GLU H  3 350 ? 26.584  -43.817 58.724   1.00 243.77 ? 348  GLU H OE1 1 
ATOM   22846 O  OE2 . GLU H  3 350 ? 28.448  -43.365 57.657   1.00 241.17 ? 348  GLU H OE2 1 
ATOM   22847 N  N   . GLN H  3 351 ? 30.395  -47.252 54.646   1.00 216.90 ? 349  GLN H N   1 
ATOM   22848 C  CA  . GLN H  3 351 ? 31.473  -47.392 53.676   1.00 211.96 ? 349  GLN H CA  1 
ATOM   22849 C  C   . GLN H  3 351 ? 31.638  -46.077 52.932   1.00 208.40 ? 349  GLN H C   1 
ATOM   22850 O  O   . GLN H  3 351 ? 30.676  -45.567 52.347   1.00 200.43 ? 349  GLN H O   1 
ATOM   22851 C  CB  . GLN H  3 351 ? 31.189  -48.540 52.703   1.00 208.98 ? 349  GLN H CB  1 
ATOM   22852 C  CG  . GLN H  3 351 ? 32.338  -48.848 51.762   1.00 212.66 ? 349  GLN H CG  1 
ATOM   22853 C  CD  . GLN H  3 351 ? 32.011  -49.958 50.786   1.00 211.31 ? 349  GLN H CD  1 
ATOM   22854 O  OE1 . GLN H  3 351 ? 30.852  -50.346 50.637   1.00 209.23 ? 349  GLN H OE1 1 
ATOM   22855 N  NE2 . GLN H  3 351 ? 33.035  -50.479 50.114   1.00 206.09 ? 349  GLN H NE2 1 
ATOM   22856 N  N   . LEU H  3 352 ? 32.850  -45.527 52.964   1.00 215.31 ? 350  LEU H N   1 
ATOM   22857 C  CA  . LEU H  3 352 ? 33.157  -44.270 52.296   1.00 217.11 ? 350  LEU H CA  1 
ATOM   22858 C  C   . LEU H  3 352 ? 33.531  -44.513 50.840   1.00 213.86 ? 350  LEU H C   1 
ATOM   22859 O  O   . LEU H  3 352 ? 34.178  -45.510 50.510   1.00 213.40 ? 350  LEU H O   1 
ATOM   22860 C  CB  . LEU H  3 352 ? 34.305  -43.552 53.007   1.00 228.25 ? 350  LEU H CB  1 
ATOM   22861 C  CG  . LEU H  3 352 ? 34.081  -43.161 54.467   1.00 242.11 ? 350  LEU H CG  1 
ATOM   22862 C  CD1 . LEU H  3 352 ? 35.307  -42.447 55.011   1.00 246.18 ? 350  LEU H CD1 1 
ATOM   22863 C  CD2 . LEU H  3 352 ? 32.844  -42.291 54.607   1.00 251.29 ? 350  LEU H CD2 1 
ATOM   22864 N  N   . SER H  3 353 ? 33.137  -43.586 49.974   1.00 217.84 ? 351  SER H N   1 
ATOM   22865 C  CA  . SER H  3 353 ? 33.394  -43.690 48.544   1.00 212.61 ? 351  SER H CA  1 
ATOM   22866 C  C   . SER H  3 353 ? 34.633  -42.883 48.176   1.00 225.49 ? 351  SER H C   1 
ATOM   22867 O  O   . SER H  3 353 ? 34.772  -41.728 48.594   1.00 230.86 ? 351  SER H O   1 
ATOM   22868 C  CB  . SER H  3 353 ? 32.189  -43.205 47.737   1.00 200.91 ? 351  SER H CB  1 
ATOM   22869 O  OG  . SER H  3 353 ? 31.849  -41.870 48.070   1.00 198.90 ? 351  SER H OG  1 
ATOM   22870 N  N   . ASN H  3 354 ? 35.526  -43.498 47.397   1.00 228.21 ? 352  ASN H N   1 
ATOM   22871 C  CA  . ASN H  3 354 ? 36.733  -42.849 46.891   1.00 224.05 ? 352  ASN H CA  1 
ATOM   22872 C  C   . ASN H  3 354 ? 37.641  -42.364 48.018   1.00 227.12 ? 352  ASN H C   1 
ATOM   22873 O  O   . ASN H  3 354 ? 37.546  -41.210 48.446   1.00 239.15 ? 352  ASN H O   1 
ATOM   22874 C  CB  . ASN H  3 354 ? 36.367  -41.681 45.970   1.00 213.85 ? 352  ASN H CB  1 
ATOM   22875 C  CG  . ASN H  3 354 ? 35.632  -42.130 44.723   1.00 214.37 ? 352  ASN H CG  1 
ATOM   22876 O  OD1 . ASN H  3 354 ? 36.251  -42.491 43.723   1.00 212.66 ? 352  ASN H OD1 1 
ATOM   22877 N  ND2 . ASN H  3 354 ? 34.306  -42.109 44.776   1.00 221.59 ? 352  ASN H ND2 1 
ATOM   22878 N  N   . MET H  3 355 ? 38.534  -43.233 48.496   1.00 215.09 ? 353  MET H N   1 
ATOM   22879 C  CA  . MET H  3 355 ? 39.461  -42.866 49.561   1.00 213.25 ? 353  MET H CA  1 
ATOM   22880 C  C   . MET H  3 355 ? 40.884  -43.310 49.245   1.00 211.42 ? 353  MET H C   1 
ATOM   22881 O  O   . MET H  3 355 ? 41.833  -42.532 49.395   1.00 213.57 ? 353  MET H O   1 
ATOM   22882 C  CB  . MET H  3 355 ? 39.011  -43.470 50.893   1.00 216.91 ? 353  MET H CB  1 
ATOM   22883 C  CG  . MET H  3 355 ? 37.688  -42.931 51.406   1.00 218.58 ? 353  MET H CG  1 
ATOM   22884 S  SD  . MET H  3 355 ? 37.740  -41.151 51.698   1.00 213.01 ? 353  MET H SD  1 
ATOM   22885 C  CE  . MET H  3 355 ? 39.039  -41.047 52.924   1.00 216.91 ? 353  MET H CE  1 
ATOM   22886 N  N   . ILE H  3 356 ? 41.040  -44.559 48.813   1.00 207.37 ? 354  ILE H N   1 
ATOM   22887 C  CA  . ILE H  3 356 ? 42.350  -45.147 48.544   1.00 207.96 ? 354  ILE H CA  1 
ATOM   22888 C  C   . ILE H  3 356 ? 42.762  -44.814 47.116   1.00 219.01 ? 354  ILE H C   1 
ATOM   22889 O  O   . ILE H  3 356 ? 42.089  -45.208 46.158   1.00 224.29 ? 354  ILE H O   1 
ATOM   22890 C  CB  . ILE H  3 356 ? 42.337  -46.667 48.763   1.00 203.83 ? 354  ILE H CB  1 
ATOM   22891 C  CG1 . ILE H  3 356 ? 42.167  -47.007 50.246   1.00 214.42 ? 354  ILE H CG1 1 
ATOM   22892 C  CG2 . ILE H  3 356 ? 43.608  -47.300 48.205   1.00 201.61 ? 354  ILE H CG2 1 
ATOM   22893 C  CD1 . ILE H  3 356 ? 40.724  -47.142 50.691   1.00 212.81 ? 354  ILE H CD1 1 
ATOM   22894 N  N   . VAL H  3 357 ? 43.881  -44.110 46.974   1.00 218.05 ? 355  VAL H N   1 
ATOM   22895 C  CA  . VAL H  3 357 ? 44.408  -43.734 45.667   1.00 205.28 ? 355  VAL H CA  1 
ATOM   22896 C  C   . VAL H  3 357 ? 45.304  -44.857 45.165   1.00 198.14 ? 355  VAL H C   1 
ATOM   22897 O  O   . VAL H  3 357 ? 46.305  -45.199 45.804   1.00 202.19 ? 355  VAL H O   1 
ATOM   22898 C  CB  . VAL H  3 357 ? 45.177  -42.408 45.740   1.00 217.72 ? 355  VAL H CB  1 
ATOM   22899 C  CG1 . VAL H  3 357 ? 45.910  -42.152 44.434   1.00 211.57 ? 355  VAL H CG1 1 
ATOM   22900 C  CG2 . VAL H  3 357 ? 44.229  -41.265 46.061   1.00 233.00 ? 355  VAL H CG2 1 
ATOM   22901 N  N   . ARG H  3 358 ? 44.954  -45.423 44.015   1.00 204.82 ? 356  ARG H N   1 
ATOM   22902 C  CA  . ARG H  3 358 ? 45.731  -46.523 43.434   1.00 200.03 ? 356  ARG H CA  1 
ATOM   22903 C  C   . ARG H  3 358 ? 46.750  -45.973 42.439   1.00 198.53 ? 356  ARG H C   1 
ATOM   22904 O  O   . ARG H  3 358 ? 47.955  -45.973 42.704   1.00 201.77 ? 356  ARG H O   1 
ATOM   22905 C  CB  . ARG H  3 358 ? 44.792  -47.536 42.779   1.00 193.95 ? 356  ARG H CB  1 
ATOM   22906 C  CG  . ARG H  3 358 ? 45.485  -48.771 42.240   1.00 204.34 ? 356  ARG H CG  1 
ATOM   22907 C  CD  . ARG H  3 358 ? 46.124  -49.592 43.357   1.00 211.93 ? 356  ARG H CD  1 
ATOM   22908 N  NE  . ARG H  3 358 ? 45.135  -50.211 44.239   1.00 213.66 ? 356  ARG H NE  1 
ATOM   22909 C  CZ  . ARG H  3 358 ? 45.432  -51.065 45.216   1.00 221.74 ? 356  ARG H CZ  1 
ATOM   22910 N  NH1 . ARG H  3 358 ? 46.693  -51.412 45.444   1.00 220.46 ? 356  ARG H NH1 1 
ATOM   22911 N  NH2 . ARG H  3 358 ? 44.468  -51.578 45.967   1.00 223.52 ? 356  ARG H NH2 1 
ATOM   22912 N  N   . SER H  3 359 ? 46.272  -45.494 41.296   1.00 189.71 ? 357  SER H N   1 
ATOM   22913 C  CA  . SER H  3 359 ? 47.123  -44.984 40.233   1.00 190.58 ? 357  SER H CA  1 
ATOM   22914 C  C   . SER H  3 359 ? 46.989  -43.470 40.122   1.00 202.34 ? 357  SER H C   1 
ATOM   22915 O  O   . SER H  3 359 ? 46.097  -42.852 40.708   1.00 207.59 ? 357  SER H O   1 
ATOM   22916 C  CB  . SER H  3 359 ? 46.771  -45.649 38.898   1.00 188.65 ? 357  SER H CB  1 
ATOM   22917 O  OG  . SER H  3 359 ? 47.617  -45.187 37.860   1.00 190.79 ? 357  SER H OG  1 
ATOM   22918 N  N   . CYS H  3 360 ? 47.898  -42.875 39.348   1.00 205.06 ? 358  CYS H N   1 
ATOM   22919 C  CA  . CYS H  3 360 ? 47.900  -41.442 39.090   1.00 199.38 ? 358  CYS H CA  1 
ATOM   22920 C  C   . CYS H  3 360 ? 48.110  -41.202 37.602   1.00 188.58 ? 358  CYS H C   1 
ATOM   22921 O  O   . CYS H  3 360 ? 48.945  -41.856 36.973   1.00 186.40 ? 358  CYS H O   1 
ATOM   22922 C  CB  . CYS H  3 360 ? 48.993  -40.721 39.897   1.00 214.09 ? 358  CYS H CB  1 
ATOM   22923 S  SG  . CYS H  3 360 ? 48.913  -40.929 41.704   1.00 215.68 ? 358  CYS H SG  1 
ATOM   22924 N  N   . LYS H  3 361 ? 47.350  -40.261 37.046   1.00 193.73 ? 359  LYS H N   1 
ATOM   22925 C  CA  . LYS H  3 361 ? 47.431  -39.908 35.634   1.00 199.01 ? 359  LYS H CA  1 
ATOM   22926 C  C   . LYS H  3 361 ? 47.641  -38.406 35.491   1.00 201.54 ? 359  LYS H C   1 
ATOM   22927 O  O   . LYS H  3 361 ? 47.571  -37.649 36.463   1.00 203.51 ? 359  LYS H O   1 
ATOM   22928 C  CB  . LYS H  3 361 ? 46.164  -40.327 34.874   1.00 195.01 ? 359  LYS H CB  1 
ATOM   22929 C  CG  . LYS H  3 361 ? 44.890  -39.649 35.384   1.00 203.93 ? 359  LYS H CG  1 
ATOM   22930 C  CD  . LYS H  3 361 ? 43.650  -40.052 34.588   1.00 199.71 ? 359  LYS H CD  1 
ATOM   22931 C  CE  . LYS H  3 361 ? 42.390  -39.381 35.140   1.00 183.96 ? 359  LYS H CE  1 
ATOM   22932 N  NZ  . LYS H  3 361 ? 41.150  -39.751 34.392   1.00 174.62 ? 359  LYS H NZ  1 
ATOM   22933 N  N   . CYS H  3 362 ? 47.898  -37.978 34.255   1.00 197.93 ? 360  CYS H N   1 
ATOM   22934 C  CA  . CYS H  3 362 ? 47.945  -36.563 33.895   1.00 203.82 ? 360  CYS H CA  1 
ATOM   22935 C  C   . CYS H  3 362 ? 46.846  -36.295 32.874   1.00 208.80 ? 360  CYS H C   1 
ATOM   22936 O  O   . CYS H  3 362 ? 46.900  -36.804 31.749   1.00 221.99 ? 360  CYS H O   1 
ATOM   22937 C  CB  . CYS H  3 362 ? 49.312  -36.160 33.337   1.00 207.22 ? 360  CYS H CB  1 
ATOM   22938 S  SG  . CYS H  3 362 ? 50.781  -36.499 34.376   1.00 216.69 ? 360  CYS H SG  1 
ATOM   22939 N  N   . SER H  3 363 ? 45.857  -35.493 33.255   1.00 194.88 ? 361  SER H N   1 
ATOM   22940 C  CA  . SER H  3 363 ? 44.758  -35.178 32.347   1.00 195.82 ? 361  SER H CA  1 
ATOM   22941 C  C   . SER H  3 363 ? 44.211  -33.769 32.573   1.00 214.70 ? 361  SER H C   1 
ATOM   22942 O  O   . SER H  3 363 ? 44.628  -33.050 33.485   1.00 223.74 ? 361  SER H O   1 
ATOM   22943 C  CB  . SER H  3 363 ? 43.636  -36.209 32.494   1.00 185.66 ? 361  SER H CB  1 
ATOM   22944 O  OG  . SER H  3 363 ? 43.157  -36.262 33.828   1.00 182.34 ? 361  SER H OG  1 
ATOM   22945 O  OXT . SER H  3 363 ? 43.338  -33.316 31.830   1.00 218.14 ? 361  SER H OXT 1 
HETATM 22946 CA CA  . CA  I  4 .   ? 6.845   -29.938 41.080   1.00 189.80 ? 2001 CA  A CA  1 
HETATM 22947 CA CA  . CA  J  4 .   ? 12.379  -20.971 49.293   1.00 222.52 ? 2002 CA  A CA  1 
HETATM 22948 CA CA  . CA  K  4 .   ? 21.117  -11.613 45.208   1.00 199.87 ? 2003 CA  A CA  1 
HETATM 22949 CA CA  . CA  L  4 .   ? 8.857   -33.021 27.335   1.00 155.88 ? 2004 CA  A CA  1 
HETATM 22950 C  C1  . NAG M  5 .   ? 7.517   10.459  20.035   1.00 160.92 ? 2005 NAG A C1  1 
HETATM 22951 C  C2  . NAG M  5 .   ? 6.700   11.026  21.194   1.00 196.07 ? 2005 NAG A C2  1 
HETATM 22952 C  C3  . NAG M  5 .   ? 5.328   11.484  20.700   1.00 207.95 ? 2005 NAG A C3  1 
HETATM 22953 C  C4  . NAG M  5 .   ? 5.461   12.411  19.497   1.00 222.55 ? 2005 NAG A C4  1 
HETATM 22954 C  C5  . NAG M  5 .   ? 6.377   11.802  18.438   1.00 234.53 ? 2005 NAG A C5  1 
HETATM 22955 C  C6  . NAG M  5 .   ? 6.693   12.748  17.305   1.00 243.90 ? 2005 NAG A C6  1 
HETATM 22956 C  C7  . NAG M  5 .   ? 7.425   9.921   23.264   1.00 169.45 ? 2005 NAG A C7  1 
HETATM 22957 C  C8  . NAG M  5 .   ? 7.116   8.855   24.270   1.00 177.71 ? 2005 NAG A C8  1 
HETATM 22958 N  N2  . NAG M  5 .   ? 6.556   10.044  22.256   1.00 178.57 ? 2005 NAG A N2  1 
HETATM 22959 O  O3  . NAG M  5 .   ? 4.643   12.154  21.752   1.00 206.85 ? 2005 NAG A O3  1 
HETATM 22960 O  O4  . NAG M  5 .   ? 4.182   12.592  18.901   1.00 202.15 ? 2005 NAG A O4  1 
HETATM 22961 O  O5  . NAG M  5 .   ? 7.634   11.429  19.020   1.00 217.76 ? 2005 NAG A O5  1 
HETATM 22962 O  O6  . NAG M  5 .   ? 7.700   12.218  16.453   1.00 244.59 ? 2005 NAG A O6  1 
HETATM 22963 O  O7  . NAG M  5 .   ? 8.416   10.637  23.360   1.00 155.19 ? 2005 NAG A O7  1 
HETATM 22964 C  C1  . NAG N  5 .   ? 3.703   13.930  19.098   1.00 207.14 ? 2006 NAG A C1  1 
HETATM 22965 C  C2  . NAG N  5 .   ? 3.056   14.371  17.789   1.00 230.21 ? 2006 NAG A C2  1 
HETATM 22966 C  C3  . NAG N  5 .   ? 2.422   15.749  17.949   1.00 237.69 ? 2006 NAG A C3  1 
HETATM 22967 C  C4  . NAG N  5 .   ? 1.466   15.764  19.136   1.00 237.11 ? 2006 NAG A C4  1 
HETATM 22968 C  C5  . NAG N  5 .   ? 2.169   15.245  20.389   1.00 214.51 ? 2006 NAG A C5  1 
HETATM 22969 C  C6  . NAG N  5 .   ? 1.232   15.088  21.564   1.00 198.53 ? 2006 NAG A C6  1 
HETATM 22970 C  C7  . NAG N  5 .   ? 3.760   13.847  15.495   1.00 236.08 ? 2006 NAG A C7  1 
HETATM 22971 C  C8  . NAG N  5 .   ? 4.864   13.941  14.485   1.00 225.29 ? 2006 NAG A C8  1 
HETATM 22972 N  N2  . NAG N  5 .   ? 4.017   14.374  16.697   1.00 228.88 ? 2006 NAG A N2  1 
HETATM 22973 O  O3  . NAG N  5 .   ? 1.736   16.091  16.750   1.00 238.05 ? 2006 NAG A O3  1 
HETATM 22974 O  O4  . NAG N  5 .   ? 0.994   17.086  19.377   1.00 255.68 ? 2006 NAG A O4  1 
HETATM 22975 O  O5  . NAG N  5 .   ? 2.738   13.951  20.138   1.00 194.86 ? 2006 NAG A O5  1 
HETATM 22976 O  O6  . NAG N  5 .   ? 1.855   14.395  22.636   1.00 197.05 ? 2006 NAG A O6  1 
HETATM 22977 O  O7  . NAG N  5 .   ? 2.683   13.319  15.233   1.00 216.40 ? 2006 NAG A O7  1 
HETATM 22978 C  C1  . BMA O  6 .   ? -0.299  17.280  18.763   1.00 252.84 ? 2007 BMA A C1  1 
HETATM 22979 C  C2  . BMA O  6 .   ? -1.305  17.844  19.792   1.00 260.73 ? 2007 BMA A C2  1 
HETATM 22980 C  C3  . BMA O  6 .   ? -2.639  18.161  19.107   1.00 247.00 ? 2007 BMA A C3  1 
HETATM 22981 C  C4  . BMA O  6 .   ? -2.427  18.987  17.832   1.00 244.99 ? 2007 BMA A C4  1 
HETATM 22982 C  C5  . BMA O  6 .   ? -1.486  18.252  16.894   1.00 226.97 ? 2007 BMA A C5  1 
HETATM 22983 C  C6  . BMA O  6 .   ? -1.244  19.022  15.613   1.00 192.16 ? 2007 BMA A C6  1 
HETATM 22984 O  O2  . BMA O  6 .   ? -0.834  19.069  20.342   1.00 242.73 ? 2007 BMA A O2  1 
HETATM 22985 O  O3  . BMA O  6 .   ? -3.530  18.847  19.979   1.00 247.10 ? 2007 BMA A O3  1 
HETATM 22986 O  O4  . BMA O  6 .   ? -3.660  19.211  17.167   1.00 230.06 ? 2007 BMA A O4  1 
HETATM 22987 O  O5  . BMA O  6 .   ? -0.226  18.064  17.569   1.00 253.18 ? 2007 BMA A O5  1 
HETATM 22988 O  O6  . BMA O  6 .   ? -0.892  18.095  14.606   1.00 181.92 ? 2007 BMA A O6  1 
HETATM 22989 C  C1  . NAG P  5 .   ? 4.705   -37.267 19.370   1.00 204.41 ? 2008 NAG A C1  1 
HETATM 22990 C  C2  . NAG P  5 .   ? 4.444   -38.698 18.917   1.00 238.89 ? 2008 NAG A C2  1 
HETATM 22991 C  C3  . NAG P  5 .   ? 3.721   -39.471 20.018   1.00 252.06 ? 2008 NAG A C3  1 
HETATM 22992 C  C4  . NAG P  5 .   ? 4.490   -39.371 21.329   1.00 253.98 ? 2008 NAG A C4  1 
HETATM 22993 C  C5  . NAG P  5 .   ? 4.792   -37.911 21.664   1.00 237.43 ? 2008 NAG A C5  1 
HETATM 22994 C  C6  . NAG P  5 .   ? 5.689   -37.756 22.870   1.00 235.10 ? 2008 NAG A C6  1 
HETATM 22995 C  C7  . NAG P  5 .   ? 4.241   -38.903 16.475   1.00 227.03 ? 2008 NAG A C7  1 
HETATM 22996 C  C8  . NAG P  5 .   ? 3.301   -38.902 15.309   1.00 239.64 ? 2008 NAG A C8  1 
HETATM 22997 N  N2  . NAG P  5 .   ? 3.682   -38.727 17.679   1.00 257.33 ? 2008 NAG A N2  1 
HETATM 22998 O  O3  . NAG P  5 .   ? 3.594   -40.834 19.630   1.00 248.77 ? 2008 NAG A O3  1 
HETATM 22999 O  O4  . NAG P  5 .   ? 3.731   -39.931 22.395   1.00 265.03 ? 2008 NAG A O4  1 
HETATM 23000 O  O5  . NAG P  5 .   ? 5.467   -37.279 20.567   1.00 218.07 ? 2008 NAG A O5  1 
HETATM 23001 O  O6  . NAG P  5 .   ? 6.782   -36.891 22.595   1.00 244.91 ? 2008 NAG A O6  1 
HETATM 23002 O  O7  . NAG P  5 .   ? 5.451   -39.056 16.335   1.00 188.95 ? 2008 NAG A O7  1 
HETATM 23003 C  C1  . NAG Q  5 .   ? 4.308   -41.203 22.740   1.00 279.94 ? 2009 NAG A C1  1 
HETATM 23004 C  C2  . NAG Q  5 .   ? 4.414   -41.376 24.253   1.00 296.99 ? 2009 NAG A C2  1 
HETATM 23005 C  C3  . NAG Q  5 .   ? 5.038   -42.730 24.586   1.00 295.85 ? 2009 NAG A C3  1 
HETATM 23006 C  C4  . NAG Q  5 .   ? 4.328   -43.862 23.854   1.00 292.33 ? 2009 NAG A C4  1 
HETATM 23007 C  C5  . NAG Q  5 .   ? 4.182   -43.544 22.366   1.00 293.14 ? 2009 NAG A C5  1 
HETATM 23008 C  C6  . NAG Q  5 .   ? 3.326   -44.542 21.620   1.00 285.26 ? 2009 NAG A C6  1 
HETATM 23009 C  C7  . NAG Q  5 .   ? 5.112   -39.965 26.137   1.00 274.76 ? 2009 NAG A C7  1 
HETATM 23010 C  C8  . NAG Q  5 .   ? 6.006   -38.850 26.581   1.00 251.98 ? 2009 NAG A C8  1 
HETATM 23011 N  N2  . NAG Q  5 .   ? 5.196   -40.304 24.846   1.00 284.03 ? 2009 NAG A N2  1 
HETATM 23012 O  O3  . NAG Q  5 .   ? 4.978   -42.952 25.990   1.00 298.27 ? 2009 NAG A O3  1 
HETATM 23013 O  O4  . NAG Q  5 .   ? 5.117   -45.037 23.994   1.00 299.75 ? 2009 NAG A O4  1 
HETATM 23014 O  O5  . NAG Q  5 .   ? 3.558   -42.264 22.194   1.00 293.20 ? 2009 NAG A O5  1 
HETATM 23015 O  O6  . NAG Q  5 .   ? 3.791   -44.734 20.292   1.00 280.82 ? 2009 NAG A O6  1 
HETATM 23016 O  O7  . NAG Q  5 .   ? 4.349   -40.534 26.911   1.00 260.83 ? 2009 NAG A O7  1 
HETATM 23017 C  C1  . BMA R  6 .   ? 4.392   -46.086 24.650   1.00 291.68 ? 2010 BMA A C1  1 
HETATM 23018 C  C2  . BMA R  6 .   ? 4.408   -47.242 23.692   1.00 305.26 ? 2010 BMA A C2  1 
HETATM 23019 C  C3  . BMA R  6 .   ? 3.636   -48.394 24.331   1.00 286.49 ? 2010 BMA A C3  1 
HETATM 23020 C  C4  . BMA R  6 .   ? 4.269   -48.798 25.681   1.00 271.49 ? 2010 BMA A C4  1 
HETATM 23021 C  C5  . BMA R  6 .   ? 4.345   -47.545 26.607   1.00 269.51 ? 2010 BMA A C5  1 
HETATM 23022 C  C6  . BMA R  6 .   ? 5.131   -47.790 27.904   1.00 286.22 ? 2010 BMA A C6  1 
HETATM 23023 O  O2  . BMA R  6 .   ? 5.761   -47.649 23.503   1.00 308.73 ? 2010 BMA A O2  1 
HETATM 23024 O  O3  . BMA R  6 .   ? 3.366   -49.518 23.419   1.00 298.94 ? 2010 BMA A O3  1 
HETATM 23025 O  O4  . BMA R  6 .   ? 3.486   -49.802 26.304   1.00 242.27 ? 2010 BMA A O4  1 
HETATM 23026 O  O5  . BMA R  6 .   ? 4.973   -46.443 25.892   1.00 283.66 ? 2010 BMA A O5  1 
HETATM 23027 O  O6  . BMA R  6 .   ? 5.055   -46.628 28.755   1.00 283.40 ? 2010 BMA A O6  1 
HETATM 23028 C  C1  . MAN S  7 .   ? 6.278   -45.862 28.649   1.00 291.15 ? 2011 MAN A C1  1 
HETATM 23029 C  C2  . MAN S  7 .   ? 7.318   -46.269 29.741   1.00 262.38 ? 2011 MAN A C2  1 
HETATM 23030 C  C3  . MAN S  7 .   ? 7.174   -45.426 31.018   1.00 272.64 ? 2011 MAN A C3  1 
HETATM 23031 C  C4  . MAN S  7 .   ? 7.022   -43.941 30.687   1.00 256.49 ? 2011 MAN A C4  1 
HETATM 23032 C  C5  . MAN S  7 .   ? 5.792   -43.778 29.797   1.00 280.52 ? 2011 MAN A C5  1 
HETATM 23033 C  C6  . MAN S  7 .   ? 5.459   -42.329 29.456   1.00 258.71 ? 2011 MAN A C6  1 
HETATM 23034 O  O2  . MAN S  7 .   ? 8.659   -46.040 29.286   1.00 242.63 ? 2011 MAN A O2  1 
HETATM 23035 O  O3  . MAN S  7 .   ? 8.266   -45.616 31.910   1.00 265.36 ? 2011 MAN A O3  1 
HETATM 23036 O  O4  . MAN S  7 .   ? 6.863   -43.189 31.876   1.00 238.86 ? 2011 MAN A O4  1 
HETATM 23037 O  O5  . MAN S  7 .   ? 6.047   -44.466 28.554   1.00 276.36 ? 2011 MAN A O5  1 
HETATM 23038 O  O6  . MAN S  7 .   ? 5.363   -41.558 30.662   1.00 244.93 ? 2011 MAN A O6  1 
HETATM 23039 C  C1  . MAN T  7 .   ? 4.059   -41.693 31.280   1.00 241.63 ? 2012 MAN A C1  1 
HETATM 23040 C  C2  . MAN T  7 .   ? 2.887   -41.742 30.234   1.00 238.93 ? 2012 MAN A C2  1 
HETATM 23041 C  C3  . MAN T  7 .   ? 2.428   -40.340 29.834   1.00 247.24 ? 2012 MAN A C3  1 
HETATM 23042 C  C4  . MAN T  7 .   ? 2.262   -39.433 31.068   1.00 238.99 ? 2012 MAN A C4  1 
HETATM 23043 C  C5  . MAN T  7 .   ? 3.581   -39.403 31.853   1.00 237.89 ? 2012 MAN A C5  1 
HETATM 23044 C  C6  . MAN T  7 .   ? 3.539   -38.499 33.072   1.00 218.22 ? 2012 MAN A C6  1 
HETATM 23045 O  O2  . MAN T  7 .   ? 1.722   -42.392 30.756   1.00 239.41 ? 2012 MAN A O2  1 
HETATM 23046 O  O3  . MAN T  7 .   ? 1.223   -40.386 29.072   1.00 233.26 ? 2012 MAN A O3  1 
HETATM 23047 O  O4  . MAN T  7 .   ? 1.918   -38.118 30.669   1.00 246.16 ? 2012 MAN A O4  1 
HETATM 23048 O  O5  . MAN T  7 .   ? 3.864   -40.740 32.306   1.00 231.50 ? 2012 MAN A O5  1 
HETATM 23049 O  O6  . MAN T  7 .   ? 4.871   -38.057 33.337   1.00 210.42 ? 2012 MAN A O6  1 
HETATM 23050 C  C1  . MAN U  7 .   ? 4.495   -50.347 23.058   1.00 288.87 ? 2013 MAN A C1  1 
HETATM 23051 C  C2  . MAN U  7 .   ? 4.951   -50.025 21.582   1.00 267.44 ? 2013 MAN A C2  1 
HETATM 23052 C  C3  . MAN U  7 .   ? 4.042   -50.700 20.550   1.00 267.54 ? 2013 MAN A C3  1 
HETATM 23053 C  C4  . MAN U  7 .   ? 3.757   -52.155 20.932   1.00 271.09 ? 2013 MAN A C4  1 
HETATM 23054 C  C5  . MAN U  7 .   ? 3.173   -52.176 22.346   1.00 256.47 ? 2013 MAN A C5  1 
HETATM 23055 C  C6  . MAN U  7 .   ? 2.716   -53.546 22.804   1.00 193.45 ? 2013 MAN A C6  1 
HETATM 23056 O  O2  . MAN U  7 .   ? 6.274   -50.500 21.292   1.00 244.08 ? 2013 MAN A O2  1 
HETATM 23057 O  O3  . MAN U  7 .   ? 4.588   -50.626 19.236   1.00 241.59 ? 2013 MAN A O3  1 
HETATM 23058 O  O4  . MAN U  7 .   ? 2.836   -52.724 20.024   1.00 278.98 ? 2013 MAN A O4  1 
HETATM 23059 O  O5  . MAN U  7 .   ? 4.193   -51.703 23.242   1.00 279.42 ? 2013 MAN A O5  1 
HETATM 23060 O  O6  . MAN U  7 .   ? 2.993   -53.672 24.193   1.00 144.69 ? 2013 MAN A O6  1 
HETATM 23061 C  C1  . NAG V  5 .   ? -7.460  -29.853 25.040   1.00 157.26 ? 2014 NAG A C1  1 
HETATM 23062 C  C2  . NAG V  5 .   ? -7.256  -31.122 24.245   1.00 208.74 ? 2014 NAG A C2  1 
HETATM 23063 C  C3  . NAG V  5 .   ? -6.910  -30.773 22.804   1.00 226.42 ? 2014 NAG A C3  1 
HETATM 23064 C  C4  . NAG V  5 .   ? -7.939  -29.810 22.221   1.00 206.13 ? 2014 NAG A C4  1 
HETATM 23065 C  C5  . NAG V  5 .   ? -8.234  -28.642 23.165   1.00 188.14 ? 2014 NAG A C5  1 
HETATM 23066 C  C6  . NAG V  5 .   ? -9.444  -27.838 22.745   1.00 193.10 ? 2014 NAG A C6  1 
HETATM 23067 C  C7  . NAG V  5 .   ? -6.350  -33.270 24.994   1.00 252.66 ? 2014 NAG A C7  1 
HETATM 23068 C  C8  . NAG V  5 .   ? -5.189  -33.975 25.628   1.00 243.26 ? 2014 NAG A C8  1 
HETATM 23069 N  N2  . NAG V  5 .   ? -6.219  -31.950 24.838   1.00 235.64 ? 2014 NAG A N2  1 
HETATM 23070 O  O3  . NAG V  5 .   ? -6.876  -31.969 22.036   1.00 231.85 ? 2014 NAG A O3  1 
HETATM 23071 O  O4  . NAG V  5 .   ? -7.441  -29.277 20.999   1.00 214.00 ? 2014 NAG A O4  1 
HETATM 23072 O  O5  . NAG V  5 .   ? -8.516  -29.120 24.486   1.00 159.30 ? 2014 NAG A O5  1 
HETATM 23073 O  O6  . NAG V  5 .   ? -10.630 -28.620 22.809   1.00 177.99 ? 2014 NAG A O6  1 
HETATM 23074 O  O7  . NAG V  5 .   ? -7.359  -33.870 24.635   1.00 231.78 ? 2014 NAG A O7  1 
HETATM 23075 C  C1  . NAG W  5 .   ? -8.399  -29.615 19.988   1.00 203.06 ? 2015 NAG A C1  1 
HETATM 23076 C  C2  . NAG W  5 .   ? -7.883  -29.267 18.602   1.00 191.80 ? 2015 NAG A C2  1 
HETATM 23077 C  C3  . NAG W  5 .   ? -8.919  -29.642 17.552   1.00 177.19 ? 2015 NAG A C3  1 
HETATM 23078 C  C4  . NAG W  5 .   ? -9.323  -31.103 17.707   1.00 165.93 ? 2015 NAG A C4  1 
HETATM 23079 C  C5  . NAG W  5 .   ? -9.753  -31.383 19.145   1.00 171.80 ? 2015 NAG A C5  1 
HETATM 23080 C  C6  . NAG W  5 .   ? -10.020 -32.844 19.416   1.00 179.27 ? 2015 NAG A C6  1 
HETATM 23081 C  C7  . NAG W  5 .   ? -6.290  -27.418 18.317   1.00 189.65 ? 2015 NAG A C7  1 
HETATM 23082 C  C8  . NAG W  5 .   ? -5.227  -28.472 18.231   1.00 185.34 ? 2015 NAG A C8  1 
HETATM 23083 N  N2  . NAG W  5 .   ? -7.541  -27.857 18.501   1.00 197.16 ? 2015 NAG A N2  1 
HETATM 23084 O  O3  . NAG W  5 .   ? -8.377  -29.400 16.260   1.00 184.57 ? 2015 NAG A O3  1 
HETATM 23085 O  O4  . NAG W  5 .   ? -10.398 -31.413 16.829   1.00 172.85 ? 2015 NAG A O4  1 
HETATM 23086 O  O5  . NAG W  5 .   ? -8.710  -30.992 20.047   1.00 193.98 ? 2015 NAG A O5  1 
HETATM 23087 O  O6  . NAG W  5 .   ? -10.968 -33.378 18.504   1.00 185.36 ? 2015 NAG A O6  1 
HETATM 23088 O  O7  . NAG W  5 .   ? -6.028  -26.223 18.227   1.00 193.76 ? 2015 NAG A O7  1 
HETATM 23089 C  C1  . BMA X  6 .   ? -9.876  -32.083 15.665   1.00 200.73 ? 2016 BMA A C1  1 
HETATM 23090 C  C2  . BMA X  6 .   ? -10.894 -33.133 15.189   1.00 192.12 ? 2016 BMA A C2  1 
HETATM 23091 C  C3  . BMA X  6 .   ? -10.478 -33.700 13.826   1.00 153.80 ? 2016 BMA A C3  1 
HETATM 23092 C  C4  . BMA X  6 .   ? -10.151 -32.590 12.853   1.00 176.94 ? 2016 BMA A C4  1 
HETATM 23093 C  C5  . BMA X  6 .   ? -9.061  -31.672 13.447   1.00 197.54 ? 2016 BMA A C5  1 
HETATM 23094 C  C6  . BMA X  6 .   ? -8.766  -30.462 12.600   1.00 199.01 ? 2016 BMA A C6  1 
HETATM 23095 O  O2  . BMA X  6 .   ? -12.187 -32.554 15.020   1.00 199.62 ? 2016 BMA A O2  1 
HETATM 23096 O  O3  . BMA X  6 .   ? -11.475 -34.523 13.251   1.00 117.12 ? 2016 BMA A O3  1 
HETATM 23097 O  O4  . BMA X  6 .   ? -9.718  -33.164 11.643   1.00 170.99 ? 2016 BMA A O4  1 
HETATM 23098 O  O5  . BMA X  6 .   ? -9.558  -31.142 14.671   1.00 216.87 ? 2016 BMA A O5  1 
HETATM 23099 O  O6  . BMA X  6 .   ? -7.614  -30.694 11.798   1.00 216.73 ? 2016 BMA A O6  1 
HETATM 23100 C  C1  . MAN Y  7 .   ? -11.705 -35.631 14.130   1.00 167.64 ? 2017 MAN A C1  1 
HETATM 23101 C  C2  . MAN Y  7 .   ? -11.549 -36.907 13.318   1.00 179.02 ? 2017 MAN A C2  1 
HETATM 23102 C  C3  . MAN Y  7 .   ? -12.774 -37.110 12.427   1.00 218.94 ? 2017 MAN A C3  1 
HETATM 23103 C  C4  . MAN Y  7 .   ? -14.095 -36.980 13.238   1.00 224.24 ? 2017 MAN A C4  1 
HETATM 23104 C  C5  . MAN Y  7 .   ? -14.122 -35.628 13.975   1.00 224.33 ? 2017 MAN A C5  1 
HETATM 23105 C  C6  . MAN Y  7 .   ? -15.371 -35.428 14.849   1.00 199.22 ? 2017 MAN A C6  1 
HETATM 23106 O  O2  . MAN Y  7 .   ? -11.470 -38.062 14.152   1.00 171.03 ? 2017 MAN A O2  1 
HETATM 23107 O  O3  . MAN Y  7 .   ? -12.716 -38.358 11.740   1.00 213.12 ? 2017 MAN A O3  1 
HETATM 23108 O  O4  . MAN Y  7 .   ? -15.221 -37.071 12.381   1.00 249.82 ? 2017 MAN A O4  1 
HETATM 23109 O  O5  . MAN Y  7 .   ? -12.944 -35.543 14.813   1.00 196.53 ? 2017 MAN A O5  1 
HETATM 23110 O  O6  . MAN Y  7 .   ? -15.314 -36.305 15.974   1.00 197.63 ? 2017 MAN A O6  1 
HETATM 23111 C  C1  . MAN Z  7 .   ? -8.004  -30.987 10.437   1.00 228.73 ? 2018 MAN A C1  1 
HETATM 23112 C  C2  . MAN Z  7 .   ? -7.127  -30.194 9.393    1.00 253.19 ? 2018 MAN A C2  1 
HETATM 23113 C  C3  . MAN Z  7 .   ? -7.930  -29.400 8.323    1.00 246.41 ? 2018 MAN A C3  1 
HETATM 23114 C  C4  . MAN Z  7 .   ? -9.391  -29.855 8.188    1.00 225.29 ? 2018 MAN A C4  1 
HETATM 23115 C  C5  . MAN Z  7 .   ? -10.012 -29.908 9.548    1.00 197.84 ? 2018 MAN A C5  1 
HETATM 23116 C  C6  . MAN Z  7 .   ? -11.478 -30.209 9.509    1.00 187.33 ? 2018 MAN A C6  1 
HETATM 23117 O  O2  . MAN Z  7 .   ? -6.257  -31.078 8.665    1.00 265.83 ? 2018 MAN A O2  1 
HETATM 23118 O  O3  . MAN Z  7 .   ? -7.298  -29.505 7.049    1.00 277.29 ? 2018 MAN A O3  1 
HETATM 23119 O  O4  . MAN Z  7 .   ? -10.119 -28.929 7.397    1.00 214.28 ? 2018 MAN A O4  1 
HETATM 23120 O  O5  . MAN Z  7 .   ? -9.419  -31.005 10.233   1.00 200.16 ? 2018 MAN A O5  1 
HETATM 23121 O  O6  . MAN Z  7 .   ? -12.109 -29.208 8.732    1.00 201.19 ? 2018 MAN A O6  1 
HETATM 23122 C  C1  . MAN AA 7 .   ? -13.336 -28.814 9.373    1.00 224.35 ? 2019 MAN A C1  1 
HETATM 23123 C  C2  . MAN AA 7 .   ? -14.168 -30.063 9.771    1.00 220.12 ? 2019 MAN A C2  1 
HETATM 23124 C  C3  . MAN AA 7 .   ? -14.889 -30.643 8.558    1.00 220.94 ? 2019 MAN A C3  1 
HETATM 23125 C  C4  . MAN AA 7 .   ? -15.637 -29.544 7.787    1.00 228.07 ? 2019 MAN A C4  1 
HETATM 23126 C  C5  . MAN AA 7 .   ? -14.649 -28.423 7.398    1.00 237.73 ? 2019 MAN A C5  1 
HETATM 23127 C  C6  . MAN AA 7 .   ? -15.305 -27.265 6.659    1.00 229.75 ? 2019 MAN A C6  1 
HETATM 23128 O  O2  . MAN AA 7 .   ? -15.201 -29.734 10.702   1.00 225.04 ? 2019 MAN A O2  1 
HETATM 23129 O  O3  . MAN AA 7 .   ? -15.781 -31.687 8.929    1.00 211.77 ? 2019 MAN A O3  1 
HETATM 23130 O  O4  . MAN AA 7 .   ? -16.222 -30.091 6.623    1.00 213.14 ? 2019 MAN A O4  1 
HETATM 23131 O  O5  . MAN AA 7 .   ? -14.058 -27.888 8.599    1.00 246.19 ? 2019 MAN A O5  1 
HETATM 23132 O  O6  . MAN AA 7 .   ? -14.285 -26.339 6.273    1.00 210.71 ? 2019 MAN A O6  1 
HETATM 23133 C  C1  . MAN BA 7 .   ? -6.478  -28.360 6.764    1.00 281.75 ? 2020 MAN A C1  1 
HETATM 23134 C  C2  . MAN BA 7 .   ? -7.380  -27.207 6.310    1.00 289.65 ? 2020 MAN A C2  1 
HETATM 23135 C  C3  . MAN BA 7 .   ? -7.958  -27.519 4.925    1.00 283.99 ? 2020 MAN A C3  1 
HETATM 23136 C  C4  . MAN BA 7 .   ? -6.856  -27.965 3.934    1.00 286.47 ? 2020 MAN A C4  1 
HETATM 23137 C  C5  . MAN BA 7 .   ? -6.040  -29.117 4.538    1.00 283.74 ? 2020 MAN A C5  1 
HETATM 23138 C  C6  . MAN BA 7 .   ? -4.880  -29.562 3.659    1.00 266.22 ? 2020 MAN A C6  1 
HETATM 23139 O  O2  . MAN BA 7 .   ? -6.645  -25.986 6.168    1.00 277.52 ? 2020 MAN A O2  1 
HETATM 23140 O  O3  . MAN BA 7 .   ? -8.682  -26.410 4.398    1.00 293.89 ? 2020 MAN A O3  1 
HETATM 23141 O  O4  . MAN BA 7 .   ? -7.442  -28.402 2.718    1.00 284.09 ? 2020 MAN A O4  1 
HETATM 23142 O  O5  . MAN BA 7 .   ? -5.501  -28.679 5.808    1.00 283.01 ? 2020 MAN A O5  1 
HETATM 23143 O  O6  . MAN BA 7 .   ? -4.474  -30.863 4.083    1.00 257.44 ? 2020 MAN A O6  1 
HETATM 23144 C  C1  . NAG CA 5 .   ? 23.993  -23.411 95.881   1.00 268.23 ? 2021 NAG A C1  1 
HETATM 23145 C  C2  . NAG CA 5 .   ? 23.341  -24.628 95.232   1.00 280.85 ? 2021 NAG A C2  1 
HETATM 23146 C  C3  . NAG CA 5 .   ? 24.394  -25.469 94.510   1.00 273.88 ? 2021 NAG A C3  1 
HETATM 23147 C  C4  . NAG CA 5 .   ? 25.205  -24.609 93.548   1.00 304.12 ? 2021 NAG A C4  1 
HETATM 23148 C  C5  . NAG CA 5 .   ? 25.759  -23.382 94.268   1.00 304.99 ? 2021 NAG A C5  1 
HETATM 23149 C  C6  . NAG CA 5 .   ? 26.467  -22.418 93.344   1.00 290.78 ? 2021 NAG A C6  1 
HETATM 23150 C  C7  . NAG CA 5 .   ? 21.329  -25.692 96.164   1.00 298.63 ? 2021 NAG A C7  1 
HETATM 23151 C  C8  . NAG CA 5 .   ? 20.590  -25.107 94.999   1.00 291.07 ? 2021 NAG A C8  1 
HETATM 23152 N  N2  . NAG CA 5 .   ? 22.639  -25.429 96.222   1.00 297.51 ? 2021 NAG A N2  1 
HETATM 23153 O  O3  . NAG CA 5 .   ? 23.748  -26.525 93.807   1.00 239.29 ? 2021 NAG A O3  1 
HETATM 23154 O  O4  . NAG CA 5 .   ? 26.295  -25.350 93.010   1.00 308.89 ? 2021 NAG A O4  1 
HETATM 23155 O  O5  . NAG CA 5 .   ? 24.690  -22.655 94.890   1.00 300.08 ? 2021 NAG A O5  1 
HETATM 23156 O  O6  . NAG CA 5 .   ? 25.621  -21.336 92.979   1.00 282.15 ? 2021 NAG A O6  1 
HETATM 23157 O  O7  . NAG CA 5 .   ? 20.765  -26.373 97.014   1.00 308.60 ? 2021 NAG A O7  1 
HETATM 23158 C  C1  . NAG DA 5 .   ? 25.949  -25.795 91.687   1.00 301.49 ? 2022 NAG A C1  1 
HETATM 23159 C  C2  . NAG DA 5 .   ? 27.140  -25.705 90.734   1.00 293.93 ? 2022 NAG A C2  1 
HETATM 23160 C  C3  . NAG DA 5 .   ? 26.735  -26.175 89.340   1.00 278.11 ? 2022 NAG A C3  1 
HETATM 23161 C  C4  . NAG DA 5 .   ? 26.097  -27.557 89.409   1.00 294.39 ? 2022 NAG A C4  1 
HETATM 23162 C  C5  . NAG DA 5 .   ? 24.969  -27.578 90.436   1.00 296.47 ? 2022 NAG A C5  1 
HETATM 23163 C  C6  . NAG DA 5 .   ? 24.399  -28.959 90.657   1.00 291.20 ? 2022 NAG A C6  1 
HETATM 23164 C  C7  . NAG DA 5 .   ? 28.977  -24.085 90.856   1.00 269.73 ? 2022 NAG A C7  1 
HETATM 23165 C  C8  . NAG DA 5 .   ? 29.365  -22.639 90.777   1.00 253.20 ? 2022 NAG A C8  1 
HETATM 23166 N  N2  . NAG DA 5 .   ? 27.678  -24.355 90.686   1.00 281.54 ? 2022 NAG A N2  1 
HETATM 23167 O  O3  . NAG DA 5 .   ? 27.885  -26.212 88.501   1.00 258.89 ? 2022 NAG A O3  1 
HETATM 23168 O  O4  . NAG DA 5 .   ? 25.541  -27.895 88.145   1.00 287.20 ? 2022 NAG A O4  1 
HETATM 23169 O  O5  . NAG DA 5 .   ? 25.454  -27.127 91.708   1.00 303.61 ? 2022 NAG A O5  1 
HETATM 23170 O  O6  . NAG DA 5 .   ? 22.989  -28.914 90.821   1.00 279.70 ? 2022 NAG A O6  1 
HETATM 23171 O  O7  . NAG DA 5 .   ? 29.802  -24.968 91.066   1.00 257.83 ? 2022 NAG A O7  1 
HETATM 23172 C  C1  . BMA EA 6 .   ? 26.289  -28.984 87.591   1.00 291.04 ? 2023 BMA A C1  1 
HETATM 23173 C  C2  . BMA EA 6 .   ? 25.290  -29.875 86.823   1.00 288.78 ? 2023 BMA A C2  1 
HETATM 23174 C  C3  . BMA EA 6 .   ? 25.990  -30.774 85.794   1.00 294.51 ? 2023 BMA A C3  1 
HETATM 23175 C  C4  . BMA EA 6 .   ? 27.122  -30.044 85.052   1.00 313.38 ? 2023 BMA A C4  1 
HETATM 23176 C  C5  . BMA EA 6 .   ? 28.085  -29.442 86.076   1.00 300.97 ? 2023 BMA A C5  1 
HETATM 23177 C  C6  . BMA EA 6 .   ? 29.267  -28.707 85.458   1.00 310.57 ? 2023 BMA A C6  1 
HETATM 23178 O  O2  . BMA EA 6 .   ? 24.353  -29.077 86.110   1.00 279.11 ? 2023 BMA A O2  1 
HETATM 23179 O  O3  . BMA EA 6 .   ? 25.054  -31.299 84.860   1.00 294.65 ? 2023 BMA A O3  1 
HETATM 23180 O  O4  . BMA EA 6 .   ? 27.815  -30.951 84.210   1.00 321.65 ? 2023 BMA A O4  1 
HETATM 23181 O  O5  . BMA EA 6 .   ? 27.346  -28.476 86.813   1.00 290.86 ? 2023 BMA A O5  1 
HETATM 23182 O  O6  . BMA EA 6 .   ? 30.041  -29.609 84.685   1.00 312.92 ? 2023 BMA A O6  1 
HETATM 23183 C  C1  . MAN FA 7 .   ? 30.235  -29.032 83.379   1.00 278.12 ? 2024 MAN A C1  1 
HETATM 23184 C  C2  . MAN FA 7 .   ? 30.657  -30.142 82.406   1.00 232.42 ? 2024 MAN A C2  1 
HETATM 23185 C  C3  . MAN FA 7 .   ? 31.582  -29.575 81.343   1.00 231.85 ? 2024 MAN A C3  1 
HETATM 23186 C  C4  . MAN FA 7 .   ? 31.112  -28.185 80.925   1.00 251.11 ? 2024 MAN A C4  1 
HETATM 23187 C  C5  . MAN FA 7 .   ? 31.313  -27.222 82.103   1.00 287.86 ? 2024 MAN A C5  1 
HETATM 23188 C  C6  . MAN FA 7 .   ? 30.396  -26.010 82.052   1.00 287.68 ? 2024 MAN A C6  1 
HETATM 23189 O  O2  . MAN FA 7 .   ? 29.529  -30.644 81.693   1.00 229.93 ? 2024 MAN A O2  1 
HETATM 23190 O  O3  . MAN FA 7 .   ? 31.666  -30.427 80.210   1.00 223.58 ? 2024 MAN A O3  1 
HETATM 23191 O  O4  . MAN FA 7 .   ? 31.864  -27.729 79.815   1.00 243.26 ? 2024 MAN A O4  1 
HETATM 23192 O  O5  . MAN FA 7 .   ? 31.107  -27.916 83.382   1.00 265.27 ? 2024 MAN A O5  1 
HETATM 23193 O  O6  . MAN FA 7 .   ? 30.859  -25.059 83.004   1.00 291.88 ? 2024 MAN A O6  1 
HETATM 23194 C  C1  . NAG GA 5 .   ? 29.576  -2.658  73.018   1.00 280.55 ? 2025 NAG A C1  1 
HETATM 23195 C  C2  . NAG GA 5 .   ? 30.145  -1.731  74.107   1.00 316.53 ? 2025 NAG A C2  1 
HETATM 23196 C  C3  . NAG GA 5 .   ? 29.196  -0.553  74.359   1.00 332.67 ? 2025 NAG A C3  1 
HETATM 23197 C  C4  . NAG GA 5 .   ? 28.767  0.103   73.051   1.00 340.17 ? 2025 NAG A C4  1 
HETATM 23198 C  C5  . NAG GA 5 .   ? 28.266  -0.952  72.073   1.00 334.16 ? 2025 NAG A C5  1 
HETATM 23199 C  C6  . NAG GA 5 .   ? 27.895  -0.393  70.721   1.00 335.42 ? 2025 NAG A C6  1 
HETATM 23200 C  C7  . NAG GA 5 .   ? 31.528  -3.093  75.623   1.00 314.93 ? 2025 NAG A C7  1 
HETATM 23201 C  C8  . NAG GA 5 .   ? 31.590  -3.786  76.952   1.00 306.91 ? 2025 NAG A C8  1 
HETATM 23202 N  N2  . NAG GA 5 .   ? 30.383  -2.461  75.344   1.00 323.29 ? 2025 NAG A N2  1 
HETATM 23203 O  O3  . NAG GA 5 .   ? 29.832  0.405   75.197   1.00 334.70 ? 2025 NAG A O3  1 
HETATM 23204 O  O4  . NAG GA 5 .   ? 27.719  1.032   73.297   1.00 345.53 ? 2025 NAG A O4  1 
HETATM 23205 O  O5  . NAG GA 5 .   ? 29.305  -1.913  71.854   1.00 319.68 ? 2025 NAG A O5  1 
HETATM 23206 O  O6  . NAG GA 5 .   ? 26.893  -1.187  70.100   1.00 340.24 ? 2025 NAG A O6  1 
HETATM 23207 O  O7  . NAG GA 5 .   ? 32.470  -3.108  74.838   1.00 315.50 ? 2025 NAG A O7  1 
HETATM 23208 C  C1  . NAG HA 5 .   ? 11.490  -10.333 72.649   1.00 229.37 ? 2026 NAG A C1  1 
HETATM 23209 C  C2  . NAG HA 5 .   ? 10.757  -9.112  73.155   1.00 265.35 ? 2026 NAG A C2  1 
HETATM 23210 C  C3  . NAG HA 5 .   ? 9.251   -9.355  73.070   1.00 266.20 ? 2026 NAG A C3  1 
HETATM 23211 C  C4  . NAG HA 5 .   ? 8.857   -9.822  71.670   1.00 273.42 ? 2026 NAG A C4  1 
HETATM 23212 C  C5  . NAG HA 5 .   ? 9.757   -10.958 71.188   1.00 242.97 ? 2026 NAG A C5  1 
HETATM 23213 C  C6  . NAG HA 5 .   ? 9.531   -11.316 69.738   1.00 201.97 ? 2026 NAG A C6  1 
HETATM 23214 C  C7  . NAG HA 5 .   ? 11.016  -7.564  75.040   1.00 284.01 ? 2026 NAG A C7  1 
HETATM 23215 C  C8  . NAG HA 5 .   ? 11.483  -7.402  76.450   1.00 283.18 ? 2026 NAG A C8  1 
HETATM 23216 N  N2  . NAG HA 5 .   ? 11.155  -8.784  74.514   1.00 290.70 ? 2026 NAG A N2  1 
HETATM 23217 O  O3  . NAG HA 5 .   ? 8.549   -8.170  73.425   1.00 255.06 ? 2026 NAG A O3  1 
HETATM 23218 O  O4  . NAG HA 5 .   ? 7.524   -10.320 71.662   1.00 295.46 ? 2026 NAG A O4  1 
HETATM 23219 O  O5  . NAG HA 5 .   ? 11.130  -10.573 71.306   1.00 249.25 ? 2026 NAG A O5  1 
HETATM 23220 O  O6  . NAG HA 5 .   ? 8.867   -12.566 69.616   1.00 170.67 ? 2026 NAG A O6  1 
HETATM 23221 O  O7  . NAG HA 5 .   ? 10.530  -6.634  74.407   1.00 256.55 ? 2026 NAG A O7  1 
HETATM 23222 C  C1  . NAG IA 5 .   ? 6.631   -9.341  71.105   1.00 276.21 ? 2027 NAG A C1  1 
HETATM 23223 C  C2  . NAG IA 5 .   ? 5.740   -9.937  70.009   1.00 242.16 ? 2027 NAG A C2  1 
HETATM 23224 C  C3  . NAG IA 5 .   ? 4.761   -8.883  69.494   1.00 227.51 ? 2027 NAG A C3  1 
HETATM 23225 C  C4  . NAG IA 5 .   ? 3.990   -8.261  70.651   1.00 245.89 ? 2027 NAG A C4  1 
HETATM 23226 C  C5  . NAG IA 5 .   ? 4.957   -7.748  71.716   1.00 272.22 ? 2027 NAG A C5  1 
HETATM 23227 C  C6  . NAG IA 5 .   ? 4.262   -7.240  72.958   1.00 281.20 ? 2027 NAG A C6  1 
HETATM 23228 C  C7  . NAG IA 5 .   ? 6.175   -11.572 68.229   1.00 220.29 ? 2027 NAG A C7  1 
HETATM 23229 C  C8  . NAG IA 5 .   ? 7.101   -11.985 67.124   1.00 222.09 ? 2027 NAG A C8  1 
HETATM 23230 N  N2  . NAG IA 5 .   ? 6.529   -10.478 68.914   1.00 235.14 ? 2027 NAG A N2  1 
HETATM 23231 O  O3  . NAG IA 5 .   ? 3.862   -9.469  68.559   1.00 189.11 ? 2027 NAG A O3  1 
HETATM 23232 O  O4  . NAG IA 5 .   ? 3.193   -7.181  70.177   1.00 245.21 ? 2027 NAG A O4  1 
HETATM 23233 O  O5  . NAG IA 5 .   ? 5.820   -8.812  72.142   1.00 265.65 ? 2027 NAG A O5  1 
HETATM 23234 O  O6  . NAG IA 5 .   ? 4.774   -7.864  74.129   1.00 286.72 ? 2027 NAG A O6  1 
HETATM 23235 O  O7  . NAG IA 5 .   ? 5.154   -12.200 68.489   1.00 197.79 ? 2027 NAG A O7  1 
HETATM 23236 MN MN  . MN  JA 8 .   ? -26.904 -11.503 12.041   1.00 181.47 ? 2001 MN  B MN  1 
HETATM 23237 MN MN  . MN  KA 8 .   ? -20.744 -8.256  14.433   1.00 110.30 ? 2002 MN  B MN  1 
HETATM 23238 MN MN  . MN  LA 8 .   ? -15.370 -7.068  16.303   1.00 144.63 ? 2003 MN  B MN  1 
HETATM 23239 C  C1  . NAG MA 5 .   ? -32.593 14.634  40.787   1.00 253.26 ? 2004 NAG B C1  1 
HETATM 23240 C  C2  . NAG MA 5 .   ? -32.934 15.648  39.687   1.00 263.47 ? 2004 NAG B C2  1 
HETATM 23241 C  C3  . NAG MA 5 .   ? -31.836 16.704  39.577   1.00 258.06 ? 2004 NAG B C3  1 
HETATM 23242 C  C4  . NAG MA 5 .   ? -31.549 17.326  40.937   1.00 265.01 ? 2004 NAG B C4  1 
HETATM 23243 C  C5  . NAG MA 5 .   ? -31.261 16.233  41.962   1.00 253.28 ? 2004 NAG B C5  1 
HETATM 23244 C  C6  . NAG MA 5 .   ? -31.063 16.766  43.362   1.00 243.43 ? 2004 NAG B C6  1 
HETATM 23245 C  C7  . NAG MA 5 .   ? -34.278 15.054  37.723   1.00 259.46 ? 2004 NAG B C7  1 
HETATM 23246 C  C8  . NAG MA 5 .   ? -34.308 14.321  36.415   1.00 255.98 ? 2004 NAG B C8  1 
HETATM 23247 N  N2  . NAG MA 5 .   ? -33.132 14.988  38.406   1.00 263.32 ? 2004 NAG B N2  1 
HETATM 23248 O  O3  . NAG MA 5 .   ? -32.243 17.710  38.656   1.00 269.83 ? 2004 NAG B O3  1 
HETATM 23249 O  O4  . NAG MA 5 .   ? -30.424 18.192  40.849   1.00 269.85 ? 2004 NAG B O4  1 
HETATM 23250 O  O5  . NAG MA 5 .   ? -32.365 15.319  42.017   1.00 260.84 ? 2004 NAG B O5  1 
HETATM 23251 O  O6  . NAG MA 5 .   ? -31.194 15.734  44.329   1.00 239.17 ? 2004 NAG B O6  1 
HETATM 23252 O  O7  . NAG MA 5 .   ? -35.249 15.674  38.143   1.00 234.87 ? 2004 NAG B O7  1 
HETATM 23253 C  C1  . NAG NA 5 .   ? -37.111 -15.447 -59.690  1.00 218.42 ? 401  NAG C C1  1 
HETATM 23254 C  C2  . NAG NA 5 .   ? -37.108 -16.577 -60.719  1.00 249.03 ? 401  NAG C C2  1 
HETATM 23255 C  C3  . NAG NA 5 .   ? -38.273 -16.415 -61.700  1.00 257.47 ? 401  NAG C C3  1 
HETATM 23256 C  C4  . NAG NA 5 .   ? -39.591 -16.235 -60.954  1.00 278.74 ? 401  NAG C C4  1 
HETATM 23257 C  C5  . NAG NA 5 .   ? -39.454 -15.109 -59.933  1.00 265.24 ? 401  NAG C C5  1 
HETATM 23258 C  C6  . NAG NA 5 .   ? -40.680 -14.926 -59.071  1.00 271.87 ? 401  NAG C C6  1 
HETATM 23259 C  C7  . NAG NA 5 .   ? -34.758 -17.242 -60.963  1.00 219.61 ? 401  NAG C C7  1 
HETATM 23260 C  C8  . NAG NA 5 .   ? -33.540 -17.189 -61.833  1.00 181.18 ? 401  NAG C C8  1 
HETATM 23261 N  N2  . NAG NA 5 .   ? -35.843 -16.620 -61.435  1.00 240.54 ? 401  NAG C N2  1 
HETATM 23262 O  O3  . NAG NA 5 .   ? -38.334 -17.555 -62.550  1.00 238.45 ? 401  NAG C O3  1 
HETATM 23263 O  O4  . NAG NA 5 .   ? -40.629 -15.880 -61.860  1.00 272.90 ? 401  NAG C O4  1 
HETATM 23264 O  O5  . NAG NA 5 .   ? -38.367 -15.394 -59.045  1.00 233.74 ? 401  NAG C O5  1 
HETATM 23265 O  O6  . NAG NA 5 .   ? -40.529 -13.819 -58.192  1.00 266.79 ? 401  NAG C O6  1 
HETATM 23266 O  O7  . NAG NA 5 .   ? -34.760 -17.820 -59.883  1.00 215.13 ? 401  NAG C O7  1 
HETATM 23267 C  C1  . NAG OA 5 .   ? -41.394 -17.018 -62.293  1.00 265.74 ? 402  NAG C C1  1 
HETATM 23268 C  C2  . NAG OA 5 .   ? -42.833 -16.898 -61.768  1.00 295.19 ? 402  NAG C C2  1 
HETATM 23269 C  C3  . NAG OA 5 .   ? -43.712 -17.999 -62.357  1.00 295.55 ? 402  NAG C C3  1 
HETATM 23270 C  C4  . NAG OA 5 .   ? -43.623 -17.994 -63.876  1.00 280.93 ? 402  NAG C C4  1 
HETATM 23271 C  C5  . NAG OA 5 .   ? -42.165 -18.133 -64.296  1.00 262.93 ? 402  NAG C C5  1 
HETATM 23272 C  C6  . NAG OA 5 .   ? -41.968 -18.067 -65.792  1.00 282.40 ? 402  NAG C C6  1 
HETATM 23273 C  C7  . NAG OA 5 .   ? -43.855 -16.421 -59.585  1.00 310.34 ? 402  NAG C C7  1 
HETATM 23274 C  C8  . NAG OA 5 .   ? -43.728 -16.572 -58.099  1.00 292.74 ? 402  NAG C C8  1 
HETATM 23275 N  N2  . NAG OA 5 .   ? -42.865 -16.949 -60.314  1.00 298.47 ? 402  NAG C N2  1 
HETATM 23276 O  O3  . NAG OA 5 .   ? -45.061 -17.806 -61.948  1.00 307.08 ? 402  NAG C O3  1 
HETATM 23277 O  O4  . NAG OA 5 .   ? -44.396 -19.058 -64.418  1.00 264.45 ? 402  NAG C O4  1 
HETATM 23278 O  O5  . NAG OA 5 .   ? -41.403 -17.058 -63.731  1.00 257.54 ? 402  NAG C O5  1 
HETATM 23279 O  O6  . NAG OA 5 .   ? -41.000 -19.010 -66.229  1.00 291.30 ? 402  NAG C O6  1 
HETATM 23280 O  O7  . NAG OA 5 .   ? -44.809 -15.848 -60.102  1.00 311.77 ? 402  NAG C O7  1 
HETATM 23281 C  C1  . BMA PA 6 .   ? -45.509 -18.491 -65.139  1.00 271.76 ? 403  BMA C C1  1 
HETATM 23282 C  C2  . BMA PA 6 .   ? -46.116 -19.522 -66.089  1.00 288.85 ? 403  BMA C C2  1 
HETATM 23283 C  C3  . BMA PA 6 .   ? -47.195 -18.825 -66.920  1.00 281.69 ? 403  BMA C C3  1 
HETATM 23284 C  C4  . BMA PA 6 .   ? -48.218 -18.130 -66.003  1.00 273.46 ? 403  BMA C C4  1 
HETATM 23285 C  C5  . BMA PA 6 .   ? -47.503 -17.183 -65.018  1.00 260.28 ? 403  BMA C C5  1 
HETATM 23286 C  C6  . BMA PA 6 .   ? -48.450 -16.573 -64.005  1.00 253.76 ? 403  BMA C C6  1 
HETATM 23287 O  O2  . BMA PA 6 .   ? -46.769 -20.552 -65.359  1.00 287.54 ? 403  BMA C O2  1 
HETATM 23288 O  O3  . BMA PA 6 .   ? -47.877 -19.709 -67.817  1.00 275.29 ? 403  BMA C O3  1 
HETATM 23289 O  O4  . BMA PA 6 .   ? -49.142 -17.390 -66.780  1.00 253.79 ? 403  BMA C O4  1 
HETATM 23290 O  O5  . BMA PA 6 .   ? -46.499 -17.927 -64.302  1.00 266.40 ? 403  BMA C O5  1 
HETATM 23291 O  O6  . BMA PA 6 .   ? -47.697 -15.739 -63.140  1.00 246.16 ? 403  BMA C O6  1 
HETATM 23292 C  C1  . MAN QA 7 .   ? -46.959 -20.536 -68.562  1.00 263.13 ? 404  MAN C C1  1 
HETATM 23293 C  C2  . MAN QA 7 .   ? -46.192 -19.706 -69.638  1.00 239.51 ? 404  MAN C C2  1 
HETATM 23294 C  C3  . MAN QA 7 .   ? -47.039 -19.506 -70.895  1.00 247.88 ? 404  MAN C C3  1 
HETATM 23295 C  C4  . MAN QA 7 .   ? -47.732 -20.813 -71.329  1.00 253.91 ? 404  MAN C C4  1 
HETATM 23296 C  C5  . MAN QA 7 .   ? -48.540 -21.375 -70.150  1.00 252.80 ? 404  MAN C C5  1 
HETATM 23297 C  C6  . MAN QA 7 .   ? -49.295 -22.662 -70.472  1.00 218.22 ? 404  MAN C C6  1 
HETATM 23298 O  O2  . MAN QA 7 .   ? -45.003 -20.375 -70.080  1.00 219.12 ? 404  MAN C O2  1 
HETATM 23299 O  O3  . MAN QA 7 .   ? -46.259 -18.982 -71.966  1.00 227.21 ? 404  MAN C O3  1 
HETATM 23300 O  O4  . MAN QA 7 .   ? -48.596 -20.554 -72.418  1.00 266.59 ? 404  MAN C O4  1 
HETATM 23301 O  O5  . MAN QA 7 .   ? -47.617 -21.662 -69.084  1.00 253.56 ? 404  MAN C O5  1 
HETATM 23302 O  O6  . MAN QA 7 .   ? -50.576 -22.326 -71.008  1.00 206.97 ? 404  MAN C O6  1 
HETATM 23303 C  C1  . NAG RA 5 .   ? -28.192 2.891   -3.828   1.00 193.48 ? 401  NAG D C1  1 
HETATM 23304 C  C2  . NAG RA 5 .   ? -27.234 2.638   -2.663   1.00 222.48 ? 401  NAG D C2  1 
HETATM 23305 C  C3  . NAG RA 5 .   ? -27.188 3.856   -1.748   1.00 233.44 ? 401  NAG D C3  1 
HETATM 23306 C  C4  . NAG RA 5 .   ? -26.855 5.103   -2.555   1.00 241.70 ? 401  NAG D C4  1 
HETATM 23307 C  C5  . NAG RA 5 .   ? -27.846 5.249   -3.708   1.00 238.11 ? 401  NAG D C5  1 
HETATM 23308 C  C6  . NAG RA 5 .   ? -27.537 6.396   -4.641   1.00 252.75 ? 401  NAG D C6  1 
HETATM 23309 C  C7  . NAG RA 5 .   ? -26.869 0.338   -1.866   1.00 223.29 ? 401  NAG D C7  1 
HETATM 23310 C  C8  . NAG RA 5 .   ? -25.584 0.372   -2.640   1.00 218.24 ? 401  NAG D C8  1 
HETATM 23311 N  N2  . NAG RA 5 .   ? -27.616 1.448   -1.916   1.00 231.41 ? 401  NAG D N2  1 
HETATM 23312 O  O3  . NAG RA 5 .   ? -26.214 3.654   -0.731   1.00 249.50 ? 401  NAG D O3  1 
HETATM 23313 O  O4  . NAG RA 5 .   ? -26.887 6.252   -1.716   1.00 229.72 ? 401  NAG D O4  1 
HETATM 23314 O  O5  . NAG RA 5 .   ? -27.809 4.065   -4.514   1.00 222.35 ? 401  NAG D O5  1 
HETATM 23315 O  O6  . NAG RA 5 .   ? -27.803 6.039   -5.990   1.00 259.61 ? 401  NAG D O6  1 
HETATM 23316 O  O7  . NAG RA 5 .   ? -27.215 -0.650  -1.226   1.00 194.38 ? 401  NAG D O7  1 
HETATM 23317 C  C1  . NAG SA 5 .   ? -25.606 6.891   -1.868   1.00 241.46 ? 402  NAG D C1  1 
HETATM 23318 C  C2  . NAG SA 5 .   ? -25.514 8.181   -1.070   1.00 223.99 ? 402  NAG D C2  1 
HETATM 23319 C  C3  . NAG SA 5 .   ? -24.193 8.882   -1.364   1.00 233.30 ? 402  NAG D C3  1 
HETATM 23320 C  C4  . NAG SA 5 .   ? -23.016 7.930   -1.185   1.00 235.28 ? 402  NAG D C4  1 
HETATM 23321 C  C5  . NAG SA 5 .   ? -23.256 6.613   -1.923   1.00 236.15 ? 402  NAG D C5  1 
HETATM 23322 C  C6  . NAG SA 5 .   ? -22.203 5.567   -1.641   1.00 213.46 ? 402  NAG D C6  1 
HETATM 23323 C  C7  . NAG SA 5 .   ? -27.298 9.746   -0.442   1.00 208.38 ? 402  NAG D C7  1 
HETATM 23324 C  C8  . NAG SA 5 .   ? -28.416 10.610  -0.938   1.00 202.83 ? 402  NAG D C8  1 
HETATM 23325 N  N2  . NAG SA 5 .   ? -26.631 9.060   -1.375   1.00 207.71 ? 402  NAG D N2  1 
HETATM 23326 O  O3  . NAG SA 5 .   ? -24.057 10.006  -0.501   1.00 211.69 ? 402  NAG D O3  1 
HETATM 23327 O  O4  . NAG SA 5 .   ? -21.838 8.531   -1.711   1.00 240.43 ? 402  NAG D O4  1 
HETATM 23328 O  O5  . NAG SA 5 .   ? -24.518 6.051   -1.539   1.00 242.14 ? 402  NAG D O5  1 
HETATM 23329 O  O6  . NAG SA 5 .   ? -21.301 5.440   -2.733   1.00 188.33 ? 402  NAG D O6  1 
HETATM 23330 O  O7  . NAG SA 5 .   ? -27.012 9.672   0.748    1.00 199.51 ? 402  NAG D O7  1 
HETATM 23331 C  C1  . BMA TA 6 .   ? -20.957 8.907   -0.635   1.00 235.54 ? 403  BMA D C1  1 
HETATM 23332 C  C2  . BMA TA 6 .   ? -19.547 8.408   -0.965   1.00 225.75 ? 403  BMA D C2  1 
HETATM 23333 C  C3  . BMA TA 6 .   ? -18.553 8.894   0.088    1.00 230.95 ? 403  BMA D C3  1 
HETATM 23334 C  C4  . BMA TA 6 .   ? -18.691 10.384  0.367    1.00 238.08 ? 403  BMA D C4  1 
HETATM 23335 C  C5  . BMA TA 6 .   ? -20.112 10.718  0.726    1.00 228.60 ? 403  BMA D C5  1 
HETATM 23336 C  C6  . BMA TA 6 .   ? -20.341 12.207  0.943    1.00 232.41 ? 403  BMA D C6  1 
HETATM 23337 O  O2  . BMA TA 6 .   ? -19.107 8.929   -2.206   1.00 193.72 ? 403  BMA D O2  1 
HETATM 23338 O  O3  . BMA TA 6 .   ? -17.217 8.602   -0.309   1.00 228.57 ? 403  BMA D O3  1 
HETATM 23339 O  O4  . BMA TA 6 .   ? -17.875 10.716  1.485    1.00 230.35 ? 403  BMA D O4  1 
HETATM 23340 O  O5  . BMA TA 6 .   ? -20.960 10.305  -0.372   1.00 242.45 ? 403  BMA D O5  1 
HETATM 23341 O  O6  . BMA TA 6 .   ? -21.316 12.680  0.012    1.00 230.97 ? 403  BMA D O6  1 
HETATM 23342 C  C1  . MAN UA 7 .   ? -16.814 7.309   0.153    1.00 219.85 ? 404  MAN D C1  1 
HETATM 23343 C  C2  . MAN UA 7 .   ? -16.381 7.468   1.604    1.00 225.62 ? 404  MAN D C2  1 
HETATM 23344 C  C3  . MAN UA 7 .   ? -15.037 8.173   1.654    1.00 204.37 ? 404  MAN D C3  1 
HETATM 23345 C  C4  . MAN UA 7 .   ? -14.017 7.478   0.742    1.00 192.91 ? 404  MAN D C4  1 
HETATM 23346 C  C5  . MAN UA 7 .   ? -14.550 7.438   -0.684   1.00 208.76 ? 404  MAN D C5  1 
HETATM 23347 C  C6  . MAN UA 7 .   ? -13.624 6.693   -1.635   1.00 225.20 ? 404  MAN D C6  1 
HETATM 23348 O  O2  . MAN UA 7 .   ? -16.176 6.203   2.232    1.00 220.93 ? 404  MAN D O2  1 
HETATM 23349 O  O3  . MAN UA 7 .   ? -14.544 8.235   2.978    1.00 205.31 ? 404  MAN D O3  1 
HETATM 23350 O  O4  . MAN UA 7 .   ? -12.812 8.196   0.753    1.00 156.71 ? 404  MAN D O4  1 
HETATM 23351 O  O5  . MAN UA 7 .   ? -15.815 6.748   -0.671   1.00 226.48 ? 404  MAN D O5  1 
HETATM 23352 O  O6  . MAN UA 7 .   ? -14.077 6.904   -2.970   1.00 234.45 ? 404  MAN D O6  1 
HETATM 23353 CA CA  . CA  VA 4 .   ? -7.156  -75.640 -39.865  1.00 218.77 ? 2001 CA  E CA  1 
HETATM 23354 CA CA  . CA  WA 4 .   ? -12.805 -66.616 -47.963  1.00 256.42 ? 2002 CA  E CA  1 
HETATM 23355 CA CA  . CA  XA 4 .   ? -21.643 -57.384 -43.405  1.00 219.87 ? 2003 CA  E CA  1 
HETATM 23356 CA CA  . CA  YA 4 .   ? -9.115  -78.946 -25.555  1.00 225.57 ? 2004 CA  E CA  1 
HETATM 23357 C  C1  . NAG ZA 5 .   ? -7.683  -35.197 -18.765  1.00 179.89 ? 2005 NAG E C1  1 
HETATM 23358 C  C2  . NAG ZA 5 .   ? -6.904  -34.616 -19.939  1.00 195.72 ? 2005 NAG E C2  1 
HETATM 23359 C  C3  . NAG ZA 5 .   ? -5.527  -34.143 -19.476  1.00 186.05 ? 2005 NAG E C3  1 
HETATM 23360 C  C4  . NAG ZA 5 .   ? -5.645  -33.217 -18.271  1.00 216.02 ? 2005 NAG E C4  1 
HETATM 23361 C  C5  . NAG ZA 5 .   ? -6.528  -33.833 -17.188  1.00 214.56 ? 2005 NAG E C5  1 
HETATM 23362 C  C6  . NAG ZA 5 .   ? -6.835  -32.876 -16.058  1.00 180.85 ? 2005 NAG E C6  1 
HETATM 23363 C  C7  . NAG ZA 5 .   ? -7.715  -35.773 -21.946  1.00 222.13 ? 2005 NAG E C7  1 
HETATM 23364 C  C8  . NAG ZA 5 .   ? -7.419  -36.817 -22.978  1.00 203.12 ? 2005 NAG E C8  1 
HETATM 23365 N  N2  . NAG ZA 5 .   ? -6.777  -35.589 -21.012  1.00 218.97 ? 2005 NAG E N2  1 
HETATM 23366 O  O3  . NAG ZA 5 .   ? -4.884  -33.457 -20.544  1.00 157.61 ? 2005 NAG E O3  1 
HETATM 23367 O  O4  . NAG ZA 5 .   ? -4.355  -32.992 -17.714  1.00 206.35 ? 2005 NAG E O4  1 
HETATM 23368 O  O5  . NAG ZA 5 .   ? -7.791  -34.226 -17.742  1.00 215.27 ? 2005 NAG E O5  1 
HETATM 23369 O  O6  . NAG ZA 5 .   ? -7.771  -33.432 -15.144  1.00 163.35 ? 2005 NAG E O6  1 
HETATM 23370 O  O7  . NAG ZA 5 .   ? -8.756  -35.126 -21.957  1.00 230.75 ? 2005 NAG E O7  1 
HETATM 23371 C  C1  . NAG AB 5 .   ? -3.977  -31.627 -17.942  1.00 183.83 ? 2006 NAG E C1  1 
HETATM 23372 C  C2  . NAG AB 5 .   ? -3.248  -31.087 -16.718  1.00 190.75 ? 2006 NAG E C2  1 
HETATM 23373 C  C3  . NAG AB 5 .   ? -2.791  -29.653 -16.966  1.00 184.63 ? 2006 NAG E C3  1 
HETATM 23374 C  C4  . NAG AB 5 .   ? -1.989  -29.547 -18.258  1.00 204.88 ? 2006 NAG E C4  1 
HETATM 23375 C  C5  . NAG AB 5 .   ? -2.763  -30.195 -19.410  1.00 196.18 ? 2006 NAG E C5  1 
HETATM 23376 C  C6  . NAG AB 5 .   ? -1.966  -30.306 -20.690  1.00 201.46 ? 2006 NAG E C6  1 
HETATM 23377 C  C7  . NAG AB 5 .   ? -3.775  -31.830 -14.435  1.00 185.36 ? 2006 NAG E C7  1 
HETATM 23378 C  C8  . NAG AB 5 .   ? -4.770  -31.776 -13.316  1.00 184.36 ? 2006 NAG E C8  1 
HETATM 23379 N  N2  . NAG AB 5 .   ? -4.098  -31.150 -15.540  1.00 187.02 ? 2006 NAG E N2  1 
HETATM 23380 O  O3  . NAG AB 5 .   ? -2.001  -29.216 -15.865  1.00 181.11 ? 2006 NAG E O3  1 
HETATM 23381 O  O4  . NAG AB 5 .   ? -1.802  -28.163 -18.541  1.00 214.42 ? 2006 NAG E O4  1 
HETATM 23382 O  O5  . NAG AB 5 .   ? -3.143  -31.535 -19.067  1.00 186.79 ? 2006 NAG E O5  1 
HETATM 23383 O  O6  . NAG AB 5 .   ? -2.407  -31.407 -21.474  1.00 185.57 ? 2006 NAG E O6  1 
HETATM 23384 O  O7  . NAG AB 5 .   ? -2.729  -32.460 -14.344  1.00 191.90 ? 2006 NAG E O7  1 
HETATM 23385 C  C1  . BMA BB 6 .   ? -0.452  -27.746 -18.846  1.00 224.36 ? 2007 BMA E C1  1 
HETATM 23386 C  C2  . BMA BB 6 .   ? -0.540  -27.092 -20.235  1.00 224.17 ? 2007 BMA E C2  1 
HETATM 23387 C  C3  . BMA BB 6 .   ? 0.759   -26.364 -20.611  1.00 205.63 ? 2007 BMA E C3  1 
HETATM 23388 C  C4  . BMA BB 6 .   ? 1.211   -25.445 -19.485  1.00 208.33 ? 2007 BMA E C4  1 
HETATM 23389 C  C5  . BMA BB 6 .   ? 1.358   -26.267 -18.190  1.00 231.24 ? 2007 BMA E C5  1 
HETATM 23390 C  C6  . BMA BB 6 .   ? 1.804   -25.422 -17.008  1.00 226.16 ? 2007 BMA E C6  1 
HETATM 23391 O  O2  . BMA BB 6 .   ? -1.568  -26.111 -20.223  1.00 230.24 ? 2007 BMA E O2  1 
HETATM 23392 O  O3  . BMA BB 6 .   ? 0.632   -25.616 -21.826  1.00 195.97 ? 2007 BMA E O3  1 
HETATM 23393 O  O4  . BMA BB 6 .   ? 2.455   -24.844 -19.835  1.00 209.23 ? 2007 BMA E O4  1 
HETATM 23394 O  O5  . BMA BB 6 .   ? 0.068   -26.854 -17.868  1.00 228.68 ? 2007 BMA E O5  1 
HETATM 23395 O  O6  . BMA BB 6 .   ? 2.473   -26.269 -16.080  1.00 223.60 ? 2007 BMA E O6  1 
HETATM 23396 C  C1  . NAG CB 5 .   ? -5.070  -82.965 -18.115  1.00 210.59 ? 2008 NAG E C1  1 
HETATM 23397 C  C2  . NAG CB 5 .   ? -4.742  -84.380 -17.654  1.00 244.83 ? 2008 NAG E C2  1 
HETATM 23398 C  C3  . NAG CB 5 .   ? -4.047  -85.148 -18.773  1.00 235.41 ? 2008 NAG E C3  1 
HETATM 23399 C  C4  . NAG CB 5 .   ? -4.884  -85.096 -20.044  1.00 229.11 ? 2008 NAG E C4  1 
HETATM 23400 C  C5  . NAG CB 5 .   ? -5.245  -83.653 -20.390  1.00 217.25 ? 2008 NAG E C5  1 
HETATM 23401 C  C6  . NAG CB 5 .   ? -6.208  -83.548 -21.549  1.00 221.59 ? 2008 NAG E C6  1 
HETATM 23402 C  C7  . NAG CB 5 .   ? -4.430  -84.590 -15.230  1.00 283.02 ? 2008 NAG E C7  1 
HETATM 23403 C  C8  . NAG CB 5 .   ? -3.450  -84.545 -14.097  1.00 266.88 ? 2008 NAG E C8  1 
HETATM 23404 N  N2  . NAG CB 5 .   ? -3.927  -84.370 -16.450  1.00 275.47 ? 2008 NAG E N2  1 
HETATM 23405 O  O3  . NAG CB 5 .   ? -3.854  -86.499 -18.371  1.00 235.96 ? 2008 NAG E O3  1 
HETATM 23406 O  O4  . NAG CB 5 .   ? -4.162  -85.660 -21.131  1.00 227.62 ? 2008 NAG E O4  1 
HETATM 23407 O  O5  . NAG CB 5 .   ? -5.884  -83.021 -19.272  1.00 210.30 ? 2008 NAG E O5  1 
HETATM 23408 O  O6  . NAG CB 5 .   ? -7.281  -82.665 -21.252  1.00 216.95 ? 2008 NAG E O6  1 
HETATM 23409 O  O7  . NAG CB 5 .   ? -5.623  -84.814 -15.050  1.00 277.99 ? 2008 NAG E O7  1 
HETATM 23410 C  C1  . NAG DB 5 .   ? -4.763  -86.925 -21.445  1.00 243.66 ? 2009 NAG E C1  1 
HETATM 23411 C  C2  . NAG DB 5 .   ? -4.843  -87.109 -22.955  1.00 260.94 ? 2009 NAG E C2  1 
HETATM 23412 C  C3  . NAG DB 5 .   ? -5.464  -88.461 -23.291  1.00 271.12 ? 2009 NAG E C3  1 
HETATM 23413 C  C4  . NAG DB 5 .   ? -4.767  -89.589 -22.543  1.00 262.84 ? 2009 NAG E C4  1 
HETATM 23414 C  C5  . NAG DB 5 .   ? -4.645  -89.264 -21.054  1.00 251.27 ? 2009 NAG E C5  1 
HETATM 23415 C  C6  . NAG DB 5 .   ? -3.796  -90.256 -20.294  1.00 242.16 ? 2009 NAG E C6  1 
HETATM 23416 C  C7  . NAG DB 5 .   ? -5.490  -85.701 -24.859  1.00 244.65 ? 2009 NAG E C7  1 
HETATM 23417 C  C8  . NAG DB 5 .   ? -6.368  -84.583 -25.328  1.00 234.96 ? 2009 NAG E C8  1 
HETATM 23418 N  N2  . NAG DB 5 .   ? -5.609  -86.037 -23.570  1.00 250.27 ? 2009 NAG E N2  1 
HETATM 23419 O  O3  . NAG DB 5 .   ? -5.380  -88.692 -24.693  1.00 275.44 ? 2009 NAG E O3  1 
HETATM 23420 O  O4  . NAG DB 5 .   ? -5.550  -90.766 -22.696  1.00 268.76 ? 2009 NAG E O4  1 
HETATM 23421 O  O5  . NAG DB 5 .   ? -4.027  -87.983 -20.879  1.00 252.88 ? 2009 NAG E O5  1 
HETATM 23422 O  O6  . NAG DB 5 .   ? -4.184  -90.333 -18.929  1.00 223.72 ? 2009 NAG E O6  1 
HETATM 23423 O  O7  . NAG DB 5 .   ? -4.707  -86.274 -25.610  1.00 228.78 ? 2009 NAG E O7  1 
HETATM 23424 C  C1  . BMA EB 6 .   ? -4.802  -91.807 -23.339  1.00 270.63 ? 2010 BMA E C1  1 
HETATM 23425 C  C2  . BMA EB 6 .   ? -4.824  -92.955 -22.373  1.00 279.46 ? 2010 BMA E C2  1 
HETATM 23426 C  C3  . BMA EB 6 .   ? -4.032  -94.105 -22.986  1.00 283.77 ? 2010 BMA E C3  1 
HETATM 23427 C  C4  . BMA EB 6 .   ? -4.638  -94.524 -24.346  1.00 280.45 ? 2010 BMA E C4  1 
HETATM 23428 C  C5  . BMA EB 6 .   ? -4.699  -93.278 -25.284  1.00 284.80 ? 2010 BMA E C5  1 
HETATM 23429 C  C6  . BMA EB 6 .   ? -5.451  -93.533 -26.597  1.00 285.74 ? 2010 BMA E C6  1 
HETATM 23430 O  O2  . BMA EB 6 .   ? -6.176  -93.372 -22.200  1.00 260.20 ? 2010 BMA E O2  1 
HETATM 23431 O  O3  . BMA EB 6 .   ? -3.767  -95.217 -22.057  1.00 289.50 ? 2010 BMA E O3  1 
HETATM 23432 O  O4  . BMA EB 6 .   ? -3.842  -95.531 -24.946  1.00 263.92 ? 2010 BMA E O4  1 
HETATM 23433 O  O5  . BMA EB 6 .   ? -5.354  -92.176 -24.592  1.00 276.91 ? 2010 BMA E O5  1 
HETATM 23434 O  O6  . BMA EB 6 .   ? -5.344  -92.375 -27.450  1.00 294.56 ? 2010 BMA E O6  1 
HETATM 23435 C  C1  . MAN FB 7 .   ? -6.580  -91.623 -27.419  1.00 292.22 ? 2011 MAN E C1  1 
HETATM 23436 C  C2  . MAN FB 7 .   ? -7.562  -92.073 -28.545  1.00 283.03 ? 2011 MAN E C2  1 
HETATM 23437 C  C3  . MAN FB 7 .   ? -7.379  -91.245 -29.832  1.00 295.55 ? 2011 MAN E C3  1 
HETATM 23438 C  C4  . MAN FB 7 .   ? -7.271  -89.750 -29.527  1.00 293.34 ? 2011 MAN E C4  1 
HETATM 23439 C  C5  . MAN FB 7 .   ? -6.094  -89.539 -28.593  1.00 281.28 ? 2011 MAN E C5  1 
HETATM 23440 C  C6  . MAN FB 7 .   ? -5.828  -88.072 -28.270  1.00 258.14 ? 2011 MAN E C6  1 
HETATM 23441 O  O2  . MAN FB 7 .   ? -8.927  -91.881 -28.152  1.00 263.97 ? 2011 MAN E O2  1 
HETATM 23442 O  O3  . MAN FB 7 .   ? -8.433  -91.474 -30.760  1.00 305.01 ? 2011 MAN E O3  1 
HETATM 23443 O  O4  . MAN FB 7 .   ? -7.064  -89.021 -30.728  1.00 279.03 ? 2011 MAN E O4  1 
HETATM 23444 O  O5  . MAN FB 7 .   ? -6.387  -90.214 -27.346  1.00 298.16 ? 2011 MAN E O5  1 
HETATM 23445 O  O6  . MAN FB 7 .   ? -5.725  -87.317 -29.488  1.00 224.68 ? 2011 MAN E O6  1 
HETATM 23446 C  C1  . MAN GB 7 .   ? -4.403  -87.406 -30.063  1.00 229.14 ? 2012 MAN E C1  1 
HETATM 23447 C  C2  . MAN GB 7 .   ? -3.281  -87.452 -28.978  1.00 229.19 ? 2012 MAN E C2  1 
HETATM 23448 C  C3  . MAN GB 7 .   ? -2.876  -86.047 -28.527  1.00 248.14 ? 2012 MAN E C3  1 
HETATM 23449 C  C4  . MAN GB 7 .   ? -2.687  -85.107 -29.728  1.00 254.00 ? 2012 MAN E C4  1 
HETATM 23450 C  C5  . MAN GB 7 .   ? -3.972  -85.090 -30.552  1.00 235.16 ? 2012 MAN E C5  1 
HETATM 23451 C  C6  . MAN GB 7 .   ? -3.906  -84.156 -31.738  1.00 199.34 ? 2012 MAN E C6  1 
HETATM 23452 O  O2  . MAN GB 7 .   ? -2.092  -88.077 -29.462  1.00 217.84 ? 2012 MAN E O2  1 
HETATM 23453 O  O3  . MAN GB 7 .   ? -1.705  -86.084 -27.722  1.00 233.67 ? 2012 MAN E O3  1 
HETATM 23454 O  O4  . MAN GB 7 .   ? -2.399  -83.791 -29.290  1.00 263.64 ? 2012 MAN E O4  1 
HETATM 23455 O  O5  . MAN GB 7 .   ? -4.198  -86.421 -31.052  1.00 236.70 ? 2012 MAN E O5  1 
HETATM 23456 O  O6  . MAN GB 7 .   ? -5.235  -83.734 -32.022  1.00 170.41 ? 2012 MAN E O6  1 
HETATM 23457 C  C1  . MAN HB 7 .   ? -4.896  -96.049 -21.703  1.00 286.19 ? 2013 MAN E C1  1 
HETATM 23458 C  C2  . MAN HB 7 .   ? -5.397  -95.732 -20.243  1.00 248.17 ? 2013 MAN E C2  1 
HETATM 23459 C  C3  . MAN HB 7 .   ? -4.522  -96.420 -19.182  1.00 253.41 ? 2013 MAN E C3  1 
HETATM 23460 C  C4  . MAN HB 7 .   ? -4.227  -97.877 -19.559  1.00 262.94 ? 2013 MAN E C4  1 
HETATM 23461 C  C5  . MAN HB 7 .   ? -3.594  -97.890 -20.953  1.00 277.90 ? 2013 MAN E C5  1 
HETATM 23462 C  C6  . MAN HB 7 .   ? -3.127  -99.257 -21.422  1.00 284.56 ? 2013 MAN E C6  1 
HETATM 23463 O  O2  . MAN HB 7 .   ? -6.733  -96.196 -20.006  1.00 228.02 ? 2013 MAN E O2  1 
HETATM 23464 O  O3  . MAN HB 7 .   ? -5.111  -96.350 -17.885  1.00 252.88 ? 2013 MAN E O3  1 
HETATM 23465 O  O4  . MAN HB 7 .   ? -3.328  -98.439 -18.617  1.00 242.09 ? 2013 MAN E O4  1 
HETATM 23466 O  O5  . MAN HB 7 .   ? -4.588  -97.404 -21.879  1.00 286.20 ? 2013 MAN E O5  1 
HETATM 23467 O  O6  . MAN HB 7 .   ? -3.339  -99.339 -22.831  1.00 279.38 ? 2013 MAN E O6  1 
HETATM 23468 C  C1  . NAG IB 5 .   ? 6.997   -75.553 -23.740  1.00 157.04 ? 2014 NAG E C1  1 
HETATM 23469 C  C2  . NAG IB 5 .   ? 6.836   -76.828 -22.950  1.00 196.32 ? 2014 NAG E C2  1 
HETATM 23470 C  C3  . NAG IB 5 .   ? 6.512   -76.493 -21.502  1.00 187.38 ? 2014 NAG E C3  1 
HETATM 23471 C  C4  . NAG IB 5 .   ? 7.536   -75.516 -20.934  1.00 176.00 ? 2014 NAG E C4  1 
HETATM 23472 C  C5  . NAG IB 5 .   ? 7.789   -74.337 -21.874  1.00 185.94 ? 2014 NAG E C5  1 
HETATM 23473 C  C6  . NAG IB 5 .   ? 9.002   -73.528 -21.477  1.00 201.38 ? 2014 NAG E C6  1 
HETATM 23474 C  C7  . NAG IB 5 .   ? 5.937   -78.995 -23.644  1.00 255.84 ? 2014 NAG E C7  1 
HETATM 23475 C  C8  . NAG IB 5 .   ? 4.778   -79.719 -24.257  1.00 258.65 ? 2014 NAG E C8  1 
HETATM 23476 N  N2  . NAG IB 5 .   ? 5.802   -77.672 -23.524  1.00 229.33 ? 2014 NAG E N2  1 
HETATM 23477 O  O3  . NAG IB 5 .   ? 6.512   -77.695 -20.741  1.00 166.69 ? 2014 NAG E O3  1 
HETATM 23478 O  O4  . NAG IB 5 .   ? 7.050   -74.996 -19.704  1.00 173.70 ? 2014 NAG E O4  1 
HETATM 23479 O  O5  . NAG IB 5 .   ? 8.047   -74.803 -23.204  1.00 172.42 ? 2014 NAG E O5  1 
HETATM 23480 O  O6  . NAG IB 5 .   ? 10.187  -74.308 -21.567  1.00 208.02 ? 2014 NAG E O6  1 
HETATM 23481 O  O7  . NAG IB 5 .   ? 6.949   -79.581 -23.273  1.00 243.23 ? 2014 NAG E O7  1 
HETATM 23482 C  C1  . NAG JB 5 .   ? 8.023   -75.355 -18.719  1.00 196.71 ? 2015 NAG E C1  1 
HETATM 23483 C  C2  . NAG JB 5 .   ? 7.548   -74.962 -17.330  1.00 199.49 ? 2015 NAG E C2  1 
HETATM 23484 C  C3  . NAG JB 5 .   ? 8.596   -75.342 -16.293  1.00 180.90 ? 2015 NAG E C3  1 
HETATM 23485 C  C4  . NAG JB 5 .   ? 8.959   -76.815 -16.428  1.00 219.49 ? 2015 NAG E C4  1 
HETATM 23486 C  C5  . NAG JB 5 .   ? 9.343   -77.142 -17.869  1.00 236.51 ? 2015 NAG E C5  1 
HETATM 23487 C  C6  . NAG JB 5 .   ? 9.569   -78.617 -18.102  1.00 262.54 ? 2015 NAG E C6  1 
HETATM 23488 C  C7  . NAG JB 5 .   ? 6.004   -73.061 -17.149  1.00 199.48 ? 2015 NAG E C7  1 
HETATM 23489 C  C8  . NAG JB 5 .   ? 4.903   -74.080 -17.110  1.00 199.80 ? 2015 NAG E C8  1 
HETATM 23490 N  N2  . NAG JB 5 .   ? 7.248   -73.541 -17.258  1.00 182.66 ? 2015 NAG E N2  1 
HETATM 23491 O  O3  . NAG JB 5 .   ? 8.080   -75.073 -14.995  1.00 156.38 ? 2015 NAG E O3  1 
HETATM 23492 O  O4  . NAG JB 5 .   ? 10.060  -77.128 -15.584  1.00 219.69 ? 2015 NAG E O4  1 
HETATM 23493 O  O5  . NAG JB 5 .   ? 8.289   -76.745 -18.756  1.00 222.05 ? 2015 NAG E O5  1 
HETATM 23494 O  O6  . NAG JB 5 .   ? 10.674  -79.092 -17.345  1.00 266.47 ? 2015 NAG E O6  1 
HETATM 23495 O  O7  . NAG JB 5 .   ? 5.776   -71.858 -17.085  1.00 203.73 ? 2015 NAG E O7  1 
HETATM 23496 C  C1  . BMA KB 6 .   ? 9.539   -77.786 -14.422  1.00 217.41 ? 2016 BMA E C1  1 
HETATM 23497 C  C2  . BMA KB 6 .   ? 10.550  -78.828 -13.960  1.00 215.15 ? 2016 BMA E C2  1 
HETATM 23498 C  C3  . BMA KB 6 .   ? 10.138  -79.394 -12.606  1.00 190.81 ? 2016 BMA E C3  1 
HETATM 23499 C  C4  . BMA KB 6 .   ? 9.817   -78.291 -11.622  1.00 201.72 ? 2016 BMA E C4  1 
HETATM 23500 C  C5  . BMA KB 6 .   ? 8.734   -77.358 -12.206  1.00 205.52 ? 2016 BMA E C5  1 
HETATM 23501 C  C6  . BMA KB 6 .   ? 8.443   -76.142 -11.347  1.00 218.47 ? 2016 BMA E C6  1 
HETATM 23502 O  O2  . BMA KB 6 .   ? 11.824  -78.224 -13.782  1.00 232.27 ? 2016 BMA E O2  1 
HETATM 23503 O  O3  . BMA KB 6 .   ? 11.141  -80.220 -12.043  1.00 192.23 ? 2016 BMA E O3  1 
HETATM 23504 O  O4  . BMA KB 6 .   ? 9.376   -78.888 -10.421  1.00 193.28 ? 2016 BMA E O4  1 
HETATM 23505 O  O5  . BMA KB 6 .   ? 9.232   -76.837 -13.435  1.00 211.51 ? 2016 BMA E O5  1 
HETATM 23506 O  O6  . BMA KB 6 .   ? 7.284   -76.364 -10.533  1.00 228.82 ? 2016 BMA E O6  1 
HETATM 23507 C  C1  . MAN LB 7 .   ? 11.371  -81.347 -12.901  1.00 208.51 ? 2017 MAN E C1  1 
HETATM 23508 C  C2  . MAN LB 7 .   ? 11.222  -82.636 -12.081  1.00 217.18 ? 2017 MAN E C2  1 
HETATM 23509 C  C3  . MAN LB 7 .   ? 12.440  -82.825 -11.183  1.00 241.92 ? 2017 MAN E C3  1 
HETATM 23510 C  C4  . MAN LB 7 .   ? 13.755  -82.684 -11.983  1.00 238.28 ? 2017 MAN E C4  1 
HETATM 23511 C  C5  . MAN LB 7 .   ? 13.775  -81.332 -12.721  1.00 237.12 ? 2017 MAN E C5  1 
HETATM 23512 C  C6  . MAN LB 7 .   ? 15.022  -81.126 -13.584  1.00 229.44 ? 2017 MAN E C6  1 
HETATM 23513 O  O2  . MAN LB 7 .   ? 11.178  -83.798 -12.911  1.00 213.00 ? 2017 MAN E O2  1 
HETATM 23514 O  O3  . MAN LB 7 .   ? 12.395  -84.076 -10.502  1.00 237.34 ? 2017 MAN E O3  1 
HETATM 23515 O  O4  . MAN LB 7 .   ? 14.867  -82.763 -11.113  1.00 241.22 ? 2017 MAN E O4  1 
HETATM 23516 O  O5  . MAN LB 7 .   ? 12.609  -81.254 -13.573  1.00 223.47 ? 2017 MAN E O5  1 
HETATM 23517 O  O6  . MAN LB 7 .   ? 14.972  -82.002 -14.709  1.00 238.28 ? 2017 MAN E O6  1 
HETATM 23518 C  C1  . MAN MB 7 .   ? 7.678   -76.688 -9.177   1.00 233.82 ? 2018 MAN E C1  1 
HETATM 23519 C  C2  . MAN MB 7 .   ? 6.781   -75.948 -8.115   1.00 237.30 ? 2018 MAN E C2  1 
HETATM 23520 C  C3  . MAN MB 7 .   ? 7.562   -75.140 -7.033   1.00 252.89 ? 2018 MAN E C3  1 
HETATM 23521 C  C4  . MAN MB 7 .   ? 9.043   -75.544 -6.912   1.00 229.88 ? 2018 MAN E C4  1 
HETATM 23522 C  C5  . MAN MB 7 .   ? 9.653   -75.551 -8.279   1.00 219.72 ? 2018 MAN E C5  1 
HETATM 23523 C  C6  . MAN MB 7 .   ? 11.133  -75.799 -8.272   1.00 205.39 ? 2018 MAN E C6  1 
HETATM 23524 O  O2  . MAN MB 7 .   ? 5.958   -76.887 -7.394   1.00 229.80 ? 2018 MAN E O2  1 
HETATM 23525 O  O3  . MAN MB 7 .   ? 6.936   -75.267 -5.758   1.00 264.35 ? 2018 MAN E O3  1 
HETATM 23526 O  O4  . MAN MB 7 .   ? 9.748   -74.614 -6.104   1.00 233.01 ? 2018 MAN E O4  1 
HETATM 23527 O  O5  . MAN MB 7 .   ? 9.090   -76.655 -8.983   1.00 222.74 ? 2018 MAN E O5  1 
HETATM 23528 O  O6  . MAN MB 7 .   ? 11.772  -74.795 -7.511   1.00 217.53 ? 2018 MAN E O6  1 
HETATM 23529 C  C1  . MAN NB 7 .   ? 13.021  -74.456 -8.149   1.00 238.57 ? 2019 MAN E C1  1 
HETATM 23530 C  C2  . MAN NB 7 .   ? 13.836  -75.730 -8.541   1.00 236.45 ? 2019 MAN E C2  1 
HETATM 23531 C  C3  . MAN NB 7 .   ? 14.568  -76.309 -7.336   1.00 241.89 ? 2019 MAN E C3  1 
HETATM 23532 C  C4  . MAN NB 7 .   ? 15.342  -75.215 -6.589   1.00 250.74 ? 2019 MAN E C4  1 
HETATM 23533 C  C5  . MAN NB 7 .   ? 14.373  -74.070 -6.196   1.00 265.67 ? 2019 MAN E C5  1 
HETATM 23534 C  C6  . MAN NB 7 .   ? 15.053  -72.913 -5.477   1.00 261.75 ? 2019 MAN E C6  1 
HETATM 23535 O  O2  . MAN NB 7 .   ? 14.865  -75.428 -9.482   1.00 239.62 ? 2019 MAN E O2  1 
HETATM 23536 O  O3  . MAN NB 7 .   ? 15.445  -77.367 -7.712   1.00 236.88 ? 2019 MAN E O3  1 
HETATM 23537 O  O4  . MAN NB 7 .   ? 15.942  -75.768 -5.428   1.00 253.20 ? 2019 MAN E O4  1 
HETATM 23538 O  O5  . MAN NB 7 .   ? 13.768  -73.535 -7.397   1.00 248.73 ? 2019 MAN E O5  1 
HETATM 23539 O  O6  . MAN NB 7 .   ? 14.053  -71.965 -5.087   1.00 267.29 ? 2019 MAN E O6  1 
HETATM 23540 C  C1  . MAN OB 7 .   ? 6.133   -74.108 -5.470   1.00 285.57 ? 2020 MAN E C1  1 
HETATM 23541 C  C2  . MAN OB 7 .   ? 7.053   -72.961 -5.024   1.00 290.25 ? 2020 MAN E C2  1 
HETATM 23542 C  C3  . MAN OB 7 .   ? 7.643   -73.278 -3.646   1.00 287.43 ? 2020 MAN E C3  1 
HETATM 23543 C  C4  . MAN OB 7 .   ? 6.546   -73.705 -2.652   1.00 259.29 ? 2020 MAN E C4  1 
HETATM 23544 C  C5  . MAN OB 7 .   ? 5.713   -74.845 -3.250   1.00 253.10 ? 2020 MAN E C5  1 
HETATM 23545 C  C6  . MAN OB 7 .   ? 4.560   -75.266 -2.370   1.00 230.16 ? 2020 MAN E C6  1 
HETATM 23546 O  O2  . MAN OB 7 .   ? 6.329   -71.733 -4.866   1.00 308.67 ? 2020 MAN E O2  1 
HETATM 23547 O  O3  . MAN OB 7 .   ? 8.386   -72.180 -3.121   1.00 281.33 ? 2020 MAN E O3  1 
HETATM 23548 O  O4  . MAN OB 7 .   ? 7.135   -74.147 -1.442   1.00 262.93 ? 2020 MAN E O4  1 
HETATM 23549 O  O5  . MAN OB 7 .   ? 5.166   -74.409 -4.510   1.00 253.96 ? 2020 MAN E O5  1 
HETATM 23550 O  O6  . MAN OB 7 .   ? 4.139   -76.554 -2.799   1.00 216.09 ? 2020 MAN E O6  1 
HETATM 23551 C  C1  . NAG PB 5 .   ? -23.979 -69.188 -94.714  1.00 255.33 ? 2021 NAG E C1  1 
HETATM 23552 C  C2  . NAG PB 5 .   ? -23.283 -70.421 -94.150  1.00 287.26 ? 2021 NAG E C2  1 
HETATM 23553 C  C3  . NAG PB 5 .   ? -24.301 -71.352 -93.494  1.00 301.90 ? 2021 NAG E C3  1 
HETATM 23554 C  C4  . NAG PB 5 .   ? -25.147 -70.597 -92.476  1.00 326.79 ? 2021 NAG E C4  1 
HETATM 23555 C  C5  . NAG PB 5 .   ? -25.747 -69.344 -93.115  1.00 318.95 ? 2021 NAG E C5  1 
HETATM 23556 C  C6  . NAG PB 5 .   ? -26.493 -68.470 -92.134  1.00 312.32 ? 2021 NAG E C6  1 
HETATM 23557 C  C7  . NAG PB 5 .   ? -21.222 -71.291 -95.167  1.00 313.51 ? 2021 NAG E C7  1 
HETATM 23558 C  C8  . NAG PB 5 .   ? -20.506 -70.710 -93.985  1.00 297.98 ? 2021 NAG E C8  1 
HETATM 23559 N  N2  . NAG PB 5 .   ? -22.548 -71.121 -95.192  1.00 300.53 ? 2021 NAG E N2  1 
HETATM 23560 O  O3  . NAG PB 5 .   ? -23.613 -72.427 -92.864  1.00 274.37 ? 2021 NAG E O3  1 
HETATM 23561 O  O4  . NAG PB 5 .   ? -26.204 -71.427 -92.005  1.00 320.27 ? 2021 NAG E O4  1 
HETATM 23562 O  O5  . NAG PB 5 .   ? -24.705 -68.534 -93.679  1.00 304.67 ? 2021 NAG E O5  1 
HETATM 23563 O  O6  . NAG PB 5 .   ? -25.649 -67.464 -91.591  1.00 303.97 ? 2021 NAG E O6  1 
HETATM 23564 O  O7  . NAG PB 5 .   ? -20.627 -71.887 -96.059  1.00 328.91 ? 2021 NAG E O7  1 
HETATM 23565 C  C1  . NAG QB 5 .   ? -25.964 -71.853 -90.647  1.00 301.56 ? 2022 NAG E C1  1 
HETATM 23566 C  C2  . NAG QB 5 .   ? -27.254 -71.722 -89.840  1.00 294.38 ? 2022 NAG E C2  1 
HETATM 23567 C  C3  . NAG QB 5 .   ? -27.031 -72.189 -88.404  1.00 293.92 ? 2022 NAG E C3  1 
HETATM 23568 C  C4  . NAG QB 5 .   ? -26.433 -73.589 -88.383  1.00 300.70 ? 2022 NAG E C4  1 
HETATM 23569 C  C5  . NAG QB 5 .   ? -25.185 -73.648 -89.261  1.00 309.27 ? 2022 NAG E C5  1 
HETATM 23570 C  C6  . NAG QB 5 .   ? -24.620 -75.043 -89.395  1.00 300.27 ? 2022 NAG E C6  1 
HETATM 23571 C  C7  . NAG QB 5 .   ? -29.055 -70.059 -89.908  1.00 267.08 ? 2022 NAG E C7  1 
HETATM 23572 C  C8  . NAG QB 5 .   ? -29.397 -68.600 -89.920  1.00 251.93 ? 2022 NAG E C8  1 
HETATM 23573 N  N2  . NAG QB 5 .   ? -27.752 -70.356 -89.861  1.00 261.82 ? 2022 NAG E N2  1 
HETATM 23574 O  O3  . NAG QB 5 .   ? -28.268 -72.174 -87.700  1.00 280.13 ? 2022 NAG E O3  1 
HETATM 23575 O  O4  . NAG QB 5 .   ? -26.088 -73.940 -87.048  1.00 294.69 ? 2022 NAG E O4  1 
HETATM 23576 O  O5  . NAG QB 5 .   ? -25.498 -73.200 -90.588  1.00 313.03 ? 2022 NAG E O5  1 
HETATM 23577 O  O6  . NAG QB 5 .   ? -23.215 -75.015 -89.606  1.00 291.32 ? 2022 NAG E O6  1 
HETATM 23578 O  O7  . NAG QB 5 .   ? -29.918 -70.930 -89.939  1.00 265.96 ? 2022 NAG E O7  1 
HETATM 23579 C  C1  . BMA RB 6 .   ? -26.909 -75.042 -86.621  1.00 295.38 ? 2023 BMA E C1  1 
HETATM 23580 C  C2  . BMA RB 6 .   ? -25.966 -76.148 -86.052  1.00 273.10 ? 2023 BMA E C2  1 
HETATM 23581 C  C3  . BMA RB 6 .   ? -26.702 -77.159 -85.145  1.00 277.58 ? 2023 BMA E C3  1 
HETATM 23582 C  C4  . BMA RB 6 .   ? -27.788 -76.494 -84.287  1.00 288.08 ? 2023 BMA E C4  1 
HETATM 23583 C  C5  . BMA RB 6 .   ? -28.715 -75.731 -85.218  1.00 305.59 ? 2023 BMA E C5  1 
HETATM 23584 C  C6  . BMA RB 6 .   ? -30.012 -75.235 -84.558  1.00 319.95 ? 2023 BMA E C6  1 
HETATM 23585 O  O2  . BMA RB 6 .   ? -24.920 -75.578 -85.279  1.00 276.92 ? 2023 BMA E O2  1 
HETATM 23586 O  O3  . BMA RB 6 .   ? -25.790 -77.868 -84.314  1.00 268.74 ? 2023 BMA E O3  1 
HETATM 23587 O  O4  . BMA RB 6 .   ? -28.523 -77.476 -83.573  1.00 291.33 ? 2023 BMA E O4  1 
HETATM 23588 O  O5  . BMA RB 6 .   ? -27.954 -74.632 -85.736  1.00 283.62 ? 2023 BMA E O5  1 
HETATM 23589 O  O6  . BMA RB 6 .   ? -29.736 -74.248 -83.559  1.00 345.50 ? 2023 BMA E O6  1 
HETATM 23590 C  C1  . MAN SB 7 .   ? -30.905 -73.405 -83.443  1.00 322.87 ? 2024 MAN E C1  1 
HETATM 23591 C  C2  . MAN SB 7 .   ? -30.523 -71.945 -83.043  1.00 270.01 ? 2024 MAN E C2  1 
HETATM 23592 C  C3  . MAN SB 7 .   ? -30.484 -71.776 -81.521  1.00 276.30 ? 2024 MAN E C3  1 
HETATM 23593 C  C4  . MAN SB 7 .   ? -31.768 -72.304 -80.894  1.00 296.18 ? 2024 MAN E C4  1 
HETATM 23594 C  C5  . MAN SB 7 .   ? -31.914 -73.796 -81.226  1.00 320.50 ? 2024 MAN E C5  1 
HETATM 23595 C  C6  . MAN SB 7 .   ? -33.185 -74.398 -80.646  1.00 321.48 ? 2024 MAN E C6  1 
HETATM 23596 O  O2  . MAN SB 7 .   ? -31.502 -71.012 -83.511  1.00 260.35 ? 2024 MAN E O2  1 
HETATM 23597 O  O3  . MAN SB 7 .   ? -30.271 -70.418 -81.133  1.00 260.57 ? 2024 MAN E O3  1 
HETATM 23598 O  O4  . MAN SB 7 .   ? -31.730 -72.123 -79.483  1.00 296.40 ? 2024 MAN E O4  1 
HETATM 23599 O  O5  . MAN SB 7 .   ? -31.962 -73.974 -82.670  1.00 303.71 ? 2024 MAN E O5  1 
HETATM 23600 O  O6  . MAN SB 7 .   ? -33.343 -75.711 -81.170  1.00 321.59 ? 2024 MAN E O6  1 
HETATM 23601 C  C1  . NAG TB 5 .   ? -29.998 -48.395 -71.398  1.00 223.42 ? 2025 NAG E C1  1 
HETATM 23602 C  C2  . NAG TB 5 .   ? -30.399 -47.499 -72.581  1.00 273.21 ? 2025 NAG E C2  1 
HETATM 23603 C  C3  . NAG TB 5 .   ? -29.457 -46.294 -72.682  1.00 261.59 ? 2025 NAG E C3  1 
HETATM 23604 C  C4  . NAG TB 5 .   ? -29.283 -45.615 -71.329  1.00 251.91 ? 2025 NAG E C4  1 
HETATM 23605 C  C5  . NAG TB 5 .   ? -28.935 -46.644 -70.261  1.00 253.07 ? 2025 NAG E C5  1 
HETATM 23606 C  C6  . NAG TB 5 .   ? -28.846 -46.058 -68.872  1.00 244.35 ? 2025 NAG E C6  1 
HETATM 23607 C  C7  . NAG TB 5 .   ? -31.530 -48.565 -74.490  1.00 282.79 ? 2025 NAG E C7  1 
HETATM 23608 C  C8  . NAG TB 5 .   ? -31.347 -49.331 -75.767  1.00 259.22 ? 2025 NAG E C8  1 
HETATM 23609 N  N2  . NAG TB 5 .   ? -30.409 -48.245 -73.831  1.00 293.56 ? 2025 NAG E N2  1 
HETATM 23610 O  O3  . NAG TB 5 .   ? -29.967 -45.364 -73.631  1.00 252.81 ? 2025 NAG E O3  1 
HETATM 23611 O  O4  . NAG TB 5 .   ? -28.224 -44.668 -71.394  1.00 233.69 ? 2025 NAG E O4  1 
HETATM 23612 O  O5  . NAG TB 5 .   ? -29.963 -47.638 -70.221  1.00 250.22 ? 2025 NAG E O5  1 
HETATM 23613 O  O6  . NAG TB 5 .   ? -28.334 -47.006 -67.947  1.00 241.95 ? 2025 NAG E O6  1 
HETATM 23614 O  O7  . NAG TB 5 .   ? -32.641 -48.254 -74.074  1.00 285.88 ? 2025 NAG E O7  1 
HETATM 23615 C  C1  . NAG UB 5 .   ? -11.785 -56.054 -71.412  1.00 256.12 ? 2026 NAG E C1  1 
HETATM 23616 C  C2  . NAG UB 5 .   ? -10.974 -54.962 -72.075  1.00 295.03 ? 2026 NAG E C2  1 
HETATM 23617 C  C3  . NAG UB 5 .   ? -9.489  -55.195 -71.805  1.00 296.73 ? 2026 NAG E C3  1 
HETATM 23618 C  C4  . NAG UB 5 .   ? -9.228  -55.406 -70.317  1.00 308.40 ? 2026 NAG E C4  1 
HETATM 23619 C  C5  . NAG UB 5 .   ? -10.194 -56.434 -69.734  1.00 300.01 ? 2026 NAG E C5  1 
HETATM 23620 C  C6  . NAG UB 5 .   ? -10.100 -56.560 -68.233  1.00 280.69 ? 2026 NAG E C6  1 
HETATM 23621 C  C7  . NAG UB 5 .   ? -10.907 -53.919 -74.299  1.00 328.53 ? 2026 NAG E C7  1 
HETATM 23622 C  C8  . NAG UB 5 .   ? -11.214 -54.096 -75.748  1.00 330.22 ? 2026 NAG E C8  1 
HETATM 23623 N  N2  . NAG UB 5 .   ? -11.223 -54.947 -73.506  1.00 321.59 ? 2026 NAG E N2  1 
HETATM 23624 O  O3  . NAG UB 5 .   ? -8.735  -54.093 -72.298  1.00 294.07 ? 2026 NAG E O3  1 
HETATM 23625 O  O4  . NAG UB 5 .   ? -7.900  -55.873 -70.102  1.00 332.85 ? 2026 NAG E O4  1 
HETATM 23626 O  O5  . NAG UB 5 .   ? -11.539 -56.052 -70.033  1.00 293.09 ? 2026 NAG E O5  1 
HETATM 23627 O  O6  . NAG UB 5 .   ? -9.480  -57.784 -67.865  1.00 270.41 ? 2026 NAG E O6  1 
HETATM 23628 O  O7  . NAG UB 5 .   ? -10.395 -52.894 -73.863  1.00 331.58 ? 2026 NAG E O7  1 
HETATM 23629 C  C1  . NAG VB 5 .   ? -7.093  -54.780 -69.627  1.00 333.35 ? 2027 NAG E C1  1 
HETATM 23630 C  C2  . NAG VB 5 .   ? -6.236  -55.204 -68.430  1.00 324.77 ? 2027 NAG E C2  1 
HETATM 23631 C  C3  . NAG VB 5 .   ? -5.351  -54.045 -67.977  1.00 319.11 ? 2027 NAG E C3  1 
HETATM 23632 C  C4  . NAG VB 5 .   ? -4.554  -53.488 -69.150  1.00 333.05 ? 2027 NAG E C4  1 
HETATM 23633 C  C5  . NAG VB 5 .   ? -5.487  -53.148 -70.310  1.00 330.92 ? 2027 NAG E C5  1 
HETATM 23634 C  C6  . NAG VB 5 .   ? -4.753  -52.712 -71.559  1.00 342.10 ? 2027 NAG E C6  1 
HETATM 23635 C  C7  . NAG VB 5 .   ? -6.690  -56.652 -66.498  1.00 278.06 ? 2027 NAG E C7  1 
HETATM 23636 C  C8  . NAG VB 5 .   ? -7.667  -57.004 -65.415  1.00 251.38 ? 2027 NAG E C8  1 
HETATM 23637 N  N2  . NAG VB 5 .   ? -7.064  -55.673 -67.330  1.00 295.00 ? 2027 NAG E N2  1 
HETATM 23638 O  O3  . NAG VB 5 .   ? -4.466  -54.487 -66.953  1.00 304.85 ? 2027 NAG E O3  1 
HETATM 23639 O  O4  . NAG VB 5 .   ? -3.860  -52.312 -68.748  1.00 331.18 ? 2027 NAG E O4  1 
HETATM 23640 O  O5  . NAG VB 5 .   ? -6.254  -54.304 -70.670  1.00 342.12 ? 2027 NAG E O5  1 
HETATM 23641 O  O6  . NAG VB 5 .   ? -5.189  -53.439 -72.700  1.00 338.69 ? 2027 NAG E O6  1 
HETATM 23642 O  O7  . NAG VB 5 .   ? -5.613  -57.228 -66.614  1.00 272.14 ? 2027 NAG E O7  1 
HETATM 23643 MN MN  . MN  WB 8 .   ? 26.241  -57.299 -10.631  1.00 217.12 ? 2001 MN  F MN  1 
HETATM 23644 MN MN  . MN  XB 8 .   ? 20.415  -53.881 -13.270  1.00 233.67 ? 2002 MN  F MN  1 
HETATM 23645 MN MN  . MN  YB 8 .   ? 14.866  -52.741 -15.060  1.00 213.88 ? 2003 MN  F MN  1 
HETATM 23646 C  C1  . NAG ZB 5 .   ? 32.732  -31.307 -41.046  1.00 272.86 ? 2004 NAG F C1  1 
HETATM 23647 C  C2  . NAG ZB 5 .   ? 31.596  -31.605 -42.019  1.00 272.14 ? 2004 NAG F C2  1 
HETATM 23648 C  C3  . NAG ZB 5 .   ? 31.009  -30.303 -42.556  1.00 279.84 ? 2004 NAG F C3  1 
HETATM 23649 C  C4  . NAG ZB 5 .   ? 30.621  -29.378 -41.408  1.00 272.94 ? 2004 NAG F C4  1 
HETATM 23650 C  C5  . NAG ZB 5 .   ? 31.790  -29.203 -40.439  1.00 272.04 ? 2004 NAG F C5  1 
HETATM 23651 C  C6  . NAG ZB 5 .   ? 31.426  -28.405 -39.209  1.00 269.72 ? 2004 NAG F C6  1 
HETATM 23652 C  C7  . NAG ZB 5 .   ? 31.640  -33.707 -43.288  1.00 263.10 ? 2004 NAG F C7  1 
HETATM 23653 C  C8  . NAG ZB 5 .   ? 32.219  -34.430 -44.466  1.00 269.09 ? 2004 NAG F C8  1 
HETATM 23654 N  N2  . NAG ZB 5 .   ? 32.055  -32.449 -43.111  1.00 270.98 ? 2004 NAG F N2  1 
HETATM 23655 O  O3  . NAG ZB 5 .   ? 29.867  -30.591 -43.355  1.00 284.36 ? 2004 NAG F O3  1 
HETATM 23656 O  O4  . NAG ZB 5 .   ? 30.241  -28.107 -41.923  1.00 278.50 ? 2004 NAG F O4  1 
HETATM 23657 O  O5  . NAG ZB 5 .   ? 32.251  -30.485 -39.984  1.00 270.35 ? 2004 NAG F O5  1 
HETATM 23658 O  O6  . NAG ZB 5 .   ? 32.318  -28.672 -38.136  1.00 265.56 ? 2004 NAG F O6  1 
HETATM 23659 O  O7  . NAG ZB 5 .   ? 30.832  -34.237 -42.534  1.00 258.24 ? 2004 NAG F O7  1 
HETATM 23660 C  C1  . NAG AC 5 .   ? 36.963  -61.688 60.646   1.00 231.88 ? 401  NAG G C1  1 
HETATM 23661 C  C2  . NAG AC 5 .   ? 37.426  -63.156 60.754   1.00 279.81 ? 401  NAG G C2  1 
HETATM 23662 C  C3  . NAG AC 5 .   ? 38.673  -63.279 61.637   1.00 278.86 ? 401  NAG G C3  1 
HETATM 23663 C  C4  . NAG AC 5 .   ? 39.753  -62.311 61.174   1.00 278.11 ? 401  NAG G C4  1 
HETATM 23664 C  C5  . NAG AC 5 .   ? 39.173  -60.905 61.193   1.00 276.54 ? 401  NAG G C5  1 
HETATM 23665 C  C6  . NAG AC 5 .   ? 40.149  -59.836 60.765   1.00 270.97 ? 401  NAG G C6  1 
HETATM 23666 C  C7  . NAG AC 5 .   ? 35.450  -64.589 60.486   1.00 261.60 ? 401  NAG G C7  1 
HETATM 23667 C  C8  . NAG AC 5 .   ? 34.417  -65.417 61.188   1.00 266.77 ? 401  NAG G C8  1 
HETATM 23668 N  N2  . NAG AC 5 .   ? 36.357  -63.996 61.269   1.00 275.09 ? 401  NAG G N2  1 
HETATM 23669 O  O3  . NAG AC 5 .   ? 39.147  -64.620 61.598   1.00 270.57 ? 401  NAG G O3  1 
HETATM 23670 O  O4  . NAG AC 5 .   ? 40.901  -62.373 62.016   1.00 274.38 ? 401  NAG G O4  1 
HETATM 23671 O  O5  . NAG AC 5 .   ? 38.071  -60.853 60.280   1.00 268.45 ? 401  NAG G O5  1 
HETATM 23672 O  O6  . NAG AC 5 .   ? 39.482  -58.645 60.371   1.00 259.45 ? 401  NAG G O6  1 
HETATM 23673 O  O7  . NAG AC 5 .   ? 35.464  -64.463 59.267   1.00 253.69 ? 401  NAG G O7  1 
HETATM 23674 C  C1  . NAG BC 5 .   ? 41.933  -63.197 61.425   1.00 266.93 ? 402  NAG G C1  1 
HETATM 23675 C  C2  . NAG BC 5 .   ? 43.132  -62.347 60.992   1.00 279.55 ? 402  NAG G C2  1 
HETATM 23676 C  C3  . NAG BC 5 .   ? 44.244  -63.234 60.438   1.00 259.28 ? 402  NAG G C3  1 
HETATM 23677 C  C4  . NAG BC 5 .   ? 44.591  -64.358 61.403   1.00 249.86 ? 402  NAG G C4  1 
HETATM 23678 C  C5  . NAG BC 5 .   ? 43.326  -65.112 61.816   1.00 220.93 ? 402  NAG G C5  1 
HETATM 23679 C  C6  . NAG BC 5 .   ? 43.562  -66.145 62.895   1.00 205.41 ? 402  NAG G C6  1 
HETATM 23680 C  C7  . NAG BC 5 .   ? 43.482  -60.290 59.699   1.00 276.02 ? 402  NAG G C7  1 
HETATM 23681 C  C8  . NAG BC 5 .   ? 42.930  -59.382 58.642   1.00 270.33 ? 402  NAG G C8  1 
HETATM 23682 N  N2  . NAG BC 5 .   ? 42.738  -61.360 60.000   1.00 284.56 ? 402  NAG G N2  1 
HETATM 23683 O  O3  . NAG BC 5 .   ? 45.405  -62.450 60.187   1.00 251.52 ? 402  NAG G O3  1 
HETATM 23684 O  O4  . NAG BC 5 .   ? 45.487  -65.230 60.725   1.00 244.94 ? 402  NAG G O4  1 
HETATM 23685 O  O5  . NAG BC 5 .   ? 42.360  -64.192 62.346   1.00 248.21 ? 402  NAG G O5  1 
HETATM 23686 O  O6  . NAG BC 5 .   ? 42.744  -67.291 62.708   1.00 202.10 ? 402  NAG G O6  1 
HETATM 23687 O  O7  . NAG BC 5 .   ? 44.553  -60.067 60.255   1.00 281.39 ? 402  NAG G O7  1 
HETATM 23688 C  C1  . BMA CC 6 .   ? 46.632  -65.607 61.512   1.00 253.94 ? 403  BMA G C1  1 
HETATM 23689 C  C2  . BMA CC 6 .   ? 46.825  -67.052 61.202   1.00 252.36 ? 403  BMA G C2  1 
HETATM 23690 C  C3  . BMA CC 6 .   ? 47.828  -67.598 62.184   1.00 247.04 ? 403  BMA G C3  1 
HETATM 23691 C  C4  . BMA CC 6 .   ? 49.177  -66.893 61.918   1.00 246.29 ? 403  BMA G C4  1 
HETATM 23692 C  C5  . BMA CC 6 .   ? 48.994  -65.345 62.052   1.00 250.41 ? 403  BMA G C5  1 
HETATM 23693 C  C6  . BMA CC 6 .   ? 50.216  -64.559 61.605   1.00 227.22 ? 403  BMA G C6  1 
HETATM 23694 O  O2  . BMA CC 6 .   ? 47.406  -67.184 59.911   1.00 268.44 ? 403  BMA G O2  1 
HETATM 23695 O  O3  . BMA CC 6 .   ? 47.936  -69.070 62.210   1.00 255.34 ? 403  BMA G O3  1 
HETATM 23696 O  O4  . BMA CC 6 .   ? 50.166  -67.334 62.824   1.00 232.46 ? 403  BMA G O4  1 
HETATM 23697 O  O5  . BMA CC 6 .   ? 47.835  -64.887 61.268   1.00 252.81 ? 403  BMA G O5  1 
HETATM 23698 O  O6  . BMA CC 6 .   ? 49.976  -63.177 61.846   1.00 207.90 ? 403  BMA G O6  1 
HETATM 23699 C  C1  . MAN DC 7 .   ? 46.850  -69.782 61.548   1.00 266.19 ? 404  MAN G C1  1 
HETATM 23700 C  C2  . MAN DC 7 .   ? 45.490  -69.856 62.396   1.00 251.47 ? 404  MAN G C2  1 
HETATM 23701 C  C3  . MAN DC 7 .   ? 45.191  -71.229 62.998   1.00 252.36 ? 404  MAN G C3  1 
HETATM 23702 C  C4  . MAN DC 7 .   ? 45.639  -72.356 62.076   1.00 262.75 ? 404  MAN G C4  1 
HETATM 23703 C  C5  . MAN DC 7 .   ? 47.123  -72.178 61.821   1.00 267.12 ? 404  MAN G C5  1 
HETATM 23704 C  C6  . MAN DC 7 .   ? 47.750  -73.356 61.108   1.00 236.74 ? 404  MAN G C6  1 
HETATM 23705 O  O2  . MAN DC 7 .   ? 44.348  -69.549 61.582   1.00 244.63 ? 404  MAN G O2  1 
HETATM 23706 O  O3  . MAN DC 7 .   ? 43.802  -71.357 63.288   1.00 210.61 ? 404  MAN G O3  1 
HETATM 23707 O  O4  . MAN DC 7 .   ? 45.406  -73.613 62.688   1.00 270.75 ? 404  MAN G O4  1 
HETATM 23708 O  O5  . MAN DC 7 .   ? 47.275  -71.021 60.983   1.00 263.06 ? 404  MAN G O5  1 
HETATM 23709 O  O6  . MAN DC 7 .   ? 47.929  -74.400 62.057   1.00 227.01 ? 404  MAN G O6  1 
HETATM 23710 C  C1  . NAG EC 5 .   ? 27.933  -42.843 5.062    1.00 178.27 ? 401  NAG H C1  1 
HETATM 23711 C  C2  . NAG EC 5 .   ? 27.006  -43.114 3.882    1.00 203.36 ? 401  NAG H C2  1 
HETATM 23712 C  C3  . NAG EC 5 .   ? 26.961  -41.903 2.956    1.00 218.55 ? 401  NAG H C3  1 
HETATM 23713 C  C4  . NAG EC 5 .   ? 26.579  -40.660 3.749    1.00 245.48 ? 401  NAG H C4  1 
HETATM 23714 C  C5  . NAG EC 5 .   ? 27.548  -40.486 4.920    1.00 248.32 ? 401  NAG H C5  1 
HETATM 23715 C  C6  . NAG EC 5 .   ? 27.203  -39.338 5.840    1.00 232.97 ? 401  NAG H C6  1 
HETATM 23716 C  C7  . NAG EC 5 .   ? 26.653  -45.405 3.077    1.00 212.51 ? 401  NAG H C7  1 
HETATM 23717 C  C8  . NAG EC 5 .   ? 25.330  -45.344 3.779    1.00 204.48 ? 401  NAG H C8  1 
HETATM 23718 N  N2  . NAG EC 5 .   ? 27.412  -44.307 3.157    1.00 202.20 ? 401  NAG H N2  1 
HETATM 23719 O  O3  . NAG EC 5 .   ? 26.033  -42.129 1.903    1.00 211.65 ? 401  NAG H O3  1 
HETATM 23720 O  O4  . NAG EC 5 .   ? 26.555  -39.513 2.905    1.00 264.75 ? 401  NAG H O4  1 
HETATM 23721 O  O5  . NAG EC 5 .   ? 27.521  -41.667 5.733    1.00 226.89 ? 401  NAG H O5  1 
HETATM 23722 O  O6  . NAG EC 5 .   ? 27.552  -39.640 7.185    1.00 230.20 ? 401  NAG H O6  1 
HETATM 23723 O  O7  . NAG EC 5 .   ? 27.016  -46.402 2.464    1.00 216.74 ? 401  NAG H O7  1 
HETATM 23724 C  C1  . NAG FC 5 .   ? 25.268  -38.879 3.090    1.00 266.77 ? 402  NAG H C1  1 
HETATM 23725 C  C2  . NAG FC 5 .   ? 25.146  -37.550 2.361    1.00 251.44 ? 402  NAG H C2  1 
HETATM 23726 C  C3  . NAG FC 5 .   ? 23.850  -36.855 2.764    1.00 238.16 ? 402  NAG H C3  1 
HETATM 23727 C  C4  . NAG FC 5 .   ? 22.655  -37.788 2.609    1.00 261.69 ? 402  NAG H C4  1 
HETATM 23728 C  C5  . NAG FC 5 .   ? 22.924  -39.150 3.251    1.00 261.96 ? 402  NAG H C5  1 
HETATM 23729 C  C6  . NAG FC 5 .   ? 21.852  -40.170 2.946    1.00 230.35 ? 402  NAG H C6  1 
HETATM 23730 C  C7  . NAG FC 5 .   ? 26.934  -36.011 1.690    1.00 230.50 ? 402  NAG H C7  1 
HETATM 23731 C  C8  . NAG FC 5 .   ? 28.083  -35.170 2.156    1.00 223.02 ? 402  NAG H C8  1 
HETATM 23732 N  N2  . NAG FC 5 .   ? 26.288  -36.695 2.638    1.00 241.72 ? 402  NAG H N2  1 
HETATM 23733 O  O3  . NAG FC 5 .   ? 23.669  -35.694 1.962    1.00 219.54 ? 402  NAG H O3  1 
HETATM 23734 O  O4  . NAG FC 5 .   ? 21.539  -37.211 3.273    1.00 275.30 ? 402  NAG H O4  1 
HETATM 23735 O  O5  . NAG FC 5 .   ? 24.162  -39.695 2.772    1.00 260.24 ? 402  NAG H O5  1 
HETATM 23736 O  O6  . NAG FC 5 .   ? 21.046  -40.429 4.087    1.00 215.66 ? 402  NAG H O6  1 
HETATM 23737 O  O7  . NAG FC 5 .   ? 26.608  -36.072 0.508    1.00 220.18 ? 402  NAG H O7  1 
HETATM 23738 C  C1  . BMA GC 6 .   ? 20.516  -36.870 2.330    1.00 277.00 ? 403  BMA H C1  1 
HETATM 23739 C  C2  . BMA GC 6 .   ? 19.201  -37.390 2.919    1.00 244.80 ? 403  BMA H C2  1 
HETATM 23740 C  C3  . BMA GC 6 .   ? 18.007  -36.843 2.102    1.00 259.80 ? 403  BMA H C3  1 
HETATM 23741 C  C4  . BMA GC 6 .   ? 18.133  -35.308 1.844    1.00 282.27 ? 403  BMA H C4  1 
HETATM 23742 C  C5  . BMA GC 6 .   ? 19.535  -35.027 1.170    1.00 277.69 ? 403  BMA H C5  1 
HETATM 23743 C  C6  . BMA GC 6 .   ? 19.824  -33.548 0.877    1.00 266.27 ? 403  BMA H C6  1 
HETATM 23744 O  O2  . BMA GC 6 .   ? 19.070  -36.967 4.272    1.00 204.20 ? 403  BMA H O2  1 
HETATM 23745 O  O3  . BMA GC 6 .   ? 16.682  -37.273 2.565    1.00 259.59 ? 403  BMA H O3  1 
HETATM 23746 O  O4  . BMA GC 6 .   ? 17.088  -34.859 1.021    1.00 272.82 ? 403  BMA H O4  1 
HETATM 23747 O  O5  . BMA GC 6 .   ? 20.541  -35.484 2.064    1.00 281.56 ? 403  BMA H O5  1 
HETATM 23748 O  O6  . BMA GC 6 .   ? 20.917  -33.102 1.703    1.00 245.89 ? 403  BMA H O6  1 
HETATM 23749 C  C1  . MAN HC 7 .   ? 16.039  -36.556 3.633    1.00 259.90 ? 404  MAN H C1  1 
HETATM 23750 C  C2  . MAN HC 7 .   ? 16.009  -37.524 4.867    1.00 255.68 ? 404  MAN H C2  1 
HETATM 23751 C  C3  . MAN HC 7 .   ? 14.747  -38.466 4.906    1.00 262.14 ? 404  MAN H C3  1 
HETATM 23752 C  C4  . MAN HC 7 .   ? 13.477  -37.856 4.252    1.00 255.76 ? 404  MAN H C4  1 
HETATM 23753 C  C5  . MAN HC 7 .   ? 13.841  -37.185 2.931    1.00 273.73 ? 404  MAN H C5  1 
HETATM 23754 C  C6  . MAN HC 7 .   ? 12.643  -36.572 2.229    1.00 269.12 ? 404  MAN H C6  1 
HETATM 23755 O  O2  . MAN HC 7 .   ? 16.174  -36.872 6.171    1.00 264.55 ? 404  MAN H O2  1 
HETATM 23756 O  O3  . MAN HC 7 .   ? 14.459  -38.937 6.226    1.00 252.45 ? 404  MAN H O3  1 
HETATM 23757 O  O4  . MAN HC 7 .   ? 12.517  -38.873 4.019    1.00 241.41 ? 404  MAN H O4  1 
HETATM 23758 O  O5  . MAN HC 7 .   ? 14.772  -36.123 3.221    1.00 267.56 ? 404  MAN H O5  1 
HETATM 23759 O  O6  . MAN HC 7 .   ? 12.896  -36.572 0.827    1.00 261.59 ? 404  MAN H O6  1 
HETATM 23760 C  C1  . MAN IC 7 .   ? 21.524  -31.924 1.117    1.00 253.99 ? 405  MAN H C1  1 
HETATM 23761 C  C2  . MAN IC 7 .   ? 22.411  -32.250 -0.136   1.00 238.58 ? 405  MAN H C2  1 
HETATM 23762 C  C3  . MAN IC 7 .   ? 23.840  -32.634 0.265    1.00 236.39 ? 405  MAN H C3  1 
HETATM 23763 C  C4  . MAN IC 7 .   ? 24.399  -31.650 1.293    1.00 261.04 ? 405  MAN H C4  1 
HETATM 23764 C  C5  . MAN IC 7 .   ? 23.460  -31.609 2.498    1.00 271.23 ? 405  MAN H C5  1 
HETATM 23765 C  C6  . MAN IC 7 .   ? 23.935  -30.687 3.599    1.00 266.66 ? 405  MAN H C6  1 
HETATM 23766 O  O2  . MAN IC 7 .   ? 22.570  -31.091 -0.966   1.00 231.76 ? 405  MAN H O2  1 
HETATM 23767 O  O3  . MAN IC 7 .   ? 24.716  -32.700 -0.864   1.00 227.69 ? 405  MAN H O3  1 
HETATM 23768 O  O4  . MAN IC 7 .   ? 25.684  -32.073 1.709    1.00 253.22 ? 405  MAN H O4  1 
HETATM 23769 O  O5  . MAN IC 7 .   ? 22.188  -31.118 2.058    1.00 268.51 ? 405  MAN H O5  1 
HETATM 23770 O  O6  . MAN IC 7 .   ? 23.619  -31.299 4.849    1.00 249.21 ? 405  MAN H O6  1 
HETATM 23771 C  C1  . MAN JC 7 .   ? 15.196  -35.859 6.477    1.00 265.12 ? 406  MAN H C1  1 
HETATM 23772 C  C2  . MAN JC 7 .   ? 15.911  -34.544 6.824    1.00 277.69 ? 406  MAN H C2  1 
HETATM 23773 C  C3  . MAN JC 7 .   ? 16.563  -34.654 8.209    1.00 282.96 ? 406  MAN H C3  1 
HETATM 23774 C  C4  . MAN JC 7 .   ? 15.556  -35.153 9.259    1.00 283.35 ? 406  MAN H C4  1 
HETATM 23775 C  C5  . MAN JC 7 .   ? 14.936  -36.482 8.797    1.00 261.24 ? 406  MAN H C5  1 
HETATM 23776 C  C6  . MAN JC 7 .   ? 13.860  -36.990 9.742    1.00 224.76 ? 406  MAN H C6  1 
HETATM 23777 O  O2  . MAN JC 7 .   ? 14.983  -33.457 6.915    1.00 263.34 ? 406  MAN H O2  1 
HETATM 23778 O  O3  . MAN JC 7 .   ? 17.144  -33.422 8.629    1.00 288.99 ? 406  MAN H O3  1 
HETATM 23779 O  O4  . MAN JC 7 .   ? 16.212  -35.345 10.500   1.00 271.55 ? 406  MAN H O4  1 
HETATM 23780 O  O5  . MAN JC 7 .   ? 14.324  -36.287 7.499    1.00 274.61 ? 406  MAN H O5  1 
HETATM 23781 O  O6  . MAN JC 7 .   ? 13.742  -38.402 9.584    1.00 182.28 ? 406  MAN H O6  1 
HETATM 23782 O  O   . HOH KC 9 .   ? -19.672 -10.110 14.919   1.00 116.69 ? 2101 HOH B O   1 
HETATM 23783 O  O   . HOH KC 9 .   ? -22.280 -8.744  15.882   1.00 104.40 ? 2102 HOH B O   1 
HETATM 23784 O  O   . HOH KC 9 .   ? -26.485 -13.469 13.024   1.00 84.87  ? 2103 HOH B O   1 
HETATM 23785 O  O   . HOH LC 9 .   ? 19.439  -55.791 -13.737  1.00 206.74 ? 2101 HOH F O   1 
HETATM 23786 O  O   . HOH LC 9 .   ? 21.746  -54.130 -14.999  1.00 198.96 ? 2102 HOH F O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N  N   . PHE A  1   ? 1.1439 3.4126 2.7791 0.4887  -0.5489 0.1089  1    PHE A N   
2     C  CA  . PHE A  1   ? 1.1593 3.5088 2.7944 0.4442  -0.5798 0.0815  1    PHE A CA  
3     C  C   . PHE A  1   ? 1.1740 3.5942 2.8637 0.4126  -0.6013 0.0917  1    PHE A C   
4     O  O   . PHE A  1   ? 1.1837 3.6642 2.8863 0.3676  -0.6240 0.0630  1    PHE A O   
5     C  CB  . PHE A  1   ? 1.1953 3.5783 2.7731 0.4426  -0.6054 0.0880  1    PHE A CB  
6     C  CG  . PHE A  1   ? 1.3819 3.7847 2.9566 0.4605  -0.6228 0.1358  1    PHE A CG  
7     C  CD1 . PHE A  1   ? 1.3801 3.7165 2.9344 0.5074  -0.6044 0.1660  1    PHE A CD1 
8     C  CD2 . PHE A  1   ? 1.6066 4.0932 3.1977 0.4297  -0.6590 0.1485  1    PHE A CD2 
9     C  CE1 . PHE A  1   ? 1.5647 3.9184 3.1188 0.5273  -0.6202 0.2057  1    PHE A CE1 
10    C  CE2 . PHE A  1   ? 1.3056 3.8110 2.8978 0.4493  -0.6753 0.1915  1    PHE A CE2 
11    C  CZ  . PHE A  1   ? 1.3073 3.7465 2.8824 0.5000  -0.6552 0.2190  1    PHE A CZ  
12    N  N   . ASN A  2   ? 1.3256 3.7386 3.0466 0.4353  -0.5941 0.1290  2    ASN A N   
13    C  CA  . ASN A  2   ? 1.3606 3.8455 3.1336 0.4105  -0.6149 0.1458  2    ASN A CA  
14    C  C   . ASN A  2   ? 1.2984 3.7777 3.1313 0.3990  -0.5965 0.1386  2    ASN A C   
15    O  O   . ASN A  2   ? 1.4386 3.9706 3.3191 0.3855  -0.6069 0.1570  2    ASN A O   
16    C  CB  . ASN A  2   ? 1.2307 3.7250 3.0049 0.4432  -0.6197 0.1881  2    ASN A CB  
17    C  CG  . ASN A  2   ? 1.2138 3.6237 2.9801 0.4956  -0.5823 0.2030  2    ASN A CG  
18    O  OD1 . ASN A  2   ? 1.2120 3.5479 2.9434 0.5134  -0.5593 0.1881  2    ASN A OD1 
19    N  ND2 . ASN A  2   ? 1.2481 3.6710 3.0451 0.5193  -0.5765 0.2308  2    ASN A ND2 
20    N  N   . LEU A  3   ? 1.3169 3.7368 3.1492 0.4035  -0.5702 0.1137  3    LEU A N   
21    C  CA  . LEU A  3   ? 1.2940 3.7118 3.1820 0.3883  -0.5561 0.1071  3    LEU A CA  
22    C  C   . LEU A  3   ? 1.2424 3.7336 3.1620 0.3303  -0.5858 0.0818  3    LEU A C   
23    O  O   . LEU A  3   ? 1.1878 3.6930 3.0782 0.3061  -0.6016 0.0462  3    LEU A O   
24    C  CB  . LEU A  3   ? 1.2568 3.5866 3.1337 0.4105  -0.5213 0.0902  3    LEU A CB  
25    C  CG  . LEU A  3   ? 1.1402 3.3930 2.9990 0.4595  -0.4892 0.1143  3    LEU A CG  
26    C  CD1 . LEU A  3   ? 1.0919 3.2593 2.9333 0.4743  -0.4599 0.0967  3    LEU A CD1 
27    C  CD2 . LEU A  3   ? 1.2003 3.4778 3.1058 0.4653  -0.4815 0.1379  3    LEU A CD2 
28    N  N   . ASP A  4   ? 1.1934 3.7328 3.1705 0.3063  -0.5936 0.0959  4    ASP A N   
29    C  CA  . ASP A  4   ? 1.2494 3.8592 3.2590 0.2447  -0.6251 0.0749  4    ASP A CA  
30    C  C   . ASP A  4   ? 1.1177 3.6936 3.1465 0.2268  -0.6120 0.0377  4    ASP A C   
31    O  O   . ASP A  4   ? 1.0933 3.6423 3.1628 0.2360  -0.5894 0.0491  4    ASP A O   
32    C  CB  . ASP A  4   ? 1.1689 3.8427 3.2335 0.2251  -0.6377 0.1059  4    ASP A CB  
33    C  CG  . ASP A  4   ? 1.1957 3.9389 3.2926 0.1548  -0.6729 0.0871  4    ASP A CG  
34    O  OD1 . ASP A  4   ? 1.2332 4.0223 3.3013 0.1200  -0.7082 0.0739  4    ASP A OD1 
35    O  OD2 . ASP A  4   ? 1.1843 3.9342 3.3318 0.1313  -0.6664 0.0850  4    ASP A OD2 
36    N  N   . VAL A  5   ? 1.1251 3.7034 3.1243 0.2014  -0.6268 -0.0124 5    VAL A N   
37    C  CA  . VAL A  5   ? 1.1294 3.6320 3.1277 0.1788  -0.6126 -0.0587 5    VAL A CA  
38    C  C   . VAL A  5   ? 1.1889 3.7026 3.1955 0.1069  -0.6397 -0.0844 5    VAL A C   
39    O  O   . VAL A  5   ? 1.2144 3.6460 3.2155 0.0802  -0.6294 -0.1215 5    VAL A O   
40    C  CB  . VAL A  5   ? 1.1420 3.5456 3.0676 0.1954  -0.5934 -0.1017 5    VAL A CB  
41    C  CG1 . VAL A  5   ? 1.1282 3.4291 3.0605 0.2038  -0.5622 -0.1284 5    VAL A CG1 
42    C  CG2 . VAL A  5   ? 1.2001 3.6170 3.0979 0.2515  -0.5834 -0.0755 5    VAL A CG2 
43    N  N   . ASP A  6   ? 1.4795 4.0910 3.4982 0.0740  -0.6763 -0.0652 6    ASP A N   
44    C  CA  . ASP A  6   ? 1.5443 4.1707 3.5681 0.0003  -0.7067 -0.0875 6    ASP A CA  
45    C  C   . ASP A  6   ? 1.3394 3.9939 3.4407 -0.0204 -0.7051 -0.0630 6    ASP A C   
46    O  O   . ASP A  6   ? 1.3408 3.9364 3.4414 -0.0686 -0.7091 -0.0948 6    ASP A O   
47    C  CB  . ASP A  6   ? 1.7969 4.5249 3.8087 -0.0306 -0.7495 -0.0710 6    ASP A CB  
48    C  CG  . ASP A  6   ? 1.8222 4.5204 3.7485 -0.0221 -0.7548 -0.0979 6    ASP A CG  
49    O  OD1 . ASP A  6   ? 1.7991 4.3925 3.6718 -0.0065 -0.7272 -0.1403 6    ASP A OD1 
50    O  OD2 . ASP A  6   ? 1.7299 4.5129 3.6437 -0.0319 -0.7869 -0.0748 6    ASP A OD2 
51    N  N   . SER A  7   ? 1.3780 4.1194 3.5453 0.0156  -0.6982 -0.0069 7    SER A N   
52    C  CA  . SER A  7   ? 1.5158 4.2990 3.7589 -0.0044 -0.6955 0.0227  7    SER A CA  
53    C  C   . SER A  7   ? 1.3263 4.0591 3.5844 0.0611  -0.6503 0.0563  7    SER A C   
54    O  O   . SER A  7   ? 1.2059 3.9605 3.4772 0.0877  -0.6393 0.0945  7    SER A O   
55    C  CB  . SER A  7   ? 1.6345 4.4965 3.9023 -0.0451 -0.7266 0.0530  7    SER A CB  
56    O  OG  . SER A  7   ? 1.6683 4.5489 3.9108 -0.0025 -0.7246 0.0833  7    SER A OG  
57    N  N   . PRO A  8   ? 1.1372 3.8010 3.3886 0.0891  -0.6227 0.0365  8    PRO A N   
58    C  CA  . PRO A  8   ? 1.3041 3.9131 3.5642 0.1431  -0.5813 0.0644  8    PRO A CA  
59    C  C   . PRO A  8   ? 1.5632 4.1875 3.8828 0.1176  -0.5729 0.0793  8    PRO A C   
60    O  O   . PRO A  8   ? 1.7437 4.3901 4.0975 0.0607  -0.5942 0.0637  8    PRO A O   
61    C  CB  . PRO A  8   ? 1.0407 3.5679 3.2614 0.1783  -0.5602 0.0338  8    PRO A CB  
62    C  CG  . PRO A  8   ? 1.0889 3.5625 3.2814 0.1258  -0.5781 -0.0192 8    PRO A CG  
63    C  CD  . PRO A  8   ? 1.1350 3.6891 3.3285 0.0752  -0.6179 -0.0207 8    PRO A CD  
64    N  N   . ALA A  9   ? 1.5041 4.1110 3.8283 0.1585  -0.5406 0.1079  9    ALA A N   
65    C  CA  . ALA A  9   ? 1.2892 3.9113 3.6593 0.1408  -0.5259 0.1256  9    ALA A CA  
66    C  C   . ALA A  9   ? 1.2057 3.7541 3.5764 0.1528  -0.5048 0.1127  9    ALA A C   
67    O  O   . ALA A  9   ? 0.9961 3.4740 3.3242 0.2063  -0.4784 0.1061  9    ALA A O   
68    C  CB  . ALA A  9   ? 1.0602 3.7019 3.4284 0.1796  -0.4987 0.1585  9    ALA A CB  
69    N  N   . GLU A  10  ? 1.2325 3.7887 3.6526 0.0998  -0.5188 0.1123  10   GLU A N   
70    C  CA  . GLU A  10  ? 1.2304 3.6837 3.6455 0.1036  -0.5011 0.0986  10   GLU A CA  
71    C  C   . GLU A  10  ? 1.1514 3.6284 3.6129 0.0995  -0.4817 0.1374  10   GLU A C   
72    O  O   . GLU A  10  ? 1.4759 4.0000 3.9847 0.0445  -0.4981 0.1532  10   GLU A O   
73    C  CB  . GLU A  10  ? 1.3820 3.7435 3.7685 0.0488  -0.5221 0.0503  10   GLU A CB  
74    C  CG  . GLU A  10  ? 1.4982 3.7336 3.8697 0.0504  -0.5041 0.0314  10   GLU A CG  
75    C  CD  . GLU A  10  ? 1.5152 3.6512 3.8535 0.0063  -0.5224 -0.0215 10   GLU A CD  
76    O  OE1 . GLU A  10  ? 1.6455 3.7990 3.9578 -0.0179 -0.5451 -0.0500 10   GLU A OE1 
77    O  OE2 . GLU A  10  ? 1.3896 3.4278 3.7261 -0.0031 -0.5141 -0.0347 10   GLU A OE2 
78    N  N   . TYR A  11  ? 1.0269 3.4532 3.4504 0.1548  -0.4438 0.1463  11   TYR A N   
79    C  CA  . TYR A  11  ? 1.0277 3.4506 3.4691 0.1554  -0.4190 0.1762  11   TYR A CA  
80    C  C   . TYR A  11  ? 1.0155 3.3422 3.4676 0.1543  -0.4127 0.1699  11   TYR A C   
81    O  O   . TYR A  11  ? 1.0946 3.3409 3.5089 0.1853  -0.4084 0.1423  11   TYR A O   
82    C  CB  . TYR A  11  ? 1.0211 3.4480 3.4156 0.2140  -0.3832 0.1911  11   TYR A CB  
83    C  CG  . TYR A  11  ? 1.2225 3.7280 3.6209 0.2169  -0.3887 0.2016  11   TYR A CG  
84    C  CD1 . TYR A  11  ? 1.3428 3.8473 3.7084 0.2396  -0.4017 0.1838  11   TYR A CD1 
85    C  CD2 . TYR A  11  ? 1.2210 3.8010 3.6597 0.1952  -0.3819 0.2329  11   TYR A CD2 
86    C  CE1 . TYR A  11  ? 1.2807 3.8516 3.6542 0.2420  -0.4090 0.1988  11   TYR A CE1 
87    C  CE2 . TYR A  11  ? 1.1676 3.8185 3.6154 0.1989  -0.3874 0.2455  11   TYR A CE2 
88    C  CZ  . TYR A  11  ? 1.1882 3.8324 3.6038 0.2229  -0.4018 0.2291  11   TYR A CZ  
89    O  OH  . TYR A  11  ? 1.1806 3.8942 3.6086 0.2269  -0.4091 0.2462  11   TYR A OH  
90    N  N   . SER A  12  ? 1.0420 3.3648 3.5359 0.1177  -0.4112 0.1923  12   SER A N   
91    C  CA  . SER A  12  ? 1.0322 3.2301 3.5027 0.1107  -0.4039 0.1774  12   SER A CA  
92    C  C   . SER A  12  ? 1.1327 3.3426 3.6267 0.1141  -0.3802 0.2198  12   SER A C   
93    O  O   . SER A  12  ? 1.0223 3.3348 3.5614 0.0968  -0.3756 0.2575  12   SER A O   
94    C  CB  . SER A  12  ? 1.1634 3.2966 3.6360 0.0464  -0.4329 0.1467  12   SER A CB  
95    O  OG  . SER A  12  ? 1.1252 3.3337 3.6468 -0.0110 -0.4484 0.1730  12   SER A OG  
96    N  N   . GLY A  13  ? 1.0575 3.1633 3.5203 0.1354  -0.3654 0.2141  13   GLY A N   
97    C  CA  . GLY A  13  ? 1.1418 3.2378 3.6149 0.1357  -0.3446 0.2506  13   GLY A CA  
98    C  C   . GLY A  13  ? 1.1464 3.1234 3.6096 0.1019  -0.3554 0.2383  13   GLY A C   
99    O  O   . GLY A  13  ? 1.0870 2.9945 3.5405 0.0773  -0.3785 0.2005  13   GLY A O   
100   N  N   . PRO A  14  ? 1.2295 3.1784 3.6929 0.1015  -0.3389 0.2698  14   PRO A N   
101   C  CA  . PRO A  14  ? 1.2666 3.1001 3.7225 0.0706  -0.3508 0.2636  14   PRO A CA  
102   C  C   . PRO A  14  ? 1.1972 2.9183 3.6153 0.0993  -0.3581 0.2205  14   PRO A C   
103   O  O   . PRO A  14  ? 1.1782 2.8928 3.5650 0.1532  -0.3432 0.2099  14   PRO A O   
104   C  CB  . PRO A  14  ? 1.2391 3.0723 3.6898 0.0819  -0.3265 0.3075  14   PRO A CB  
105   C  CG  . PRO A  14  ? 1.2481 3.2179 3.7226 0.0934  -0.3057 0.3404  14   PRO A CG  
106   C  CD  . PRO A  14  ? 1.2231 3.2461 3.6928 0.1278  -0.3085 0.3136  14   PRO A CD  
107   N  N   . GLU A  15  ? 1.1646 2.7967 3.5867 0.0624  -0.3809 0.1957  15   GLU A N   
108   C  CA  . GLU A  15  ? 1.1711 2.6986 3.5643 0.0879  -0.3869 0.1538  15   GLU A CA  
109   C  C   . GLU A  15  ? 1.1578 2.6163 3.5294 0.1240  -0.3715 0.1710  15   GLU A C   
110   O  O   . GLU A  15  ? 1.1717 2.6272 3.5509 0.1107  -0.3647 0.2108  15   GLU A O   
111   C  CB  . GLU A  15  ? 1.2626 2.7084 3.6667 0.0414  -0.4136 0.1225  15   GLU A CB  
112   C  CG  . GLU A  15  ? 1.4510 2.8043 3.8646 0.0175  -0.4206 0.1414  15   GLU A CG  
113   C  CD  . GLU A  15  ? 1.6958 2.9467 4.1128 -0.0144 -0.4450 0.1024  15   GLU A CD  
114   O  OE1 . GLU A  15  ? 1.7653 3.0280 4.1781 -0.0285 -0.4571 0.0627  15   GLU A OE1 
115   O  OE2 . GLU A  15  ? 1.7922 2.9477 4.2136 -0.0237 -0.4522 0.1110  15   GLU A OE2 
116   N  N   . GLY A  16  ? 1.2065 2.6137 3.5491 0.1684  -0.3664 0.1424  16   GLY A N   
117   C  CA  . GLY A  16  ? 1.2285 2.5718 3.5490 0.2030  -0.3548 0.1566  16   GLY A CA  
118   C  C   . GLY A  16  ? 1.2286 2.6311 3.5290 0.2360  -0.3307 0.1929  16   GLY A C   
119   O  O   . GLY A  16  ? 1.1246 2.4767 3.4010 0.2625  -0.3217 0.2074  16   GLY A O   
120   N  N   . SER A  17  ? 1.1020 2.6091 3.4107 0.2361  -0.3203 0.2077  17   SER A N   
121   C  CA  . SER A  17  ? 1.0177 2.5842 3.3089 0.2671  -0.2948 0.2421  17   SER A CA  
122   C  C   . SER A  17  ? 0.9703 2.5577 3.2277 0.3214  -0.2819 0.2261  17   SER A C   
123   O  O   . SER A  17  ? 1.1260 2.7565 3.3632 0.3528  -0.2599 0.2503  17   SER A O   
124   C  CB  . SER A  17  ? 1.0207 2.6956 3.3457 0.2398  -0.2881 0.2715  17   SER A CB  
125   O  OG  . SER A  17  ? 1.0050 2.7511 3.3498 0.2342  -0.2977 0.2512  17   SER A OG  
126   N  N   . TYR A  18  ? 0.9607 2.5156 3.2087 0.3325  -0.2942 0.1862  18   TYR A N   
127   C  CA  . TYR A  18  ? 0.9260 2.4983 3.1316 0.3772  -0.2837 0.1694  18   TYR A CA  
128   C  C   . TYR A  18  ? 0.9175 2.5869 3.1070 0.3831  -0.2721 0.1806  18   TYR A C   
129   O  O   . TYR A  18  ? 0.9113 2.5874 3.0302 0.4205  -0.2526 0.1808  18   TYR A O   
130   C  CB  . TYR A  18  ? 0.9254 2.4308 3.0575 0.4146  -0.2648 0.1771  18   TYR A CB  
131   C  CG  . TYR A  18  ? 0.9348 2.3433 3.0652 0.4167  -0.2760 0.1596  18   TYR A CG  
132   C  CD1 . TYR A  18  ? 0.9485 2.3276 3.1401 0.3889  -0.2991 0.1373  18   TYR A CD1 
133   C  CD2 . TYR A  18  ? 0.9372 2.2814 3.0008 0.4456  -0.2638 0.1634  18   TYR A CD2 
134   C  CE1 . TYR A  18  ? 0.9639 2.2542 3.1521 0.3941  -0.3075 0.1200  18   TYR A CE1 
135   C  CE2 . TYR A  18  ? 0.9839 2.2452 3.0462 0.4471  -0.2740 0.1497  18   TYR A CE2 
136   C  CZ  . TYR A  18  ? 1.1117 2.3489 3.2416 0.4242  -0.2953 0.1284  18   TYR A CZ  
137   O  OH  . TYR A  18  ? 1.2356 2.3910 3.3659 0.4299  -0.3039 0.1141  18   TYR A OH  
138   N  N   . PHE A  19  ? 0.9348 2.6778 3.1926 0.3445  -0.2866 0.1892  19   PHE A N   
139   C  CA  . PHE A  19  ? 0.9188 2.7606 3.1714 0.3450  -0.2806 0.1979  19   PHE A CA  
140   C  C   . PHE A  19  ? 0.9094 2.7540 3.1073 0.3728  -0.2825 0.1667  19   PHE A C   
141   O  O   . PHE A  19  ? 0.9091 2.7417 3.1271 0.3562  -0.3038 0.1384  19   PHE A O   
142   C  CB  . PHE A  19  ? 0.9298 2.8413 3.2682 0.2897  -0.3034 0.2083  19   PHE A CB  
143   C  CG  . PHE A  19  ? 0.9315 2.9486 3.2702 0.2853  -0.3011 0.2175  19   PHE A CG  
144   C  CD1 . PHE A  19  ? 0.9384 3.0207 3.2780 0.2895  -0.2794 0.2509  19   PHE A CD1 
145   C  CD2 . PHE A  19  ? 0.9302 2.9814 3.2701 0.2774  -0.3210 0.1915  19   PHE A CD2 
146   C  CE1 . PHE A  19  ? 0.9459 3.1193 3.2892 0.2875  -0.2780 0.2559  19   PHE A CE1 
147   C  CE2 . PHE A  19  ? 0.9360 3.0819 3.2776 0.2736  -0.3220 0.1998  19   PHE A CE2 
148   C  CZ  . PHE A  19  ? 0.9616 3.1653 3.3061 0.2795  -0.3007 0.2307  19   PHE A CZ  
149   N  N   . GLY A  20  ? 0.9062 2.7676 3.0401 0.4129  -0.2619 0.1703  20   GLY A N   
150   C  CA  . GLY A  20  ? 0.9001 2.7570 2.9777 0.4421  -0.2635 0.1442  20   GLY A CA  
151   C  C   . GLY A  20  ? 0.8970 2.6687 2.8965 0.4820  -0.2490 0.1326  20   GLY A C   
152   O  O   . GLY A  20  ? 0.8930 2.6514 2.8446 0.5039  -0.2516 0.1117  20   GLY A O   
153   N  N   . PHE A  21  ? 0.9008 2.6169 2.8879 0.4892  -0.2356 0.1478  21   PHE A N   
154   C  CA  . PHE A  21  ? 0.9020 2.5385 2.8147 0.5232  -0.2238 0.1394  21   PHE A CA  
155   C  C   . PHE A  21  ? 0.9088 2.5515 2.7676 0.5583  -0.2120 0.1338  21   PHE A C   
156   O  O   . PHE A  21  ? 0.9099 2.4969 2.7077 0.5837  -0.2105 0.1167  21   PHE A O   
157   C  CB  . PHE A  21  ? 0.9086 2.4933 2.8287 0.5193  -0.2152 0.1609  21   PHE A CB  
158   C  CG  . PHE A  21  ? 0.9121 2.4116 2.7640 0.5455  -0.2083 0.1534  21   PHE A CG  
159   C  CD1 . PHE A  21  ? 0.9103 2.3460 2.7574 0.5377  -0.2187 0.1387  21   PHE A CD1 
160   C  CD2 . PHE A  21  ? 0.9941 2.4745 2.7907 0.5761  -0.1924 0.1600  21   PHE A CD2 
161   C  CE1 . PHE A  21  ? 0.9152 2.2786 2.7014 0.5583  -0.2133 0.1346  21   PHE A CE1 
162   C  CE2 . PHE A  21  ? 0.9273 2.3311 2.6635 0.5960  -0.1894 0.1541  21   PHE A CE2 
163   C  CZ  . PHE A  21  ? 0.9228 2.2725 2.6524 0.5864  -0.1998 0.1432  21   PHE A CZ  
164   N  N   . ALA A  22  ? 1.2229 2.9259 3.1099 0.5573  -0.2040 0.1498  22   ALA A N   
165   C  CA  . ALA A  22  ? 1.2165 2.9202 3.0715 0.5853  -0.1935 0.1492  22   ALA A CA  
166   C  C   . ALA A  22  ? 0.9378 2.7308 2.8425 0.5711  -0.1982 0.1584  22   ALA A C   
167   O  O   . ALA A  22  ? 0.9382 2.7959 2.8968 0.5458  -0.1965 0.1781  22   ALA A O   
168   C  CB  . ALA A  22  ? 1.1793 2.8534 3.0043 0.6077  -0.1679 0.1715  22   ALA A CB  
169   N  N   . VAL A  23  ? 0.9448 2.7412 2.8343 0.5846  -0.2053 0.1483  23   VAL A N   
170   C  CA  . VAL A  23  ? 1.0650 2.9446 2.9971 0.5733  -0.2125 0.1588  23   VAL A CA  
171   C  C   . VAL A  23  ? 1.1879 3.0591 3.0868 0.6069  -0.1987 0.1703  23   VAL A C   
172   O  O   . VAL A  23  ? 1.4067 3.2030 3.2497 0.6337  -0.1923 0.1633  23   VAL A O   
173   C  CB  . VAL A  23  ? 0.9416 2.8490 2.9004 0.5492  -0.2419 0.1392  23   VAL A CB  
174   C  CG1 . VAL A  23  ? 0.9227 2.8448 2.9165 0.5165  -0.2543 0.1293  23   VAL A CG1 
175   C  CG2 . VAL A  23  ? 0.9389 2.7779 2.8498 0.5689  -0.2496 0.1206  23   VAL A CG2 
176   N  N   . ASP A  24  ? 0.9969 2.9477 2.9320 0.6048  -0.1947 0.1896  24   ASP A N   
177   C  CA  . ASP A  24  ? 1.0262 2.9828 2.9383 0.6380  -0.1824 0.2027  24   ASP A CA  
178   C  C   . ASP A  24  ? 1.2112 3.2735 3.1809 0.6242  -0.1885 0.2203  24   ASP A C   
179   O  O   . ASP A  24  ? 1.3223 3.4481 3.3456 0.5872  -0.2007 0.2232  24   ASP A O   
180   C  CB  . ASP A  24  ? 1.0449 2.9633 2.9200 0.6695  -0.1501 0.2151  24   ASP A CB  
181   C  CG  . ASP A  24  ? 1.0758 2.9603 2.9060 0.7099  -0.1397 0.2196  24   ASP A CG  
182   O  OD1 . ASP A  24  ? 1.0752 2.8762 2.8519 0.7248  -0.1439 0.2064  24   ASP A OD1 
183   O  OD2 . ASP A  24  ? 1.5729 3.5159 3.4233 0.7267  -0.1275 0.2375  24   ASP A OD2 
184   N  N   . PHE A  25  ? 1.1915 3.2739 3.1515 0.6534  -0.1806 0.2335  25   PHE A N   
185   C  CA  . PHE A  25  ? 1.0899 3.2737 3.1030 0.6465  -0.1845 0.2532  25   PHE A CA  
186   C  C   . PHE A  25  ? 1.1138 3.3405 3.1427 0.6658  -0.1511 0.2764  25   PHE A C   
187   O  O   . PHE A  25  ? 1.1184 3.2933 3.1110 0.6882  -0.1249 0.2773  25   PHE A O   
188   C  CB  . PHE A  25  ? 1.1118 3.3019 3.1119 0.6673  -0.2000 0.2557  25   PHE A CB  
189   C  CG  . PHE A  25  ? 1.0938 3.2662 3.0871 0.6453  -0.2335 0.2384  25   PHE A CG  
190   C  CD1 . PHE A  25  ? 1.0824 3.1622 3.0194 0.6577  -0.2378 0.2206  25   PHE A CD1 
191   C  CD2 . PHE A  25  ? 1.0915 3.3445 3.1351 0.6108  -0.2607 0.2415  25   PHE A CD2 
192   C  CE1 . PHE A  25  ? 1.1638 3.2341 3.0955 0.6381  -0.2661 0.2066  25   PHE A CE1 
193   C  CE2 . PHE A  25  ? 1.0789 3.3210 3.1149 0.5907  -0.2907 0.2261  25   PHE A CE2 
194   C  CZ  . PHE A  25  ? 1.0668 3.2189 3.0472 0.6054  -0.2921 0.2089  25   PHE A CZ  
195   N  N   . PHE A  26  ? 1.1320 3.4595 3.2170 0.6563  -0.1524 0.2964  26   PHE A N   
196   C  CA  . PHE A  26  ? 1.1596 3.5454 3.2683 0.6749  -0.1202 0.3208  26   PHE A CA  
197   C  C   . PHE A  26  ? 1.1918 3.6586 3.3379 0.6882  -0.1261 0.3380  26   PHE A C   
198   O  O   . PHE A  26  ? 1.2635 3.8033 3.4598 0.6544  -0.1518 0.3437  26   PHE A O   
199   C  CB  . PHE A  26  ? 1.1456 3.5898 3.3019 0.6366  -0.1113 0.3339  26   PHE A CB  
200   C  CG  . PHE A  26  ? 1.1730 3.6710 3.3475 0.6558  -0.0732 0.3593  26   PHE A CG  
201   C  CD1 . PHE A  26  ? 1.2007 3.6556 3.3290 0.7077  -0.0431 0.3612  26   PHE A CD1 
202   C  CD2 . PHE A  26  ? 1.3551 3.9495 3.5933 0.6209  -0.0669 0.3821  26   PHE A CD2 
203   C  CE1 . PHE A  26  ? 1.2302 3.7392 3.3750 0.7274  -0.0054 0.3839  26   PHE A CE1 
204   C  CE2 . PHE A  26  ? 1.3268 3.9778 3.5834 0.6382  -0.0294 0.4071  26   PHE A CE2 
205   C  CZ  . PHE A  26  ? 1.2809 3.8903 3.4905 0.6931  0.0024  0.4072  26   PHE A CZ  
206   N  N   . VAL A  27  ? 1.4103 3.8645 3.5324 0.7371  -0.1038 0.3465  27   VAL A N   
207   C  CA  . VAL A  27  ? 1.5333 4.0647 3.6927 0.7571  -0.1065 0.3652  27   VAL A CA  
208   C  C   . VAL A  27  ? 1.5316 4.1047 3.7042 0.7921  -0.0649 0.3849  27   VAL A C   
209   O  O   . VAL A  27  ? 1.6246 4.1416 3.7516 0.8399  -0.0431 0.3823  27   VAL A O   
210   C  CB  . VAL A  27  ? 1.5518 4.0292 3.6723 0.7855  -0.1268 0.3563  27   VAL A CB  
211   C  CG1 . VAL A  27  ? 1.2790 3.6354 3.3210 0.8180  -0.1118 0.3394  27   VAL A CG1 
212   C  CG2 . VAL A  27  ? 1.7919 4.3413 3.9470 0.8172  -0.1247 0.3782  27   VAL A CG2 
213   N  N   . PRO A  28  ? 1.3471 4.0192 3.5807 0.7692  -0.0518 0.4052  28   PRO A N   
214   C  CA  . PRO A  28  ? 1.3840 4.1023 3.6314 0.8021  -0.0086 0.4244  28   PRO A CA  
215   C  C   . PRO A  28  ? 1.4877 4.2692 3.7654 0.8417  -0.0017 0.4410  28   PRO A C   
216   O  O   . PRO A  28  ? 1.4425 4.2091 3.7143 0.8553  -0.0281 0.4364  28   PRO A O   
217   C  CB  . PRO A  28  ? 1.5952 4.4010 3.9008 0.7551  -0.0013 0.4420  28   PRO A CB  
218   C  CG  . PRO A  28  ? 1.6045 4.4498 3.9503 0.7054  -0.0451 0.4395  28   PRO A CG  
219   C  CD  . PRO A  28  ? 1.3200 4.0610 3.6091 0.7094  -0.0741 0.4110  28   PRO A CD  
220   N  N   . SER A  29  ? 1.5539 4.4090 3.8655 0.8611  0.0352  0.4617  29   SER A N   
221   C  CA  . SER A  29  ? 1.5631 4.4742 3.9013 0.9092  0.0518  0.4774  29   SER A CA  
222   C  C   . SER A  29  ? 1.8653 4.8605 4.2649 0.8939  0.0168  0.4910  29   SER A C   
223   O  O   . SER A  29  ? 1.8707 4.9308 4.3179 0.8407  -0.0077 0.4987  29   SER A O   
224   C  CB  . SER A  29  ? 1.5949 4.5844 3.9669 0.9235  0.0984  0.4980  29   SER A CB  
225   O  OG  . SER A  29  ? 1.5892 4.5042 3.9025 0.9355  0.1298  0.4871  29   SER A OG  
226   N  N   . ALA A  30  ? 2.0871 5.0804 4.4849 0.9408  0.0138  0.4950  30   ALA A N   
227   C  CA  . ALA A  30  ? 2.1280 5.2046 4.5836 0.9395  -0.0161 0.5121  30   ALA A CA  
228   C  C   . ALA A  30  ? 2.2527 5.3175 4.7087 0.8873  -0.0666 0.5026  30   ALA A C   
229   O  O   . ALA A  30  ? 2.2762 5.2448 4.6752 0.8686  -0.0797 0.4788  30   ALA A O   
230   C  CB  . ALA A  30  ? 1.7918 5.0070 4.3302 0.9358  0.0043  0.5412  30   ALA A CB  
231   N  N   . SER A  31  ? 2.1674 5.3330 4.6882 0.8639  -0.0953 0.5215  31   SER A N   
232   C  CA  . SER A  31  ? 2.0085 5.1770 4.5342 0.8141  -0.1441 0.5146  31   SER A CA  
233   C  C   . SER A  31  ? 1.9650 5.1929 4.5310 0.7497  -0.1502 0.5182  31   SER A C   
234   O  O   . SER A  31  ? 1.8942 5.2315 4.5276 0.7167  -0.1676 0.5390  31   SER A O   
235   C  CB  . SER A  31  ? 1.8447 5.0852 4.4126 0.8241  -0.1755 0.5337  31   SER A CB  
236   O  OG  . SER A  31  ? 1.7479 5.1146 4.3939 0.8291  -0.1619 0.5635  31   SER A OG  
237   N  N   . SER A  32  ? 1.8456 4.9994 4.3700 0.7307  -0.1366 0.4988  32   SER A N   
238   C  CA  . SER A  32  ? 1.7035 4.8987 4.2600 0.6708  -0.1406 0.5011  32   SER A CA  
239   C  C   . SER A  32  ? 1.3516 4.4909 3.8820 0.6251  -0.1806 0.4777  32   SER A C   
240   O  O   . SER A  32  ? 1.3488 4.4396 3.8463 0.6362  -0.2078 0.4641  32   SER A O   
241   C  CB  . SER A  32  ? 1.5873 4.7503 4.1232 0.6805  -0.0965 0.4998  32   SER A CB  
242   O  OG  . SER A  32  ? 1.6699 4.8877 4.2288 0.7241  -0.0578 0.5203  32   SER A OG  
243   N  N   . ARG A  33  ? 1.3235 4.4698 3.8684 0.5740  -0.1837 0.4736  33   ARG A N   
244   C  CA  . ARG A  33  ? 1.2875 4.3780 3.8087 0.5318  -0.2169 0.4493  33   ARG A CA  
245   C  C   . ARG A  33  ? 1.3174 4.2778 3.7633 0.5590  -0.2029 0.4219  33   ARG A C   
246   O  O   . ARG A  33  ? 1.5300 4.4469 3.9440 0.6027  -0.1671 0.4231  33   ARG A O   
247   C  CB  . ARG A  33  ? 1.2752 4.4234 3.8446 0.4663  -0.2264 0.4568  33   ARG A CB  
248   C  CG  . ARG A  33  ? 1.3277 4.6000 3.9687 0.4274  -0.2509 0.4811  33   ARG A CG  
249   C  CD  . ARG A  33  ? 1.3030 4.6378 3.9948 0.3636  -0.2534 0.4948  33   ARG A CD  
250   N  NE  . ARG A  33  ? 1.3053 4.6537 4.0068 0.3770  -0.2087 0.5116  33   ARG A NE  
251   C  CZ  . ARG A  33  ? 1.3870 4.6770 4.0656 0.3621  -0.1927 0.5029  33   ARG A CZ  
252   N  NH1 . ARG A  33  ? 1.4729 4.6863 4.1212 0.3346  -0.2176 0.4764  33   ARG A NH1 
253   N  NH2 . ARG A  33  ? 1.3305 4.6425 4.0185 0.3745  -0.1519 0.5222  33   ARG A NH2 
254   N  N   . MET A  34  ? 1.3691 4.2693 3.7866 0.5325  -0.2319 0.3972  34   MET A N   
255   C  CA  . MET A  34  ? 1.2191 3.9982 3.5681 0.5529  -0.2245 0.3705  34   MET A CA  
256   C  C   . MET A  34  ? 1.2487 4.0013 3.6019 0.5076  -0.2310 0.3564  34   MET A C   
257   O  O   . MET A  34  ? 1.3136 4.1288 3.7147 0.4557  -0.2540 0.3607  34   MET A O   
258   C  CB  . MET A  34  ? 1.3692 4.0945 3.6770 0.5679  -0.2522 0.3532  34   MET A CB  
259   C  CG  . MET A  34  ? 1.3716 4.1116 3.6708 0.6152  -0.2484 0.3676  34   MET A CG  
260   S  SD  . MET A  34  ? 1.7592 4.3729 3.9751 0.6751  -0.2255 0.3531  34   MET A SD  
261   C  CE  . MET A  34  ? 1.6529 4.3094 3.8783 0.7184  -0.2324 0.3741  34   MET A CE  
262   N  N   . PHE A  35  ? 1.1441 3.8023 3.4471 0.5260  -0.2123 0.3402  35   PHE A N   
263   C  CA  . PHE A  35  ? 1.1149 3.7453 3.4231 0.4892  -0.2144 0.3302  35   PHE A CA  
264   C  C   . PHE A  35  ? 1.0880 3.6040 3.3347 0.5044  -0.2193 0.3005  35   PHE A C   
265   O  O   . PHE A  35  ? 1.0934 3.5453 3.2877 0.5466  -0.2121 0.2912  35   PHE A O   
266   C  CB  . PHE A  35  ? 1.1448 3.7968 3.4688 0.4902  -0.1793 0.3509  35   PHE A CB  
267   C  CG  . PHE A  35  ? 1.2202 3.9898 3.6085 0.4722  -0.1709 0.3823  35   PHE A CG  
268   C  CD1 . PHE A  35  ? 1.1589 4.0001 3.6066 0.4122  -0.1895 0.3941  35   PHE A CD1 
269   C  CD2 . PHE A  35  ? 1.1784 3.9876 3.5693 0.5141  -0.1444 0.4008  35   PHE A CD2 
270   C  CE1 . PHE A  35  ? 1.1735 4.1250 3.6811 0.3925  -0.1821 0.4247  35   PHE A CE1 
271   C  CE2 . PHE A  35  ? 1.2057 4.1278 3.6588 0.4986  -0.1353 0.4304  35   PHE A CE2 
272   C  CZ  . PHE A  35  ? 1.2026 4.1969 3.7138 0.4369  -0.1542 0.4429  35   PHE A CZ  
273   N  N   . LEU A  36  ? 1.0620 3.5545 3.3181 0.4681  -0.2319 0.2874  36   LEU A N   
274   C  CA  . LEU A  36  ? 1.0361 3.4261 3.2422 0.4788  -0.2337 0.2613  36   LEU A CA  
275   C  C   . LEU A  36  ? 1.0270 3.3796 3.2219 0.4840  -0.2064 0.2693  36   LEU A C   
276   O  O   . LEU A  36  ? 1.0267 3.4315 3.2684 0.4504  -0.2026 0.2874  36   LEU A O   
277   C  CB  . LEU A  36  ? 1.0166 3.4049 3.2420 0.4375  -0.2681 0.2399  36   LEU A CB  
278   C  CG  . LEU A  36  ? 1.0237 3.4422 3.2554 0.4259  -0.3003 0.2287  36   LEU A CG  
279   C  CD1 . LEU A  36  ? 1.3485 3.8774 3.6424 0.3881  -0.3174 0.2485  36   LEU A CD1 
280   C  CD2 . LEU A  36  ? 1.0012 3.3764 3.2241 0.4036  -0.3245 0.1994  36   LEU A CD2 
281   N  N   . LEU A  37  ? 1.0237 3.2868 3.1570 0.5228  -0.1891 0.2586  37   LEU A N   
282   C  CA  . LEU A  37  ? 1.1073 3.3233 3.2206 0.5297  -0.1664 0.2650  37   LEU A CA  
283   C  C   . LEU A  37  ? 0.9882 3.1272 3.0788 0.5182  -0.1832 0.2404  37   LEU A C   
284   O  O   . LEU A  37  ? 0.9816 3.0544 3.0263 0.5387  -0.1926 0.2167  37   LEU A O   
285   C  CB  . LEU A  37  ? 1.0351 3.2047 3.0942 0.5795  -0.1360 0.2711  37   LEU A CB  
286   C  CG  . LEU A  37  ? 1.0668 3.3111 3.1476 0.5978  -0.1127 0.2966  37   LEU A CG  
287   C  CD1 . LEU A  37  ? 1.0896 3.2775 3.1120 0.6478  -0.0831 0.2990  37   LEU A CD1 
288   C  CD2 . LEU A  37  ? 1.0691 3.3955 3.2081 0.5660  -0.1004 0.3237  37   LEU A CD2 
289   N  N   . VAL A  38  ? 0.9755 3.1246 3.1013 0.4844  -0.1872 0.2487  38   VAL A N   
290   C  CA  . VAL A  38  ? 0.9538 3.0372 3.0685 0.4717  -0.2032 0.2289  38   VAL A CA  
291   C  C   . VAL A  38  ? 0.9651 3.0036 3.0710 0.4741  -0.1850 0.2464  38   VAL A C   
292   O  O   . VAL A  38  ? 0.9604 3.0490 3.1067 0.4549  -0.1724 0.2773  38   VAL A O   
293   C  CB  . VAL A  38  ? 0.9450 3.0756 3.1197 0.4223  -0.2331 0.2234  38   VAL A CB  
294   C  CG1 . VAL A  38  ? 1.1478 3.2049 3.3096 0.4154  -0.2477 0.2018  38   VAL A CG1 
295   C  CG2 . VAL A  38  ? 0.9520 3.1398 3.1400 0.4162  -0.2522 0.2118  38   VAL A CG2 
296   N  N   . GLY A  39  ? 1.1442 3.0909 3.1992 0.4953  -0.1848 0.2292  39   GLY A N   
297   C  CA  . GLY A  39  ? 0.9416 2.8362 2.9874 0.4965  -0.1724 0.2461  39   GLY A CA  
298   C  C   . GLY A  39  ? 0.9298 2.7986 3.0203 0.4595  -0.1935 0.2460  39   GLY A C   
299   O  O   . GLY A  39  ? 0.9197 2.7665 3.0136 0.4495  -0.2148 0.2199  39   GLY A O   
300   N  N   . ALA A  40  ? 0.9352 2.8072 3.0663 0.4375  -0.1876 0.2775  40   ALA A N   
301   C  CA  . ALA A  40  ? 0.9321 2.7583 3.1119 0.4032  -0.2081 0.2814  40   ALA A CA  
302   C  C   . ALA A  40  ? 0.9388 2.7070 3.1023 0.4147  -0.1945 0.3054  40   ALA A C   
303   O  O   . ALA A  40  ? 0.9481 2.7527 3.1557 0.3929  -0.1867 0.3430  40   ALA A O   
304   C  CB  . ALA A  40  ? 0.9380 2.8343 3.2066 0.3493  -0.2249 0.3001  40   ALA A CB  
305   N  N   . PRO A  41  ? 0.9365 2.6178 3.0369 0.4463  -0.1923 0.2868  41   PRO A N   
306   C  CA  . PRO A  41  ? 0.9462 2.5772 3.0206 0.4618  -0.1786 0.3109  41   PRO A CA  
307   C  C   . PRO A  41  ? 0.9560 2.5453 3.0846 0.4279  -0.1952 0.3321  41   PRO A C   
308   O  O   . PRO A  41  ? 0.9799 2.5366 3.0797 0.4287  -0.1832 0.3576  41   PRO A O   
309   C  CB  . PRO A  41  ? 0.9442 2.4951 2.9354 0.4989  -0.1775 0.2807  41   PRO A CB  
310   C  CG  . PRO A  41  ? 0.9322 2.4726 2.9273 0.4906  -0.1973 0.2440  41   PRO A CG  
311   C  CD  . PRO A  41  ? 0.9275 2.5602 2.9742 0.4685  -0.2012 0.2458  41   PRO A CD  
312   N  N   . LYS A  42  ? 0.9653 2.5253 3.1295 0.3929  -0.2208 0.3124  42   LYS A N   
313   C  CA  . LYS A  42  ? 1.0047 2.4937 3.1817 0.3547  -0.2365 0.3219  42   LYS A CA  
314   C  C   . LYS A  42  ? 1.0347 2.5725 3.2578 0.3029  -0.2419 0.3422  42   LYS A C   
315   O  O   . LYS A  42  ? 1.0731 2.5520 3.3153 0.2644  -0.2611 0.3449  42   LYS A O   
316   C  CB  . LYS A  42  ? 1.0072 2.4138 3.1900 0.3521  -0.2610 0.2858  42   LYS A CB  
317   C  CG  . LYS A  42  ? 0.9953 2.3289 3.1354 0.3898  -0.2595 0.2778  42   LYS A CG  
318   C  CD  . LYS A  42  ? 1.0089 2.2588 3.1638 0.3823  -0.2824 0.2495  42   LYS A CD  
319   C  CE  . LYS A  42  ? 1.1557 2.3354 3.2751 0.4125  -0.2827 0.2522  42   LYS A CE  
320   N  NZ  . LYS A  42  ? 1.3437 2.4466 3.4838 0.4094  -0.3030 0.2266  42   LYS A NZ  
321   N  N   . ALA A  43  ? 1.3341 2.9781 3.5770 0.3011  -0.2262 0.3579  43   ALA A N   
322   C  CA  . ALA A  43  ? 1.2340 2.9389 3.5260 0.2492  -0.2324 0.3770  43   ALA A CA  
323   C  C   . ALA A  43  ? 1.2352 2.9397 3.5232 0.2239  -0.2190 0.4206  43   ALA A C   
324   O  O   . ALA A  43  ? 1.0795 2.8126 3.3368 0.2528  -0.1908 0.4438  43   ALA A O   
325   C  CB  . ALA A  43  ? 1.0187 2.8476 3.3395 0.2578  -0.2216 0.3792  43   ALA A CB  
326   N  N   . ASN A  44  ? 1.1302 2.8028 3.4471 0.1683  -0.2388 0.4319  44   ASN A N   
327   C  CA  . ASN A  44  ? 1.1723 2.8553 3.4907 0.1342  -0.2283 0.4767  44   ASN A CA  
328   C  C   . ASN A  44  ? 1.1624 2.9810 3.5088 0.1267  -0.2032 0.5043  44   ASN A C   
329   O  O   . ASN A  44  ? 1.1443 3.0418 3.5333 0.1144  -0.2098 0.4935  44   ASN A O   
330   C  CB  . ASN A  44  ? 1.2279 2.8453 3.5742 0.0733  -0.2587 0.4821  44   ASN A CB  
331   C  CG  . ASN A  44  ? 1.3240 2.8074 3.6402 0.0794  -0.2762 0.4749  44   ASN A CG  
332   O  OD1 . ASN A  44  ? 1.2739 2.7231 3.5483 0.1043  -0.2623 0.4939  44   ASN A OD1 
333   N  ND2 . ASN A  44  ? 2.2287 3.6357 4.5659 0.0572  -0.3071 0.4471  44   ASN A ND2 
334   N  N   . THR A  45  ? 1.3778 3.2265 3.6994 0.1354  -0.1736 0.5401  45   THR A N   
335   C  CA  . THR A  45  ? 1.2950 3.2750 3.6437 0.1308  -0.1442 0.5701  45   THR A CA  
336   C  C   . THR A  45  ? 1.2400 3.2302 3.5986 0.0756  -0.1388 0.6145  45   THR A C   
337   O  O   . THR A  45  ? 1.4391 3.3307 3.7821 0.0422  -0.1599 0.6223  45   THR A O   
338   C  CB  . THR A  45  ? 1.2549 3.2761 3.5625 0.1964  -0.1063 0.5719  45   THR A CB  
339   O  OG1 . THR A  45  ? 1.3082 3.2547 3.5547 0.2073  -0.0920 0.5889  45   THR A OG1 
340   C  CG2 . THR A  45  ? 1.2445 3.2410 3.5357 0.2487  -0.1144 0.5302  45   THR A CG2 
341   N  N   . THR A  46  ? 1.2789 3.3921 3.6650 0.0669  -0.1097 0.6456  46   THR A N   
342   C  CA  . THR A  46  ? 1.5074 3.6503 3.9045 0.0132  -0.0994 0.6916  46   THR A CA  
343   C  C   . THR A  46  ? 1.5082 3.6285 3.8423 0.0378  -0.0654 0.7168  46   THR A C   
344   O  O   . THR A  46  ? 1.6528 3.8033 3.9869 -0.0028 -0.0509 0.7578  46   THR A O   
345   C  CB  . THR A  46  ? 1.4004 3.6980 3.8644 -0.0139 -0.0843 0.7152  46   THR A CB  
346   O  OG1 . THR A  46  ? 1.2443 3.6398 3.7058 0.0474  -0.0457 0.7130  46   THR A OG1 
347   C  CG2 . THR A  46  ? 1.2702 3.5873 3.7928 -0.0484 -0.1221 0.6928  46   THR A CG2 
348   N  N   . GLN A  47  ? 1.3818 3.4497 3.6593 0.1002  -0.0531 0.6936  47   GLN A N   
349   C  CA  . GLN A  47  ? 1.4378 3.4790 3.6461 0.1261  -0.0214 0.7132  47   GLN A CA  
350   C  C   . GLN A  47  ? 1.5574 3.5005 3.7333 0.0790  -0.0396 0.7395  47   GLN A C   
351   O  O   . GLN A  47  ? 1.6258 3.4644 3.8024 0.0618  -0.0791 0.7238  47   GLN A O   
352   C  CB  . GLN A  47  ? 1.4308 3.4139 3.5833 0.1956  -0.0149 0.6792  47   GLN A CB  
353   C  CG  . GLN A  47  ? 1.4075 3.4869 3.5788 0.2490  0.0100  0.6603  47   GLN A CG  
354   C  CD  . GLN A  47  ? 1.3541 3.3636 3.4823 0.3077  0.0027  0.6214  47   GLN A CD  
355   O  OE1 . GLN A  47  ? 1.4118 3.3085 3.5098 0.3048  -0.0257 0.6044  47   GLN A OE1 
356   N  NE2 . GLN A  47  ? 1.2856 3.3627 3.4122 0.3614  0.0281  0.6087  47   GLN A NE2 
357   N  N   . PRO A  48  ? 1.4272 3.4013 3.5750 0.0577  -0.0116 0.7802  48   PRO A N   
358   C  CA  . PRO A  48  ? 1.5052 3.3924 3.6238 0.0069  -0.0305 0.8120  48   PRO A CA  
359   C  C   . PRO A  48  ? 1.6789 3.4286 3.7332 0.0340  -0.0515 0.7957  48   PRO A C   
360   O  O   . PRO A  48  ? 1.6288 3.3613 3.6205 0.0827  -0.0284 0.7869  48   PRO A O   
361   C  CB  . PRO A  48  ? 1.5399 3.5050 3.6300 -0.0071 0.0138  0.8548  48   PRO A CB  
362   C  CG  . PRO A  48  ? 1.5848 3.6967 3.7214 0.0185  0.0497  0.8495  48   PRO A CG  
363   C  CD  . PRO A  48  ? 1.4322 3.5278 3.5753 0.0789  0.0400  0.8002  48   PRO A CD  
364   N  N   . GLY A  49  ? 1.7829 3.4335 3.8541 0.0021  -0.0965 0.7914  49   GLY A N   
365   C  CA  . GLY A  49  ? 1.6717 3.1945 3.6927 0.0210  -0.1207 0.7817  49   GLY A CA  
366   C  C   . GLY A  49  ? 1.4719 2.9594 3.4838 0.0803  -0.1282 0.7332  49   GLY A C   
367   O  O   . GLY A  49  ? 1.5305 2.9179 3.5043 0.0988  -0.1484 0.7237  49   GLY A O   
368   N  N   . ILE A  50  ? 1.4390 3.0076 3.4851 0.1094  -0.1136 0.7045  50   ILE A N   
369   C  CA  . ILE A  50  ? 1.4783 3.0237 3.5137 0.1655  -0.1177 0.6603  50   ILE A CA  
370   C  C   . ILE A  50  ? 1.5624 3.0749 3.6550 0.1510  -0.1545 0.6292  50   ILE A C   
371   O  O   . ILE A  50  ? 1.5699 3.1525 3.7196 0.1272  -0.1576 0.6242  50   ILE A O   
372   C  CB  . ILE A  50  ? 1.4363 3.0856 3.4683 0.2100  -0.0795 0.6490  50   ILE A CB  
373   C  CG1 . ILE A  50  ? 1.3512 3.0273 3.3219 0.2245  -0.0400 0.6777  50   ILE A CG1 
374   C  CG2 . ILE A  50  ? 1.4985 3.1178 3.5166 0.2648  -0.0863 0.6055  50   ILE A CG2 
375   C  CD1 . ILE A  50  ? 1.3220 3.0791 3.2772 0.2795  -0.0011 0.6638  50   ILE A CD1 
376   N  N   . VAL A  51  ? 1.4256 2.8327 3.5024 0.1643  -0.1825 0.6083  51   VAL A N   
377   C  CA  . VAL A  51  ? 1.4113 2.7760 3.5343 0.1565  -0.2151 0.5738  51   VAL A CA  
378   C  C   . VAL A  51  ? 1.2789 2.6629 3.3968 0.2093  -0.2094 0.5310  51   VAL A C   
379   O  O   . VAL A  51  ? 1.2235 2.5696 3.2933 0.2515  -0.2021 0.5217  51   VAL A O   
380   C  CB  . VAL A  51  ? 1.6317 2.8740 3.7490 0.1404  -0.2486 0.5764  51   VAL A CB  
381   C  CG1 . VAL A  51  ? 1.7108 2.8943 3.7644 0.1706  -0.2433 0.5895  51   VAL A CG1 
382   C  CG2 . VAL A  51  ? 1.6072 2.8003 3.7602 0.1506  -0.2757 0.5314  51   VAL A CG2 
383   N  N   . GLU A  52  ? 1.2107 2.6533 3.3757 0.2037  -0.2141 0.5067  52   GLU A N   
384   C  CA  . GLU A  52  ? 1.1556 2.6208 3.3200 0.2475  -0.2118 0.4669  52   GLU A CA  
385   C  C   . GLU A  52  ? 1.1546 2.6677 3.2741 0.2973  -0.1792 0.4718  52   GLU A C   
386   O  O   . GLU A  52  ? 1.1038 2.5751 3.1857 0.3398  -0.1782 0.4508  52   GLU A O   
387   C  CB  . GLU A  52  ? 1.1470 2.5134 3.3043 0.2631  -0.2376 0.4339  52   GLU A CB  
388   C  CG  . GLU A  52  ? 1.1715 2.4950 3.3758 0.2233  -0.2680 0.4168  52   GLU A CG  
389   C  CD  . GLU A  52  ? 1.6349 2.8765 3.8363 0.2464  -0.2877 0.3786  52   GLU A CD  
390   O  OE1 . GLU A  52  ? 1.6671 2.8764 3.9040 0.2230  -0.3096 0.3539  52   GLU A OE1 
391   O  OE2 . GLU A  52  ? 1.8252 3.0355 3.9881 0.2874  -0.2808 0.3727  52   GLU A OE2 
392   N  N   . GLY A  53  ? 1.2089 2.8100 3.3323 0.2912  -0.1517 0.5004  53   GLY A N   
393   C  CA  . GLY A  53  ? 1.1346 2.7865 3.2188 0.3403  -0.1179 0.5034  53   GLY A CA  
394   C  C   . GLY A  53  ? 1.1342 2.8354 3.2333 0.3789  -0.1161 0.4720  53   GLY A C   
395   O  O   . GLY A  53  ? 1.0536 2.7529 3.1093 0.4287  -0.0984 0.4624  53   GLY A O   
396   N  N   . GLY A  54  ? 1.2408 2.9824 3.3970 0.3550  -0.1356 0.4561  54   GLY A N   
397   C  CA  . GLY A  54  ? 1.0080 2.8029 3.1809 0.3853  -0.1370 0.4294  54   GLY A CA  
398   C  C   . GLY A  54  ? 0.9982 2.9214 3.2031 0.3942  -0.1129 0.4482  54   GLY A C   
399   O  O   . GLY A  54  ? 1.0204 2.9896 3.2186 0.3950  -0.0850 0.4792  54   GLY A O   
400   N  N   . GLN A  55  ? 0.9772 2.9486 3.2018 0.3986  -0.1233 0.4242  55   GLN A N   
401   C  CA  . GLN A  55  ? 0.9877 3.0568 3.2173 0.4040  -0.1035 0.4303  55   GLN A CA  
402   C  C   . GLN A  55  ? 0.9809 3.0461 3.1740 0.4286  -0.1126 0.3887  55   GLN A C   
403   O  O   . GLN A  55  ? 0.9659 2.9698 3.1418 0.4303  -0.1365 0.3567  55   GLN A O   
404   C  CB  . GLN A  55  ? 1.0993 3.2599 3.4125 0.3473  -0.1122 0.4591  55   GLN A CB  
405   C  CG  . GLN A  55  ? 0.9893 3.1357 3.3549 0.3012  -0.1528 0.4429  55   GLN A CG  
406   C  CD  . GLN A  55  ? 1.1328 3.3510 3.5686 0.2370  -0.1630 0.4722  55   GLN A CD  
407   O  OE1 . GLN A  55  ? 1.0247 3.3108 3.4770 0.2264  -0.1386 0.5089  55   GLN A OE1 
408   N  NE2 . GLN A  55  ? 1.1480 3.3416 3.6121 0.1913  -0.1981 0.4520  55   GLN A NE2 
409   N  N   . VAL A  56  ? 1.2540 3.3876 3.4388 0.4472  -0.0929 0.3916  56   VAL A N   
410   C  CA  . VAL A  56  ? 1.1943 3.3412 3.3587 0.4654  -0.1025 0.3609  56   VAL A CA  
411   C  C   . VAL A  56  ? 1.1206 3.3757 3.3499 0.4305  -0.1091 0.3751  56   VAL A C   
412   O  O   . VAL A  56  ? 1.0225 3.3511 3.2798 0.4242  -0.0859 0.4061  56   VAL A O   
413   C  CB  . VAL A  56  ? 1.2057 3.3254 3.3035 0.5213  -0.0766 0.3518  56   VAL A CB  
414   C  CG1 . VAL A  56  ? 1.3138 3.4502 3.4007 0.5364  -0.0886 0.3272  56   VAL A CG1 
415   C  CG2 . VAL A  56  ? 1.0062 3.0179 3.0386 0.5502  -0.0737 0.3380  56   VAL A CG2 
416   N  N   . LEU A  57  ? 0.9936 3.2619 3.2466 0.4066  -0.1404 0.3534  57   LEU A N   
417   C  CA  . LEU A  57  ? 1.0040 3.3709 3.3212 0.3649  -0.1542 0.3660  57   LEU A CA  
418   C  C   . LEU A  57  ? 1.0155 3.4236 3.3193 0.3895  -0.1553 0.3520  57   LEU A C   
419   O  O   . LEU A  57  ? 1.0078 3.3599 3.2639 0.4216  -0.1634 0.3229  57   LEU A O   
420   C  CB  . LEU A  57  ? 0.9923 3.3536 3.3546 0.3128  -0.1920 0.3555  57   LEU A CB  
421   C  CG  . LEU A  57  ? 0.9900 3.3247 3.3930 0.2722  -0.1987 0.3775  57   LEU A CG  
422   C  CD1 . LEU A  57  ? 1.1379 3.3583 3.4996 0.2973  -0.2016 0.3588  57   LEU A CD1 
423   C  CD2 . LEU A  57  ? 0.9976 3.3721 3.4703 0.2062  -0.2339 0.3800  57   LEU A CD2 
424   N  N   . LYS A  58  ? 1.4457 3.9528 3.7953 0.3722  -0.1481 0.3760  58   LYS A N   
425   C  CA  . LYS A  58  ? 1.3253 3.8871 3.6801 0.3877  -0.1526 0.3711  58   LYS A CA  
426   C  C   . LYS A  58  ? 1.0820 3.7014 3.4903 0.3341  -0.1903 0.3669  58   LYS A C   
427   O  O   . LYS A  58  ? 1.1396 3.8295 3.6058 0.2852  -0.1956 0.3909  58   LYS A O   
428   C  CB  . LYS A  58  ? 1.0828 3.7202 3.4555 0.4058  -0.1191 0.4017  58   LYS A CB  
429   C  CG  . LYS A  58  ? 1.1056 3.7982 3.4862 0.4288  -0.1210 0.4015  58   LYS A CG  
430   C  CD  . LYS A  58  ? 1.1665 3.9556 3.5856 0.4335  -0.0905 0.4359  58   LYS A CD  
431   C  CE  . LYS A  58  ? 1.1432 4.0184 3.6323 0.3692  -0.0994 0.4621  58   LYS A CE  
432   N  NZ  . LYS A  58  ? 1.1771 4.1559 3.7078 0.3710  -0.0700 0.4965  58   LYS A NZ  
433   N  N   . CYS A  59  ? 1.1022 3.6915 3.4903 0.3400  -0.2171 0.3377  59   CYS A N   
434   C  CA  . CYS A  59  ? 1.1103 3.7490 3.5416 0.2905  -0.2553 0.3300  59   CYS A CA  
435   C  C   . CYS A  59  ? 1.1320 3.8392 3.5753 0.3008  -0.2639 0.3348  59   CYS A C   
436   O  O   . CYS A  59  ? 1.1330 3.8130 3.5353 0.3519  -0.2514 0.3286  59   CYS A O   
437   C  CB  . CYS A  59  ? 1.2003 3.7651 3.6060 0.2838  -0.2820 0.2952  59   CYS A CB  
438   S  SG  . CYS A  59  ? 1.3374 3.8179 3.7378 0.2693  -0.2784 0.2903  59   CYS A SG  
439   N  N   . ASP A  60  ? 1.0911 3.8855 3.5918 0.2496  -0.2870 0.3482  60   ASP A N   
440   C  CA  . ASP A  60  ? 1.1882 4.0611 3.7113 0.2514  -0.2987 0.3588  60   ASP A CA  
441   C  C   . ASP A  60  ? 1.1370 4.0035 3.6547 0.2292  -0.3408 0.3340  60   ASP A C   
442   O  O   . ASP A  60  ? 1.1066 3.9503 3.6335 0.1860  -0.3655 0.3168  60   ASP A O   
443   C  CB  . ASP A  60  ? 1.2335 4.2140 3.8237 0.2067  -0.2979 0.3926  60   ASP A CB  
444   C  CG  . ASP A  60  ? 1.1796 4.2492 3.8004 0.2031  -0.3146 0.4058  60   ASP A CG  
445   O  OD1 . ASP A  60  ? 1.1859 4.2500 3.7806 0.2572  -0.3029 0.4057  60   ASP A OD1 
446   O  OD2 . ASP A  60  ? 1.2028 4.3469 3.8744 0.1443  -0.3408 0.4181  60   ASP A OD2 
447   N  N   . TRP A  61  ? 1.4449 4.3245 3.9438 0.2615  -0.3481 0.3316  61   TRP A N   
448   C  CA  . TRP A  61  ? 1.3533 4.2431 3.8488 0.2392  -0.3887 0.3140  61   TRP A CA  
449   C  C   . TRP A  61  ? 1.4681 4.4678 4.0211 0.1897  -0.4161 0.3340  61   TRP A C   
450   O  O   . TRP A  61  ? 1.2555 4.3272 3.8470 0.1891  -0.4003 0.3640  61   TRP A O   
451   C  CB  . TRP A  61  ? 1.1961 4.0408 3.6398 0.2953  -0.3863 0.3045  61   TRP A CB  
452   C  CG  . TRP A  61  ? 1.2147 4.0954 3.6594 0.2772  -0.4255 0.2984  61   TRP A CG  
453   C  CD1 . TRP A  61  ? 1.2829 4.2151 3.7322 0.2980  -0.4341 0.3163  61   TRP A CD1 
454   C  CD2 . TRP A  61  ? 1.3640 4.2351 3.8044 0.2336  -0.4626 0.2738  61   TRP A CD2 
455   N  NE1 . TRP A  61  ? 1.4570 4.4119 3.9022 0.2693  -0.4751 0.3059  61   TRP A NE1 
456   C  CE2 . TRP A  61  ? 1.5368 4.4554 3.9750 0.2288  -0.4926 0.2787  61   TRP A CE2 
457   C  CE3 . TRP A  61  ? 1.3226 4.1513 3.7617 0.1981  -0.4738 0.2484  61   TRP A CE3 
458   C  CZ2 . TRP A  61  ? 1.6013 4.5267 4.0307 0.1879  -0.5329 0.2582  61   TRP A CZ2 
459   C  CZ3 . TRP A  61  ? 1.4026 4.2383 3.8371 0.1588  -0.5129 0.2263  61   TRP A CZ3 
460   C  CH2 . TRP A  61  ? 1.4829 4.3666 3.9099 0.1531  -0.5417 0.2308  61   TRP A CH2 
461   N  N   . ARG A  65  ? 1.2724 4.3343 3.9664 -0.0314 -0.4501 0.3559  65   ARG A N   
462   C  CA  . ARG A  65  ? 1.4570 4.4221 4.0952 0.0259  -0.4327 0.3302  65   ARG A CA  
463   C  C   . ARG A  65  ? 1.4149 4.3130 4.0511 0.0206  -0.4143 0.3305  65   ARG A C   
464   O  O   . ARG A  65  ? 1.1828 4.0004 3.7912 0.0290  -0.4211 0.3038  65   ARG A O   
465   C  CB  . ARG A  65  ? 1.3382 4.2672 3.9479 0.0196  -0.4673 0.2945  65   ARG A CB  
466   C  CG  . ARG A  65  ? 1.2562 4.2551 3.8723 0.0106  -0.4940 0.2974  65   ARG A CG  
467   C  CD  . ARG A  65  ? 1.2731 4.2380 3.8566 0.0026  -0.5276 0.2634  65   ARG A CD  
468   N  NE  . ARG A  65  ? 1.3665 4.3367 3.9742 -0.0739 -0.5657 0.2468  65   ARG A NE  
469   C  CZ  . ARG A  65  ? 1.4210 4.3671 4.0059 -0.0971 -0.5990 0.2149  65   ARG A CZ  
470   N  NH1 . ARG A  65  ? 1.3879 4.3069 3.9259 -0.0492 -0.5981 0.1990  65   ARG A NH1 
471   N  NH2 . ARG A  65  ? 1.4051 4.3510 4.0117 -0.1714 -0.6340 0.1992  65   ARG A NH2 
472   N  N   . ARG A  66  ? 1.3426 4.2766 4.0099 0.0076  -0.3908 0.3633  66   ARG A N   
473   C  CA  . ARG A  66  ? 1.2217 4.1020 3.8940 -0.0032 -0.3744 0.3732  66   ARG A CA  
474   C  C   . ARG A  66  ? 1.2254 4.0533 3.8509 0.0695  -0.3310 0.3758  66   ARG A C   
475   O  O   . ARG A  66  ? 1.1250 3.9780 3.7276 0.1197  -0.3082 0.3808  66   ARG A O   
476   C  CB  . ARG A  66  ? 1.1835 4.1313 3.9128 -0.0622 -0.3730 0.4108  66   ARG A CB  
477   C  CG  . ARG A  66  ? 1.2227 4.2197 3.9960 -0.1419 -0.4172 0.4103  66   ARG A CG  
478   C  CD  . ARG A  66  ? 1.4504 4.5273 4.2756 -0.1940 -0.4115 0.4514  66   ARG A CD  
479   N  NE  . ARG A  66  ? 1.4625 4.6198 4.2928 -0.1512 -0.3777 0.4767  66   ARG A NE  
480   C  CZ  . ARG A  66  ? 1.2946 4.5372 4.1455 -0.1561 -0.3887 0.4842  66   ARG A CZ  
481   N  NH1 . ARG A  66  ? 1.3765 4.6369 4.2399 -0.2040 -0.4333 0.4679  66   ARG A NH1 
482   N  NH2 . ARG A  66  ? 1.3014 4.6111 4.1610 -0.1136 -0.3559 0.5084  66   ARG A NH2 
483   N  N   . CYS A  67  ? 1.2580 4.0079 3.8701 0.0727  -0.3220 0.3733  67   CYS A N   
484   C  CA  . CYS A  67  ? 1.0605 3.7524 3.6259 0.1330  -0.2839 0.3764  67   CYS A CA  
485   C  C   . CYS A  67  ? 1.0733 3.7984 3.6658 0.1188  -0.2560 0.4165  67   CYS A C   
486   O  O   . CYS A  67  ? 1.0888 3.8363 3.7313 0.0578  -0.2703 0.4374  67   CYS A O   
487   C  CB  . CYS A  67  ? 1.2254 3.8074 3.7556 0.1501  -0.2909 0.3500  67   CYS A CB  
488   S  SG  . CYS A  67  ? 1.4767 4.0123 3.9659 0.1735  -0.3175 0.3023  67   CYS A SG  
489   N  N   . GLN A  68  ? 1.0807 3.8051 3.6385 0.1733  -0.2167 0.4277  68   GLN A N   
490   C  CA  . GLN A  68  ? 1.2967 4.0592 3.8727 0.1686  -0.1842 0.4661  68   GLN A CA  
491   C  C   . GLN A  68  ? 1.0777 3.7599 3.5973 0.2219  -0.1539 0.4635  68   GLN A C   
492   O  O   . GLN A  68  ? 1.0695 3.7086 3.5329 0.2801  -0.1413 0.4406  68   GLN A O   
493   C  CB  . GLN A  68  ? 1.3910 4.2575 3.9885 0.1795  -0.1630 0.4875  68   GLN A CB  
494   C  CG  . GLN A  68  ? 1.1527 4.1196 3.8209 0.1116  -0.1803 0.5136  68   GLN A CG  
495   C  CD  . GLN A  68  ? 1.1638 4.1415 3.8689 0.0578  -0.1758 0.5469  68   GLN A CD  
496   O  OE1 . GLN A  68  ? 1.1563 4.1011 3.8406 0.0799  -0.1464 0.5625  68   GLN A OE1 
497   N  NE2 . GLN A  68  ? 1.2867 4.3071 4.0452 -0.0162 -0.2071 0.5590  68   GLN A NE2 
498   N  N   . PRO A  69  ? 1.1233 3.7799 3.6550 0.2016  -0.1439 0.4877  69   PRO A N   
499   C  CA  . PRO A  69  ? 1.3820 3.9665 3.8599 0.2501  -0.1157 0.4887  69   PRO A CA  
500   C  C   . PRO A  69  ? 1.1301 3.7579 3.5782 0.2989  -0.0728 0.5019  69   PRO A C   
501   O  O   . PRO A  69  ? 1.1546 3.8790 3.6408 0.2828  -0.0560 0.5287  69   PRO A O   
502   C  CB  . PRO A  69  ? 1.3179 3.8869 3.8329 0.2051  -0.1184 0.5212  69   PRO A CB  
503   C  CG  . PRO A  69  ? 1.2348 3.8251 3.8117 0.1363  -0.1588 0.5219  69   PRO A CG  
504   C  CD  . PRO A  69  ? 1.1346 3.8143 3.7289 0.1291  -0.1639 0.5143  69   PRO A CD  
505   N  N   . ILE A  70  ? 1.3908 3.9450 3.7705 0.3582  -0.0555 0.4819  70   ILE A N   
506   C  CA  . ILE A  70  ? 1.1316 3.7073 3.4759 0.4084  -0.0136 0.4925  70   ILE A CA  
507   C  C   . ILE A  70  ? 1.1662 3.7218 3.4971 0.4119  0.0140  0.5205  70   ILE A C   
508   O  O   . ILE A  70  ? 1.1776 3.6429 3.4749 0.4203  0.0058  0.5115  70   ILE A O   
509   C  CB  . ILE A  70  ? 1.1652 3.6694 3.4407 0.4676  -0.0115 0.4571  70   ILE A CB  
510   C  CG1 . ILE A  70  ? 1.0913 3.6159 3.3818 0.4616  -0.0410 0.4330  70   ILE A CG1 
511   C  CG2 . ILE A  70  ? 1.1669 3.6932 3.4100 0.5177  0.0311  0.4685  70   ILE A CG2 
512   C  CD1 . ILE A  70  ? 1.2401 3.6944 3.4673 0.5131  -0.0426 0.4017  70   ILE A CD1 
513   N  N   . GLU A  71  ? 1.2385 3.8816 3.5978 0.4043  0.0466  0.5563  71   GLU A N   
514   C  CA  . GLU A  71  ? 1.3226 3.9652 3.6731 0.4049  0.0769  0.5891  71   GLU A CA  
515   C  C   . GLU A  71  ? 1.3754 3.9647 3.6499 0.4738  0.1103  0.5768  71   GLU A C   
516   O  O   . GLU A  71  ? 1.4526 4.0955 3.7138 0.5078  0.1466  0.5838  71   GLU A O   
517   C  CB  . GLU A  71  ? 1.5581 4.3200 3.9645 0.3695  0.1019  0.6318  71   GLU A CB  
518   C  CG  . GLU A  71  ? 1.5711 4.3411 3.9747 0.3596  0.1312  0.6708  71   GLU A CG  
519   C  CD  . GLU A  71  ? 1.6043 4.4965 4.0591 0.3226  0.1591  0.7136  71   GLU A CD  
520   O  OE1 . GLU A  71  ? 1.3345 4.3049 3.8266 0.3092  0.1564  0.7119  71   GLU A OE1 
521   O  OE2 . GLU A  71  ? 1.6297 4.5417 4.0869 0.3060  0.1840  0.7504  71   GLU A OE2 
522   N  N   . PHE A  72  ? 1.4247 3.9053 3.6487 0.4942  0.0977  0.5584  72   PHE A N   
523   C  CA  . PHE A  72  ? 1.4410 3.8619 3.5898 0.5532  0.1268  0.5498  72   PHE A CA  
524   C  C   . PHE A  72  ? 1.2312 3.6690 3.3762 0.5511  0.1583  0.5885  72   PHE A C   
525   O  O   . PHE A  72  ? 1.2640 3.7154 3.3667 0.5940  0.1997  0.5956  72   PHE A O   
526   C  CB  . PHE A  72  ? 1.1932 3.4905 3.2865 0.5749  0.0982  0.5130  72   PHE A CB  
527   C  CG  . PHE A  72  ? 1.2517 3.5260 3.3259 0.5939  0.0785  0.4740  72   PHE A CG  
528   C  CD1 . PHE A  72  ? 1.2556 3.5092 3.2760 0.6464  0.0992  0.4573  72   PHE A CD1 
529   C  CD2 . PHE A  72  ? 1.2046 3.4782 3.3157 0.5584  0.0391  0.4561  72   PHE A CD2 
530   C  CE1 . PHE A  72  ? 1.2130 3.4465 3.2203 0.6610  0.0795  0.4269  72   PHE A CE1 
531   C  CE2 . PHE A  72  ? 1.1584 3.4161 3.2528 0.5746  0.0212  0.4238  72   PHE A CE2 
532   C  CZ  . PHE A  72  ? 1.1833 3.4213 3.2275 0.6249  0.0407  0.4110  72   PHE A CZ  
533   N  N   . ASP A  73  ? 1.2287 3.6659 3.4185 0.5009  0.1392  0.6151  73   ASP A N   
534   C  CA  . ASP A  73  ? 1.3204 3.7318 3.4764 0.4833  0.1612  0.6443  73   ASP A CA  
535   C  C   . ASP A  73  ? 1.3955 3.8016 3.5913 0.4037  0.1341  0.6657  73   ASP A C   
536   O  O   . ASP A  73  ? 1.4461 3.7808 3.6550 0.3735  0.0902  0.6487  73   ASP A O   
537   C  CB  . ASP A  73  ? 1.4125 3.6790 3.4728 0.5112  0.1548  0.6228  73   ASP A CB  
538   C  CG  . ASP A  73  ? 1.5378 3.7414 3.5388 0.4802  0.1664  0.6458  73   ASP A CG  
539   O  OD1 . ASP A  73  ? 1.5606 3.8385 3.5623 0.4719  0.2042  0.6746  73   ASP A OD1 
540   O  OD2 . ASP A  73  ? 1.6891 3.7717 3.6432 0.4639  0.1378  0.6364  73   ASP A OD2 
541   N  N   . ALA A  74  ? 1.4419 3.9223 3.6565 0.3697  0.1608  0.7029  74   ALA A N   
542   C  CA  . ALA A  74  ? 1.5341 4.0101 3.7830 0.2909  0.1375  0.7288  74   ALA A CA  
543   C  C   . ALA A  74  ? 1.5870 3.9650 3.7648 0.2639  0.1410  0.7476  74   ALA A C   
544   O  O   . ALA A  74  ? 1.6258 3.9726 3.8216 0.1991  0.1162  0.7684  74   ALA A O   
545   C  CB  . ALA A  74  ? 1.5530 4.1856 3.8791 0.2591  0.1599  0.7630  74   ALA A CB  
546   N  N   . THR A  75  ? 1.5580 3.8856 3.6540 0.3103  0.1698  0.7421  75   THR A N   
547   C  CA  . THR A  75  ? 1.5610 3.8051 3.5832 0.2865  0.1760  0.7630  75   THR A CA  
548   C  C   . THR A  75  ? 1.5221 3.6148 3.5036 0.2754  0.1298  0.7444  75   THR A C   
549   O  O   . THR A  75  ? 1.5500 3.5958 3.5427 0.3012  0.1021  0.7097  75   THR A O   
550   C  CB  . THR A  75  ? 1.6532 3.9053 3.5984 0.3392  0.2264  0.7636  75   THR A CB  
551   O  OG1 . THR A  75  ? 1.5928 3.7647 3.4862 0.3993  0.2196  0.7253  75   THR A OG1 
552   C  CG2 . THR A  75  ? 1.8321 4.2391 3.8247 0.3629  0.2746  0.7767  75   THR A CG2 
553   N  N   . GLY A  76  ? 1.4498 3.4696 3.3847 0.2361  0.1221  0.7699  76   GLY A N   
554   C  CA  . GLY A  76  ? 1.5392 3.4178 3.4316 0.2265  0.0818  0.7592  76   GLY A CA  
555   C  C   . GLY A  76  ? 1.6229 3.4255 3.4209 0.2755  0.0959  0.7446  76   GLY A C   
556   O  O   . GLY A  76  ? 1.6745 3.5154 3.4472 0.3309  0.1273  0.7253  76   GLY A O   
557   N  N   . ASN A  77  ? 1.5356 3.2259 3.2807 0.2543  0.0703  0.7547  77   ASN A N   
558   C  CA  . ASN A  77  ? 1.6347 3.2422 3.2851 0.2912  0.0770  0.7442  77   ASN A CA  
559   C  C   . ASN A  77  ? 1.7555 3.3930 3.3353 0.2894  0.1213  0.7721  77   ASN A C   
560   O  O   . ASN A  77  ? 1.9150 3.5507 3.4845 0.2386  0.1208  0.8101  77   ASN A O   
561   C  CB  . ASN A  77  ? 1.7669 3.2483 3.3938 0.2681  0.0292  0.7462  77   ASN A CB  
562   C  CG  . ASN A  77  ? 1.7278 3.1717 3.4135 0.2779  -0.0103 0.7132  77   ASN A CG  
563   O  OD1 . ASN A  77  ? 1.7526 3.2659 3.5048 0.2867  -0.0079 0.6942  77   ASN A OD1 
564   N  ND2 . ASN A  77  ? 1.6668 3.0035 3.3280 0.2763  -0.0467 0.7065  77   ASN A ND2 
565   N  N   . ARG A  78  ? 1.7694 3.4302 3.2969 0.3445  0.1598  0.7531  78   ARG A N   
566   C  CA  . ARG A  78  ? 2.0011 3.6757 3.4465 0.3491  0.2037  0.7731  78   ARG A CA  
567   C  C   . ARG A  78  ? 2.1385 3.6931 3.4941 0.3259  0.1810  0.7878  78   ARG A C   
568   O  O   . ARG A  78  ? 2.0935 3.5505 3.4319 0.3333  0.1406  0.7705  78   ARG A O   
569   C  CB  . ARG A  78  ? 2.0444 3.7534 3.4486 0.4185  0.2473  0.7443  78   ARG A CB  
570   C  CG  . ARG A  78  ? 1.9969 3.8474 3.4774 0.4406  0.2845  0.7425  78   ARG A CG  
571   C  CD  . ARG A  78  ? 1.9748 3.8446 3.4210 0.5162  0.3199  0.7104  78   ARG A CD  
572   N  NE  . ARG A  78  ? 1.9914 3.7873 3.4370 0.5505  0.2851  0.6743  78   ARG A NE  
573   C  CZ  . ARG A  78  ? 1.8884 3.6888 3.3155 0.6145  0.3035  0.6441  78   ARG A CZ  
574   N  NH1 . ARG A  78  ? 1.8374 3.7107 3.2466 0.6557  0.3571  0.6437  78   ARG A NH1 
575   N  NH2 . ARG A  78  ? 1.9206 3.6521 3.3471 0.6379  0.2689  0.6148  78   ARG A NH2 
576   N  N   . ASP A  79  ? 2.0814 3.6484 3.3807 0.2959  0.2071  0.8218  79   ASP A N   
577   C  CA  . ASP A  79  ? 2.2183 3.6810 3.4233 0.2711  0.1894  0.8413  79   ASP A CA  
578   C  C   . ASP A  79  ? 2.2861 3.7189 3.3790 0.3162  0.2264  0.8236  79   ASP A C   
579   O  O   . ASP A  79  ? 2.2939 3.8069 3.3673 0.3418  0.2815  0.8207  79   ASP A O   
580   C  CB  . ASP A  79  ? 2.3310 3.8162 3.5316 0.2052  0.1925  0.8921  79   ASP A CB  
581   C  CG  . ASP A  79  ? 2.3328 3.7823 3.6083 0.1520  0.1381  0.9134  79   ASP A CG  
582   O  OD1 . ASP A  79  ? 2.3991 3.7530 3.6777 0.1559  0.0903  0.8995  79   ASP A OD1 
583   O  OD2 . ASP A  79  ? 2.2641 3.7799 3.5945 0.1056  0.1436  0.9446  79   ASP A OD2 
584   N  N   . TYR A  80  ? 2.2724 3.5900 3.2929 0.3264  0.1961  0.8112  80   TYR A N   
585   C  CA  . TYR A  80  ? 2.3888 3.6581 3.2848 0.3537  0.2251  0.8014  80   TYR A CA  
586   C  C   . TYR A  80  ? 2.6275 3.8924 3.4490 0.3074  0.2429  0.8424  80   TYR A C   
587   O  O   . TYR A  80  ? 2.7495 4.0444 3.4943 0.3251  0.2949  0.8410  80   TYR A O   
588   C  CB  . TYR A  80  ? 2.4287 3.5781 3.2711 0.3716  0.1832  0.7790  80   TYR A CB  
589   C  CG  . TYR A  80  ? 2.5982 3.6772 3.3013 0.3870  0.2025  0.7730  80   TYR A CG  
590   C  CD1 . TYR A  80  ? 2.6630 3.7430 3.3118 0.4455  0.2399  0.7361  80   TYR A CD1 
591   C  CD2 . TYR A  80  ? 2.7451 3.7526 3.3681 0.3420  0.1814  0.8046  80   TYR A CD2 
592   C  CE1 . TYR A  80  ? 2.7916 3.7995 3.3066 0.4580  0.2570  0.7279  80   TYR A CE1 
593   C  CE2 . TYR A  80  ? 2.8795 3.8202 3.3689 0.3522  0.1973  0.7983  80   TYR A CE2 
594   C  CZ  . TYR A  80  ? 2.9105 3.8497 3.3448 0.4099  0.2355  0.7584  80   TYR A CZ  
595   O  OH  . TYR A  80  ? 3.0471 3.9120 3.3420 0.4186  0.2508  0.7495  80   TYR A OH  
596   N  N   . ALA A  81  ? 2.6087 3.8350 3.4500 0.2484  0.2010  0.8793  81   ALA A N   
597   C  CA  . ALA A  81  ? 2.6806 3.9066 3.4621 0.1957  0.2120  0.9250  81   ALA A CA  
598   C  C   . ALA A  81  ? 2.6165 3.8503 3.4847 0.1358  0.1717  0.9632  81   ALA A C   
599   O  O   . ALA A  81  ? 2.6458 3.8837 3.6141 0.1384  0.1385  0.9502  81   ALA A O   
600   C  CB  . ALA A  81  ? 2.6880 3.8029 3.3400 0.1884  0.1954  0.9313  81   ALA A CB  
601   N  N   . LYS A  82  ? 2.3931 3.6267 3.2191 0.0805  0.1751  1.0104  82   LYS A N   
602   C  CA  . LYS A  82  ? 2.3244 3.5539 3.2217 0.0193  0.1357  1.0513  82   LYS A CA  
603   C  C   . LYS A  82  ? 2.3930 3.5112 3.3150 0.0127  0.0660  1.0485  82   LYS A C   
604   O  O   . LYS A  82  ? 2.4760 3.5026 3.3168 0.0183  0.0425  1.0489  82   LYS A O   
605   C  CB  . LYS A  82  ? 2.4325 3.6676 3.2609 -0.0385 0.1503  1.1048  82   LYS A CB  
606   C  CG  . LYS A  82  ? 2.4452 3.6719 3.3397 -0.1060 0.1106  1.1522  82   LYS A CG  
607   C  CD  . LYS A  82  ? 2.5613 3.7820 3.3740 -0.1641 0.1217  1.2075  82   LYS A CD  
608   C  CE  . LYS A  82  ? 2.5826 3.7797 3.4566 -0.2325 0.0766  1.2572  82   LYS A CE  
609   N  NZ  . LYS A  82  ? 2.7020 3.8824 3.4902 -0.2922 0.0814  1.3150  82   LYS A NZ  
610   N  N   . ASP A  83  ? 2.4227 3.5511 3.4578 0.0016  0.0335  1.0445  83   ASP A N   
611   C  CA  . ASP A  83  ? 2.4129 3.4482 3.4919 0.0005  -0.0293 1.0372  83   ASP A CA  
612   C  C   . ASP A  83  ? 2.4627 3.4494 3.5170 0.0594  -0.0384 0.9900  83   ASP A C   
613   O  O   . ASP A  83  ? 2.4049 3.3023 3.4589 0.0610  -0.0865 0.9879  83   ASP A O   
614   C  CB  . ASP A  83  ? 2.4303 3.3765 3.4661 -0.0503 -0.0724 1.0857  83   ASP A CB  
615   C  CG  . ASP A  83  ? 2.3929 3.3761 3.4546 -0.1140 -0.0700 1.1363  83   ASP A CG  
616   O  OD1 . ASP A  83  ? 2.3170 3.3056 3.4749 -0.1378 -0.0967 1.1426  83   ASP A OD1 
617   O  OD2 . ASP A  83  ? 2.5796 3.5832 3.5618 -0.1424 -0.0418 1.1700  83   ASP A OD2 
618   N  N   . ASP A  84  ? 2.6002 3.6454 3.6364 0.1083  0.0067  0.9533  84   ASP A N   
619   C  CA  . ASP A  84  ? 2.5014 3.5038 3.5068 0.1640  0.0028  0.9090  84   ASP A CA  
620   C  C   . ASP A  84  ? 2.3714 3.4547 3.4449 0.2089  0.0312  0.8683  84   ASP A C   
621   O  O   . ASP A  84  ? 2.3787 3.5195 3.4149 0.2430  0.0807  0.8513  84   ASP A O   
622   C  CB  . ASP A  84  ? 2.5798 3.5455 3.4539 0.1801  0.0288  0.9081  84   ASP A CB  
623   C  CG  . ASP A  84  ? 2.4732 3.3601 3.3036 0.2201  0.0060  0.8743  84   ASP A CG  
624   O  OD1 . ASP A  84  ? 2.3054 3.1439 3.1937 0.2210  -0.0416 0.8658  84   ASP A OD1 
625   O  OD2 . ASP A  84  ? 2.5439 3.4162 3.2803 0.2500  0.0364  0.8562  84   ASP A OD2 
626   N  N   . PRO A  85  ? 2.2212 3.3111 3.3951 0.2105  0.0009  0.8521  85   PRO A N   
627   C  CA  . PRO A  85  ? 2.0488 3.2195 3.2912 0.2482  0.0238  0.8167  85   PRO A CA  
628   C  C   . PRO A  85  ? 2.1202 3.2734 3.3128 0.3095  0.0406  0.7760  85   PRO A C   
629   O  O   . PRO A  85  ? 2.1458 3.2112 3.2940 0.3237  0.0125  0.7632  85   PRO A O   
630   C  CB  . PRO A  85  ? 1.8695 3.0218 3.2119 0.2319  -0.0218 0.8081  85   PRO A CB  
631   C  CG  . PRO A  85  ? 1.9619 3.0506 3.3019 0.1769  -0.0581 0.8489  85   PRO A CG  
632   C  CD  . PRO A  85  ? 2.1284 3.1532 3.3580 0.1767  -0.0553 0.8666  85   PRO A CD  
633   N  N   . LEU A  86  ? 2.1411 3.3802 3.3431 0.3458  0.0862  0.7571  86   LEU A N   
634   C  CA  . LEU A  86  ? 2.0238 3.2475 3.1763 0.4057  0.1056  0.7197  86   LEU A CA  
635   C  C   . LEU A  86  ? 1.9944 3.2117 3.2133 0.4356  0.0791  0.6843  86   LEU A C   
636   O  O   . LEU A  86  ? 2.0121 3.1703 3.1853 0.4718  0.0708  0.6574  86   LEU A O   
637   C  CB  . LEU A  86  ? 1.9445 3.2605 3.0790 0.4375  0.1664  0.7147  86   LEU A CB  
638   C  CG  . LEU A  86  ? 1.8912 3.1968 2.9827 0.5036  0.1891  0.6755  86   LEU A CG  
639   C  CD1 . LEU A  86  ? 2.0989 3.3084 3.0619 0.5158  0.1946  0.6712  86   LEU A CD1 
640   C  CD2 . LEU A  86  ? 1.8316 3.2516 2.9543 0.5385  0.2424  0.6686  86   LEU A CD2 
641   N  N   . GLU A  87  ? 2.0294 3.3053 3.3513 0.4192  0.0658  0.6835  87   GLU A N   
642   C  CA  . GLU A  87  ? 1.7302 3.0121 3.1140 0.4472  0.0457  0.6491  87   GLU A CA  
643   C  C   . GLU A  87  ? 1.6793 2.9534 3.1493 0.4068  0.0045  0.6549  87   GLU A C   
644   O  O   . GLU A  87  ? 1.8737 3.1547 3.3667 0.3587  -0.0039 0.6864  87   GLU A O   
645   C  CB  . GLU A  87  ? 1.6306 3.0144 3.0509 0.4853  0.0828  0.6314  87   GLU A CB  
646   C  CG  . GLU A  87  ? 1.7503 3.2404 3.2267 0.4565  0.1083  0.6574  87   GLU A CG  
647   C  CD  . GLU A  87  ? 1.7883 3.3825 3.2854 0.4994  0.1523  0.6457  87   GLU A CD  
648   O  OE1 . GLU A  87  ? 1.7866 3.3635 3.2523 0.5528  0.1619  0.6168  87   GLU A OE1 
649   O  OE2 . GLU A  87  ? 1.8010 3.4952 3.3473 0.4793  0.1765  0.6673  87   GLU A OE2 
650   N  N   . PHE A  88  ? 1.6120 2.8706 3.1281 0.4267  -0.0203 0.6234  88   PHE A N   
651   C  CA  . PHE A  88  ? 1.5666 2.8095 3.1616 0.3952  -0.0590 0.6203  88   PHE A CA  
652   C  C   . PHE A  88  ? 1.3372 2.6444 2.9984 0.4184  -0.0569 0.5887  88   PHE A C   
653   O  O   . PHE A  88  ? 1.2961 2.5749 2.9519 0.4528  -0.0676 0.5575  88   PHE A O   
654   C  CB  . PHE A  88  ? 1.6691 2.8055 3.2455 0.3917  -0.0993 0.6143  88   PHE A CB  
655   C  CG  . PHE A  88  ? 1.6289 2.6987 3.1311 0.3739  -0.1044 0.6445  88   PHE A CG  
656   C  CD1 . PHE A  88  ? 1.6205 2.6539 3.0339 0.4038  -0.0898 0.6394  88   PHE A CD1 
657   C  CD2 . PHE A  88  ? 1.6618 2.7008 3.1795 0.3253  -0.1259 0.6787  88   PHE A CD2 
658   C  CE1 . PHE A  88  ? 1.7643 2.7358 3.1040 0.3841  -0.0966 0.6674  88   PHE A CE1 
659   C  CE2 . PHE A  88  ? 1.7997 2.7780 3.2467 0.3068  -0.1333 0.7092  88   PHE A CE2 
660   C  CZ  . PHE A  88  ? 1.8530 2.7993 3.2101 0.3355  -0.1188 0.7033  88   PHE A CZ  
661   N  N   . LYS A  89  ? 1.3244 2.7186 3.0471 0.3961  -0.0452 0.5986  89   LYS A N   
662   C  CA  . LYS A  89  ? 1.3138 2.7794 3.0998 0.4130  -0.0437 0.5729  89   LYS A CA  
663   C  C   . LYS A  89  ? 1.2433 2.6819 3.0955 0.3837  -0.0832 0.5582  89   LYS A C   
664   O  O   . LYS A  89  ? 1.4085 2.8943 3.3095 0.3944  -0.0884 0.5336  89   LYS A O   
665   C  CB  . LYS A  89  ? 1.5397 3.1241 3.3609 0.4051  -0.0103 0.5913  89   LYS A CB  
666   C  CG  . LYS A  89  ? 1.5996 3.2277 3.3648 0.4474  0.0351  0.5964  89   LYS A CG  
667   C  CD  . LYS A  89  ? 1.4387 3.1894 3.2457 0.4353  0.0690  0.6198  89   LYS A CD  
668   C  CE  . LYS A  89  ? 1.3584 3.1482 3.1077 0.4801  0.1175  0.6241  89   LYS A CE  
669   N  NZ  . LYS A  89  ? 1.4223 3.3383 3.2162 0.4678  0.1534  0.6498  89   LYS A NZ  
670   N  N   . SER A  90  ? 1.2744 2.6383 3.1282 0.3470  -0.1109 0.5731  90   SER A N   
671   C  CA  . SER A  90  ? 1.2490 2.5718 3.1594 0.3239  -0.1479 0.5556  90   SER A CA  
672   C  C   . SER A  90  ? 1.2058 2.4808 3.1079 0.3629  -0.1634 0.5169  90   SER A C   
673   O  O   . SER A  90  ? 1.2107 2.4326 3.0558 0.3914  -0.1619 0.5140  90   SER A O   
674   C  CB  . SER A  90  ? 1.3738 2.6188 3.2835 0.2815  -0.1737 0.5825  90   SER A CB  
675   O  OG  . SER A  90  ? 1.4378 2.7291 3.3640 0.2377  -0.1631 0.6183  90   SER A OG  
676   N  N   . HIS A  91  ? 1.1785 2.4743 3.1353 0.3618  -0.1782 0.4872  91   HIS A N   
677   C  CA  . HIS A  91  ? 1.1562 2.4155 3.1118 0.3947  -0.1923 0.4491  91   HIS A CA  
678   C  C   . HIS A  91  ? 1.1136 2.3955 3.0180 0.4444  -0.1691 0.4383  91   HIS A C   
679   O  O   . HIS A  91  ? 1.2662 2.4940 3.1401 0.4720  -0.1782 0.4197  91   HIS A O   
680   C  CB  . HIS A  91  ? 1.4342 2.5907 3.3820 0.3890  -0.2210 0.4460  91   HIS A CB  
681   C  CG  . HIS A  91  ? 1.6052 2.7239 3.5976 0.3433  -0.2450 0.4591  91   HIS A CG  
682   N  ND1 . HIS A  91  ? 1.6070 2.7363 3.6587 0.3219  -0.2608 0.4371  91   HIS A ND1 
683   C  CD2 . HIS A  91  ? 1.6198 2.6851 3.6026 0.3142  -0.2571 0.4925  91   HIS A CD2 
684   C  CE1 . HIS A  91  ? 1.4901 2.5700 3.5675 0.2827  -0.2812 0.4553  91   HIS A CE1 
685   N  NE2 . HIS A  91  ? 1.5271 2.5688 3.5652 0.2775  -0.2800 0.4905  91   HIS A NE2 
686   N  N   . GLN A  92  ? 1.1027 2.4646 2.9986 0.4563  -0.1390 0.4503  92   GLN A N   
687   C  CA  . GLN A  92  ? 1.0911 2.4713 2.9363 0.5051  -0.1149 0.4419  92   GLN A CA  
688   C  C   . GLN A  92  ? 1.0424 2.4638 2.9125 0.5335  -0.1171 0.4104  92   GLN A C   
689   O  O   . GLN A  92  ? 1.0337 2.4599 2.8622 0.5761  -0.1016 0.4008  92   GLN A O   
690   C  CB  . GLN A  92  ? 1.1193 2.5673 2.9440 0.5112  -0.0784 0.4682  92   GLN A CB  
691   C  CG  . GLN A  92  ? 1.0995 2.6586 2.9873 0.5017  -0.0654 0.4720  92   GLN A CG  
692   C  CD  . GLN A  92  ? 1.3260 2.9562 3.1989 0.5061  -0.0271 0.5008  92   GLN A CD  
693   O  OE1 . GLN A  92  ? 1.4420 3.0399 3.2472 0.5283  -0.0054 0.5108  92   GLN A OE1 
694   N  NE2 . GLN A  92  ? 1.3432 3.0719 3.2783 0.4836  -0.0181 0.5142  92   GLN A NE2 
695   N  N   . TRP A  93  ? 1.0175 2.4670 2.9503 0.5098  -0.1363 0.3951  93   TRP A N   
696   C  CA  . TRP A  93  ? 0.9817 2.4605 2.9258 0.5289  -0.1422 0.3619  93   TRP A CA  
697   C  C   . TRP A  93  ? 0.9858 2.5361 2.9027 0.5526  -0.1154 0.3594  93   TRP A C   
698   O  O   . TRP A  93  ? 0.9859 2.5157 2.8446 0.5808  -0.1117 0.3289  93   TRP A O   
699   C  CB  . TRP A  93  ? 0.9805 2.3678 2.8586 0.5502  -0.1543 0.3285  93   TRP A CB  
700   C  CG  . TRP A  93  ? 0.9748 2.3039 2.8844 0.5260  -0.1831 0.3131  93   TRP A CG  
701   C  CD1 . TRP A  93  ? 0.9854 2.2733 2.9380 0.5038  -0.1995 0.3355  93   TRP A CD1 
702   C  CD2 . TRP A  93  ? 0.9626 2.2688 2.8637 0.5230  -0.1982 0.2723  93   TRP A CD2 
703   N  NE1 . TRP A  93  ? 0.9824 2.2195 2.9549 0.4897  -0.2231 0.3081  93   TRP A NE1 
704   C  CE2 . TRP A  93  ? 0.9680 2.2181 2.9085 0.5011  -0.2206 0.2693  93   TRP A CE2 
705   C  CE3 . TRP A  93  ? 0.9507 2.2798 2.8159 0.5377  -0.1950 0.2398  93   TRP A CE3 
706   C  CZ2 . TRP A  93  ? 1.0703 2.2890 3.0143 0.4950  -0.2355 0.2333  93   TRP A CZ2 
707   C  CZ3 . TRP A  93  ? 0.9426 2.2451 2.8112 0.5291  -0.2109 0.2083  93   TRP A CZ3 
708   C  CH2 . TRP A  93  ? 0.9860 2.2345 2.8935 0.5086  -0.2290 0.2043  93   TRP A CH2 
709   N  N   . PHE A  94  ? 1.4166 3.0511 3.3784 0.5399  -0.0972 0.3928  94   PHE A N   
710   C  CA  . PHE A  94  ? 1.0019 2.7115 2.9495 0.5594  -0.0721 0.3911  94   PHE A CA  
711   C  C   . PHE A  94  ? 0.9870 2.7337 2.9574 0.5460  -0.0888 0.3612  94   PHE A C   
712   O  O   . PHE A  94  ? 0.9754 2.7590 3.0118 0.5064  -0.1072 0.3663  94   PHE A O   
713   C  CB  . PHE A  94  ? 1.0154 2.8139 3.0097 0.5452  -0.0474 0.4359  94   PHE A CB  
714   C  CG  . PHE A  94  ? 1.0293 2.9105 3.0184 0.5627  -0.0214 0.4344  94   PHE A CG  
715   C  CD1 . PHE A  94  ? 1.0525 2.9188 2.9752 0.6106  0.0057  0.4263  94   PHE A CD1 
716   C  CD2 . PHE A  94  ? 1.0241 2.9944 3.0766 0.5307  -0.0260 0.4411  94   PHE A CD2 
717   C  CE1 . PHE A  94  ? 1.0710 3.0068 2.9934 0.6287  0.0284  0.4249  94   PHE A CE1 
718   C  CE2 . PHE A  94  ? 1.0407 3.0856 3.0920 0.5472  -0.0041 0.4405  94   PHE A CE2 
719   C  CZ  . PHE A  94  ? 1.0644 3.0905 3.0522 0.5975  0.0234  0.4323  94   PHE A CZ  
720   N  N   . GLY A  95  ? 0.9916 2.7312 2.9110 0.5773  -0.0830 0.3332  95   GLY A N   
721   C  CA  . GLY A  95  ? 0.9805 2.7439 2.9115 0.5695  -0.1016 0.3035  95   GLY A CA  
722   C  C   . GLY A  95  ? 1.2891 2.9743 3.1787 0.5780  -0.1238 0.2666  95   GLY A C   
723   O  O   . GLY A  95  ? 1.3382 3.0436 3.2432 0.5667  -0.1421 0.2433  95   GLY A O   
724   N  N   . ALA A  96  ? 0.9697 2.5711 2.8068 0.5970  -0.1222 0.2622  96   ALA A N   
725   C  CA  . ALA A  96  ? 0.9597 2.4907 2.7535 0.6054  -0.1406 0.2287  96   ALA A CA  
726   C  C   . ALA A  96  ? 0.9658 2.4911 2.7136 0.6319  -0.1389 0.2047  96   ALA A C   
727   O  O   . ALA A  96  ? 1.1447 2.6438 2.8740 0.6322  -0.1562 0.1762  96   ALA A O   
728   C  CB  . ALA A  96  ? 1.3199 2.7671 3.0731 0.6154  -0.1404 0.2346  96   ALA A CB  
729   N  N   . SER A  97  ? 0.9870 2.5354 2.7182 0.6543  -0.1173 0.2184  97   SER A N   
730   C  CA  . SER A  97  ? 1.0390 2.5839 2.7396 0.6768  -0.1155 0.2035  97   SER A CA  
731   C  C   . SER A  97  ? 1.0670 2.6911 2.7968 0.6841  -0.0956 0.2238  97   SER A C   
732   O  O   . SER A  97  ? 1.0890 2.7330 2.8173 0.6956  -0.0706 0.2485  97   SER A O   
733   C  CB  . SER A  97  ? 1.1837 2.6452 2.8126 0.7067  -0.1079 0.1985  97   SER A CB  
734   O  OG  . SER A  97  ? 1.4051 2.8661 3.0143 0.7263  -0.0812 0.2238  97   SER A OG  
735   N  N   . VAL A  98  ? 1.0145 2.6879 2.7718 0.6779  -0.1062 0.2150  98   VAL A N   
736   C  CA  . VAL A  98  ? 1.0336 2.7889 2.8235 0.6839  -0.0906 0.2335  98   VAL A CA  
737   C  C   . VAL A  98  ? 1.1708 2.9127 2.9311 0.7105  -0.0918 0.2246  98   VAL A C   
738   O  O   . VAL A  98  ? 1.4554 3.1743 3.2098 0.7037  -0.1152 0.2054  98   VAL A O   
739   C  CB  . VAL A  98  ? 1.0165 2.8598 2.8803 0.6463  -0.1047 0.2392  98   VAL A CB  
740   C  CG1 . VAL A  98  ? 1.0392 2.9736 2.9399 0.6512  -0.0862 0.2628  98   VAL A CG1 
741   C  CG2 . VAL A  98  ? 1.1220 2.9670 3.0171 0.6155  -0.1096 0.2481  98   VAL A CG2 
742   N  N   . ARG A  99  ? 1.0876 2.8460 2.8309 0.7417  -0.0657 0.2407  99   ARG A N   
743   C  CA  . ARG A  99  ? 1.1145 2.8619 2.8318 0.7709  -0.0646 0.2377  99   ARG A CA  
744   C  C   . ARG A  99  ? 1.1443 2.9764 2.8954 0.7869  -0.0423 0.2593  99   ARG A C   
745   O  O   . ARG A  99  ? 1.1594 3.0197 2.9160 0.7956  -0.0145 0.2765  99   ARG A O   
746   C  CB  . ARG A  99  ? 1.2931 2.9459 2.9358 0.8033  -0.0544 0.2318  99   ARG A CB  
747   C  CG  . ARG A  99  ? 1.4201 2.9911 3.0277 0.7916  -0.0792 0.2103  99   ARG A CG  
748   C  CD  . ARG A  99  ? 1.5270 3.1144 3.1551 0.7772  -0.1063 0.1983  99   ARG A CD  
749   N  NE  . ARG A  99  ? 1.7584 3.3724 3.4298 0.7391  -0.1277 0.1863  99   ARG A NE  
750   C  CZ  . ARG A  99  ? 1.4713 3.0306 3.1274 0.7231  -0.1450 0.1676  99   ARG A CZ  
751   N  NH1 . ARG A  99  ? 1.3572 2.8339 2.9568 0.7386  -0.1444 0.1608  99   ARG A NH1 
752   N  NH2 . ARG A  99  ? 1.2954 2.8854 2.9941 0.6919  -0.1626 0.1559  99   ARG A NH2 
753   N  N   . SER A  100 ? 1.1919 3.0677 2.9667 0.7914  -0.0539 0.2602  100  SER A N   
754   C  CA  . SER A  100 ? 1.2317 3.1994 3.0498 0.8035  -0.0372 0.2807  100  SER A CA  
755   C  C   . SER A  100 ? 1.2433 3.1994 3.0379 0.8426  -0.0345 0.2825  100  SER A C   
756   O  O   . SER A  100 ? 1.4074 3.3229 3.1815 0.8434  -0.0590 0.2705  100  SER A O   
757   C  CB  . SER A  100 ? 1.1607 3.2198 3.0511 0.7642  -0.0577 0.2862  100  SER A CB  
758   O  OG  . SER A  100 ? 1.1871 3.3425 3.1251 0.7719  -0.0397 0.3091  100  SER A OG  
759   N  N   . LYS A  101 ? 1.2682 3.2644 3.0684 0.8755  -0.0041 0.2993  101  LYS A N   
760   C  CA  . LYS A  101 ? 1.3131 3.3079 3.0989 0.9168  0.0013  0.3042  101  LYS A CA  
761   C  C   . LYS A  101 ? 1.4693 3.5747 3.3160 0.9274  0.0198  0.3260  101  LYS A C   
762   O  O   . LYS A  101 ? 1.6278 3.7626 3.4779 0.9447  0.0547  0.3379  101  LYS A O   
763   C  CB  . LYS A  101 ? 1.3498 3.2559 3.0630 0.9588  0.0242  0.2990  101  LYS A CB  
764   C  CG  . LYS A  101 ? 1.4918 3.3903 3.1886 1.0048  0.0311  0.3044  101  LYS A CG  
765   C  CD  . LYS A  101 ? 1.4468 3.2581 3.0706 1.0459  0.0559  0.2992  101  LYS A CD  
766   C  CE  . LYS A  101 ? 1.6472 3.4444 3.2544 1.0928  0.0606  0.3039  101  LYS A CE  
767   N  NZ  . LYS A  101 ? 1.8137 3.7120 3.4793 1.1153  0.0806  0.3216  101  LYS A NZ  
768   N  N   . GLN A  102 ? 1.3349 3.5050 3.2298 0.9171  -0.0034 0.3325  102  GLN A N   
769   C  CA  . GLN A  102 ? 1.3610 3.6455 3.3223 0.9235  0.0083  0.3546  102  GLN A CA  
770   C  C   . GLN A  102 ? 1.3382 3.6934 3.3457 0.8880  0.0217  0.3657  102  GLN A C   
771   O  O   . GLN A  102 ? 1.2943 3.6551 3.3212 0.8412  -0.0024 0.3590  102  GLN A O   
772   C  CB  . GLN A  102 ? 1.4214 3.7029 3.3637 0.9814  0.0402  0.3639  102  GLN A CB  
773   C  CG  . GLN A  102 ? 1.4509 3.6569 3.3448 1.0181  0.0289  0.3552  102  GLN A CG  
774   C  CD  . GLN A  102 ? 1.5122 3.6933 3.3736 1.0748  0.0666  0.3599  102  GLN A CD  
775   O  OE1 . GLN A  102 ? 1.5331 3.7638 3.4127 1.0873  0.1019  0.3702  102  GLN A OE1 
776   N  NE2 . GLN A  102 ? 1.5782 3.6847 3.3918 1.1099  0.0600  0.3531  102  GLN A NE2 
777   N  N   . ASP A  103 ? 1.5859 3.9948 3.6113 0.9082  0.0599  0.3830  103  ASP A N   
778   C  CA  . ASP A  103 ? 1.6051 4.0869 3.6746 0.8760  0.0765  0.3987  103  ASP A CA  
779   C  C   . ASP A  103 ? 1.3403 3.7555 3.3614 0.8741  0.0972  0.3930  103  ASP A C   
780   O  O   . ASP A  103 ? 1.3385 3.8092 3.3872 0.8570  0.1200  0.4101  103  ASP A O   
781   C  CB  . ASP A  103 ? 1.4243 4.0142 3.5454 0.8978  0.1078  0.4240  103  ASP A CB  
782   C  CG  . ASP A  103 ? 1.4508 4.0067 3.5267 0.9573  0.1493  0.4249  103  ASP A CG  
783   O  OD1 . ASP A  103 ? 1.6455 4.1008 3.6565 0.9890  0.1451  0.4068  103  ASP A OD1 
784   O  OD2 . ASP A  103 ? 1.4841 4.1154 3.5893 0.9724  0.1864  0.4439  103  ASP A OD2 
785   N  N   . LYS A  104 ? 1.3320 3.6329 3.2833 0.8892  0.0887  0.3717  104  LYS A N   
786   C  CA  . LYS A  104 ? 1.4295 3.6595 3.3303 0.8893  0.1042  0.3661  104  LYS A CA  
787   C  C   . LYS A  104 ? 1.5135 3.6959 3.4115 0.8446  0.0693  0.3510  104  LYS A C   
788   O  O   . LYS A  104 ? 1.6168 3.7569 3.5037 0.8363  0.0368  0.3332  104  LYS A O   
789   C  CB  . LYS A  104 ? 1.4422 3.5758 3.2648 0.9387  0.1197  0.3536  104  LYS A CB  
790   C  CG  . LYS A  104 ? 1.4196 3.5900 3.2414 0.9892  0.1521  0.3643  104  LYS A CG  
791   C  CD  . LYS A  104 ? 1.4591 3.5252 3.2019 1.0355  0.1607  0.3496  104  LYS A CD  
792   C  CE  . LYS A  104 ? 1.5276 3.6256 3.2695 1.0890  0.1932  0.3584  104  LYS A CE  
793   N  NZ  . LYS A  104 ? 1.6932 3.8523 3.4474 1.1024  0.2386  0.3744  104  LYS A NZ  
794   N  N   . ILE A  105 ? 1.3355 3.5253 3.2437 0.8174  0.0769  0.3594  105  ILE A N   
795   C  CA  . ILE A  105 ? 1.1972 3.3399 3.1041 0.7782  0.0473  0.3461  105  ILE A CA  
796   C  C   . ILE A  105 ? 1.1965 3.2667 3.0519 0.7887  0.0639  0.3465  105  ILE A C   
797   O  O   . ILE A  105 ? 1.2123 3.3210 3.0758 0.7929  0.0946  0.3687  105  ILE A O   
798   C  CB  . ILE A  105 ? 1.1700 3.3985 3.1518 0.7268  0.0330  0.3596  105  ILE A CB  
799   C  CG1 . ILE A  105 ? 1.2627 3.5674 3.2954 0.7155  0.0148  0.3611  105  ILE A CG1 
800   C  CG2 . ILE A  105 ? 1.1279 3.3017 3.1070 0.6907  0.0039  0.3448  105  ILE A CG2 
801   C  CD1 . ILE A  105 ? 1.1584 3.5484 3.2643 0.6620  -0.0022 0.3742  105  ILE A CD1 
802   N  N   . LEU A  106 ? 1.2086 3.1780 3.0116 0.7929  0.0444  0.3240  106  LEU A N   
803   C  CA  . LEU A  106 ? 1.1814 3.0744 2.9326 0.8027  0.0546  0.3234  106  LEU A CA  
804   C  C   . LEU A  106 ? 1.1365 2.9930 2.9008 0.7633  0.0242  0.3134  106  LEU A C   
805   O  O   . LEU A  106 ? 1.1141 2.9330 2.8743 0.7504  -0.0064 0.2901  106  LEU A O   
806   C  CB  . LEU A  106 ? 1.2103 3.0128 2.8855 0.8439  0.0593  0.3077  106  LEU A CB  
807   C  CG  . LEU A  106 ? 1.2171 2.9325 2.8303 0.8571  0.0670  0.3059  106  LEU A CG  
808   C  CD1 . LEU A  106 ? 1.2461 2.9990 2.8555 0.8741  0.1061  0.3316  106  LEU A CD1 
809   C  CD2 . LEU A  106 ? 1.2449 2.8717 2.7879 0.8906  0.0639  0.2885  106  LEU A CD2 
810   N  N   . ALA A  107 ? 1.1911 3.0629 2.9744 0.7445  0.0334  0.3330  107  ALA A N   
811   C  CA  . ALA A  107 ? 1.0910 2.9237 2.8876 0.7109  0.0073  0.3276  107  ALA A CA  
812   C  C   . ALA A  107 ? 1.0997 2.8735 2.8561 0.7232  0.0208  0.3410  107  ALA A C   
813   O  O   . ALA A  107 ? 1.1287 2.9273 2.8710 0.7451  0.0539  0.3642  107  ALA A O   
814   C  CB  . ALA A  107 ? 1.0694 2.9848 2.9461 0.6655  -0.0028 0.3445  107  ALA A CB  
815   N  N   . CYS A  108 ? 1.0771 2.7765 2.8167 0.7095  -0.0045 0.3275  108  CYS A N   
816   C  CA  . CYS A  108 ? 1.2303 2.8619 2.9270 0.7222  0.0020  0.3387  108  CYS A CA  
817   C  C   . CYS A  108 ? 1.0589 2.6670 2.7920 0.6861  -0.0221 0.3466  108  CYS A C   
818   O  O   . CYS A  108 ? 1.1217 2.7398 2.8960 0.6562  -0.0478 0.3318  108  CYS A O   
819   C  CB  . CYS A  108 ? 1.3420 2.8806 2.9620 0.7522  -0.0041 0.3134  108  CYS A CB  
820   S  SG  . CYS A  108 ? 1.8086 3.3536 3.3795 0.7992  0.0249  0.3089  108  CYS A SG  
821   N  N   . ALA A  109 ? 1.0702 2.6434 2.7869 0.6910  -0.0138 0.3713  109  ALA A N   
822   C  CA  . ALA A  109 ? 1.0522 2.5924 2.8042 0.6596  -0.0364 0.3858  109  ALA A CA  
823   C  C   . ALA A  109 ? 1.0613 2.5006 2.7517 0.6773  -0.0473 0.3773  109  ALA A C   
824   O  O   . ALA A  109 ? 1.0866 2.5039 2.7466 0.6931  -0.0322 0.4034  109  ALA A O   
825   C  CB  . ALA A  109 ? 1.0879 2.6840 2.8871 0.6385  -0.0208 0.4311  109  ALA A CB  
826   N  N   . PRO A  110 ? 1.0460 2.4243 2.7120 0.6744  -0.0728 0.3413  110  PRO A N   
827   C  CA  . PRO A  110 ? 1.2638 2.5502 2.8700 0.6892  -0.0841 0.3324  110  PRO A CA  
828   C  C   . PRO A  110 ? 1.4006 2.6457 3.0275 0.6709  -0.0981 0.3597  110  PRO A C   
829   O  O   . PRO A  110 ? 1.2824 2.4671 2.8606 0.6869  -0.0998 0.3685  110  PRO A O   
830   C  CB  . PRO A  110 ? 1.1664 2.4186 2.7578 0.6830  -0.1077 0.2893  110  PRO A CB  
831   C  CG  . PRO A  110 ? 1.2634 2.5871 2.8826 0.6811  -0.1011 0.2751  110  PRO A CG  
832   C  CD  . PRO A  110 ? 1.0688 2.4678 2.7529 0.6624  -0.0886 0.3072  110  PRO A CD  
833   N  N   . LEU A  111 ? 1.3770 2.6492 3.0768 0.6364  -0.1112 0.3751  111  LEU A N   
834   C  CA  . LEU A  111 ? 1.0918 2.2975 2.7842 0.6054  -0.1290 0.3906  111  LEU A CA  
835   C  C   . LEU A  111 ? 1.2650 2.4849 2.9386 0.5850  -0.1108 0.4238  111  LEU A C   
836   O  O   . LEU A  111 ? 1.3526 2.5348 3.0362 0.5499  -0.1266 0.4420  111  LEU A O   
837   C  CB  . LEU A  111 ? 1.0448 2.2402 2.8053 0.5738  -0.1580 0.3792  111  LEU A CB  
838   C  CG  . LEU A  111 ? 1.0247 2.1615 2.7696 0.5845  -0.1791 0.3471  111  LEU A CG  
839   C  CD1 . LEU A  111 ? 1.1666 2.2901 2.9669 0.5550  -0.2023 0.3296  111  LEU A CD1 
840   C  CD2 . LEU A  111 ? 1.0920 2.1551 2.7916 0.5947  -0.1886 0.3605  111  LEU A CD2 
841   N  N   . TYR A  112 ? 1.4140 2.6894 3.0619 0.6069  -0.0773 0.4327  112  TYR A N   
842   C  CA  . TYR A  112 ? 1.2234 2.5104 2.8379 0.5931  -0.0541 0.4631  112  TYR A CA  
843   C  C   . TYR A  112 ? 1.2324 2.4287 2.7627 0.5973  -0.0576 0.4719  112  TYR A C   
844   O  O   . TYR A  112 ? 1.2390 2.3960 2.7122 0.6322  -0.0530 0.4565  112  TYR A O   
845   C  CB  . TYR A  112 ? 1.1919 2.5636 2.8005 0.6232  -0.0143 0.4664  112  TYR A CB  
846   C  CG  . TYR A  112 ? 1.2543 2.6325 2.8052 0.6242  0.0188  0.4915  112  TYR A CG  
847   C  CD1 . TYR A  112 ? 1.4434 2.8755 3.0246 0.5876  0.0317  0.5201  112  TYR A CD1 
848   C  CD2 . TYR A  112 ? 1.2958 2.6265 2.7587 0.6607  0.0384  0.4860  112  TYR A CD2 
849   C  CE1 . TYR A  112 ? 1.5567 2.9989 3.0819 0.5879  0.0650  0.5428  112  TYR A CE1 
850   C  CE2 . TYR A  112 ? 1.4084 2.7433 2.8120 0.6623  0.0712  0.5059  112  TYR A CE2 
851   C  CZ  . TYR A  112 ? 1.4821 2.8754 2.9173 0.6264  0.0855  0.5343  112  TYR A CZ  
852   O  OH  . TYR A  112 ? 1.5700 2.9707 2.9428 0.6271  0.1208  0.5539  112  TYR A OH  
853   N  N   . HIS A  113 ? 1.2709 2.4324 2.7913 0.5595  -0.0677 0.4983  113  HIS A N   
854   C  CA  . HIS A  113 ? 1.3245 2.4045 2.7643 0.5563  -0.0733 0.5121  113  HIS A CA  
855   C  C   . HIS A  113 ? 1.5162 2.6228 2.9018 0.5522  -0.0379 0.5372  113  HIS A C   
856   O  O   . HIS A  113 ? 1.8485 3.0276 3.2748 0.5336  -0.0191 0.5536  113  HIS A O   
857   C  CB  . HIS A  113 ? 1.4069 2.4227 2.8682 0.5176  -0.1125 0.5269  113  HIS A CB  
858   C  CG  . HIS A  113 ? 1.5250 2.5109 3.0364 0.5229  -0.1451 0.5016  113  HIS A CG  
859   N  ND1 . HIS A  113 ? 1.4233 2.4581 3.0149 0.5197  -0.1514 0.4829  113  HIS A ND1 
860   C  CD2 . HIS A  113 ? 1.3254 2.2406 2.8175 0.5303  -0.1722 0.4919  113  HIS A CD2 
861   C  CE1 . HIS A  113 ? 1.2087 2.2027 2.8254 0.5265  -0.1785 0.4610  113  HIS A CE1 
862   N  NE2 . HIS A  113 ? 1.2197 2.1442 2.7806 0.5335  -0.1911 0.4669  113  HIS A NE2 
863   N  N   . TRP A  114 ? 1.5229 2.5709 2.8144 0.5673  -0.0285 0.5401  114  TRP A N   
864   C  CA  . TRP A  114 ? 1.8191 2.8863 3.0467 0.5662  0.0085  0.5605  114  TRP A CA  
865   C  C   . TRP A  114 ? 1.6977 2.6734 2.8345 0.5487  -0.0051 0.5772  114  TRP A C   
866   O  O   . TRP A  114 ? 1.6830 2.5844 2.7762 0.5620  -0.0276 0.5630  114  TRP A O   
867   C  CB  . TRP A  114 ? 2.1209 3.2320 3.3152 0.6174  0.0504  0.5404  114  TRP A CB  
868   C  CG  . TRP A  114 ? 2.2684 3.3530 3.3576 0.6316  0.0850  0.5484  114  TRP A CG  
869   C  CD1 . TRP A  114 ? 2.3088 3.4495 3.3788 0.6235  0.1244  0.5691  114  TRP A CD1 
870   C  CD2 . TRP A  114 ? 2.2586 3.2551 3.2449 0.6561  0.0849  0.5341  114  TRP A CD2 
871   N  NE1 . TRP A  114 ? 2.3483 3.4386 3.3070 0.6428  0.1502  0.5666  114  TRP A NE1 
872   C  CE2 . TRP A  114 ? 2.4324 3.4309 3.3365 0.6622  0.1253  0.5450  114  TRP A CE2 
873   C  CE3 . TRP A  114 ? 2.0526 2.9688 3.0067 0.6710  0.0545  0.5135  114  TRP A CE3 
874   C  CZ2 . TRP A  114 ? 2.5254 3.4419 3.3129 0.6825  0.1348  0.5337  114  TRP A CZ2 
875   C  CZ3 . TRP A  114 ? 2.0885 2.9263 2.9306 0.6889  0.0623  0.5050  114  TRP A CZ3 
876   C  CH2 . TRP A  114 ? 2.3879 3.2229 3.1457 0.6945  0.1015  0.5141  114  TRP A CH2 
877   N  N   . ARG A  115 ? 1.6357 2.6197 2.7451 0.5153  0.0072  0.6094  115  ARG A N   
878   C  CA  . ARG A  115 ? 1.7605 2.6628 2.7848 0.4906  -0.0083 0.6313  115  ARG A CA  
879   C  C   . ARG A  115 ? 1.9363 2.8129 2.8484 0.5211  0.0265  0.6210  115  ARG A C   
880   O  O   . ARG A  115 ? 2.1715 3.1116 3.0724 0.5471  0.0729  0.6134  115  ARG A O   
881   C  CB  . ARG A  115 ? 1.8650 2.7858 2.9022 0.4395  -0.0099 0.6723  115  ARG A CB  
882   C  CG  . ARG A  115 ? 2.0817 2.9307 3.0188 0.4131  -0.0180 0.6995  115  ARG A CG  
883   C  CD  . ARG A  115 ? 2.2339 3.1238 3.1684 0.3702  -0.0006 0.7391  115  ARG A CD  
884   N  NE  . ARG A  115 ? 2.4704 3.2950 3.3030 0.3420  -0.0072 0.7675  115  ARG A NE  
885   C  CZ  . ARG A  115 ? 2.7521 3.5656 3.4768 0.3569  0.0290  0.7641  115  ARG A CZ  
886   N  NH1 . ARG A  115 ? 2.8858 3.7482 3.5952 0.4032  0.0752  0.7336  115  ARG A NH1 
887   N  NH2 . ARG A  115 ? 2.8834 3.6348 3.5134 0.3261  0.0188  0.7909  115  ARG A NH2 
888   N  N   . THR A  116 ? 1.9273 2.7107 2.7574 0.5187  0.0036  0.6200  116  THR A N   
889   C  CA  . THR A  116 ? 2.0827 2.8267 2.8004 0.5494  0.0323  0.6040  116  THR A CA  
890   C  C   . THR A  116 ? 2.3576 3.1285 3.0104 0.5353  0.0734  0.6258  116  THR A C   
891   O  O   . THR A  116 ? 2.5500 3.3406 3.2230 0.4914  0.0666  0.6597  116  THR A O   
892   C  CB  . THR A  116 ? 2.1388 2.7749 2.7813 0.5403  -0.0065 0.6023  116  THR A CB  
893   O  OG1 . THR A  116 ? 2.0877 2.7077 2.7992 0.5501  -0.0439 0.5846  116  THR A OG1 
894   C  CG2 . THR A  116 ? 2.3035 2.8870 2.8255 0.5719  0.0197  0.5811  116  THR A CG2 
895   N  N   . GLU A  117 ? 2.1478 2.9160 2.7189 0.5727  0.1168  0.6064  117  GLU A N   
896   C  CA  . GLU A  117 ? 2.1223 2.9190 2.6246 0.5655  0.1631  0.6222  117  GLU A CA  
897   C  C   . GLU A  117 ? 2.3055 3.0041 2.6753 0.5427  0.1529  0.6326  117  GLU A C   
898   O  O   . GLU A  117 ? 2.4960 3.2020 2.7867 0.5332  0.1897  0.6452  117  GLU A O   
899   C  CB  . GLU A  117 ? 2.1333 2.9879 2.6240 0.6224  0.2207  0.5947  117  GLU A CB  
900   C  CG  . GLU A  117 ? 2.2609 3.1940 2.7349 0.6177  0.2755  0.6123  117  GLU A CG  
901   C  CD  . GLU A  117 ? 2.2126 3.2146 2.6963 0.6786  0.3309  0.5860  117  GLU A CD  
902   O  OE1 . GLU A  117 ? 2.1571 3.1335 2.6481 0.7243  0.3250  0.5542  117  GLU A OE1 
903   O  OE2 . GLU A  117 ? 2.3974 3.4836 2.8873 0.6804  0.3796  0.5992  117  GLU A OE2 
904   N  N   . MET A  118 ? 2.6262 3.2361 2.9705 0.5327  0.1035  0.6278  118  MET A N   
905   C  CA  . MET A  118 ? 2.7144 3.2258 2.9429 0.5046  0.0793  0.6402  118  MET A CA  
906   C  C   . MET A  118 ? 2.6867 3.1755 2.9520 0.4476  0.0277  0.6800  118  MET A C   
907   O  O   . MET A  118 ? 2.8378 3.2824 3.0193 0.4103  0.0194  0.7074  118  MET A O   
908   C  CB  . MET A  118 ? 2.8564 3.2845 3.0306 0.5327  0.0575  0.6085  118  MET A CB  
909   C  CG  . MET A  118 ? 2.9718 3.3947 3.0763 0.5873  0.1074  0.5711  118  MET A CG  
910   S  SD  . MET A  118 ? 3.1021 3.4561 3.1963 0.6266  0.0813  0.5322  118  MET A SD  
911   C  CE  . MET A  118 ? 2.9623 3.3310 2.9955 0.6929  0.1483  0.4946  118  MET A CE  
912   N  N   . LYS A  119 ? 2.6402 3.1570 3.0276 0.4408  -0.0071 0.6840  119  LYS A N   
913   C  CA  . LYS A  119 ? 2.5599 3.0567 2.9975 0.3925  -0.0566 0.7205  119  LYS A CA  
914   C  C   . LYS A  119 ? 2.3645 2.9313 2.9463 0.3919  -0.0658 0.7211  119  LYS A C   
915   O  O   . LYS A  119 ? 2.2832 2.9151 2.9211 0.4260  -0.0359 0.6949  119  LYS A O   
916   C  CB  . LYS A  119 ? 2.6136 3.0200 3.0182 0.3827  -0.1102 0.7210  119  LYS A CB  
917   C  CG  . LYS A  119 ? 2.6450 3.0243 3.0384 0.4265  -0.1109 0.6790  119  LYS A CG  
918   C  CD  . LYS A  119 ? 2.7755 3.0647 3.1127 0.4116  -0.1593 0.6832  119  LYS A CD  
919   C  CE  . LYS A  119 ? 2.7930 3.0478 3.0910 0.4520  -0.1533 0.6428  119  LYS A CE  
920   N  NZ  . LYS A  119 ? 2.9060 3.1490 3.0951 0.4785  -0.1025 0.6216  119  LYS A NZ  
921   N  N   . GLN A  120 ? 2.2394 2.7896 2.8798 0.3526  -0.1093 0.7515  120  GLN A N   
922   C  CA  . GLN A  120 ? 2.0749 2.6805 2.8448 0.3437  -0.1213 0.7556  120  GLN A CA  
923   C  C   . GLN A  120 ? 2.0131 2.5991 2.8560 0.3669  -0.1551 0.7279  120  GLN A C   
924   O  O   . GLN A  120 ? 1.8900 2.4271 2.7647 0.3479  -0.2022 0.7417  120  GLN A O   
925   C  CB  . GLN A  120 ? 2.1133 2.7057 2.9078 0.2906  -0.1494 0.8023  120  GLN A CB  
926   C  CG  . GLN A  120 ? 2.2977 2.9300 3.0438 0.2625  -0.1129 0.8322  120  GLN A CG  
927   C  CD  . GLN A  120 ? 2.3517 2.9546 3.1062 0.2068  -0.1465 0.8826  120  GLN A CD  
928   O  OE1 . GLN A  120 ? 2.3089 2.8758 3.1320 0.1921  -0.1944 0.8937  120  GLN A OE1 
929   N  NE2 . GLN A  120 ? 2.5248 3.1431 3.2101 0.1763  -0.1208 0.9141  120  GLN A NE2 
930   N  N   . GLU A  121 ? 2.1637 2.7908 3.0349 0.4093  -0.1305 0.6895  121  GLU A N   
931   C  CA  . GLU A  121 ? 2.1161 2.7386 3.0611 0.4317  -0.1561 0.6614  121  GLU A CA  
932   C  C   . GLU A  121 ? 1.9117 2.6142 2.9635 0.4390  -0.1427 0.6481  121  GLU A C   
933   O  O   . GLU A  121 ? 1.8236 2.5848 2.8982 0.4236  -0.1175 0.6634  121  GLU A O   
934   C  CB  . GLU A  121 ? 2.1158 2.7093 3.0010 0.4727  -0.1462 0.6278  121  GLU A CB  
935   C  CG  . GLU A  121 ? 2.0799 2.5881 2.8595 0.4635  -0.1653 0.6375  121  GLU A CG  
936   C  CD  . GLU A  121 ? 1.9564 2.4120 2.7715 0.4398  -0.2208 0.6525  121  GLU A CD  
937   O  OE1 . GLU A  121 ? 2.0363 2.4283 2.7776 0.4179  -0.2444 0.6734  121  GLU A OE1 
938   O  OE2 . GLU A  121 ? 1.7756 2.2550 2.6925 0.4432  -0.2409 0.6433  121  GLU A OE2 
939   N  N   . ARG A  122 ? 1.9360 2.6416 3.0530 0.4603  -0.1609 0.6197  122  ARG A N   
940   C  CA  . ARG A  122 ? 1.7945 2.5703 3.0087 0.4689  -0.1525 0.6016  122  ARG A CA  
941   C  C   . ARG A  122 ? 1.7978 2.5742 3.0226 0.5100  -0.1531 0.5625  122  ARG A C   
942   O  O   . ARG A  122 ? 1.6708 2.4249 2.9465 0.5120  -0.1834 0.5480  122  ARG A O   
943   C  CB  . ARG A  122 ? 1.7460 2.5165 3.0471 0.4350  -0.1863 0.6160  122  ARG A CB  
944   C  CG  . ARG A  122 ? 1.6945 2.5372 3.0882 0.4343  -0.1769 0.6010  122  ARG A CG  
945   C  CD  . ARG A  122 ? 1.6964 2.5260 3.1607 0.3939  -0.2063 0.6211  122  ARG A CD  
946   N  NE  . ARG A  122 ? 1.7465 2.6461 3.2870 0.3841  -0.1948 0.6122  122  ARG A NE  
947   C  CZ  . ARG A  122 ? 1.6813 2.5983 3.2911 0.3954  -0.2068 0.5816  122  ARG A CZ  
948   N  NH1 . ARG A  122 ? 1.4054 2.2780 3.0211 0.4183  -0.2282 0.5570  122  ARG A NH1 
949   N  NH2 . ARG A  122 ? 1.7003 2.6813 3.3720 0.3816  -0.1974 0.5760  122  ARG A NH2 
950   N  N   . GLU A  123 ? 1.6840 2.4863 2.8592 0.5439  -0.1181 0.5457  123  GLU A N   
951   C  CA  . GLU A  123 ? 1.5529 2.3424 2.7157 0.5824  -0.1184 0.5131  123  GLU A CA  
952   C  C   . GLU A  123 ? 1.5240 2.3941 2.7489 0.6080  -0.0962 0.4911  123  GLU A C   
953   O  O   . GLU A  123 ? 1.6351 2.5655 2.8565 0.6175  -0.0608 0.4961  123  GLU A O   
954   C  CB  . GLU A  123 ? 1.6974 2.4390 2.7477 0.6050  -0.0999 0.5091  123  GLU A CB  
955   C  CG  . GLU A  123 ? 2.0079 2.6677 2.9886 0.5780  -0.1251 0.5307  123  GLU A CG  
956   C  CD  . GLU A  123 ? 2.0589 2.6619 2.9220 0.5982  -0.1101 0.5227  123  GLU A CD  
957   O  OE1 . GLU A  123 ? 2.1834 2.7144 2.9831 0.5771  -0.1350 0.5371  123  GLU A OE1 
958   O  OE2 . GLU A  123 ? 1.8813 2.5093 2.7152 0.6351  -0.0749 0.5023  123  GLU A OE2 
959   N  N   . PRO A  124 ? 1.4696 2.3465 2.7518 0.6189  -0.1157 0.4679  124  PRO A N   
960   C  CA  . PRO A  124 ? 1.3838 2.3384 2.7287 0.6393  -0.1004 0.4478  124  PRO A CA  
961   C  C   . PRO A  124 ? 1.3708 2.3428 2.6692 0.6852  -0.0724 0.4297  124  PRO A C   
962   O  O   . PRO A  124 ? 1.4391 2.3968 2.7363 0.7097  -0.0815 0.4069  124  PRO A O   
963   C  CB  . PRO A  124 ? 1.2271 2.1675 2.6359 0.6320  -0.1342 0.4294  124  PRO A CB  
964   C  CG  . PRO A  124 ? 1.2494 2.1049 2.6094 0.6290  -0.1592 0.4312  124  PRO A CG  
965   C  CD  . PRO A  124 ? 1.3403 2.1576 2.6381 0.6092  -0.1549 0.4610  124  PRO A CD  
966   N  N   . VAL A  125 ? 1.3355 2.3397 2.5943 0.6980  -0.0362 0.4410  125  VAL A N   
967   C  CA  . VAL A  125 ? 1.3537 2.3711 2.5662 0.7456  -0.0068 0.4253  125  VAL A CA  
968   C  C   . VAL A  125 ? 1.3068 2.4166 2.5925 0.7678  0.0069  0.4133  125  VAL A C   
969   O  O   . VAL A  125 ? 1.3957 2.5166 2.6568 0.8107  0.0246  0.3984  125  VAL A O   
970   C  CB  . VAL A  125 ? 1.4744 2.4878 2.6105 0.7564  0.0304  0.4393  125  VAL A CB  
971   C  CG1 . VAL A  125 ? 1.5897 2.5031 2.6349 0.7394  0.0162  0.4479  125  VAL A CG1 
972   C  CG2 . VAL A  125 ? 1.4866 2.5813 2.6712 0.7325  0.0520  0.4626  125  VAL A CG2 
973   N  N   . GLY A  126 ? 1.2571 2.4327 2.6294 0.7393  -0.0012 0.4211  126  GLY A N   
974   C  CA  . GLY A  126 ? 1.2107 2.4787 2.6532 0.7548  0.0087  0.4122  126  GLY A CA  
975   C  C   . GLY A  126 ? 1.3596 2.7044 2.7988 0.7793  0.0511  0.4236  126  GLY A C   
976   O  O   . GLY A  126 ? 1.5683 2.8838 2.9325 0.8058  0.0780  0.4266  126  GLY A O   
977   N  N   . THR A  127 ? 1.2080 2.6532 2.7286 0.7714  0.0577  0.4292  127  THR A N   
978   C  CA  . THR A  127 ? 1.2227 2.7595 2.7579 0.7943  0.0978  0.4418  127  THR A CA  
979   C  C   . THR A  127 ? 1.1812 2.7941 2.7832 0.7931  0.0910  0.4274  127  THR A C   
980   O  O   . THR A  127 ? 1.1429 2.7455 2.7846 0.7585  0.0569  0.4122  127  THR A O   
981   C  CB  . THR A  127 ? 1.3804 2.9535 2.9247 0.7567  0.1158  0.4710  127  THR A CB  
982   O  OG1 . THR A  127 ? 1.5467 3.2077 3.0963 0.7852  0.1604  0.4826  127  THR A OG1 
983   C  CG2 . THR A  127 ? 1.2145 2.8308 2.8450 0.7033  0.0892  0.4814  127  THR A CG2 
984   N  N   . CYS A  128 ? 1.2654 2.9279 2.8551 0.8207  0.1208  0.4225  128  CYS A N   
985   C  CA  . CYS A  128 ? 1.1959 2.9119 2.8254 0.8090  0.1130  0.4044  128  CYS A CA  
986   C  C   . CYS A  128 ? 1.2154 3.0434 2.8888 0.8110  0.1481  0.4292  128  CYS A C   
987   O  O   . CYS A  128 ? 1.2525 3.1061 2.9024 0.8377  0.1868  0.4508  128  CYS A O   
988   C  CB  . CYS A  128 ? 1.2230 2.8819 2.7975 0.8403  0.1075  0.3710  128  CYS A CB  
989   S  SG  . CYS A  128 ? 1.6867 3.2200 3.2082 0.8360  0.0684  0.3424  128  CYS A SG  
990   N  N   . PHE A  129 ? 1.1927 3.0906 2.9304 0.7813  0.1349  0.4266  129  PHE A N   
991   C  CA  . PHE A  129 ? 1.2374 3.2458 3.0208 0.7808  0.1638  0.4461  129  PHE A CA  
992   C  C   . PHE A  129 ? 1.2223 3.2478 3.0079 0.7970  0.1576  0.4221  129  PHE A C   
993   O  O   . PHE A  129 ? 1.1929 3.1934 2.9927 0.7776  0.1213  0.3994  129  PHE A O   
994   C  CB  . PHE A  129 ? 1.3097 3.3986 3.1764 0.7264  0.1533  0.4728  129  PHE A CB  
995   C  CG  . PHE A  129 ? 1.3439 3.4381 3.2199 0.7108  0.1664  0.5081  129  PHE A CG  
996   C  CD1 . PHE A  129 ? 1.4463 3.6163 3.3299 0.7210  0.2109  0.5416  129  PHE A CD1 
997   C  CD2 . PHE A  129 ? 1.1523 3.1762 3.0303 0.6866  0.1347  0.5092  129  PHE A CD2 
998   C  CE1 . PHE A  129 ? 1.3773 3.5304 3.2492 0.6959  0.2197  0.5701  129  PHE A CE1 
999   C  CE2 . PHE A  129 ? 1.1741 3.1691 3.0374 0.6602  0.1400  0.5355  129  PHE A CE2 
1000  C  CZ  . PHE A  129 ? 1.2235 3.2666 3.0682 0.6583  0.1801  0.5617  129  PHE A CZ  
1001  N  N   . LEU A  130 ? 1.3535 3.4215 3.1252 0.8343  0.1936  0.4283  130  LEU A N   
1002  C  CA  . LEU A  130 ? 1.2865 3.3761 3.0638 0.8553  0.1914  0.4122  130  LEU A CA  
1003  C  C   . LEU A  130 ? 1.2997 3.5158 3.1467 0.8433  0.2111  0.4349  130  LEU A C   
1004  O  O   . LEU A  130 ? 1.3270 3.6025 3.1832 0.8514  0.2496  0.4599  130  LEU A O   
1005  C  CB  . LEU A  130 ? 1.3377 3.3650 3.0409 0.9133  0.2153  0.3993  130  LEU A CB  
1006  C  CG  . LEU A  130 ? 1.3675 3.4178 3.0775 0.9414  0.2170  0.3883  130  LEU A CG  
1007  C  CD1 . LEU A  130 ? 1.3297 3.3538 3.0585 0.9174  0.1705  0.3680  130  LEU A CD1 
1008  C  CD2 . LEU A  130 ? 1.4260 3.4090 3.0606 0.9989  0.2429  0.3780  130  LEU A CD2 
1009  N  N   . GLN A  131 ? 1.3547 3.6150 3.2506 0.8234  0.1852  0.4272  131  GLN A N   
1010  C  CA  . GLN A  131 ? 1.7699 4.1525 3.7368 0.8086  0.1976  0.4483  131  GLN A CA  
1011  C  C   . GLN A  131 ? 1.7019 4.1012 3.6699 0.8431  0.1975  0.4368  131  GLN A C   
1012  O  O   . GLN A  131 ? 1.6290 4.0049 3.6049 0.8333  0.1615  0.4188  131  GLN A O   
1013  C  CB  . GLN A  131 ? 1.6526 4.0888 3.6888 0.7469  0.1648  0.4562  131  GLN A CB  
1014  C  CG  . GLN A  131 ? 1.4775 4.0447 3.5892 0.7250  0.1770  0.4820  131  GLN A CG  
1015  C  CD  . GLN A  131 ? 1.3853 4.0050 3.5619 0.6590  0.1502  0.4962  131  GLN A CD  
1016  O  OE1 . GLN A  131 ? 1.3409 3.9003 3.5079 0.6314  0.1264  0.4888  131  GLN A OE1 
1017  N  NE2 . GLN A  131 ? 1.3184 4.0502 3.5632 0.6327  0.1528  0.5171  131  GLN A NE2 
1018  N  N   . ASP A  132 ? 1.4538 3.8948 3.4146 0.8846  0.2383  0.4482  132  ASP A N   
1019  C  CA  . ASP A  132 ? 1.4898 3.9585 3.4618 0.9195  0.2409  0.4428  132  ASP A CA  
1020  C  C   . ASP A  132 ? 1.6803 4.2860 3.7341 0.9039  0.2544  0.4682  132  ASP A C   
1021  O  O   . ASP A  132 ? 1.7079 4.3675 3.7697 0.9413  0.2914  0.4796  132  ASP A O   
1022  C  CB  . ASP A  132 ? 1.7862 4.1984 3.6915 0.9829  0.2758  0.4347  132  ASP A CB  
1023  C  CG  . ASP A  132 ? 2.1495 4.5667 4.0595 1.0214  0.2714  0.4265  132  ASP A CG  
1024  O  OD1 . ASP A  132 ? 2.2832 4.6932 4.2158 1.0028  0.2312  0.4172  132  ASP A OD1 
1025  O  OD2 . ASP A  132 ? 2.3264 4.7560 4.2184 1.0709  0.3086  0.4301  132  ASP A OD2 
1026  N  N   . GLY A  133 ? 1.5323 4.1957 3.6475 0.8484  0.2249  0.4771  133  GLY A N   
1027  C  CA  . GLY A  133 ? 1.5058 4.3011 3.7015 0.8255  0.2331  0.5029  133  GLY A CA  
1028  C  C   . GLY A  133 ? 1.5014 4.3576 3.7289 0.7845  0.2519  0.5291  133  GLY A C   
1029  O  O   . GLY A  133 ? 1.5643 4.4222 3.8185 0.7301  0.2232  0.5327  133  GLY A O   
1030  N  N   . THR A  134 ? 1.4358 4.3420 3.6601 0.8101  0.3011  0.5481  134  THR A N   
1031  C  CA  . THR A  134 ? 1.4345 4.4049 3.6863 0.7736  0.3253  0.5777  134  THR A CA  
1032  C  C   . THR A  134 ? 1.4306 4.3190 3.6148 0.7868  0.3457  0.5753  134  THR A C   
1033  O  O   . THR A  134 ? 1.3971 4.2778 3.5912 0.7416  0.3343  0.5885  134  THR A O   
1034  C  CB  . THR A  134 ? 1.4882 4.5787 3.7827 0.7893  0.3699  0.6036  134  THR A CB  
1035  O  OG1 . THR A  134 ? 1.5426 4.5963 3.7772 0.8558  0.4138  0.5945  134  THR A OG1 
1036  C  CG2 . THR A  134 ? 1.5377 4.7071 3.8967 0.7858  0.3503  0.6060  134  THR A CG2 
1037  N  N   . LYS A  135 ? 1.4682 4.2933 3.5839 0.8480  0.3743  0.5597  135  LYS A N   
1038  C  CA  . LYS A  135 ? 1.4743 4.2256 3.5215 0.8654  0.3971  0.5589  135  LYS A CA  
1039  C  C   . LYS A  135 ? 1.4205 4.0630 3.4344 0.8437  0.3535  0.5402  135  LYS A C   
1040  O  O   . LYS A  135 ? 1.4011 3.9785 3.3993 0.8514  0.3178  0.5130  135  LYS A O   
1041  C  CB  . LYS A  135 ? 1.5351 4.2382 3.5131 0.9371  0.4351  0.5431  135  LYS A CB  
1042  C  CG  . LYS A  135 ? 1.5975 4.4022 3.6047 0.9670  0.4818  0.5580  135  LYS A CG  
1043  C  CD  . LYS A  135 ? 1.6158 4.5056 3.6422 0.9444  0.5242  0.5909  135  LYS A CD  
1044  C  CE  . LYS A  135 ? 1.6792 4.6806 3.7424 0.9694  0.5704  0.6060  135  LYS A CE  
1045  N  NZ  . LYS A  135 ? 1.7094 4.7848 3.7749 0.9538  0.6196  0.6359  135  LYS A NZ  
1046  N  N   . THR A  136 ? 1.3985 4.0260 3.4053 0.8147  0.3563  0.5570  136  THR A N   
1047  C  CA  . THR A  136 ? 1.3542 3.8780 3.3280 0.7982  0.3203  0.5426  136  THR A CA  
1048  C  C   . THR A  136 ? 1.3791 3.8371 3.2793 0.8330  0.3505  0.5456  136  THR A C   
1049  O  O   . THR A  136 ? 1.5110 4.0239 3.4173 0.8268  0.3865  0.5757  136  THR A O   
1050  C  CB  . THR A  136 ? 1.3068 3.8672 3.3446 0.7297  0.2904  0.5627  136  THR A CB  
1051  O  OG1 . THR A  136 ? 1.2893 3.9069 3.3897 0.6983  0.2613  0.5575  136  THR A OG1 
1052  C  CG2 . THR A  136 ? 1.2668 3.7191 3.2724 0.7166  0.2553  0.5483  136  THR A CG2 
1053  N  N   . VAL A  137 ? 1.3804 3.7231 3.2105 0.8671  0.3357  0.5162  137  VAL A N   
1054  C  CA  . VAL A  137 ? 1.4105 3.6814 3.1629 0.9041  0.3615  0.5160  137  VAL A CA  
1055  C  C   . VAL A  137 ? 1.3669 3.5379 3.0934 0.8847  0.3213  0.5061  137  VAL A C   
1056  O  O   . VAL A  137 ? 1.3227 3.4611 3.0740 0.8560  0.2758  0.4886  137  VAL A O   
1057  C  CB  . VAL A  137 ? 1.4697 3.6871 3.1509 0.9691  0.3862  0.4915  137  VAL A CB  
1058  C  CG1 . VAL A  137 ? 1.7290 4.0444 3.4417 0.9908  0.4240  0.5000  137  VAL A CG1 
1059  C  CG2 . VAL A  137 ? 1.4504 3.5768 3.1055 0.9773  0.3433  0.4571  137  VAL A CG2 
1060  N  N   . GLU A  138 ? 1.3846 3.5097 3.0607 0.9014  0.3396  0.5183  138  GLU A N   
1061  C  CA  . GLU A  138 ? 1.3536 3.3777 2.9970 0.8917  0.3051  0.5108  138  GLU A CA  
1062  C  C   . GLU A  138 ? 1.3894 3.3040 2.9397 0.9426  0.3064  0.4805  138  GLU A C   
1063  O  O   . GLU A  138 ? 1.4488 3.3628 2.9484 0.9903  0.3460  0.4754  138  GLU A O   
1064  C  CB  . GLU A  138 ? 1.3777 3.3721 2.9924 0.8543  0.3110  0.5351  138  GLU A CB  
1065  C  CG  . GLU A  138 ? 1.3581 3.2322 2.9394 0.8168  0.2622  0.5242  138  GLU A CG  
1066  C  CD  . GLU A  138 ? 1.4366 3.2533 2.9672 0.7691  0.2618  0.5436  138  GLU A CD  
1067  O  OE1 . GLU A  138 ? 1.5804 3.4303 3.0758 0.7724  0.3031  0.5608  138  GLU A OE1 
1068  O  OE2 . GLU A  138 ? 1.4351 3.1735 2.9599 0.7296  0.2206  0.5421  138  GLU A OE2 
1069  N  N   . TYR A  139 ? 1.4543 3.2742 2.9816 0.9308  0.2629  0.4602  139  TYR A N   
1070  C  CA  . TYR A  139 ? 1.5721 3.2826 3.0137 0.9700  0.2568  0.4323  139  TYR A CA  
1071  C  C   . TYR A  139 ? 1.4521 3.0741 2.8674 0.9533  0.2229  0.4319  139  TYR A C   
1072  O  O   . TYR A  139 ? 1.3124 2.9090 2.7612 0.9162  0.1806  0.4193  139  TYR A O   
1073  C  CB  . TYR A  139 ? 1.6619 3.3519 3.1042 0.9747  0.2355  0.4007  139  TYR A CB  
1074  C  CG  . TYR A  139 ? 1.6551 3.2338 3.0140 1.0089  0.2265  0.3749  139  TYR A CG  
1075  C  CD1 . TYR A  139 ? 1.7025 3.2431 2.9874 1.0605  0.2628  0.3744  139  TYR A CD1 
1076  C  CD2 . TYR A  139 ? 1.3816 2.8942 2.7342 0.9892  0.1831  0.3511  139  TYR A CD2 
1077  C  CE1 . TYR A  139 ? 1.5899 3.0257 2.7975 1.0896  0.2531  0.3523  139  TYR A CE1 
1078  C  CE2 . TYR A  139 ? 1.4123 2.8276 2.6917 1.0163  0.1744  0.3311  139  TYR A CE2 
1079  C  CZ  . TYR A  139 ? 1.4821 2.8579 2.6898 1.0655  0.2080  0.3325  139  TYR A CZ  
1080  O  OH  . TYR A  139 ? 1.5180 2.7938 2.6518 1.0906  0.1978  0.3138  139  TYR A OH  
1081  N  N   . ALA A  140 ? 1.5993 3.1450 2.9302 0.9627  0.2370  0.4357  140  ALA A N   
1082  C  CA  . ALA A  140 ? 1.7304 3.1591 3.0058 0.9313  0.2009  0.4284  140  ALA A CA  
1083  C  C   . ALA A  140 ? 1.9488 3.2735 3.1121 0.9693  0.2115  0.4116  140  ALA A C   
1084  O  O   . ALA A  140 ? 2.1530 3.4228 3.2355 0.9621  0.2290  0.4176  140  ALA A O   
1085  C  CB  . ALA A  140 ? 1.7066 3.1249 2.9795 0.8741  0.1949  0.4510  140  ALA A CB  
1086  N  N   . PRO A  141 ? 1.8604 3.1521 3.0116 1.0077  0.2000  0.3907  141  PRO A N   
1087  C  CA  . PRO A  141 ? 1.8218 3.0097 2.8636 1.0441  0.2093  0.3741  141  PRO A CA  
1088  C  C   . PRO A  141 ? 1.7817 2.8528 2.7522 1.0092  0.1772  0.3706  141  PRO A C   
1089  O  O   . PRO A  141 ? 1.8984 2.8769 2.7669 1.0286  0.1848  0.3599  141  PRO A O   
1090  C  CB  . PRO A  141 ? 1.7544 2.9449 2.8166 1.0834  0.1985  0.3555  141  PRO A CB  
1091  C  CG  . PRO A  141 ? 1.7599 2.9869 2.9037 1.0298  0.1599  0.3501  141  PRO A CG  
1092  C  CD  . PRO A  141 ? 1.7865 3.1152 3.0066 1.0051  0.1738  0.3767  141  PRO A CD  
1093  N  N   . CYS A  142 ? 1.5151 2.5869 2.5368 0.9591  0.1406  0.3791  142  CYS A N   
1094  C  CA  . CYS A  142 ? 1.5580 2.5315 2.5268 0.9233  0.1077  0.3803  142  CYS A CA  
1095  C  C   . CYS A  142 ? 1.6508 2.6155 2.5944 0.8829  0.1138  0.4029  142  CYS A C   
1096  O  O   . CYS A  142 ? 1.7663 2.6472 2.6533 0.8549  0.0899  0.4077  142  CYS A O   
1097  C  CB  . CYS A  142 ? 1.7373 2.7114 2.7769 0.8971  0.0634  0.3748  142  CYS A CB  
1098  S  SG  . CYS A  142 ? 1.7804 2.7190 2.8074 0.9369  0.0477  0.3487  142  CYS A SG  
1099  N  N   . ARG A  143 ? 1.6988 2.7512 2.6853 0.8771  0.1436  0.4192  143  ARG A N   
1100  C  CA  . ARG A  143 ? 1.8055 2.8557 2.7599 0.8417  0.1566  0.4431  143  ARG A CA  
1101  C  C   . ARG A  143 ? 2.0658 3.0655 2.9051 0.8708  0.1933  0.4378  143  ARG A C   
1102  O  O   . ARG A  143 ? 2.1342 3.1952 2.9670 0.8962  0.2395  0.4409  143  ARG A O   
1103  C  CB  . ARG A  143 ? 1.7505 2.9176 2.7936 0.8243  0.1763  0.4628  143  ARG A CB  
1104  C  CG  . ARG A  143 ? 1.8412 3.0129 2.8702 0.7763  0.1812  0.4923  143  ARG A CG  
1105  C  CD  . ARG A  143 ? 1.7754 3.0670 2.9010 0.7568  0.1976  0.5117  143  ARG A CD  
1106  N  NE  . ARG A  143 ? 1.8857 3.2617 3.0173 0.8003  0.2479  0.5081  143  ARG A NE  
1107  C  CZ  . ARG A  143 ? 2.0310 3.5266 3.2555 0.7998  0.2646  0.5185  143  ARG A CZ  
1108  N  NH1 . ARG A  143 ? 1.8688 3.4066 3.1821 0.7554  0.2343  0.5312  143  ARG A NH1 
1109  N  NH2 . ARG A  143 ? 2.1417 3.7144 3.3710 0.8437  0.3112  0.5161  143  ARG A NH2 
1110  N  N   . SER A  144 ? 2.1838 3.0704 2.9304 0.8675  0.1730  0.4285  144  SER A N   
1111  C  CA  . SER A  144 ? 2.3906 3.2088 3.0147 0.8952  0.2029  0.4176  144  SER A CA  
1112  C  C   . SER A  144 ? 2.5841 3.3190 3.1207 0.8511  0.1861  0.4327  144  SER A C   
1113  O  O   . SER A  144 ? 2.7031 3.4438 3.2803 0.8017  0.1559  0.4553  144  SER A O   
1114  C  CB  . SER A  144 ? 2.2748 3.0260 2.8539 0.9385  0.1951  0.3888  144  SER A CB  
1115  O  OG  . SER A  144 ? 2.3543 3.0410 2.8169 0.9717  0.2283  0.3746  144  SER A OG  
1116  N  N   . GLN A  145 ? 2.6033 3.2548 3.0158 0.8697  0.2038  0.4199  145  GLN A N   
1117  C  CA  . GLN A  145 ? 2.6177 3.1765 2.9307 0.8302  0.1837  0.4312  145  GLN A CA  
1118  C  C   . GLN A  145 ? 2.4901 2.9561 2.7777 0.8161  0.1313  0.4225  145  GLN A C   
1119  O  O   . GLN A  145 ? 2.5070 2.8991 2.7280 0.7775  0.1029  0.4351  145  GLN A O   
1120  C  CB  . GLN A  145 ? 2.8221 3.3304 3.0037 0.8536  0.2279  0.4198  145  GLN A CB  
1121  C  CG  . GLN A  145 ? 2.8649 3.4657 3.0597 0.8764  0.2890  0.4248  145  GLN A CG  
1122  C  CD  . GLN A  145 ? 2.7267 3.4112 2.9929 0.8291  0.2887  0.4599  145  GLN A CD  
1123  O  OE1 . GLN A  145 ? 2.6436 3.4400 3.0041 0.8403  0.3144  0.4681  145  GLN A OE1 
1124  N  NE2 . GLN A  145 ? 2.8091 3.4394 3.0286 0.7747  0.2587  0.4827  145  GLN A NE2 
1125  N  N   . ASP A  146 ? 2.4265 2.8991 2.7662 0.8455  0.1180  0.4028  146  ASP A N   
1126  C  CA  . ASP A  146 ? 2.3176 2.7220 2.6560 0.8319  0.0686  0.3957  146  ASP A CA  
1127  C  C   . ASP A  146 ? 2.1447 2.5954 2.5908 0.7905  0.0303  0.4158  146  ASP A C   
1128  O  O   . ASP A  146 ? 2.0822 2.5936 2.6297 0.7996  0.0207  0.4100  146  ASP A O   
1129  C  CB  . ASP A  146 ? 2.2110 2.6105 2.5631 0.8788  0.0727  0.3688  146  ASP A CB  
1130  C  CG  . ASP A  146 ? 2.1784 2.5024 2.5136 0.8650  0.0259  0.3611  146  ASP A CG  
1131  O  OD1 . ASP A  146 ? 2.2709 2.5242 2.5481 0.8275  -0.0037 0.3718  146  ASP A OD1 
1132  O  OD2 . ASP A  146 ? 2.1851 2.5251 2.5676 0.8901  0.0179  0.3460  146  ASP A OD2 
1133  N  N   . ILE A  147 ? 2.2130 2.6325 2.6335 0.7444  0.0085  0.4400  147  ILE A N   
1134  C  CA  . ILE A  147 ? 2.2179 2.6791 2.7354 0.7047  -0.0230 0.4628  147  ILE A CA  
1135  C  C   . ILE A  147 ? 2.0253 2.4338 2.5638 0.6846  -0.0753 0.4625  147  ILE A C   
1136  O  O   . ILE A  147 ? 2.0306 2.3737 2.5087 0.6981  -0.0880 0.4462  147  ILE A O   
1137  C  CB  . ILE A  147 ? 2.4106 2.8731 2.8983 0.6652  -0.0190 0.4941  147  ILE A CB  
1138  C  CG1 . ILE A  147 ? 2.4723 2.8338 2.8476 0.6393  -0.0433 0.5041  147  ILE A CG1 
1139  C  CG2 . ILE A  147 ? 2.4470 2.9675 2.9122 0.6847  0.0367  0.4948  147  ILE A CG2 
1140  C  CD1 . ILE A  147 ? 2.5267 2.8825 2.8589 0.5989  -0.0408 0.5367  147  ILE A CD1 
1141  N  N   . ASP A  148 ? 2.1184 2.5566 2.7449 0.6523  -0.1053 0.4810  148  ASP A N   
1142  C  CA  . ASP A  148 ? 2.1914 2.5929 2.8551 0.6309  -0.1543 0.4850  148  ASP A CA  
1143  C  C   . ASP A  148 ? 2.0324 2.4473 2.7465 0.6585  -0.1626 0.4574  148  ASP A C   
1144  O  O   . ASP A  148 ? 1.8841 2.3259 2.5924 0.6953  -0.1330 0.4357  148  ASP A O   
1145  C  CB  . ASP A  148 ? 2.3988 2.7089 2.9608 0.6088  -0.1797 0.4967  148  ASP A CB  
1146  C  CG  . ASP A  148 ? 2.2115 2.5001 2.8209 0.5716  -0.2297 0.5193  148  ASP A CG  
1147  O  OD1 . ASP A  148 ? 1.9971 2.3255 2.7114 0.5726  -0.2474 0.5145  148  ASP A OD1 
1148  O  OD2 . ASP A  148 ? 2.2632 2.4956 2.8047 0.5420  -0.2513 0.5418  148  ASP A OD2 
1149  N  N   . ALA A  149 ? 2.0376 2.4369 2.8038 0.6411  -0.2028 0.4597  149  ALA A N   
1150  C  CA  . ALA A  149 ? 1.8626 2.2771 2.6785 0.6624  -0.2121 0.4354  149  ALA A CA  
1151  C  C   . ALA A  149 ? 1.9784 2.3415 2.7051 0.6888  -0.2024 0.4164  149  ALA A C   
1152  O  O   . ALA A  149 ? 1.9177 2.3045 2.6669 0.7182  -0.1914 0.3943  149  ALA A O   
1153  C  CB  . ALA A  149 ? 1.6428 2.0443 2.5196 0.6378  -0.2556 0.4429  149  ALA A CB  
1154  N  N   . ASP A  150 ? 2.1630 2.4512 2.7845 0.6769  -0.2085 0.4254  150  ASP A N   
1155  C  CA  . ASP A  150 ? 2.1489 2.3744 2.6736 0.6994  -0.2000 0.4074  150  ASP A CA  
1156  C  C   . ASP A  150 ? 2.1565 2.4105 2.6590 0.7428  -0.1535 0.3885  150  ASP A C   
1157  O  O   . ASP A  150 ? 2.1657 2.3860 2.6220 0.7718  -0.1452 0.3686  150  ASP A O   
1158  C  CB  . ASP A  150 ? 2.2666 2.4067 2.6766 0.6748  -0.2127 0.4210  150  ASP A CB  
1159  C  CG  . ASP A  150 ? 2.4442 2.5660 2.8817 0.6306  -0.2586 0.4463  150  ASP A CG  
1160  O  OD1 . ASP A  150 ? 2.6174 2.7097 3.0628 0.6201  -0.2920 0.4443  150  ASP A OD1 
1161  O  OD2 . ASP A  150 ? 2.2934 2.4327 2.7469 0.6063  -0.2616 0.4699  150  ASP A OD2 
1162  N  N   . GLY A  151 ? 2.1979 2.5130 2.7317 0.7478  -0.1234 0.3962  151  GLY A N   
1163  C  CA  . GLY A  151 ? 2.1754 2.5312 2.7011 0.7902  -0.0784 0.3811  151  GLY A CA  
1164  C  C   . GLY A  151 ? 2.1195 2.5741 2.7637 0.8050  -0.0695 0.3757  151  GLY A C   
1165  O  O   . GLY A  151 ? 2.0411 2.5111 2.7492 0.8032  -0.0942 0.3675  151  GLY A O   
1166  N  N   . GLN A  152 ? 1.7849 2.3095 2.4589 0.8168  -0.0344 0.3812  152  GLN A N   
1167  C  CA  . GLN A  152 ? 1.5949 2.2181 2.3762 0.8296  -0.0238 0.3772  152  GLN A CA  
1168  C  C   . GLN A  152 ? 1.5513 2.2303 2.4115 0.7907  -0.0333 0.3981  152  GLN A C   
1169  O  O   . GLN A  152 ? 1.5012 2.2664 2.4415 0.7950  -0.0188 0.3993  152  GLN A O   
1170  C  CB  . GLN A  152 ? 1.6220 2.2935 2.3895 0.8739  0.0224  0.3687  152  GLN A CB  
1171  C  CG  . GLN A  152 ? 1.6714 2.2884 2.3690 0.9179  0.0322  0.3471  152  GLN A CG  
1172  C  CD  . GLN A  152 ? 1.7159 2.3749 2.3939 0.9654  0.0805  0.3405  152  GLN A CD  
1173  O  OE1 . GLN A  152 ? 1.9358 2.6656 2.6455 0.9634  0.1091  0.3530  152  GLN A OE1 
1174  N  NE2 . GLN A  152 ? 1.7501 2.3655 2.3766 1.0086  0.0899  0.3219  152  GLN A NE2 
1175  N  N   . GLY A  153 ? 1.9780 2.6070 2.8156 0.7515  -0.0592 0.4161  153  GLY A N   
1176  C  CA  . GLY A  153 ? 1.9569 2.6259 2.8624 0.7135  -0.0705 0.4384  153  GLY A CA  
1177  C  C   . GLY A  153 ? 1.8540 2.5734 2.8718 0.7052  -0.0923 0.4311  153  GLY A C   
1178  O  O   . GLY A  153 ? 1.9472 2.7272 3.0364 0.6870  -0.0883 0.4421  153  GLY A O   
1179  N  N   . PHE A  154 ? 1.5526 2.2466 2.5849 0.7166  -0.1151 0.4121  154  PHE A N   
1180  C  CA  . PHE A  154 ? 1.3728 2.1079 2.5033 0.7096  -0.1354 0.4012  154  PHE A CA  
1181  C  C   . PHE A  154 ? 1.4436 2.2201 2.5958 0.7454  -0.1218 0.3761  154  PHE A C   
1182  O  O   . PHE A  154 ? 1.2439 2.0320 2.4481 0.7462  -0.1409 0.3605  154  PHE A O   
1183  C  CB  . PHE A  154 ? 1.3435 2.0231 2.4848 0.6879  -0.1755 0.4027  154  PHE A CB  
1184  C  CG  . PHE A  154 ? 1.5298 2.1825 2.6772 0.6505  -0.1945 0.4301  154  PHE A CG  
1185  C  CD1 . PHE A  154 ? 1.6882 2.2909 2.7501 0.6390  -0.1913 0.4505  154  PHE A CD1 
1186  C  CD2 . PHE A  154 ? 1.4927 2.1679 2.7281 0.6267  -0.2154 0.4359  154  PHE A CD2 
1187  C  CE1 . PHE A  154 ? 1.5510 2.1292 2.6161 0.6034  -0.2109 0.4790  154  PHE A CE1 
1188  C  CE2 . PHE A  154 ? 1.3448 1.9917 2.5861 0.5935  -0.2346 0.4639  154  PHE A CE2 
1189  C  CZ  . PHE A  154 ? 1.4654 2.0656 2.6222 0.5814  -0.2332 0.4870  154  PHE A CZ  
1190  N  N   . CYS A  155 ? 1.7964 2.5965 2.9079 0.7758  -0.0876 0.3733  155  CYS A N   
1191  C  CA  . CYS A  155 ? 1.4714 2.3093 2.5945 0.8143  -0.0725 0.3537  155  CYS A CA  
1192  C  C   . CYS A  155 ? 1.3091 2.2327 2.5348 0.8096  -0.0761 0.3469  155  CYS A C   
1193  O  O   . CYS A  155 ? 1.2195 2.1473 2.4567 0.8171  -0.0855 0.3218  155  CYS A O   
1194  C  CB  . CYS A  155 ? 1.3956 2.2467 2.4616 0.8477  -0.0327 0.3561  155  CYS A CB  
1195  S  SG  . CYS A  155 ? 1.3345 2.2646 2.4402 0.8950  -0.0079 0.3416  155  CYS A SG  
1196  N  N   . GLN A  156 ? 1.2689 2.2464 2.5501 0.7845  -0.0705 0.3613  156  GLN A N   
1197  C  CA  . GLN A  156 ? 1.2934 2.3548 2.6673 0.7768  -0.0721 0.3558  156  GLN A CA  
1198  C  C   . GLN A  156 ? 1.3832 2.4797 2.7375 0.7994  -0.0521 0.3321  156  GLN A C   
1199  O  O   . GLN A  156 ? 1.3605 2.4600 2.7271 0.7882  -0.0666 0.3009  156  GLN A O   
1200  C  CB  . GLN A  156 ? 1.1447 2.1729 2.5476 0.7445  -0.1075 0.3304  156  GLN A CB  
1201  C  CG  . GLN A  156 ? 1.3300 2.3203 2.7604 0.7193  -0.1305 0.3525  156  GLN A CG  
1202  C  CD  . GLN A  156 ? 1.4093 2.3756 2.8701 0.6899  -0.1595 0.3244  156  GLN A CD  
1203  O  OE1 . GLN A  156 ? 1.3522 2.2590 2.7827 0.6866  -0.1788 0.3124  156  GLN A OE1 
1204  N  NE2 . GLN A  156 ? 1.2888 2.3043 2.8080 0.6694  -0.1610 0.3150  156  GLN A NE2 
1205  N  N   . GLY A  157 ? 1.2189 2.3411 2.5415 0.8330  -0.0182 0.3484  157  GLY A N   
1206  C  CA  . GLY A  157 ? 1.2219 2.3744 2.5278 0.8561  0.0018  0.3297  157  GLY A CA  
1207  C  C   . GLY A  157 ? 1.4969 2.7286 2.8750 0.8310  -0.0009 0.3211  157  GLY A C   
1208  O  O   . GLY A  157 ? 1.5708 2.8599 3.0088 0.8075  0.0010  0.3411  157  GLY A O   
1209  N  N   . GLY A  158 ? 1.6327 2.8668 3.0062 0.8348  -0.0072 0.2941  158  GLY A N   
1210  C  CA  . GLY A  158 ? 1.4709 2.7741 2.9067 0.8122  -0.0144 0.2840  158  GLY A CA  
1211  C  C   . GLY A  158 ? 1.3237 2.6076 2.7885 0.7790  -0.0498 0.2612  158  GLY A C   
1212  O  O   . GLY A  158 ? 1.2046 2.5464 2.7241 0.7569  -0.0585 0.2543  158  GLY A O   
1213  N  N   . PHE A  159 ? 1.1015 2.3089 2.5309 0.7758  -0.0696 0.2495  159  PHE A N   
1214  C  CA  . PHE A  159 ? 1.0663 2.2560 2.5173 0.7493  -0.0997 0.2247  159  PHE A CA  
1215  C  C   . PHE A  159 ? 1.0566 2.2670 2.5136 0.7496  -0.1075 0.2001  159  PHE A C   
1216  O  O   . PHE A  159 ? 1.0285 2.2729 2.5273 0.7273  -0.1234 0.1845  159  PHE A O   
1217  C  CB  . PHE A  159 ? 1.1659 2.2729 2.5727 0.7502  -0.1162 0.2183  159  PHE A CB  
1218  C  CG  . PHE A  159 ? 1.0932 2.1854 2.5199 0.7254  -0.1426 0.1960  159  PHE A CG  
1219  C  CD1 . PHE A  159 ? 1.0626 2.1714 2.5344 0.7014  -0.1502 0.2057  159  PHE A CD1 
1220  C  CD2 . PHE A  159 ? 1.0297 2.0917 2.4301 0.7270  -0.1576 0.1684  159  PHE A CD2 
1221  C  CE1 . PHE A  159 ? 1.0005 2.0959 2.4851 0.6824  -0.1690 0.1871  159  PHE A CE1 
1222  C  CE2 . PHE A  159 ? 1.0060 2.0638 2.4162 0.7098  -0.1757 0.1489  159  PHE A CE2 
1223  C  CZ  . PHE A  159 ? 0.9931 2.0676 2.4422 0.6888  -0.1790 0.1591  159  PHE A CZ  
1224  N  N   . SER A  160 ? 1.0841 2.2770 2.5009 0.7756  -0.0955 0.1995  160  SER A N   
1225  C  CA  . SER A  160 ? 1.0827 2.2996 2.5080 0.7786  -0.1000 0.1860  160  SER A CA  
1226  C  C   . SER A  160 ? 1.1222 2.3617 2.5274 0.8100  -0.0735 0.2010  160  SER A C   
1227  O  O   . SER A  160 ? 1.1568 2.3584 2.5143 0.8356  -0.0556 0.2129  160  SER A O   
1228  C  CB  . SER A  160 ? 1.0788 2.2335 2.4693 0.7784  -0.1189 0.1679  160  SER A CB  
1229  O  OG  . SER A  160 ? 1.2032 2.2943 2.5314 0.8029  -0.1093 0.1766  160  SER A OG  
1230  N  N   . ILE A  161 ? 1.1217 2.4229 2.5618 0.8101  -0.0712 0.2003  161  ILE A N   
1231  C  CA  . ILE A  161 ? 1.1610 2.4959 2.5920 0.8408  -0.0460 0.2139  161  ILE A CA  
1232  C  C   . ILE A  161 ? 1.1651 2.5205 2.6072 0.8453  -0.0571 0.2062  161  ILE A C   
1233  O  O   . ILE A  161 ? 1.1342 2.4952 2.6006 0.8211  -0.0822 0.1927  161  ILE A O   
1234  C  CB  . ILE A  161 ? 1.1622 2.5803 2.6407 0.8373  -0.0249 0.2327  161  ILE A CB  
1235  C  CG1 . ILE A  161 ? 1.1186 2.5957 2.6651 0.7977  -0.0448 0.2280  161  ILE A CG1 
1236  C  CG2 . ILE A  161 ? 1.1773 2.5738 2.6307 0.8471  -0.0047 0.2490  161  ILE A CG2 
1237  C  CD1 . ILE A  161 ? 1.1185 2.6851 2.7193 0.7881  -0.0268 0.2496  161  ILE A CD1 
1238  N  N   . ASP A  162 ? 1.3000 2.6675 2.7233 0.8790  -0.0375 0.2161  162  ASP A N   
1239  C  CA  . ASP A  162 ? 1.3270 2.7207 2.7623 0.8898  -0.0454 0.2152  162  ASP A CA  
1240  C  C   . ASP A  162 ? 1.2754 2.6940 2.6986 0.9305  -0.0161 0.2296  162  ASP A C   
1241  O  O   . ASP A  162 ? 1.3060 2.7006 2.6946 0.9538  0.0096  0.2365  162  ASP A O   
1242  C  CB  . ASP A  162 ? 1.4254 2.7484 2.8191 0.8914  -0.0669 0.2039  162  ASP A CB  
1243  C  CG  . ASP A  162 ? 1.3294 2.6921 2.7549 0.8825  -0.0877 0.2017  162  ASP A CG  
1244  O  OD1 . ASP A  162 ? 1.3219 2.7616 2.7934 0.8850  -0.0829 0.2105  162  ASP A OD1 
1245  O  OD2 . ASP A  162 ? 1.2024 2.5229 2.6071 0.8734  -0.1086 0.1932  162  ASP A OD2 
1246  N  N   . PHE A  163 ? 1.2897 2.7591 2.7427 0.9406  -0.0198 0.2345  163  PHE A N   
1247  C  CA  . PHE A  163 ? 1.3448 2.8406 2.7920 0.9824  0.0057  0.2469  163  PHE A CA  
1248  C  C   . PHE A  163 ? 1.3818 2.8269 2.7903 1.0104  -0.0040 0.2448  163  PHE A C   
1249  O  O   . PHE A  163 ? 1.3596 2.7923 2.7732 0.9928  -0.0331 0.2388  163  PHE A O   
1250  C  CB  . PHE A  163 ? 1.3402 2.9467 2.8605 0.9758  0.0110  0.2592  163  PHE A CB  
1251  C  CG  . PHE A  163 ? 1.3262 2.9912 2.8809 0.9617  0.0322  0.2689  163  PHE A CG  
1252  C  CD1 . PHE A  163 ? 1.3686 3.0453 2.9057 0.9940  0.0701  0.2806  163  PHE A CD1 
1253  C  CD2 . PHE A  163 ? 1.2751 2.9849 2.8793 0.9170  0.0151  0.2675  163  PHE A CD2 
1254  C  CE1 . PHE A  163 ? 1.3575 3.0939 2.9271 0.9804  0.0908  0.2935  163  PHE A CE1 
1255  C  CE2 . PHE A  163 ? 1.2648 3.0306 2.9027 0.9025  0.0337  0.2803  163  PHE A CE2 
1256  C  CZ  . PHE A  163 ? 1.3168 3.0980 2.9380 0.9334  0.0718  0.2948  163  PHE A CZ  
1257  N  N   . THR A  164 ? 1.6036 3.0209 2.9729 1.0553  0.0214  0.2507  164  THR A N   
1258  C  CA  . THR A  164 ? 1.4910 2.8699 2.8296 1.0887  0.0161  0.2526  164  THR A CA  
1259  C  C   . THR A  164 ? 1.5782 3.0414 2.9702 1.1094  0.0227  0.2655  164  THR A C   
1260  O  O   . THR A  164 ? 1.5029 3.0529 2.9514 1.0998  0.0347  0.2733  164  THR A O   
1261  C  CB  . THR A  164 ? 1.5532 2.8499 2.8174 1.1298  0.0396  0.2507  164  THR A CB  
1262  O  OG1 . THR A  164 ? 1.7993 3.1392 3.0722 1.1613  0.0774  0.2585  164  THR A OG1 
1263  C  CG2 . THR A  164 ? 1.5307 2.7522 2.7450 1.1104  0.0349  0.2408  164  THR A CG2 
1264  N  N   . LYS A  165 ? 1.5613 2.9994 2.9360 1.1392  0.0144  0.2698  165  LYS A N   
1265  C  CA  . LYS A  165 ? 1.5938 3.1085 3.0189 1.1637  0.0188  0.2838  165  LYS A CA  
1266  C  C   . LYS A  165 ? 1.8116 3.3385 3.2277 1.2119  0.0593  0.2900  165  LYS A C   
1267  O  O   . LYS A  165 ? 2.2069 3.8102 3.6733 1.2338  0.0692  0.3025  165  LYS A O   
1268  C  CB  . LYS A  165 ? 1.6173 3.1049 3.0323 1.1774  -0.0087 0.2886  165  LYS A CB  
1269  C  CG  . LYS A  165 ? 1.8331 3.4072 3.3092 1.1974  -0.0131 0.3051  165  LYS A CG  
1270  C  CD  . LYS A  165 ? 1.9519 3.5118 3.4267 1.1976  -0.0486 0.3119  165  LYS A CD  
1271  C  CE  . LYS A  165 ? 1.6899 3.3320 3.2226 1.2248  -0.0520 0.3307  165  LYS A CE  
1272  N  NZ  . LYS A  165 ? 1.7062 3.3352 3.2354 1.2303  -0.0866 0.3409  165  LYS A NZ  
1273  N  N   . ALA A  166 ? 1.6971 3.1555 3.0522 1.2289  0.0839  0.2819  166  ALA A N   
1274  C  CA  . ALA A  166 ? 2.2219 3.6833 3.5579 1.2777  0.1256  0.2853  166  ALA A CA  
1275  C  C   . ALA A  166 ? 2.0617 3.5635 3.4071 1.2661  0.1554  0.2861  166  ALA A C   
1276  O  O   . ALA A  166 ? 2.1770 3.6468 3.4767 1.3002  0.1905  0.2837  166  ALA A O   
1277  C  CB  . ALA A  166 ? 2.1800 3.5260 3.4287 1.3162  0.1339  0.2765  166  ALA A CB  
1278  N  N   . ASP A  167 ? 1.7545 3.3257 3.1568 1.2188  0.1419  0.2900  167  ASP A N   
1279  C  CA  . ASP A  167 ? 1.6920 3.3170 3.1159 1.2036  0.1675  0.2956  167  ASP A CA  
1280  C  C   . ASP A  167 ? 1.6655 3.2058 3.0162 1.2075  0.1822  0.2869  167  ASP A C   
1281  O  O   . ASP A  167 ? 1.6994 3.2533 3.0322 1.2289  0.2195  0.2919  167  ASP A O   
1282  C  CB  . ASP A  167 ? 1.8607 3.5736 3.3242 1.2372  0.2055  0.3096  167  ASP A CB  
1283  C  CG  . ASP A  167 ? 1.6952 3.5042 3.2390 1.2306  0.1902  0.3214  167  ASP A CG  
1284  O  OD1 . ASP A  167 ? 2.0415 3.8309 3.5936 1.2185  0.1539  0.3179  167  ASP A OD1 
1285  O  OD2 . ASP A  167 ? 1.7077 3.6156 3.3070 1.2363  0.2143  0.3357  167  ASP A OD2 
1286  N  N   . ARG A  168 ? 1.7101 3.1651 3.0182 1.1871  0.1529  0.2749  168  ARG A N   
1287  C  CA  . ARG A  168 ? 1.8741 3.2552 3.1229 1.1798  0.1575  0.2681  168  ARG A CA  
1288  C  C   . ARG A  168 ? 1.6225 3.0139 2.9036 1.1235  0.1271  0.2650  168  ARG A C   
1289  O  O   . ARG A  168 ? 1.5808 2.9821 2.8942 1.0953  0.0940  0.2600  168  ARG A O   
1290  C  CB  . ARG A  168 ? 1.7502 3.0150 2.9157 1.2058  0.1504  0.2570  168  ARG A CB  
1291  C  CG  . ARG A  168 ? 2.1932 3.4295 3.3137 1.2655  0.1829  0.2572  168  ARG A CG  
1292  C  CD  . ARG A  168 ? 2.2244 3.3357 3.2505 1.2895  0.1799  0.2463  168  ARG A CD  
1293  N  NE  . ARG A  168 ? 1.9006 2.9629 2.8730 1.2862  0.1935  0.2430  168  ARG A NE  
1294  C  CZ  . ARG A  168 ? 1.9872 2.9964 2.8889 1.3294  0.2274  0.2394  168  ARG A CZ  
1295  N  NH1 . ARG A  168 ? 2.0630 3.0597 2.9407 1.3792  0.2522  0.2366  168  ARG A NH1 
1296  N  NH2 . ARG A  168 ? 1.9827 2.9493 2.8360 1.3247  0.2365  0.2384  168  ARG A NH2 
1297  N  N   . VAL A  169 ? 1.5231 2.9126 2.7953 1.1093  0.1389  0.2686  169  VAL A N   
1298  C  CA  . VAL A  169 ? 1.4532 2.8434 2.7522 1.0597  0.1118  0.2655  169  VAL A CA  
1299  C  C   . VAL A  169 ? 1.4503 2.7341 2.6849 1.0553  0.0929  0.2538  169  VAL A C   
1300  O  O   . VAL A  169 ? 1.4999 2.7194 2.6672 1.0866  0.1111  0.2539  169  VAL A O   
1301  C  CB  . VAL A  169 ? 1.4354 2.8883 2.7680 1.0450  0.1327  0.2803  169  VAL A CB  
1302  C  CG1 . VAL A  169 ? 1.3754 2.8087 2.7231 1.0004  0.1060  0.2773  169  VAL A CG1 
1303  C  CG2 . VAL A  169 ? 1.4474 3.0139 2.8549 1.0384  0.1443  0.2927  169  VAL A CG2 
1304  N  N   . LEU A  170 ? 1.3963 2.6621 2.6504 1.0171  0.0570  0.2437  170  LEU A N   
1305  C  CA  . LEU A  170 ? 1.3851 2.5616 2.5903 1.0057  0.0363  0.2339  170  LEU A CA  
1306  C  C   . LEU A  170 ? 1.3303 2.5190 2.5670 0.9663  0.0225  0.2340  170  LEU A C   
1307  O  O   . LEU A  170 ? 1.2810 2.5177 2.5763 0.9321  0.0032  0.2292  170  LEU A O   
1308  C  CB  . LEU A  170 ? 1.3740 2.5158 2.5726 0.9968  0.0073  0.2225  170  LEU A CB  
1309  C  CG  . LEU A  170 ? 1.3549 2.4174 2.5152 0.9783  -0.0168 0.2132  170  LEU A CG  
1310  C  CD1 . LEU A  170 ? 1.4077 2.3923 2.4916 1.0084  -0.0018 0.2168  170  LEU A CD1 
1311  C  CD2 . LEU A  170 ? 1.4729 2.5156 2.6314 0.9712  -0.0414 0.2057  170  LEU A CD2 
1312  N  N   . LEU A  171 ? 1.3439 2.4868 2.5404 0.9728  0.0312  0.2400  171  LEU A N   
1313  C  CA  . LEU A  171 ? 1.3012 2.4518 2.5253 0.9407  0.0198  0.2447  171  LEU A CA  
1314  C  C   . LEU A  171 ? 1.2946 2.3580 2.4743 0.9312  -0.0032 0.2372  171  LEU A C   
1315  O  O   . LEU A  171 ? 1.3655 2.3610 2.4772 0.9588  0.0033  0.2378  171  LEU A O   
1316  C  CB  . LEU A  171 ? 1.3230 2.5120 2.5495 0.9552  0.0512  0.2663  171  LEU A CB  
1317  C  CG  . LEU A  171 ? 1.2900 2.4882 2.5434 0.9277  0.0435  0.2800  171  LEU A CG  
1318  C  CD1 . LEU A  171 ? 1.2909 2.5783 2.5913 0.9270  0.0709  0.3029  171  LEU A CD1 
1319  C  CD2 . LEU A  171 ? 1.3200 2.4381 2.5071 0.9442  0.0444  0.2875  171  LEU A CD2 
1320  N  N   . GLY A  172 ? 1.2422 2.3079 2.4607 0.8930  -0.0300 0.2299  172  GLY A N   
1321  C  CA  . GLY A  172 ? 1.2304 2.2253 2.4202 0.8793  -0.0535 0.2237  172  GLY A CA  
1322  C  C   . GLY A  172 ? 1.2180 2.2122 2.4212 0.8659  -0.0549 0.2388  172  GLY A C   
1323  O  O   . GLY A  172 ? 1.1898 2.2438 2.4502 0.8464  -0.0531 0.2458  172  GLY A O   
1324  N  N   . GLY A  173 ? 1.2439 2.1700 2.3938 0.8769  -0.0590 0.2471  173  GLY A N   
1325  C  CA  . GLY A  173 ? 1.2385 2.1533 2.3958 0.8657  -0.0643 0.2665  173  GLY A CA  
1326  C  C   . GLY A  173 ? 1.2307 2.0760 2.3644 0.8509  -0.0938 0.2618  173  GLY A C   
1327  O  O   . GLY A  173 ? 1.4164 2.1990 2.4856 0.8716  -0.0941 0.2694  173  GLY A O   
1328  N  N   . PRO A  174 ? 1.1822 2.0383 2.3662 0.8163  -0.1189 0.2485  174  PRO A N   
1329  C  CA  . PRO A  174 ? 1.1719 1.9713 2.3393 0.8017  -0.1469 0.2391  174  PRO A CA  
1330  C  C   . PRO A  174 ? 1.1926 1.9469 2.3388 0.8004  -0.1561 0.2651  174  PRO A C   
1331  O  O   . PRO A  174 ? 1.1965 1.8997 2.3174 0.7941  -0.1771 0.2623  174  PRO A O   
1332  C  CB  . PRO A  174 ? 1.1216 1.9565 2.3473 0.7708  -0.1647 0.2163  174  PRO A CB  
1333  C  CG  . PRO A  174 ? 1.1083 2.0113 2.3730 0.7711  -0.1486 0.2101  174  PRO A CG  
1334  C  CD  . PRO A  174 ? 1.1402 2.0619 2.3936 0.7921  -0.1220 0.2381  174  PRO A CD  
1335  N  N   . GLY A  175 ? 1.2070 1.9815 2.3661 0.8045  -0.1426 0.2938  175  GLY A N   
1336  C  CA  . GLY A  175 ? 1.2280 1.9597 2.3739 0.7943  -0.1561 0.3215  175  GLY A CA  
1337  C  C   . GLY A  175 ? 1.5414 2.2060 2.5829 0.8050  -0.1445 0.3301  175  GLY A C   
1338  O  O   . GLY A  175 ? 1.5899 2.1996 2.5924 0.7808  -0.1596 0.3439  175  GLY A O   
1339  N  N   . SER A  176 ? 1.7075 2.3764 2.7028 0.8410  -0.1172 0.3227  176  SER A N   
1340  C  CA  . SER A  176 ? 1.6556 2.2578 2.5455 0.8549  -0.1014 0.3267  176  SER A CA  
1341  C  C   . SER A  176 ? 1.7875 2.2967 2.6078 0.8433  -0.1286 0.3243  176  SER A C   
1342  O  O   . SER A  176 ? 1.7292 2.2287 2.5696 0.8432  -0.1500 0.3140  176  SER A O   
1343  C  CB  . SER A  176 ? 1.4567 2.0795 2.3179 0.9021  -0.0683 0.3156  176  SER A CB  
1344  O  OG  . SER A  176 ? 1.4410 2.1466 2.3514 0.9114  -0.0392 0.3227  176  SER A OG  
1345  N  N   . PHE A  177 ? 1.8138 2.2561 2.5487 0.8313  -0.1277 0.3347  177  PHE A N   
1346  C  CA  . PHE A  177 ? 1.8294 2.1773 2.4813 0.8190  -0.1519 0.3342  177  PHE A CA  
1347  C  C   . PHE A  177 ? 1.7294 2.0744 2.4367 0.7864  -0.1928 0.3392  177  PHE A C   
1348  O  O   . PHE A  177 ? 1.7135 2.0302 2.4117 0.7885  -0.2113 0.3297  177  PHE A O   
1349  C  CB  . PHE A  177 ? 1.9630 2.2655 2.5489 0.8547  -0.1413 0.3160  177  PHE A CB  
1350  C  CG  . PHE A  177 ? 2.1354 2.4516 2.6830 0.8964  -0.0985 0.3081  177  PHE A CG  
1351  C  CD1 . PHE A  177 ? 2.3354 2.6450 2.8359 0.8952  -0.0734 0.3167  177  PHE A CD1 
1352  C  CD2 . PHE A  177 ? 2.1658 2.5025 2.7238 0.9377  -0.0831 0.2931  177  PHE A CD2 
1353  C  CE1 . PHE A  177 ? 2.4036 2.7317 2.8726 0.9365  -0.0307 0.3088  177  PHE A CE1 
1354  C  CE2 . PHE A  177 ? 2.2629 2.6161 2.7919 0.9802  -0.0432 0.2869  177  PHE A CE2 
1355  C  CZ  . PHE A  177 ? 2.2763 2.6270 2.7623 0.9807  -0.0156 0.2938  177  PHE A CZ  
1356  N  N   . TYR A  178 ? 1.6478 2.0217 2.4122 0.7561  -0.2064 0.3556  178  TYR A N   
1357  C  CA  . TYR A  178 ? 1.6446 2.0259 2.4762 0.7284  -0.2422 0.3611  178  TYR A CA  
1358  C  C   . TYR A  178 ? 1.4985 1.9298 2.4040 0.7437  -0.2445 0.3418  178  TYR A C   
1359  O  O   . TYR A  178 ? 1.4014 1.8140 2.3157 0.7362  -0.2677 0.3363  178  TYR A O   
1360  C  CB  . TYR A  178 ? 1.7011 2.0043 2.4668 0.7053  -0.2731 0.3711  178  TYR A CB  
1361  C  CG  . TYR A  178 ? 1.7475 2.0376 2.5294 0.6687  -0.2984 0.3965  178  TYR A CG  
1362  C  CD1 . TYR A  178 ? 1.8537 2.1848 2.7365 0.6515  -0.3210 0.4031  178  TYR A CD1 
1363  C  CD2 . TYR A  178 ? 1.8176 2.0522 2.5121 0.6522  -0.3000 0.4140  178  TYR A CD2 
1364  C  CE1 . TYR A  178 ? 2.0723 2.3897 2.9733 0.6207  -0.3459 0.4288  178  TYR A CE1 
1365  C  CE2 . TYR A  178 ? 1.9119 2.1346 2.6205 0.6178  -0.3261 0.4407  178  TYR A CE2 
1366  C  CZ  . TYR A  178 ? 2.0506 2.3148 2.8649 0.6031  -0.3498 0.4492  178  TYR A CZ  
1367  O  OH  . TYR A  178 ? 2.1136 2.3637 2.9444 0.5714  -0.3775 0.4781  178  TYR A OH  
1368  N  N   . TRP A  179 ? 1.3525 1.8506 2.3082 0.7642  -0.2196 0.3320  179  TRP A N   
1369  C  CA  . TRP A  179 ? 1.2760 1.8319 2.3049 0.7770  -0.2194 0.3141  179  TRP A CA  
1370  C  C   . TRP A  179 ? 1.2891 1.8166 2.2724 0.7990  -0.2205 0.2998  179  TRP A C   
1371  O  O   . TRP A  179 ? 1.2473 1.7953 2.2648 0.7911  -0.2307 0.2785  179  TRP A O   
1372  C  CB  . TRP A  179 ? 1.2192 1.7988 2.3285 0.7488  -0.2446 0.3113  179  TRP A CB  
1373  C  CG  . TRP A  179 ? 1.1994 1.8157 2.3679 0.7298  -0.2427 0.3217  179  TRP A CG  
1374  C  CD1 . TRP A  179 ? 1.1668 1.8397 2.3814 0.7234  -0.2287 0.3043  179  TRP A CD1 
1375  C  CD2 . TRP A  179 ? 1.2940 1.8822 2.4645 0.7056  -0.2577 0.3474  179  TRP A CD2 
1376  N  NE1 . TRP A  179 ? 1.1622 1.8501 2.4258 0.7041  -0.2335 0.3254  179  TRP A NE1 
1377  C  CE2 . TRP A  179 ? 1.2448 1.8816 2.4844 0.6938  -0.2518 0.3529  179  TRP A CE2 
1378  C  CE3 . TRP A  179 ? 1.4855 2.0081 2.5977 0.6881  -0.2774 0.3651  179  TRP A CE3 
1379  C  CZ2 . TRP A  179 ? 1.2890 1.9082 2.5407 0.6665  -0.2643 0.3765  179  TRP A CZ2 
1380  C  CZ3 . TRP A  179 ? 1.2958 1.8053 2.4208 0.6616  -0.2905 0.3886  179  TRP A CZ3 
1381  C  CH2 . TRP A  179 ? 1.2678 1.8240 2.4620 0.6517  -0.2837 0.3947  179  TRP A CH2 
1382  N  N   . GLN A  180 ? 1.4969 1.9637 2.3843 0.8152  -0.2101 0.3013  180  GLN A N   
1383  C  CA  . GLN A  180 ? 1.5198 1.9645 2.3648 0.8431  -0.2046 0.2880  180  GLN A CA  
1384  C  C   . GLN A  180 ? 1.5020 2.0136 2.3891 0.8685  -0.1803 0.2747  180  GLN A C   
1385  O  O   . GLN A  180 ? 1.7203 2.2292 2.6042 0.8678  -0.1831 0.2563  180  GLN A O   
1386  C  CB  . GLN A  180 ? 1.7366 2.0935 2.4648 0.8555  -0.1971 0.2901  180  GLN A CB  
1387  C  CG  . GLN A  180 ? 1.7687 2.0473 2.4393 0.8236  -0.2267 0.2990  180  GLN A CG  
1388  C  CD  . GLN A  180 ? 2.0361 2.2202 2.5828 0.8351  -0.2202 0.2975  180  GLN A CD  
1389  O  OE1 . GLN A  180 ? 2.3085 2.4791 2.8126 0.8723  -0.1952 0.2866  180  GLN A OE1 
1390  N  NE2 . GLN A  180 ? 2.0146 2.1310 2.5021 0.8034  -0.2436 0.3085  180  GLN A NE2 
1391  N  N   . GLY A  181 ? 1.3595 1.9227 2.2794 0.8731  -0.1586 0.2797  181  GLY A N   
1392  C  CA  . GLY A  181 ? 1.4179 2.0367 2.3669 0.8803  -0.1363 0.2636  181  GLY A CA  
1393  C  C   . GLY A  181 ? 1.6103 2.2094 2.4934 0.9243  -0.1071 0.2661  181  GLY A C   
1394  O  O   . GLY A  181 ? 1.6513 2.1797 2.4538 0.9513  -0.1064 0.2726  181  GLY A O   
1395  N  N   . GLN A  182 ? 1.4871 2.1478 2.4034 0.9326  -0.0835 0.2596  182  GLN A N   
1396  C  CA  . GLN A  182 ? 1.4408 2.0941 2.3054 0.9759  -0.0518 0.2604  182  GLN A CA  
1397  C  C   . GLN A  182 ? 1.4138 2.1399 2.3326 0.9731  -0.0378 0.2487  182  GLN A C   
1398  O  O   . GLN A  182 ? 1.3572 2.1502 2.3501 0.9439  -0.0431 0.2471  182  GLN A O   
1399  C  CB  . GLN A  182 ? 1.5435 2.1979 2.3759 1.0034  -0.0259 0.2816  182  GLN A CB  
1400  C  CG  . GLN A  182 ? 1.7068 2.3373 2.4696 1.0555  0.0097  0.2796  182  GLN A CG  
1401  C  CD  . GLN A  182 ? 1.7692 2.3846 2.4831 1.0545  0.0354  0.2902  182  GLN A CD  
1402  O  OE1 . GLN A  182 ? 1.8014 2.4530 2.5547 1.0179  0.0315  0.3031  182  GLN A OE1 
1403  N  NE2 . GLN A  182 ? 1.8954 2.4483 2.5156 1.0885  0.0609  0.2827  182  GLN A NE2 
1404  N  N   . LEU A  183 ? 1.4610 2.1694 2.3400 1.0044  -0.0219 0.2415  183  LEU A N   
1405  C  CA  . LEU A  183 ? 1.4547 2.2296 2.3759 1.0108  -0.0059 0.2354  183  LEU A CA  
1406  C  C   . LEU A  183 ? 1.5158 2.3047 2.4039 1.0548  0.0340  0.2440  183  LEU A C   
1407  O  O   . LEU A  183 ? 1.5880 2.3073 2.3961 1.0920  0.0476  0.2443  183  LEU A O   
1408  C  CB  . LEU A  183 ? 1.7450 2.4946 2.6551 1.0125  -0.0204 0.2228  183  LEU A CB  
1409  C  CG  . LEU A  183 ? 1.4025 2.1404 2.3410 0.9731  -0.0559 0.2137  183  LEU A CG  
1410  C  CD1 . LEU A  183 ? 1.5891 2.3129 2.5172 0.9795  -0.0654 0.2065  183  LEU A CD1 
1411  C  CD2 . LEU A  183 ? 1.3312 2.1412 2.3521 0.9347  -0.0664 0.2095  183  LEU A CD2 
1412  N  N   . ILE A  184 ? 1.5911 2.4686 2.5384 1.0514  0.0534  0.2503  184  ILE A N   
1413  C  CA  . ILE A  184 ? 1.6666 2.5760 2.5952 1.0917  0.0953  0.2591  184  ILE A CA  
1414  C  C   . ILE A  184 ? 1.5439 2.5240 2.5230 1.0963  0.1052  0.2544  184  ILE A C   
1415  O  O   . ILE A  184 ? 1.4819 2.5259 2.5349 1.0608  0.0877  0.2530  184  ILE A O   
1416  C  CB  . ILE A  184 ? 1.7576 2.7169 2.7106 1.0862  0.1138  0.2787  184  ILE A CB  
1417  C  CG1 . ILE A  184 ? 1.6999 2.5851 2.5989 1.0861  0.1020  0.2874  184  ILE A CG1 
1418  C  CG2 . ILE A  184 ? 1.8881 2.8940 2.8279 1.1275  0.1618  0.2877  184  ILE A CG2 
1419  C  CD1 . ILE A  184 ? 1.6221 2.5483 2.5355 1.0870  0.1214  0.3128  184  ILE A CD1 
1420  N  N   . SER A  185 ? 1.6945 2.6600 2.6323 1.1415  0.1323  0.2518  185  SER A N   
1421  C  CA  . SER A  185 ? 1.7013 2.7322 2.6840 1.1530  0.1432  0.2506  185  SER A CA  
1422  C  C   . SER A  185 ? 1.9688 3.0364 2.9359 1.1965  0.1906  0.2586  185  SER A C   
1423  O  O   . SER A  185 ? 2.0889 3.0886 2.9768 1.2380  0.2137  0.2549  185  SER A O   
1424  C  CB  . SER A  185 ? 1.8006 2.7756 2.7543 1.1666  0.1251  0.2391  185  SER A CB  
1425  O  OG  . SER A  185 ? 1.9698 3.0123 2.9752 1.1748  0.1298  0.2407  185  SER A OG  
1426  N  N   . ASP A  186 ? 1.9742 3.1482 3.0143 1.1874  0.2061  0.2690  186  ASP A N   
1427  C  CA  . ASP A  186 ? 1.9928 3.2191 3.0304 1.2264  0.2534  0.2777  186  ASP A CA  
1428  C  C   . ASP A  186 ? 1.8872 3.1976 2.9914 1.2312  0.2578  0.2802  186  ASP A C   
1429  O  O   . ASP A  186 ? 1.8896 3.2531 3.0627 1.1930  0.2288  0.2819  186  ASP A O   
1430  C  CB  . ASP A  186 ? 1.8230 3.1095 2.8840 1.2130  0.2764  0.2953  186  ASP A CB  
1431  C  CG  . ASP A  186 ? 1.9137 3.1198 2.8950 1.2286  0.2865  0.2966  186  ASP A CG  
1432  O  OD1 . ASP A  186 ? 2.1470 3.3029 3.0531 1.2778  0.3196  0.2908  186  ASP A OD1 
1433  O  OD2 . ASP A  186 ? 1.7745 2.9638 2.7662 1.1933  0.2607  0.3029  186  ASP A OD2 
1434  N  N   . GLN A  187 ? 1.8772 3.1983 2.9587 1.2804  0.2949  0.2803  187  GLN A N   
1435  C  CA  . GLN A  187 ? 1.8872 3.2949 3.0334 1.2918  0.3039  0.2860  187  GLN A CA  
1436  C  C   . GLN A  187 ? 1.8460 3.3771 3.0720 1.2658  0.3194  0.3042  187  GLN A C   
1437  O  O   . GLN A  187 ? 1.8680 3.4238 3.0810 1.2705  0.3513  0.3140  187  GLN A O   
1438  C  CB  . GLN A  187 ? 2.0210 3.4014 3.1189 1.3547  0.3414  0.2805  187  GLN A CB  
1439  C  CG  . GLN A  187 ? 2.0921 3.3544 3.1173 1.3805  0.3241  0.2645  187  GLN A CG  
1440  C  CD  . GLN A  187 ? 2.3936 3.6134 3.3590 1.4448  0.3637  0.2568  187  GLN A CD  
1441  O  OE1 . GLN A  187 ? 2.5657 3.8382 3.5346 1.4714  0.4080  0.2616  187  GLN A OE1 
1442  N  NE2 . GLN A  187 ? 2.2742 3.3982 3.1840 1.4704  0.3490  0.2447  187  GLN A NE2 
1443  N  N   . VAL A  188 ? 1.7150 3.3238 3.0222 1.2372  0.2962  0.3100  188  VAL A N   
1444  C  CA  . VAL A  188 ? 1.7157 3.4420 3.1031 1.2058  0.3049  0.3281  188  VAL A CA  
1445  C  C   . VAL A  188 ? 1.8193 3.6171 3.2159 1.2422  0.3576  0.3412  188  VAL A C   
1446  O  O   . VAL A  188 ? 1.8460 3.7273 3.2856 1.2211  0.3770  0.3589  188  VAL A O   
1447  C  CB  . VAL A  188 ? 1.6738 3.4641 3.1392 1.1734  0.2697  0.3302  188  VAL A CB  
1448  C  CG1 . VAL A  188 ? 1.5690 3.2885 3.0211 1.1379  0.2211  0.3155  188  VAL A CG1 
1449  C  CG2 . VAL A  188 ? 1.6769 3.4986 3.1613 1.2123  0.2786  0.3309  188  VAL A CG2 
1450  N  N   . ALA A  189 ? 1.8898 3.6578 3.2476 1.2968  0.3823  0.3333  189  ALA A N   
1451  C  CA  . ALA A  189 ? 1.9570 3.7879 3.3178 1.3354  0.4362  0.3428  189  ALA A CA  
1452  C  C   . ALA A  189 ? 1.9834 3.7818 3.2815 1.3450  0.4712  0.3449  189  ALA A C   
1453  O  O   . ALA A  189 ? 2.0321 3.9105 3.3506 1.3525  0.5132  0.3596  189  ALA A O   
1454  C  CB  . ALA A  189 ? 2.0425 3.8395 3.3736 1.3947  0.4539  0.3315  189  ALA A CB  
1455  N  N   . GLU A  190 ? 2.0078 3.6920 3.2291 1.3450  0.4549  0.3316  190  GLU A N   
1456  C  CA  . GLU A  190 ? 2.1047 3.7492 3.2603 1.3540  0.4835  0.3343  190  GLU A CA  
1457  C  C   . GLU A  190 ? 1.9831 3.6792 3.1839 1.2997  0.4694  0.3535  190  GLU A C   
1458  O  O   . GLU A  190 ? 2.1308 3.8511 3.3105 1.3038  0.5042  0.3670  190  GLU A O   
1459  C  CB  . GLU A  190 ? 2.1783 3.6774 3.2320 1.3780  0.4700  0.3134  190  GLU A CB  
1460  C  CG  . GLU A  190 ? 2.2899 3.7304 3.2533 1.4066  0.5074  0.3115  190  GLU A CG  
1461  C  CD  . GLU A  190 ? 2.3152 3.6079 3.1780 1.4273  0.4883  0.2909  190  GLU A CD  
1462  O  OE1 . GLU A  190 ? 2.4495 3.6726 3.2190 1.4636  0.5209  0.2830  190  GLU A OE1 
1463  O  OE2 . GLU A  190 ? 2.1343 3.3794 3.0083 1.4069  0.4414  0.2822  190  GLU A OE2 
1464  N  N   . ILE A  191 ? 1.8748 3.5870 3.1356 1.2495  0.4204  0.3554  191  ILE A N   
1465  C  CA  . ILE A  191 ? 1.8023 3.5532 3.1066 1.1974  0.4028  0.3724  191  ILE A CA  
1466  C  C   . ILE A  191 ? 1.8718 3.7525 3.2427 1.1829  0.4361  0.3987  191  ILE A C   
1467  O  O   . ILE A  191 ? 1.9403 3.8497 3.3120 1.1671  0.4543  0.4186  191  ILE A O   
1468  C  CB  . ILE A  191 ? 1.7239 3.4628 3.0768 1.1496  0.3452  0.3642  191  ILE A CB  
1469  C  CG1 . ILE A  191 ? 1.7886 3.4010 3.0736 1.1590  0.3139  0.3410  191  ILE A CG1 
1470  C  CG2 . ILE A  191 ? 1.6552 3.4423 3.0633 1.0955  0.3276  0.3821  191  ILE A CG2 
1471  C  CD1 . ILE A  191 ? 1.7910 3.3883 3.1161 1.1153  0.2613  0.3301  191  ILE A CD1 
1472  N  N   . VAL A  192 ? 1.9232 3.8878 3.3541 1.1863  0.4435  0.4021  192  VAL A N   
1473  C  CA  . VAL A  192 ? 1.9277 4.0230 3.4287 1.1678  0.4723  0.4284  192  VAL A CA  
1474  C  C   . VAL A  192 ? 1.9158 4.0375 3.3738 1.2136  0.5359  0.4357  192  VAL A C   
1475  O  O   . VAL A  192 ? 1.9128 4.1128 3.3946 1.1966  0.5674  0.4602  192  VAL A O   
1476  C  CB  . VAL A  192 ? 1.8742 4.0518 3.4574 1.1534  0.4541  0.4304  192  VAL A CB  
1477  C  CG1 . VAL A  192 ? 1.8439 3.9814 3.3987 1.2045  0.4582  0.4106  192  VAL A CG1 
1478  C  CG2 . VAL A  192 ? 1.9316 4.2478 3.5867 1.1361  0.4860  0.4585  192  VAL A CG2 
1479  N  N   . SER A  193 ? 1.8529 3.9076 3.2440 1.2711  0.5569  0.4145  193  SER A N   
1480  C  CA  . SER A  193 ? 1.9431 4.0203 3.2898 1.3184  0.6200  0.4165  193  SER A CA  
1481  C  C   . SER A  193 ? 1.9634 3.9941 3.2366 1.3224  0.6471  0.4221  193  SER A C   
1482  O  O   . SER A  193 ? 2.0044 4.1019 3.2720 1.3294  0.6978  0.4383  193  SER A O   
1483  C  CB  . SER A  193 ? 2.0240 4.0300 3.3154 1.3793  0.6324  0.3905  193  SER A CB  
1484  O  OG  . SER A  193 ? 2.0435 3.9082 3.2408 1.3994  0.6155  0.3687  193  SER A OG  
1485  N  N   . LYS A  194 ? 1.9373 3.8579 3.1544 1.3164  0.6143  0.4104  194  LYS A N   
1486  C  CA  . LYS A  194 ? 1.9600 3.8268 3.1025 1.3239  0.6360  0.4158  194  LYS A CA  
1487  C  C   . LYS A  194 ? 1.8787 3.8043 3.0790 1.2662  0.6180  0.4461  194  LYS A C   
1488  O  O   . LYS A  194 ? 1.8904 3.7688 3.0348 1.2613  0.6268  0.4543  194  LYS A O   
1489  C  CB  . LYS A  194 ? 1.9812 3.6960 3.0318 1.3488  0.6090  0.3896  194  LYS A CB  
1490  C  CG  . LYS A  194 ? 2.0800 3.7180 3.0536 1.4095  0.6321  0.3610  194  LYS A CG  
1491  C  CD  . LYS A  194 ? 2.1811 3.8438 3.0986 1.4530  0.7027  0.3606  194  LYS A CD  
1492  C  CE  . LYS A  194 ? 2.3052 3.8805 3.1441 1.5139  0.7234  0.3298  194  LYS A CE  
1493  N  NZ  . LYS A  194 ? 2.2695 3.8772 3.1788 1.5168  0.6973  0.3238  194  LYS A NZ  
1494  N  N   . TYR A  195 ? 1.8066 3.8220 3.1104 1.2171  0.5895  0.4617  195  TYR A N   
1495  C  CA  . TYR A  195 ? 1.7338 3.8053 3.0991 1.1590  0.5701  0.4916  195  TYR A CA  
1496  C  C   . TYR A  195 ? 2.0116 4.1772 3.3838 1.1545  0.6263  0.5232  195  TYR A C   
1497  O  O   . TYR A  195 ? 1.9905 4.2361 3.3784 1.1710  0.6690  0.5275  195  TYR A O   
1498  C  CB  . TYR A  195 ? 1.6620 3.8005 3.1291 1.1087  0.5272  0.4967  195  TYR A CB  
1499  C  CG  . TYR A  195 ? 1.5982 3.8066 3.1373 1.0466  0.5109  0.5297  195  TYR A CG  
1500  C  CD1 . TYR A  195 ? 1.5504 3.6954 3.0808 1.0196  0.4766  0.5360  195  TYR A CD1 
1501  C  CD2 . TYR A  195 ? 1.7704 4.1079 3.3883 1.0136  0.5290  0.5564  195  TYR A CD2 
1502  C  CE1 . TYR A  195 ? 1.5168 3.6883 3.0927 0.9471  0.4529  0.5598  195  TYR A CE1 
1503  C  CE2 . TYR A  195 ? 1.7203 4.1188 3.4047 0.9529  0.5129  0.5888  195  TYR A CE2 
1504  C  CZ  . TYR A  195 ? 1.5733 3.8817 3.2335 0.9188  0.4736  0.5893  195  TYR A CZ  
1505  O  OH  . TYR A  195 ? 1.4819 3.8047 3.1812 0.8430  0.4475  0.6126  195  TYR A OH  
1506  N  N   . ASP A  196 ? 2.1861 4.2732 3.5006 1.0933  0.6058  0.5313  196  ASP A N   
1507  C  CA  . ASP A  196 ? 2.2070 4.3298 3.4921 1.0544  0.6405  0.5552  196  ASP A CA  
1508  C  C   . ASP A  196 ? 2.1523 4.2392 3.4497 0.9689  0.5940  0.5763  196  ASP A C   
1509  O  O   . ASP A  196 ? 2.1284 4.0829 3.3532 0.9468  0.5564  0.5645  196  ASP A O   
1510  C  CB  . ASP A  196 ? 2.1741 4.2004 3.3188 1.0858  0.6806  0.5379  196  ASP A CB  
1511  C  CG  . ASP A  196 ? 2.2321 4.3321 3.3717 1.1600  0.7477  0.5283  196  ASP A CG  
1512  O  OD1 . ASP A  196 ? 2.1081 4.3608 3.3550 1.1714  0.7736  0.5473  196  ASP A OD1 
1513  O  OD2 . ASP A  196 ? 2.3639 4.3688 3.3923 1.2072  0.7744  0.5017  196  ASP A OD2 
1514  N  N   . PRO A  197 ? 2.0482 4.2484 3.4361 0.9192  0.5946  0.6085  197  PRO A N   
1515  C  CA  . PRO A  197 ? 2.0583 4.2204 3.4642 0.8389  0.5471  0.6289  197  PRO A CA  
1516  C  C   . PRO A  197 ? 2.2257 4.2859 3.5208 0.8024  0.5495  0.6380  197  PRO A C   
1517  O  O   . PRO A  197 ? 2.1612 4.1632 3.4576 0.7419  0.5051  0.6521  197  PRO A O   
1518  C  CB  . PRO A  197 ? 1.9576 4.2736 3.4776 0.8000  0.5587  0.6627  197  PRO A CB  
1519  C  CG  . PRO A  197 ? 1.9215 4.3456 3.4471 0.8512  0.6264  0.6666  197  PRO A CG  
1520  C  CD  . PRO A  197 ? 1.9428 4.3115 3.4223 0.9331  0.6379  0.6293  197  PRO A CD  
1521  N  N   . ASN A  198 ? 2.3995 4.4343 3.5977 0.8372  0.5988  0.6303  198  ASN A N   
1522  C  CA  . ASN A  198 ? 2.4979 4.4336 3.5788 0.8046  0.6022  0.6380  198  ASN A CA  
1523  C  C   . ASN A  198 ? 2.6270 4.4099 3.5958 0.8359  0.5835  0.6051  198  ASN A C   
1524  O  O   . ASN A  198 ? 2.7308 4.4199 3.5929 0.8108  0.5814  0.6089  198  ASN A O   
1525  C  CB  . ASN A  198 ? 2.5295 4.5370 3.5657 0.8138  0.6714  0.6528  198  ASN A CB  
1526  C  CG  . ASN A  198 ? 2.5590 4.6067 3.5768 0.8985  0.7265  0.6252  198  ASN A CG  
1527  O  OD1 . ASN A  198 ? 2.4419 4.5319 3.5330 0.9441  0.7193  0.6084  198  ASN A OD1 
1528  N  ND2 . ASN A  198 ? 2.7153 4.7493 3.6337 0.9204  0.7821  0.6207  198  ASN A ND2 
1529  N  N   . VAL A  199 ? 2.5819 4.3386 3.5711 0.8870  0.5680  0.5748  199  VAL A N   
1530  C  CA  . VAL A  199 ? 2.5274 4.1420 3.4189 0.9156  0.5463  0.5437  199  VAL A CA  
1531  C  C   . VAL A  199 ? 2.2834 3.8482 3.2299 0.8918  0.4796  0.5378  199  VAL A C   
1532  O  O   . VAL A  199 ? 2.0726 3.7062 3.1197 0.9068  0.4651  0.5333  199  VAL A O   
1533  C  CB  . VAL A  199 ? 2.5531 4.1671 3.4104 0.9979  0.5861  0.5127  199  VAL A CB  
1534  C  CG1 . VAL A  199 ? 2.6398 4.0988 3.3889 1.0208  0.5614  0.4822  199  VAL A CG1 
1535  C  CG2 . VAL A  199 ? 2.6058 4.2803 3.4174 1.0246  0.6572  0.5175  199  VAL A CG2 
1536  N  N   . TYR A  200 ? 2.2831 3.7313 3.1636 0.8543  0.4392  0.5382  200  TYR A N   
1537  C  CA  . TYR A  200 ? 2.3545 3.7548 3.2854 0.8279  0.3775  0.5341  200  TYR A CA  
1538  C  C   . TYR A  200 ? 2.2980 3.6057 3.1819 0.8698  0.3564  0.5008  200  TYR A C   
1539  O  O   . TYR A  200 ? 2.3073 3.5974 3.2475 0.8622  0.3129  0.4922  200  TYR A O   
1540  C  CB  . TYR A  200 ? 2.5153 3.8476 3.4161 0.7618  0.3405  0.5571  200  TYR A CB  
1541  C  CG  . TYR A  200 ? 2.5730 3.9753 3.4951 0.7151  0.3610  0.5933  200  TYR A CG  
1542  C  CD1 . TYR A  200 ? 2.4509 3.9839 3.4776 0.7083  0.3807  0.6089  200  TYR A CD1 
1543  C  CD2 . TYR A  200 ? 2.7029 4.0414 3.5395 0.6746  0.3586  0.6141  200  TYR A CD2 
1544  C  CE1 . TYR A  200 ? 2.4832 4.0808 3.5290 0.6617  0.3989  0.6443  200  TYR A CE1 
1545  C  CE2 . TYR A  200 ? 2.7750 4.1756 3.6274 0.6290  0.3766  0.6499  200  TYR A CE2 
1546  C  CZ  . TYR A  200 ? 2.6980 4.2278 3.6555 0.6223  0.3973  0.6649  200  TYR A CZ  
1547  O  OH  . TYR A  200 ? 2.8061 4.3984 3.7791 0.5732  0.4148  0.7027  200  TYR A OH  
1548  N  N   . SER A  201 ? 2.3285 3.5760 3.1093 0.9128  0.3869  0.4815  201  SER A N   
1549  C  CA  . SER A  201 ? 2.3725 3.5264 3.0988 0.9526  0.3695  0.4508  201  SER A CA  
1550  C  C   . SER A  201 ? 2.4261 3.6092 3.1249 1.0229  0.4207  0.4310  201  SER A C   
1551  O  O   . SER A  201 ? 2.4497 3.5802 3.0431 1.0452  0.4559  0.4213  201  SER A O   
1552  C  CB  . SER A  201 ? 2.5349 3.5531 3.1433 0.9279  0.3456  0.4465  201  SER A CB  
1553  O  OG  . SER A  201 ? 2.6389 3.6325 3.2825 0.8680  0.2959  0.4656  201  SER A OG  
1554  N  N   . ILE A  202 ? 2.4563 3.7218 3.2485 1.0584  0.4243  0.4249  202  ILE A N   
1555  C  CA  . ILE A  202 ? 2.4806 3.7849 3.2649 1.1294  0.4706  0.4089  202  ILE A CA  
1556  C  C   . ILE A  202 ? 2.4104 3.6098 3.1369 1.1711  0.4505  0.3797  202  ILE A C   
1557  O  O   . ILE A  202 ? 2.2979 3.4774 3.0706 1.1602  0.4045  0.3750  202  ILE A O   
1558  C  CB  . ILE A  202 ? 2.3315 3.7892 3.2509 1.1457  0.4846  0.4221  202  ILE A CB  
1559  C  CG1 . ILE A  202 ? 2.2832 3.8435 3.2626 1.0959  0.4998  0.4537  202  ILE A CG1 
1560  C  CG2 . ILE A  202 ? 2.3056 3.8077 3.2209 1.2232  0.5335  0.4082  202  ILE A CG2 
1561  C  CD1 . ILE A  202 ? 2.2064 3.9219 3.3210 1.1032  0.5099  0.4695  202  ILE A CD1 
1562  N  N   . LYS A  203 ? 2.4732 3.6025 3.0949 1.2175  0.4855  0.3599  203  LYS A N   
1563  C  CA  . LYS A  203 ? 2.4851 3.5085 3.0411 1.2602  0.4715  0.3324  203  LYS A CA  
1564  C  C   . LYS A  203 ? 2.3427 3.4362 2.9531 1.3319  0.5019  0.3232  203  LYS A C   
1565  O  O   . LYS A  203 ? 2.2608 3.4215 2.8740 1.3705  0.5563  0.3244  203  LYS A O   
1566  C  CB  . LYS A  203 ? 2.7110 3.6017 3.1117 1.2674  0.4882  0.3145  203  LYS A CB  
1567  C  CG  . LYS A  203 ? 2.7115 3.4686 3.0341 1.2888  0.4582  0.2895  203  LYS A CG  
1568  C  CD  . LYS A  203 ? 2.4366 3.1751 2.8164 1.2447  0.3940  0.2970  203  LYS A CD  
1569  C  CE  . LYS A  203 ? 2.4662 3.0850 2.7792 1.2654  0.3644  0.2750  203  LYS A CE  
1570  N  NZ  . LYS A  203 ? 2.3476 2.9601 2.7229 1.2256  0.3060  0.2818  203  LYS A NZ  
1571  N  N   . TYR A  204 ? 2.3865 3.4665 3.0407 1.3499  0.4669  0.3152  204  TYR A N   
1572  C  CA  . TYR A  204 ? 2.4259 3.5574 3.1297 1.4050  0.4817  0.3068  204  TYR A CA  
1573  C  C   . TYR A  204 ? 2.6646 3.6609 3.2640 1.4469  0.4785  0.2788  204  TYR A C   
1574  O  O   . TYR A  204 ? 2.7974 3.6927 3.3454 1.4381  0.4420  0.2715  204  TYR A O   
1575  C  CB  . TYR A  204 ? 2.2837 3.4718 3.0922 1.3521  0.4312  0.3117  204  TYR A CB  
1576  C  CG  . TYR A  204 ? 2.0127 3.3178 2.9200 1.3047  0.4263  0.3381  204  TYR A CG  
1577  C  CD1 . TYR A  204 ? 1.9265 3.3517 2.9025 1.3023  0.4572  0.3511  204  TYR A CD1 
1578  C  CD2 . TYR A  204 ? 1.8936 3.1878 2.8265 1.2616  0.3898  0.3514  204  TYR A CD2 
1579  C  CE1 . TYR A  204 ? 1.8554 3.3845 2.9196 1.2566  0.4520  0.3764  204  TYR A CE1 
1580  C  CE2 . TYR A  204 ? 1.8193 3.2152 2.8424 1.2174  0.3844  0.3763  204  TYR A CE2 
1581  C  CZ  . TYR A  204 ? 1.7920 3.3041 2.8788 1.2143  0.4157  0.3888  204  TYR A CZ  
1582  O  OH  . TYR A  204 ? 1.7260 3.3375 2.9011 1.1681  0.4098  0.4148  204  TYR A OH  
1583  N  N   . ASN A  205 ? 2.7576 3.7516 3.3266 1.4916  0.5161  0.2643  205  ASN A N   
1584  C  CA  . ASN A  205 ? 2.7450 3.6057 3.2070 1.5356  0.5192  0.2379  205  ASN A CA  
1585  C  C   . ASN A  205 ? 2.5614 3.3785 3.0493 1.5177  0.4672  0.2293  205  ASN A C   
1586  O  O   . ASN A  205 ? 2.5690 3.2624 2.9766 1.5270  0.4438  0.2149  205  ASN A O   
1587  C  CB  . ASN A  205 ? 2.8474 3.7193 3.2716 1.5895  0.5767  0.2251  205  ASN A CB  
1588  C  CG  . ASN A  205 ? 2.8045 3.7169 3.1912 1.6077  0.6345  0.2313  205  ASN A CG  
1589  O  OD1 . ASN A  205 ? 2.6326 3.6686 3.0895 1.6052  0.6677  0.2453  205  ASN A OD1 
1590  N  ND2 . ASN A  205 ? 2.9184 3.7190 3.1868 1.6112  0.6417  0.2202  205  ASN A ND2 
1591  N  N   . ASN A  206 ? 2.2260 3.1411 2.8214 1.4911  0.4488  0.2385  206  ASN A N   
1592  C  CA  . ASN A  206 ? 2.1902 3.0752 2.8137 1.4736  0.4032  0.2319  206  ASN A CA  
1593  C  C   . ASN A  206 ? 2.1541 3.0380 2.8186 1.4153  0.3514  0.2392  206  ASN A C   
1594  O  O   . ASN A  206 ? 2.1549 3.0592 2.8755 1.3875  0.3154  0.2387  206  ASN A O   
1595  C  CB  . ASN A  206 ? 2.1741 3.1581 2.8855 1.4772  0.4088  0.2371  206  ASN A CB  
1596  C  CG  . ASN A  206 ? 2.2832 3.2686 2.9599 1.5366  0.4586  0.2292  206  ASN A CG  
1597  O  OD1 . ASN A  206 ? 2.4095 3.2872 2.9859 1.5786  0.4760  0.2123  206  ASN A OD1 
1598  N  ND2 . ASN A  206 ? 2.2710 3.3766 3.0285 1.5402  0.4822  0.2407  206  ASN A ND2 
1599  N  N   . GLN A  207 ? 2.3612 3.2213 2.9980 1.3981  0.3479  0.2461  207  GLN A N   
1600  C  CA  . GLN A  207 ? 2.1515 3.0077 2.8263 1.3443  0.3002  0.2528  207  GLN A CA  
1601  C  C   . GLN A  207 ? 2.0603 2.7994 2.6725 1.3425  0.2639  0.2389  207  GLN A C   
1602  O  O   . GLN A  207 ? 2.2662 2.9005 2.7767 1.3788  0.2752  0.2286  207  GLN A O   
1603  C  CB  . GLN A  207 ? 2.0509 2.9173 2.7155 1.3320  0.3088  0.2682  207  GLN A CB  
1604  C  CG  . GLN A  207 ? 1.9564 2.8345 2.6744 1.2751  0.2626  0.2784  207  GLN A CG  
1605  C  CD  . GLN A  207 ? 2.0143 2.9118 2.7305 1.2632  0.2725  0.2988  207  GLN A CD  
1606  O  OE1 . GLN A  207 ? 2.0767 3.0023 2.7689 1.2703  0.3123  0.3043  207  GLN A OE1 
1607  N  NE2 . GLN A  207 ? 1.9621 2.8207 2.6859 1.2085  0.2287  0.3024  207  GLN A NE2 
1608  N  N   . LEU A  208 ? 1.9098 2.6649 2.5793 1.3000  0.2213  0.2381  208  LEU A N   
1609  C  CA  . LEU A  208 ? 1.9623 2.6225 2.5870 1.2879  0.1837  0.2289  208  LEU A CA  
1610  C  C   . LEU A  208 ? 2.0288 2.6897 2.6816 1.2391  0.1497  0.2360  208  LEU A C   
1611  O  O   . LEU A  208 ? 2.1429 2.8882 2.8837 1.1989  0.1358  0.2423  208  LEU A O   
1612  C  CB  . LEU A  208 ? 2.0221 2.6998 2.6879 1.2798  0.1634  0.2228  208  LEU A CB  
1613  C  CG  . LEU A  208 ? 1.9744 2.6452 2.6159 1.3294  0.1916  0.2172  208  LEU A CG  
1614  C  CD1 . LEU A  208 ? 1.9496 2.6391 2.6360 1.3187  0.1658  0.2159  208  LEU A CD1 
1615  C  CD2 . LEU A  208 ? 2.0870 2.6368 2.6117 1.3755  0.2086  0.2067  208  LEU A CD2 
1616  N  N   . ALA A  209 ? 2.0503 2.6142 2.6278 1.2426  0.1347  0.2348  209  ALA A N   
1617  C  CA  . ALA A  209 ? 1.9815 2.5452 2.5850 1.1999  0.1035  0.2439  209  ALA A CA  
1618  C  C   . ALA A  209 ? 1.9040 2.3594 2.4395 1.1941  0.0707  0.2389  209  ALA A C   
1619  O  O   . ALA A  209 ? 2.0317 2.3915 2.4703 1.2318  0.0795  0.2322  209  ALA A O   
1620  C  CB  . ALA A  209 ? 1.9486 2.5347 2.5440 1.2083  0.1249  0.2601  209  ALA A CB  
1621  N  N   . THR A  210 ? 1.7863 2.2553 2.3718 1.1465  0.0330  0.2415  210  THR A N   
1622  C  CA  . THR A  210 ? 1.8279 2.2088 2.3621 1.1332  -0.0010 0.2409  210  THR A CA  
1623  C  C   . THR A  210 ? 2.1075 2.4333 2.5855 1.1221  -0.0054 0.2505  210  THR A C   
1624  O  O   . THR A  210 ? 2.1458 2.5188 2.6771 1.0829  -0.0149 0.2604  210  THR A O   
1625  C  CB  . THR A  210 ? 1.7770 2.1984 2.3877 1.0819  -0.0359 0.2383  210  THR A CB  
1626  O  OG1 . THR A  210 ? 1.6467 2.1523 2.3417 1.0502  -0.0370 0.2448  210  THR A OG1 
1627  C  CG2 . THR A  210 ? 1.9064 2.3556 2.5480 1.0802  -0.0371 0.2269  210  THR A CG2 
1628  N  N   . ARG A  211 ? 2.2657 2.4806 2.6285 1.1326  -0.0010 0.2426  211  ARG A N   
1629  C  CA  . ARG A  211 ? 2.3732 2.5190 2.6614 1.0975  -0.0066 0.2456  211  ARG A CA  
1630  C  C   . ARG A  211 ? 2.4884 2.5998 2.7844 1.0434  -0.0535 0.2527  211  ARG A C   
1631  O  O   . ARG A  211 ? 2.4879 2.6096 2.8260 1.0366  -0.0792 0.2516  211  ARG A O   
1632  C  CB  . ARG A  211 ? 2.5619 2.5974 2.7196 1.1273  0.0135  0.2322  211  ARG A CB  
1633  C  CG  . ARG A  211 ? 2.7875 2.8673 2.9441 1.1817  0.0650  0.2260  211  ARG A CG  
1634  C  CD  . ARG A  211 ? 2.9490 2.9188 2.9776 1.2203  0.0899  0.2085  211  ARG A CD  
1635  N  NE  . ARG A  211 ? 2.6738 2.6984 2.7112 1.2728  0.1425  0.2033  211  ARG A NE  
1636  C  CZ  . ARG A  211 ? 2.4639 2.5343 2.5447 1.3298  0.1642  0.1988  211  ARG A CZ  
1637  N  NH1 . ARG A  211 ? 2.3854 2.4496 2.4999 1.3409  0.1371  0.1989  211  ARG A NH1 
1638  N  NH2 . ARG A  211 ? 2.4797 2.6064 2.5717 1.3755  0.2132  0.1957  211  ARG A NH2 
1639  N  N   . THR A  212 ? 2.5334 2.6071 2.7888 1.0045  -0.0642 0.2612  212  THR A N   
1640  C  CA  . THR A  212 ? 2.5002 2.5522 2.7720 0.9526  -0.1076 0.2715  212  THR A CA  
1641  C  C   . THR A  212 ? 2.5389 2.4949 2.7387 0.9444  -0.1360 0.2651  212  THR A C   
1642  O  O   . THR A  212 ? 2.7647 2.6322 2.8604 0.9658  -0.1254 0.2543  212  THR A O   
1643  C  CB  . THR A  212 ? 2.6071 2.6378 2.8447 0.9156  -0.1123 0.2851  212  THR A CB  
1644  O  OG1 . THR A  212 ? 2.5868 2.5864 2.8308 0.8682  -0.1563 0.2963  212  THR A OG1 
1645  C  CG2 . THR A  212 ? 2.8066 2.7482 2.9136 0.9301  -0.0898 0.2775  212  THR A CG2 
1646  N  N   . ALA A  213 ? 2.4045 2.3789 2.6610 0.9134  -0.1715 0.2714  213  ALA A N   
1647  C  CA  . ALA A  213 ? 2.5442 2.4431 2.7493 0.8974  -0.2023 0.2693  213  ALA A CA  
1648  C  C   . ALA A  213 ? 2.5391 2.4116 2.7404 0.8425  -0.2401 0.2840  213  ALA A C   
1649  O  O   . ALA A  213 ? 2.5944 2.4854 2.8089 0.8200  -0.2416 0.2954  213  ALA A O   
1650  C  CB  . ALA A  213 ? 2.5013 2.4508 2.7769 0.9121  -0.2093 0.2644  213  ALA A CB  
1651  N  N   . GLN A  214 ? 2.3984 2.2278 2.5811 0.8205  -0.2717 0.2859  214  GLN A N   
1652  C  CA  . GLN A  214 ? 2.4169 2.2228 2.5975 0.7695  -0.3101 0.3014  214  GLN A CA  
1653  C  C   . GLN A  214 ? 2.3367 2.2413 2.6419 0.7488  -0.3212 0.3127  214  GLN A C   
1654  O  O   . GLN A  214 ? 2.3490 2.3374 2.7448 0.7692  -0.3051 0.3064  214  GLN A O   
1655  C  CB  . GLN A  214 ? 2.4063 2.1571 2.5502 0.7507  -0.3398 0.3020  214  GLN A CB  
1656  C  CG  . GLN A  214 ? 2.5658 2.2007 2.5774 0.7636  -0.3361 0.2922  214  GLN A CG  
1657  C  CD  . GLN A  214 ? 2.5451 2.1806 2.5511 0.8132  -0.3094 0.2763  214  GLN A CD  
1658  O  OE1 . GLN A  214 ? 2.4815 2.2027 2.5672 0.8446  -0.2842 0.2712  214  GLN A OE1 
1659  N  NE2 . GLN A  214 ? 2.7159 2.2539 2.6273 0.8194  -0.3169 0.2697  214  GLN A NE2 
1660  N  N   . ALA A  215 ? 2.3311 2.2212 2.6378 0.7071  -0.3510 0.3301  215  ALA A N   
1661  C  CA  . ALA A  215 ? 2.2282 2.1982 2.6453 0.6868  -0.3638 0.3427  215  ALA A CA  
1662  C  C   . ALA A  215 ? 2.1593 2.1960 2.6754 0.6857  -0.3744 0.3378  215  ALA A C   
1663  O  O   . ALA A  215 ? 2.0813 2.1932 2.6987 0.6812  -0.3752 0.3409  215  ALA A O   
1664  C  CB  . ALA A  215 ? 2.2280 2.1602 2.6184 0.6434  -0.3973 0.3649  215  ALA A CB  
1665  N  N   . ILE A  216 ? 2.2000 2.2087 2.6868 0.6881  -0.3828 0.3303  216  ILE A N   
1666  C  CA  . ILE A  216 ? 1.9964 2.0699 2.5713 0.6854  -0.3909 0.3255  216  ILE A CA  
1667  C  C   . ILE A  216 ? 1.8916 2.0422 2.5393 0.7187  -0.3619 0.3100  216  ILE A C   
1668  O  O   . ILE A  216 ? 1.7019 1.9228 2.4405 0.7150  -0.3653 0.3052  216  ILE A O   
1669  C  CB  . ILE A  216 ? 2.0020 2.0260 2.5215 0.6784  -0.4056 0.3232  216  ILE A CB  
1670  C  CG1 . ILE A  216 ? 1.9700 2.0630 2.5792 0.6664  -0.4174 0.3218  216  ILE A CG1 
1671  C  CG2 . ILE A  216 ? 2.1204 2.1034 2.5713 0.7158  -0.3812 0.3087  216  ILE A CG2 
1672  C  CD1 . ILE A  216 ? 2.0853 2.1389 2.6461 0.6582  -0.4300 0.3212  216  ILE A CD1 
1673  N  N   . PHE A  217 ? 2.1045 2.2458 2.7147 0.7507  -0.3332 0.3019  217  PHE A N   
1674  C  CA  . PHE A  217 ? 2.0642 2.2791 2.7381 0.7818  -0.3068 0.2892  217  PHE A CA  
1675  C  C   . PHE A  217 ? 1.9558 2.2347 2.7034 0.7791  -0.2956 0.2927  217  PHE A C   
1676  O  O   . PHE A  217 ? 1.8573 2.2009 2.6602 0.8009  -0.2748 0.2835  217  PHE A O   
1677  C  CB  . PHE A  217 ? 1.9240 2.1038 2.5272 0.8209  -0.2810 0.2802  217  PHE A CB  
1678  C  CG  . PHE A  217 ? 1.9861 2.1035 2.5219 0.8277  -0.2908 0.2761  217  PHE A CG  
1679  C  CD1 . PHE A  217 ? 2.2278 2.3856 2.8074 0.8350  -0.2948 0.2697  217  PHE A CD1 
1680  C  CD2 . PHE A  217 ? 2.1139 2.1283 2.5379 0.8242  -0.2972 0.2790  217  PHE A CD2 
1681  C  CE1 . PHE A  217 ? 2.3794 2.4771 2.8952 0.8387  -0.3053 0.2688  217  PHE A CE1 
1682  C  CE2 . PHE A  217 ? 2.2849 2.2345 2.6441 0.8281  -0.3081 0.2763  217  PHE A CE2 
1683  C  CZ  . PHE A  217 ? 2.4308 2.4226 2.8372 0.8353  -0.3124 0.2725  217  PHE A CZ  
1684  N  N   . ASP A  218 ? 2.1251 2.3873 2.8742 0.7513  -0.3105 0.3075  218  ASP A N   
1685  C  CA  . ASP A  218 ? 1.9639 2.2840 2.7878 0.7443  -0.3041 0.3134  218  ASP A CA  
1686  C  C   . ASP A  218 ? 1.7487 2.1453 2.6819 0.7415  -0.3090 0.3038  218  ASP A C   
1687  O  O   . ASP A  218 ? 1.8666 2.2693 2.8204 0.7353  -0.3236 0.2972  218  ASP A O   
1688  C  CB  . ASP A  218 ? 1.8787 2.1645 2.6884 0.7117  -0.3260 0.3343  218  ASP A CB  
1689  C  CG  . ASP A  218 ? 1.9009 2.1128 2.5994 0.7110  -0.3196 0.3431  218  ASP A CG  
1690  O  OD1 . ASP A  218 ? 2.0291 2.2178 2.6655 0.7396  -0.2942 0.3316  218  ASP A OD1 
1691  O  OD2 . ASP A  218 ? 1.8154 1.9921 2.4880 0.6822  -0.3401 0.3619  218  ASP A OD2 
1692  N  N   . ASP A  219 ? 1.3144 1.7692 2.3152 0.7449  -0.2955 0.3025  219  ASP A N   
1693  C  CA  . ASP A  219 ? 1.2279 1.7374 2.2867 0.7265  -0.2934 0.2757  219  ASP A CA  
1694  C  C   . ASP A  219 ? 1.1869 1.7191 2.2332 0.7384  -0.2831 0.2472  219  ASP A C   
1695  O  O   . ASP A  219 ? 1.1607 1.7103 2.2201 0.7242  -0.2883 0.2331  219  ASP A O   
1696  C  CB  . ASP A  219 ? 1.4522 1.9539 2.5388 0.6952  -0.3160 0.2807  219  ASP A CB  
1697  C  CG  . ASP A  219 ? 1.8204 2.3718 2.9576 0.6775  -0.3073 0.2568  219  ASP A CG  
1698  O  OD1 . ASP A  219 ? 1.3330 1.9174 2.4978 0.6789  -0.2926 0.2489  219  ASP A OD1 
1699  O  OD2 . ASP A  219 ? 2.2192 2.7765 3.3701 0.6622  -0.3152 0.2481  219  ASP A OD2 
1700  N  N   . SER A  220 ? 1.2038 1.7373 2.2278 0.7635  -0.2669 0.2417  220  SER A N   
1701  C  CA  . SER A  220 ? 1.4897 2.0375 2.5098 0.7711  -0.2614 0.2182  220  SER A CA  
1702  C  C   . SER A  220 ? 1.5422 2.1456 2.6029 0.7701  -0.2444 0.1980  220  SER A C   
1703  O  O   . SER A  220 ? 1.4489 2.0767 2.5281 0.7647  -0.2449 0.1772  220  SER A O   
1704  C  CB  . SER A  220 ? 1.6553 2.1523 2.6119 0.7966  -0.2537 0.2339  220  SER A CB  
1705  O  OG  . SER A  220 ? 1.7806 2.2265 2.6974 0.7959  -0.2743 0.2493  220  SER A OG  
1706  N  N   . TYR A  221 ? 1.3407 1.9660 2.4175 0.7742  -0.2298 0.2081  221  TYR A N   
1707  C  CA  . TYR A  221 ? 1.1413 1.8253 2.2605 0.7711  -0.2152 0.1935  221  TYR A CA  
1708  C  C   . TYR A  221 ? 1.1550 1.8473 2.2601 0.7874  -0.1993 0.1886  221  TYR A C   
1709  O  O   . TYR A  221 ? 1.1273 1.8598 2.2670 0.7781  -0.1986 0.1702  221  TYR A O   
1710  C  CB  . TYR A  221 ? 1.0974 1.8236 2.2555 0.7498  -0.2253 0.1689  221  TYR A CB  
1711  C  CG  . TYR A  221 ? 1.0862 1.8158 2.2648 0.7315  -0.2300 0.1819  221  TYR A CG  
1712  C  CD1 . TYR A  221 ? 1.1107 1.8037 2.2821 0.7306  -0.2343 0.2105  221  TYR A CD1 
1713  C  CD2 . TYR A  221 ? 1.0550 1.8195 2.2677 0.7118  -0.2299 0.1699  221  TYR A CD2 
1714  C  CE1 . TYR A  221 ? 1.5030 2.1916 2.7075 0.7077  -0.2437 0.2238  221  TYR A CE1 
1715  C  CE2 . TYR A  221 ? 1.0490 1.8046 2.2955 0.6898  -0.2362 0.1822  221  TYR A CE2 
1716  C  CZ  . TYR A  221 ? 1.0722 1.7894 2.3161 0.6871  -0.2450 0.2080  221  TYR A CZ  
1717  O  OH  . TYR A  221 ? 1.0703 1.7750 2.3516 0.6647  -0.2560 0.2199  221  TYR A OH  
1718  N  N   . LEU A  222 ? 1.2052 1.8568 2.2509 0.8144  -0.1867 0.2056  222  LEU A N   
1719  C  CA  . LEU A  222 ? 1.5088 2.1696 2.5310 0.8374  -0.1672 0.2032  222  LEU A CA  
1720  C  C   . LEU A  222 ? 1.4501 2.1727 2.5089 0.8424  -0.1462 0.2034  222  LEU A C   
1721  O  O   . LEU A  222 ? 1.3685 2.1007 2.4268 0.8500  -0.1341 0.2180  222  LEU A O   
1722  C  CB  . LEU A  222 ? 1.5936 2.1907 2.5323 0.8719  -0.1573 0.2172  222  LEU A CB  
1723  C  CG  . LEU A  222 ? 1.3422 1.9465 2.2509 0.9045  -0.1321 0.2159  222  LEU A CG  
1724  C  CD1 . LEU A  222 ? 1.3255 1.9474 2.2518 0.8984  -0.1384 0.2037  222  LEU A CD1 
1725  C  CD2 . LEU A  222 ? 1.4234 1.9557 2.2415 0.9438  -0.1202 0.2265  222  LEU A CD2 
1726  N  N   . GLY A  223 ? 1.4146 2.1815 2.5045 0.8391  -0.1416 0.1911  223  GLY A N   
1727  C  CA  . GLY A  223 ? 1.1929 2.0274 2.3260 0.8398  -0.1252 0.1913  223  GLY A CA  
1728  C  C   . GLY A  223 ? 1.1391 2.0249 2.3411 0.8073  -0.1393 0.1775  223  GLY A C   
1729  O  O   . GLY A  223 ? 1.1284 2.0731 2.3705 0.8040  -0.1282 0.1804  223  GLY A O   
1730  N  N   . TYR A  224 ? 1.4113 2.2778 2.6262 0.7852  -0.1626 0.1624  224  TYR A N   
1731  C  CA  . TYR A  224 ? 1.4336 2.3435 2.7037 0.7595  -0.1761 0.1439  224  TYR A CA  
1732  C  C   . TYR A  224 ? 1.0531 2.0199 2.3607 0.7553  -0.1722 0.1349  224  TYR A C   
1733  O  O   . TYR A  224 ? 1.0318 2.0526 2.3850 0.7422  -0.1731 0.1283  224  TYR A O   
1734  C  CB  . TYR A  224 ? 1.0475 1.9269 2.3118 0.7452  -0.1985 0.1260  224  TYR A CB  
1735  C  CG  . TYR A  224 ? 1.0192 1.9374 2.3070 0.7280  -0.2070 0.1080  224  TYR A CG  
1736  C  CD1 . TYR A  224 ? 1.0181 1.9324 2.3041 0.7241  -0.2062 0.1219  224  TYR A CD1 
1737  C  CD2 . TYR A  224 ? 1.0008 1.9583 2.3051 0.7146  -0.2096 0.0884  224  TYR A CD2 
1738  C  CE1 . TYR A  224 ? 0.9971 1.9428 2.3101 0.7063  -0.2050 0.1227  224  TYR A CE1 
1739  C  CE2 . TYR A  224 ? 0.9818 1.9841 2.2939 0.7050  -0.2052 0.0888  224  TYR A CE2 
1740  C  CZ  . TYR A  224 ? 0.9770 1.9699 2.3068 0.7000  -0.2034 0.1075  224  TYR A CZ  
1741  O  OH  . TYR A  224 ? 0.9609 1.9716 2.3320 0.6770  -0.2017 0.1116  224  TYR A OH  
1742  N  N   . SER A  225 ? 1.0691 2.0265 2.3556 0.7671  -0.1685 0.1376  225  SER A N   
1743  C  CA  . SER A  225 ? 1.0647 2.0753 2.3802 0.7672  -0.1650 0.1352  225  SER A CA  
1744  C  C   . SER A  225 ? 1.1072 2.1024 2.3792 0.7970  -0.1504 0.1496  225  SER A C   
1745  O  O   . SER A  225 ? 1.1362 2.0724 2.3542 0.8135  -0.1480 0.1567  225  SER A O   
1746  C  CB  . SER A  225 ? 1.0362 2.0588 2.3783 0.7472  -0.1828 0.1201  225  SER A CB  
1747  O  OG  . SER A  225 ? 1.0520 2.0241 2.3534 0.7526  -0.1887 0.1236  225  SER A OG  
1748  N  N   . VAL A  226 ? 1.1153 2.1650 2.4108 0.8057  -0.1415 0.1537  226  VAL A N   
1749  C  CA  . VAL A  226 ? 1.1610 2.2032 2.4204 0.8383  -0.1268 0.1658  226  VAL A CA  
1750  C  C   . VAL A  226 ? 1.1593 2.2521 2.4476 0.8386  -0.1331 0.1656  226  VAL A C   
1751  O  O   . VAL A  226 ? 1.1471 2.2933 2.4876 0.8149  -0.1442 0.1582  226  VAL A O   
1752  C  CB  . VAL A  226 ? 1.1907 2.2507 2.4427 0.8611  -0.1005 0.1784  226  VAL A CB  
1753  C  CG1 . VAL A  226 ? 1.2061 2.2071 2.4145 0.8683  -0.0940 0.1834  226  VAL A CG1 
1754  C  CG2 . VAL A  226 ? 1.3082 2.4467 2.6241 0.8437  -0.0961 0.1791  226  VAL A CG2 
1755  N  N   . ALA A  227 ? 1.2014 2.2751 2.4534 0.8674  -0.1274 0.1746  227  ALA A N   
1756  C  CA  . ALA A  227 ? 1.2120 2.3313 2.4851 0.8756  -0.1329 0.1794  227  ALA A CA  
1757  C  C   . ALA A  227 ? 1.2723 2.3632 2.5009 0.9172  -0.1180 0.1916  227  ALA A C   
1758  O  O   . ALA A  227 ? 1.3037 2.3287 2.4778 0.9357  -0.1086 0.1937  227  ALA A O   
1759  C  CB  . ALA A  227 ? 1.1891 2.3042 2.4664 0.8563  -0.1574 0.1736  227  ALA A CB  
1760  N  N   . VAL A  228 ? 1.2929 2.4333 2.5450 0.9333  -0.1165 0.1998  228  VAL A N   
1761  C  CA  . VAL A  228 ? 1.3558 2.4749 2.5731 0.9766  -0.1007 0.2109  228  VAL A CA  
1762  C  C   . VAL A  228 ? 1.3773 2.5019 2.5924 0.9884  -0.1181 0.2184  228  VAL A C   
1763  O  O   . VAL A  228 ? 1.3450 2.5194 2.6003 0.9659  -0.1378 0.2179  228  VAL A O   
1764  C  CB  . VAL A  228 ? 1.3754 2.5538 2.6241 0.9956  -0.0748 0.2178  228  VAL A CB  
1765  C  CG1 . VAL A  228 ? 1.3613 2.5308 2.6045 0.9874  -0.0567 0.2140  228  VAL A CG1 
1766  C  CG2 . VAL A  228 ? 1.4952 2.7678 2.8153 0.9777  -0.0842 0.2211  228  VAL A CG2 
1767  N  N   . GLY A  229 ? 1.4569 2.5288 2.6224 1.0259  -0.1112 0.2264  229  GLY A N   
1768  C  CA  . GLY A  229 ? 1.4903 2.5570 2.6457 1.0441  -0.1272 0.2371  229  GLY A CA  
1769  C  C   . GLY A  229 ? 1.5615 2.5460 2.6496 1.0840  -0.1188 0.2433  229  GLY A C   
1770  O  O   . GLY A  229 ? 1.5761 2.4943 2.6153 1.0887  -0.1079 0.2371  229  GLY A O   
1771  N  N   . ASP A  230 ? 1.8380 2.8242 2.9220 1.1142  -0.1249 0.2561  230  ASP A N   
1772  C  CA  . ASP A  230 ? 1.9449 2.8498 2.9654 1.1554  -0.1185 0.2626  230  ASP A CA  
1773  C  C   . ASP A  230 ? 2.0841 2.9248 3.0583 1.1431  -0.1443 0.2658  230  ASP A C   
1774  O  O   . ASP A  230 ? 2.1574 3.0336 3.1566 1.1209  -0.1690 0.2713  230  ASP A O   
1775  C  CB  . ASP A  230 ? 1.7992 2.7337 2.8393 1.1962  -0.1141 0.2763  230  ASP A CB  
1776  C  CG  . ASP A  230 ? 1.8921 2.7401 2.8677 1.2451  -0.1002 0.2802  230  ASP A CG  
1777  O  OD1 . ASP A  230 ? 1.9851 2.7586 2.9025 1.2496  -0.0871 0.2706  230  ASP A OD1 
1778  O  OD2 . ASP A  230 ? 1.9494 2.8014 2.9311 1.2797  -0.1038 0.2931  230  ASP A OD2 
1779  N  N   . PHE A  231 ? 2.0520 2.7999 2.9569 1.1577  -0.1386 0.2633  231  PHE A N   
1780  C  CA  . PHE A  231 ? 1.8270 2.5134 2.6860 1.1441  -0.1624 0.2674  231  PHE A CA  
1781  C  C   . PHE A  231 ? 1.9415 2.5299 2.7259 1.1831  -0.1618 0.2758  231  PHE A C   
1782  O  O   . PHE A  231 ? 2.0863 2.6362 2.8405 1.1841  -0.1848 0.2876  231  PHE A O   
1783  C  CB  . PHE A  231 ? 1.7707 2.4396 2.6204 1.1074  -0.1641 0.2547  231  PHE A CB  
1784  C  CG  . PHE A  231 ? 1.6838 2.4356 2.6006 1.0653  -0.1719 0.2467  231  PHE A CG  
1785  C  CD1 . PHE A  231 ? 1.6472 2.4285 2.5830 1.0400  -0.1967 0.2501  231  PHE A CD1 
1786  C  CD2 . PHE A  231 ? 1.6530 2.4529 2.6116 1.0527  -0.1542 0.2362  231  PHE A CD2 
1787  C  CE1 . PHE A  231 ? 1.5759 2.4284 2.5694 1.0035  -0.2030 0.2407  231  PHE A CE1 
1788  C  CE2 . PHE A  231 ? 1.6792 2.5485 2.6974 1.0148  -0.1623 0.2283  231  PHE A CE2 
1789  C  CZ  . PHE A  231 ? 1.5567 2.4502 2.5916 0.9905  -0.1864 0.2294  231  PHE A CZ  
1790  N  N   . ASN A  232 ? 1.9333 2.4787 2.6844 1.2165  -0.1356 0.2703  232  ASN A N   
1791  C  CA  . ASN A  232 ? 2.0777 2.5232 2.7541 1.2575  -0.1324 0.2757  232  ASN A CA  
1792  C  C   . ASN A  232 ? 2.0342 2.4944 2.7268 1.2984  -0.1298 0.2877  232  ASN A C   
1793  O  O   . ASN A  232 ? 2.1302 2.5095 2.7654 1.3395  -0.1216 0.2904  232  ASN A O   
1794  C  CB  . ASN A  232 ? 2.0142 2.3999 2.6390 1.2771  -0.1047 0.2623  232  ASN A CB  
1795  C  CG  . ASN A  232 ? 1.9928 2.4530 2.6671 1.2864  -0.0748 0.2543  232  ASN A CG  
1796  O  OD1 . ASN A  232 ? 1.9278 2.4870 2.6790 1.2666  -0.0773 0.2566  232  ASN A OD1 
1797  N  ND2 . ASN A  232 ? 2.0531 2.4650 2.6800 1.3170  -0.0464 0.2451  232  ASN A ND2 
1798  N  N   . GLY A  233 ? 1.9885 2.5469 2.7561 1.2886  -0.1377 0.2952  233  GLY A N   
1799  C  CA  . GLY A  233 ? 2.0438 2.6247 2.8349 1.3244  -0.1415 0.3101  233  GLY A CA  
1800  C  C   . GLY A  233 ? 2.2857 2.8510 3.0681 1.3745  -0.1093 0.3060  233  GLY A C   
1801  O  O   . GLY A  233 ? 2.5864 3.0931 3.3346 1.4167  -0.1095 0.3149  233  GLY A O   
1802  N  N   . ASP A  234 ? 2.0889 2.7046 2.9005 1.3718  -0.0810 0.2931  234  ASP A N   
1803  C  CA  . ASP A  234 ? 2.1609 2.7718 2.9663 1.4203  -0.0463 0.2885  234  ASP A CA  
1804  C  C   . ASP A  234 ? 2.1312 2.8622 3.0224 1.4224  -0.0306 0.2910  234  ASP A C   
1805  O  O   . ASP A  234 ? 2.4105 3.1617 3.3200 1.4672  -0.0126 0.2962  234  ASP A O   
1806  C  CB  . ASP A  234 ? 2.1877 2.7274 2.9265 1.4269  -0.0200 0.2711  234  ASP A CB  
1807  C  CG  . ASP A  234 ? 2.1009 2.7065 2.8762 1.3894  -0.0079 0.2611  234  ASP A CG  
1808  O  OD1 . ASP A  234 ? 2.0112 2.6835 2.8410 1.3445  -0.0292 0.2643  234  ASP A OD1 
1809  O  OD2 . ASP A  234 ? 2.1273 2.7159 2.8747 1.4056  0.0229  0.2501  234  ASP A OD2 
1810  N  N   . GLY A  235 ? 2.0285 2.8393 2.9735 1.3760  -0.0371 0.2878  235  GLY A N   
1811  C  CA  . GLY A  235 ? 1.9951 2.9206 3.0217 1.3737  -0.0259 0.2919  235  GLY A CA  
1812  C  C   . GLY A  235 ? 1.9414 2.9075 2.9851 1.3488  -0.0033 0.2797  235  GLY A C   
1813  O  O   . GLY A  235 ? 1.8993 2.9638 3.0120 1.3348  0.0030  0.2828  235  GLY A O   
1814  N  N   . ILE A  236 ? 1.9473 2.8374 2.9274 1.3437  0.0079  0.2674  236  ILE A N   
1815  C  CA  . ILE A  236 ? 1.9018 2.8195 2.8899 1.3212  0.0278  0.2575  236  ILE A CA  
1816  C  C   . ILE A  236 ? 1.8116 2.7370 2.8143 1.2635  0.0004  0.2529  236  ILE A C   
1817  O  O   . ILE A  236 ? 1.8080 2.6613 2.7643 1.2497  -0.0204 0.2502  236  ILE A O   
1818  C  CB  . ILE A  236 ? 1.9663 2.7986 2.8754 1.3513  0.0561  0.2476  236  ILE A CB  
1819  C  CG1 . ILE A  236 ? 2.0655 2.8858 2.9573 1.4122  0.0854  0.2497  236  ILE A CG1 
1820  C  CG2 . ILE A  236 ? 1.9201 2.7846 2.8383 1.3283  0.0750  0.2406  236  ILE A CG2 
1821  C  CD1 . ILE A  236 ? 2.0572 2.9903 3.0245 1.4244  0.1086  0.2561  236  ILE A CD1 
1822  N  N   . ASP A  237 ? 1.7431 2.7563 2.8112 1.2305  0.0005  0.2523  237  ASP A N   
1823  C  CA  . ASP A  237 ? 1.6615 2.6847 2.7478 1.1774  -0.0228 0.2458  237  ASP A CA  
1824  C  C   . ASP A  237 ? 1.6590 2.6026 2.6847 1.1680  -0.0183 0.2361  237  ASP A C   
1825  O  O   . ASP A  237 ? 1.6844 2.6144 2.6863 1.1848  0.0090  0.2332  237  ASP A O   
1826  C  CB  . ASP A  237 ? 1.6031 2.7268 2.7641 1.1489  -0.0184 0.2460  237  ASP A CB  
1827  C  CG  . ASP A  237 ? 1.5820 2.7826 2.8057 1.1385  -0.0384 0.2544  237  ASP A CG  
1828  O  OD1 . ASP A  237 ? 1.6215 2.8048 2.8337 1.1617  -0.0505 0.2625  237  ASP A OD1 
1829  O  OD2 . ASP A  237 ? 1.5305 2.8082 2.8139 1.1079  -0.0429 0.2539  237  ASP A OD2 
1830  N  N   . ASP A  238 ? 1.6737 2.5674 2.6743 1.1421  -0.0449 0.2327  238  ASP A N   
1831  C  CA  . ASP A  238 ? 1.6347 2.4520 2.5794 1.1314  -0.0466 0.2255  238  ASP A CA  
1832  C  C   . ASP A  238 ? 1.5527 2.4049 2.5368 1.0831  -0.0580 0.2183  238  ASP A C   
1833  O  O   . ASP A  238 ? 1.4980 2.4192 2.5441 1.0545  -0.0712 0.2172  238  ASP A O   
1834  C  CB  . ASP A  238 ? 1.6653 2.4022 2.5546 1.1365  -0.0682 0.2281  238  ASP A CB  
1835  C  CG  . ASP A  238 ? 1.7544 2.4468 2.6020 1.1854  -0.0594 0.2355  238  ASP A CG  
1836  O  OD1 . ASP A  238 ? 1.8130 2.4846 2.6321 1.2216  -0.0311 0.2335  238  ASP A OD1 
1837  O  OD2 . ASP A  238 ? 1.8353 2.5113 2.6764 1.1893  -0.0805 0.2435  238  ASP A OD2 
1838  N  N   . PHE A  239 ? 1.6340 2.4336 2.5792 1.0754  -0.0544 0.2135  239  PHE A N   
1839  C  CA  . PHE A  239 ? 1.5677 2.3949 2.5478 1.0363  -0.0608 0.2076  239  PHE A CA  
1840  C  C   . PHE A  239 ? 1.7174 2.5080 2.6895 1.0041  -0.0895 0.2027  239  PHE A C   
1841  O  O   . PHE A  239 ? 1.5605 2.2751 2.4730 1.0129  -0.0957 0.2041  239  PHE A O   
1842  C  CB  . PHE A  239 ? 1.7559 2.5574 2.7040 1.0496  -0.0385 0.2085  239  PHE A CB  
1843  C  CG  . PHE A  239 ? 1.9229 2.7588 2.8719 1.0858  -0.0053 0.2139  239  PHE A CG  
1844  C  CD1 . PHE A  239 ? 1.9983 2.9206 3.0106 1.0857  0.0018  0.2173  239  PHE A CD1 
1845  C  CD2 . PHE A  239 ? 1.9853 2.7680 2.8703 1.1214  0.0196  0.2158  239  PHE A CD2 
1846  C  CE1 . PHE A  239 ? 2.1489 3.1094 3.1661 1.1198  0.0341  0.2235  239  PHE A CE1 
1847  C  CE2 . PHE A  239 ? 1.9911 2.8084 2.8762 1.1574  0.0539  0.2201  239  PHE A CE2 
1848  C  CZ  . PHE A  239 ? 2.0422 2.9512 2.9963 1.1562  0.0616  0.2244  239  PHE A CZ  
1849  N  N   . VAL A  240 ? 1.4647 2.3101 2.4959 0.9679  -0.1063 0.1970  240  VAL A N   
1850  C  CA  . VAL A  240 ? 1.3348 2.1604 2.3699 0.9358  -0.1303 0.1909  240  VAL A CA  
1851  C  C   . VAL A  240 ? 1.2819 2.1311 2.3562 0.9042  -0.1325 0.1825  240  VAL A C   
1852  O  O   . VAL A  240 ? 1.2552 2.1663 2.3810 0.8934  -0.1258 0.1794  240  VAL A O   
1853  C  CB  . VAL A  240 ? 1.3120 2.1780 2.3793 0.9224  -0.1483 0.1901  240  VAL A CB  
1854  C  CG1 . VAL A  240 ? 1.7657 2.6109 2.8312 0.8941  -0.1693 0.1845  240  VAL A CG1 
1855  C  CG2 . VAL A  240 ? 1.4016 2.2510 2.4365 0.9564  -0.1470 0.2012  240  VAL A CG2 
1856  N  N   . SER A  241 ? 1.4525 2.2540 2.5051 0.8892  -0.1437 0.1798  241  SER A N   
1857  C  CA  . SER A  241 ? 1.2256 2.0418 2.3132 0.8624  -0.1474 0.1730  241  SER A CA  
1858  C  C   . SER A  241 ? 1.1979 1.9821 2.2835 0.8384  -0.1681 0.1676  241  SER A C   
1859  O  O   . SER A  241 ? 1.2258 1.9549 2.2615 0.8484  -0.1747 0.1740  241  SER A O   
1860  C  CB  . SER A  241 ? 1.2537 2.0465 2.3137 0.8796  -0.1305 0.1809  241  SER A CB  
1861  O  OG  . SER A  241 ? 1.2137 2.0280 2.3132 0.8548  -0.1354 0.1770  241  SER A OG  
1862  N  N   . GLY A  242 ? 1.1469 1.9672 2.2879 0.8080  -0.1779 0.1558  242  GLY A N   
1863  C  CA  . GLY A  242 ? 1.1193 1.9172 2.2684 0.7856  -0.1949 0.1494  242  GLY A CA  
1864  C  C   . GLY A  242 ? 1.1254 1.8830 2.2565 0.7846  -0.1974 0.1536  242  GLY A C   
1865  O  O   . GLY A  242 ? 1.1275 1.8962 2.2682 0.7880  -0.1890 0.1556  242  GLY A O   
1866  N  N   . VAL A  243 ? 1.1308 1.8449 2.2351 0.7806  -0.2101 0.1579  243  VAL A N   
1867  C  CA  . VAL A  243 ? 1.3779 2.0529 2.4647 0.7785  -0.2181 0.1643  243  VAL A CA  
1868  C  C   . VAL A  243 ? 1.4184 2.1003 2.5400 0.7523  -0.2371 0.1517  243  VAL A C   
1869  O  O   . VAL A  243 ? 1.2965 1.9477 2.3934 0.7500  -0.2474 0.1598  243  VAL A O   
1870  C  CB  . VAL A  243 ? 1.2748 1.8861 2.2863 0.8034  -0.2166 0.1830  243  VAL A CB  
1871  C  CG1 . VAL A  243 ? 1.2140 1.7902 2.2034 0.8071  -0.2205 0.1948  243  VAL A CG1 
1872  C  CG2 . VAL A  243 ? 1.2378 1.8453 2.2121 0.8333  -0.1972 0.1877  243  VAL A CG2 
1873  N  N   . PRO A  244 ? 1.2162 1.9373 2.3737 0.7319  -0.2386 0.1294  244  PRO A N   
1874  C  CA  . PRO A  244 ? 1.0482 1.7897 2.2018 0.7159  -0.2491 0.1035  244  PRO A CA  
1875  C  C   . PRO A  244 ? 1.0588 1.7989 2.1460 0.7297  -0.2440 0.1223  244  PRO A C   
1876  O  O   . PRO A  244 ? 1.1209 1.8862 2.2116 0.7210  -0.2350 0.1359  244  PRO A O   
1877  C  CB  . PRO A  244 ? 1.0305 1.8435 2.1792 0.7205  -0.2337 0.0910  244  PRO A CB  
1878  C  CG  . PRO A  244 ? 1.0387 1.8398 2.2130 0.7246  -0.2324 0.1001  244  PRO A CG  
1879  C  CD  . PRO A  244 ? 1.0609 1.8197 2.2428 0.7345  -0.2301 0.1218  244  PRO A CD  
1880  N  N   . ARG A  245 ? 1.0763 1.7792 2.1579 0.7348  -0.2500 0.1384  245  ARG A N   
1881  C  CA  . ARG A  245 ? 1.0761 1.7601 2.1565 0.7287  -0.2567 0.1609  245  ARG A CA  
1882  C  C   . ARG A  245 ? 1.1118 1.7391 2.1497 0.7388  -0.2714 0.1755  245  ARG A C   
1883  O  O   . ARG A  245 ? 1.5196 2.1235 2.5598 0.7271  -0.2836 0.1934  245  ARG A O   
1884  C  CB  . ARG A  245 ? 1.0773 1.7507 2.1824 0.7185  -0.2589 0.1724  245  ARG A CB  
1885  C  CG  . ARG A  245 ? 1.0458 1.7625 2.2010 0.6993  -0.2500 0.1623  245  ARG A CG  
1886  C  CD  . ARG A  245 ? 1.0517 1.7474 2.2347 0.6836  -0.2580 0.1767  245  ARG A CD  
1887  N  NE  . ARG A  245 ? 1.1881 1.8496 2.3715 0.6695  -0.2745 0.1892  245  ARG A NE  
1888  C  CZ  . ARG A  245 ? 1.0436 1.7163 2.2612 0.6503  -0.2784 0.1823  245  ARG A CZ  
1889  N  NH1 . ARG A  245 ? 1.0199 1.7306 2.2713 0.6435  -0.2664 0.1635  245  ARG A NH1 
1890  N  NH2 . ARG A  245 ? 1.0540 1.7000 2.2746 0.6385  -0.2953 0.1949  245  ARG A NH2 
1891  N  N   . ALA A  246 ? 1.1361 1.7260 2.1644 0.7464  -0.2793 0.1669  246  ALA A N   
1892  C  CA  . ALA A  246 ? 1.1717 1.7041 2.1733 0.7536  -0.2893 0.1949  246  ALA A CA  
1893  C  C   . ALA A  246 ? 1.1658 1.7052 2.1516 0.7461  -0.3027 0.1891  246  ALA A C   
1894  O  O   . ALA A  246 ? 1.1303 1.7374 2.1236 0.7419  -0.2843 0.1833  246  ALA A O   
1895  C  CB  . ALA A  246 ? 1.2051 1.7212 2.1724 0.7780  -0.2709 0.2060  246  ALA A CB  
1896  N  N   . ALA A  247 ? 1.4049 1.8946 2.3646 0.7497  -0.3139 0.2224  247  ALA A N   
1897  C  CA  . ALA A  247 ? 1.4530 1.9569 2.3891 0.7502  -0.3208 0.2342  247  ALA A CA  
1898  C  C   . ALA A  247 ? 1.1837 1.7297 2.1716 0.7206  -0.3280 0.2231  247  ALA A C   
1899  O  O   . ALA A  247 ? 1.1304 1.7185 2.1472 0.7084  -0.3273 0.2140  247  ALA A O   
1900  C  CB  . ALA A  247 ? 1.5432 2.0635 2.5012 0.7485  -0.3184 0.2268  247  ALA A CB  
1901  N  N   . ARG A  248 ? 1.1569 1.6907 2.1604 0.7073  -0.3331 0.2279  248  ARG A N   
1902  C  CA  . ARG A  248 ? 1.1252 1.6907 2.1798 0.6786  -0.3384 0.2236  248  ARG A CA  
1903  C  C   . ARG A  248 ? 1.1691 1.8018 2.2647 0.6736  -0.3159 0.1980  248  ARG A C   
1904  O  O   . ARG A  248 ? 1.5026 2.1703 2.6316 0.6593  -0.3167 0.1900  248  ARG A O   
1905  C  CB  . ARG A  248 ? 1.1443 1.6953 2.2051 0.6609  -0.3640 0.2386  248  ARG A CB  
1906  C  CG  . ARG A  248 ? 1.5374 2.0956 2.6383 0.6346  -0.3782 0.2469  248  ARG A CG  
1907  C  CD  . ARG A  248 ? 1.7246 2.2371 2.8065 0.6342  -0.3890 0.2635  248  ARG A CD  
1908  N  NE  . ARG A  248 ? 1.5964 2.1125 2.7147 0.6086  -0.4074 0.2764  248  ARG A NE  
1909  C  CZ  . ARG A  248 ? 1.4782 1.9576 2.5837 0.5924  -0.4404 0.3035  248  ARG A CZ  
1910  N  NH1 . ARG A  248 ? 1.6365 2.0627 2.6851 0.5979  -0.4592 0.3192  248  ARG A NH1 
1911  N  NH2 . ARG A  248 ? 1.1820 1.6736 2.3259 0.5692  -0.4562 0.3155  248  ARG A NH2 
1912  N  N   . THR A  249 ? 1.1782 1.8291 2.2715 0.6858  -0.2969 0.1863  249  THR A N   
1913  C  CA  . THR A  249 ? 1.0824 1.7897 2.2089 0.6816  -0.2772 0.1653  249  THR A CA  
1914  C  C   . THR A  249 ? 1.0237 1.7672 2.1477 0.6885  -0.2688 0.1572  249  THR A C   
1915  O  O   . THR A  249 ? 0.9973 1.7883 2.1527 0.6814  -0.2549 0.1428  249  THR A O   
1916  C  CB  . THR A  249 ? 1.2950 2.0237 2.4715 0.6585  -0.2773 0.1570  249  THR A CB  
1917  O  OG1 . THR A  249 ? 1.3502 2.0901 2.5439 0.6473  -0.2864 0.1572  249  THR A OG1 
1918  C  CG2 . THR A  249 ? 1.0281 1.7220 2.2117 0.6500  -0.2883 0.1698  249  THR A CG2 
1919  N  N   . LEU A  250 ? 1.0467 1.7656 2.1358 0.7018  -0.2783 0.1692  250  LEU A N   
1920  C  CA  . LEU A  250 ? 1.0423 1.7878 2.1270 0.7049  -0.2701 0.1683  250  LEU A CA  
1921  C  C   . LEU A  250 ? 1.0405 1.7973 2.1274 0.7070  -0.2459 0.1780  250  LEU A C   
1922  O  O   . LEU A  250 ? 1.0175 1.7972 2.1618 0.6891  -0.2423 0.1769  250  LEU A O   
1923  C  CB  . LEU A  250 ? 1.0745 1.7785 2.1270 0.7132  -0.2885 0.1870  250  LEU A CB  
1924  C  CG  . LEU A  250 ? 1.2998 2.0347 2.3732 0.7055  -0.2966 0.1875  250  LEU A CG  
1925  C  CD1 . LEU A  250 ? 1.0256 1.8146 2.1503 0.6870  -0.2948 0.1677  250  LEU A CD1 
1926  C  CD2 . LEU A  250 ? 1.5027 2.1871 2.5425 0.7135  -0.3261 0.2052  250  LEU A CD2 
1927  N  N   . GLY A  251 ? 1.0575 1.7837 2.1305 0.7141  -0.2387 0.1892  251  GLY A N   
1928  C  CA  . GLY A  251 ? 1.5629 2.2596 2.7050 0.7006  -0.2575 0.1567  251  GLY A CA  
1929  C  C   . GLY A  251 ? 1.2854 1.9604 2.3816 0.7308  -0.2619 0.1666  251  GLY A C   
1930  O  O   . GLY A  251 ? 1.5008 2.1761 2.5777 0.7358  -0.2695 0.1730  251  GLY A O   
1931  N  N   . MET A  252 ? 1.1144 1.7714 2.1867 0.7510  -0.2544 0.1689  252  MET A N   
1932  C  CA  . MET A  252 ? 1.1635 1.7909 2.1747 0.7777  -0.2504 0.1794  252  MET A CA  
1933  C  C   . MET A  252 ? 1.1681 1.8220 2.1906 0.7892  -0.2344 0.1738  252  MET A C   
1934  O  O   . MET A  252 ? 1.1384 1.8265 2.2073 0.7777  -0.2277 0.1638  252  MET A O   
1935  C  CB  . MET A  252 ? 1.2182 1.7754 2.1608 0.7982  -0.2552 0.1954  252  MET A CB  
1936  C  CG  . MET A  252 ? 1.2254 1.7536 2.1470 0.7906  -0.2748 0.2054  252  MET A CG  
1937  S  SD  . MET A  252 ? 1.3061 1.7406 2.1324 0.8171  -0.2849 0.2251  252  MET A SD  
1938  C  CE  . MET A  252 ? 1.5106 1.9087 2.2718 0.8481  -0.2795 0.2292  252  MET A CE  
1939  N  N   . VAL A  253 ? 1.2092 1.8482 2.1898 0.8133  -0.2297 0.1810  253  VAL A N   
1940  C  CA  . VAL A  253 ? 1.2881 1.9500 2.2735 0.8304  -0.2140 0.1796  253  VAL A CA  
1941  C  C   . VAL A  253 ? 1.5894 2.1921 2.5034 0.8662  -0.2066 0.1920  253  VAL A C   
1942  O  O   . VAL A  253 ? 1.9943 2.5590 2.8627 0.8797  -0.2158 0.2005  253  VAL A O   
1943  C  CB  . VAL A  253 ? 1.5500 2.2675 2.5698 0.8246  -0.2158 0.1744  253  VAL A CB  
1944  C  CG1 . VAL A  253 ? 1.2346 1.9703 2.2500 0.8488  -0.2020 0.1782  253  VAL A CG1 
1945  C  CG2 . VAL A  253 ? 1.1650 1.9388 2.2542 0.7924  -0.2192 0.1599  253  VAL A CG2 
1946  N  N   . TYR A  254 ? 1.4695 2.0616 2.3705 0.8833  -0.1900 0.1934  254  TYR A N   
1947  C  CA  . TYR A  254 ? 1.4601 1.9940 2.2915 0.9213  -0.1785 0.2024  254  TYR A CA  
1948  C  C   . TYR A  254 ? 1.4184 1.9873 2.2611 0.9437  -0.1621 0.2018  254  TYR A C   
1949  O  O   . TYR A  254 ? 1.7593 2.3953 2.6598 0.9328  -0.1534 0.1958  254  TYR A O   
1950  C  CB  . TYR A  254 ? 1.4690 1.9690 2.2714 0.9321  -0.1678 0.2055  254  TYR A CB  
1951  C  CG  . TYR A  254 ? 1.4123 1.8734 2.1991 0.9140  -0.1861 0.2099  254  TYR A CG  
1952  C  CD1 . TYR A  254 ? 1.3999 1.8430 2.1814 0.8976  -0.2085 0.2122  254  TYR A CD1 
1953  C  CD2 . TYR A  254 ? 1.5800 2.0270 2.3591 0.9142  -0.1819 0.2141  254  TYR A CD2 
1954  C  CE1 . TYR A  254 ? 1.9811 2.3952 2.7539 0.8812  -0.2264 0.2179  254  TYR A CE1 
1955  C  CE2 . TYR A  254 ? 1.8186 2.2330 2.5871 0.8979  -0.2017 0.2208  254  TYR A CE2 
1956  C  CZ  . TYR A  254 ? 1.9551 2.3544 2.7226 0.8810  -0.2242 0.2223  254  TYR A CZ  
1957  O  OH  . TYR A  254 ? 1.7816 2.1546 2.5433 0.8650  -0.2451 0.2308  254  TYR A OH  
1958  N  N   . ILE A  255 ? 1.5672 2.0897 2.3555 0.9754  -0.1595 0.2088  255  ILE A N   
1959  C  CA  . ILE A  255 ? 1.6007 2.1487 2.3944 1.0038  -0.1429 0.2105  255  ILE A CA  
1960  C  C   . ILE A  255 ? 1.6811 2.1662 2.4083 1.0446  -0.1226 0.2134  255  ILE A C   
1961  O  O   . ILE A  255 ? 1.7390 2.1392 2.3944 1.0608  -0.1294 0.2175  255  ILE A O   
1962  C  CB  . ILE A  255 ? 1.6148 2.1677 2.4076 1.0100  -0.1570 0.2166  255  ILE A CB  
1963  C  CG1 . ILE A  255 ? 1.5916 2.2147 2.4500 0.9725  -0.1734 0.2120  255  ILE A CG1 
1964  C  CG2 . ILE A  255 ? 1.6630 2.2322 2.4554 1.0453  -0.1407 0.2208  255  ILE A CG2 
1965  C  CD1 . ILE A  255 ? 1.5507 2.1976 2.4172 0.9794  -0.1859 0.2195  255  ILE A CD1 
1966  N  N   . TYR A  256 ? 1.7455 2.2703 2.4933 1.0617  -0.0974 0.2112  256  TYR A N   
1967  C  CA  . TYR A  256 ? 1.8263 2.3001 2.5130 1.1046  -0.0725 0.2121  256  TYR A CA  
1968  C  C   . TYR A  256 ? 1.8670 2.3730 2.5668 1.1382  -0.0537 0.2139  256  TYR A C   
1969  O  O   . TYR A  256 ? 1.9540 2.5445 2.7248 1.1251  -0.0539 0.2148  256  TYR A O   
1970  C  CB  . TYR A  256 ? 1.9330 2.4231 2.6244 1.1021  -0.0545 0.2103  256  TYR A CB  
1971  C  CG  . TYR A  256 ? 1.9820 2.4308 2.6527 1.0763  -0.0728 0.2111  256  TYR A CG  
1972  C  CD1 . TYR A  256 ? 2.0417 2.3938 2.6246 1.0976  -0.0738 0.2134  256  TYR A CD1 
1973  C  CD2 . TYR A  256 ? 1.8316 2.3346 2.5689 1.0319  -0.0899 0.2096  256  TYR A CD2 
1974  C  CE1 . TYR A  256 ? 2.0394 2.3559 2.6054 1.0744  -0.0936 0.2169  256  TYR A CE1 
1975  C  CE2 . TYR A  256 ? 1.6826 2.1518 2.4072 1.0098  -0.1073 0.2119  256  TYR A CE2 
1976  C  CZ  . TYR A  256 ? 1.9181 2.2976 2.5593 1.0307  -0.1100 0.2171  256  TYR A CZ  
1977  O  OH  . TYR A  256 ? 1.7772 2.1261 2.4084 1.0086  -0.1306 0.2221  256  TYR A OH  
1978  N  N   . ASP A  257 ? 2.0110 2.4460 2.6405 1.1826  -0.0384 0.2142  257  ASP A N   
1979  C  CA  . ASP A  257 ? 2.3383 2.7988 2.9771 1.2212  -0.0169 0.2159  257  ASP A CA  
1980  C  C   . ASP A  257 ? 2.2562 2.7950 2.9408 1.2282  0.0129  0.2143  257  ASP A C   
1981  O  O   . ASP A  257 ? 2.2595 2.7871 2.9220 1.2285  0.0286  0.2112  257  ASP A O   
1982  C  CB  . ASP A  257 ? 2.4560 2.8112 3.0019 1.2689  -0.0053 0.2138  257  ASP A CB  
1983  C  CG  . ASP A  257 ? 2.4618 2.8392 3.0183 1.3125  0.0166  0.2155  257  ASP A CG  
1984  O  OD1 . ASP A  257 ? 2.5129 2.9689 3.1406 1.3038  0.0082  0.2226  257  ASP A OD1 
1985  O  OD2 . ASP A  257 ? 2.5136 2.8284 3.0057 1.3567  0.0421  0.2095  257  ASP A OD2 
1986  N  N   . GLY A  258 ? 2.1392 2.7593 2.8875 1.2344  0.0198  0.2185  258  GLY A N   
1987  C  CA  . GLY A  258 ? 2.0165 2.7228 2.8174 1.2380  0.0461  0.2198  258  GLY A CA  
1988  C  C   . GLY A  258 ? 2.1044 2.7958 2.8679 1.2913  0.0849  0.2189  258  GLY A C   
1989  O  O   . GLY A  258 ? 2.0994 2.8724 2.9124 1.3017  0.1087  0.2227  258  GLY A O   
1990  N  N   . LYS A  259 ? 2.0925 2.6796 2.7671 1.3260  0.0924  0.2134  259  LYS A N   
1991  C  CA  . LYS A  259 ? 2.1909 2.7483 2.8169 1.3807  0.1312  0.2089  259  LYS A CA  
1992  C  C   . LYS A  259 ? 2.4264 2.8993 2.9638 1.3960  0.1487  0.2004  259  LYS A C   
1993  O  O   . LYS A  259 ? 2.5342 3.0248 3.0555 1.4244  0.1862  0.1976  259  LYS A O   
1994  C  CB  . LYS A  259 ? 2.3054 2.8051 2.8968 1.4205  0.1288  0.2083  259  LYS A CB  
1995  C  CG  . LYS A  259 ? 2.3797 2.8643 2.9374 1.4801  0.1707  0.2028  259  LYS A CG  
1996  C  CD  . LYS A  259 ? 2.4714 2.8842 2.9892 1.5200  0.1654  0.2019  259  LYS A CD  
1997  C  CE  . LYS A  259 ? 2.6251 2.8954 3.0375 1.5246  0.1492  0.1936  259  LYS A CE  
1998  N  NZ  . LYS A  259 ? 2.7901 2.9813 3.1575 1.5657  0.1455  0.1930  259  LYS A NZ  
1999  N  N   . ASN A  260 ? 2.1448 2.5270 2.6224 1.3786  0.1226  0.1971  260  ASN A N   
2000  C  CA  . ASN A  260 ? 2.2172 2.5095 2.6028 1.3936  0.1348  0.1897  260  ASN A CA  
2001  C  C   . ASN A  260 ? 2.1356 2.4099 2.5201 1.3473  0.1041  0.1935  260  ASN A C   
2002  O  O   . ASN A  260 ? 2.1885 2.3722 2.4892 1.3563  0.1037  0.1892  260  ASN A O   
2003  C  CB  . ASN A  260 ? 2.6605 2.8200 2.9377 1.4359  0.1386  0.1794  260  ASN A CB  
2004  C  CG  . ASN A  260 ? 2.7407 2.8478 3.0089 1.4192  0.0993  0.1831  260  ASN A CG  
2005  O  OD1 . ASN A  260 ? 2.2342 2.3790 2.5535 1.3727  0.0667  0.1912  260  ASN A OD1 
2006  N  ND2 . ASN A  260 ? 3.9380 3.9557 4.1388 1.4582  0.1035  0.1773  260  ASN A ND2 
2007  N  N   . MET A  261 ? 2.0264 2.3798 2.4984 1.2994  0.0776  0.2008  261  MET A N   
2008  C  CA  . MET A  261 ? 1.9539 2.3060 2.4413 1.2538  0.0497  0.2046  261  MET A CA  
2009  C  C   . MET A  261 ? 1.9993 2.2354 2.4054 1.2519  0.0228  0.2026  261  MET A C   
2010  O  O   . MET A  261 ? 2.1562 2.3174 2.4918 1.2585  0.0216  0.2017  261  MET A O   
2011  C  CB  . MET A  261 ? 1.9665 2.3459 2.4556 1.2518  0.0691  0.2080  261  MET A CB  
2012  C  CG  . MET A  261 ? 1.8413 2.2656 2.3896 1.1997  0.0425  0.2146  261  MET A CG  
2013  S  SD  . MET A  261 ? 1.7345 2.2767 2.4047 1.1573  0.0268  0.2153  261  MET A SD  
2014  C  CE  . MET A  261 ? 1.7117 2.3571 2.4420 1.1623  0.0606  0.2217  261  MET A CE  
2015  N  N   . SER A  262 ? 2.0718 2.2935 2.4868 1.2434  0.0000  0.2037  262  SER A N   
2016  C  CA  . SER A  262 ? 2.2023 2.3259 2.5520 1.2360  -0.0293 0.2049  262  SER A CA  
2017  C  C   . SER A  262 ? 2.0186 2.1928 2.4348 1.1920  -0.0617 0.2112  262  SER A C   
2018  O  O   . SER A  262 ? 1.9711 2.2242 2.4577 1.1837  -0.0615 0.2130  262  SER A O   
2019  C  CB  . SER A  262 ? 2.5474 2.5773 2.8166 1.2798  -0.0224 0.2010  262  SER A CB  
2020  O  OG  . SER A  262 ? 2.7670 2.6967 2.9686 1.2704  -0.0527 0.2038  262  SER A OG  
2021  N  N   . SER A  263 ? 2.0946 2.2187 2.4829 1.1660  -0.0900 0.2148  263  SER A N   
2022  C  CA  . SER A  263 ? 1.9992 2.1698 2.4459 1.1250  -0.1185 0.2198  263  SER A CA  
2023  C  C   . SER A  263 ? 2.2140 2.3621 2.6464 1.1373  -0.1299 0.2248  263  SER A C   
2024  O  O   . SER A  263 ? 2.5690 2.6199 2.9189 1.1654  -0.1329 0.2268  263  SER A O   
2025  C  CB  . SER A  263 ? 2.0247 2.1491 2.4446 1.0973  -0.1447 0.2240  263  SER A CB  
2026  O  OG  . SER A  263 ? 2.0392 2.2203 2.5226 1.0582  -0.1676 0.2272  263  SER A OG  
2027  N  N   . LEU A  264 ? 2.0556 2.2884 2.5642 1.1168  -0.1374 0.2271  264  LEU A N   
2028  C  CA  . LEU A  264 ? 2.0079 2.2320 2.5114 1.1279  -0.1498 0.2350  264  LEU A CA  
2029  C  C   . LEU A  264 ? 1.9624 2.1927 2.4793 1.0942  -0.1807 0.2422  264  LEU A C   
2030  O  O   . LEU A  264 ? 2.0188 2.1765 2.4771 1.1032  -0.1983 0.2515  264  LEU A O   
2031  C  CB  . LEU A  264 ? 2.1218 2.4346 2.6936 1.1364  -0.1364 0.2347  264  LEU A CB  
2032  C  CG  . LEU A  264 ? 2.1457 2.4620 2.7090 1.1767  -0.1049 0.2306  264  LEU A CG  
2033  C  CD1 . LEU A  264 ? 2.0052 2.4151 2.6427 1.1800  -0.0993 0.2339  264  LEU A CD1 
2034  C  CD2 . LEU A  264 ? 2.2439 2.4526 2.7169 1.2208  -0.0988 0.2323  264  LEU A CD2 
2035  N  N   . TYR A  265 ? 1.9054 2.2179 2.4953 1.0560  -0.1875 0.2380  265  TYR A N   
2036  C  CA  . TYR A  265 ? 1.9684 2.3016 2.5788 1.0257  -0.2130 0.2430  265  TYR A CA  
2037  C  C   . TYR A  265 ? 1.7012 2.0778 2.3591 0.9877  -0.2169 0.2344  265  TYR A C   
2038  O  O   . TYR A  265 ? 1.6697 2.0802 2.3617 0.9814  -0.2011 0.2255  265  TYR A O   
2039  C  CB  . TYR A  265 ? 2.1568 2.5579 2.8155 1.0223  -0.2189 0.2467  265  TYR A CB  
2040  C  CG  . TYR A  265 ? 2.5126 2.8737 3.1305 1.0589  -0.2203 0.2588  265  TYR A CG  
2041  C  CD1 . TYR A  265 ? 2.4781 2.7774 3.0414 1.0663  -0.2418 0.2730  265  TYR A CD1 
2042  C  CD2 . TYR A  265 ? 2.3248 2.7111 2.9607 1.0866  -0.2010 0.2575  265  TYR A CD2 
2043  C  CE1 . TYR A  265 ? 2.3015 2.5589 2.8279 1.1001  -0.2448 0.2854  265  TYR A CE1 
2044  C  CE2 . TYR A  265 ? 2.1018 2.4521 2.7054 1.1219  -0.2027 0.2690  265  TYR A CE2 
2045  C  CZ  . TYR A  265 ? 1.9854 2.2688 2.5341 1.1284  -0.2249 0.2828  265  TYR A CZ  
2046  O  OH  . TYR A  265 ? 2.0656 2.3082 2.5827 1.1637  -0.2282 0.2955  265  TYR A OH  
2047  N  N   . ASN A  266 ? 1.7459 2.1194 2.4044 0.9640  -0.2387 0.2384  266  ASN A N   
2048  C  CA  . ASN A  266 ? 1.9578 2.3734 2.6659 0.9283  -0.2444 0.2306  266  ASN A CA  
2049  C  C   . ASN A  266 ? 1.8988 2.3774 2.6561 0.9019  -0.2580 0.2281  266  ASN A C   
2050  O  O   . ASN A  266 ? 2.0783 2.5450 2.8091 0.9083  -0.2723 0.2381  266  ASN A O   
2051  C  CB  . ASN A  266 ? 2.2282 2.5775 2.8886 0.9248  -0.2571 0.2368  266  ASN A CB  
2052  C  CG  . ASN A  266 ? 2.3253 2.6350 2.9579 0.9388  -0.2431 0.2344  266  ASN A CG  
2053  O  OD1 . ASN A  266 ? 1.9680 2.3200 2.6376 0.9415  -0.2231 0.2261  266  ASN A OD1 
2054  N  ND2 . ASN A  266 ? 3.0827 3.3100 3.6459 0.9479  -0.2552 0.2426  266  ASN A ND2 
2055  N  N   . PHE A  267 ? 1.4206 1.9630 2.2462 0.8733  -0.2537 0.2148  267  PHE A N   
2056  C  CA  . PHE A  267 ? 1.3663 1.9644 2.2379 0.8458  -0.2645 0.2084  267  PHE A CA  
2057  C  C   . PHE A  267 ? 1.6923 2.2942 2.5926 0.8210  -0.2681 0.2018  267  PHE A C   
2058  O  O   . PHE A  267 ? 1.5974 2.1851 2.5066 0.8188  -0.2597 0.1984  267  PHE A O   
2059  C  CB  . PHE A  267 ? 1.3250 1.9971 2.2558 0.8346  -0.2567 0.1969  267  PHE A CB  
2060  C  CG  . PHE A  267 ? 1.8097 2.4887 2.7228 0.8584  -0.2547 0.2048  267  PHE A CG  
2061  C  CD1 . PHE A  267 ? 1.9309 2.6252 2.8303 0.8629  -0.2687 0.2132  267  PHE A CD1 
2062  C  CD2 . PHE A  267 ? 1.8987 2.5729 2.8105 0.8778  -0.2391 0.2053  267  PHE A CD2 
2063  C  CE1 . PHE A  267 ? 1.9357 2.6368 2.8219 0.8860  -0.2692 0.2231  267  PHE A CE1 
2064  C  CE2 . PHE A  267 ? 1.4227 2.1071 2.3246 0.9015  -0.2372 0.2136  267  PHE A CE2 
2065  C  CZ  . PHE A  267 ? 1.7236 2.4197 2.6135 0.9054  -0.2532 0.2230  267  PHE A CZ  
2066  N  N   . THR A  268 ? 1.6946 2.3189 2.6101 0.8037  -0.2811 0.2009  268  THR A N   
2067  C  CA  . THR A  268 ? 1.2618 1.8948 2.2101 0.7811  -0.2859 0.1960  268  THR A CA  
2068  C  C   . THR A  268 ? 1.2071 1.9102 2.2168 0.7568  -0.2853 0.1818  268  THR A C   
2069  O  O   . THR A  268 ? 1.2099 1.9414 2.2124 0.7589  -0.2913 0.1822  268  THR A O   
2070  C  CB  . THR A  268 ? 1.5473 2.1279 2.4439 0.7880  -0.3039 0.2120  268  THR A CB  
2071  O  OG1 . THR A  268 ? 1.3761 1.8829 2.2036 0.8145  -0.3039 0.2247  268  THR A OG1 
2072  C  CG2 . THR A  268 ? 1.6100 2.1985 2.5428 0.7669  -0.3099 0.2100  268  THR A CG2 
2073  N  N   . GLY A  269 ? 1.1038 1.8333 2.1711 0.7357  -0.2774 0.1704  269  GLY A N   
2074  C  CA  . GLY A  269 ? 1.1581 1.9464 2.2807 0.7140  -0.2735 0.1585  269  GLY A CA  
2075  C  C   . GLY A  269 ? 1.0478 1.8434 2.1626 0.7092  -0.2858 0.1625  269  GLY A C   
2076  O  O   . GLY A  269 ? 1.0770 1.8292 2.1515 0.7183  -0.2997 0.1763  269  GLY A O   
2077  N  N   . GLU A  270 ? 1.0183 1.8726 2.1704 0.6957  -0.2812 0.1499  270  GLU A N   
2078  C  CA  . GLU A  270 ? 1.2966 2.1737 2.4474 0.6914  -0.2926 0.1495  270  GLU A CA  
2079  C  C   . GLU A  270 ? 1.3485 2.2675 2.5537 0.6725  -0.2802 0.1406  270  GLU A C   
2080  O  O   . GLU A  270 ? 0.9744 1.9237 2.1924 0.6664  -0.2882 0.1350  270  GLU A O   
2081  C  CB  . GLU A  270 ? 1.2432 2.1616 2.3752 0.6980  -0.2984 0.1436  270  GLU A CB  
2082  C  CG  . GLU A  270 ? 1.0726 1.9524 2.1401 0.7213  -0.3083 0.1617  270  GLU A CG  
2083  C  CD  . GLU A  270 ? 1.1921 2.0219 2.2009 0.7357  -0.3268 0.1860  270  GLU A CD  
2084  O  OE1 . GLU A  270 ? 1.1952 2.0221 2.2149 0.7250  -0.3337 0.1894  270  GLU A OE1 
2085  O  OE2 . GLU A  270 ? 1.2789 2.0690 2.2296 0.7569  -0.3352 0.2037  270  GLU A OE2 
2086  N  N   . GLN A  271 ? 1.4442 2.3698 2.6663 0.6674  -0.2596 0.1383  271  GLN A N   
2087  C  CA  . GLN A  271 ? 1.1469 2.1050 2.3970 0.6574  -0.2494 0.1211  271  GLN A CA  
2088  C  C   . GLN A  271 ? 1.1692 2.0944 2.4029 0.6602  -0.2460 0.1216  271  GLN A C   
2089  O  O   . GLN A  271 ? 1.4885 2.3978 2.7036 0.6684  -0.2382 0.1277  271  GLN A O   
2090  C  CB  . GLN A  271 ? 0.9220 1.9284 2.2138 0.6473  -0.2348 0.0987  271  GLN A CB  
2091  C  CG  . GLN A  271 ? 0.9089 1.9387 2.2378 0.6359  -0.2256 0.0777  271  GLN A CG  
2092  C  CD  . GLN A  271 ? 0.8979 1.9690 2.2633 0.6287  -0.2133 0.0519  271  GLN A CD  
2093  O  OE1 . GLN A  271 ? 0.8957 1.9636 2.2711 0.6271  -0.2049 0.0430  271  GLN A OE1 
2094  N  NE2 . GLN A  271 ? 0.8946 2.0068 2.2783 0.6249  -0.2152 0.0366  271  GLN A NE2 
2095  N  N   . MET A  272 ? 1.0584 1.9744 2.3081 0.6499  -0.2530 0.1159  272  MET A N   
2096  C  CA  . MET A  272 ? 0.9532 1.8334 2.1976 0.6474  -0.2551 0.1183  272  MET A CA  
2097  C  C   . MET A  272 ? 0.9411 1.8380 2.2063 0.6449  -0.2387 0.1049  272  MET A C   
2098  O  O   . MET A  272 ? 0.9258 1.8608 2.2282 0.6371  -0.2275 0.0881  272  MET A O   
2099  C  CB  . MET A  272 ? 0.9526 1.8276 2.2261 0.6326  -0.2658 0.1193  272  MET A CB  
2100  C  CG  . MET A  272 ? 1.2228 2.0838 2.4855 0.6299  -0.2864 0.1353  272  MET A CG  
2101  S  SD  . MET A  272 ? 1.8460 2.6319 3.0537 0.6386  -0.3074 0.1618  272  MET A SD  
2102  C  CE  . MET A  272 ? 1.7145 2.4871 2.9208 0.6290  -0.3352 0.1836  272  MET A CE  
2103  N  N   . ALA A  273 ? 0.9514 1.8195 2.1946 0.6519  -0.2387 0.1119  273  ALA A N   
2104  C  CA  . ALA A  273 ? 0.9440 1.8219 2.2101 0.6476  -0.2286 0.1019  273  ALA A CA  
2105  C  C   . ALA A  273 ? 1.0722 1.9948 2.3581 0.6473  -0.2152 0.0902  273  ALA A C   
2106  O  O   . ALA A  273 ? 0.9461 1.8858 2.2694 0.6377  -0.2090 0.0745  273  ALA A O   
2107  C  CB  . ALA A  273 ? 0.9416 1.8124 2.2473 0.6328  -0.2313 0.0936  273  ALA A CB  
2108  N  N   . ALA A  274 ? 1.2747 2.2133 2.5408 0.6566  -0.2129 0.0992  274  ALA A N   
2109  C  CA  . ALA A  274 ? 0.9241 1.9024 2.2114 0.6548  -0.2038 0.0946  274  ALA A CA  
2110  C  C   . ALA A  274 ? 0.9244 1.9024 2.1995 0.6622  -0.1984 0.1044  274  ALA A C   
2111  O  O   . ALA A  274 ? 0.9708 1.9816 2.2700 0.6577  -0.1937 0.1021  274  ALA A O   
2112  C  CB  . ALA A  274 ? 0.9188 1.9094 2.2035 0.6564  -0.2075 0.1036  274  ALA A CB  
2113  N  N   . TYR A  275 ? 0.9404 1.8822 2.1815 0.6714  -0.2014 0.1127  275  TYR A N   
2114  C  CA  . TYR A  275 ? 0.9517 1.8922 2.1761 0.6793  -0.1959 0.1194  275  TYR A CA  
2115  C  C   . TYR A  275 ? 0.9580 1.8981 2.1850 0.6773  -0.1869 0.1450  275  TYR A C   
2116  O  O   . TYR A  275 ? 0.9514 1.9101 2.2190 0.6685  -0.1819 0.1509  275  TYR A O   
2117  C  CB  . TYR A  275 ? 0.9363 1.9123 2.2053 0.6721  -0.1935 0.1057  275  TYR A CB  
2118  C  CG  . TYR A  275 ? 0.9455 1.9015 2.2112 0.6780  -0.1984 0.1050  275  TYR A CG  
2119  C  CD1 . TYR A  275 ? 0.9487 1.8681 2.2251 0.6690  -0.2067 0.1036  275  TYR A CD1 
2120  C  CD2 . TYR A  275 ? 0.9565 1.9236 2.2107 0.6866  -0.1959 0.1058  275  TYR A CD2 
2121  C  CE1 . TYR A  275 ? 0.9598 1.8555 2.2408 0.6688  -0.2118 0.1094  275  TYR A CE1 
2122  C  CE2 . TYR A  275 ? 0.9642 1.9150 2.2273 0.6909  -0.2019 0.1058  275  TYR A CE2 
2123  C  CZ  . TYR A  275 ? 0.9655 1.8797 2.2424 0.6810  -0.2088 0.1117  275  TYR A CZ  
2124  O  OH  . TYR A  275 ? 0.9769 1.8708 2.2658 0.6792  -0.2130 0.1205  275  TYR A OH  
2125  N  N   . PHE A  276 ? 1.2654 2.1644 2.5013 0.6710  -0.1969 0.1554  276  PHE A N   
2126  C  CA  . PHE A  276 ? 1.1076 1.9740 2.3622 0.6746  -0.2218 0.1368  276  PHE A CA  
2127  C  C   . PHE A  276 ? 0.9993 1.8366 2.2424 0.6891  -0.2276 0.1285  276  PHE A C   
2128  O  O   . PHE A  276 ? 1.0198 1.8118 2.2316 0.6996  -0.2336 0.1314  276  PHE A O   
2129  C  CB  . PHE A  276 ? 0.9963 1.8343 2.2133 0.6868  -0.2364 0.1402  276  PHE A CB  
2130  C  CG  . PHE A  276 ? 1.1237 1.9557 2.3088 0.7115  -0.2473 0.1416  276  PHE A CG  
2131  C  CD1 . PHE A  276 ? 1.4543 2.3266 2.6387 0.7118  -0.2503 0.1374  276  PHE A CD1 
2132  C  CD2 . PHE A  276 ? 1.1763 1.9597 2.3114 0.7332  -0.2494 0.1505  276  PHE A CD2 
2133  C  CE1 . PHE A  276 ? 1.6126 2.4764 2.7521 0.7325  -0.2567 0.1452  276  PHE A CE1 
2134  C  CE2 . PHE A  276 ? 1.3255 2.0984 2.4149 0.7552  -0.2515 0.1588  276  PHE A CE2 
2135  C  CZ  . PHE A  276 ? 1.4481 2.2605 2.5416 0.7545  -0.2563 0.1571  276  PHE A CZ  
2136  N  N   . GLY A  277 ? 0.9975 1.8693 2.2607 0.6944  -0.2243 0.1220  277  GLY A N   
2137  C  CA  . GLY A  277 ? 1.0164 1.8809 2.2704 0.7129  -0.2221 0.1207  277  GLY A CA  
2138  C  C   . GLY A  277 ? 1.0010 1.8951 2.2929 0.7007  -0.2180 0.1075  277  GLY A C   
2139  O  O   . GLY A  277 ? 1.0157 1.9113 2.3012 0.7176  -0.2134 0.1094  277  GLY A O   
2140  N  N   . PHE A  278 ? 0.9748 1.8938 2.3070 0.6740  -0.2173 0.0989  278  PHE A N   
2141  C  CA  . PHE A  278 ? 0.9672 1.9181 2.3252 0.6680  -0.2216 0.0735  278  PHE A CA  
2142  C  C   . PHE A  278 ? 0.9698 1.9689 2.3518 0.6780  -0.2153 0.0821  278  PHE A C   
2143  O  O   . PHE A  278 ? 0.9746 1.9974 2.3621 0.6871  -0.2132 0.0760  278  PHE A O   
2144  C  CB  . PHE A  278 ? 0.9550 2.0188 2.2300 0.6841  -0.1715 0.1337  278  PHE A CB  
2145  C  CG  . PHE A  278 ? 0.9466 2.0532 2.2544 0.6823  -0.1832 0.1018  278  PHE A CG  
2146  C  CD1 . PHE A  278 ? 0.9441 2.0290 2.2718 0.6809  -0.1905 0.0928  278  PHE A CD1 
2147  C  CD2 . PHE A  278 ? 0.9349 2.0989 2.2878 0.6706  -0.1793 0.1107  278  PHE A CD2 
2148  C  CE1 . PHE A  278 ? 0.9315 2.0523 2.3181 0.6708  -0.1933 0.0904  278  PHE A CE1 
2149  C  CE2 . PHE A  278 ? 0.9245 2.1274 2.3275 0.6625  -0.1876 0.0943  278  PHE A CE2 
2150  C  CZ  . PHE A  278 ? 0.9219 2.1020 2.3456 0.6617  -0.1929 0.0878  278  PHE A CZ  
2151  N  N   . SER A  279 ? 1.1424 2.1682 2.5342 0.6804  -0.2137 0.0945  279  SER A N   
2152  C  CA  . SER A  279 ? 0.9753 2.0515 2.3863 0.6938  -0.2130 0.0981  279  SER A CA  
2153  C  C   . SER A  279 ? 0.9986 2.0644 2.3727 0.7159  -0.2139 0.1112  279  SER A C   
2154  O  O   . SER A  279 ? 0.9983 2.0449 2.3506 0.7136  -0.2194 0.1142  279  SER A O   
2155  C  CB  . SER A  279 ? 0.9557 2.0924 2.4169 0.6731  -0.2170 0.0932  279  SER A CB  
2156  O  OG  . SER A  279 ? 0.9466 2.0913 2.4057 0.6644  -0.2200 0.0995  279  SER A OG  
2157  N  N   . VAL A  280 ? 1.0262 2.1048 2.3840 0.7367  -0.2062 0.1203  280  VAL A N   
2158  C  CA  . VAL A  280 ? 1.0608 2.1278 2.3761 0.7597  -0.2057 0.1333  280  VAL A CA  
2159  C  C   . VAL A  280 ? 1.0733 2.2001 2.4137 0.7693  -0.2031 0.1394  280  VAL A C   
2160  O  O   . VAL A  280 ? 1.0623 2.2313 2.4423 0.7631  -0.1972 0.1363  280  VAL A O   
2161  C  CB  . VAL A  280 ? 1.0975 2.1013 2.3547 0.7846  -0.1957 0.1432  280  VAL A CB  
2162  C  CG1 . VAL A  280 ? 1.0909 2.0388 2.3191 0.7763  -0.2028 0.1410  280  VAL A CG1 
2163  C  CG2 . VAL A  280 ? 1.1055 2.1129 2.3695 0.7932  -0.1802 0.1447  280  VAL A CG2 
2164  N  N   . ALA A  281 ? 1.0986 2.2324 2.4169 0.7851  -0.2091 0.1495  281  ALA A N   
2165  C  CA  . ALA A  281 ? 1.1166 2.3073 2.4573 0.7975  -0.2091 0.1585  281  ALA A CA  
2166  C  C   . ALA A  281 ? 1.1616 2.3265 2.4567 0.8272  -0.2113 0.1734  281  ALA A C   
2167  O  O   . ALA A  281 ? 1.1708 2.2895 2.4249 0.8303  -0.2192 0.1754  281  ALA A O   
2168  C  CB  . ALA A  281 ? 1.0890 2.3487 2.4793 0.7736  -0.2245 0.1529  281  ALA A CB  
2169  N  N   . ALA A  282 ? 1.1930 2.3890 2.4966 0.8505  -0.2043 0.1848  282  ALA A N   
2170  C  CA  . ALA A  282 ? 1.2433 2.4157 2.5084 0.8831  -0.2062 0.2001  282  ALA A CA  
2171  C  C   . ALA A  282 ? 1.2578 2.5022 2.5603 0.8918  -0.2144 0.2111  282  ALA A C   
2172  O  O   . ALA A  282 ? 1.2631 2.5544 2.6015 0.8990  -0.2024 0.2141  282  ALA A O   
2173  C  CB  . ALA A  282 ? 1.2853 2.4035 2.5104 0.9143  -0.1849 0.2054  282  ALA A CB  
2174  N  N   . THR A  283 ? 1.3521 2.6094 2.6463 0.8915  -0.2356 0.2188  283  THR A N   
2175  C  CA  . THR A  283 ? 1.5111 2.8337 2.8352 0.9021  -0.2481 0.2327  283  THR A CA  
2176  C  C   . THR A  283 ? 1.5527 2.8547 2.8393 0.9146  -0.2686 0.2458  283  THR A C   
2177  O  O   . THR A  283 ? 1.6426 2.9129 2.8999 0.8991  -0.2787 0.2401  283  THR A O   
2178  C  CB  . THR A  283 ? 1.3529 2.7580 2.7367 0.8698  -0.2594 0.2255  283  THR A CB  
2179  O  OG1 . THR A  283 ? 1.6288 3.0985 3.0380 0.8788  -0.2763 0.2413  283  THR A OG1 
2180  C  CG2 . THR A  283 ? 1.2063 2.6049 2.5852 0.8370  -0.2729 0.2114  283  THR A CG2 
2181  N  N   . ASP A  284 ? 1.6631 2.9857 2.9519 0.9438  -0.2748 0.2647  284  ASP A N   
2182  C  CA  . ASP A  284 ? 1.5130 2.8224 2.7694 0.9583  -0.2972 0.2815  284  ASP A CA  
2183  C  C   . ASP A  284 ? 1.4842 2.8606 2.7651 0.9290  -0.3230 0.2817  284  ASP A C   
2184  O  O   . ASP A  284 ? 1.8774 3.3311 3.2075 0.9213  -0.3316 0.2859  284  ASP A O   
2185  C  CB  . ASP A  284 ? 1.7751 3.0914 3.0346 0.9992  -0.2969 0.3023  284  ASP A CB  
2186  C  CG  . ASP A  284 ? 1.8491 3.1526 3.0773 1.0156  -0.3228 0.3230  284  ASP A CG  
2187  O  OD1 . ASP A  284 ? 1.7915 3.0451 2.9726 1.0068  -0.3326 0.3221  284  ASP A OD1 
2188  O  OD2 . ASP A  284 ? 1.6571 3.0025 2.9087 1.0374  -0.3343 0.3417  284  ASP A OD2 
2189  N  N   . ILE A  285 ? 1.3568 2.7082 2.6030 0.9128  -0.3358 0.2776  285  ILE A N   
2190  C  CA  . ILE A  285 ? 1.3285 2.7436 2.5927 0.8831  -0.3576 0.2737  285  ILE A CA  
2191  C  C   . ILE A  285 ? 1.3691 2.8031 2.6072 0.8951  -0.3855 0.2961  285  ILE A C   
2192  O  O   . ILE A  285 ? 1.3573 2.8607 2.6138 0.8741  -0.4067 0.2972  285  ILE A O   
2193  C  CB  . ILE A  285 ? 1.2823 2.6741 2.5326 0.8540  -0.3526 0.2519  285  ILE A CB  
2194  C  CG1 . ILE A  285 ? 1.2427 2.7121 2.5334 0.8191  -0.3647 0.2380  285  ILE A CG1 
2195  C  CG2 . ILE A  285 ? 1.3033 2.6442 2.4938 0.8624  -0.3623 0.2596  285  ILE A CG2 
2196  C  CD1 . ILE A  285 ? 1.2143 2.7232 2.5631 0.8043  -0.3528 0.2264  285  ILE A CD1 
2197  N  N   . ASN A  286 ? 1.4207 2.7952 2.6146 0.9275  -0.3877 0.3146  286  ASN A N   
2198  C  CA  . ASN A  286 ? 1.4652 2.8465 2.6273 0.9397  -0.4157 0.3387  286  ASN A CA  
2199  C  C   . ASN A  286 ? 1.5268 2.9094 2.6966 0.9769  -0.4227 0.3640  286  ASN A C   
2200  O  O   . ASN A  286 ? 1.5792 2.9380 2.7126 0.9967  -0.4429 0.3876  286  ASN A O   
2201  C  CB  . ASN A  286 ? 1.4807 2.7871 2.5781 0.9445  -0.4181 0.3419  286  ASN A CB  
2202  C  CG  . ASN A  286 ? 1.5041 2.7195 2.5727 0.9695  -0.3950 0.3399  286  ASN A CG  
2203  O  OD1 . ASN A  286 ? 1.4873 2.6961 2.5839 0.9729  -0.3713 0.3264  286  ASN A OD1 
2204  N  ND2 . ASN A  286 ? 1.5519 2.6974 2.5614 0.9867  -0.4030 0.3543  286  ASN A ND2 
2205  N  N   . GLY A  287 ? 1.5247 2.9368 2.7425 0.9872  -0.4070 0.3605  287  GLY A N   
2206  C  CA  . GLY A  287 ? 1.5809 3.0108 2.8188 1.0225  -0.4124 0.3828  287  GLY A CA  
2207  C  C   . GLY A  287 ? 1.6476 2.9925 2.8381 1.0644  -0.4088 0.3990  287  GLY A C   
2208  O  O   . GLY A  287 ? 1.9621 3.3104 3.1444 1.0886  -0.4307 0.4248  287  GLY A O   
2209  N  N   . ASP A  288 ? 1.7207 2.9875 2.8789 1.0738  -0.3830 0.3852  288  ASP A N   
2210  C  CA  . ASP A  288 ? 1.7901 2.9702 2.9011 1.1142  -0.3774 0.3983  288  ASP A CA  
2211  C  C   . ASP A  288 ? 1.8069 2.9582 2.9290 1.1402  -0.3436 0.3874  288  ASP A C   
2212  O  O   . ASP A  288 ? 1.8666 2.9392 2.9463 1.1741  -0.3341 0.3937  288  ASP A O   
2213  C  CB  . ASP A  288 ? 1.8958 2.9947 2.9384 1.1050  -0.3831 0.3968  288  ASP A CB  
2214  C  CG  . ASP A  288 ? 1.9268 3.0170 2.9663 1.0695  -0.3661 0.3692  288  ASP A CG  
2215  O  OD1 . ASP A  288 ? 2.0091 3.1671 3.0981 1.0420  -0.3596 0.3530  288  ASP A OD1 
2216  O  OD2 . ASP A  288 ? 1.7314 2.7453 2.7190 1.0691  -0.3608 0.3648  288  ASP A OD2 
2217  N  N   . ASP A  289 ? 1.7195 2.9330 2.8951 1.1258  -0.3258 0.3723  289  ASP A N   
2218  C  CA  . ASP A  289 ? 1.7299 2.9328 2.9204 1.1465  -0.2925 0.3617  289  ASP A CA  
2219  C  C   . ASP A  289 ? 1.8361 2.9541 2.9757 1.1430  -0.2706 0.3442  289  ASP A C   
2220  O  O   . ASP A  289 ? 1.7452 2.8374 2.8800 1.1659  -0.2427 0.3371  289  ASP A O   
2221  C  CB  . ASP A  289 ? 1.8087 3.0051 3.0061 1.1978  -0.2871 0.3796  289  ASP A CB  
2222  C  CG  . ASP A  289 ? 1.8196 3.1070 3.0745 1.2031  -0.3085 0.3983  289  ASP A CG  
2223  O  OD1 . ASP A  289 ? 1.9426 3.2297 3.1837 1.2055  -0.3394 0.4173  289  ASP A OD1 
2224  O  OD2 . ASP A  289 ? 1.8044 3.1662 3.1179 1.2041  -0.2955 0.3956  289  ASP A OD2 
2225  N  N   . TYR A  290 ? 1.9424 3.0194 3.0433 1.1160  -0.2826 0.3380  290  TYR A N   
2226  C  CA  . TYR A  290 ? 1.8169 2.8243 2.8759 1.1050  -0.2657 0.3212  290  TYR A CA  
2227  C  C   . TYR A  290 ? 1.5910 2.6440 2.6837 1.0595  -0.2627 0.3015  290  TYR A C   
2228  O  O   . TYR A  290 ? 1.5526 2.6384 2.6552 1.0301  -0.2829 0.3003  290  TYR A O   
2229  C  CB  . TYR A  290 ? 1.7463 2.6724 2.7381 1.1093  -0.2813 0.3297  290  TYR A CB  
2230  C  CG  . TYR A  290 ? 1.7963 2.6511 2.7432 1.1555  -0.2793 0.3456  290  TYR A CG  
2231  C  CD1 . TYR A  290 ? 1.8381 2.6652 2.7809 1.1881  -0.2519 0.3404  290  TYR A CD1 
2232  C  CD2 . TYR A  290 ? 1.8454 2.6600 2.7525 1.1677  -0.3047 0.3662  290  TYR A CD2 
2233  C  CE1 . TYR A  290 ? 1.9281 2.6858 2.8285 1.2325  -0.2491 0.3529  290  TYR A CE1 
2234  C  CE2 . TYR A  290 ? 1.9349 2.6777 2.8004 1.2102  -0.3043 0.3809  290  TYR A CE2 
2235  C  CZ  . TYR A  290 ? 1.9769 2.6899 2.8395 1.2431  -0.2760 0.3731  290  TYR A CZ  
2236  O  OH  . TYR A  290 ? 2.1308 2.7676 2.9502 1.2877  -0.2748 0.3861  290  TYR A OH  
2237  N  N   . ALA A  291 ? 1.5803 2.6363 2.6902 1.0552  -0.2376 0.2867  291  ALA A N   
2238  C  CA  . ALA A  291 ? 1.5090 2.5976 2.6493 1.0143  -0.2340 0.2683  291  ALA A CA  
2239  C  C   . ALA A  291 ? 1.4830 2.5214 2.5849 0.9906  -0.2444 0.2607  291  ALA A C   
2240  O  O   . ALA A  291 ? 1.5244 2.4861 2.5699 1.0065  -0.2428 0.2646  291  ALA A O   
2241  C  CB  . ALA A  291 ? 1.5013 2.5871 2.6544 1.0183  -0.2055 0.2571  291  ALA A CB  
2242  N  N   . ASP A  292 ? 1.7879 2.8715 2.9214 0.9533  -0.2551 0.2498  292  ASP A N   
2243  C  CA  . ASP A  292 ? 1.6247 2.6782 2.7325 0.9296  -0.2656 0.2423  292  ASP A CA  
2244  C  C   . ASP A  292 ? 1.3466 2.4009 2.4780 0.9005  -0.2531 0.2219  292  ASP A C   
2245  O  O   . ASP A  292 ? 1.5695 2.6724 2.7494 0.8880  -0.2446 0.2134  292  ASP A O   
2246  C  CB  . ASP A  292 ? 1.6227 2.7290 2.7438 0.9133  -0.2899 0.2470  292  ASP A CB  
2247  C  CG  . ASP A  292 ? 2.0081 3.1203 3.1106 0.9416  -0.3058 0.2702  292  ASP A CG  
2248  O  OD1 . ASP A  292 ? 2.1413 3.1872 3.1964 0.9707  -0.3038 0.2826  292  ASP A OD1 
2249  O  OD2 . ASP A  292 ? 2.0227 3.2040 3.1573 0.9354  -0.3215 0.2769  292  ASP A OD2 
2250  N  N   . VAL A  293 ? 1.3185 2.3204 2.4171 0.8898  -0.2538 0.2158  293  VAL A N   
2251  C  CA  . VAL A  293 ? 1.2775 2.2656 2.3916 0.8671  -0.2426 0.1995  293  VAL A CA  
2252  C  C   . VAL A  293 ? 1.3976 2.4250 2.5439 0.8330  -0.2532 0.1867  293  VAL A C   
2253  O  O   . VAL A  293 ? 1.3573 2.3802 2.4816 0.8281  -0.2667 0.1893  293  VAL A O   
2254  C  CB  . VAL A  293 ? 1.4897 2.3961 2.5498 0.8783  -0.2366 0.2018  293  VAL A CB  
2255  C  CG1 . VAL A  293 ? 1.5285 2.4236 2.6073 0.8554  -0.2277 0.1874  293  VAL A CG1 
2256  C  CG2 . VAL A  293 ? 1.3610 2.2264 2.3852 0.9152  -0.2243 0.2130  293  VAL A CG2 
2257  N  N   . PHE A  294 ? 1.3031 2.3684 2.5000 0.8110  -0.2465 0.1730  294  PHE A N   
2258  C  CA  . PHE A  294 ? 1.2139 2.3140 2.4462 0.7799  -0.2528 0.1585  294  PHE A CA  
2259  C  C   . PHE A  294 ? 1.0841 2.1509 2.3290 0.7647  -0.2419 0.1469  294  PHE A C   
2260  O  O   . PHE A  294 ? 1.2907 2.3596 2.5577 0.7649  -0.2312 0.1438  294  PHE A O   
2261  C  CB  . PHE A  294 ? 1.0930 2.2696 2.3784 0.7668  -0.2578 0.1540  294  PHE A CB  
2262  C  CG  . PHE A  294 ? 1.1195 2.3370 2.3973 0.7797  -0.2722 0.1669  294  PHE A CG  
2263  C  CD1 . PHE A  294 ? 1.2844 2.5070 2.5571 0.8051  -0.2695 0.1815  294  PHE A CD1 
2264  C  CD2 . PHE A  294 ? 1.1119 2.3666 2.3881 0.7679  -0.2885 0.1649  294  PHE A CD2 
2265  C  CE1 . PHE A  294 ? 1.2647 2.5254 2.5338 0.8181  -0.2847 0.1960  294  PHE A CE1 
2266  C  CE2 . PHE A  294 ? 1.3303 2.6252 2.5982 0.7797  -0.3048 0.1790  294  PHE A CE2 
2267  C  CZ  . PHE A  294 ? 1.5008 2.7970 2.7666 0.8047  -0.3038 0.1957  294  PHE A CZ  
2268  N  N   . ILE A  295 ? 1.0690 2.1092 2.3007 0.7528  -0.2454 0.1418  295  ILE A N   
2269  C  CA  . ILE A  295 ? 1.3448 2.3501 2.5867 0.7397  -0.2379 0.1341  295  ILE A CA  
2270  C  C   . ILE A  295 ? 1.2769 2.3170 2.5632 0.7127  -0.2391 0.1218  295  ILE A C   
2271  O  O   . ILE A  295 ? 1.4760 2.5315 2.7526 0.7074  -0.2458 0.1193  295  ILE A O   
2272  C  CB  . ILE A  295 ? 1.5491 2.4897 2.7378 0.7516  -0.2397 0.1421  295  ILE A CB  
2273  C  CG1 . ILE A  295 ? 1.7277 2.6321 2.8682 0.7821  -0.2365 0.1562  295  ILE A CG1 
2274  C  CG2 . ILE A  295 ? 1.0502 1.9589 2.2522 0.7386  -0.2347 0.1365  295  ILE A CG2 
2275  C  CD1 . ILE A  295 ? 1.8632 2.7034 2.9440 0.7970  -0.2414 0.1670  295  ILE A CD1 
2276  N  N   . GLY A  296 ? 0.9822 2.0355 2.3150 0.6977  -0.2318 0.1150  296  GLY A N   
2277  C  CA  . GLY A  296 ? 0.9505 2.0346 2.3238 0.6750  -0.2274 0.1094  296  GLY A CA  
2278  C  C   . GLY A  296 ? 0.9439 1.9840 2.3014 0.6653  -0.2177 0.1133  296  GLY A C   
2279  O  O   . GLY A  296 ? 0.9541 1.9467 2.2960 0.6683  -0.2151 0.1167  296  GLY A O   
2280  N  N   . ALA A  297 ? 1.1431 2.2069 2.5031 0.6573  -0.2142 0.1104  297  ALA A N   
2281  C  CA  . ALA A  297 ? 0.9227 1.9669 2.2647 0.6532  -0.2033 0.1146  297  ALA A CA  
2282  C  C   . ALA A  297 ? 0.9041 2.0012 2.2729 0.6467  -0.1981 0.0956  297  ALA A C   
2283  O  O   . ALA A  297 ? 0.8997 2.0127 2.2751 0.6412  -0.2025 0.0754  297  ALA A O   
2284  C  CB  . ALA A  297 ? 0.9296 1.9479 2.2478 0.6584  -0.2131 0.1139  297  ALA A CB  
2285  N  N   . PRO A  298 ? 0.8997 2.0164 2.2834 0.6447  -0.1924 0.0918  298  PRO A N   
2286  C  CA  . PRO A  298 ? 0.8919 2.0445 2.3129 0.6320  -0.1961 0.0599  298  PRO A CA  
2287  C  C   . PRO A  298 ? 0.8914 2.0231 2.3185 0.6250  -0.1954 0.0365  298  PRO A C   
2288  O  O   . PRO A  298 ? 0.8901 2.0432 2.3537 0.6136  -0.1982 0.0053  298  PRO A O   
2289  C  CB  . PRO A  298 ? 0.8918 2.0565 2.3287 0.6315  -0.1944 0.0629  298  PRO A CB  
2290  C  CG  . PRO A  298 ? 0.9099 2.0597 2.3143 0.6442  -0.1878 0.0957  298  PRO A CG  
2291  C  CD  . PRO A  298 ? 0.9107 2.0086 2.2733 0.6504  -0.1855 0.1082  298  PRO A CD  
2292  N  N   . LEU A  299 ? 1.0531 2.1446 2.4497 0.6316  -0.1927 0.0493  299  LEU A N   
2293  C  CA  . LEU A  299 ? 0.8960 1.9674 2.3044 0.6249  -0.1924 0.0322  299  LEU A CA  
2294  C  C   . LEU A  299 ? 0.8943 1.9709 2.2932 0.6258  -0.1933 0.0311  299  LEU A C   
2295  O  O   . LEU A  299 ? 1.3731 2.4377 2.7809 0.6221  -0.1922 0.0221  299  LEU A O   
2296  C  CB  . LEU A  299 ? 0.9032 1.9305 2.2918 0.6288  -0.1938 0.0448  299  LEU A CB  
2297  C  CG  . LEU A  299 ? 0.9308 1.9515 2.3281 0.6285  -0.1950 0.0483  299  LEU A CG  
2298  C  CD1 . LEU A  299 ? 0.9169 1.8918 2.3004 0.6296  -0.2001 0.0577  299  LEU A CD1 
2299  C  CD2 . LEU A  299 ? 0.9047 1.9475 2.3564 0.6151  -0.1960 0.0236  299  LEU A CD2 
2300  N  N   . PHE A  300 ? 0.8938 1.9889 2.2797 0.6300  -0.1970 0.0407  300  PHE A N   
2301  C  CA  . PHE A  300 ? 0.8943 1.9983 2.2747 0.6300  -0.2019 0.0372  300  PHE A CA  
2302  C  C   . PHE A  300 ? 0.8905 2.0290 2.3074 0.6202  -0.1986 0.0014  300  PHE A C   
2303  O  O   . PHE A  300 ? 0.8902 2.0606 2.3332 0.6147  -0.1981 -0.0235 300  PHE A O   
2304  C  CB  . PHE A  300 ? 0.9002 2.0182 2.2650 0.6355  -0.2119 0.0462  300  PHE A CB  
2305  C  CG  . PHE A  300 ? 0.9060 2.0325 2.2564 0.6378  -0.2217 0.0425  300  PHE A CG  
2306  C  CD1 . PHE A  300 ? 0.9167 2.0032 2.2358 0.6462  -0.2300 0.0656  300  PHE A CD1 
2307  C  CD2 . PHE A  300 ? 0.9044 2.0824 2.2705 0.6325  -0.2240 0.0134  300  PHE A CD2 
2308  C  CE1 . PHE A  300 ? 0.9255 2.0242 2.2277 0.6495  -0.2421 0.0626  300  PHE A CE1 
2309  C  CE2 . PHE A  300 ? 0.9112 2.1077 2.2601 0.6359  -0.2330 0.0108  300  PHE A CE2 
2310  C  CZ  . PHE A  300 ? 0.9215 2.0788 2.2380 0.6444  -0.2427 0.0370  300  PHE A CZ  
2311  N  N   . MET A  301 ? 0.8898 2.0258 2.3114 0.6187  -0.1968 -0.0027 301  MET A N   
2312  C  CA  . MET A  301 ? 0.8894 2.0607 2.3477 0.6120  -0.1901 -0.0367 301  MET A CA  
2313  C  C   . MET A  301 ? 0.8899 2.0987 2.3386 0.6134  -0.1964 -0.0422 301  MET A C   
2314  O  O   . MET A  301 ? 0.8906 2.0836 2.3141 0.6178  -0.2049 -0.0178 301  MET A O   
2315  C  CB  . MET A  301 ? 0.8904 2.0409 2.3683 0.6098  -0.1825 -0.0376 301  MET A CB  
2316  C  CG  . MET A  301 ? 0.8942 2.0029 2.3713 0.6100  -0.1817 -0.0280 301  MET A CG  
2317  S  SD  . MET A  301 ? 0.9000 1.9909 2.4019 0.6082  -0.1774 -0.0297 301  MET A SD  
2318  C  CE  . MET A  301 ? 0.9075 2.0381 2.4665 0.6055  -0.1628 -0.0747 301  MET A CE  
2319  N  N   . ASP A  302 ? 0.8932 2.1539 2.3577 0.6105  -0.1950 -0.0755 302  ASP A N   
2320  C  CA  . ASP A  302 ? 1.0163 2.3256 2.4693 0.6121  -0.2001 -0.0858 302  ASP A CA  
2321  C  C   . ASP A  302 ? 1.1689 2.5189 2.6612 0.6065  -0.1839 -0.1215 302  ASP A C   
2322  O  O   . ASP A  302 ? 1.2317 2.5701 2.7601 0.6034  -0.1702 -0.1419 302  ASP A O   
2323  C  CB  . ASP A  302 ? 1.0943 2.4465 2.5228 0.6153  -0.2124 -0.0942 302  ASP A CB  
2324  C  CG  . ASP A  302 ? 1.0755 2.4795 2.5334 0.6088  -0.2057 -0.1391 302  ASP A CG  
2325  O  OD1 . ASP A  302 ? 1.2267 2.6100 2.7204 0.6040  -0.1948 -0.1568 302  ASP A OD1 
2326  O  OD2 . ASP A  302 ? 0.9428 2.4105 2.3859 0.6090  -0.2130 -0.1570 302  ASP A OD2 
2327  N  N   . ARG A  303 ? 1.2894 2.6914 2.7729 0.6068  -0.1849 -0.1294 303  ARG A N   
2328  C  CA  . ARG A  303 ? 1.2322 2.6860 2.7518 0.6022  -0.1657 -0.1635 303  ARG A CA  
2329  C  C   . ARG A  303 ? 1.3313 2.8371 2.8435 0.5949  -0.1571 -0.2044 303  ARG A C   
2330  O  O   . ARG A  303 ? 1.4083 2.9243 2.8672 0.5873  -0.1689 -0.1953 303  ARG A O   
2331  C  CB  . ARG A  303 ? 1.3531 2.8279 2.8492 0.5949  -0.1659 -0.1433 303  ARG A CB  
2332  C  CG  . ARG A  303 ? 1.3284 2.8472 2.8561 0.5847  -0.1400 -0.1697 303  ARG A CG  
2333  C  CD  . ARG A  303 ? 1.2515 2.7503 2.8495 0.5953  -0.1297 -0.1772 303  ARG A CD  
2334  N  NE  . ARG A  303 ? 1.3837 2.8487 2.9833 0.5935  -0.1408 -0.1357 303  ARG A NE  
2335  C  CZ  . ARG A  303 ? 1.6923 3.1282 3.3281 0.5928  -0.1322 -0.1248 303  ARG A CZ  
2336  N  NH1 . ARG A  303 ? 1.7868 3.2187 3.4583 0.5963  -0.1117 -0.1518 303  ARG A NH1 
2337  N  NH2 . ARG A  303 ? 1.7361 3.1492 3.3704 0.5898  -0.1463 -0.0874 303  ARG A NH2 
2338  N  N   . GLY A  304 ? 1.3628 2.8892 2.9194 0.5937  -0.1356 -0.2463 304  GLY A N   
2339  C  CA  . GLY A  304 ? 1.5845 3.1452 3.1206 0.5797  -0.1233 -0.2866 304  GLY A CA  
2340  C  C   . GLY A  304 ? 1.6298 3.2349 3.1251 0.5613  -0.1052 -0.2962 304  GLY A C   
2341  O  O   . GLY A  304 ? 1.5002 3.1126 2.9879 0.5583  -0.1013 -0.2715 304  GLY A O   
2342  N  N   . SER A  305 ? 1.9232 3.5591 3.3891 0.5459  -0.0943 -0.3330 305  SER A N   
2343  C  CA  . SER A  305 ? 2.0407 3.7229 3.4621 0.5256  -0.0746 -0.3459 305  SER A CA  
2344  C  C   . SER A  305 ? 2.2777 3.9809 3.7495 0.5317  -0.0418 -0.3710 305  SER A C   
2345  O  O   . SER A  305 ? 2.3904 4.1309 3.8390 0.5184  -0.0255 -0.3650 305  SER A O   
2346  C  CB  . SER A  305 ? 2.0347 3.7424 3.4087 0.5063  -0.0717 -0.3814 305  SER A CB  
2347  O  OG  . SER A  305 ? 2.0624 3.7595 3.3951 0.5010  -0.1032 -0.3562 305  SER A OG  
2348  N  N   . ASP A  306 ? 2.3939 4.0753 3.9369 0.5517  -0.0325 -0.3966 306  ASP A N   
2349  C  CA  . ASP A  306 ? 2.1466 3.8465 3.7510 0.5641  -0.0020 -0.4221 306  ASP A CA  
2350  C  C   . ASP A  306 ? 1.8869 3.5773 3.5381 0.5771  -0.0085 -0.3815 306  ASP A C   
2351  O  O   . ASP A  306 ? 1.5654 3.2735 3.2787 0.5903  0.0134  -0.3958 306  ASP A O   
2352  C  CB  . ASP A  306 ? 2.0658 3.7397 3.7252 0.5810  0.0084  -0.4678 306  ASP A CB  
2353  C  CG  . ASP A  306 ? 2.1271 3.7480 3.7991 0.5887  -0.0226 -0.4521 306  ASP A CG  
2354  O  OD1 . ASP A  306 ? 2.0236 3.6225 3.6950 0.5935  -0.0471 -0.4041 306  ASP A OD1 
2355  O  OD2 . ASP A  306 ? 2.2172 3.8181 3.8976 0.5886  -0.0220 -0.4881 306  ASP A OD2 
2356  N  N   . GLY A  307 ? 1.9057 3.5680 3.5290 0.5743  -0.0384 -0.3319 307  GLY A N   
2357  C  CA  . GLY A  307 ? 1.7206 3.3668 3.3785 0.5828  -0.0489 -0.2922 307  GLY A CA  
2358  C  C   . GLY A  307 ? 1.7695 3.3501 3.4707 0.5989  -0.0614 -0.2784 307  GLY A C   
2359  O  O   . GLY A  307 ? 1.8335 3.3778 3.5411 0.5978  -0.0710 -0.2368 307  GLY A O   
2360  N  N   . LYS A  308 ? 1.9394 3.4858 3.6477 0.6039  -0.0599 -0.3039 308  LYS A N   
2361  C  CA  . LYS A  308 ? 1.7994 3.2649 3.5183 0.6083  -0.0691 -0.2817 308  LYS A CA  
2362  C  C   . LYS A  308 ? 1.5660 2.9886 3.2421 0.6046  -0.0967 -0.2483 308  LYS A C   
2363  O  O   . LYS A  308 ? 1.2153 2.6642 2.8644 0.6021  -0.1071 -0.2602 308  LYS A O   
2364  C  CB  . LYS A  308 ? 1.7414 3.1937 3.4948 0.6156  -0.0536 -0.3276 308  LYS A CB  
2365  C  CG  . LYS A  308 ? 1.6561 3.0354 3.4299 0.6215  -0.0583 -0.3087 308  LYS A CG  
2366  C  CD  . LYS A  308 ? 1.3034 2.6681 3.1117 0.6292  -0.0473 -0.3579 308  LYS A CD  
2367  C  CE  . LYS A  308 ? 1.6507 3.0600 3.4960 0.6388  -0.0159 -0.4052 308  LYS A CE  
2368  N  NZ  . LYS A  308 ? 1.6964 3.1020 3.5683 0.6466  -0.0029 -0.3805 308  LYS A NZ  
2369  N  N   . LEU A  309 ? 1.4677 2.8297 3.1360 0.6051  -0.1079 -0.2063 309  LEU A N   
2370  C  CA  . LEU A  309 ? 1.3374 2.6552 2.9663 0.6034  -0.1287 -0.1748 309  LEU A CA  
2371  C  C   . LEU A  309 ? 1.2761 2.5788 2.9124 0.6036  -0.1303 -0.1991 309  LEU A C   
2372  O  O   . LEU A  309 ? 1.4067 2.7040 3.0805 0.6063  -0.1184 -0.2304 309  LEU A O   
2373  C  CB  . LEU A  309 ? 1.4194 2.6825 3.0375 0.6041  -0.1366 -0.1320 309  LEU A CB  
2374  C  CG  . LEU A  309 ? 1.5525 2.8265 3.1608 0.6022  -0.1426 -0.1028 309  LEU A CG  
2375  C  CD1 . LEU A  309 ? 1.5539 2.7797 3.1556 0.6031  -0.1504 -0.0708 309  LEU A CD1 
2376  C  CD2 . LEU A  309 ? 1.0583 2.3406 2.6244 0.6013  -0.1591 -0.0851 309  LEU A CD2 
2377  N  N   . GLN A  310 ? 0.9531 2.2506 2.5569 0.6015  -0.1459 -0.1850 310  GLN A N   
2378  C  CA  . GLN A  310 ? 0.9593 2.2454 2.5730 0.5996  -0.1513 -0.2013 310  GLN A CA  
2379  C  C   . GLN A  310 ? 1.0659 2.3212 2.6427 0.5991  -0.1667 -0.1606 310  GLN A C   
2380  O  O   . GLN A  310 ? 0.9387 2.2064 2.4800 0.6010  -0.1759 -0.1382 310  GLN A O   
2381  C  CB  . GLN A  310 ? 1.0272 2.3741 2.6533 0.5973  -0.1509 -0.2482 310  GLN A CB  
2382  C  CG  . GLN A  310 ? 1.0853 2.4846 2.6763 0.5972  -0.1587 -0.2433 310  GLN A CG  
2383  C  CD  . GLN A  310 ? 1.1124 2.5790 2.7074 0.5938  -0.1631 -0.2868 310  GLN A CD  
2384  O  OE1 . GLN A  310 ? 1.4031 2.8852 3.0351 0.5919  -0.1540 -0.3325 310  GLN A OE1 
2385  N  NE2 . GLN A  310 ? 0.9704 2.4776 2.5248 0.5929  -0.1780 -0.2730 310  GLN A NE2 
2386  N  N   . GLU A  311 ? 0.9136 2.1292 2.4998 0.5978  -0.1689 -0.1517 311  GLU A N   
2387  C  CA  . GLU A  311 ? 0.9051 2.0971 2.4611 0.5982  -0.1792 -0.1171 311  GLU A CA  
2388  C  C   . GLU A  311 ? 0.9049 2.1360 2.4642 0.5948  -0.1886 -0.1312 311  GLU A C   
2389  O  O   . GLU A  311 ? 0.9128 2.1572 2.5082 0.5891  -0.1906 -0.1613 311  GLU A O   
2390  C  CB  . GLU A  311 ? 0.9097 2.0562 2.4774 0.5972  -0.1789 -0.1066 311  GLU A CB  
2391  C  CG  . GLU A  311 ? 0.9440 2.0740 2.4830 0.5986  -0.1864 -0.0745 311  GLU A CG  
2392  C  CD  . GLU A  311 ? 0.9195 2.0138 2.4763 0.5958  -0.1882 -0.0708 311  GLU A CD  
2393  O  OE1 . GLU A  311 ? 1.3877 2.4606 2.9747 0.5940  -0.1850 -0.0869 311  GLU A OE1 
2394  O  OE2 . GLU A  311 ? 0.9070 1.9969 2.4512 0.5960  -0.1931 -0.0519 311  GLU A OE2 
2395  N  N   . VAL A  312 ? 0.8987 2.1483 2.4232 0.5985  -0.1967 -0.1095 312  VAL A N   
2396  C  CA  . VAL A  312 ? 0.9776 2.2708 2.5031 0.5959  -0.2085 -0.1181 312  VAL A CA  
2397  C  C   . VAL A  312 ? 0.8955 2.1742 2.3922 0.6015  -0.2150 -0.0761 312  VAL A C   
2398  O  O   . VAL A  312 ? 0.8970 2.2099 2.4020 0.5987  -0.2248 -0.0773 312  VAL A O   
2399  C  CB  . VAL A  312 ? 1.0232 2.3722 2.5389 0.5965  -0.2145 -0.1410 312  VAL A CB  
2400  C  CG1 . VAL A  312 ? 0.9138 2.2900 2.4646 0.5916  -0.2048 -0.1907 312  VAL A CG1 
2401  C  CG2 . VAL A  312 ? 0.9944 2.3297 2.4699 0.6050  -0.2157 -0.1115 312  VAL A CG2 
2402  N  N   . GLY A  313 ? 0.8922 2.1256 2.3582 0.6096  -0.2102 -0.0401 313  GLY A N   
2403  C  CA  . GLY A  313 ? 1.0706 2.2885 2.5116 0.6177  -0.2132 -0.0035 313  GLY A CA  
2404  C  C   . GLY A  313 ? 0.9334 2.1669 2.3479 0.6251  -0.2243 0.0066  313  GLY A C   
2405  O  O   . GLY A  313 ? 0.9046 2.1830 2.3215 0.6223  -0.2326 -0.0172 313  GLY A O   
2406  N  N   . GLN A  314 ? 0.9070 2.1042 2.2941 0.6359  -0.2261 0.0386  314  GLN A N   
2407  C  CA  . GLN A  314 ? 0.9233 2.1242 2.2784 0.6465  -0.2398 0.0473  314  GLN A CA  
2408  C  C   . GLN A  314 ? 1.1896 2.3639 2.5324 0.6575  -0.2430 0.0714  314  GLN A C   
2409  O  O   . GLN A  314 ? 1.3568 2.4879 2.7035 0.6595  -0.2343 0.0860  314  GLN A O   
2410  C  CB  . GLN A  314 ? 0.9305 2.1014 2.2547 0.6525  -0.2430 0.0523  314  GLN A CB  
2411  C  CG  . GLN A  314 ? 0.9540 2.1355 2.2363 0.6660  -0.2593 0.0604  314  GLN A CG  
2412  C  CD  . GLN A  314 ? 0.9648 2.1170 2.2145 0.6729  -0.2649 0.0692  314  GLN A CD  
2413  O  OE1 . GLN A  314 ? 0.9754 2.0696 2.2038 0.6809  -0.2655 0.0879  314  GLN A OE1 
2414  N  NE2 . GLN A  314 ? 1.5073 2.7045 2.7525 0.6700  -0.2702 0.0551  314  GLN A NE2 
2415  N  N   . VAL A  315 ? 0.9532 2.1566 2.2801 0.6661  -0.2559 0.0743  315  VAL A N   
2416  C  CA  . VAL A  315 ? 0.9747 2.1548 2.2830 0.6818  -0.2601 0.0935  315  VAL A CA  
2417  C  C   . VAL A  315 ? 1.0049 2.1695 2.2599 0.6998  -0.2722 0.1052  315  VAL A C   
2418  O  O   . VAL A  315 ? 1.0110 2.2187 2.2538 0.6994  -0.2834 0.1001  315  VAL A O   
2419  C  CB  . VAL A  315 ? 1.3855 2.6186 2.7244 0.6787  -0.2647 0.0927  315  VAL A CB  
2420  C  CG1 . VAL A  315 ? 1.2940 2.5091 2.6123 0.6988  -0.2682 0.1109  315  VAL A CG1 
2421  C  CG2 . VAL A  315 ? 1.2645 2.5106 2.6541 0.6621  -0.2536 0.0852  315  VAL A CG2 
2422  N  N   . SER A  316 ? 1.0439 2.1485 2.2644 0.7165  -0.2709 0.1210  316  SER A N   
2423  C  CA  . SER A  316 ? 1.0818 2.1628 2.2476 0.7375  -0.2824 0.1375  316  SER A CA  
2424  C  C   . SER A  316 ? 1.2572 2.3441 2.4119 0.7565  -0.2865 0.1520  316  SER A C   
2425  O  O   . SER A  316 ? 1.1136 2.1872 2.2851 0.7611  -0.2765 0.1533  316  SER A O   
2426  C  CB  . SER A  316 ? 1.0972 2.1074 2.2267 0.7466  -0.2800 0.1463  316  SER A CB  
2427  O  OG  . SER A  316 ? 1.6155 2.5843 2.7470 0.7534  -0.2693 0.1500  316  SER A OG  
2428  N  N   . VAL A  317 ? 1.1541 2.2651 2.2821 0.7684  -0.3015 0.1637  317  VAL A N   
2429  C  CA  . VAL A  317 ? 1.1577 2.2796 2.2767 0.7885  -0.3080 0.1803  317  VAL A CA  
2430  C  C   . VAL A  317 ? 1.2090 2.2698 2.2683 0.8162  -0.3143 0.2019  317  VAL A C   
2431  O  O   . VAL A  317 ? 1.2272 2.2847 2.2512 0.8200  -0.3285 0.2112  317  VAL A O   
2432  C  CB  . VAL A  317 ? 1.2311 2.4307 2.3669 0.7813  -0.3239 0.1805  317  VAL A CB  
2433  C  CG1 . VAL A  317 ? 1.2896 2.5059 2.4261 0.8012  -0.3312 0.1990  317  VAL A CG1 
2434  C  CG2 . VAL A  317 ? 1.1100 2.3655 2.2994 0.7529  -0.3189 0.1568  317  VAL A CG2 
2435  N  N   . SER A  318 ? 1.4623 2.4764 2.5089 0.8365  -0.3040 0.2103  318  SER A N   
2436  C  CA  . SER A  318 ? 1.7152 2.6603 2.7033 0.8654  -0.3075 0.2294  318  SER A CA  
2437  C  C   . SER A  318 ? 1.7289 2.6819 2.7134 0.8924  -0.3105 0.2456  318  SER A C   
2438  O  O   . SER A  318 ? 1.4660 2.4263 2.4763 0.9007  -0.2961 0.2419  318  SER A O   
2439  C  CB  . SER A  318 ? 1.4253 2.3031 2.3944 0.8701  -0.2921 0.2246  318  SER A CB  
2440  O  OG  . SER A  318 ? 1.3852 2.2594 2.3633 0.8455  -0.2913 0.2116  318  SER A OG  
2441  N  N   . LEU A  319 ? 1.6635 2.6178 2.6173 0.9070  -0.3298 0.2647  319  LEU A N   
2442  C  CA  . LEU A  319 ? 1.7733 2.7361 2.7249 0.9343  -0.3363 0.2831  319  LEU A CA  
2443  C  C   . LEU A  319 ? 1.8902 2.7666 2.7925 0.9687  -0.3295 0.2965  319  LEU A C   
2444  O  O   . LEU A  319 ? 1.7116 2.5259 2.5588 0.9771  -0.3393 0.3077  319  LEU A O   
2445  C  CB  . LEU A  319 ? 1.7905 2.7949 2.7313 0.9340  -0.3629 0.3001  319  LEU A CB  
2446  C  CG  . LEU A  319 ? 1.6758 2.7782 2.6681 0.9125  -0.3722 0.2933  319  LEU A CG  
2447  C  CD1 . LEU A  319 ? 1.6048 2.7450 2.6337 0.8773  -0.3617 0.2655  319  LEU A CD1 
2448  C  CD2 . LEU A  319 ? 1.7606 2.8970 2.7288 0.9137  -0.4007 0.3130  319  LEU A CD2 
2449  N  N   . GLN A  320 ? 1.9031 2.7762 2.8238 0.9888  -0.3128 0.2952  320  GLN A N   
2450  C  CA  . GLN A  320 ? 1.6160 2.4111 2.4919 1.0250  -0.3031 0.3051  320  GLN A CA  
2451  C  C   . GLN A  320 ? 1.6865 2.4595 2.5316 1.0544  -0.3221 0.3306  320  GLN A C   
2452  O  O   . GLN A  320 ? 1.6864 2.5218 2.5639 1.0559  -0.3358 0.3410  320  GLN A O   
2453  C  CB  . GLN A  320 ? 1.6171 2.4284 2.5258 1.0395  -0.2780 0.2957  320  GLN A CB  
2454  C  CG  . GLN A  320 ? 1.6918 2.4261 2.5544 1.0795  -0.2635 0.3022  320  GLN A CG  
2455  C  CD  . GLN A  320 ? 1.7089 2.4739 2.6068 1.0975  -0.2382 0.2948  320  GLN A CD  
2456  O  OE1 . GLN A  320 ? 1.8984 2.6147 2.7664 1.1345  -0.2236 0.2990  320  GLN A OE1 
2457  N  NE2 . GLN A  320 ? 1.6346 2.4807 2.5950 1.0725  -0.2328 0.2840  320  GLN A NE2 
2458  N  N   . ARG A  321 ? 2.0185 2.6991 2.7989 1.0776  -0.3248 0.3420  321  ARG A N   
2459  C  CA  . ARG A  321 ? 2.2195 2.8596 2.9636 1.1092  -0.3420 0.3676  321  ARG A CA  
2460  C  C   . ARG A  321 ? 2.0177 2.5790 2.7269 1.1496  -0.3246 0.3698  321  ARG A C   
2461  O  O   . ARG A  321 ? 2.0184 2.5317 2.7053 1.1513  -0.3040 0.3544  321  ARG A O   
2462  C  CB  . ARG A  321 ? 2.3396 2.9348 3.0280 1.0992  -0.3683 0.3842  321  ARG A CB  
2463  C  CG  . ARG A  321 ? 2.2286 2.9010 2.9450 1.0607  -0.3830 0.3796  321  ARG A CG  
2464  C  CD  . ARG A  321 ? 2.2137 2.9666 2.9688 1.0615  -0.3999 0.3925  321  ARG A CD  
2465  N  NE  . ARG A  321 ? 2.1306 2.9587 2.9058 1.0273  -0.4150 0.3885  321  ARG A NE  
2466  C  CZ  . ARG A  321 ? 1.9413 2.8453 2.7441 1.0212  -0.4335 0.3990  321  ARG A CZ  
2467  N  NH1 . ARG A  321 ? 1.8862 2.8023 2.7044 1.0468  -0.4407 0.4159  321  ARG A NH1 
2468  N  NH2 . ARG A  321 ? 1.7825 2.7534 2.5980 0.9899  -0.4451 0.3925  321  ARG A NH2 
2469  N  N   . ALA A  322 ? 2.0238 2.5722 2.7274 1.1835  -0.3338 0.3896  322  ALA A N   
2470  C  CA  . ALA A  322 ? 2.2950 2.7695 2.9660 1.2270  -0.3171 0.3917  322  ALA A CA  
2471  C  C   . ALA A  322 ? 2.3746 2.7286 2.9601 1.2344  -0.3196 0.3940  322  ALA A C   
2472  O  O   . ALA A  322 ? 2.4083 2.6929 2.9579 1.2613  -0.2986 0.3849  322  ALA A O   
2473  C  CB  . ALA A  322 ? 2.1541 2.6388 2.8389 1.2618  -0.3305 0.4147  322  ALA A CB  
2474  N  N   . SER A  323 ? 2.1590 2.4867 2.7079 1.2106  -0.3452 0.4061  323  SER A N   
2475  C  CA  . SER A  323 ? 2.2204 2.4325 2.6854 1.2136  -0.3516 0.4106  323  SER A CA  
2476  C  C   . SER A  323 ? 2.1763 2.3686 2.6295 1.1940  -0.3326 0.3867  323  SER A C   
2477  O  O   . SER A  323 ? 2.3322 2.4289 2.7150 1.1930  -0.3385 0.3887  323  SER A O   
2478  C  CB  . SER A  323 ? 2.2301 2.4263 2.6601 1.1926  -0.3862 0.4337  323  SER A CB  
2479  O  OG  . SER A  323 ? 2.2830 2.4874 2.7154 1.2117  -0.4069 0.4597  323  SER A OG  
2480  N  N   . GLY A  324 ? 2.2442 2.5209 2.7623 1.1770  -0.3126 0.3660  324  GLY A N   
2481  C  CA  . GLY A  324 ? 2.5130 2.7779 3.0272 1.1593  -0.2947 0.3447  324  GLY A CA  
2482  C  C   . GLY A  324 ? 2.6192 2.9325 3.1581 1.1148  -0.3061 0.3383  324  GLY A C   
2483  O  O   . GLY A  324 ? 2.4378 2.7742 3.0011 1.0955  -0.2907 0.3197  324  GLY A O   
2484  N  N   . ASP A  325 ? 2.6973 3.0274 3.2304 1.0992  -0.3325 0.3538  325  ASP A N   
2485  C  CA  . ASP A  325 ? 2.4827 2.8584 3.0361 1.0603  -0.3431 0.3477  325  ASP A CA  
2486  C  C   . ASP A  325 ? 2.4075 2.8978 3.0453 1.0363  -0.3335 0.3310  325  ASP A C   
2487  O  O   . ASP A  325 ? 2.5161 3.0503 3.1958 1.0477  -0.3201 0.3258  325  ASP A O   
2488  C  CB  . ASP A  325 ? 2.4441 2.8044 2.9594 1.0540  -0.3738 0.3708  325  ASP A CB  
2489  C  CG  . ASP A  325 ? 2.5121 2.7514 2.9396 1.0781  -0.3871 0.3912  325  ASP A CG  
2490  O  OD1 . ASP A  325 ? 2.6354 2.8057 3.0138 1.0695  -0.3911 0.3901  325  ASP A OD1 
2491  O  OD2 . ASP A  325 ? 2.2640 2.4740 2.6705 1.1047  -0.3952 0.4090  325  ASP A OD2 
2492  N  N   . PHE A  326 ? 2.1541 2.6918 2.8160 1.0026  -0.3410 0.3228  326  PHE A N   
2493  C  CA  . PHE A  326 ? 1.9873 2.6255 2.7221 0.9759  -0.3352 0.3062  326  PHE A CA  
2494  C  C   . PHE A  326 ? 2.0440 2.7303 2.7832 0.9535  -0.3558 0.3108  326  PHE A C   
2495  O  O   . PHE A  326 ? 2.2074 2.8612 2.9122 0.9446  -0.3661 0.3155  326  PHE A O   
2496  C  CB  . PHE A  326 ? 1.7613 2.4115 2.5312 0.9555  -0.3148 0.2824  326  PHE A CB  
2497  C  CG  . PHE A  326 ? 1.7837 2.4187 2.5650 0.9734  -0.2923 0.2753  326  PHE A CG  
2498  C  CD1 . PHE A  326 ? 1.8560 2.4071 2.5850 0.9970  -0.2829 0.2788  326  PHE A CD1 
2499  C  CD2 . PHE A  326 ? 1.6422 2.3486 2.4843 0.9669  -0.2808 0.2652  326  PHE A CD2 
2500  C  CE1 . PHE A  326 ? 1.8306 2.3744 2.5680 1.0157  -0.2603 0.2716  326  PHE A CE1 
2501  C  CE2 . PHE A  326 ? 1.6574 2.3578 2.5108 0.9842  -0.2598 0.2599  326  PHE A CE2 
2502  C  CZ  . PHE A  326 ? 1.7126 2.3342 2.5139 1.0094  -0.2483 0.2628  326  PHE A CZ  
2503  N  N   . GLN A  327 ? 1.8959 2.6627 2.6761 0.9448  -0.3623 0.3100  327  GLN A N   
2504  C  CA  . GLN A  327 ? 1.6986 2.5281 2.4891 0.9218  -0.3785 0.3098  327  GLN A CA  
2505  C  C   . GLN A  327 ? 1.5958 2.4900 2.4474 0.8906  -0.3640 0.2805  327  GLN A C   
2506  O  O   . GLN A  327 ? 1.5547 2.5048 2.4546 0.8834  -0.3571 0.2697  327  GLN A O   
2507  C  CB  . GLN A  327 ? 1.7423 2.6188 2.5332 0.9309  -0.3975 0.3281  327  GLN A CB  
2508  C  CG  . GLN A  327 ? 1.9446 2.7528 2.6798 0.9638  -0.4121 0.3584  327  GLN A CG  
2509  C  CD  . GLN A  327 ? 2.1373 2.9929 2.8665 0.9682  -0.4374 0.3811  327  GLN A CD  
2510  O  OE1 . GLN A  327 ? 2.1767 3.1182 2.9529 0.9542  -0.4399 0.3730  327  GLN A OE1 
2511  N  NE2 . GLN A  327 ? 2.2163 3.0134 2.8845 0.9864  -0.4586 0.4113  327  GLN A NE2 
2512  N  N   . THR A  328 ? 1.5829 2.4691 2.4333 0.8721  -0.3609 0.2689  328  THR A N   
2513  C  CA  . THR A  328 ? 1.6509 2.5813 2.5570 0.8442  -0.3458 0.2409  328  THR A CA  
2514  C  C   . THR A  328 ? 1.5864 2.5903 2.5129 0.8221  -0.3547 0.2306  328  THR A C   
2515  O  O   . THR A  328 ? 1.5195 2.5221 2.4131 0.8220  -0.3678 0.2410  328  THR A O   
2516  C  CB  . THR A  328 ? 1.7012 2.5740 2.6000 0.8391  -0.3343 0.2332  328  THR A CB  
2517  O  OG1 . THR A  328 ? 1.4026 2.2113 2.2780 0.8608  -0.3250 0.2411  328  THR A OG1 
2518  C  CG2 . THR A  328 ? 1.5987 2.5124 2.5575 0.8107  -0.3198 0.2066  328  THR A CG2 
2519  N  N   . THR A  329 ? 1.3312 2.4011 2.3107 0.8037  -0.3476 0.2103  329  THR A N   
2520  C  CA  . THR A  329 ? 1.1814 2.3235 2.1886 0.7805  -0.3501 0.1912  329  THR A CA  
2521  C  C   . THR A  329 ? 1.1305 2.2829 2.1920 0.7588  -0.3308 0.1629  329  THR A C   
2522  O  O   . THR A  329 ? 1.1638 2.2730 2.2396 0.7608  -0.3179 0.1619  329  THR A O   
2523  C  CB  . THR A  329 ? 1.2177 2.4335 2.2319 0.7789  -0.3646 0.1942  329  THR A CB  
2524  O  OG1 . THR A  329 ? 1.1873 2.4130 2.2327 0.7816  -0.3594 0.1934  329  THR A OG1 
2525  C  CG2 . THR A  329 ? 1.4288 2.6355 2.3870 0.7984  -0.3868 0.2257  329  THR A CG2 
2526  N  N   . LYS A  330 ? 1.0978 2.3072 2.1883 0.7385  -0.3286 0.1401  330  LYS A N   
2527  C  CA  . LYS A  330 ? 1.0559 2.2706 2.1974 0.7187  -0.3114 0.1145  330  LYS A CA  
2528  C  C   . LYS A  330 ? 1.0349 2.3279 2.2136 0.7021  -0.3120 0.0903  330  LYS A C   
2529  O  O   . LYS A  330 ? 1.0409 2.3912 2.2077 0.6990  -0.3227 0.0827  330  LYS A O   
2530  C  CB  . LYS A  330 ? 1.0403 2.2297 2.1833 0.7110  -0.3043 0.1063  330  LYS A CB  
2531  C  CG  . LYS A  330 ? 1.2037 2.3122 2.3229 0.7219  -0.3013 0.1245  330  LYS A CG  
2532  C  CD  . LYS A  330 ? 1.3323 2.4229 2.4482 0.7158  -0.3007 0.1221  330  LYS A CD  
2533  C  CE  . LYS A  330 ? 1.4731 2.4854 2.5661 0.7248  -0.2998 0.1385  330  LYS A CE  
2534  N  NZ  . LYS A  330 ? 1.5751 2.5418 2.6132 0.7493  -0.3094 0.1626  330  LYS A NZ  
2535  N  N   . LEU A  331 ? 1.0135 2.3116 2.2354 0.6912  -0.3016 0.0784  331  LEU A N   
2536  C  CA  . LEU A  331 ? 0.9983 2.3661 2.2569 0.6754  -0.3036 0.0544  331  LEU A CA  
2537  C  C   . LEU A  331 ? 0.9683 2.3290 2.2693 0.6587  -0.2868 0.0286  331  LEU A C   
2538  O  O   . LEU A  331 ? 0.9987 2.3177 2.3213 0.6563  -0.2751 0.0362  331  LEU A O   
2539  C  CB  . LEU A  331 ? 1.0065 2.3944 2.2809 0.6779  -0.3099 0.0666  331  LEU A CB  
2540  C  CG  . LEU A  331 ? 0.9995 2.4682 2.3058 0.6621  -0.3194 0.0456  331  LEU A CG  
2541  C  CD1 . LEU A  331 ? 1.1204 2.6505 2.3989 0.6613  -0.3368 0.0375  331  LEU A CD1 
2542  C  CD2 . LEU A  331 ? 1.0078 2.4952 2.3348 0.6641  -0.3261 0.0624  331  LEU A CD2 
2543  N  N   . ASN A  332 ? 0.9597 2.3635 2.2728 0.6481  -0.2855 -0.0019 332  ASN A N   
2544  C  CA  . ASN A  332 ? 0.9389 2.3354 2.2920 0.6347  -0.2697 -0.0296 332  ASN A CA  
2545  C  C   . ASN A  332 ? 0.9330 2.3734 2.3256 0.6221  -0.2712 -0.0550 332  ASN A C   
2546  O  O   . ASN A  332 ? 0.9433 2.4438 2.3335 0.6193  -0.2862 -0.0631 332  ASN A O   
2547  C  CB  . ASN A  332 ? 0.9370 2.3588 2.2891 0.6310  -0.2653 -0.0552 332  ASN A CB  
2548  C  CG  . ASN A  332 ? 1.1256 2.4995 2.4517 0.6394  -0.2622 -0.0325 332  ASN A CG  
2549  O  OD1 . ASN A  332 ? 1.2192 2.5423 2.5183 0.6501  -0.2669 0.0007  332  ASN A OD1 
2550  N  ND2 . ASN A  332 ? 1.0408 2.4335 2.3771 0.6345  -0.2546 -0.0523 332  ASN A ND2 
2551  N  N   . GLY A  333 ? 0.9195 2.3313 2.3475 0.6139  -0.2579 -0.0659 333  GLY A N   
2552  C  CA  . GLY A  333 ? 0.9170 2.3652 2.3860 0.6013  -0.2607 -0.0935 333  GLY A CA  
2553  C  C   . GLY A  333 ? 0.9230 2.4273 2.4110 0.5919  -0.2635 -0.1443 333  GLY A C   
2554  O  O   . GLY A  333 ? 0.9266 2.4440 2.3988 0.5950  -0.2592 -0.1585 333  GLY A O   
2555  N  N   . PHE A  334 ? 0.9261 2.4693 2.4516 0.5794  -0.2710 -0.1747 334  PHE A N   
2556  C  CA  . PHE A  334 ? 1.0910 2.6900 2.6332 0.5668  -0.2740 -0.2282 334  PHE A CA  
2557  C  C   . PHE A  334 ? 1.2695 2.8370 2.8535 0.5579  -0.2584 -0.2678 334  PHE A C   
2558  O  O   . PHE A  334 ? 1.4502 3.0190 3.0199 0.5444  -0.2452 -0.3043 334  PHE A O   
2559  C  CB  . PHE A  334 ? 1.1573 2.8058 2.6884 0.5456  -0.2929 -0.2334 334  PHE A CB  
2560  C  CG  . PHE A  334 ? 1.1761 2.8607 2.6742 0.5564  -0.3112 -0.1929 334  PHE A CG  
2561  C  CD1 . PHE A  334 ? 1.0552 2.7646 2.4964 0.5486  -0.3168 -0.1898 334  PHE A CD1 
2562  C  CD2 . PHE A  334 ? 1.1747 2.8512 2.6862 0.5688  -0.3187 -0.1527 334  PHE A CD2 
2563  C  CE1 . PHE A  334 ? 1.0244 2.7631 2.4367 0.5609  -0.3356 -0.1503 334  PHE A CE1 
2564  C  CE2 . PHE A  334 ? 1.1408 2.8349 2.6175 0.5781  -0.3319 -0.1130 334  PHE A CE2 
2565  C  CZ  . PHE A  334 ? 1.0732 2.8137 2.5119 0.5814  -0.3451 -0.1147 334  PHE A CZ  
2566  N  N   . GLU A  335 ? 1.2262 2.7531 2.8482 0.5610  -0.2563 -0.2573 335  GLU A N   
2567  C  CA  . GLU A  335 ? 1.1485 2.6471 2.8198 0.5561  -0.2462 -0.2945 335  GLU A CA  
2568  C  C   . GLU A  335 ? 1.1083 2.5285 2.7728 0.5653  -0.2282 -0.2661 335  GLU A C   
2569  O  O   . GLU A  335 ? 1.0107 2.3941 2.6466 0.5702  -0.2275 -0.2165 335  GLU A O   
2570  C  CB  . GLU A  335 ? 1.1051 2.6121 2.8140 0.5402  -0.2601 -0.3048 335  GLU A CB  
2571  C  CG  . GLU A  335 ? 1.0460 2.5884 2.7286 0.5095  -0.2686 -0.3367 335  GLU A CG  
2572  C  CD  . GLU A  335 ? 1.2319 2.7639 2.9499 0.4861  -0.2784 -0.3556 335  GLU A CD  
2573  O  OE1 . GLU A  335 ? 1.3419 2.9134 3.0436 0.4609  -0.2952 -0.3610 335  GLU A OE1 
2574  O  OE2 . GLU A  335 ? 1.3303 2.8143 3.0923 0.4913  -0.2712 -0.3633 335  GLU A OE2 
2575  N  N   . VAL A  336 ? 1.1232 2.5226 2.8150 0.5679  -0.2133 -0.2992 336  VAL A N   
2576  C  CA  . VAL A  336 ? 1.0893 2.4218 2.7788 0.5750  -0.1986 -0.2754 336  VAL A CA  
2577  C  C   . VAL A  336 ? 0.9526 2.2400 2.6632 0.5710  -0.2039 -0.2569 336  VAL A C   
2578  O  O   . VAL A  336 ? 1.1208 2.4189 2.8765 0.5629  -0.2127 -0.2866 336  VAL A O   
2579  C  CB  . VAL A  336 ? 0.9607 2.2904 2.6804 0.5800  -0.1813 -0.3173 336  VAL A CB  
2580  C  CG1 . VAL A  336 ? 0.9575 2.2337 2.6652 0.5874  -0.1683 -0.2855 336  VAL A CG1 
2581  C  CG2 . VAL A  336 ? 0.9652 2.3607 2.6734 0.5811  -0.1767 -0.3495 336  VAL A CG2 
2582  N  N   . PHE A  337 ? 0.9319 2.1729 2.6117 0.5758  -0.2000 -0.2098 337  PHE A N   
2583  C  CA  . PHE A  337 ? 0.9322 2.1318 2.6235 0.5731  -0.2038 -0.1876 337  PHE A CA  
2584  C  C   . PHE A  337 ? 1.3157 2.5434 3.0141 0.5653  -0.2172 -0.1767 337  PHE A C   
2585  O  O   . PHE A  337 ? 1.2170 2.4218 2.9354 0.5606  -0.2219 -0.1643 337  PHE A O   
2586  C  CB  . PHE A  337 ? 0.9528 2.1196 2.6972 0.5714  -0.2011 -0.2186 337  PHE A CB  
2587  C  CG  . PHE A  337 ? 0.9615 2.0991 2.7023 0.5803  -0.1870 -0.2215 337  PHE A CG  
2588  C  CD1 . PHE A  337 ? 0.9475 2.0753 2.6395 0.5862  -0.1809 -0.1856 337  PHE A CD1 
2589  C  CD2 . PHE A  337 ? 1.1372 2.2601 2.9275 0.5837  -0.1803 -0.2608 337  PHE A CD2 
2590  C  CE1 . PHE A  337 ? 1.0679 2.1782 2.7623 0.5926  -0.1699 -0.1865 337  PHE A CE1 
2591  C  CE2 . PHE A  337 ? 1.1267 2.2301 2.9173 0.5930  -0.1665 -0.2610 337  PHE A CE2 
2592  C  CZ  . PHE A  337 ? 1.0877 2.1884 2.8313 0.5962  -0.1621 -0.2226 337  PHE A CZ  
2593  N  N   . ALA A  338 ? 1.1415 2.4231 2.8265 0.5634  -0.2248 -0.1799 338  ALA A N   
2594  C  CA  . ALA A  338 ? 0.9138 2.2326 2.6076 0.5560  -0.2381 -0.1665 338  ALA A CA  
2595  C  C   . ALA A  338 ? 0.9020 2.2029 2.5537 0.5650  -0.2333 -0.1127 338  ALA A C   
2596  O  O   . ALA A  338 ? 1.2990 2.6238 2.9631 0.5606  -0.2401 -0.0957 338  ALA A O   
2597  C  CB  . ALA A  338 ? 0.9149 2.3015 2.6060 0.5518  -0.2500 -0.1859 338  ALA A CB  
2598  N  N   . ARG A  339 ? 0.8978 2.1612 2.5039 0.5774  -0.2217 -0.0878 339  ARG A N   
2599  C  CA  . ARG A  339 ? 0.8912 2.1355 2.4547 0.5889  -0.2160 -0.0421 339  ARG A CA  
2600  C  C   . ARG A  339 ? 1.0741 2.3635 2.6265 0.5926  -0.2223 -0.0232 339  ARG A C   
2601  O  O   . ARG A  339 ? 1.0647 2.3662 2.6170 0.5963  -0.2216 0.0029  339  ARG A O   
2602  C  CB  . ARG A  339 ? 0.8926 2.1095 2.4663 0.5878  -0.2139 -0.0286 339  ARG A CB  
2603  C  CG  . ARG A  339 ? 0.8995 2.0645 2.4816 0.5857  -0.2100 -0.0402 339  ARG A CG  
2604  C  CD  . ARG A  339 ? 0.9032 2.0373 2.4867 0.5859  -0.2104 -0.0215 339  ARG A CD  
2605  N  NE  . ARG A  339 ? 0.9135 1.9990 2.5147 0.5821  -0.2105 -0.0320 339  ARG A NE  
2606  C  CZ  . ARG A  339 ? 0.9206 1.9708 2.5269 0.5807  -0.2135 -0.0176 339  ARG A CZ  
2607  N  NH1 . ARG A  339 ? 0.9177 1.9777 2.5118 0.5833  -0.2148 0.0050  339  ARG A NH1 
2608  N  NH2 . ARG A  339 ? 0.9327 1.9404 2.5589 0.5775  -0.2153 -0.0254 339  ARG A NH2 
2609  N  N   . PHE A  340 ? 1.1965 2.5151 2.7429 0.5920  -0.2291 -0.0380 340  PHE A N   
2610  C  CA  . PHE A  340 ? 0.8928 2.2458 2.4237 0.5973  -0.2379 -0.0187 340  PHE A CA  
2611  C  C   . PHE A  340 ? 0.8930 2.2037 2.3899 0.6124  -0.2292 0.0245  340  PHE A C   
2612  O  O   . PHE A  340 ? 1.1029 2.3674 2.5705 0.6197  -0.2215 0.0334  340  PHE A O   
2613  C  CB  . PHE A  340 ? 0.8993 2.2812 2.4170 0.5968  -0.2471 -0.0428 340  PHE A CB  
2614  C  CG  . PHE A  340 ? 1.0090 2.4236 2.5045 0.6037  -0.2601 -0.0249 340  PHE A CG  
2615  C  CD1 . PHE A  340 ? 0.9830 2.4636 2.4988 0.5953  -0.2765 -0.0360 340  PHE A CD1 
2616  C  CD2 . PHE A  340 ? 0.9923 2.3717 2.4465 0.6183  -0.2588 0.0009  340  PHE A CD2 
2617  C  CE1 . PHE A  340 ? 0.9278 2.4393 2.4211 0.6028  -0.2904 -0.0174 340  PHE A CE1 
2618  C  CE2 . PHE A  340 ? 0.9309 2.3348 2.3624 0.6272  -0.2728 0.0156  340  PHE A CE2 
2619  C  CZ  . PHE A  340 ? 0.9373 2.4078 2.3876 0.6201  -0.2881 0.0083  340  PHE A CZ  
2620  N  N   . GLY A  341 ? 0.8953 2.2218 2.4020 0.6160  -0.2321 0.0483  341  GLY A N   
2621  C  CA  . GLY A  341 ? 0.9008 2.1799 2.3888 0.6293  -0.2259 0.0790  341  GLY A CA  
2622  C  C   . GLY A  341 ? 0.8989 2.1540 2.3935 0.6293  -0.2123 0.0972  341  GLY A C   
2623  O  O   . GLY A  341 ? 0.9112 2.1088 2.3841 0.6359  -0.2085 0.1089  341  GLY A O   
2624  N  N   . SER A  342 ? 0.8895 2.1842 2.4072 0.6225  -0.2093 0.0891  342  SER A N   
2625  C  CA  . SER A  342 ? 0.8945 2.1790 2.3999 0.6261  -0.1987 0.1006  342  SER A CA  
2626  C  C   . SER A  342 ? 0.9039 2.1907 2.4368 0.6213  -0.1981 0.1229  342  SER A C   
2627  O  O   . SER A  342 ? 0.9121 2.1515 2.4494 0.6212  -0.1926 0.1323  342  SER A O   
2628  C  CB  . SER A  342 ? 0.8849 2.2023 2.4298 0.6158  -0.2072 0.0713  342  SER A CB  
2629  O  OG  . SER A  342 ? 1.2027 2.4790 2.7440 0.6082  -0.2094 0.0444  342  SER A OG  
2630  N  N   . ALA A  343 ? 0.9390 2.2663 2.5178 0.6134  -0.2159 0.1113  343  ALA A N   
2631  C  CA  . ALA A  343 ? 0.9847 2.3229 2.5942 0.6181  -0.2306 0.0967  343  ALA A CA  
2632  C  C   . ALA A  343 ? 0.9230 2.2922 2.5217 0.6319  -0.2435 0.0961  343  ALA A C   
2633  O  O   . ALA A  343 ? 0.9154 2.3237 2.5207 0.6242  -0.2516 0.0952  343  ALA A O   
2634  C  CB  . ALA A  343 ? 1.0069 2.4065 2.6720 0.6009  -0.2354 0.0956  343  ALA A CB  
2635  N  N   . ILE A  344 ? 0.9431 2.3006 2.5188 0.6554  -0.2439 0.0993  344  ILE A N   
2636  C  CA  . ILE A  344 ? 0.9666 2.3417 2.5106 0.6702  -0.2514 0.1082  344  ILE A CA  
2637  C  C   . ILE A  344 ? 1.3635 2.7785 2.9207 0.6835  -0.2499 0.1171  344  ILE A C   
2638  O  O   . ILE A  344 ? 1.4280 2.8140 2.9681 0.7007  -0.2361 0.1219  344  ILE A O   
2639  C  CB  . ILE A  344 ? 0.9843 2.2932 2.4657 0.6895  -0.2470 0.1140  344  ILE A CB  
2640  C  CG1 . ILE A  344 ? 1.0683 2.3399 2.5403 0.6762  -0.2448 0.1067  344  ILE A CG1 
2641  C  CG2 . ILE A  344 ? 1.0101 2.3402 2.4621 0.7040  -0.2580 0.1245  344  ILE A CG2 
2642  C  CD1 . ILE A  344 ? 1.1461 2.3530 2.5600 0.6920  -0.2419 0.1118  344  ILE A CD1 
2643  N  N   . ALA A  345 ? 1.4046 2.8916 2.9928 0.6754  -0.2632 0.1209  345  ALA A N   
2644  C  CA  . ALA A  345 ? 1.0098 2.5494 2.6203 0.6857  -0.2621 0.1325  345  ALA A CA  
2645  C  C   . ALA A  345 ? 1.0386 2.6045 2.6290 0.7021  -0.2736 0.1472  345  ALA A C   
2646  O  O   . ALA A  345 ? 1.0352 2.6440 2.6360 0.6876  -0.2928 0.1459  345  ALA A O   
2647  C  CB  . ALA A  345 ? 0.9921 2.6056 2.6671 0.6594  -0.2706 0.1268  345  ALA A CB  
2648  N  N   . PRO A  346 ? 1.0708 2.6143 2.6314 0.7328  -0.2635 0.1616  346  PRO A N   
2649  C  CA  . PRO A  346 ? 1.1031 2.6799 2.6543 0.7505  -0.2760 0.1784  346  PRO A CA  
2650  C  C   . PRO A  346 ? 1.1038 2.7751 2.7117 0.7368  -0.2887 0.1845  346  PRO A C   
2651  O  O   . PRO A  346 ? 1.0980 2.8047 2.7451 0.7315  -0.2783 0.1848  346  PRO A O   
2652  C  CB  . PRO A  346 ? 1.1391 2.6728 2.6569 0.7872  -0.2577 0.1912  346  PRO A CB  
2653  C  CG  . PRO A  346 ? 1.1738 2.6357 2.6642 0.7872  -0.2394 0.1799  346  PRO A CG  
2654  C  CD  . PRO A  346 ? 1.0838 2.5717 2.6172 0.7543  -0.2406 0.1641  346  PRO A CD  
2655  N  N   . LEU A  347 ? 1.1128 2.8298 2.7246 0.7297  -0.3125 0.1906  347  LEU A N   
2656  C  CA  . LEU A  347 ? 1.1337 2.9453 2.7984 0.7108  -0.3305 0.1963  347  LEU A CA  
2657  C  C   . LEU A  347 ? 1.1552 3.0114 2.8279 0.7355  -0.3373 0.2201  347  LEU A C   
2658  O  O   . LEU A  347 ? 1.1619 3.1017 2.8802 0.7210  -0.3532 0.2283  347  LEU A O   
2659  C  CB  . LEU A  347 ? 1.1230 2.9693 2.7909 0.6815  -0.3558 0.1862  347  LEU A CB  
2660  C  CG  . LEU A  347 ? 1.0629 2.8730 2.7268 0.6581  -0.3507 0.1626  347  LEU A CG  
2661  C  CD1 . LEU A  347 ? 1.0569 2.9125 2.7203 0.6328  -0.3751 0.1524  347  LEU A CD1 
2662  C  CD2 . LEU A  347 ? 1.0391 2.8631 2.7513 0.6400  -0.3392 0.1527  347  LEU A CD2 
2663  N  N   . GLY A  348 ? 1.1860 2.9903 2.8177 0.7721  -0.3268 0.2321  348  GLY A N   
2664  C  CA  . GLY A  348 ? 1.2288 3.0747 2.8676 0.7967  -0.3380 0.2554  348  GLY A CA  
2665  C  C   . GLY A  348 ? 1.2384 3.1099 2.8611 0.7864  -0.3695 0.2616  348  GLY A C   
2666  O  O   . GLY A  348 ? 1.2212 3.0536 2.8076 0.7737  -0.3761 0.2499  348  GLY A O   
2667  N  N   . ASP A  349 ? 1.3162 3.2596 2.9668 0.7916  -0.3897 0.2812  349  ASP A N   
2668  C  CA  . ASP A  349 ? 1.3503 3.3332 2.9888 0.7784  -0.4234 0.2894  349  ASP A CA  
2669  C  C   . ASP A  349 ? 1.3547 3.4222 3.0414 0.7352  -0.4419 0.2804  349  ASP A C   
2670  O  O   . ASP A  349 ? 1.3262 3.4734 3.0567 0.7293  -0.4576 0.2953  349  ASP A O   
2671  C  CB  . ASP A  349 ? 1.3853 3.3928 3.0216 0.8104  -0.4384 0.3185  349  ASP A CB  
2672  C  CG  . ASP A  349 ? 1.4671 3.4846 3.0670 0.8048  -0.4703 0.3287  349  ASP A CG  
2673  O  OD1 . ASP A  349 ? 1.5282 3.5578 3.1144 0.7710  -0.4833 0.3127  349  ASP A OD1 
2674  O  OD2 . ASP A  349 ? 1.5836 3.5987 3.1682 0.8350  -0.4826 0.3530  349  ASP A OD2 
2675  N  N   . LEU A  350 ? 1.3067 3.3569 2.9858 0.7045  -0.4405 0.2557  350  LEU A N   
2676  C  CA  . LEU A  350 ? 1.2847 3.4059 3.0084 0.6614  -0.4559 0.2426  350  LEU A CA  
2677  C  C   . LEU A  350 ? 1.3127 3.5201 3.0484 0.6427  -0.4936 0.2557  350  LEU A C   
2678  O  O   . LEU A  350 ? 1.3141 3.5989 3.0993 0.6146  -0.5085 0.2569  350  LEU A O   
2679  C  CB  . LEU A  350 ? 1.2462 3.3296 2.9517 0.6366  -0.4505 0.2139  350  LEU A CB  
2680  C  CG  . LEU A  350 ? 1.3293 3.4738 3.0789 0.5916  -0.4637 0.1951  350  LEU A CG  
2681  C  CD1 . LEU A  350 ? 1.2114 3.3758 3.0161 0.5852  -0.4484 0.1964  350  LEU A CD1 
2682  C  CD2 . LEU A  350 ? 1.4192 3.5255 3.1460 0.5735  -0.4587 0.1664  350  LEU A CD2 
2683  N  N   . ASP A  351 ? 1.3923 3.5899 3.0825 0.6559  -0.5111 0.2672  351  ASP A N   
2684  C  CA  . ASP A  351 ? 1.4230 3.7005 3.1159 0.6358  -0.5499 0.2800  351  ASP A CA  
2685  C  C   . ASP A  351 ? 1.5839 3.8784 3.2750 0.6696  -0.5620 0.3143  351  ASP A C   
2686  O  O   . ASP A  351 ? 1.7478 4.1039 3.4359 0.6572  -0.5963 0.3301  351  ASP A O   
2687  C  CB  . ASP A  351 ? 1.5632 3.8345 3.2052 0.6153  -0.5670 0.2646  351  ASP A CB  
2688  C  CG  . ASP A  351 ? 1.7280 3.9105 3.3105 0.6469  -0.5497 0.2649  351  ASP A CG  
2689  O  OD1 . ASP A  351 ? 1.8250 3.9345 3.4053 0.6701  -0.5174 0.2595  351  ASP A OD1 
2690  O  OD2 . ASP A  351 ? 1.7085 3.8963 3.2443 0.6456  -0.5698 0.2703  351  ASP A OD2 
2691  N  N   . GLN A  352 ? 1.3885 3.6323 3.0821 0.7111  -0.5354 0.3256  352  GLN A N   
2692  C  CA  . GLN A  352 ? 1.5544 3.8136 3.2549 0.7482  -0.5430 0.3569  352  GLN A CA  
2693  C  C   . GLN A  352 ? 1.6307 3.8813 3.2811 0.7582  -0.5711 0.3743  352  GLN A C   
2694  O  O   . GLN A  352 ? 1.5972 3.9106 3.2612 0.7587  -0.6014 0.3984  352  GLN A O   
2695  C  CB  . GLN A  352 ? 1.4566 3.8148 3.2237 0.7362  -0.5576 0.3720  352  GLN A CB  
2696  C  CG  . GLN A  352 ? 1.4686 3.8409 3.2877 0.7332  -0.5286 0.3621  352  GLN A CG  
2697  C  CD  . GLN A  352 ? 1.4552 3.7667 3.2694 0.7809  -0.4925 0.3677  352  GLN A CD  
2698  O  OE1 . GLN A  352 ? 1.4290 3.6491 3.1947 0.7995  -0.4719 0.3561  352  GLN A OE1 
2699  N  NE2 . GLN A  352 ? 1.4665 3.8326 3.3309 0.8000  -0.4852 0.3857  352  GLN A NE2 
2700  N  N   . ASP A  353 ? 1.6574 3.8311 3.2491 0.7654  -0.5619 0.3636  353  ASP A N   
2701  C  CA  . ASP A  353 ? 1.5966 3.7533 3.1340 0.7760  -0.5858 0.3806  353  ASP A CA  
2702  C  C   . ASP A  353 ? 1.6672 3.7439 3.1718 0.8256  -0.5715 0.3983  353  ASP A C   
2703  O  O   . ASP A  353 ? 1.8068 3.8618 3.2652 0.8386  -0.5912 0.4164  353  ASP A O   
2704  C  CB  . ASP A  353 ? 1.5630 3.7014 3.0543 0.7458  -0.5901 0.3578  353  ASP A CB  
2705  C  CG  . ASP A  353 ? 1.8711 3.9265 3.3451 0.7510  -0.5530 0.3314  353  ASP A CG  
2706  O  OD1 . ASP A  353 ? 1.9947 3.9913 3.4745 0.7817  -0.5260 0.3343  353  ASP A OD1 
2707  O  OD2 . ASP A  353 ? 1.8138 3.8646 3.2676 0.7237  -0.5512 0.3069  353  ASP A OD2 
2708  N  N   . GLY A  354 ? 1.5639 3.5983 3.0897 0.8527  -0.5393 0.3943  354  GLY A N   
2709  C  CA  . GLY A  354 ? 1.5994 3.5553 3.0938 0.8987  -0.5241 0.4075  354  GLY A CA  
2710  C  C   . GLY A  354 ? 1.5805 3.4399 3.0287 0.9034  -0.4962 0.3871  354  GLY A C   
2711  O  O   . GLY A  354 ? 1.6061 3.3931 3.0231 0.9395  -0.4828 0.3960  354  GLY A O   
2712  N  N   . PHE A  355 ? 1.4372 3.2935 2.8802 0.8681  -0.4883 0.3606  355  PHE A N   
2713  C  CA  . PHE A  355 ? 1.4092 3.1802 2.8130 0.8688  -0.4633 0.3409  355  PHE A CA  
2714  C  C   . PHE A  355 ? 1.3537 3.1345 2.7928 0.8416  -0.4417 0.3132  355  PHE A C   
2715  O  O   . PHE A  355 ? 1.3260 3.1730 2.7975 0.8075  -0.4540 0.3023  355  PHE A O   
2716  C  CB  . PHE A  355 ? 1.4062 3.1545 2.7558 0.8550  -0.4792 0.3384  355  PHE A CB  
2717  C  CG  . PHE A  355 ? 1.4642 3.1943 2.7724 0.8808  -0.5016 0.3676  355  PHE A CG  
2718  C  CD1 . PHE A  355 ? 1.5008 3.1473 2.7729 0.9178  -0.4893 0.3797  355  PHE A CD1 
2719  C  CD2 . PHE A  355 ? 1.4875 3.2827 2.7901 0.8668  -0.5367 0.3838  355  PHE A CD2 
2720  C  CE1 . PHE A  355 ? 1.5601 3.1851 2.7940 0.9418  -0.5118 0.4082  355  PHE A CE1 
2721  C  CE2 . PHE A  355 ? 1.5457 3.3223 2.8088 0.8898  -0.5596 0.4135  355  PHE A CE2 
2722  C  CZ  . PHE A  355 ? 1.5824 3.2719 2.8122 0.9281  -0.5473 0.4262  355  PHE A CZ  
2723  N  N   . ASN A  356 ? 1.3425 3.0574 2.7741 0.8561  -0.4111 0.3027  356  ASN A N   
2724  C  CA  . ASN A  356 ? 1.4171 3.1334 2.8794 0.8324  -0.3905 0.2789  356  ASN A CA  
2725  C  C   . ASN A  356 ? 1.4530 3.1627 2.9013 0.7984  -0.3952 0.2571  356  ASN A C   
2726  O  O   . ASN A  356 ? 1.2581 2.9380 2.6608 0.7988  -0.4048 0.2575  356  ASN A O   
2727  C  CB  . ASN A  356 ? 1.5238 3.1668 2.9707 0.8558  -0.3589 0.2739  356  ASN A CB  
2728  C  CG  . ASN A  356 ? 1.3410 3.0073 2.8164 0.8854  -0.3481 0.2892  356  ASN A CG  
2729  O  OD1 . ASN A  356 ? 1.5556 3.3021 3.0807 0.8791  -0.3585 0.2977  356  ASN A OD1 
2730  N  ND2 . ASN A  356 ? 1.3611 2.9606 2.8053 0.9183  -0.3273 0.2931  356  ASN A ND2 
2731  N  N   . ASP A  357 ? 1.3582 3.1005 2.8483 0.7695  -0.3886 0.2384  357  ASP A N   
2732  C  CA  . ASP A  357 ? 1.1741 2.9196 2.6634 0.7371  -0.3913 0.2152  357  ASP A CA  
2733  C  C   . ASP A  357 ? 1.1397 2.8389 2.6442 0.7292  -0.3647 0.1968  357  ASP A C   
2734  O  O   . ASP A  357 ? 1.1451 2.8255 2.6647 0.7442  -0.3469 0.2016  357  ASP A O   
2735  C  CB  . ASP A  357 ? 1.3305 3.1700 2.8591 0.7056  -0.4155 0.2105  357  ASP A CB  
2736  C  CG  . ASP A  357 ? 1.3551 3.2491 2.8748 0.7134  -0.4441 0.2332  357  ASP A CG  
2737  O  OD1 . ASP A  357 ? 1.3002 3.1642 2.7702 0.7298  -0.4526 0.2438  357  ASP A OD1 
2738  O  OD2 . ASP A  357 ? 1.2586 3.2264 2.8212 0.7027  -0.4594 0.2424  357  ASP A OD2 
2739  N  N   . ILE A  358 ? 1.1693 2.8535 2.6699 0.7062  -0.3622 0.1757  358  ILE A N   
2740  C  CA  . ILE A  358 ? 1.0773 2.7104 2.5880 0.6993  -0.3392 0.1603  358  ILE A CA  
2741  C  C   . ILE A  358 ? 1.0432 2.7061 2.5831 0.6663  -0.3433 0.1379  358  ILE A C   
2742  O  O   . ILE A  358 ? 1.0422 2.7440 2.5737 0.6521  -0.3599 0.1290  358  ILE A O   
2743  C  CB  . ILE A  358 ? 1.0832 2.6264 2.5400 0.7191  -0.3243 0.1612  358  ILE A CB  
2744  C  CG1 . ILE A  358 ? 1.0665 2.5576 2.5328 0.7204  -0.3009 0.1537  358  ILE A CG1 
2745  C  CG2 . ILE A  358 ? 1.0709 2.6018 2.4982 0.7075  -0.3313 0.1494  358  ILE A CG2 
2746  C  CD1 . ILE A  358 ? 1.0894 2.5033 2.5066 0.7478  -0.2871 0.1624  358  ILE A CD1 
2747  N  N   . ALA A  359 ? 1.0191 2.6670 2.5931 0.6549  -0.3284 0.1281  359  ALA A N   
2748  C  CA  . ALA A  359 ? 0.9895 2.6543 2.5936 0.6271  -0.3286 0.1077  359  ALA A CA  
2749  C  C   . ALA A  359 ? 0.9705 2.5573 2.5571 0.6303  -0.3079 0.0994  359  ALA A C   
2750  O  O   . ALA A  359 ? 0.9740 2.5056 2.5484 0.6463  -0.2927 0.1076  359  ALA A O   
2751  C  CB  . ALA A  359 ? 0.9798 2.7018 2.6464 0.6075  -0.3327 0.1062  359  ALA A CB  
2752  N  N   . ILE A  360 ? 0.9544 2.5408 2.5369 0.6159  -0.3080 0.0812  360  ILE A N   
2753  C  CA  . ILE A  360 ? 1.0468 2.5699 2.6181 0.6159  -0.2896 0.0742  360  ILE A CA  
2754  C  C   . ILE A  360 ? 1.0891 2.6453 2.6960 0.5936  -0.2894 0.0528  360  ILE A C   
2755  O  O   . ILE A  360 ? 1.0744 2.6852 2.6883 0.5802  -0.3050 0.0282  360  ILE A O   
2756  C  CB  . ILE A  360 ? 1.1091 2.5909 2.6267 0.6272  -0.2878 0.0693  360  ILE A CB  
2757  C  CG1 . ILE A  360 ? 0.9690 2.4216 2.4459 0.6507  -0.2912 0.0892  360  ILE A CG1 
2758  C  CG2 . ILE A  360 ? 0.9279 2.3481 2.4368 0.6264  -0.2695 0.0649  360  ILE A CG2 
2759  C  CD1 . ILE A  360 ? 0.9798 2.4030 2.4049 0.6610  -0.2940 0.0878  360  ILE A CD1 
2760  N  N   . ALA A  361 ? 0.9049 2.4299 2.5307 0.5906  -0.2736 0.0582  361  ALA A N   
2761  C  CA  . ALA A  361 ? 0.8955 2.4490 2.5529 0.5725  -0.2752 0.0343  361  ALA A CA  
2762  C  C   . ALA A  361 ? 1.1745 2.6755 2.8098 0.5739  -0.2647 0.0098  361  ALA A C   
2763  O  O   . ALA A  361 ? 1.4721 2.9138 3.0715 0.5884  -0.2492 0.0271  361  ALA A O   
2764  C  CB  . ALA A  361 ? 0.8884 2.4562 2.5828 0.5677  -0.2685 0.0543  361  ALA A CB  
2765  N  N   . ALA A  362 ? 1.4110 2.9321 3.0747 0.5572  -0.2753 -0.0341 362  ALA A N   
2766  C  CA  . ALA A  362 ? 1.3101 2.7807 2.9752 0.5553  -0.2670 -0.0636 362  ALA A CA  
2767  C  C   . ALA A  362 ? 1.2764 2.7482 2.9962 0.5385  -0.2728 -0.0841 362  ALA A C   
2768  O  O   . ALA A  362 ? 1.1456 2.6444 2.9093 0.5212  -0.2871 -0.1270 362  ALA A O   
2769  C  CB  . ALA A  362 ? 1.0762 2.5604 2.7361 0.5520  -0.2734 -0.1036 362  ALA A CB  
2770  N  N   . PRO A  363 ? 0.9116 2.3531 2.6323 0.5426  -0.2632 -0.0573 363  PRO A N   
2771  C  CA  . PRO A  363 ? 1.0176 2.4694 2.7974 0.5240  -0.2728 -0.0690 363  PRO A CA  
2772  C  C   . PRO A  363 ? 0.9980 2.4175 2.8231 0.5105  -0.2798 -0.1149 363  PRO A C   
2773  O  O   . PRO A  363 ? 1.2818 2.7134 3.1688 0.4907  -0.2933 -0.1318 363  PRO A O   
2774  C  CB  . PRO A  363 ? 0.9105 2.3267 2.6686 0.5358  -0.2587 -0.0322 363  PRO A CB  
2775  C  CG  . PRO A  363 ? 0.9048 2.3160 2.5969 0.5602  -0.2442 0.0015  363  PRO A CG  
2776  C  CD  . PRO A  363 ? 0.9064 2.3051 2.5756 0.5633  -0.2451 -0.0176 363  PRO A CD  
2777  N  N   . TYR A  364 ? 0.9106 2.2912 2.7127 0.5202  -0.2711 -0.1357 364  TYR A N   
2778  C  CA  . TYR A  364 ? 0.9257 2.2714 2.7717 0.5136  -0.2732 -0.1790 364  TYR A CA  
2779  C  C   . TYR A  364 ? 1.0786 2.4538 2.9311 0.5125  -0.2769 -0.2255 364  TYR A C   
2780  O  O   . TYR A  364 ? 1.2258 2.5696 3.1022 0.5152  -0.2713 -0.2622 364  TYR A O   
2781  C  CB  . TYR A  364 ? 0.9282 2.1997 2.7488 0.5270  -0.2572 -0.1631 364  TYR A CB  
2782  C  CG  . TYR A  364 ? 1.0501 2.2983 2.8503 0.5307  -0.2528 -0.1176 364  TYR A CG  
2783  C  CD1 . TYR A  364 ? 0.9501 2.1975 2.8012 0.5169  -0.2630 -0.1134 364  TYR A CD1 
2784  C  CD2 . TYR A  364 ? 1.1441 2.3735 2.8772 0.5475  -0.2394 -0.0812 364  TYR A CD2 
2785  C  CE1 . TYR A  364 ? 1.1796 2.4119 3.0127 0.5206  -0.2583 -0.0745 364  TYR A CE1 
2786  C  CE2 . TYR A  364 ? 1.0464 2.2586 2.7597 0.5528  -0.2352 -0.0465 364  TYR A CE2 
2787  C  CZ  . TYR A  364 ? 0.9121 2.1275 2.6745 0.5397  -0.2439 -0.0436 364  TYR A CZ  
2788  O  OH  . TYR A  364 ? 0.9107 2.1136 2.6555 0.5451  -0.2395 -0.0116 364  TYR A OH  
2789  N  N   . GLY A  365 ? 1.0059 2.4442 2.8385 0.5097  -0.2860 -0.2253 365  GLY A N   
2790  C  CA  . GLY A  365 ? 1.0158 2.4960 2.8521 0.5067  -0.2922 -0.2711 365  GLY A CA  
2791  C  C   . GLY A  365 ? 1.0603 2.5556 2.9071 0.4703  -0.3047 -0.3037 365  GLY A C   
2792  O  O   . GLY A  365 ? 1.2613 2.7460 3.1438 0.4524  -0.3136 -0.2996 365  GLY A O   
2793  N  N   . GLY A  366 ? 1.1596 2.6758 2.9678 0.4555  -0.3052 -0.3360 366  GLY A N   
2794  C  CA  . GLY A  366 ? 1.2743 2.8023 3.0771 0.4167  -0.3182 -0.3690 366  GLY A CA  
2795  C  C   . GLY A  366 ? 1.3219 2.7824 3.1479 0.4039  -0.3095 -0.4122 366  GLY A C   
2796  O  O   . GLY A  366 ? 1.2533 2.6615 3.1061 0.4262  -0.2942 -0.4142 366  GLY A O   
2797  N  N   . GLU A  367 ? 1.2213 2.6816 3.0352 0.3668  -0.3207 -0.4478 367  GLU A N   
2798  C  CA  . GLU A  367 ? 1.3642 2.7544 3.1962 0.3523  -0.3144 -0.4924 367  GLU A CA  
2799  C  C   . GLU A  367 ? 1.2717 2.6184 3.1611 0.3554  -0.3187 -0.4685 367  GLU A C   
2800  O  O   . GLU A  367 ? 1.2505 2.6306 3.1614 0.3453  -0.3346 -0.4289 367  GLU A O   
2801  C  CB  . GLU A  367 ? 1.5998 2.9973 3.4026 0.3069  -0.3301 -0.5312 367  GLU A CB  
2802  C  CG  . GLU A  367 ? 1.6142 3.0652 3.4277 0.2753  -0.3591 -0.4997 367  GLU A CG  
2803  C  CD  . GLU A  367 ? 1.6934 3.1464 3.4776 0.2255  -0.3775 -0.5390 367  GLU A CD  
2804  O  OE1 . GLU A  367 ? 1.5873 3.0640 3.3931 0.1925  -0.4015 -0.5213 367  GLU A OE1 
2805  O  OE2 . GLU A  367 ? 1.9353 3.3658 3.6738 0.2177  -0.3677 -0.5882 367  GLU A OE2 
2806  N  N   . ASP A  368 ? 1.3212 2.5953 3.2366 0.3701  -0.3039 -0.4915 368  ASP A N   
2807  C  CA  . ASP A  368 ? 1.3538 2.5753 3.3215 0.3726  -0.3081 -0.4717 368  ASP A CA  
2808  C  C   . ASP A  368 ? 1.4146 2.6626 3.4040 0.3972  -0.3088 -0.4123 368  ASP A C   
2809  O  O   . ASP A  368 ? 1.5012 2.7283 3.5269 0.3905  -0.3177 -0.3842 368  ASP A O   
2810  C  CB  . ASP A  368 ? 1.4078 2.6152 3.3885 0.3282  -0.3296 -0.4795 368  ASP A CB  
2811  C  CG  . ASP A  368 ? 1.6986 2.8226 3.7239 0.3255  -0.3308 -0.4842 368  ASP A CG  
2812  O  OD1 . ASP A  368 ? 1.9844 3.0749 4.0383 0.3589  -0.3190 -0.4653 368  ASP A OD1 
2813  O  OD2 . ASP A  368 ? 1.7393 2.8293 3.7698 0.2881  -0.3455 -0.5056 368  ASP A OD2 
2814  N  N   . LYS A  369 ? 1.4206 2.7118 3.3843 0.4239  -0.2996 -0.3931 369  LYS A N   
2815  C  CA  . LYS A  369 ? 1.4007 2.7136 3.3742 0.4493  -0.2986 -0.3402 369  LYS A CA  
2816  C  C   . LYS A  369 ? 1.3418 2.6887 3.3338 0.4306  -0.3150 -0.3037 369  LYS A C   
2817  O  O   . LYS A  369 ? 1.0292 2.3572 3.0505 0.4386  -0.3155 -0.2704 369  LYS A O   
2818  C  CB  . LYS A  369 ? 1.3828 2.6366 3.3864 0.4763  -0.2871 -0.3305 369  LYS A CB  
2819  C  CG  . LYS A  369 ? 1.1846 2.4122 3.1793 0.4964  -0.2693 -0.3639 369  LYS A CG  
2820  C  CD  . LYS A  369 ? 1.0266 2.2241 3.0168 0.5255  -0.2572 -0.3309 369  LYS A CD  
2821  C  CE  . LYS A  369 ? 1.0343 2.1728 3.0501 0.5235  -0.2615 -0.3030 369  LYS A CE  
2822  N  NZ  . LYS A  369 ? 1.1612 2.2533 3.1206 0.5369  -0.2467 -0.2606 369  LYS A NZ  
2823  N  N   . LYS A  370 ? 1.2319 2.6340 3.2063 0.4043  -0.3285 -0.3091 370  LYS A N   
2824  C  CA  . LYS A  370 ? 1.1058 2.5521 3.1023 0.3823  -0.3444 -0.2773 370  LYS A CA  
2825  C  C   . LYS A  370 ? 1.0342 2.5470 3.0205 0.4061  -0.3436 -0.2318 370  LYS A C   
2826  O  O   . LYS A  370 ? 1.0098 2.5410 3.0228 0.4094  -0.3451 -0.1934 370  LYS A O   
2827  C  CB  . LYS A  370 ? 1.2023 2.6776 3.1897 0.3383  -0.3626 -0.3046 370  LYS A CB  
2828  C  CG  . LYS A  370 ? 1.4684 2.8741 3.4710 0.3076  -0.3673 -0.3445 370  LYS A CG  
2829  C  CD  . LYS A  370 ? 1.6668 3.1029 3.6558 0.2592  -0.3886 -0.3680 370  LYS A CD  
2830  C  CE  . LYS A  370 ? 1.8123 3.1674 3.7974 0.2328  -0.3902 -0.4216 370  LYS A CE  
2831  N  NZ  . LYS A  370 ? 1.7490 3.1266 3.7166 0.1803  -0.4136 -0.4450 370  LYS A NZ  
2832  N  N   . GLY A  371 ? 1.0690 2.6151 3.0157 0.4237  -0.3403 -0.2355 371  GLY A N   
2833  C  CA  . GLY A  371 ? 1.0246 2.6218 2.9568 0.4522  -0.3385 -0.1945 371  GLY A CA  
2834  C  C   . GLY A  371 ? 1.0327 2.6969 2.9320 0.4457  -0.3504 -0.1963 371  GLY A C   
2835  O  O   . GLY A  371 ? 1.1333 2.8267 3.0312 0.4109  -0.3660 -0.2171 371  GLY A O   
2836  N  N   . ILE A  372 ? 0.9195 2.5893 2.7697 0.4732  -0.3404 -0.1677 372  ILE A N   
2837  C  CA  . ILE A  372 ? 0.9247 2.6571 2.7449 0.4739  -0.3533 -0.1636 372  ILE A CA  
2838  C  C   . ILE A  372 ? 0.9154 2.6431 2.6931 0.4958  -0.3411 -0.1023 372  ILE A C   
2839  O  O   . ILE A  372 ? 0.9058 2.5694 2.6544 0.5161  -0.3186 -0.0750 372  ILE A O   
2840  C  CB  . ILE A  372 ? 1.3174 3.0388 3.1029 0.4804  -0.3503 -0.1994 372  ILE A CB  
2841  C  CG1 . ILE A  372 ? 1.2378 2.9181 3.0247 0.4499  -0.3471 -0.2507 372  ILE A CG1 
2842  C  CG2 . ILE A  372 ? 1.3850 3.1681 3.1308 0.4768  -0.3655 -0.1912 372  ILE A CG2 
2843  C  CD1 . ILE A  372 ? 1.2692 2.9887 3.0533 0.4080  -0.3672 -0.2719 372  ILE A CD1 
2844  N  N   . VAL A  373 ? 0.9223 2.7165 2.6990 0.4909  -0.3570 -0.0815 373  VAL A N   
2845  C  CA  . VAL A  373 ? 0.9218 2.7080 2.6652 0.5130  -0.3483 -0.0301 373  VAL A CA  
2846  C  C   . VAL A  373 ? 0.9590 2.7832 2.6678 0.5161  -0.3647 -0.0344 373  VAL A C   
2847  O  O   . VAL A  373 ? 1.3782 3.2769 3.1041 0.4947  -0.3897 -0.0531 373  VAL A O   
2848  C  CB  . VAL A  373 ? 0.9206 2.7449 2.7032 0.5075  -0.3513 0.0058  373  VAL A CB  
2849  C  CG1 . VAL A  373 ? 1.0529 2.8576 2.8092 0.5317  -0.3453 0.0440  373  VAL A CG1 
2850  C  CG2 . VAL A  373 ? 0.9059 2.6993 2.7180 0.5052  -0.3348 0.0138  373  VAL A CG2 
2851  N  N   . TYR A  374 ? 0.9420 2.7177 2.6010 0.5403  -0.3532 -0.0164 374  TYR A N   
2852  C  CA  . TYR A  374 ? 0.9601 2.7658 2.5795 0.5462  -0.3682 -0.0169 374  TYR A CA  
2853  C  C   . TYR A  374 ? 1.2707 3.0793 2.8771 0.5628  -0.3729 0.0265  374  TYR A C   
2854  O  O   . TYR A  374 ? 1.3902 3.1412 2.9935 0.5810  -0.3555 0.0517  374  TYR A O   
2855  C  CB  . TYR A  374 ? 0.9579 2.7115 2.5321 0.5607  -0.3558 -0.0307 374  TYR A CB  
2856  C  CG  . TYR A  374 ? 1.0407 2.7881 2.6295 0.5481  -0.3503 -0.0800 374  TYR A CG  
2857  C  CD1 . TYR A  374 ? 1.0183 2.8263 2.6084 0.5325  -0.3672 -0.1237 374  TYR A CD1 
2858  C  CD2 . TYR A  374 ? 1.2105 2.8903 2.8117 0.5523  -0.3285 -0.0847 374  TYR A CD2 
2859  C  CE1 . TYR A  374 ? 0.9603 2.7523 2.5664 0.5213  -0.3588 -0.1741 374  TYR A CE1 
2860  C  CE2 . TYR A  374 ? 1.1995 2.8663 2.8195 0.5433  -0.3230 -0.1312 374  TYR A CE2 
2861  C  CZ  . TYR A  374 ? 1.0328 2.7568 2.6608 0.5300  -0.3376 -0.1785 374  TYR A CZ  
2862  O  OH  . TYR A  374 ? 0.9537 2.6460 2.5935 0.5182  -0.3257 -0.2238 374  TYR A OH  
2863  N  N   . ILE A  375 ? 1.2007 3.0776 2.8016 0.5557  -0.3977 0.0313  375  ILE A N   
2864  C  CA  . ILE A  375 ? 1.0187 2.9048 2.6093 0.5726  -0.4060 0.0681  375  ILE A CA  
2865  C  C   . ILE A  375 ? 1.0392 2.9084 2.5709 0.5914  -0.4124 0.0769  375  ILE A C   
2866  O  O   . ILE A  375 ? 1.2009 3.1156 2.7110 0.5788  -0.4294 0.0585  375  ILE A O   
2867  C  CB  . ILE A  375 ? 1.0346 3.0118 2.6622 0.5507  -0.4323 0.0739  375  ILE A CB  
2868  C  CG1 . ILE A  375 ? 1.0149 3.0157 2.7020 0.5264  -0.4289 0.0612  375  ILE A CG1 
2869  C  CG2 . ILE A  375 ? 1.0610 3.0447 2.6849 0.5720  -0.4383 0.1107  375  ILE A CG2 
2870  C  CD1 . ILE A  375 ? 0.9985 2.9382 2.7068 0.5430  -0.4022 0.0777  375  ILE A CD1 
2871  N  N   . PHE A  376 ? 1.0931 2.9007 2.5974 0.6206  -0.4004 0.1029  376  PHE A N   
2872  C  CA  . PHE A  376 ? 1.1169 2.9027 2.5653 0.6404  -0.4073 0.1159  376  PHE A CA  
2873  C  C   . PHE A  376 ? 1.1517 2.9457 2.5936 0.6617  -0.4182 0.1494  376  PHE A C   
2874  O  O   . PHE A  376 ? 1.1948 2.9631 2.6589 0.6755  -0.4055 0.1626  376  PHE A O   
2875  C  CB  . PHE A  376 ? 1.1065 2.8037 2.5204 0.6571  -0.3847 0.1133  376  PHE A CB  
2876  C  CG  . PHE A  376 ? 1.0775 2.7649 2.4958 0.6401  -0.3738 0.0809  376  PHE A CG  
2877  C  CD1 . PHE A  376 ? 1.2868 3.0077 2.6792 0.6318  -0.3843 0.0605  376  PHE A CD1 
2878  C  CD2 . PHE A  376 ? 1.2914 2.9390 2.7406 0.6335  -0.3532 0.0701  376  PHE A CD2 
2879  C  CE1 . PHE A  376 ? 1.2240 2.9372 2.6245 0.6191  -0.3725 0.0256  376  PHE A CE1 
2880  C  CE2 . PHE A  376 ? 1.2314 2.8678 2.6873 0.6205  -0.3432 0.0403  376  PHE A CE2 
2881  C  CZ  . PHE A  376 ? 1.0774 2.7456 2.5106 0.6143  -0.3520 0.0157  376  PHE A CZ  
2882  N  N   . ASN A  377 ? 1.1674 2.9995 2.5785 0.6654  -0.4420 0.1623  377  ASN A N   
2883  C  CA  . ASN A  377 ? 1.2427 3.0876 2.6473 0.6868  -0.4563 0.1951  377  ASN A CA  
2884  C  C   . ASN A  377 ? 1.4515 3.2256 2.8020 0.7192  -0.4510 0.2141  377  ASN A C   
2885  O  O   . ASN A  377 ? 1.5641 3.3072 2.8739 0.7188  -0.4485 0.2053  377  ASN A O   
2886  C  CB  . ASN A  377 ? 1.2896 3.2257 2.6960 0.6683  -0.4909 0.2022  377  ASN A CB  
2887  C  CG  . ASN A  377 ? 1.2976 3.3080 2.7589 0.6351  -0.5005 0.1866  377  ASN A CG  
2888  O  OD1 . ASN A  377 ? 1.3324 3.3727 2.7999 0.6063  -0.5030 0.1562  377  ASN A OD1 
2889  N  ND2 . ASN A  377 ? 1.2308 3.2749 2.7323 0.6390  -0.5072 0.2060  377  ASN A ND2 
2890  N  N   . GLY A  378 ? 1.2373 2.9866 2.5893 0.7479  -0.4486 0.2391  378  GLY A N   
2891  C  CA  . GLY A  378 ? 1.2735 2.9587 2.5754 0.7801  -0.4477 0.2596  378  GLY A CA  
2892  C  C   . GLY A  378 ? 1.3176 3.0410 2.5903 0.7867  -0.4791 0.2838  378  GLY A C   
2893  O  O   . GLY A  378 ? 1.3257 3.1289 2.6203 0.7693  -0.5025 0.2886  378  GLY A O   
2894  N  N   . ARG A  379 ? 1.3740 3.0382 2.5941 0.8110  -0.4817 0.3010  379  ARG A N   
2895  C  CA  . ARG A  379 ? 1.4026 3.0886 2.5883 0.8219  -0.5121 0.3299  379  ARG A CA  
2896  C  C   . ARG A  379 ? 1.4466 3.0444 2.5879 0.8591  -0.5068 0.3515  379  ARG A C   
2897  O  O   . ARG A  379 ? 1.4357 2.9628 2.5730 0.8736  -0.4802 0.3419  379  ARG A O   
2898  C  CB  . ARG A  379 ? 1.3945 3.1283 2.5491 0.7935  -0.5319 0.3221  379  ARG A CB  
2899  C  CG  . ARG A  379 ? 1.3559 3.0508 2.4870 0.7820  -0.5123 0.2960  379  ARG A CG  
2900  C  CD  . ARG A  379 ? 1.3410 3.1025 2.4540 0.7504  -0.5276 0.2788  379  ARG A CD  
2901  N  NE  . ARG A  379 ? 1.5410 3.2644 2.6365 0.7443  -0.5068 0.2542  379  ARG A NE  
2902  C  CZ  . ARG A  379 ? 1.4958 3.2672 2.5769 0.7202  -0.5111 0.2311  379  ARG A CZ  
2903  N  NH1 . ARG A  379 ? 1.3930 3.2532 2.4686 0.6967  -0.5365 0.2278  379  ARG A NH1 
2904  N  NH2 . ARG A  379 ? 1.2592 2.9931 2.3313 0.7185  -0.4904 0.2099  379  ARG A NH2 
2905  N  N   . SER A  380 ? 1.5026 3.1046 2.6096 0.8739  -0.5342 0.3822  380  SER A N   
2906  C  CA  . SER A  380 ? 1.5570 3.0749 2.6216 0.9107  -0.5338 0.4060  380  SER A CA  
2907  C  C   . SER A  380 ? 1.5426 2.9829 2.5621 0.9113  -0.5164 0.3942  380  SER A C   
2908  O  O   . SER A  380 ? 1.7539 3.1119 2.7535 0.9383  -0.5009 0.3991  380  SER A O   
2909  C  CB  . SER A  380 ? 1.6211 3.1575 2.6511 0.9202  -0.5706 0.4417  380  SER A CB  
2910  O  OG  . SER A  380 ? 1.6136 3.1801 2.6032 0.8927  -0.5885 0.4414  380  SER A OG  
2911  N  N   . THR A  381 ? 1.5156 2.9837 2.5194 0.8817  -0.5188 0.3776  381  THR A N   
2912  C  CA  . THR A  381 ? 1.5018 2.9075 2.4659 0.8798  -0.5052 0.3675  381  THR A CA  
2913  C  C   . THR A  381 ? 1.4418 2.8270 2.4399 0.8678  -0.4729 0.3334  381  THR A C   
2914  O  O   . THR A  381 ? 1.5215 2.8551 2.4939 0.8655  -0.4600 0.3232  381  THR A O   
2915  C  CB  . THR A  381 ? 1.7282 3.1802 2.6578 0.8557  -0.5242 0.3680  381  THR A CB  
2916  O  OG1 . THR A  381 ? 1.9623 3.4534 2.8679 0.8589  -0.5575 0.3996  381  THR A OG1 
2917  C  CG2 . THR A  381 ? 1.5076 2.8909 2.3845 0.8615  -0.5190 0.3724  381  THR A CG2 
2918  N  N   . GLY A  382 ? 1.4007 2.8241 2.4553 0.8595  -0.4613 0.3182  382  GLY A N   
2919  C  CA  . GLY A  382 ? 1.3499 2.7519 2.4359 0.8470  -0.4328 0.2895  382  GLY A CA  
2920  C  C   . GLY A  382 ? 1.3005 2.7782 2.4390 0.8154  -0.4305 0.2652  382  GLY A C   
2921  O  O   . GLY A  382 ? 1.3084 2.8554 2.4739 0.8082  -0.4472 0.2717  382  GLY A O   
2922  N  N   . LEU A  383 ? 1.3304 2.7937 2.4848 0.7963  -0.4113 0.2378  383  LEU A N   
2923  C  CA  . LEU A  383 ? 1.2870 2.8109 2.4913 0.7669  -0.4075 0.2127  383  LEU A CA  
2924  C  C   . LEU A  383 ? 1.3886 2.9734 2.5832 0.7437  -0.4226 0.1975  383  LEU A C   
2925  O  O   . LEU A  383 ? 1.3399 2.9029 2.4980 0.7438  -0.4220 0.1931  383  LEU A O   
2926  C  CB  . LEU A  383 ? 1.5512 3.0284 2.7792 0.7583  -0.3802 0.1915  383  LEU A CB  
2927  C  CG  . LEU A  383 ? 1.5015 3.0301 2.7853 0.7309  -0.3750 0.1685  383  LEU A CG  
2928  C  CD1 . LEU A  383 ? 1.2218 2.7964 2.5436 0.7334  -0.3823 0.1808  383  LEU A CD1 
2929  C  CD2 . LEU A  383 ? 1.4229 2.8977 2.7237 0.7235  -0.3501 0.1516  383  LEU A CD2 
2930  N  N   . ASN A  384 ? 1.1988 2.8647 2.4266 0.7227  -0.4364 0.1879  384  ASN A N   
2931  C  CA  . ASN A  384 ? 1.1882 2.9221 2.4093 0.6976  -0.4501 0.1660  384  ASN A CA  
2932  C  C   . ASN A  384 ? 1.1441 2.8646 2.3862 0.6805  -0.4284 0.1284  384  ASN A C   
2933  O  O   . ASN A  384 ? 1.2272 2.9472 2.5152 0.6691  -0.4156 0.1127  384  ASN A O   
2934  C  CB  . ASN A  384 ? 1.2444 3.0684 2.4938 0.6779  -0.4732 0.1652  384  ASN A CB  
2935  C  CG  . ASN A  384 ? 1.2372 3.1385 2.4700 0.6513  -0.4916 0.1418  384  ASN A CG  
2936  O  OD1 . ASN A  384 ? 1.1890 3.1585 2.4526 0.6244  -0.5020 0.1197  384  ASN A OD1 
2937  N  ND2 . ASN A  384 ? 1.3048 3.1991 2.4876 0.6567  -0.4963 0.1448  384  ASN A ND2 
2938  N  N   . ALA A  385 ? 1.2863 2.9980 2.4967 0.6790  -0.4249 0.1152  385  ALA A N   
2939  C  CA  . ALA A  385 ? 1.4157 3.1079 2.6467 0.6667  -0.4031 0.0802  385  ALA A CA  
2940  C  C   . ALA A  385 ? 1.3545 3.1167 2.6260 0.6396  -0.4057 0.0414  385  ALA A C   
2941  O  O   . ALA A  385 ? 1.3272 3.0672 2.6319 0.6302  -0.3868 0.0135  385  ALA A O   
2942  C  CB  . ALA A  385 ? 1.3125 2.9925 2.5042 0.6711  -0.4005 0.0750  385  ALA A CB  
2943  N  N   . VAL A  386 ? 1.2327 3.0780 2.5007 0.6257  -0.4307 0.0383  386  VAL A N   
2944  C  CA  . VAL A  386 ? 1.2009 3.1097 2.5006 0.5949  -0.4359 -0.0028 386  VAL A CA  
2945  C  C   . VAL A  386 ? 1.2663 3.1968 2.6134 0.5888  -0.4432 0.0069  386  VAL A C   
2946  O  O   . VAL A  386 ? 1.4181 3.3564 2.7597 0.5979  -0.4575 0.0445  386  VAL A O   
2947  C  CB  . VAL A  386 ? 1.4346 3.3785 2.6782 0.5601  -0.4511 -0.0149 386  VAL A CB  
2948  C  CG1 . VAL A  386 ? 1.6771 3.5758 2.8697 0.5489  -0.4316 -0.0336 386  VAL A CG1 
2949  C  CG2 . VAL A  386 ? 1.3565 3.3413 2.5739 0.5730  -0.4815 0.0301  386  VAL A CG2 
2950  N  N   . PRO A  387 ? 1.1314 3.0642 2.5255 0.5726  -0.4324 -0.0247 387  PRO A N   
2951  C  CA  . PRO A  387 ? 1.2684 3.2212 2.7075 0.5620  -0.4387 -0.0131 387  PRO A CA  
2952  C  C   . PRO A  387 ? 1.3101 3.3609 2.7549 0.5367  -0.4717 -0.0190 387  PRO A C   
2953  O  O   . PRO A  387 ? 1.3522 3.4318 2.7695 0.5080  -0.4805 -0.0531 387  PRO A O   
2954  C  CB  . PRO A  387 ? 1.1748 3.1014 2.6576 0.5503  -0.4198 -0.0479 387  PRO A CB  
2955  C  CG  . PRO A  387 ? 1.0860 3.0112 2.5489 0.5414  -0.4130 -0.0923 387  PRO A CG  
2956  C  CD  . PRO A  387 ? 1.0981 3.0040 2.5054 0.5615  -0.4121 -0.0703 387  PRO A CD  
2957  N  N   . SER A  388 ? 1.4110 3.4824 2.8778 0.5363  -0.4839 0.0151  388  SER A N   
2958  C  CA  . SER A  388 ? 1.2353 3.3981 2.7108 0.5093  -0.5177 0.0168  388  SER A CA  
2959  C  C   . SER A  388 ? 1.3952 3.6010 2.9264 0.4774  -0.5240 -0.0088 388  SER A C   
2960  O  O   . SER A  388 ? 1.4466 3.7326 2.9860 0.4458  -0.5544 -0.0155 388  SER A O   
2961  C  CB  . SER A  388 ? 1.2629 3.4300 2.7337 0.5271  -0.5307 0.0695  388  SER A CB  
2962  O  OG  . SER A  388 ? 1.2473 3.3681 2.7578 0.5440  -0.5109 0.0909  388  SER A OG  
2963  N  N   . GLN A  389 ? 1.3630 3.5174 2.9306 0.4819  -0.4986 -0.0220 389  GLN A N   
2964  C  CA  . GLN A  389 ? 1.3491 3.5390 2.9715 0.4513  -0.5049 -0.0470 389  GLN A CA  
2965  C  C   . GLN A  389 ? 1.3857 3.5077 3.0309 0.4587  -0.4759 -0.0745 389  GLN A C   
2966  O  O   . GLN A  389 ? 1.2259 3.2699 2.8574 0.4885  -0.4489 -0.0524 389  GLN A O   
2967  C  CB  . GLN A  389 ? 1.0847 3.3002 2.7478 0.4473  -0.5126 -0.0055 389  GLN A CB  
2968  C  CG  . GLN A  389 ? 1.0849 3.3579 2.8024 0.4070  -0.5286 -0.0281 389  GLN A CG  
2969  C  CD  . GLN A  389 ? 1.0981 3.4148 2.8547 0.3989  -0.5414 0.0136  389  GLN A CD  
2970  O  OE1 . GLN A  389 ? 1.3283 3.6206 3.0768 0.4296  -0.5327 0.0549  389  GLN A OE1 
2971  N  NE2 . GLN A  389 ? 1.1070 3.4874 2.9079 0.3569  -0.5624 -0.0010 389  GLN A NE2 
2972  N  N   . ILE A  390 ? 1.5334 3.6506 3.1954 0.4220  -0.4778 -0.1185 390  ILE A N   
2973  C  CA  . ILE A  390 ? 1.5273 3.5701 3.2094 0.4227  -0.4522 -0.1463 390  ILE A CA  
2974  C  C   . ILE A  390 ? 1.4363 3.4965 3.1771 0.3975  -0.4592 -0.1476 390  ILE A C   
2975  O  O   . ILE A  390 ? 1.4741 3.5633 3.2162 0.3534  -0.4788 -0.1686 390  ILE A O   
2976  C  CB  . ILE A  390 ? 1.5594 3.5468 3.1965 0.4002  -0.4407 -0.1987 390  ILE A CB  
2977  C  CG1 . ILE A  390 ? 1.7146 3.6899 3.2928 0.4213  -0.4332 -0.1949 390  ILE A CG1 
2978  C  CG2 . ILE A  390 ? 1.4516 3.3649 3.1178 0.4041  -0.4164 -0.2241 390  ILE A CG2 
2979  C  CD1 . ILE A  390 ? 1.6698 3.7002 3.1978 0.3982  -0.4571 -0.1948 390  ILE A CD1 
2980  N  N   . LEU A  391 ? 1.3816 3.4228 3.1671 0.4225  -0.4440 -0.1246 391  LEU A N   
2981  C  CA  . LEU A  391 ? 1.2709 3.3226 3.1127 0.3993  -0.4474 -0.1221 391  LEU A CA  
2982  C  C   . LEU A  391 ? 1.1784 3.1440 3.0240 0.3842  -0.4309 -0.1617 391  LEU A C   
2983  O  O   . LEU A  391 ? 1.0301 2.9350 2.8710 0.4142  -0.4084 -0.1623 391  LEU A O   
2984  C  CB  . LEU A  391 ? 1.0200 3.0619 2.8793 0.4241  -0.4307 -0.0649 391  LEU A CB  
2985  C  CG  . LEU A  391 ? 1.0327 3.1381 2.9034 0.4201  -0.4445 -0.0202 391  LEU A CG  
2986  C  CD1 . LEU A  391 ? 1.1559 3.2888 2.9798 0.4287  -0.4595 -0.0131 391  LEU A CD1 
2987  C  CD2 . LEU A  391 ? 1.0203 3.0803 2.8989 0.4472  -0.4196 0.0256  391  LEU A CD2 
2988  N  N   . GLU A  392 ? 1.3218 3.2804 3.1764 0.3377  -0.4433 -0.1936 392  GLU A N   
2989  C  CA  . GLU A  392 ? 1.3275 3.2015 3.1847 0.3223  -0.4300 -0.2348 392  GLU A CA  
2990  C  C   . GLU A  392 ? 1.3095 3.1697 3.2234 0.3064  -0.4310 -0.2220 392  GLU A C   
2991  O  O   . GLU A  392 ? 1.4152 3.3361 3.3598 0.2803  -0.4499 -0.2014 392  GLU A O   
2992  C  CB  . GLU A  392 ? 1.4708 3.3288 3.2898 0.2812  -0.4411 -0.2861 392  GLU A CB  
2993  C  CG  . GLU A  392 ? 1.6530 3.5098 3.4100 0.2936  -0.4350 -0.3061 392  GLU A CG  
2994  C  CD  . GLU A  392 ? 1.9220 3.6954 3.6578 0.3030  -0.4097 -0.3500 392  GLU A CD  
2995  O  OE1 . GLU A  392 ? 1.9237 3.6372 3.6947 0.3036  -0.3982 -0.3629 392  GLU A OE1 
2996  O  OE2 . GLU A  392 ? 2.1305 3.9006 3.8159 0.3104  -0.4012 -0.3697 392  GLU A OE2 
2997  N  N   . GLY A  393 ? 1.2220 3.0047 3.1506 0.3211  -0.4115 -0.2320 393  GLY A N   
2998  C  CA  . GLY A  393 ? 1.2234 2.9781 3.1998 0.3017  -0.4125 -0.2243 393  GLY A CA  
2999  C  C   . GLY A  393 ? 1.4678 3.1869 3.4441 0.2518  -0.4266 -0.2672 393  GLY A C   
3000  O  O   . GLY A  393 ? 1.8139 3.4886 3.7539 0.2438  -0.4234 -0.3132 393  GLY A O   
3001  N  N   . GLN A  394 ? 1.2337 2.9713 3.2498 0.2172  -0.4414 -0.2518 394  GLN A N   
3002  C  CA  . GLN A  394 ? 1.2823 2.9873 3.2989 0.1639  -0.4591 -0.2879 394  GLN A CA  
3003  C  C   . GLN A  394 ? 1.3817 3.0027 3.4309 0.1523  -0.4532 -0.2948 394  GLN A C   
3004  O  O   . GLN A  394 ? 1.5571 3.1298 3.6036 0.1106  -0.4661 -0.3292 394  GLN A O   
3005  C  CB  . GLN A  394 ? 1.2422 3.0373 3.2776 0.1217  -0.4872 -0.2659 394  GLN A CB  
3006  C  CG  . GLN A  394 ? 1.2098 3.0977 3.2200 0.1314  -0.4982 -0.2509 394  GLN A CG  
3007  C  CD  . GLN A  394 ? 1.2578 3.1245 3.2058 0.1196  -0.5038 -0.2990 394  GLN A CD  
3008  O  OE1 . GLN A  394 ? 1.3606 3.1538 3.2858 0.0929  -0.5040 -0.3478 394  GLN A OE1 
3009  N  NE2 . GLN A  394 ? 1.2349 3.1650 3.1532 0.1398  -0.5079 -0.2853 394  GLN A NE2 
3010  N  N   . TRP A  395 ? 1.3639 2.9636 3.4407 0.1863  -0.4358 -0.2625 395  TRP A N   
3011  C  CA  . TRP A  395 ? 1.4286 2.9631 3.5421 0.1733  -0.4340 -0.2548 395  TRP A CA  
3012  C  C   . TRP A  395 ? 1.5017 2.9392 3.6069 0.2056  -0.4146 -0.2790 395  TRP A C   
3013  O  O   . TRP A  395 ? 1.5651 3.0034 3.6624 0.2513  -0.3964 -0.2629 395  TRP A O   
3014  C  CB  . TRP A  395 ? 1.2566 2.8446 3.4089 0.1824  -0.4306 -0.1960 395  TRP A CB  
3015  C  CG  . TRP A  395 ? 1.4520 3.1474 3.6193 0.1565  -0.4476 -0.1694 395  TRP A CG  
3016  C  CD1 . TRP A  395 ? 1.6157 3.3434 3.8155 0.1055  -0.4673 -0.1566 395  TRP A CD1 
3017  C  CD2 . TRP A  395 ? 1.4455 3.2321 3.5982 0.1793  -0.4483 -0.1515 395  TRP A CD2 
3018  N  NE1 . TRP A  395 ? 1.6152 3.4556 3.8260 0.0963  -0.4796 -0.1308 395  TRP A NE1 
3019  C  CE2 . TRP A  395 ? 1.4636 3.3399 3.6459 0.1427  -0.4685 -0.1272 395  TRP A CE2 
3020  C  CE3 . TRP A  395 ? 1.4302 3.2307 3.5487 0.2263  -0.4349 -0.1515 395  TRP A CE3 
3021  C  CZ2 . TRP A  395 ? 1.3004 3.2803 3.4823 0.1555  -0.4758 -0.1030 395  TRP A CZ2 
3022  C  CZ3 . TRP A  395 ? 1.3870 3.2829 3.5003 0.2377  -0.4425 -0.1279 395  TRP A CZ3 
3023  C  CH2 . TRP A  395 ? 1.3159 3.3008 3.4622 0.2043  -0.4628 -0.1039 395  TRP A CH2 
3024  N  N   . ALA A  396 ? 1.6067 2.9610 3.7143 0.1817  -0.4194 -0.3175 396  ALA A N   
3025  C  CA  . ALA A  396 ? 1.7128 2.9747 3.8212 0.2106  -0.4028 -0.3421 396  ALA A CA  
3026  C  C   . ALA A  396 ? 1.8056 3.0353 3.9513 0.2307  -0.3955 -0.3002 396  ALA A C   
3027  O  O   . ALA A  396 ? 1.7147 2.9791 3.8863 0.2134  -0.4037 -0.2583 396  ALA A O   
3028  C  CB  . ALA A  396 ? 1.6621 2.8417 3.7644 0.1800  -0.4107 -0.3949 396  ALA A CB  
3029  N  N   . ALA A  397 ? 1.6821 2.8473 3.8303 0.2666  -0.3798 -0.3115 397  ALA A N   
3030  C  CA  . ALA A  397 ? 1.3624 2.4925 3.5394 0.2893  -0.3731 -0.2735 397  ALA A CA  
3031  C  C   . ALA A  397 ? 1.5110 2.5550 3.7184 0.2638  -0.3841 -0.2825 397  ALA A C   
3032  O  O   . ALA A  397 ? 1.5723 2.5422 3.7811 0.2703  -0.3810 -0.3231 397  ALA A O   
3033  C  CB  . ALA A  397 ? 1.1801 2.2887 3.3466 0.3388  -0.3540 -0.2777 397  ALA A CB  
3034  N  N   . ARG A  398 ? 1.4092 2.4629 3.6411 0.2356  -0.3961 -0.2439 398  ARG A N   
3035  C  CA  . ARG A  398 ? 1.4806 2.4516 3.7419 0.2106  -0.4083 -0.2407 398  ARG A CA  
3036  C  C   . ARG A  398 ? 1.5603 2.4534 3.8382 0.2476  -0.3991 -0.2359 398  ARG A C   
3037  O  O   . ARG A  398 ? 1.7629 2.5773 4.0471 0.2546  -0.3991 -0.2747 398  ARG A O   
3038  C  CB  . ARG A  398 ? 1.5106 2.5229 3.7930 0.1768  -0.4194 -0.1902 398  ARG A CB  
3039  C  CG  . ARG A  398 ? 1.4651 2.5587 3.7435 0.2043  -0.4058 -0.1427 398  ARG A CG  
3040  C  CD  . ARG A  398 ? 1.4386 2.5833 3.7383 0.1714  -0.4129 -0.0950 398  ARG A CD  
3041  N  NE  . ARG A  398 ? 1.5102 2.7330 3.8097 0.1354  -0.4241 -0.1003 398  ARG A NE  
3042  C  CZ  . ARG A  398 ? 1.3240 2.6183 3.6444 0.1058  -0.4292 -0.0609 398  ARG A CZ  
3043  N  NH1 . ARG A  398 ? 1.2696 2.5640 3.6075 0.1080  -0.4219 -0.0149 398  ARG A NH1 
3044  N  NH2 . ARG A  398 ? 1.2724 2.6417 3.5961 0.0733  -0.4417 -0.0665 398  ARG A NH2 
3045  N  N   . SER A  399 ? 1.5981 2.5131 3.8829 0.2720  -0.3915 -0.1890 399  SER A N   
3046  C  CA  . SER A  399 ? 1.6508 2.5000 3.9525 0.3038  -0.3866 -0.1753 399  SER A CA  
3047  C  C   . SER A  399 ? 1.4085 2.3050 3.7025 0.3260  -0.3778 -0.1239 399  SER A C   
3048  O  O   . SER A  399 ? 1.4178 2.3613 3.7120 0.3040  -0.3811 -0.0869 399  SER A O   
3049  C  CB  . SER A  399 ? 1.8493 2.6110 4.1826 0.2778  -0.4031 -0.1688 399  SER A CB  
3050  O  OG  . SER A  399 ? 1.8514 2.6423 4.1916 0.2350  -0.4152 -0.1334 399  SER A OG  
3051  N  N   . GLY A  400 ? 1.3921 2.2793 3.6777 0.3684  -0.3659 -0.1217 400  GLY A N   
3052  C  CA  . GLY A  400 ? 1.2778 2.1959 3.5502 0.3889  -0.3587 -0.0753 400  GLY A CA  
3053  C  C   . GLY A  400 ? 1.2201 2.2032 3.4583 0.4170  -0.3440 -0.0828 400  GLY A C   
3054  O  O   . GLY A  400 ? 1.2191 2.1897 3.4493 0.4422  -0.3366 -0.1123 400  GLY A O   
3055  N  N   . CYS A  401 ? 1.2907 2.3440 3.5090 0.4135  -0.3390 -0.0544 401  CYS A N   
3056  C  CA  . CYS A  401 ? 1.2744 2.3853 3.4510 0.4372  -0.3259 -0.0590 401  CYS A CA  
3057  C  C   . CYS A  401 ? 1.3960 2.5446 3.5739 0.4242  -0.3299 -0.1000 401  CYS A C   
3058  O  O   . CYS A  401 ? 1.4471 2.6006 3.6422 0.3886  -0.3410 -0.1116 401  CYS A O   
3059  C  CB  . CYS A  401 ? 0.9735 2.1375 3.1097 0.4366  -0.3157 -0.0173 401  CYS A CB  
3060  S  SG  . CYS A  401 ? 0.9679 2.0915 3.0223 0.4608  -0.2965 0.0228  401  CYS A SG  
3061  N  N   . PRO A  402 ? 1.3083 2.4760 3.4495 0.4469  -0.3198 -0.1203 402  PRO A N   
3062  C  CA  . PRO A  402 ? 1.1822 2.3965 3.3165 0.4348  -0.3238 -0.1546 402  PRO A CA  
3063  C  C   . PRO A  402 ? 0.9749 2.2679 3.1044 0.4181  -0.3292 -0.1306 402  PRO A C   
3064  O  O   . PRO A  402 ? 0.9506 2.2676 3.0807 0.4249  -0.3250 -0.0887 402  PRO A O   
3065  C  CB  . PRO A  402 ? 0.9718 2.1851 3.0514 0.4639  -0.3081 -0.1671 402  PRO A CB  
3066  C  CG  . PRO A  402 ? 1.4146 2.5908 3.4284 0.4815  -0.2912 -0.1242 402  PRO A CG  
3067  C  CD  . PRO A  402 ? 1.4057 2.5347 3.4645 0.4734  -0.2990 -0.1073 402  PRO A CD  
3068  N  N   . PRO A  403 ? 0.9953 2.3296 3.1173 0.3945  -0.3380 -0.1554 403  PRO A N   
3069  C  CA  . PRO A  403 ? 0.9833 2.4002 3.1091 0.3772  -0.3456 -0.1305 403  PRO A CA  
3070  C  C   . PRO A  403 ? 1.0594 2.5312 3.1661 0.4122  -0.3344 -0.0948 403  PRO A C   
3071  O  O   . PRO A  403 ? 1.2691 2.7907 3.3806 0.4061  -0.3330 -0.0589 403  PRO A O   
3072  C  CB  . PRO A  403 ? 1.1197 2.5665 3.2296 0.3528  -0.3572 -0.1684 403  PRO A CB  
3073  C  CG  . PRO A  403 ? 1.0594 2.4255 3.1677 0.3447  -0.3569 -0.2140 403  PRO A CG  
3074  C  CD  . PRO A  403 ? 1.0332 2.3448 3.1412 0.3831  -0.3411 -0.2069 403  PRO A CD  
3075  N  N   . SER A  404 ? 0.9235 2.3636 2.9614 0.4411  -0.3176 -0.0980 404  SER A N   
3076  C  CA  . SER A  404 ? 0.9082 2.3576 2.8686 0.4673  -0.2977 -0.0596 404  SER A CA  
3077  C  C   . SER A  404 ? 0.8994 2.4356 2.8538 0.4645  -0.3026 -0.0430 404  SER A C   
3078  O  O   . SER A  404 ? 0.8910 2.4533 2.8130 0.4798  -0.2901 -0.0056 404  SER A O   
3079  C  CB  . SER A  404 ? 0.9063 2.3204 2.8515 0.4765  -0.2850 -0.0241 404  SER A CB  
3080  O  OG  . SER A  404 ? 0.9176 2.2542 2.8738 0.4771  -0.2841 -0.0350 404  SER A OG  
3081  N  N   . PHE A  405 ? 0.9049 2.4889 2.8923 0.4457  -0.3220 -0.0731 405  PHE A N   
3082  C  CA  . PHE A  405 ? 0.9004 2.5695 2.8824 0.4418  -0.3306 -0.0578 405  PHE A CA  
3083  C  C   . PHE A  405 ? 1.2906 2.9546 3.1961 0.4748  -0.3131 -0.0328 405  PHE A C   
3084  O  O   . PHE A  405 ? 1.1554 2.7843 3.0266 0.4855  -0.3099 -0.0533 405  PHE A O   
3085  C  CB  . PHE A  405 ? 0.9131 2.6282 2.9384 0.4134  -0.3582 -0.1022 405  PHE A CB  
3086  C  CG  . PHE A  405 ? 1.1427 2.9472 3.1598 0.4072  -0.3717 -0.0878 405  PHE A CG  
3087  C  CD1 . PHE A  405 ? 1.3062 3.1847 3.3699 0.3825  -0.3864 -0.0672 405  PHE A CD1 
3088  C  CD2 . PHE A  405 ? 1.0772 2.8937 3.0428 0.4239  -0.3712 -0.0927 405  PHE A CD2 
3089  C  CE1 . PHE A  405 ? 1.1927 3.1559 3.2503 0.3769  -0.4002 -0.0505 405  PHE A CE1 
3090  C  CE2 . PHE A  405 ? 1.0101 2.9055 2.9689 0.4183  -0.3861 -0.0759 405  PHE A CE2 
3091  C  CZ  . PHE A  405 ? 0.9223 2.8907 2.9268 0.3955  -0.4006 -0.0542 405  PHE A CZ  
3092  N  N   . GLY A  406 ? 1.3792 3.0777 3.2623 0.4911  -0.3014 0.0119  406  GLY A N   
3093  C  CA  . GLY A  406 ? 1.2177 2.9023 3.0409 0.5209  -0.2856 0.0419  406  GLY A CA  
3094  C  C   . GLY A  406 ? 1.0020 2.6278 2.7743 0.5489  -0.2603 0.0665  406  GLY A C   
3095  O  O   . GLY A  406 ? 0.9153 2.5058 2.6458 0.5662  -0.2473 0.0934  406  GLY A O   
3096  N  N   . TYR A  407 ? 0.8787 2.4673 2.6589 0.5448  -0.2565 0.0540  407  TYR A N   
3097  C  CA  . TYR A  407 ? 0.8804 2.4092 2.6068 0.5692  -0.2383 0.0666  407  TYR A CA  
3098  C  C   . TYR A  407 ? 0.8927 2.4386 2.5670 0.5940  -0.2274 0.0817  407  TYR A C   
3099  O  O   . TYR A  407 ? 0.9680 2.4549 2.5741 0.6171  -0.2183 0.0765  407  TYR A O   
3100  C  CB  . TYR A  407 ? 0.8841 2.3715 2.6454 0.5534  -0.2411 0.0564  407  TYR A CB  
3101  C  CG  . TYR A  407 ? 1.0102 2.4333 2.7201 0.5742  -0.2272 0.0673  407  TYR A CG  
3102  C  CD1 . TYR A  407 ? 0.9365 2.2906 2.6100 0.5805  -0.2229 0.0590  407  TYR A CD1 
3103  C  CD2 . TYR A  407 ? 0.8937 2.3261 2.5949 0.5861  -0.2205 0.0821  407  TYR A CD2 
3104  C  CE1 . TYR A  407 ? 0.8977 2.1958 2.5263 0.5963  -0.2142 0.0693  407  TYR A CE1 
3105  C  CE2 . TYR A  407 ? 1.0570 2.4280 2.7146 0.6027  -0.2118 0.0888  407  TYR A CE2 
3106  C  CZ  . TYR A  407 ? 0.9034 2.2089 2.5235 0.6072  -0.2097 0.0840  407  TYR A CZ  
3107  O  OH  . TYR A  407 ? 0.9131 2.1612 2.4928 0.6207  -0.2044 0.0920  407  TYR A OH  
3108  N  N   . SER A  408 ? 1.0229 2.6300 2.7305 0.5878  -0.2399 0.0664  408  SER A N   
3109  C  CA  . SER A  408 ? 0.9105 2.4794 2.6555 0.5947  -0.2485 0.0514  408  SER A CA  
3110  C  C   . SER A  408 ? 0.9114 2.5404 2.7147 0.5808  -0.2608 0.0641  408  SER A C   
3111  O  O   . SER A  408 ? 0.9058 2.5990 2.7511 0.5568  -0.2746 0.0567  408  SER A O   
3112  C  CB  . SER A  408 ? 0.9094 2.5038 2.6742 0.6007  -0.2356 0.0701  408  SER A CB  
3113  O  OG  . SER A  408 ? 0.9004 2.5755 2.7248 0.5758  -0.2414 0.0791  408  SER A OG  
3114  N  N   . MET A  409 ? 0.9217 2.5465 2.7137 0.6012  -0.2567 0.0822  409  MET A N   
3115  C  CA  . MET A  409 ? 0.9329 2.6274 2.7505 0.5961  -0.2671 0.0956  409  MET A CA  
3116  C  C   . MET A  409 ? 1.3184 3.0025 3.0977 0.6257  -0.2535 0.1148  409  MET A C   
3117  O  O   . MET A  409 ? 1.3189 2.9343 3.0488 0.6486  -0.2391 0.1171  409  MET A O   
3118  C  CB  . MET A  409 ? 0.9268 2.6322 2.7495 0.5820  -0.2851 0.0926  409  MET A CB  
3119  C  CG  . MET A  409 ? 0.9241 2.5542 2.6959 0.5948  -0.2792 0.0923  409  MET A CG  
3120  S  SD  . MET A  409 ? 0.9183 2.5854 2.6905 0.5753  -0.2956 0.0909  409  MET A SD  
3121  C  CE  . MET A  409 ? 0.9248 2.5128 2.6229 0.5983  -0.2855 0.0920  409  MET A CE  
3122  N  N   . LYS A  410 ? 1.3021 3.0584 3.1073 0.6248  -0.2591 0.1292  410  LYS A N   
3123  C  CA  . LYS A  410 ? 1.1379 2.8983 2.9179 0.6547  -0.2477 0.1484  410  LYS A CA  
3124  C  C   . LYS A  410 ? 1.0228 2.8545 2.8268 0.6498  -0.2666 0.1591  410  LYS A C   
3125  O  O   . LYS A  410 ? 1.0146 2.9190 2.8696 0.6217  -0.2821 0.1582  410  LYS A O   
3126  C  CB  . LYS A  410 ? 1.0189 2.8025 2.8126 0.6655  -0.2248 0.1614  410  LYS A CB  
3127  C  CG  . LYS A  410 ? 1.0540 2.8280 2.8171 0.7023  -0.2076 0.1790  410  LYS A CG  
3128  C  CD  . LYS A  410 ? 1.0623 2.7384 2.7592 0.7269  -0.1959 0.1740  410  LYS A CD  
3129  C  CE  . LYS A  410 ? 1.3010 2.9617 2.9630 0.7615  -0.1909 0.1875  410  LYS A CE  
3130  N  NZ  . LYS A  410 ? 1.6124 3.3363 3.3013 0.7809  -0.1755 0.2064  410  LYS A NZ  
3131  N  N   . GLY A  411 ? 1.0485 2.8615 2.8158 0.6765  -0.2673 0.1703  411  GLY A N   
3132  C  CA  . GLY A  411 ? 1.0682 2.9480 2.8545 0.6755  -0.2871 0.1831  411  GLY A CA  
3133  C  C   . GLY A  411 ? 1.1067 3.0003 2.8824 0.7108  -0.2768 0.2045  411  GLY A C   
3134  O  O   . GLY A  411 ? 1.1187 2.9923 2.8866 0.7324  -0.2516 0.2105  411  GLY A O   
3135  N  N   . ALA A  412 ? 1.1295 3.0598 2.9050 0.7177  -0.2967 0.2166  412  ALA A N   
3136  C  CA  . ALA A  412 ? 1.2160 3.1591 2.9825 0.7543  -0.2917 0.2379  412  ALA A CA  
3137  C  C   . ALA A  412 ? 1.3622 3.3845 3.1824 0.7593  -0.2811 0.2535  412  ALA A C   
3138  O  O   . ALA A  412 ? 1.4211 3.4428 3.2355 0.7952  -0.2642 0.2685  412  ALA A O   
3139  C  CB  . ALA A  412 ? 1.2112 3.0622 2.9186 0.7902  -0.2702 0.2380  412  ALA A CB  
3140  N  N   . THR A  413 ? 1.1684 3.2616 3.0423 0.7237  -0.2902 0.2509  413  THR A N   
3141  C  CA  . THR A  413 ? 1.1844 3.3661 3.1154 0.7222  -0.2828 0.2682  413  THR A CA  
3142  C  C   . THR A  413 ? 1.1819 3.4553 3.1634 0.6852  -0.3148 0.2731  413  THR A C   
3143  O  O   . THR A  413 ? 1.3094 3.5879 3.3021 0.6467  -0.3308 0.2569  413  THR A O   
3144  C  CB  . THR A  413 ? 1.1659 3.3446 3.1139 0.7134  -0.2558 0.2633  413  THR A CB  
3145  O  OG1 . THR A  413 ? 1.1763 3.2768 3.0757 0.7492  -0.2268 0.2614  413  THR A OG1 
3146  C  CG2 . THR A  413 ? 1.2067 3.4878 3.2183 0.7063  -0.2488 0.2833  413  THR A CG2 
3147  N  N   . ASP A  414 ? 1.2159 3.5635 3.2294 0.6966  -0.3249 0.2956  414  ASP A N   
3148  C  CA  . ASP A  414 ? 1.2219 3.6634 3.2829 0.6612  -0.3580 0.3038  414  ASP A CA  
3149  C  C   . ASP A  414 ? 1.2185 3.7408 3.3433 0.6357  -0.3491 0.3124  414  ASP A C   
3150  O  O   . ASP A  414 ? 1.2469 3.8321 3.4085 0.6529  -0.3381 0.3349  414  ASP A O   
3151  C  CB  . ASP A  414 ? 1.2635 3.7463 3.3275 0.6851  -0.3766 0.3259  414  ASP A CB  
3152  C  CG  . ASP A  414 ? 1.2735 3.8486 3.3776 0.6462  -0.4156 0.3342  414  ASP A CG  
3153  O  OD1 . ASP A  414 ? 1.2473 3.8346 3.3601 0.6006  -0.4329 0.3172  414  ASP A OD1 
3154  O  OD2 . ASP A  414 ? 1.3115 3.9479 3.4387 0.6611  -0.4301 0.3578  414  ASP A OD2 
3155  N  N   . ILE A  415 ? 1.1861 3.7096 3.3265 0.5936  -0.3544 0.2956  415  ILE A N   
3156  C  CA  . ILE A  415 ? 1.2801 3.8660 3.4749 0.5674  -0.3422 0.3032  415  ILE A CA  
3157  C  C   . ILE A  415 ? 1.2023 3.9041 3.4594 0.5327  -0.3688 0.3212  415  ILE A C   
3158  O  O   . ILE A  415 ? 1.2102 3.9806 3.5179 0.5174  -0.3571 0.3370  415  ILE A O   
3159  C  CB  . ILE A  415 ? 1.1418 3.6826 3.3312 0.5353  -0.3393 0.2799  415  ILE A CB  
3160  C  CG1 . ILE A  415 ? 1.1366 3.7111 3.3639 0.5234  -0.3139 0.2900  415  ILE A CG1 
3161  C  CG2 . ILE A  415 ? 1.1311 3.7050 3.3405 0.4853  -0.3770 0.2661  415  ILE A CG2 
3162  C  CD1 . ILE A  415 ? 1.1025 3.6315 3.3260 0.4956  -0.3102 0.2705  415  ILE A CD1 
3163  N  N   . ASP A  416 ? 1.2164 3.9457 3.4704 0.5191  -0.4045 0.3216  416  ASP A N   
3164  C  CA  . ASP A  416 ? 1.2411 4.0791 3.5501 0.4811  -0.4347 0.3379  416  ASP A CA  
3165  C  C   . ASP A  416 ? 1.2825 4.1715 3.6006 0.5107  -0.4466 0.3634  416  ASP A C   
3166  O  O   . ASP A  416 ? 1.3079 4.2834 3.6636 0.4802  -0.4783 0.3773  416  ASP A O   
3167  C  CB  . ASP A  416 ? 1.2297 4.0744 3.5348 0.4288  -0.4727 0.3179  416  ASP A CB  
3168  C  CG  . ASP A  416 ? 1.2309 4.0229 3.4795 0.4443  -0.4923 0.3060  416  ASP A CG  
3169  O  OD1 . ASP A  416 ? 1.2275 3.9469 3.4301 0.4929  -0.4719 0.3055  416  ASP A OD1 
3170  O  OD2 . ASP A  416 ? 1.2388 4.0632 3.4870 0.4046  -0.5289 0.2974  416  ASP A OD2 
3171  N  N   . LYS A  417 ? 1.2941 4.1317 3.5789 0.5679  -0.4236 0.3703  417  LYS A N   
3172  C  CA  . LYS A  417 ? 1.3378 4.2202 3.6342 0.6025  -0.4319 0.3962  417  LYS A CA  
3173  C  C   . LYS A  417 ? 1.3556 4.2687 3.6433 0.5810  -0.4779 0.3993  417  LYS A C   
3174  O  O   . LYS A  417 ? 1.3939 4.3881 3.7169 0.5821  -0.4994 0.4239  417  LYS A O   
3175  C  CB  . LYS A  417 ? 1.3648 4.3489 3.7310 0.6041  -0.4200 0.4231  417  LYS A CB  
3176  C  CG  . LYS A  417 ? 1.3760 4.3369 3.7482 0.6289  -0.3729 0.4233  417  LYS A CG  
3177  C  CD  . LYS A  417 ? 1.3716 4.2610 3.7004 0.6936  -0.3453 0.4249  417  LYS A CD  
3178  C  CE  . LYS A  417 ? 1.4221 4.3735 3.7795 0.7290  -0.3544 0.4525  417  LYS A CE  
3179  N  NZ  . LYS A  417 ? 1.4458 4.3268 3.7624 0.7919  -0.3285 0.4540  417  LYS A NZ  
3180  N  N   . ASN A  418 ? 1.4520 4.3019 3.6916 0.5614  -0.4930 0.3749  418  ASN A N   
3181  C  CA  . ASN A  418 ? 1.4494 4.3197 3.6692 0.5362  -0.5357 0.3732  418  ASN A CA  
3182  C  C   . ASN A  418 ? 1.3634 4.1790 3.5294 0.5792  -0.5407 0.3799  418  ASN A C   
3183  O  O   . ASN A  418 ? 1.3805 4.2127 3.5237 0.5627  -0.5758 0.3818  418  ASN A O   
3184  C  CB  . ASN A  418 ? 1.4811 4.3169 3.6791 0.4903  -0.5476 0.3419  418  ASN A CB  
3185  C  CG  . ASN A  418 ? 1.2786 4.0008 3.4121 0.5165  -0.5280 0.3198  418  ASN A CG  
3186  O  OD1 . ASN A  418 ? 1.2740 3.9350 3.3864 0.5621  -0.4954 0.3232  418  ASN A OD1 
3187  N  ND2 . ASN A  418 ? 1.2597 3.9549 3.3633 0.4853  -0.5463 0.2960  418  ASN A ND2 
3188  N  N   . GLY A  419 ? 1.3650 4.1158 3.5076 0.6317  -0.5075 0.3839  419  GLY A N   
3189  C  CA  . GLY A  419 ? 1.3866 4.0787 3.4776 0.6727  -0.5107 0.3910  419  GLY A CA  
3190  C  C   . GLY A  419 ? 1.3549 3.9416 3.3791 0.6755  -0.5011 0.3658  419  GLY A C   
3191  O  O   . GLY A  419 ? 1.3721 3.9002 3.3482 0.7089  -0.5012 0.3711  419  GLY A O   
3192  N  N   . TYR A  420 ? 1.3155 3.8783 3.3376 0.6412  -0.4937 0.3398  420  TYR A N   
3193  C  CA  . TYR A  420 ? 1.4536 3.9246 3.4191 0.6397  -0.4853 0.3152  420  TYR A CA  
3194  C  C   . TYR A  420 ? 1.3399 3.7580 3.3089 0.6385  -0.4507 0.2960  420  TYR A C   
3195  O  O   . TYR A  420 ? 1.4486 3.9148 3.4653 0.6101  -0.4471 0.2918  420  TYR A O   
3196  C  CB  . TYR A  420 ? 1.5009 3.9973 3.4554 0.5937  -0.5184 0.2997  420  TYR A CB  
3197  C  CG  . TYR A  420 ? 1.5694 4.1169 3.5113 0.5895  -0.5559 0.3174  420  TYR A CG  
3198  C  CD1 . TYR A  420 ? 1.4048 4.0526 3.3947 0.5687  -0.5827 0.3365  420  TYR A CD1 
3199  C  CD2 . TYR A  420 ? 1.4343 3.9324 3.3155 0.6045  -0.5659 0.3166  420  TYR A CD2 
3200  C  CE1 . TYR A  420 ? 1.3780 4.0730 3.3544 0.5634  -0.6194 0.3542  420  TYR A CE1 
3201  C  CE2 . TYR A  420 ? 1.3650 3.9111 3.2314 0.5995  -0.6018 0.3346  420  TYR A CE2 
3202  C  CZ  . TYR A  420 ? 1.3868 4.0301 3.3002 0.5790  -0.6290 0.3532  420  TYR A CZ  
3203  O  OH  . TYR A  420 ? 1.4303 4.1207 3.3264 0.5728  -0.6669 0.3726  420  TYR A OH  
3204  N  N   . PRO A  421 ? 1.2298 3.5502 3.1482 0.6660  -0.4271 0.2852  421  PRO A N   
3205  C  CA  . PRO A  421 ? 1.3930 3.6599 3.3100 0.6639  -0.3965 0.2676  421  PRO A CA  
3206  C  C   . PRO A  421 ? 1.4346 3.6987 3.3589 0.6202  -0.4071 0.2431  421  PRO A C   
3207  O  O   . PRO A  421 ? 1.4170 3.6783 3.3191 0.6023  -0.4298 0.2333  421  PRO A O   
3208  C  CB  . PRO A  421 ? 1.4702 3.6349 3.3249 0.7030  -0.3754 0.2645  421  PRO A CB  
3209  C  CG  . PRO A  421 ? 1.4775 3.6338 3.2953 0.7097  -0.4007 0.2711  421  PRO A CG  
3210  C  CD  . PRO A  421 ? 1.2496 3.5055 3.1096 0.7001  -0.4281 0.2912  421  PRO A CD  
3211  N  N   . ASP A  422 ? 1.3726 3.6424 3.3296 0.6030  -0.3908 0.2338  422  ASP A N   
3212  C  CA  . ASP A  422 ? 1.1048 3.3797 3.0808 0.5612  -0.4005 0.2117  422  ASP A CA  
3213  C  C   . ASP A  422 ? 1.0752 3.2587 3.0223 0.5715  -0.3744 0.1936  422  ASP A C   
3214  O  O   . ASP A  422 ? 1.0806 3.1987 2.9899 0.6075  -0.3506 0.1979  422  ASP A O   
3215  C  CB  . ASP A  422 ? 1.1067 3.4714 3.1496 0.5266  -0.4089 0.2180  422  ASP A CB  
3216  C  CG  . ASP A  422 ? 1.1417 3.5983 3.2142 0.5190  -0.4336 0.2400  422  ASP A CG  
3217  O  OD1 . ASP A  422 ? 1.1665 3.6452 3.2482 0.5498  -0.4206 0.2624  422  ASP A OD1 
3218  O  OD2 . ASP A  422 ? 1.1480 3.6561 3.2339 0.4825  -0.4669 0.2349  422  ASP A OD2 
3219  N  N   . LEU A  423 ? 1.1308 3.3109 3.0967 0.5385  -0.3807 0.1732  423  LEU A N   
3220  C  CA  . LEU A  423 ? 1.2699 3.3644 3.2088 0.5450  -0.3623 0.1549  423  LEU A CA  
3221  C  C   . LEU A  423 ? 1.2009 3.3126 3.1854 0.5144  -0.3600 0.1422  423  LEU A C   
3222  O  O   . LEU A  423 ? 1.2387 3.4094 3.2631 0.4765  -0.3831 0.1342  423  LEU A O   
3223  C  CB  . LEU A  423 ? 1.0117 3.0655 2.9114 0.5425  -0.3745 0.1407  423  LEU A CB  
3224  C  CG  . LEU A  423 ? 0.9834 2.9626 2.8654 0.5408  -0.3608 0.1213  423  LEU A CG  
3225  C  CD1 . LEU A  423 ? 1.2666 3.1623 3.1092 0.5750  -0.3327 0.1259  423  LEU A CD1 
3226  C  CD2 . LEU A  423 ? 0.9998 2.9668 2.8497 0.5334  -0.3743 0.1089  423  LEU A CD2 
3227  N  N   . ILE A  424 ? 0.9858 3.0469 2.9620 0.5296  -0.3342 0.1403  424  ILE A N   
3228  C  CA  . ILE A  424 ? 0.9650 3.0304 2.9768 0.5053  -0.3305 0.1287  424  ILE A CA  
3229  C  C   . ILE A  424 ? 1.2828 3.2643 3.2661 0.5109  -0.3251 0.1074  424  ILE A C   
3230  O  O   . ILE A  424 ? 1.1725 3.0780 3.1039 0.5413  -0.3090 0.1077  424  ILE A O   
3231  C  CB  . ILE A  424 ? 0.9714 3.0491 2.9946 0.5159  -0.3059 0.1450  424  ILE A CB  
3232  C  CG1 . ILE A  424 ? 1.2411 3.4052 3.2969 0.5129  -0.3084 0.1693  424  ILE A CG1 
3233  C  CG2 . ILE A  424 ? 0.9537 3.0445 3.0134 0.4876  -0.3045 0.1379  424  ILE A CG2 
3234  C  CD1 . ILE A  424 ? 1.4385 3.6180 3.5021 0.5291  -0.2796 0.1898  424  ILE A CD1 
3235  N  N   . VAL A  425 ? 1.4057 3.4021 3.4254 0.4806  -0.3390 0.0899  425  VAL A N   
3236  C  CA  . VAL A  425 ? 1.2759 3.1968 3.2741 0.4821  -0.3331 0.0739  425  VAL A CA  
3237  C  C   . VAL A  425 ? 1.1905 3.1295 3.1911 0.4708  -0.3269 0.0538  425  VAL A C   
3238  O  O   . VAL A  425 ? 1.0360 3.0589 3.0809 0.4372  -0.3398 0.0612  425  VAL A O   
3239  C  CB  . VAL A  425 ? 1.2735 3.2146 3.2715 0.4625  -0.3477 0.0806  425  VAL A CB  
3240  C  CG1 . VAL A  425 ? 1.2082 3.1049 3.1592 0.4711  -0.3311 0.0720  425  VAL A CG1 
3241  C  CG2 . VAL A  425 ? 1.2421 3.1852 3.1987 0.4815  -0.3551 0.0808  425  VAL A CG2 
3242  N  N   . GLY A  426 ? 1.2211 3.1068 3.1686 0.4964  -0.3027 0.0582  426  GLY A N   
3243  C  CA  . GLY A  426 ? 1.1141 2.9961 3.0930 0.4800  -0.2941 0.0775  426  GLY A CA  
3244  C  C   . GLY A  426 ? 0.8839 2.6940 2.8697 0.4639  -0.2984 0.0651  426  GLY A C   
3245  O  O   . GLY A  426 ? 0.8817 2.6410 2.8187 0.4826  -0.2924 0.0552  426  GLY A O   
3246  N  N   . ALA A  427 ? 0.8973 2.6950 2.9514 0.4277  -0.3120 0.0557  427  ALA A N   
3247  C  CA  . ALA A  427 ? 0.8964 2.6147 2.9710 0.4142  -0.3209 0.0235  427  ALA A CA  
3248  C  C   . ALA A  427 ? 0.9024 2.5833 3.0216 0.3982  -0.3197 0.0362  427  ALA A C   
3249  O  O   . ALA A  427 ? 1.0203 2.7178 3.2156 0.3600  -0.3399 0.0291  427  ALA A O   
3250  C  CB  . ALA A  427 ? 0.9066 2.6509 3.0317 0.3822  -0.3493 -0.0157 427  ALA A CB  
3251  N  N   . PHE A  428 ? 0.8993 2.5256 2.9719 0.4249  -0.2986 0.0551  428  PHE A N   
3252  C  CA  . PHE A  428 ? 0.9058 2.5075 3.0175 0.4111  -0.2967 0.0768  428  PHE A CA  
3253  C  C   . PHE A  428 ? 0.9196 2.4580 3.0898 0.3868  -0.3151 0.0541  428  PHE A C   
3254  O  O   . PHE A  428 ? 0.9373 2.4654 3.1521 0.3593  -0.3217 0.0709  428  PHE A O   
3255  C  CB  . PHE A  428 ? 0.9031 2.4607 2.9478 0.4453  -0.2727 0.0989  428  PHE A CB  
3256  C  CG  . PHE A  428 ? 0.9050 2.3747 2.8976 0.4663  -0.2678 0.0808  428  PHE A CG  
3257  C  CD1 . PHE A  428 ? 0.9161 2.3133 2.9350 0.4568  -0.2744 0.0765  428  PHE A CD1 
3258  C  CD2 . PHE A  428 ? 0.9484 2.4103 2.8683 0.4944  -0.2576 0.0707  428  PHE A CD2 
3259  C  CE1 . PHE A  428 ? 0.9202 2.2431 2.8921 0.4750  -0.2698 0.0612  428  PHE A CE1 
3260  C  CE2 . PHE A  428 ? 1.3616 2.7494 3.2355 0.5096  -0.2526 0.0575  428  PHE A CE2 
3261  C  CZ  . PHE A  428 ? 0.9120 2.2323 2.8113 0.4999  -0.2582 0.0520  428  PHE A CZ  
3262  N  N   . GLY A  429 ? 0.9239 2.4136 3.0805 0.3945  -0.3212 0.0161  429  GLY A N   
3263  C  CA  . GLY A  429 ? 1.1460 2.5584 3.3300 0.3754  -0.3328 -0.0101 429  GLY A CA  
3264  C  C   . GLY A  429 ? 1.1812 2.5972 3.3951 0.3250  -0.3504 -0.0241 429  GLY A C   
3265  O  O   . GLY A  429 ? 1.2906 2.6345 3.5220 0.3036  -0.3586 -0.0348 429  GLY A O   
3266  N  N   . VAL A  430 ? 1.0020 2.4986 3.2220 0.3049  -0.3582 -0.0233 430  VAL A N   
3267  C  CA  . VAL A  430 ? 1.0492 2.5597 3.2961 0.2519  -0.3773 -0.0325 430  VAL A CA  
3268  C  C   . VAL A  430 ? 1.0389 2.6375 3.3147 0.2312  -0.3782 0.0106  430  VAL A C   
3269  O  O   . VAL A  430 ? 1.0725 2.7078 3.3715 0.1854  -0.3955 0.0085  430  VAL A O   
3270  C  CB  . VAL A  430 ? 1.0889 2.6150 3.3186 0.2361  -0.3909 -0.0762 430  VAL A CB  
3271  C  CG1 . VAL A  430 ? 1.1021 2.5328 3.3118 0.2451  -0.3900 -0.1227 430  VAL A CG1 
3272  C  CG2 . VAL A  430 ? 1.0528 2.6608 3.2597 0.2659  -0.3850 -0.0694 430  VAL A CG2 
3273  N  N   . ASP A  431 ? 1.0977 2.7321 3.3716 0.2639  -0.3593 0.0493  431  ASP A N   
3274  C  CA  . ASP A  431 ? 0.9859 2.7069 3.2883 0.2521  -0.3533 0.0932  431  ASP A CA  
3275  C  C   . ASP A  431 ? 0.9820 2.8065 3.3018 0.2344  -0.3653 0.0929  431  ASP A C   
3276  O  O   . ASP A  431 ? 1.0930 2.9660 3.4487 0.1882  -0.3787 0.1056  431  ASP A O   
3277  C  CB  . ASP A  431 ? 1.0874 2.7765 3.4202 0.2083  -0.3594 0.1130  431  ASP A CB  
3278  C  CG  . ASP A  431 ? 1.3745 2.9598 3.6919 0.2231  -0.3520 0.1155  431  ASP A CG  
3279  O  OD1 . ASP A  431 ? 1.5128 3.1007 3.8144 0.2573  -0.3323 0.1432  431  ASP A OD1 
3280  O  OD2 . ASP A  431 ? 1.6384 3.1380 3.9583 0.2015  -0.3665 0.0892  431  ASP A OD2 
3281  N  N   . ARG A  432 ? 0.9505 2.8098 3.2446 0.2703  -0.3620 0.0810  432  ARG A N   
3282  C  CA  . ARG A  432 ? 0.9496 2.9027 3.2561 0.2559  -0.3769 0.0792  432  ARG A CA  
3283  C  C   . ARG A  432 ? 0.9166 2.9198 3.1829 0.3073  -0.3607 0.0924  432  ARG A C   
3284  O  O   . ARG A  432 ? 0.9047 2.8442 3.1068 0.3490  -0.3419 0.0841  432  ARG A O   
3285  C  CB  . ARG A  432 ? 0.9875 2.9014 3.2763 0.2250  -0.4000 0.0314  432  ARG A CB  
3286  C  CG  . ARG A  432 ? 1.0609 3.0512 3.3769 0.1749  -0.4251 0.0310  432  ARG A CG  
3287  C  CD  . ARG A  432 ? 1.1232 3.0964 3.4764 0.1213  -0.4352 0.0418  432  ARG A CD  
3288  N  NE  . ARG A  432 ? 1.1696 3.0202 3.5064 0.1015  -0.4401 0.0075  432  ARG A NE  
3289  C  CZ  . ARG A  432 ? 1.1689 2.9774 3.5001 0.0544  -0.4632 -0.0290 432  ARG A CZ  
3290  N  NH1 . ARG A  432 ? 1.1898 3.0701 3.5273 0.0179  -0.4856 -0.0355 432  ARG A NH1 
3291  N  NH2 . ARG A  432 ? 1.3401 3.0327 3.6583 0.0440  -0.4647 -0.0591 432  ARG A NH2 
3292  N  N   . ALA A  433 ? 1.1390 3.2392 3.4119 0.3003  -0.3655 0.1092  433  ALA A N   
3293  C  CA  . ALA A  433 ? 1.0718 3.2034 3.2849 0.3422  -0.3542 0.1081  433  ALA A CA  
3294  C  C   . ALA A  433 ? 0.9246 3.1391 3.1651 0.3161  -0.3822 0.1010  433  ALA A C   
3295  O  O   . ALA A  433 ? 0.9398 3.2197 3.2380 0.2703  -0.4002 0.1140  433  ALA A O   
3296  C  CB  . ALA A  433 ? 1.0439 3.1850 3.2375 0.3701  -0.3278 0.1317  433  ALA A CB  
3297  N  N   . ILE A  434 ? 0.9213 3.1286 3.1218 0.3418  -0.3884 0.0816  434  ILE A N   
3298  C  CA  . ILE A  434 ? 0.9354 3.2042 3.1592 0.3157  -0.4193 0.0752  434  ILE A CA  
3299  C  C   . ILE A  434 ? 1.0097 3.2764 3.1967 0.3489  -0.4123 0.0926  434  ILE A C   
3300  O  O   . ILE A  434 ? 1.0200 3.2155 3.1560 0.3904  -0.3945 0.0916  434  ILE A O   
3301  C  CB  . ILE A  434 ? 0.9293 3.1831 3.1432 0.3006  -0.4368 0.0538  434  ILE A CB  
3302  C  CG1 . ILE A  434 ? 1.1783 3.3509 3.4109 0.2676  -0.4398 0.0194  434  ILE A CG1 
3303  C  CG2 . ILE A  434 ? 0.9539 3.2783 3.1793 0.2670  -0.4717 0.0393  434  ILE A CG2 
3304  C  CD1 . ILE A  434 ? 1.1307 3.1999 3.3331 0.3040  -0.4148 0.0071  434  ILE A CD1 
3305  N  N   . LEU A  435 ? 1.0767 3.4226 3.2887 0.3285  -0.4273 0.1105  435  LEU A N   
3306  C  CA  . LEU A  435 ? 1.0323 3.3922 3.2152 0.3573  -0.4248 0.1291  435  LEU A CA  
3307  C  C   . LEU A  435 ? 1.0086 3.3999 3.1779 0.3410  -0.4561 0.1208  435  LEU A C   
3308  O  O   . LEU A  435 ? 1.0856 3.5480 3.2900 0.2939  -0.4861 0.1162  435  LEU A O   
3309  C  CB  . LEU A  435 ? 1.0159 3.4492 3.2354 0.3493  -0.4206 0.1570  435  LEU A CB  
3310  C  CG  . LEU A  435 ? 1.0419 3.5036 3.2433 0.3784  -0.4202 0.1784  435  LEU A CG  
3311  C  CD1 . LEU A  435 ? 1.0376 3.4211 3.1866 0.4354  -0.3888 0.1836  435  LEU A CD1 
3312  C  CD2 . LEU A  435 ? 1.0666 3.6208 3.3189 0.3596  -0.4225 0.2047  435  LEU A CD2 
3313  N  N   . TYR A  436 ? 1.0086 3.3493 3.1229 0.3762  -0.4504 0.1196  436  TYR A N   
3314  C  CA  . TYR A  436 ? 1.0274 3.4001 3.1165 0.3662  -0.4777 0.1154  436  TYR A CA  
3315  C  C   . TYR A  436 ? 1.0557 3.4603 3.1328 0.3905  -0.4801 0.1432  436  TYR A C   
3316  O  O   . TYR A  436 ? 1.0556 3.4084 3.1026 0.4352  -0.4552 0.1564  436  TYR A O   
3317  C  CB  . TYR A  436 ? 1.0130 3.3163 3.0469 0.3859  -0.4710 0.0965  436  TYR A CB  
3318  C  CG  . TYR A  436 ? 0.9919 3.2754 3.0359 0.3619  -0.4720 0.0649  436  TYR A CG  
3319  C  CD1 . TYR A  436 ? 1.0050 3.3436 3.0558 0.3202  -0.5019 0.0336  436  TYR A CD1 
3320  C  CD2 . TYR A  436 ? 0.9652 3.1758 3.0091 0.3806  -0.4441 0.0610  436  TYR A CD2 
3321  C  CE1 . TYR A  436 ? 0.9946 3.3097 3.0530 0.3017  -0.5032 -0.0126 436  TYR A CE1 
3322  C  CE2 . TYR A  436 ? 1.0110 3.2029 3.0622 0.3626  -0.4447 0.0275  436  TYR A CE2 
3323  C  CZ  . TYR A  436 ? 1.0498 3.2879 3.1108 0.3249  -0.4746 -0.0169 436  TYR A CZ  
3324  O  OH  . TYR A  436 ? 1.0540 3.2231 3.1110 0.3040  -0.4726 -0.0644 436  TYR A OH  
3325  N  N   . ARG A  437 ? 1.0841 3.5736 3.1837 0.3600  -0.5114 0.1514  437  ARG A N   
3326  C  CA  . ARG A  437 ? 1.1158 3.6493 3.2143 0.3797  -0.5181 0.1799  437  ARG A CA  
3327  C  C   . ARG A  437 ? 1.1343 3.6636 3.1829 0.3904  -0.5383 0.1801  437  ARG A C   
3328  O  O   . ARG A  437 ? 1.1382 3.6881 3.1724 0.3573  -0.5641 0.1604  437  ARG A O   
3329  C  CB  . ARG A  437 ? 1.1417 3.7759 3.2973 0.3386  -0.5416 0.1935  437  ARG A CB  
3330  C  CG  . ARG A  437 ? 1.1301 3.7812 3.3361 0.3275  -0.5215 0.1997  437  ARG A CG  
3331  C  CD  . ARG A  437 ? 1.1618 3.9166 3.4222 0.2858  -0.5456 0.2172  437  ARG A CD  
3332  N  NE  . ARG A  437 ? 1.2352 4.0295 3.5094 0.2236  -0.5834 0.1976  437  ARG A NE  
3333  C  CZ  . ARG A  437 ? 1.2126 4.0879 3.5059 0.1837  -0.6200 0.2067  437  ARG A CZ  
3334  N  NH1 . ARG A  437 ? 1.2410 4.1692 3.5470 0.2037  -0.6230 0.2374  437  ARG A NH1 
3335  N  NH2 . ARG A  437 ? 1.2286 4.1316 3.5268 0.1230  -0.6548 0.1844  437  ARG A NH2 
3336  N  N   . ALA A  438 ? 1.1499 3.6557 3.1705 0.4355  -0.5272 0.2016  438  ALA A N   
3337  C  CA  . ALA A  438 ? 1.1713 3.6724 3.1430 0.4485  -0.5460 0.2066  438  ALA A CA  
3338  C  C   . ALA A  438 ? 1.4110 4.0089 3.4033 0.4190  -0.5854 0.2213  438  ALA A C   
3339  O  O   . ALA A  438 ? 1.3848 4.0370 3.4168 0.4235  -0.5883 0.2455  438  ALA A O   
3340  C  CB  . ALA A  438 ? 1.1805 3.6223 3.1174 0.5050  -0.5230 0.2257  438  ALA A CB  
3341  N  N   . ARG A  439 ? 1.7987 3.3472 2.8071 0.0655  -0.4264 -0.1352 439  ARG A N   
3342  C  CA  . ARG A  439 ? 1.8408 3.4295 2.8361 0.0469  -0.4426 -0.1360 439  ARG A CA  
3343  C  C   . ARG A  439 ? 1.8873 3.5033 2.8538 0.0980  -0.4393 -0.1433 439  ARG A C   
3344  O  O   . ARG A  439 ? 1.8552 3.4072 2.7960 0.1361  -0.4254 -0.1589 439  ARG A O   
3345  C  CB  . ARG A  439 ? 1.8994 3.3949 2.8738 0.0099  -0.4486 -0.1577 439  ARG A CB  
3346  C  CG  . ARG A  439 ? 1.9304 3.3868 2.9213 -0.0403 -0.4570 -0.1525 439  ARG A CG  
3347  C  CD  . ARG A  439 ? 2.0059 3.3480 2.9684 -0.0603 -0.4587 -0.1800 439  ARG A CD  
3348  N  NE  . ARG A  439 ? 2.0367 3.3776 2.9744 -0.0773 -0.4723 -0.1901 439  ARG A NE  
3349  C  CZ  . ARG A  439 ? 2.1238 3.3755 3.0317 -0.0905 -0.4751 -0.2152 439  ARG A CZ  
3350  N  NH1 . ARG A  439 ? 2.1716 3.3329 3.0709 -0.0870 -0.4653 -0.2332 439  ARG A NH1 
3351  N  NH2 . ARG A  439 ? 2.2055 3.4614 3.0910 -0.1053 -0.4880 -0.2228 439  ARG A NH2 
3352  N  N   . PRO A  440 ? 2.0531 3.7622 3.0195 0.0994  -0.4534 -0.1320 440  PRO A N   
3353  C  CA  . PRO A  440 ? 2.0817 3.8106 3.0129 0.1503  -0.4535 -0.1403 440  PRO A CA  
3354  C  C   . PRO A  440 ? 2.1540 3.7771 3.0425 0.1521  -0.4502 -0.1687 440  PRO A C   
3355  O  O   . PRO A  440 ? 2.2774 3.8475 3.1647 0.1095  -0.4547 -0.1800 440  PRO A O   
3356  C  CB  . PRO A  440 ? 2.0299 3.8813 2.9737 0.1392  -0.4719 -0.1232 440  PRO A CB  
3357  C  CG  . PRO A  440 ? 1.9199 3.8377 2.9111 0.0927  -0.4779 -0.0988 440  PRO A CG  
3358  C  CD  . PRO A  440 ? 1.9533 3.7585 2.9492 0.0549  -0.4711 -0.1096 440  PRO A CD  
3359  N  N   . VAL A  441 ? 2.1070 3.6974 2.9554 0.2022  -0.4435 -0.1800 441  VAL A N   
3360  C  CA  . VAL A  441 ? 2.1553 3.6446 2.9585 0.2070  -0.4386 -0.2058 441  VAL A CA  
3361  C  C   . VAL A  441 ? 2.2809 3.8015 3.0481 0.2252  -0.4523 -0.2109 441  VAL A C   
3362  O  O   . VAL A  441 ? 2.3358 3.9096 3.0835 0.2709  -0.4577 -0.2030 441  VAL A O   
3363  C  CB  . VAL A  441 ? 2.1352 3.5500 2.9108 0.2431  -0.4226 -0.2151 441  VAL A CB  
3364  C  CG1 . VAL A  441 ? 2.1040 3.4221 2.8319 0.2418  -0.4180 -0.2402 441  VAL A CG1 
3365  C  CG2 . VAL A  441 ? 2.1321 3.5212 2.9453 0.2261  -0.4095 -0.2100 441  VAL A CG2 
3366  N  N   . ILE A  442 ? 2.2835 3.7709 3.0397 0.1915  -0.4591 -0.2245 442  ILE A N   
3367  C  CA  . ILE A  442 ? 2.1841 3.6928 2.9057 0.2026  -0.4727 -0.2314 442  ILE A CA  
3368  C  C   . ILE A  442 ? 2.1881 3.5936 2.8532 0.2215  -0.4654 -0.2550 442  ILE A C   
3369  O  O   . ILE A  442 ? 2.3081 3.6314 2.9686 0.1946  -0.4558 -0.2712 442  ILE A O   
3370  C  CB  . ILE A  442 ? 2.0772 3.6152 2.8189 0.1514  -0.4867 -0.2305 442  ILE A CB  
3371  C  CG1 . ILE A  442 ? 1.9422 3.5670 2.7389 0.1193  -0.4935 -0.2061 442  ILE A CG1 
3372  C  CG2 . ILE A  442 ? 2.1057 3.6875 2.8174 0.1659  -0.5024 -0.2336 442  ILE A CG2 
3373  C  CD1 . ILE A  442 ? 1.8676 3.6161 2.6801 0.1508  -0.5008 -0.1838 442  ILE A CD1 
3374  N  N   . THR A  443 ? 2.0794 3.4885 2.6977 0.2685  -0.4707 -0.2570 443  THR A N   
3375  C  CA  . THR A  443 ? 2.1457 3.4628 2.7011 0.2832  -0.4685 -0.2773 443  THR A CA  
3376  C  C   . THR A  443 ? 2.3388 3.6719 2.8691 0.2748  -0.4841 -0.2856 443  THR A C   
3377  O  O   . THR A  443 ? 2.4615 3.8738 2.9875 0.2987  -0.4992 -0.2755 443  THR A O   
3378  C  CB  . THR A  443 ? 2.1493 3.4436 2.6562 0.3385  -0.4682 -0.2748 443  THR A CB  
3379  O  OG1 . THR A  443 ? 2.1211 3.3869 2.6484 0.3417  -0.4526 -0.2693 443  THR A OG1 
3380  C  CG2 . THR A  443 ? 2.2655 3.4686 2.6985 0.3506  -0.4705 -0.2933 443  THR A CG2 
3381  N  N   . VAL A  444 ? 2.4371 3.6996 2.9506 0.2427  -0.4806 -0.3042 444  VAL A N   
3382  C  CA  . VAL A  444 ? 2.4079 3.6766 2.8992 0.2286  -0.4945 -0.3137 444  VAL A CA  
3383  C  C   . VAL A  444 ? 2.5311 3.7128 2.9517 0.2459  -0.4932 -0.3325 444  VAL A C   
3384  O  O   . VAL A  444 ? 2.7093 3.8102 3.1125 0.2365  -0.4785 -0.3446 444  VAL A O   
3385  C  CB  . VAL A  444 ? 2.3838 3.6467 2.9123 0.1729  -0.4949 -0.3192 444  VAL A CB  
3386  C  CG1 . VAL A  444 ? 2.5283 3.7081 3.0643 0.1511  -0.4766 -0.3321 444  VAL A CG1 
3387  C  CG2 . VAL A  444 ? 2.4044 3.6546 2.9020 0.1580  -0.5077 -0.3324 444  VAL A CG2 
3388  N  N   . ASN A  445 ? 2.5030 3.7040 2.8807 0.2707  -0.5094 -0.3344 445  ASN A N   
3389  C  CA  . ASN A  445 ? 2.6750 3.7953 2.9795 0.2827  -0.5125 -0.3515 445  ASN A CA  
3390  C  C   . ASN A  445 ? 2.7730 3.9013 3.0706 0.2564  -0.5240 -0.3620 445  ASN A C   
3391  O  O   . ASN A  445 ? 2.7664 3.9636 3.0631 0.2708  -0.5413 -0.3552 445  ASN A O   
3392  C  CB  . ASN A  445 ? 2.7098 3.8280 2.9547 0.3396  -0.5244 -0.3463 445  ASN A CB  
3393  C  CG  . ASN A  445 ? 2.6014 3.6772 2.8321 0.3636  -0.5132 -0.3407 445  ASN A CG  
3394  O  OD1 . ASN A  445 ? 2.5213 3.6444 2.7539 0.4034  -0.5190 -0.3267 445  ASN A OD1 
3395  N  ND2 . ASN A  445 ? 2.6188 3.6083 2.8334 0.3400  -0.4977 -0.3515 445  ASN A ND2 
3396  N  N   . ALA A  446 ? 2.7938 3.8573 3.0878 0.2184  -0.5145 -0.3785 446  ALA A N   
3397  C  CA  . ALA A  446 ? 2.7915 3.8501 3.0747 0.1918  -0.5243 -0.3905 446  ALA A CA  
3398  C  C   . ALA A  446 ? 2.8493 3.8338 3.0561 0.2041  -0.5274 -0.4068 446  ALA A C   
3399  O  O   . ALA A  446 ? 2.8176 3.7309 2.9867 0.2110  -0.5158 -0.4140 446  ALA A O   
3400  C  CB  . ALA A  446 ? 2.6900 3.7254 3.0136 0.1433  -0.5147 -0.3995 446  ALA A CB  
3401  N  N   . GLY A  447 ? 3.0433 4.0460 3.2259 0.2039  -0.5440 -0.4117 447  GLY A N   
3402  C  CA  . GLY A  447 ? 3.2188 4.1540 3.3267 0.2129  -0.5499 -0.4266 447  GLY A CA  
3403  C  C   . GLY A  447 ? 3.3356 4.2579 3.4424 0.1771  -0.5545 -0.4410 447  GLY A C   
3404  O  O   . GLY A  447 ? 3.4411 4.4201 3.5967 0.1535  -0.5611 -0.4367 447  GLY A O   
3405  N  N   . LEU A  448 ? 3.1228 3.9678 3.1692 0.1713  -0.5521 -0.4576 448  LEU A N   
3406  C  CA  . LEU A  448 ? 2.9554 3.7803 2.9927 0.1397  -0.5562 -0.4732 448  LEU A CA  
3407  C  C   . LEU A  448 ? 2.9195 3.6803 2.8737 0.1513  -0.5631 -0.4853 448  LEU A C   
3408  O  O   . LEU A  448 ? 2.9351 3.6279 2.8459 0.1516  -0.5517 -0.4920 448  LEU A O   
3409  C  CB  . LEU A  448 ? 2.8730 3.6654 2.9441 0.1010  -0.5380 -0.4848 448  LEU A CB  
3410  C  CG  . LEU A  448 ? 2.8620 3.6398 2.9303 0.0687  -0.5436 -0.5005 448  LEU A CG  
3411  C  CD1 . LEU A  448 ? 2.8853 3.7348 2.9887 0.0614  -0.5634 -0.4903 448  LEU A CD1 
3412  C  CD2 . LEU A  448 ? 2.8241 3.5671 2.9193 0.0385  -0.5266 -0.5134 448  LEU A CD2 
3413  N  N   . GLU A  449 ? 3.0694 3.8534 2.9995 0.1596  -0.5829 -0.4871 449  GLU A N   
3414  C  CA  . GLU A  449 ? 3.1724 3.8963 3.0219 0.1678  -0.5928 -0.4991 449  GLU A CA  
3415  C  C   . GLU A  449 ? 3.2374 3.9535 3.0892 0.1337  -0.5962 -0.5139 449  GLU A C   
3416  O  O   . GLU A  449 ? 3.2283 4.0059 3.1283 0.1202  -0.6051 -0.5103 449  GLU A O   
3417  C  CB  . GLU A  449 ? 3.1973 3.9476 3.0033 0.2139  -0.6159 -0.4904 449  GLU A CB  
3418  C  CG  . GLU A  449 ? 3.2571 4.0112 3.0504 0.2542  -0.6161 -0.4766 449  GLU A CG  
3419  C  CD  . GLU A  449 ? 3.2732 4.0626 3.0251 0.3055  -0.6410 -0.4691 449  GLU A CD  
3420  O  OE1 . GLU A  449 ? 3.3704 4.1931 3.1283 0.3429  -0.6443 -0.4560 449  GLU A OE1 
3421  O  OE2 . GLU A  449 ? 3.1281 3.9135 2.8402 0.3107  -0.6580 -0.4772 449  GLU A OE2 
3422  N  N   . VAL A  450 ? 3.2045 3.8456 3.0012 0.1184  -0.5902 -0.5299 450  VAL A N   
3423  C  CA  . VAL A  450 ? 3.1686 3.7919 2.9546 0.0893  -0.5937 -0.5459 450  VAL A CA  
3424  C  C   . VAL A  450 ? 3.2947 3.8649 2.9938 0.1028  -0.6067 -0.5537 450  VAL A C   
3425  O  O   . VAL A  450 ? 3.2636 3.7655 2.9069 0.0993  -0.5977 -0.5602 450  VAL A O   
3426  C  CB  . VAL A  450 ? 3.1131 3.6994 2.9186 0.0536  -0.5720 -0.5602 450  VAL A CB  
3427  C  CG1 . VAL A  450 ? 3.1916 3.7573 2.9791 0.0279  -0.5772 -0.5777 450  VAL A CG1 
3428  C  CG2 . VAL A  450 ? 3.0319 3.6624 2.9168 0.0421  -0.5616 -0.5529 450  VAL A CG2 
3429  N  N   . TYR A  451 ? 3.4317 4.0339 3.1165 0.1166  -0.6287 -0.5524 451  TYR A N   
3430  C  CA  . TYR A  451 ? 3.5265 4.0784 3.1264 0.1309  -0.6445 -0.5603 451  TYR A CA  
3431  C  C   . TYR A  451 ? 3.6739 4.2435 3.2765 0.1119  -0.6569 -0.5708 451  TYR A C   
3432  O  O   . TYR A  451 ? 3.7868 4.4306 3.4391 0.1134  -0.6686 -0.5637 451  TYR A O   
3433  C  CB  . TYR A  451 ? 3.4173 3.9834 2.9765 0.1813  -0.6641 -0.5478 451  TYR A CB  
3434  C  CG  . TYR A  451 ? 3.2871 3.9563 2.9093 0.2043  -0.6750 -0.5330 451  TYR A CG  
3435  C  CD1 . TYR A  451 ? 3.2520 3.9648 2.9275 0.2154  -0.6646 -0.5188 451  TYR A CD1 
3436  C  CD2 . TYR A  451 ? 3.2660 3.9933 2.8927 0.2142  -0.6960 -0.5325 451  TYR A CD2 
3437  C  CE1 . TYR A  451 ? 3.2203 4.0341 2.9522 0.2341  -0.6743 -0.5041 451  TYR A CE1 
3438  C  CE2 . TYR A  451 ? 3.2029 4.0351 2.8867 0.2323  -0.7060 -0.5177 451  TYR A CE2 
3439  C  CZ  . TYR A  451 ? 3.2187 4.0949 2.9547 0.2416  -0.6949 -0.5033 451  TYR A CZ  
3440  O  OH  . TYR A  451 ? 3.2293 4.2170 3.0215 0.2572  -0.7047 -0.4875 451  TYR A OH  
3441  N  N   . PRO A  452 ? 3.5146 4.0181 3.0620 0.0922  -0.6551 -0.5869 452  PRO A N   
3442  C  CA  . PRO A  452 ? 3.4710 3.8914 2.9546 0.0840  -0.6425 -0.5944 452  PRO A CA  
3443  C  C   . PRO A  452 ? 3.3740 3.7806 2.8964 0.0535  -0.6148 -0.6000 452  PRO A C   
3444  O  O   . PRO A  452 ? 3.2160 3.6620 2.8065 0.0337  -0.6058 -0.6033 452  PRO A O   
3445  C  CB  . PRO A  452 ? 3.3797 3.7547 2.8019 0.0698  -0.6525 -0.6096 452  PRO A CB  
3446  C  CG  . PRO A  452 ? 3.3647 3.7934 2.8440 0.0523  -0.6577 -0.6150 452  PRO A CG  
3447  C  CD  . PRO A  452 ? 3.4090 3.9200 2.9517 0.0736  -0.6670 -0.5984 452  PRO A CD  
3448  N  N   . SER A  453 ? 3.4749 3.8232 2.9476 0.0498  -0.6031 -0.6009 453  SER A N   
3449  C  CA  . SER A  453 ? 3.2828 3.6174 2.7809 0.0212  -0.5768 -0.6082 453  SER A CA  
3450  C  C   . SER A  453 ? 3.3045 3.6175 2.7880 -0.0105 -0.5693 -0.6280 453  SER A C   
3451  O  O   . SER A  453 ? 3.1509 3.4782 2.6796 -0.0315 -0.5510 -0.6377 453  SER A O   
3452  C  CB  . SER A  453 ? 3.1934 3.4778 2.6392 0.0241  -0.5683 -0.6015 453  SER A CB  
3453  O  OG  . SER A  453 ? 3.1974 3.4181 2.5474 0.0238  -0.5814 -0.6043 453  SER A OG  
3454  N  N   . ILE A  454 ? 3.5171 3.7940 2.9343 -0.0121 -0.5839 -0.6350 454  ILE A N   
3455  C  CA  . ILE A  454 ? 3.5345 3.7854 2.9249 -0.0407 -0.5776 -0.6538 454  ILE A CA  
3456  C  C   . ILE A  454 ? 3.5146 3.7931 2.9263 -0.0400 -0.5945 -0.6603 454  ILE A C   
3457  O  O   . ILE A  454 ? 3.5550 3.8309 2.9325 -0.0215 -0.6169 -0.6553 454  ILE A O   
3458  C  CB  . ILE A  454 ? 3.5665 3.7507 2.8592 -0.0490 -0.5812 -0.6567 454  ILE A CB  
3459  C  CG1 . ILE A  454 ? 3.5480 3.7056 2.7821 -0.0184 -0.6073 -0.6440 454  ILE A CG1 
3460  C  CG2 . ILE A  454 ? 3.4956 3.6564 2.7714 -0.0655 -0.5600 -0.6544 454  ILE A CG2 
3461  C  CD1 . ILE A  454 ? 3.4810 3.5616 2.6087 -0.0272 -0.6153 -0.6451 454  ILE A CD1 
3462  N  N   . LEU A  455 ? 3.5499 3.8539 3.0151 -0.0589 -0.5855 -0.6716 455  LEU A N   
3463  C  CA  . LEU A  455 ? 3.6412 3.9681 3.1264 -0.0643 -0.6020 -0.6780 455  LEU A CA  
3464  C  C   . LEU A  455 ? 3.6573 3.9424 3.0888 -0.0835 -0.6024 -0.6972 455  LEU A C   
3465  O  O   . LEU A  455 ? 3.7480 4.0142 3.1756 -0.1024 -0.5838 -0.7117 455  LEU A O   
3466  C  CB  . LEU A  455 ? 3.5876 3.9560 3.1518 -0.0750 -0.5969 -0.6787 455  LEU A CB  
3467  C  CG  . LEU A  455 ? 3.4776 3.8904 3.0999 -0.0600 -0.5942 -0.6598 455  LEU A CG  
3468  C  CD1 . LEU A  455 ? 3.4839 3.9276 3.1746 -0.0757 -0.5917 -0.6616 455  LEU A CD1 
3469  C  CD2 . LEU A  455 ? 3.4280 3.8761 3.0471 -0.0344 -0.6152 -0.6420 455  LEU A CD2 
3470  N  N   . ASN A  456 ? 3.5006 3.7747 2.8891 -0.0765 -0.6237 -0.6976 456  ASN A N   
3471  C  CA  . ASN A  456 ? 3.3666 3.6033 2.7044 -0.0939 -0.6267 -0.7152 456  ASN A CA  
3472  C  C   . ASN A  456 ? 3.4295 3.6846 2.8125 -0.1128 -0.6253 -0.7290 456  ASN A C   
3473  O  O   . ASN A  456 ? 3.3703 3.6671 2.8157 -0.1116 -0.6315 -0.7223 456  ASN A O   
3474  C  CB  . ASN A  456 ? 3.3305 3.5537 2.6151 -0.0791 -0.6525 -0.7115 456  ASN A CB  
3475  C  CG  . ASN A  456 ? 3.4235 3.5998 2.6438 -0.0964 -0.6556 -0.7285 456  ASN A CG  
3476  O  OD1 . ASN A  456 ? 3.6142 3.7991 2.8458 -0.1076 -0.6643 -0.7395 456  ASN A OD1 
3477  N  ND2 . ASN A  456 ? 3.3729 3.4973 2.5213 -0.1004 -0.6498 -0.7298 456  ASN A ND2 
3478  N  N   . GLN A  457 ? 3.6552 3.8765 3.0012 -0.1310 -0.6186 -0.7484 457  GLN A N   
3479  C  CA  . GLN A  457 ? 3.6850 3.9125 3.0612 -0.1463 -0.6199 -0.7637 457  GLN A CA  
3480  C  C   . GLN A  457 ? 3.6627 3.9031 3.0418 -0.1471 -0.6473 -0.7620 457  GLN A C   
3481  O  O   . GLN A  457 ? 3.6735 3.9234 3.0850 -0.1594 -0.6548 -0.7692 457  GLN A O   
3482  C  CB  . GLN A  457 ? 3.6887 3.8806 3.0221 -0.1620 -0.6042 -0.7860 457  GLN A CB  
3483  C  CG  . GLN A  457 ? 3.5838 3.7742 2.9410 -0.1733 -0.6049 -0.8045 457  GLN A CG  
3484  C  CD  . GLN A  457 ? 3.4007 3.6181 2.8266 -0.1705 -0.6006 -0.7998 457  GLN A CD  
3485  O  OE1 . GLN A  457 ? 3.3464 3.5747 2.7942 -0.1652 -0.5809 -0.7965 457  GLN A OE1 
3486  N  NE2 . GLN A  457 ? 3.3776 3.6051 2.8353 -0.1761 -0.6206 -0.7982 457  GLN A NE2 
3487  N  N   . ASP A  458 ? 3.4335 3.6737 2.7765 -0.1336 -0.6642 -0.7522 458  ASP A N   
3488  C  CA  . ASP A  458 ? 3.2290 3.4894 2.5728 -0.1328 -0.6911 -0.7497 458  ASP A CA  
3489  C  C   . ASP A  458 ? 3.1721 3.4549 2.4992 -0.1056 -0.7068 -0.7318 458  ASP A C   
3490  O  O   . ASP A  458 ? 3.1885 3.4377 2.4496 -0.0953 -0.7155 -0.7343 458  ASP A O   
3491  C  CB  . ASP A  458 ? 3.2140 3.4329 2.5043 -0.1472 -0.6976 -0.7687 458  ASP A CB  
3492  C  CG  . ASP A  458 ? 3.1980 3.4390 2.4901 -0.1486 -0.7259 -0.7664 458  ASP A CG  
3493  O  OD1 . ASP A  458 ? 3.1932 3.4550 2.5274 -0.1646 -0.7344 -0.7687 458  ASP A OD1 
3494  O  OD2 . ASP A  458 ? 3.2148 3.4508 2.4627 -0.1340 -0.7412 -0.7622 458  ASP A OD2 
3495  N  N   . ASN A  459 ? 3.2060 3.5447 2.5894 -0.0927 -0.7112 -0.7142 459  ASN A N   
3496  C  CA  . ASN A  459 ? 3.3113 3.6839 2.6859 -0.0613 -0.7272 -0.6971 459  ASN A CA  
3497  C  C   . ASN A  459 ? 3.3342 3.7850 2.7717 -0.0619 -0.7449 -0.6845 459  ASN A C   
3498  O  O   . ASN A  459 ? 3.3441 3.8428 2.8400 -0.0587 -0.7397 -0.6707 459  ASN A O   
3499  C  CB  . ASN A  459 ? 3.4257 3.7926 2.7997 -0.0409 -0.7127 -0.6857 459  ASN A CB  
3500  C  CG  . ASN A  459 ? 3.6656 4.0709 3.0317 -0.0032 -0.7306 -0.6687 459  ASN A CG  
3501  O  OD1 . ASN A  459 ? 3.3694 3.7867 2.7037 0.0121  -0.7532 -0.6685 459  ASN A OD1 
3502  N  ND2 . ASN A  459 ? 4.8956 5.3229 4.2899 0.0144  -0.7214 -0.6550 459  ASN A ND2 
3503  N  N   . LYS A  460 ? 3.3968 3.8631 2.8202 -0.0674 -0.7666 -0.6882 460  LYS A N   
3504  C  CA  . LYS A  460 ? 3.3490 3.8930 2.8265 -0.0752 -0.7860 -0.6761 460  LYS A CA  
3505  C  C   . LYS A  460 ? 3.2902 3.8971 2.7648 -0.0379 -0.8033 -0.6596 460  LYS A C   
3506  O  O   . LYS A  460 ? 3.3668 3.9576 2.7838 -0.0156 -0.8175 -0.6641 460  LYS A O   
3507  C  CB  . LYS A  460 ? 3.4716 4.0018 2.9336 -0.1019 -0.8018 -0.6886 460  LYS A CB  
3508  C  CG  . LYS A  460 ? 3.4051 3.8767 2.8692 -0.1346 -0.7870 -0.7060 460  LYS A CG  
3509  C  CD  . LYS A  460 ? 3.3630 3.8011 2.7908 -0.1550 -0.8015 -0.7221 460  LYS A CD  
3510  C  CE  . LYS A  460 ? 3.2992 3.6911 2.6518 -0.1374 -0.8035 -0.7330 460  LYS A CE  
3511  N  NZ  . LYS A  460 ? 3.2877 3.6414 2.6039 -0.1582 -0.8149 -0.7504 460  LYS A NZ  
3512  N  N   . THR A  461 ? 3.2744 3.9536 2.8082 -0.0291 -0.8028 -0.6411 461  THR A N   
3513  C  CA  . THR A  461 ? 3.2489 3.9941 2.7803 0.0125  -0.8175 -0.6258 461  THR A CA  
3514  C  C   . THR A  461 ? 3.1968 4.0548 2.8012 0.0060  -0.8298 -0.6062 461  THR A C   
3515  O  O   . THR A  461 ? 3.2049 4.1324 2.8095 0.0184  -0.8527 -0.5993 461  THR A O   
3516  C  CB  . THR A  461 ? 3.3566 4.0697 2.8658 0.0455  -0.8020 -0.6215 461  THR A CB  
3517  O  OG1 . THR A  461 ? 3.4158 4.0271 2.8524 0.0463  -0.7923 -0.6377 461  THR A OG1 
3518  C  CG2 . THR A  461 ? 3.4312 4.2048 2.9266 0.0957  -0.8192 -0.6081 461  THR A CG2 
3519  N  N   . CYS A  462 ? 3.2629 4.1433 2.9277 -0.0139 -0.8156 -0.5966 462  CYS A N   
3520  C  CA  . CYS A  462 ? 3.3583 4.3450 3.0915 -0.0272 -0.8271 -0.5762 462  CYS A CA  
3521  C  C   . CYS A  462 ? 3.1689 4.1842 2.9150 -0.0670 -0.8476 -0.5772 462  CYS A C   
3522  O  O   . CYS A  462 ? 3.2011 4.1427 2.9225 -0.0960 -0.8461 -0.5940 462  CYS A O   
3523  C  CB  . CYS A  462 ? 3.5547 4.5432 3.3436 -0.0475 -0.8084 -0.5675 462  CYS A CB  
3524  S  SG  . CYS A  462 ? 3.9282 4.8107 3.7118 -0.0915 -0.7913 -0.5874 462  CYS A SG  
3525  N  N   . SER A  463 ? 3.0628 4.1897 2.8471 -0.0689 -0.8674 -0.5586 463  SER A N   
3526  C  CA  . SER A  463 ? 3.1145 4.2795 2.9089 -0.1074 -0.8906 -0.5564 463  SER A CA  
3527  C  C   . SER A  463 ? 3.1059 4.2352 2.9328 -0.1654 -0.8882 -0.5565 463  SER A C   
3528  O  O   . SER A  463 ? 3.0168 4.1612 2.8885 -0.1795 -0.8774 -0.5450 463  SER A O   
3529  C  CB  . SER A  463 ? 3.0659 4.3726 2.8964 -0.0969 -0.9119 -0.5340 463  SER A CB  
3530  O  OG  . SER A  463 ? 3.2130 4.5587 3.0442 -0.1314 -0.9366 -0.5321 463  SER A OG  
3531  N  N   . LEU A  464 ? 3.0728 4.1487 2.8713 -0.1973 -0.8999 -0.5703 464  LEU A N   
3532  C  CA  . LEU A  464 ? 2.9291 3.9568 2.7405 -0.2508 -0.9044 -0.5741 464  LEU A CA  
3533  C  C   . LEU A  464 ? 2.9906 3.9908 2.7630 -0.2733 -0.9258 -0.5861 464  LEU A C   
3534  O  O   . LEU A  464 ? 2.9915 3.9696 2.7182 -0.2441 -0.9266 -0.5992 464  LEU A O   
3535  C  CB  . LEU A  464 ? 2.7519 3.6741 2.5509 -0.2499 -0.8777 -0.5913 464  LEU A CB  
3536  C  CG  . LEU A  464 ? 2.7835 3.6426 2.5906 -0.2953 -0.8795 -0.5980 464  LEU A CG  
3537  C  CD1 . LEU A  464 ? 2.7423 3.6598 2.6073 -0.3210 -0.8845 -0.5746 464  LEU A CD1 
3538  C  CD2 . LEU A  464 ? 2.8215 3.5759 2.5993 -0.2826 -0.8533 -0.6218 464  LEU A CD2 
3539  N  N   . PRO A  465 ? 2.9359 3.9321 2.7195 -0.3253 -0.9454 -0.5820 465  PRO A N   
3540  C  CA  . PRO A  465 ? 2.8468 3.8082 2.5875 -0.3443 -0.9654 -0.5951 465  PRO A CA  
3541  C  C   . PRO A  465 ? 2.9146 3.7512 2.5994 -0.3334 -0.9497 -0.6255 465  PRO A C   
3542  O  O   . PRO A  465 ? 2.9604 3.7220 2.6289 -0.3656 -0.9534 -0.6378 465  PRO A O   
3543  C  CB  . PRO A  465 ? 2.8695 3.8428 2.6314 -0.4052 -0.9899 -0.5827 465  PRO A CB  
3544  C  CG  . PRO A  465 ? 2.8653 3.8346 2.6677 -0.4175 -0.9768 -0.5718 465  PRO A CG  
3545  C  CD  . PRO A  465 ? 2.8720 3.9047 2.7027 -0.3692 -0.9554 -0.5624 465  PRO A CD  
3546  N  N   . LYS A  470 ? 3.2804 4.0411 2.9323 -0.2129 -0.8724 -0.6435 470  LYS A N   
3547  C  CA  . LYS A  470 ? 3.2108 3.9453 2.8466 -0.1741 -0.8484 -0.6468 470  LYS A CA  
3548  C  C   . LYS A  470 ? 3.2015 3.8413 2.8173 -0.1826 -0.8238 -0.6662 470  LYS A C   
3549  O  O   . LYS A  470 ? 3.2662 3.8408 2.8412 -0.1962 -0.8240 -0.6859 470  LYS A O   
3550  C  CB  . LYS A  470 ? 3.2261 3.9565 2.8067 -0.1371 -0.8545 -0.6521 470  LYS A CB  
3551  C  CG  . LYS A  470 ? 3.1719 4.0004 2.7676 -0.1069 -0.8718 -0.6331 470  LYS A CG  
3552  C  CD  . LYS A  470 ? 3.1286 4.0434 2.7624 -0.1337 -0.8979 -0.6197 470  LYS A CD  
3553  C  CE  . LYS A  470 ? 3.0661 3.9521 2.6559 -0.1476 -0.9165 -0.6334 470  LYS A CE  
3554  N  NZ  . LYS A  470 ? 2.9536 3.9250 2.5774 -0.1777 -0.9437 -0.6194 470  LYS A NZ  
3555  N  N   . VAL A  471 ? 3.1247 3.7621 2.7698 -0.1736 -0.8029 -0.6607 471  VAL A N   
3556  C  CA  . VAL A  471 ? 3.1498 3.7114 2.7799 -0.1770 -0.7778 -0.6776 471  VAL A CA  
3557  C  C   . VAL A  471 ? 3.2607 3.8226 2.8906 -0.1457 -0.7565 -0.6714 471  VAL A C   
3558  O  O   . VAL A  471 ? 3.3232 3.9444 2.9749 -0.1237 -0.7612 -0.6530 471  VAL A O   
3559  C  CB  . VAL A  471 ? 3.1682 3.7156 2.8375 -0.2079 -0.7755 -0.6794 471  VAL A CB  
3560  C  CG1 . VAL A  471 ? 3.1538 3.6792 2.8083 -0.2401 -0.7976 -0.6887 471  VAL A CG1 
3561  C  CG2 . VAL A  471 ? 3.2808 3.8989 3.0124 -0.2107 -0.7792 -0.6550 471  VAL A CG2 
3562  N  N   . SER A  472 ? 3.2898 3.7865 2.8917 -0.1435 -0.7336 -0.6872 472  SER A N   
3563  C  CA  . SER A  472 ? 3.2112 3.6971 2.8065 -0.1194 -0.7128 -0.6825 472  SER A CA  
3564  C  C   . SER A  472 ? 3.1595 3.6970 2.8172 -0.1133 -0.7069 -0.6636 472  SER A C   
3565  O  O   . SER A  472 ? 3.0781 3.6065 2.7721 -0.1296 -0.6951 -0.6662 472  SER A O   
3566  C  CB  . SER A  472 ? 3.1665 3.5849 2.7316 -0.1276 -0.6892 -0.7021 472  SER A CB  
3567  O  OG  . SER A  472 ? 3.1465 3.5529 2.6999 -0.1087 -0.6706 -0.6968 472  SER A OG  
3568  N  N   . CYS A  473 ? 3.3362 3.9268 3.0035 -0.0872 -0.7155 -0.6453 473  CYS A N   
3569  C  CA  . CYS A  473 ? 3.4025 4.0535 3.1292 -0.0798 -0.7128 -0.6254 473  CYS A CA  
3570  C  C   . CYS A  473 ? 3.3448 4.0000 3.0546 -0.0423 -0.7036 -0.6157 473  CYS A C   
3571  O  O   . CYS A  473 ? 3.2748 3.8947 2.9239 -0.0202 -0.7061 -0.6211 473  CYS A O   
3572  C  CB  . CYS A  473 ? 3.4888 4.2236 3.2552 -0.0874 -0.7370 -0.6089 473  CYS A CB  
3573  S  SG  . CYS A  473 ? 3.8622 4.6384 3.5872 -0.0586 -0.7612 -0.6044 473  CYS A SG  
3574  N  N   . PHE A  474 ? 3.4426 4.1383 3.2033 -0.0356 -0.6949 -0.6006 474  PHE A N   
3575  C  CA  . PHE A  474 ? 3.5270 4.2261 3.2773 -0.0009 -0.6858 -0.5902 474  PHE A CA  
3576  C  C   . PHE A  474 ? 3.5642 4.3470 3.3784 0.0084  -0.6896 -0.5684 474  PHE A C   
3577  O  O   . PHE A  474 ? 3.5439 4.3704 3.4123 -0.0190 -0.6944 -0.5620 474  PHE A O   
3578  C  CB  . PHE A  474 ? 3.5168 4.1462 3.2498 -0.0058 -0.6601 -0.6004 474  PHE A CB  
3579  C  CG  . PHE A  474 ? 3.4336 4.0615 3.2208 -0.0343 -0.6451 -0.6037 474  PHE A CG  
3580  C  CD1 . PHE A  474 ? 3.4271 4.0196 3.2110 -0.0645 -0.6433 -0.6212 474  PHE A CD1 
3581  C  CD2 . PHE A  474 ? 3.3775 4.0358 3.2142 -0.0283 -0.6341 -0.5903 474  PHE A CD2 
3582  C  CE1 . PHE A  474 ? 3.4026 3.9872 3.2282 -0.0861 -0.6323 -0.6258 474  PHE A CE1 
3583  C  CE2 . PHE A  474 ? 3.3123 3.9638 3.1933 -0.0524 -0.6222 -0.5941 474  PHE A CE2 
3584  C  CZ  . PHE A  474 ? 3.3764 3.9894 3.2500 -0.0802 -0.6220 -0.6123 474  PHE A CZ  
3585  N  N   . ASN A  475 ? 3.6282 4.4309 3.4307 0.0470  -0.6889 -0.5568 475  ASN A N   
3586  C  CA  . ASN A  475 ? 3.5473 4.4351 3.4035 0.0634  -0.6926 -0.5356 475  ASN A CA  
3587  C  C   . ASN A  475 ? 3.5224 4.3921 3.4114 0.0614  -0.6701 -0.5305 475  ASN A C   
3588  O  O   . ASN A  475 ? 3.6432 4.4466 3.4934 0.0745  -0.6557 -0.5375 475  ASN A O   
3589  C  CB  . ASN A  475 ? 3.5566 4.4821 3.3771 0.1137  -0.7079 -0.5264 475  ASN A CB  
3590  C  CG  . ASN A  475 ? 3.6462 4.6006 3.4368 0.1201  -0.7318 -0.5304 475  ASN A CG  
3591  O  OD1 . ASN A  475 ? 3.7575 4.6451 3.4816 0.1273  -0.7367 -0.5449 475  ASN A OD1 
3592  N  ND2 . ASN A  475 ? 3.5964 4.6533 3.4348 0.1158  -0.7475 -0.5168 475  ASN A ND2 
3593  N  N   . VAL A  476 ? 3.4751 4.4038 3.4327 0.0430  -0.6683 -0.5174 476  VAL A N   
3594  C  CA  . VAL A  476 ? 3.4313 4.3545 3.4268 0.0422  -0.6490 -0.5103 476  VAL A CA  
3595  C  C   . VAL A  476 ? 3.4139 4.4241 3.4433 0.0710  -0.6555 -0.4877 476  VAL A C   
3596  O  O   . VAL A  476 ? 3.3558 4.4493 3.4319 0.0575  -0.6683 -0.4736 476  VAL A O   
3597  C  CB  . VAL A  476 ? 3.4373 4.3490 3.4796 -0.0021 -0.6417 -0.5141 476  VAL A CB  
3598  C  CG1 . VAL A  476 ? 3.4528 4.3579 3.5316 0.0002  -0.6223 -0.5072 476  VAL A CG1 
3599  C  CG2 . VAL A  476 ? 3.4670 4.2982 3.4721 -0.0254 -0.6365 -0.5379 476  VAL A CG2 
3600  N  N   . ARG A  477 ? 3.5044 4.4976 3.5071 0.1102  -0.6479 -0.4837 477  ARG A N   
3601  C  CA  . ARG A  477 ? 3.4507 4.5218 3.4786 0.1449  -0.6531 -0.4639 477  ARG A CA  
3602  C  C   . ARG A  477 ? 3.3844 4.4394 3.4451 0.1449  -0.6325 -0.4570 477  ARG A C   
3603  O  O   . ARG A  477 ? 3.3923 4.3693 3.4159 0.1550  -0.6185 -0.4657 477  ARG A O   
3604  C  CB  . ARG A  477 ? 3.4637 4.5292 3.4259 0.1978  -0.6661 -0.4642 477  ARG A CB  
3605  C  CG  . ARG A  477 ? 3.4150 4.5680 3.3965 0.2416  -0.6744 -0.4453 477  ARG A CG  
3606  C  CD  . ARG A  477 ? 3.4601 4.6072 3.3682 0.2976  -0.6929 -0.4479 477  ARG A CD  
3607  N  NE  . ARG A  477 ? 3.4900 4.7258 3.4128 0.3455  -0.7020 -0.4314 477  ARG A NE  
3608  C  CZ  . ARG A  477 ? 3.5335 4.7424 3.4327 0.3839  -0.6962 -0.4262 477  ARG A CZ  
3609  N  NH1 . ARG A  477 ? 3.5948 4.6917 3.4555 0.3761  -0.6816 -0.4350 477  ARG A NH1 
3610  N  NH2 . ARG A  477 ? 3.4822 4.7790 3.3946 0.4299  -0.7057 -0.4119 477  ARG A NH2 
3611  N  N   . PHE A  478 ? 3.4125 4.5422 3.5407 0.1315  -0.6317 -0.4405 478  PHE A N   
3612  C  CA  . PHE A  478 ? 3.4124 4.5377 3.5784 0.1309  -0.6139 -0.4320 478  PHE A CA  
3613  C  C   . PHE A  478 ? 3.3720 4.5930 3.5685 0.1631  -0.6206 -0.4100 478  PHE A C   
3614  O  O   . PHE A  478 ? 3.4060 4.7210 3.6347 0.1570  -0.6361 -0.3973 478  PHE A O   
3615  C  CB  . PHE A  478 ? 3.4509 4.5673 3.6687 0.0803  -0.6058 -0.4335 478  PHE A CB  
3616  C  CG  . PHE A  478 ? 3.4741 4.6734 3.7365 0.0508  -0.6233 -0.4206 478  PHE A CG  
3617  C  CD1 . PHE A  478 ? 3.4717 4.6703 3.7173 0.0271  -0.6390 -0.4290 478  PHE A CD1 
3618  C  CD2 . PHE A  478 ? 3.4739 4.7526 3.7927 0.0441  -0.6249 -0.3990 478  PHE A CD2 
3619  C  CE1 . PHE A  478 ? 3.4684 4.7431 3.7513 -0.0045 -0.6569 -0.4156 478  PHE A CE1 
3620  C  CE2 . PHE A  478 ? 3.4866 4.8441 3.8427 0.0113  -0.6425 -0.3848 478  PHE A CE2 
3621  C  CZ  . PHE A  478 ? 3.4755 4.8306 3.8131 -0.0141 -0.6590 -0.3929 478  PHE A CZ  
3622  N  N   . CYS A  479 ? 3.2557 4.4563 3.4408 0.1966  -0.6095 -0.4052 479  CYS A N   
3623  C  CA  . CYS A  479 ? 3.2037 4.4897 3.4125 0.2332  -0.6144 -0.3856 479  CYS A CA  
3624  C  C   . CYS A  479 ? 3.0350 4.3311 3.3001 0.2172  -0.5972 -0.3745 479  CYS A C   
3625  O  O   . CYS A  479 ? 2.8984 4.1148 3.1635 0.1964  -0.5799 -0.3843 479  CYS A O   
3626  C  CB  . CYS A  479 ? 3.2125 4.4670 3.3538 0.2926  -0.6196 -0.3878 479  CYS A CB  
3627  S  SG  . CYS A  479 ? 3.3714 4.6104 3.4343 0.3228  -0.6431 -0.4001 479  CYS A SG  
3628  N  N   . LEU A  480 ? 3.0105 4.4093 3.3221 0.2285  -0.6023 -0.3540 480  LEU A N   
3629  C  CA  . LEU A  480 ? 2.8047 4.2253 3.1739 0.2103  -0.5887 -0.3410 480  LEU A CA  
3630  C  C   . LEU A  480 ? 2.6470 4.1529 3.0317 0.2547  -0.5914 -0.3219 480  LEU A C   
3631  O  O   . LEU A  480 ? 2.6907 4.2965 3.0815 0.2751  -0.6077 -0.3108 480  LEU A O   
3632  C  CB  . LEU A  480 ? 2.8946 4.3599 3.3208 0.1525  -0.5933 -0.3335 480  LEU A CB  
3633  C  CG  . LEU A  480 ? 2.7605 4.2016 3.2333 0.1206  -0.5781 -0.3280 480  LEU A CG  
3634  C  CD1 . LEU A  480 ? 2.6953 4.0164 3.1385 0.1212  -0.5593 -0.3479 480  LEU A CD1 
3635  C  CD2 . LEU A  480 ? 2.8341 4.3024 3.3470 0.0619  -0.5879 -0.3221 480  LEU A CD2 
3636  N  N   . LYS A  481 ? 2.5879 4.0578 2.9778 0.2712  -0.5758 -0.3185 481  LYS A N   
3637  C  CA  . LYS A  481 ? 2.8003 4.3412 3.2023 0.3155  -0.5767 -0.3014 481  LYS A CA  
3638  C  C   . LYS A  481 ? 2.9223 4.4478 3.3696 0.2983  -0.5582 -0.2928 481  LYS A C   
3639  O  O   . LYS A  481 ? 2.9105 4.3374 3.3477 0.2800  -0.5431 -0.3050 481  LYS A O   
3640  C  CB  . LYS A  481 ? 2.9357 4.4302 3.2628 0.3785  -0.5821 -0.3089 481  LYS A CB  
3641  C  CG  . LYS A  481 ? 3.0585 4.6272 3.3877 0.4333  -0.5866 -0.2930 481  LYS A CG  
3642  C  CD  . LYS A  481 ? 3.1543 4.6652 3.3956 0.4965  -0.5975 -0.3022 481  LYS A CD  
3643  C  CE  . LYS A  481 ? 3.1352 4.5103 3.3323 0.4952  -0.5837 -0.3130 481  LYS A CE  
3644  N  NZ  . LYS A  481 ? 2.9382 4.3179 3.1774 0.4937  -0.5670 -0.3013 481  LYS A NZ  
3645  N  N   . ALA A  482 ? 2.7812 4.4089 3.2783 0.3038  -0.5598 -0.2716 482  ALA A N   
3646  C  CA  . ALA A  482 ? 2.4694 4.0938 3.0130 0.2869  -0.5441 -0.2611 482  ALA A CA  
3647  C  C   . ALA A  482 ? 2.3039 4.0157 2.8613 0.3331  -0.5456 -0.2422 482  ALA A C   
3648  O  O   . ALA A  482 ? 2.3587 4.1610 2.9055 0.3684  -0.5604 -0.2343 482  ALA A O   
3649  C  CB  . ALA A  482 ? 2.4090 4.0647 3.0121 0.2219  -0.5443 -0.2529 482  ALA A CB  
3650  N  N   . ASP A  483 ? 2.1710 3.8561 2.7504 0.3353  -0.5302 -0.2360 483  ASP A N   
3651  C  CA  . ASP A  483 ? 2.1807 3.9442 2.7762 0.3770  -0.5296 -0.2181 483  ASP A CA  
3652  C  C   . ASP A  483 ? 2.2250 3.9613 2.8628 0.3552  -0.5120 -0.2102 483  ASP A C   
3653  O  O   . ASP A  483 ? 2.3476 3.9881 2.9880 0.3212  -0.4996 -0.2220 483  ASP A O   
3654  C  CB  . ASP A  483 ? 2.2095 3.9396 2.7358 0.4481  -0.5349 -0.2252 483  ASP A CB  
3655  C  CG  . ASP A  483 ? 2.1069 3.9433 2.6429 0.5000  -0.5409 -0.2074 483  ASP A CG  
3656  O  OD1 . ASP A  483 ? 1.9478 3.9139 2.5325 0.4883  -0.5482 -0.1908 483  ASP A OD1 
3657  O  OD2 . ASP A  483 ? 2.2128 4.0042 2.7052 0.5518  -0.5391 -0.2095 483  ASP A OD2 
3658  N  N   . GLY A  484 ? 2.1869 4.0133 2.8567 0.3775  -0.5114 -0.1902 484  GLY A N   
3659  C  CA  . GLY A  484 ? 2.0624 3.8738 2.7713 0.3632  -0.4960 -0.1804 484  GLY A CA  
3660  C  C   . GLY A  484 ? 1.9587 3.8272 2.6607 0.4223  -0.4953 -0.1674 484  GLY A C   
3661  O  O   . GLY A  484 ? 2.1152 4.0479 2.7872 0.4720  -0.5083 -0.1647 484  GLY A O   
3662  N  N   . LYS A  485 ? 1.7788 3.6219 2.5062 0.4196  -0.4809 -0.1602 485  LYS A N   
3663  C  CA  . LYS A  485 ? 1.7837 3.6648 2.5010 0.4769  -0.4788 -0.1492 485  LYS A CA  
3664  C  C   . LYS A  485 ? 1.9520 3.8946 2.7355 0.4495  -0.4691 -0.1289 485  LYS A C   
3665  O  O   . LYS A  485 ? 1.9238 3.7918 2.7208 0.4328  -0.4545 -0.1310 485  LYS A O   
3666  C  CB  . LYS A  485 ? 1.7776 3.5342 2.4344 0.5145  -0.4718 -0.1643 485  LYS A CB  
3667  C  CG  . LYS A  485 ? 1.8106 3.5968 2.4338 0.5854  -0.4763 -0.1563 485  LYS A CG  
3668  C  CD  . LYS A  485 ? 1.8100 3.4649 2.3552 0.6216  -0.4759 -0.1722 485  LYS A CD  
3669  C  CE  . LYS A  485 ? 1.8654 3.5412 2.3643 0.6966  -0.4851 -0.1655 485  LYS A CE  
3670  N  NZ  . LYS A  485 ? 1.9252 3.4652 2.3382 0.7287  -0.4886 -0.1793 485  LYS A NZ  
3671  N  N   . GLY A  486 ? 2.1058 4.1885 2.9284 0.4456  -0.4781 -0.1087 486  GLY A N   
3672  C  CA  . GLY A  486 ? 2.0998 4.2599 2.9848 0.4142  -0.4723 -0.0861 486  GLY A CA  
3673  C  C   . GLY A  486 ? 1.9809 4.2946 2.9027 0.3915  -0.4865 -0.0665 486  GLY A C   
3674  O  O   . GLY A  486 ? 1.9318 4.3162 2.8296 0.4257  -0.4996 -0.0679 486  GLY A O   
3675  N  N   . VAL A  487 ? 1.8859 4.2500 2.8631 0.3325  -0.4852 -0.0478 487  VAL A N   
3676  C  CA  . VAL A  487 ? 1.8068 4.3150 2.8214 0.2950  -0.4996 -0.0263 487  VAL A CA  
3677  C  C   . VAL A  487 ? 1.7712 4.2233 2.7909 0.2239  -0.5079 -0.0335 487  VAL A C   
3678  O  O   . VAL A  487 ? 1.7500 4.1394 2.7924 0.1669  -0.5043 -0.0308 487  VAL A O   
3679  C  CB  . VAL A  487 ? 1.6889 4.2972 2.7547 0.2727  -0.4963 0.0022  487  VAL A CB  
3680  C  CG1 . VAL A  487 ? 1.7692 4.5220 2.8717 0.2206  -0.5126 0.0259  487  VAL A CG1 
3681  C  CG2 . VAL A  487 ? 1.5974 4.2703 2.6547 0.3487  -0.4896 0.0088  487  VAL A CG2 
3682  N  N   . LEU A  488 ? 2.0034 4.4741 2.9977 0.2295  -0.5205 -0.0436 488  LEU A N   
3683  C  CA  . LEU A  488 ? 2.1585 4.5852 3.1519 0.1675  -0.5311 -0.0509 488  LEU A CA  
3684  C  C   . LEU A  488 ? 2.1073 4.6567 3.0984 0.1694  -0.5497 -0.0433 488  LEU A C   
3685  O  O   . LEU A  488 ? 1.9871 4.6158 2.9606 0.2327  -0.5526 -0.0428 488  LEU A O   
3686  C  CB  . LEU A  488 ? 2.2486 4.5095 3.1988 0.1740  -0.5234 -0.0820 488  LEU A CB  
3687  C  CG  . LEU A  488 ? 2.3151 4.5222 3.2096 0.2409  -0.5205 -0.1038 488  LEU A CG  
3688  C  CD1 . LEU A  488 ? 2.3670 4.4450 3.2274 0.2181  -0.5199 -0.1295 488  LEU A CD1 
3689  C  CD2 . LEU A  488 ? 2.0954 4.2548 2.9728 0.2965  -0.5053 -0.1075 488  LEU A CD2 
3690  N  N   . PRO A  489 ? 2.0755 4.6433 3.0809 0.1022  -0.5641 -0.0374 489  PRO A N   
3691  C  CA  . PRO A  489 ? 1.9390 4.6234 2.9418 0.1001  -0.5827 -0.0307 489  PRO A CA  
3692  C  C   . PRO A  489 ? 1.9722 4.5985 2.9229 0.1532  -0.5844 -0.0573 489  PRO A C   
3693  O  O   . PRO A  489 ? 2.0279 4.5117 2.9431 0.1757  -0.5730 -0.0813 489  PRO A O   
3694  C  CB  . PRO A  489 ? 1.9025 4.5765 2.9234 0.0097  -0.5974 -0.0219 489  PRO A CB  
3695  C  CG  . PRO A  489 ? 1.9986 4.5060 3.0107 -0.0198 -0.5863 -0.0371 489  PRO A CG  
3696  C  CD  . PRO A  489 ? 2.1222 4.6046 3.1426 0.0253  -0.5663 -0.0363 489  PRO A CD  
3697  N  N   . ARG A  490 ? 1.8628 4.6054 2.8071 0.1721  -0.5999 -0.0523 490  ARG A N   
3698  C  CA  . ARG A  490 ? 1.8682 4.5623 2.7591 0.2215  -0.6049 -0.0763 490  ARG A CA  
3699  C  C   . ARG A  490 ? 1.8729 4.4729 2.7467 0.1686  -0.6126 -0.0919 490  ARG A C   
3700  O  O   . ARG A  490 ? 1.9700 4.4429 2.7979 0.1910  -0.6074 -0.1177 490  ARG A O   
3701  C  CB  . ARG A  490 ? 1.8887 4.7440 2.7751 0.2696  -0.6195 -0.0668 490  ARG A CB  
3702  C  CG  . ARG A  490 ? 2.0034 4.9087 2.8727 0.3560  -0.6129 -0.0654 490  ARG A CG  
3703  C  CD  . ARG A  490 ? 2.0215 4.7731 2.8253 0.4161  -0.6049 -0.0933 490  ARG A CD  
3704  N  NE  . ARG A  490 ? 2.0700 4.8496 2.8524 0.4946  -0.5997 -0.0916 490  ARG A NE  
3705  C  CZ  . ARG A  490 ? 2.1270 4.7801 2.8517 0.5486  -0.5930 -0.1107 490  ARG A CZ  
3706  N  NH1 . ARG A  490 ? 2.1839 4.6813 2.8698 0.5313  -0.5892 -0.1325 490  ARG A NH1 
3707  N  NH2 . ARG A  490 ? 2.1930 4.8762 2.8958 0.6189  -0.5912 -0.1074 490  ARG A NH2 
3708  N  N   . LYS A  491 ? 1.7915 4.4504 2.6980 0.0966  -0.6260 -0.0761 491  LYS A N   
3709  C  CA  . LYS A  491 ? 1.8910 4.4775 2.7793 0.0471  -0.6373 -0.0892 491  LYS A CA  
3710  C  C   . LYS A  491 ? 1.9590 4.3912 2.8455 0.0003  -0.6275 -0.1006 491  LYS A C   
3711  O  O   . LYS A  491 ? 1.9499 4.3903 2.8696 -0.0550 -0.6294 -0.0837 491  LYS A O   
3712  C  CB  . LYS A  491 ? 1.8957 4.6158 2.8132 -0.0086 -0.6594 -0.0663 491  LYS A CB  
3713  C  CG  . LYS A  491 ? 1.8754 4.7661 2.7977 0.0393  -0.6695 -0.0543 491  LYS A CG  
3714  C  CD  . LYS A  491 ? 1.8790 4.7243 2.7486 0.1056  -0.6708 -0.0806 491  LYS A CD  
3715  C  CE  . LYS A  491 ? 2.0031 5.0134 2.8714 0.1645  -0.6813 -0.0712 491  LYS A CE  
3716  N  NZ  . LYS A  491 ? 2.0725 5.0281 2.8809 0.2300  -0.6855 -0.0973 491  LYS A NZ  
3717  N  N   . LEU A  492 ? 1.9982 4.2910 2.8428 0.0235  -0.6178 -0.1294 492  LEU A N   
3718  C  CA  . LEU A  492 ? 2.0737 4.2194 2.9098 -0.0140 -0.6089 -0.1451 492  LEU A CA  
3719  C  C   . LEU A  492 ? 2.1178 4.2042 2.9283 -0.0541 -0.6226 -0.1601 492  LEU A C   
3720  O  O   . LEU A  492 ? 2.1985 4.2596 2.9716 -0.0225 -0.6248 -0.1778 492  LEU A O   
3721  C  CB  . LEU A  492 ? 2.0866 4.1215 2.8937 0.0377  -0.5873 -0.1663 492  LEU A CB  
3722  C  CG  . LEU A  492 ? 2.0487 4.1235 2.8703 0.0864  -0.5733 -0.1553 492  LEU A CG  
3723  C  CD1 . LEU A  492 ? 2.1586 4.1184 2.9385 0.1361  -0.5562 -0.1780 492  LEU A CD1 
3724  C  CD2 . LEU A  492 ? 1.9826 4.0759 2.8508 0.0467  -0.5683 -0.1362 492  LEU A CD2 
3725  N  N   . ASN A  493 ? 2.1118 4.1714 2.9375 -0.1230 -0.6335 -0.1530 493  ASN A N   
3726  C  CA  . ASN A  493 ? 2.2949 4.2957 3.0953 -0.1662 -0.6490 -0.1657 493  ASN A CA  
3727  C  C   . ASN A  493 ? 2.2779 4.1156 3.0452 -0.1632 -0.6360 -0.1957 493  ASN A C   
3728  O  O   . ASN A  493 ? 2.2754 4.0406 3.0517 -0.1829 -0.6277 -0.1977 493  ASN A O   
3729  C  CB  . ASN A  493 ? 2.3815 4.4243 3.2045 -0.2429 -0.6707 -0.1435 493  ASN A CB  
3730  C  CG  . ASN A  493 ? 2.3598 4.5701 3.2076 -0.2561 -0.6886 -0.1164 493  ASN A CG  
3731  O  OD1 . ASN A  493 ? 2.4671 4.7779 3.3258 -0.2029 -0.6821 -0.1099 493  ASN A OD1 
3732  N  ND2 . ASN A  493 ? 2.1421 4.3839 2.9950 -0.3269 -0.7128 -0.1005 493  ASN A ND2 
3733  N  N   . PHE A  494 ? 2.3277 4.1118 3.0555 -0.1400 -0.6352 -0.2188 494  PHE A N   
3734  C  CA  . PHE A  494 ? 2.3573 3.9995 3.0503 -0.1350 -0.6230 -0.2482 494  PHE A CA  
3735  C  C   . PHE A  494 ? 2.5371 4.1231 3.2071 -0.1832 -0.6402 -0.2598 494  PHE A C   
3736  O  O   . PHE A  494 ? 2.7037 4.3532 3.3697 -0.2021 -0.6597 -0.2522 494  PHE A O   
3737  C  CB  . PHE A  494 ? 2.3596 3.9704 3.0171 -0.0745 -0.6091 -0.2668 494  PHE A CB  
3738  C  CG  . PHE A  494 ? 2.3281 3.9423 2.9938 -0.0271 -0.5897 -0.2632 494  PHE A CG  
3739  C  CD1 . PHE A  494 ? 2.3541 4.0796 3.0410 0.0042  -0.5920 -0.2424 494  PHE A CD1 
3740  C  CD2 . PHE A  494 ? 2.3682 3.8774 3.0183 -0.0127 -0.5698 -0.2807 494  PHE A CD2 
3741  C  CE1 . PHE A  494 ? 2.3950 4.1187 3.0850 0.0489  -0.5757 -0.2392 494  PHE A CE1 
3742  C  CE2 . PHE A  494 ? 2.4056 3.9151 3.0604 0.0287  -0.5534 -0.2766 494  PHE A CE2 
3743  C  CZ  . PHE A  494 ? 2.3883 4.0008 3.0615 0.0599  -0.5568 -0.2560 494  PHE A CZ  
3744  N  N   . GLN A  495 ? 2.6428 4.1106 3.2953 -0.2007 -0.6337 -0.2788 495  GLN A N   
3745  C  CA  . GLN A  495 ? 2.8601 4.2511 3.4802 -0.2367 -0.6477 -0.2960 495  GLN A CA  
3746  C  C   . GLN A  495 ? 2.8505 4.1486 3.4312 -0.2010 -0.6306 -0.3274 495  GLN A C   
3747  O  O   . GLN A  495 ? 2.8911 4.1184 3.4680 -0.1826 -0.6111 -0.3409 495  GLN A O   
3748  C  CB  . GLN A  495 ? 2.9536 4.2810 3.5776 -0.2854 -0.6574 -0.2940 495  GLN A CB  
3749  C  CG  . GLN A  495 ? 3.0645 4.4749 3.7213 -0.3307 -0.6769 -0.2615 495  GLN A CG  
3750  C  CD  . GLN A  495 ? 3.1238 4.4520 3.7689 -0.3824 -0.6923 -0.2613 495  GLN A CD  
3751  O  OE1 . GLN A  495 ? 3.2778 4.6534 3.9426 -0.4259 -0.7092 -0.2353 495  GLN A OE1 
3752  N  NE2 . GLN A  495 ? 3.0543 4.2584 3.6630 -0.3775 -0.6877 -0.2905 495  GLN A NE2 
3753  N  N   . VAL A  496 ? 2.7591 4.0611 3.3097 -0.1924 -0.6380 -0.3382 496  VAL A N   
3754  C  CA  . VAL A  496 ? 2.6650 3.8908 3.1745 -0.1596 -0.6232 -0.3655 496  VAL A CA  
3755  C  C   . VAL A  496 ? 2.7215 3.8707 3.1970 -0.1911 -0.6347 -0.3858 496  VAL A C   
3756  O  O   . VAL A  496 ? 2.7618 3.9433 3.2328 -0.2225 -0.6575 -0.3791 496  VAL A O   
3757  C  CB  . VAL A  496 ? 2.5774 3.8598 3.0704 -0.1173 -0.6221 -0.3636 496  VAL A CB  
3758  C  CG1 . VAL A  496 ? 2.6018 3.8001 3.0470 -0.0885 -0.6080 -0.3900 496  VAL A CG1 
3759  C  CG2 . VAL A  496 ? 2.5825 3.9409 3.1049 -0.0831 -0.6133 -0.3436 496  VAL A CG2 
3760  N  N   . GLU A  497 ? 2.7075 3.7589 3.1577 -0.1822 -0.6194 -0.4107 497  GLU A N   
3761  C  CA  . GLU A  497 ? 2.7066 3.6788 3.1184 -0.2024 -0.6270 -0.4342 497  GLU A CA  
3762  C  C   . GLU A  497 ? 2.7120 3.6385 3.0851 -0.1685 -0.6101 -0.4574 497  GLU A C   
3763  O  O   . GLU A  497 ? 2.7560 3.6672 3.1288 -0.1365 -0.5879 -0.4623 497  GLU A O   
3764  C  CB  . GLU A  497 ? 2.7357 3.6300 3.1464 -0.2248 -0.6265 -0.4450 497  GLU A CB  
3765  C  CG  . GLU A  497 ? 2.7897 3.7167 3.2379 -0.2524 -0.6373 -0.4213 497  GLU A CG  
3766  C  CD  . GLU A  497 ? 2.7137 3.6914 3.1674 -0.2975 -0.6681 -0.4014 497  GLU A CD  
3767  O  OE1 . GLU A  497 ? 2.7032 3.7575 3.1935 -0.3133 -0.6758 -0.3736 497  GLU A OE1 
3768  O  OE2 . GLU A  497 ? 2.7054 3.6497 3.1257 -0.3184 -0.6849 -0.4129 497  GLU A OE2 
3769  N  N   . LEU A  498 ? 2.7981 3.7017 3.1355 -0.1781 -0.6217 -0.4710 498  LEU A N   
3770  C  CA  . LEU A  498 ? 2.8718 3.7278 3.1661 -0.1529 -0.6085 -0.4934 498  LEU A CA  
3771  C  C   . LEU A  498 ? 3.0462 3.8226 3.3071 -0.1737 -0.6128 -0.5183 498  LEU A C   
3772  O  O   . LEU A  498 ? 3.0923 3.8642 3.3487 -0.2061 -0.6353 -0.5170 498  LEU A O   
3773  C  CB  . LEU A  498 ? 2.8407 3.7473 3.1162 -0.1369 -0.6181 -0.4872 498  LEU A CB  
3774  C  CG  . LEU A  498 ? 2.7649 3.7143 3.0412 -0.0950 -0.6065 -0.4764 498  LEU A CG  
3775  C  CD1 . LEU A  498 ? 2.7050 3.7243 3.0313 -0.0907 -0.6062 -0.4513 498  LEU A CD1 
3776  C  CD2 . LEU A  498 ? 2.7947 3.7811 3.0413 -0.0790 -0.6202 -0.4746 498  LEU A CD2 
3777  N  N   . LEU A  499 ? 3.2275 3.9433 3.4626 -0.1554 -0.5923 -0.5406 499  LEU A N   
3778  C  CA  . LEU A  499 ? 3.3033 3.9465 3.5023 -0.1670 -0.5936 -0.5673 499  LEU A CA  
3779  C  C   . LEU A  499 ? 3.1962 3.8141 3.3522 -0.1465 -0.5799 -0.5855 499  LEU A C   
3780  O  O   . LEU A  499 ? 3.1901 3.8040 3.3417 -0.1224 -0.5580 -0.5885 499  LEU A O   
3781  C  CB  . LEU A  499 ? 3.4527 4.0467 3.6609 -0.1674 -0.5825 -0.5790 499  LEU A CB  
3782  C  CG  . LEU A  499 ? 3.5213 4.1291 3.7678 -0.1869 -0.5942 -0.5613 499  LEU A CG  
3783  C  CD1 . LEU A  499 ? 3.5283 4.0936 3.7837 -0.1743 -0.5771 -0.5726 499  LEU A CD1 
3784  C  CD2 . LEU A  499 ? 3.5350 4.1213 3.7676 -0.2240 -0.6246 -0.5604 499  LEU A CD2 
3785  N  N   . LEU A  500 ? 3.1208 3.7199 3.2421 -0.1585 -0.5940 -0.5970 500  LEU A N   
3786  C  CA  . LEU A  500 ? 3.1694 3.7398 3.2441 -0.1442 -0.5836 -0.6150 500  LEU A CA  
3787  C  C   . LEU A  500 ? 3.2792 3.7860 3.3276 -0.1448 -0.5713 -0.6427 500  LEU A C   
3788  O  O   . LEU A  500 ? 3.3794 3.8538 3.4287 -0.1612 -0.5823 -0.6522 500  LEU A O   
3789  C  CB  . LEU A  500 ? 3.1722 3.7546 3.2208 -0.1554 -0.6049 -0.6146 500  LEU A CB  
3790  C  CG  . LEU A  500 ? 3.2242 3.8778 3.2912 -0.1502 -0.6188 -0.5899 500  LEU A CG  
3791  C  CD1 . LEU A  500 ? 3.2822 3.9469 3.3273 -0.1674 -0.6430 -0.5911 500  LEU A CD1 
3792  C  CD2 . LEU A  500 ? 3.3131 3.9816 3.3640 -0.1170 -0.6038 -0.5852 500  LEU A CD2 
3793  N  N   . ASP A  501 ? 3.2193 3.7088 3.2400 -0.1269 -0.5498 -0.6554 501  ASP A N   
3794  C  CA  . ASP A  501 ? 3.1679 3.6100 3.1594 -0.1244 -0.5362 -0.6827 501  ASP A CA  
3795  C  C   . ASP A  501 ? 3.1421 3.5653 3.1602 -0.1244 -0.5316 -0.6894 501  ASP A C   
3796  O  O   . ASP A  501 ? 3.1298 3.5126 3.1307 -0.1309 -0.5393 -0.7085 501  ASP A O   
3797  C  CB  . ASP A  501 ? 3.2538 3.6643 3.2043 -0.1371 -0.5511 -0.7004 501  ASP A CB  
3798  C  CG  . ASP A  501 ? 3.3325 3.7052 3.2448 -0.1294 -0.5348 -0.7287 501  ASP A CG  
3799  O  OD1 . ASP A  501 ? 3.1850 3.5656 3.0923 -0.1157 -0.5111 -0.7319 501  ASP A OD1 
3800  O  OD2 . ASP A  501 ? 3.5654 3.9026 3.4508 -0.1376 -0.5464 -0.7473 501  ASP A OD2 
3801  N  N   . LYS A  502 ? 3.0597 3.5092 3.1166 -0.1150 -0.5203 -0.6738 502  LYS A N   
3802  C  CA  . LYS A  502 ? 3.0732 3.5049 3.1556 -0.1138 -0.5171 -0.6784 502  LYS A CA  
3803  C  C   . LYS A  502 ? 3.1271 3.5255 3.1848 -0.0995 -0.4986 -0.7063 502  LYS A C   
3804  O  O   . LYS A  502 ? 3.1517 3.5152 3.2065 -0.0988 -0.5044 -0.7214 502  LYS A O   
3805  C  CB  . LYS A  502 ? 3.0043 3.4732 3.1324 -0.1055 -0.5077 -0.6557 502  LYS A CB  
3806  C  CG  . LYS A  502 ? 3.0205 3.4673 3.1722 -0.1048 -0.5064 -0.6604 502  LYS A CG  
3807  C  CD  . LYS A  502 ? 2.9054 3.3846 3.1003 -0.0947 -0.4941 -0.6411 502  LYS A CD  
3808  C  CE  . LYS A  502 ? 2.9263 3.3754 3.1379 -0.0947 -0.4959 -0.6482 502  LYS A CE  
3809  N  NZ  . LYS A  502 ? 2.9509 3.3788 3.1640 -0.1198 -0.5253 -0.6420 502  LYS A NZ  
3810  N  N   . LEU A  503 ? 3.1759 3.5857 3.2123 -0.0876 -0.4774 -0.7131 503  LEU A N   
3811  C  CA  . LEU A  503 ? 3.2267 3.6231 3.2420 -0.0742 -0.4566 -0.7374 503  LEU A CA  
3812  C  C   . LEU A  503 ? 3.3574 3.7127 3.3450 -0.0737 -0.4669 -0.7644 503  LEU A C   
3813  O  O   . LEU A  503 ? 3.3885 3.7328 3.3707 -0.0581 -0.4549 -0.7842 503  LEU A O   
3814  C  CB  . LEU A  503 ? 3.2601 3.6710 3.2412 -0.0723 -0.4402 -0.7403 503  LEU A CB  
3815  C  CG  . LEU A  503 ? 3.2085 3.6476 3.2017 -0.0642 -0.4188 -0.7269 503  LEU A CG  
3816  C  CD1 . LEU A  503 ? 3.1565 3.6155 3.1943 -0.0618 -0.4250 -0.6999 503  LEU A CD1 
3817  C  CD2 . LEU A  503 ? 3.2062 3.6490 3.1551 -0.0695 -0.4118 -0.7246 503  LEU A CD2 
3818  N  N   . LYS A  504 ? 3.4384 3.7713 3.4057 -0.0888 -0.4903 -0.7658 504  LYS A N   
3819  C  CA  . LYS A  504 ? 3.4864 3.7710 3.4232 -0.0895 -0.5062 -0.7893 504  LYS A CA  
3820  C  C   . LYS A  504 ? 3.5046 3.7620 3.4649 -0.0930 -0.5234 -0.7842 504  LYS A C   
3821  O  O   . LYS A  504 ? 3.4549 3.7171 3.4377 -0.1135 -0.5434 -0.7618 504  LYS A O   
3822  C  CB  . LYS A  504 ? 3.4458 3.7142 3.3513 -0.1074 -0.5270 -0.7902 504  LYS A CB  
3823  C  CG  . LYS A  504 ? 3.4156 3.6970 3.2852 -0.1040 -0.5129 -0.8004 504  LYS A CG  
3824  C  CD  . LYS A  504 ? 3.3797 3.6441 3.2146 -0.0863 -0.4973 -0.8317 504  LYS A CD  
3825  C  CE  . LYS A  504 ? 3.3460 3.6209 3.1397 -0.0887 -0.4868 -0.8413 504  LYS A CE  
3826  N  NZ  . LYS A  504 ? 3.3625 3.6315 3.1219 -0.0720 -0.4715 -0.8718 504  LYS A NZ  
3827  N  N   . GLN A  505 ? 3.5943 3.8258 3.5470 -0.0731 -0.5163 -0.8046 505  GLN A N   
3828  C  CA  . GLN A  505 ? 3.5952 3.7889 3.5597 -0.0744 -0.5341 -0.8028 505  GLN A CA  
3829  C  C   . GLN A  505 ? 3.7075 3.8454 3.6396 -0.0956 -0.5698 -0.8060 505  GLN A C   
3830  O  O   . GLN A  505 ? 3.9073 4.0293 3.8024 -0.1014 -0.5782 -0.8179 505  GLN A O   
3831  C  CB  . GLN A  505 ? 3.5295 3.7034 3.4820 -0.0428 -0.5203 -0.8287 505  GLN A CB  
3832  C  CG  . GLN A  505 ? 3.4083 3.6376 3.3937 -0.0246 -0.4866 -0.8245 505  GLN A CG  
3833  C  CD  . GLN A  505 ? 3.2528 3.5029 3.2899 -0.0314 -0.4852 -0.7972 505  GLN A CD  
3834  O  OE1 . GLN A  505 ? 3.2860 3.5095 3.3350 -0.0485 -0.5090 -0.7826 505  GLN A OE1 
3835  N  NE2 . GLN A  505 ? 3.1473 3.4455 3.2129 -0.0198 -0.4580 -0.7894 505  GLN A NE2 
3836  N  N   . LYS A  506 ? 3.4241 3.5298 3.3673 -0.1095 -0.5921 -0.7942 506  LYS A N   
3837  C  CA  . LYS A  506 ? 3.2942 3.3417 3.2040 -0.1356 -0.6298 -0.7936 506  LYS A CA  
3838  C  C   . LYS A  506 ? 3.4571 3.4354 3.3025 -0.1175 -0.6406 -0.8292 506  LYS A C   
3839  O  O   . LYS A  506 ? 3.5932 3.5229 3.4154 -0.0939 -0.6435 -0.8493 506  LYS A O   
3840  C  CB  . LYS A  506 ? 3.1525 3.1733 3.0801 -0.1538 -0.6509 -0.7753 506  LYS A CB  
3841  C  CG  . LYS A  506 ? 3.1988 3.1677 3.0948 -0.1918 -0.6924 -0.7663 506  LYS A CG  
3842  C  CD  . LYS A  506 ? 3.1694 3.1894 3.0782 -0.2202 -0.6988 -0.7470 506  LYS A CD  
3843  C  CE  . LYS A  506 ? 3.2320 3.2070 3.1097 -0.2627 -0.7412 -0.7361 506  LYS A CE  
3844  N  NZ  . LYS A  506 ? 3.2615 3.2292 3.1604 -0.2911 -0.7610 -0.7109 506  LYS A NZ  
3845  N  N   . GLY A  507 ? 3.3231 3.2965 3.1367 -0.1258 -0.6472 -0.8379 507  GLY A N   
3846  C  CA  . GLY A  507 ? 3.2806 3.1914 3.0299 -0.1089 -0.6586 -0.8713 507  GLY A CA  
3847  C  C   . GLY A  507 ? 3.1854 3.1324 2.9192 -0.0973 -0.6377 -0.8855 507  GLY A C   
3848  O  O   . GLY A  507 ? 3.2046 3.1096 2.8853 -0.0900 -0.6487 -0.9093 507  GLY A O   
3849  N  N   . ALA A  508 ? 3.2110 3.2329 2.9869 -0.0960 -0.6085 -0.8705 508  ALA A N   
3850  C  CA  . ALA A  508 ? 3.1838 3.2422 2.9444 -0.0883 -0.5875 -0.8805 508  ALA A CA  
3851  C  C   . ALA A  508 ? 3.2244 3.2815 2.9702 -0.1163 -0.6063 -0.8693 508  ALA A C   
3852  O  O   . ALA A  508 ? 3.2114 3.2281 2.9447 -0.1389 -0.6382 -0.8623 508  ALA A O   
3853  C  CB  . ALA A  508 ? 3.1021 3.2309 2.9046 -0.0800 -0.5539 -0.8666 508  ALA A CB  
3854  N  N   . ILE A  509 ? 3.3857 3.4852 3.1289 -0.1161 -0.5883 -0.8673 509  ILE A N   
3855  C  CA  . ILE A  509 ? 3.4896 3.5944 3.2181 -0.1387 -0.6034 -0.8573 509  ILE A CA  
3856  C  C   . ILE A  509 ? 3.4043 3.5695 3.1763 -0.1496 -0.5947 -0.8263 509  ILE A C   
3857  O  O   . ILE A  509 ? 3.2962 3.4996 3.0786 -0.1366 -0.5682 -0.8234 509  ILE A O   
3858  C  CB  . ILE A  509 ? 3.4512 3.5480 3.1308 -0.1287 -0.5937 -0.8813 509  ILE A CB  
3859  C  CG1 . ILE A  509 ? 3.3506 3.4623 3.0195 -0.1498 -0.6051 -0.8680 509  ILE A CG1 
3860  C  CG2 . ILE A  509 ? 3.4459 3.5797 3.1267 -0.1056 -0.5578 -0.8923 509  ILE A CG2 
3861  C  CD1 . ILE A  509 ? 3.3208 3.3972 2.9784 -0.1743 -0.6415 -0.8614 509  ILE A CD1 
3862  N  N   . ARG A  510 ? 3.5057 3.6804 3.3004 -0.1733 -0.6183 -0.8027 510  ARG A N   
3863  C  CA  . ARG A  510 ? 3.4838 3.7181 3.3191 -0.1802 -0.6143 -0.7729 510  ARG A CA  
3864  C  C   . ARG A  510 ? 3.5573 3.8112 3.3693 -0.1862 -0.6185 -0.7694 510  ARG A C   
3865  O  O   . ARG A  510 ? 3.7027 3.9241 3.4750 -0.1946 -0.6326 -0.7842 510  ARG A O   
3866  C  CB  . ARG A  510 ? 3.4449 3.6912 3.3163 -0.2026 -0.6378 -0.7487 510  ARG A CB  
3867  C  CG  . ARG A  510 ? 3.3310 3.6439 3.2526 -0.2014 -0.6293 -0.7190 510  ARG A CG  
3868  C  CD  . ARG A  510 ? 3.2725 3.5934 3.2222 -0.1806 -0.6042 -0.7190 510  ARG A CD  
3869  N  NE  . ARG A  510 ? 3.3021 3.5836 3.2591 -0.1855 -0.6133 -0.7248 510  ARG A NE  
3870  C  CZ  . ARG A  510 ? 3.2530 3.5404 3.2401 -0.1726 -0.5986 -0.7209 510  ARG A CZ  
3871  N  NH1 . ARG A  510 ? 3.1678 3.5001 3.1817 -0.1553 -0.5737 -0.7108 510  ARG A NH1 
3872  N  NH2 . ARG A  510 ? 3.3144 3.5579 3.3003 -0.1769 -0.6106 -0.7272 510  ARG A NH2 
3873  N  N   . ARG A  511 ? 3.5132 3.8171 3.3459 -0.1798 -0.6074 -0.7501 511  ARG A N   
3874  C  CA  . ARG A  511 ? 3.4500 3.7691 3.2547 -0.1800 -0.6101 -0.7475 511  ARG A CA  
3875  C  C   . ARG A  511 ? 3.4205 3.7931 3.2516 -0.1837 -0.6222 -0.7194 511  ARG A C   
3876  O  O   . ARG A  511 ? 3.3461 3.7304 3.1508 -0.1810 -0.6273 -0.7170 511  ARG A O   
3877  C  CB  . ARG A  511 ? 3.3836 3.6997 3.1604 -0.1617 -0.5828 -0.7592 511  ARG A CB  
3878  C  CG  . ARG A  511 ? 3.4282 3.7046 3.1731 -0.1558 -0.5698 -0.7886 511  ARG A CG  
3879  C  CD  . ARG A  511 ? 3.4042 3.6926 3.1390 -0.1407 -0.5397 -0.7945 511  ARG A CD  
3880  N  NE  . ARG A  511 ? 3.4737 3.7880 3.2533 -0.1318 -0.5267 -0.7795 511  ARG A NE  
3881  C  CZ  . ARG A  511 ? 3.6275 3.9573 3.4067 -0.1210 -0.5018 -0.7796 511  ARG A CZ  
3882  N  NH1 . ARG A  511 ? 3.6281 3.9525 3.3633 -0.1203 -0.4873 -0.7929 511  ARG A NH1 
3883  N  NH2 . ARG A  511 ? 3.6697 4.0214 3.4905 -0.1133 -0.4921 -0.7654 511  ARG A NH2 
3884  N  N   . ALA A  512 ? 3.5209 3.9283 3.4002 -0.1878 -0.6273 -0.6985 512  ALA A N   
3885  C  CA  . ALA A  512 ? 3.4676 3.9363 3.3730 -0.1875 -0.6385 -0.6721 512  ALA A CA  
3886  C  C   . ALA A  512 ? 3.6239 4.1201 3.5676 -0.2118 -0.6610 -0.6546 512  ALA A C   
3887  O  O   . ALA A  512 ? 3.7913 4.2592 3.7497 -0.2236 -0.6626 -0.6583 512  ALA A O   
3888  C  CB  . ALA A  512 ? 3.2977 3.7983 3.2228 -0.1626 -0.6177 -0.6591 512  ALA A CB  
3889  N  N   . LEU A  513 ? 3.5036 4.0575 3.4605 -0.2191 -0.6793 -0.6347 513  LEU A N   
3890  C  CA  . LEU A  513 ? 3.4728 4.0707 3.4664 -0.2462 -0.7021 -0.6132 513  LEU A CA  
3891  C  C   . LEU A  513 ? 3.3942 4.0718 3.3988 -0.2421 -0.7158 -0.5930 513  LEU A C   
3892  O  O   . LEU A  513 ? 3.3311 4.0071 3.3012 -0.2304 -0.7188 -0.6011 513  LEU A O   
3893  C  CB  . LEU A  513 ? 3.4191 3.9670 3.3920 -0.2812 -0.7253 -0.6235 513  LEU A CB  
3894  C  CG  . LEU A  513 ? 3.2735 3.7990 3.2032 -0.2945 -0.7438 -0.6355 513  LEU A CG  
3895  C  CD1 . LEU A  513 ? 3.2537 3.8436 3.2009 -0.3228 -0.7731 -0.6123 513  LEU A CD1 
3896  C  CD2 . LEU A  513 ? 3.3106 3.7472 3.2021 -0.3087 -0.7506 -0.6602 513  LEU A CD2 
3897  N  N   . PHE A  514 ? 3.3195 4.0690 3.3703 -0.2497 -0.7239 -0.5670 514  PHE A N   
3898  C  CA  . PHE A  514 ? 3.2489 4.0889 3.3150 -0.2376 -0.7343 -0.5467 514  PHE A CA  
3899  C  C   . PHE A  514 ? 3.3184 4.1768 3.3615 -0.2584 -0.7603 -0.5474 514  PHE A C   
3900  O  O   . PHE A  514 ? 3.3474 4.1580 3.3721 -0.2917 -0.7752 -0.5572 514  PHE A O   
3901  C  CB  . PHE A  514 ? 3.0730 3.9925 3.1945 -0.2471 -0.7396 -0.5186 514  PHE A CB  
3902  C  CG  . PHE A  514 ? 2.9975 3.9160 3.1433 -0.2193 -0.7145 -0.5145 514  PHE A CG  
3903  C  CD1 . PHE A  514 ? 3.0013 3.8484 3.1487 -0.2247 -0.6990 -0.5271 514  PHE A CD1 
3904  C  CD2 . PHE A  514 ? 2.9200 3.9088 3.0837 -0.1852 -0.7075 -0.4988 514  PHE A CD2 
3905  C  CE1 . PHE A  514 ? 2.8939 3.7421 3.0635 -0.2000 -0.6764 -0.5230 514  PHE A CE1 
3906  C  CE2 . PHE A  514 ? 2.8470 3.8317 3.0298 -0.1601 -0.6858 -0.4947 514  PHE A CE2 
3907  C  CZ  . PHE A  514 ? 2.8287 3.7441 3.0161 -0.1692 -0.6699 -0.5063 514  PHE A CZ  
3908  N  N   . LEU A  515 ? 3.2751 4.2031 3.3159 -0.2361 -0.7671 -0.5370 515  LEU A N   
3909  C  CA  . LEU A  515 ? 3.1703 4.1168 3.1840 -0.2476 -0.7895 -0.5399 515  LEU A CA  
3910  C  C   . LEU A  515 ? 3.0524 4.0534 3.0936 -0.2946 -0.8174 -0.5218 515  LEU A C   
3911  O  O   . LEU A  515 ? 3.1255 4.0875 3.1414 -0.3269 -0.8354 -0.5309 515  LEU A O   
3912  C  CB  . LEU A  515 ? 3.1537 4.1611 3.1547 -0.2059 -0.7902 -0.5339 515  LEU A CB  
3913  C  CG  . LEU A  515 ? 3.1819 4.2101 3.1500 -0.2081 -0.8118 -0.5385 515  LEU A CG  
3914  C  CD1 . LEU A  515 ? 3.2061 4.1300 3.1199 -0.2142 -0.8076 -0.5662 515  LEU A CD1 
3915  C  CD2 . LEU A  515 ? 3.2147 4.3076 3.1708 -0.1607 -0.8139 -0.5310 515  LEU A CD2 
3916  N  N   . TYR A  516 ? 2.9690 4.0603 3.0592 -0.3011 -0.8223 -0.4955 516  TYR A N   
3917  C  CA  . TYR A  516 ? 2.9936 4.1486 3.1100 -0.3503 -0.8499 -0.4742 516  TYR A CA  
3918  C  C   . TYR A  516 ? 3.0637 4.1750 3.1992 -0.3907 -0.8524 -0.4682 516  TYR A C   
3919  O  O   . TYR A  516 ? 3.1285 4.2329 3.2593 -0.4418 -0.8779 -0.4607 516  TYR A O   
3920  C  CB  . TYR A  516 ? 2.9729 4.2695 3.1297 -0.3370 -0.8575 -0.4467 516  TYR A CB  
3921  C  CG  . TYR A  516 ? 2.9487 4.3323 3.1190 -0.3816 -0.8896 -0.4268 516  TYR A CG  
3922  C  CD1 . TYR A  516 ? 2.9260 4.2518 3.0677 -0.4298 -0.9113 -0.4343 516  TYR A CD1 
3923  C  CD2 . TYR A  516 ? 2.9045 4.4314 3.1140 -0.3755 -0.8991 -0.4003 516  TYR A CD2 
3924  C  CE1 . TYR A  516 ? 2.9028 4.3085 3.0544 -0.4751 -0.9422 -0.4147 516  TYR A CE1 
3925  C  CE2 . TYR A  516 ? 2.8452 4.4623 3.0679 -0.4194 -0.9286 -0.3808 516  TYR A CE2 
3926  C  CZ  . TYR A  516 ? 2.8040 4.3587 2.9976 -0.4712 -0.9504 -0.3874 516  TYR A CZ  
3927  O  OH  . TYR A  516 ? 2.6980 4.3427 2.9023 -0.5192 -0.9813 -0.3665 516  TYR A OH  
3928  N  N   . SER A  517 ? 3.0573 4.1348 3.2097 -0.3696 -0.8282 -0.4712 517  SER A N   
3929  C  CA  . SER A  517 ? 3.0979 4.1274 3.2643 -0.4032 -0.8306 -0.4670 517  SER A CA  
3930  C  C   . SER A  517 ? 3.2417 4.1489 3.3618 -0.4254 -0.8377 -0.4919 517  SER A C   
3931  O  O   . SER A  517 ? 3.3382 4.2019 3.4566 -0.4638 -0.8523 -0.4876 517  SER A O   
3932  C  CB  . SER A  517 ? 2.9683 3.9907 3.1620 -0.3704 -0.8019 -0.4661 517  SER A CB  
3933  O  OG  . SER A  517 ? 2.9556 3.9321 3.1615 -0.4006 -0.8051 -0.4619 517  SER A OG  
3934  N  N   . ARG A  518 ? 3.1669 4.0163 3.2453 -0.4011 -0.8289 -0.5179 518  ARG A N   
3935  C  CA  . ARG A  518 ? 3.1505 3.8870 3.1806 -0.4144 -0.8339 -0.5445 518  ARG A CA  
3936  C  C   . ARG A  518 ? 3.1617 3.8232 3.1929 -0.4134 -0.8211 -0.5548 518  ARG A C   
3937  O  O   . ARG A  518 ? 3.1514 3.7327 3.1519 -0.4388 -0.8364 -0.5667 518  ARG A O   
3938  C  CB  . ARG A  518 ? 3.2870 4.0138 3.2942 -0.4643 -0.8703 -0.5390 518  ARG A CB  
3939  C  CG  . ARG A  518 ? 3.3178 4.1436 3.3363 -0.4742 -0.8881 -0.5208 518  ARG A CG  
3940  C  CD  . ARG A  518 ? 3.2428 4.0727 3.2380 -0.4315 -0.8733 -0.5377 518  ARG A CD  
3941  N  NE  . ARG A  518 ? 3.2026 4.0946 3.1890 -0.4464 -0.8970 -0.5286 518  ARG A NE  
3942  C  CZ  . ARG A  518 ? 3.1783 4.0196 3.1231 -0.4719 -0.9176 -0.5412 518  ARG A CZ  
3943  N  NH1 . ARG A  518 ? 3.2277 3.9549 3.1342 -0.4828 -0.9174 -0.5638 518  ARG A NH1 
3944  N  NH2 . ARG A  518 ? 3.1040 4.0097 3.0436 -0.4844 -0.9389 -0.5317 518  ARG A NH2 
3945  N  N   . SER A  519 ? 3.2891 3.9736 3.3515 -0.3813 -0.7941 -0.5511 519  SER A N   
3946  C  CA  . SER A  519 ? 3.3260 3.9548 3.3968 -0.3791 -0.7822 -0.5573 519  SER A CA  
3947  C  C   . SER A  519 ? 3.2744 3.9106 3.3614 -0.3324 -0.7466 -0.5645 519  SER A C   
3948  O  O   . SER A  519 ? 3.1413 3.8544 3.2589 -0.3126 -0.7366 -0.5474 519  SER A O   
3949  C  CB  . SER A  519 ? 3.2792 3.9483 3.3861 -0.4147 -0.7999 -0.5293 519  SER A CB  
3950  O  OG  . SER A  519 ? 3.1720 3.7826 3.2836 -0.4122 -0.7904 -0.5354 519  SER A OG  
3951  N  N   . PRO A  520 ? 3.4120 3.9705 3.4755 -0.3131 -0.7280 -0.5900 520  PRO A N   
3952  C  CA  . PRO A  520 ? 3.3568 3.9188 3.4290 -0.2724 -0.6948 -0.5978 520  PRO A CA  
3953  C  C   . PRO A  520 ? 3.2277 3.8498 3.3505 -0.2616 -0.6833 -0.5745 520  PRO A C   
3954  O  O   . PRO A  520 ? 3.1502 3.7882 3.2809 -0.2291 -0.6591 -0.5753 520  PRO A O   
3955  C  CB  . PRO A  520 ? 3.3454 3.8211 3.3898 -0.2643 -0.6832 -0.6257 520  PRO A CB  
3956  C  CG  . PRO A  520 ? 3.3771 3.7983 3.3794 -0.2889 -0.7078 -0.6403 520  PRO A CG  
3957  C  CD  . PRO A  520 ? 3.4286 3.8942 3.4482 -0.3264 -0.7385 -0.6146 520  PRO A CD  
3958  N  N   . SER A  521 ? 3.1451 3.7985 3.2986 -0.2903 -0.7013 -0.5530 521  SER A N   
3959  C  CA  . SER A  521 ? 3.0865 3.8007 3.2888 -0.2832 -0.6925 -0.5294 521  SER A CA  
3960  C  C   . SER A  521 ? 3.1099 3.9182 3.3402 -0.3044 -0.7135 -0.5002 521  SER A C   
3961  O  O   . SER A  521 ? 3.1041 3.9175 3.3213 -0.3399 -0.7401 -0.4952 521  SER A O   
3962  C  CB  . SER A  521 ? 3.0842 3.7528 3.3002 -0.2976 -0.6924 -0.5294 521  SER A CB  
3963  O  OG  . SER A  521 ? 3.1332 3.7610 3.3296 -0.3396 -0.7217 -0.5290 521  SER A OG  
3964  N  N   . HIS A  522 ? 3.0892 3.9751 3.3560 -0.2817 -0.7019 -0.4808 522  HIS A N   
3965  C  CA  . HIS A  522 ? 3.0732 4.0656 3.3708 -0.2948 -0.7189 -0.4523 522  HIS A CA  
3966  C  C   . HIS A  522 ? 2.9359 3.9813 3.2810 -0.2914 -0.7105 -0.4301 522  HIS A C   
3967  O  O   . HIS A  522 ? 2.7481 3.7903 3.1038 -0.2534 -0.6863 -0.4330 522  HIS A O   
3968  C  CB  . HIS A  522 ? 2.9834 4.0335 3.2698 -0.2605 -0.7159 -0.4516 522  HIS A CB  
3969  C  CG  . HIS A  522 ? 2.8991 4.0706 3.2171 -0.2661 -0.7322 -0.4236 522  HIS A CG  
3970  N  ND1 . HIS A  522 ? 2.7668 4.0174 3.1182 -0.2357 -0.7216 -0.4054 522  HIS A ND1 
3971  C  CD2 . HIS A  522 ? 2.9158 4.1488 3.2363 -0.2981 -0.7588 -0.4106 522  HIS A CD2 
3972  C  CE1 . HIS A  522 ? 2.7474 4.1079 3.1212 -0.2463 -0.7402 -0.3831 522  HIS A CE1 
3973  N  NE2 . HIS A  522 ? 2.8573 4.2117 3.2142 -0.2857 -0.7629 -0.3852 522  HIS A NE2 
3974  N  N   . SER A  523 ? 2.9169 4.0096 3.2876 -0.3333 -0.7314 -0.4072 523  SER A N   
3975  C  CA  . SER A  523 ? 2.7088 3.8615 3.1251 -0.3361 -0.7265 -0.3831 523  SER A CA  
3976  C  C   . SER A  523 ? 2.7344 4.0225 3.1813 -0.3298 -0.7350 -0.3568 523  SER A C   
3977  O  O   . SER A  523 ? 2.7948 4.1329 3.2326 -0.3491 -0.7555 -0.3505 523  SER A O   
3978  C  CB  . SER A  523 ? 2.6938 3.8100 3.1148 -0.3894 -0.7452 -0.3732 523  SER A CB  
3979  O  OG  . SER A  523 ? 2.6791 3.8497 3.1427 -0.3929 -0.7398 -0.3500 523  SER A OG  
3980  N  N   . LYS A  524 ? 2.6982 4.0482 3.1802 -0.3008 -0.7194 -0.3419 524  LYS A N   
3981  C  CA  . LYS A  524 ? 2.6640 4.1496 3.1751 -0.2863 -0.7257 -0.3176 524  LYS A CA  
3982  C  C   . LYS A  524 ? 2.6088 4.1498 3.1636 -0.2786 -0.7148 -0.2966 524  LYS A C   
3983  O  O   . LYS A  524 ? 2.4174 3.9065 2.9744 -0.2457 -0.6918 -0.3061 524  LYS A O   
3984  C  CB  . LYS A  524 ? 2.5137 4.0210 3.0022 -0.2288 -0.7156 -0.3295 524  LYS A CB  
3985  C  CG  . LYS A  524 ? 2.3969 4.0458 2.9104 -0.2033 -0.7225 -0.3069 524  LYS A CG  
3986  C  CD  . LYS A  524 ? 2.2881 4.0303 2.8152 -0.2487 -0.7509 -0.2884 524  LYS A CD  
3987  C  CE  . LYS A  524 ? 2.1856 4.0864 2.7463 -0.2264 -0.7571 -0.2628 524  LYS A CE  
3988  N  NZ  . LYS A  524 ? 2.1647 4.0961 2.7006 -0.1577 -0.7504 -0.2733 524  LYS A NZ  
3989  N  N   . ASN A  525 ? 2.6867 4.3362 3.2753 -0.3111 -0.7320 -0.2675 525  ASN A N   
3990  C  CA  . ASN A  525 ? 2.5145 4.2369 3.1466 -0.3070 -0.7244 -0.2439 525  ASN A CA  
3991  C  C   . ASN A  525 ? 2.4853 4.3161 3.1311 -0.2488 -0.7154 -0.2357 525  ASN A C   
3992  O  O   . ASN A  525 ? 2.5674 4.4895 3.2112 -0.2446 -0.7302 -0.2281 525  ASN A O   
3993  C  CB  . ASN A  525 ? 2.6115 4.3992 3.2678 -0.3753 -0.7492 -0.2157 525  ASN A CB  
3994  C  CG  . ASN A  525 ? 2.9924 4.6573 3.6266 -0.4279 -0.7597 -0.2244 525  ASN A CG  
3995  O  OD1 . ASN A  525 ? 2.5973 4.1511 3.2174 -0.4092 -0.7424 -0.2446 525  ASN A OD1 
3996  N  ND2 . ASN A  525 ? 4.4246 6.1050 5.0503 -0.4922 -0.7892 -0.2103 525  ASN A ND2 
3997  N  N   . MET A  526 ? 2.3659 4.1885 3.0234 -0.2031 -0.6930 -0.2368 526  MET A N   
3998  C  CA  . MET A  526 ? 2.3424 4.2331 2.9963 -0.1367 -0.6836 -0.2361 526  MET A CA  
3999  C  C   . MET A  526 ? 2.2290 4.2090 2.9238 -0.1178 -0.6752 -0.2130 526  MET A C   
4000  O  O   . MET A  526 ? 2.2812 4.2017 2.9857 -0.1083 -0.6576 -0.2155 526  MET A O   
4001  C  CB  . MET A  526 ? 2.4122 4.1903 3.0230 -0.0882 -0.6647 -0.2646 526  MET A CB  
4002  C  CG  . MET A  526 ? 2.5082 4.3281 3.0872 -0.0310 -0.6670 -0.2711 526  MET A CG  
4003  S  SD  . MET A  526 ? 2.6206 4.3140 3.1432 0.0248  -0.6466 -0.2995 526  MET A SD  
4004  C  CE  . MET A  526 ? 2.5454 4.3218 3.0352 0.0906  -0.6576 -0.2971 526  MET A CE  
4005  N  N   . THR A  527 ? 2.2523 4.3795 2.9710 -0.1118 -0.6881 -0.1907 527  THR A N   
4006  C  CA  . THR A  527 ? 2.2153 4.4443 2.9661 -0.0774 -0.6801 -0.1708 527  THR A CA  
4007  C  C   . THR A  527 ? 2.2645 4.4995 2.9836 0.0054  -0.6705 -0.1839 527  THR A C   
4008  O  O   . THR A  527 ? 2.3707 4.6598 3.0666 0.0326  -0.6827 -0.1883 527  THR A O   
4009  C  CB  . THR A  527 ? 2.2223 4.6175 3.0124 -0.1097 -0.6990 -0.1401 527  THR A CB  
4010  O  OG1 . THR A  527 ? 2.2641 4.6422 3.0777 -0.1893 -0.7091 -0.1255 527  THR A OG1 
4011  C  CG2 . THR A  527 ? 2.0749 4.5885 2.8935 -0.0629 -0.6907 -0.1216 527  THR A CG2 
4012  N  N   . ILE A  528 ? 2.1545 4.3287 2.8677 0.0451  -0.6505 -0.1904 528  ILE A N   
4013  C  CA  . ILE A  528 ? 2.1260 4.3003 2.8036 0.1234  -0.6435 -0.2001 528  ILE A CA  
4014  C  C   . ILE A  528 ? 2.1550 4.4078 2.8633 0.1554  -0.6347 -0.1812 528  ILE A C   
4015  O  O   . ILE A  528 ? 2.1179 4.3711 2.8665 0.1201  -0.6264 -0.1680 528  ILE A O   
4016  C  CB  . ILE A  528 ? 2.0013 4.0158 2.6282 0.1471  -0.6291 -0.2280 528  ILE A CB  
4017  C  CG1 . ILE A  528 ? 2.0130 3.9510 2.6562 0.1425  -0.6083 -0.2285 528  ILE A CG1 
4018  C  CG2 . ILE A  528 ? 2.0726 4.0027 2.6770 0.1041  -0.6351 -0.2458 528  ILE A CG2 
4019  C  CD1 . ILE A  528 ? 2.0913 3.8882 2.6854 0.1664  -0.5938 -0.2534 528  ILE A CD1 
4020  N  N   . SER A  529 ? 2.2338 4.5486 2.9179 0.2252  -0.6375 -0.1808 529  SER A N   
4021  C  CA  . SER A  529 ? 2.1861 4.5798 2.8911 0.2671  -0.6305 -0.1646 529  SER A CA  
4022  C  C   . SER A  529 ? 1.9544 4.2328 2.6150 0.3220  -0.6154 -0.1809 529  SER A C   
4023  O  O   . SER A  529 ? 1.9416 4.1428 2.5416 0.3608  -0.6186 -0.2010 529  SER A O   
4024  C  CB  . SER A  529 ? 2.2691 4.8244 2.9753 0.3127  -0.6463 -0.1517 529  SER A CB  
4025  O  OG  . SER A  529 ? 2.2732 4.7915 2.9147 0.3752  -0.6543 -0.1712 529  SER A OG  
4026  N  N   . ARG A  530 ? 1.9203 4.1844 2.6081 0.3219  -0.6003 -0.1715 530  ARG A N   
4027  C  CA  . ARG A  530 ? 1.9787 4.1397 2.6264 0.3703  -0.5867 -0.1841 530  ARG A CA  
4028  C  C   . ARG A  530 ? 1.9484 4.1746 2.5593 0.4523  -0.5948 -0.1815 530  ARG A C   
4029  O  O   . ARG A  530 ? 1.8679 4.2406 2.5051 0.4711  -0.6051 -0.1643 530  ARG A O   
4030  C  CB  . ARG A  530 ? 2.1150 4.2426 2.8047 0.3434  -0.5687 -0.1746 530  ARG A CB  
4031  C  CG  . ARG A  530 ? 2.0719 4.3070 2.7922 0.3764  -0.5661 -0.1531 530  ARG A CG  
4032  C  CD  . ARG A  530 ? 1.8608 4.0580 2.6239 0.3419  -0.5492 -0.1438 530  ARG A CD  
4033  N  NE  . ARG A  530 ? 1.7877 4.0692 2.5709 0.3816  -0.5447 -0.1260 530  ARG A NE  
4034  C  CZ  . ARG A  530 ? 1.8400 4.2722 2.6694 0.3719  -0.5518 -0.1018 530  ARG A CZ  
4035  N  NH1 . ARG A  530 ? 1.9604 4.4745 2.8186 0.3220  -0.5649 -0.0918 530  ARG A NH1 
4036  N  NH2 . ARG A  530 ? 1.7675 4.2722 2.6116 0.4118  -0.5466 -0.0870 530  ARG A NH2 
4037  N  N   . GLY A  531 ? 2.0697 4.1855 2.6143 0.5014  -0.5920 -0.1989 531  GLY A N   
4038  C  CA  . GLY A  531 ? 2.1306 4.2767 2.6262 0.5840  -0.6007 -0.1989 531  GLY A CA  
4039  C  C   . GLY A  531 ? 2.1065 4.2977 2.5498 0.6315  -0.6226 -0.2073 531  GLY A C   
4040  O  O   . GLY A  531 ? 2.0818 4.2320 2.4540 0.7015  -0.6320 -0.2168 531  GLY A O   
4041  N  N   . GLY A  532 ? 2.2291 4.5001 2.7018 0.5950  -0.6329 -0.2040 532  GLY A N   
4042  C  CA  . GLY A  532 ? 2.3052 4.6410 2.7358 0.6403  -0.6547 -0.2101 532  GLY A CA  
4043  C  C   . GLY A  532 ? 2.3730 4.5726 2.7204 0.6611  -0.6628 -0.2348 532  GLY A C   
4044  O  O   . GLY A  532 ? 2.4374 4.5764 2.7105 0.7285  -0.6706 -0.2452 532  GLY A O   
4045  N  N   . LEU A  533 ? 2.3752 4.5190 2.7297 0.6023  -0.6619 -0.2443 533  LEU A N   
4046  C  CA  . LEU A  533 ? 2.3883 4.4059 2.6679 0.6113  -0.6690 -0.2672 533  LEU A CA  
4047  C  C   . LEU A  533 ? 2.4169 4.3505 2.7247 0.5320  -0.6561 -0.2748 533  LEU A C   
4048  O  O   . LEU A  533 ? 2.4946 4.4786 2.8748 0.4745  -0.6471 -0.2626 533  LEU A O   
4049  C  CB  . LEU A  533 ? 2.1714 4.2558 2.4122 0.6476  -0.6933 -0.2731 533  LEU A CB  
4050  C  CG  . LEU A  533 ? 2.0019 4.1931 2.2100 0.7311  -0.7124 -0.2683 533  LEU A CG  
4051  C  CD1 . LEU A  533 ? 2.0253 4.2895 2.2134 0.7441  -0.7344 -0.2740 533  LEU A CD1 
4052  C  CD2 . LEU A  533 ? 2.0826 4.1639 2.2000 0.8027  -0.7174 -0.2803 533  LEU A CD2 
4053  N  N   . MET A  534 ? 2.3384 4.1404 2.5841 0.5297  -0.6563 -0.2951 534  MET A N   
4054  C  CA  . MET A  534 ? 2.3362 4.0573 2.6003 0.4611  -0.6451 -0.3052 534  MET A CA  
4055  C  C   . MET A  534 ? 2.4089 4.1909 2.6898 0.4286  -0.6594 -0.3067 534  MET A C   
4056  O  O   . MET A  534 ? 2.4534 4.2488 2.6850 0.4626  -0.6771 -0.3146 534  MET A O   
4057  C  CB  . MET A  534 ? 2.4232 3.9881 2.6140 0.4687  -0.6393 -0.3255 534  MET A CB  
4058  C  CG  . MET A  534 ? 2.5138 3.9936 2.7199 0.4037  -0.6258 -0.3377 534  MET A CG  
4059  S  SD  . MET A  534 ? 2.6433 3.9587 2.7571 0.4131  -0.6216 -0.3603 534  MET A SD  
4060  C  CE  . MET A  534 ? 2.6505 3.9227 2.7382 0.4574  -0.6124 -0.3531 534  MET A CE  
4061  N  N   . GLN A  535 ? 2.3708 4.1854 2.7166 0.3631  -0.6535 -0.2992 535  GLN A N   
4062  C  CA  . GLN A  535 ? 2.3481 4.2097 2.7095 0.3231  -0.6675 -0.3001 535  GLN A CA  
4063  C  C   . GLN A  535 ? 2.4536 4.1861 2.7855 0.2840  -0.6617 -0.3212 535  GLN A C   
4064  O  O   . GLN A  535 ? 2.4338 4.0899 2.7849 0.2472  -0.6450 -0.3256 535  GLN A O   
4065  C  CB  . GLN A  535 ? 2.2307 4.2008 2.6707 0.2714  -0.6693 -0.2787 535  GLN A CB  
4066  C  CG  . GLN A  535 ? 2.1285 4.2635 2.5967 0.3012  -0.6827 -0.2578 535  GLN A CG  
4067  C  CD  . GLN A  535 ? 2.0673 4.3046 2.6105 0.2434  -0.6839 -0.2340 535  GLN A CD  
4068  O  OE1 . GLN A  535 ? 2.1390 4.3170 2.7128 0.1944  -0.6716 -0.2314 535  GLN A OE1 
4069  N  NE2 . GLN A  535 ? 1.9837 4.3765 2.5536 0.2482  -0.7000 -0.2162 535  GLN A NE2 
4070  N  N   . CYS A  536 ? 2.6694 4.3815 2.9539 0.2938  -0.6759 -0.3345 536  CYS A N   
4071  C  CA  . CYS A  536 ? 2.7780 4.3736 3.0262 0.2632  -0.6721 -0.3555 536  CYS A CA  
4072  C  C   . CYS A  536 ? 2.7461 4.3885 3.0085 0.2243  -0.6883 -0.3565 536  CYS A C   
4073  O  O   . CYS A  536 ? 2.7315 4.4922 3.0146 0.2334  -0.7050 -0.3432 536  CYS A O   
4074  C  CB  . CYS A  536 ? 3.0294 4.5336 3.1926 0.3120  -0.6742 -0.3723 536  CYS A CB  
4075  S  SG  . CYS A  536 ? 3.3790 4.7224 3.4938 0.2804  -0.6604 -0.3967 536  CYS A SG  
4076  N  N   . GLU A  537 ? 2.7880 4.3403 3.0376 0.1811  -0.6838 -0.3724 537  GLU A N   
4077  C  CA  . GLU A  537 ? 2.8665 4.4480 3.1249 0.1406  -0.6997 -0.3747 537  GLU A CA  
4078  C  C   . GLU A  537 ? 2.9644 4.4268 3.1723 0.1239  -0.6967 -0.3992 537  GLU A C   
4079  O  O   . GLU A  537 ? 3.0039 4.3691 3.2031 0.1087  -0.6787 -0.4111 537  GLU A O   
4080  C  CB  . GLU A  537 ? 2.7976 4.4282 3.1228 0.0812  -0.7004 -0.3598 537  GLU A CB  
4081  C  CG  . GLU A  537 ? 2.9771 4.6007 3.3042 0.0287  -0.7151 -0.3650 537  GLU A CG  
4082  C  CD  . GLU A  537 ? 3.0400 4.7138 3.4245 -0.0298 -0.7211 -0.3473 537  GLU A CD  
4083  O  OE1 . GLU A  537 ? 3.0259 4.7984 3.4537 -0.0266 -0.7225 -0.3247 537  GLU A OE1 
4084  O  OE2 . GLU A  537 ? 3.0902 4.7025 3.4719 -0.0791 -0.7258 -0.3559 537  GLU A OE2 
4085  N  N   . GLU A  538 ? 2.9266 4.4026 3.1016 0.1273  -0.7144 -0.4067 538  GLU A N   
4086  C  CA  . GLU A  538 ? 2.9567 4.3309 3.0809 0.1125  -0.7142 -0.4294 538  GLU A CA  
4087  C  C   . GLU A  538 ? 3.0422 4.4244 3.1910 0.0548  -0.7244 -0.4316 538  GLU A C   
4088  O  O   . GLU A  538 ? 2.9926 4.4728 3.1839 0.0326  -0.7394 -0.4150 538  GLU A O   
4089  C  CB  . GLU A  538 ? 2.9837 4.3511 3.0417 0.1602  -0.7280 -0.4382 538  GLU A CB  
4090  C  CG  . GLU A  538 ? 3.1073 4.3574 3.1008 0.1539  -0.7250 -0.4617 538  GLU A CG  
4091  C  CD  . GLU A  538 ? 3.2459 4.4951 3.1733 0.1957  -0.7438 -0.4690 538  GLU A CD  
4092  O  OE1 . GLU A  538 ? 3.2953 4.6357 3.2263 0.2347  -0.7588 -0.4569 538  GLU A OE1 
4093  O  OE2 . GLU A  538 ? 3.3116 4.4709 3.1814 0.1908  -0.7440 -0.4871 538  GLU A OE2 
4094  N  N   . LEU A  539 ? 3.1437 4.4219 3.2621 0.0298  -0.7173 -0.4521 539  LEU A N   
4095  C  CA  . LEU A  539 ? 3.2077 4.4712 3.3369 -0.0223 -0.7276 -0.4579 539  LEU A CA  
4096  C  C   . LEU A  539 ? 3.1718 4.3240 3.2442 -0.0265 -0.7212 -0.4840 539  LEU A C   
4097  O  O   . LEU A  539 ? 3.2520 4.3330 3.2906 -0.0025 -0.7039 -0.4956 539  LEU A O   
4098  C  CB  . LEU A  539 ? 3.1473 4.4109 3.3293 -0.0662 -0.7214 -0.4491 539  LEU A CB  
4099  C  CG  . LEU A  539 ? 3.1445 4.4318 3.3488 -0.1215 -0.7409 -0.4439 539  LEU A CG  
4100  C  CD1 . LEU A  539 ? 3.0689 4.4818 3.2951 -0.1238 -0.7642 -0.4232 539  LEU A CD1 
4101  C  CD2 . LEU A  539 ? 3.1241 4.3918 3.3687 -0.1590 -0.7346 -0.4365 539  LEU A CD2 
4102  N  N   . ILE A  540 ? 2.7884 3.9273 2.8486 -0.0588 -0.7358 -0.4926 540  ILE A N   
4103  C  CA  . ILE A  540 ? 2.6854 3.7308 2.6893 -0.0621 -0.7327 -0.5170 540  ILE A CA  
4104  C  C   . ILE A  540 ? 2.7322 3.7071 2.7440 -0.1048 -0.7253 -0.5303 540  ILE A C   
4105  O  O   . ILE A  540 ? 2.7123 3.7134 2.7562 -0.1430 -0.7385 -0.5229 540  ILE A O   
4106  C  CB  . ILE A  540 ? 2.6945 3.7689 2.6668 -0.0596 -0.7556 -0.5203 540  ILE A CB  
4107  C  CG1 . ILE A  540 ? 2.6699 3.8028 2.6217 -0.0081 -0.7635 -0.5112 540  ILE A CG1 
4108  C  CG2 . ILE A  540 ? 2.7634 3.7411 2.6798 -0.0690 -0.7528 -0.5451 540  ILE A CG2 
4109  C  CD1 . ILE A  540 ? 2.6798 3.8406 2.5958 0.0009  -0.7863 -0.5156 540  ILE A CD1 
4110  N  N   . ALA A  541 ? 3.0694 3.9552 3.0479 -0.0978 -0.7055 -0.5496 541  ALA A N   
4111  C  CA  . ALA A  541 ? 3.1116 3.9231 3.0831 -0.1285 -0.6978 -0.5677 541  ALA A CA  
4112  C  C   . ALA A  541 ? 3.1130 3.8555 3.0225 -0.1233 -0.6947 -0.5908 541  ALA A C   
4113  O  O   . ALA A  541 ? 3.1458 3.8798 3.0164 -0.0940 -0.6912 -0.5931 541  ALA A O   
4114  C  CB  . ALA A  541 ? 3.1569 3.9349 3.1520 -0.1266 -0.6745 -0.5697 541  ALA A CB  
4115  N  N   . TYR A  542 ? 3.1622 3.8529 3.0576 -0.1517 -0.6977 -0.6078 542  TYR A N   
4116  C  CA  . TYR A  542 ? 3.2974 3.9264 3.1346 -0.1502 -0.6953 -0.6300 542  TYR A CA  
4117  C  C   . TYR A  542 ? 3.2565 3.8138 3.0801 -0.1626 -0.6781 -0.6517 542  TYR A C   
4118  O  O   . TYR A  542 ? 3.2154 3.7649 3.0723 -0.1771 -0.6741 -0.6515 542  TYR A O   
4119  C  CB  . TYR A  542 ? 3.4344 4.0762 3.2541 -0.1685 -0.7212 -0.6323 542  TYR A CB  
4120  C  CG  . TYR A  542 ? 3.5130 4.1394 3.3507 -0.2065 -0.7349 -0.6361 542  TYR A CG  
4121  C  CD1 . TYR A  542 ? 3.5415 4.2243 3.4274 -0.2280 -0.7506 -0.6157 542  TYR A CD1 
4122  C  CD2 . TYR A  542 ? 3.5516 4.1051 3.3524 -0.2214 -0.7339 -0.6600 542  TYR A CD2 
4123  C  CE1 . TYR A  542 ? 3.5483 4.2063 3.4407 -0.2658 -0.7669 -0.6183 542  TYR A CE1 
4124  C  CE2 . TYR A  542 ? 3.6064 4.1348 3.4137 -0.2539 -0.7497 -0.6645 542  TYR A CE2 
4125  C  CZ  . TYR A  542 ? 3.5717 4.1481 3.4225 -0.2772 -0.7672 -0.6432 542  TYR A CZ  
4126  O  OH  . TYR A  542 ? 3.5768 4.1186 3.4252 -0.3126 -0.7866 -0.6465 542  TYR A OH  
4127  N  N   . LEU A  543 ? 3.3501 3.8565 3.1207 -0.1550 -0.6685 -0.6706 543  LEU A N   
4128  C  CA  . LEU A  543 ? 3.4023 3.8475 3.1501 -0.1635 -0.6529 -0.6942 543  LEU A CA  
4129  C  C   . LEU A  543 ? 3.5213 3.9357 3.2471 -0.1862 -0.6702 -0.7096 543  LEU A C   
4130  O  O   . LEU A  543 ? 3.5669 3.9957 3.2756 -0.1926 -0.6906 -0.7062 543  LEU A O   
4131  C  CB  . LEU A  543 ? 3.4245 3.8367 3.1233 -0.1469 -0.6338 -0.7051 543  LEU A CB  
4132  C  CG  . LEU A  543 ? 3.4887 3.8489 3.1559 -0.1531 -0.6158 -0.7301 543  LEU A CG  
4133  C  CD1 . LEU A  543 ? 3.5003 3.8577 3.2045 -0.1525 -0.5978 -0.7336 543  LEU A CD1 
4134  C  CD2 . LEU A  543 ? 3.5553 3.8912 3.1669 -0.1432 -0.6025 -0.7365 543  LEU A CD2 
4135  N  N   . ARG A  544 ? 3.5749 3.9450 3.2968 -0.1957 -0.6625 -0.7278 544  ARG A N   
4136  C  CA  . ARG A  544 ? 3.7038 4.0310 3.3946 -0.2132 -0.6773 -0.7466 544  ARG A CA  
4137  C  C   . ARG A  544 ? 3.6998 3.9946 3.3323 -0.2063 -0.6705 -0.7654 544  ARG A C   
4138  O  O   . ARG A  544 ? 3.6486 3.9414 3.2606 -0.1903 -0.6501 -0.7683 544  ARG A O   
4139  C  CB  . ARG A  544 ? 3.7278 4.0138 3.4255 -0.2191 -0.6724 -0.7619 544  ARG A CB  
4140  C  CG  . ARG A  544 ? 3.6374 3.9382 3.3799 -0.2355 -0.6883 -0.7459 544  ARG A CG  
4141  C  CD  . ARG A  544 ? 3.5970 3.8370 3.3242 -0.2427 -0.6931 -0.7659 544  ARG A CD  
4142  N  NE  . ARG A  544 ? 3.6015 3.8403 3.3578 -0.2647 -0.7145 -0.7516 544  ARG A NE  
4143  C  CZ  . ARG A  544 ? 3.6745 3.9391 3.4752 -0.2625 -0.7071 -0.7358 544  ARG A CZ  
4144  N  NH1 . ARG A  544 ? 3.7047 3.9993 3.5279 -0.2379 -0.6788 -0.7322 544  ARG A NH1 
4145  N  NH2 . ARG A  544 ? 3.6891 3.9476 3.5087 -0.2872 -0.7295 -0.7227 544  ARG A NH2 
4146  N  N   . ASP A  545 ? 3.7425 4.0096 3.3449 -0.2214 -0.6896 -0.7775 545  ASP A N   
4147  C  CA  . ASP A  545 ? 3.6839 3.9170 3.2287 -0.2188 -0.6869 -0.7966 545  ASP A CA  
4148  C  C   . ASP A  545 ? 3.8536 4.0535 3.3726 -0.2074 -0.6596 -0.8185 545  ASP A C   
4149  O  O   . ASP A  545 ? 3.9068 4.0991 3.4484 -0.2030 -0.6474 -0.8247 545  ASP A O   
4150  C  CB  . ASP A  545 ? 3.6528 3.8579 3.1745 -0.2384 -0.7133 -0.8066 545  ASP A CB  
4151  C  CG  . ASP A  545 ? 3.7980 3.9705 3.2602 -0.2364 -0.7126 -0.8252 545  ASP A CG  
4152  O  OD1 . ASP A  545 ? 3.8424 4.0335 3.2871 -0.2353 -0.7226 -0.8163 545  ASP A OD1 
4153  O  OD2 . ASP A  545 ? 3.9074 4.0370 3.3382 -0.2340 -0.7024 -0.8491 545  ASP A OD2 
4154  N  N   . GLU A  546 ? 4.0679 4.2515 3.5370 -0.2028 -0.6507 -0.8299 546  GLU A N   
4155  C  CA  . GLU A  546 ? 4.1335 4.2966 3.5729 -0.1949 -0.6249 -0.8498 546  GLU A CA  
4156  C  C   . GLU A  546 ? 4.1002 4.2298 3.5289 -0.1963 -0.6261 -0.8745 546  GLU A C   
4157  O  O   . GLU A  546 ? 4.0351 4.1632 3.4699 -0.1857 -0.6061 -0.8868 546  GLU A O   
4158  C  CB  . GLU A  546 ? 4.1352 4.2858 3.5167 -0.1955 -0.6200 -0.8556 546  GLU A CB  
4159  C  CG  . GLU A  546 ? 4.0926 4.2329 3.4400 -0.1918 -0.5929 -0.8736 546  GLU A CG  
4160  C  CD  . GLU A  546 ? 4.0424 4.1681 3.3279 -0.1974 -0.5903 -0.8767 546  GLU A CD  
4161  O  OE1 . GLU A  546 ? 3.9843 4.1034 3.2527 -0.2006 -0.6102 -0.8664 546  GLU A OE1 
4162  O  OE2 . GLU A  546 ? 4.0362 4.1591 3.2882 -0.1993 -0.5692 -0.8892 546  GLU A OE2 
4163  N  N   . SER A  547 ? 4.1145 4.2165 3.5242 -0.2076 -0.6507 -0.8824 547  SER A N   
4164  C  CA  . SER A  547 ? 4.1091 4.1685 3.4942 -0.2062 -0.6556 -0.9082 547  SER A CA  
4165  C  C   . SER A  547 ? 4.2247 4.2723 3.6454 -0.2048 -0.6628 -0.9076 547  SER A C   
4166  O  O   . SER A  547 ? 4.3171 4.3247 3.7144 -0.1974 -0.6660 -0.9303 547  SER A O   
4167  C  CB  . SER A  547 ? 3.8571 3.8840 3.2042 -0.2201 -0.6825 -0.9161 547  SER A CB  
4168  O  OG  . SER A  547 ? 3.7472 3.7751 3.0515 -0.2197 -0.6756 -0.9217 547  SER A OG  
4169  N  N   . GLU A  548 ? 4.0377 4.1171 3.5099 -0.2103 -0.6665 -0.8826 548  GLU A N   
4170  C  CA  . GLU A  548 ? 3.8745 3.9422 3.3800 -0.2129 -0.6759 -0.8784 548  GLU A CA  
4171  C  C   . GLU A  548 ? 3.6908 3.7669 3.2158 -0.1919 -0.6486 -0.8858 548  GLU A C   
4172  O  O   . GLU A  548 ? 3.6892 3.7436 3.2304 -0.1894 -0.6552 -0.8890 548  GLU A O   
4173  C  CB  . GLU A  548 ? 3.7495 3.8547 3.3018 -0.2308 -0.6934 -0.8468 548  GLU A CB  
4174  C  CG  . GLU A  548 ? 3.6840 3.7877 3.2211 -0.2538 -0.7239 -0.8383 548  GLU A CG  
4175  C  CD  . GLU A  548 ? 3.5599 3.7089 3.1439 -0.2730 -0.7430 -0.8078 548  GLU A CD  
4176  O  OE1 . GLU A  548 ? 3.5802 3.7334 3.1563 -0.2957 -0.7709 -0.7992 548  GLU A OE1 
4177  O  OE2 . GLU A  548 ? 3.5245 3.7092 3.1529 -0.2661 -0.7305 -0.7919 548  GLU A OE2 
4178  N  N   . PHE A  549 ? 3.6260 3.7317 3.1468 -0.1783 -0.6199 -0.8880 549  PHE A N   
4179  C  CA  . PHE A  549 ? 3.7101 3.8307 3.2479 -0.1595 -0.5931 -0.8952 549  PHE A CA  
4180  C  C   . PHE A  549 ? 3.8171 3.9593 3.3253 -0.1513 -0.5663 -0.9043 549  PHE A C   
4181  O  O   . PHE A  549 ? 3.8058 3.9686 3.3077 -0.1593 -0.5632 -0.8889 549  PHE A O   
4182  C  CB  . PHE A  549 ? 3.6223 3.7763 3.2175 -0.1602 -0.5889 -0.8695 549  PHE A CB  
4183  C  CG  . PHE A  549 ? 3.6668 3.8607 3.2764 -0.1656 -0.5842 -0.8450 549  PHE A CG  
4184  C  CD1 . PHE A  549 ? 3.7916 3.9955 3.4092 -0.1801 -0.6078 -0.8268 549  PHE A CD1 
4185  C  CD2 . PHE A  549 ? 3.6812 3.9024 3.2923 -0.1553 -0.5580 -0.8403 549  PHE A CD2 
4186  C  CE1 . PHE A  549 ? 3.8926 4.1318 3.5177 -0.1788 -0.6055 -0.8061 549  PHE A CE1 
4187  C  CE2 . PHE A  549 ? 3.8040 4.0513 3.4183 -0.1572 -0.5571 -0.8187 549  PHE A CE2 
4188  C  CZ  . PHE A  549 ? 3.9110 4.1667 3.5316 -0.1661 -0.5810 -0.8024 549  PHE A CZ  
4189  N  N   . ARG A  550 ? 3.8572 3.9943 3.3418 -0.1356 -0.5490 -0.9294 550  ARG A N   
4190  C  CA  . ARG A  550 ? 3.8043 3.9692 3.2604 -0.1318 -0.5225 -0.9375 550  ARG A CA  
4191  C  C   . ARG A  550 ? 3.7677 3.9745 3.2562 -0.1279 -0.4985 -0.9223 550  ARG A C   
4192  O  O   . ARG A  550 ? 3.7842 4.0162 3.2493 -0.1315 -0.4782 -0.9224 550  ARG A O   
4193  C  CB  . ARG A  550 ? 3.7169 3.8725 3.1350 -0.1155 -0.5129 -0.9705 550  ARG A CB  
4194  C  CG  . ARG A  550 ? 3.6510 3.7930 3.0876 -0.0937 -0.5143 -0.9859 550  ARG A CG  
4195  C  CD  . ARG A  550 ? 3.5994 3.7359 2.9917 -0.0716 -0.5058 -1.0205 550  ARG A CD  
4196  N  NE  . ARG A  550 ? 3.5383 3.6657 2.9429 -0.0442 -0.5045 -1.0369 550  ARG A NE  
4197  C  CZ  . ARG A  550 ? 3.5761 3.6453 2.9642 -0.0317 -0.5299 -1.0519 550  ARG A CZ  
4198  N  NH1 . ARG A  550 ? 3.6044 3.6228 2.9656 -0.0471 -0.5581 -1.0518 550  ARG A NH1 
4199  N  NH2 . ARG A  550 ? 3.5935 3.6520 2.9874 -0.0040 -0.5288 -1.0671 550  ARG A NH2 
4200  N  N   . ASP A  551 ? 3.7280 3.9409 3.2665 -0.1230 -0.5017 -0.9085 551  ASP A N   
4201  C  CA  . ASP A  551 ? 3.6400 3.8893 3.2122 -0.1175 -0.4803 -0.8947 551  ASP A CA  
4202  C  C   . ASP A  551 ? 3.6657 3.9296 3.2470 -0.1301 -0.4832 -0.8661 551  ASP A C   
4203  O  O   . ASP A  551 ? 3.6943 3.9605 3.3125 -0.1324 -0.4972 -0.8461 551  ASP A O   
4204  C  CB  . ASP A  551 ? 3.5841 3.8296 3.2024 -0.1056 -0.4842 -0.8933 551  ASP A CB  
4205  C  CG  . ASP A  551 ? 3.6522 3.9345 3.3001 -0.0952 -0.4591 -0.8872 551  ASP A CG  
4206  O  OD1 . ASP A  551 ? 3.6359 3.9464 3.2768 -0.1021 -0.4426 -0.8753 551  ASP A OD1 
4207  O  OD2 . ASP A  551 ? 3.7451 4.0244 3.4200 -0.0806 -0.4575 -0.8941 551  ASP A OD2 
4208  N  N   . LYS A  552 ? 3.7393 4.0132 3.2823 -0.1377 -0.4708 -0.8641 552  LYS A N   
4209  C  CA  . LYS A  552 ? 3.7558 4.0354 3.2932 -0.1456 -0.4742 -0.8392 552  LYS A CA  
4210  C  C   . LYS A  552 ? 3.7738 4.0779 3.3152 -0.1449 -0.4515 -0.8285 552  LYS A C   
4211  O  O   . LYS A  552 ? 3.8684 4.1697 3.3866 -0.1514 -0.4523 -0.8112 552  LYS A O   
4212  C  CB  . LYS A  552 ? 3.7536 4.0126 3.2334 -0.1575 -0.4838 -0.8416 552  LYS A CB  
4213  C  CG  . LYS A  552 ? 3.6923 3.9285 3.1681 -0.1606 -0.5107 -0.8442 552  LYS A CG  
4214  C  CD  . LYS A  552 ? 3.6554 3.8720 3.1043 -0.1617 -0.5122 -0.8717 552  LYS A CD  
4215  C  CE  . LYS A  552 ? 3.6764 3.8667 3.1059 -0.1695 -0.5390 -0.8736 552  LYS A CE  
4216  N  NZ  . LYS A  552 ? 3.8336 3.9988 3.2316 -0.1691 -0.5423 -0.9010 552  LYS A NZ  
4217  N  N   . LEU A  553 ? 3.6434 3.9691 3.2103 -0.1363 -0.4331 -0.8387 553  LEU A N   
4218  C  CA  . LEU A  553 ? 3.5651 3.9181 3.1362 -0.1376 -0.4109 -0.8299 553  LEU A CA  
4219  C  C   . LEU A  553 ? 3.5119 3.8792 3.1412 -0.1261 -0.4088 -0.8142 553  LEU A C   
4220  O  O   . LEU A  553 ? 3.4908 3.8730 3.1236 -0.1287 -0.3970 -0.7987 553  LEU A O   
4221  C  CB  . LEU A  553 ? 3.5214 3.9010 3.0757 -0.1362 -0.3884 -0.8529 553  LEU A CB  
4222  C  CG  . LEU A  553 ? 3.4388 3.8156 2.9348 -0.1471 -0.3852 -0.8713 553  LEU A CG  
4223  C  CD1 . LEU A  553 ? 3.5095 3.8627 2.9569 -0.1675 -0.3946 -0.8556 553  LEU A CD1 
4224  C  CD2 . LEU A  553 ? 3.4001 3.7556 2.8935 -0.1352 -0.3988 -0.8944 553  LEU A CD2 
4225  N  N   . THR A  554 ? 3.4268 3.7870 3.0978 -0.1153 -0.4210 -0.8174 554  THR A N   
4226  C  CA  . THR A  554 ? 3.3630 3.7360 3.0897 -0.1052 -0.4201 -0.8036 554  THR A CA  
4227  C  C   . THR A  554 ? 3.4807 3.8541 3.2228 -0.1081 -0.4339 -0.7756 554  THR A C   
4228  O  O   . THR A  554 ? 3.7328 4.0947 3.4810 -0.1110 -0.4559 -0.7699 554  THR A O   
4229  C  CB  . THR A  554 ? 3.3190 3.6773 3.0751 -0.0963 -0.4320 -0.8165 554  THR A CB  
4230  O  OG1 . THR A  554 ? 3.3278 3.6850 3.0634 -0.0870 -0.4203 -0.8448 554  THR A OG1 
4231  C  CG2 . THR A  554 ? 3.2667 3.6372 3.0777 -0.0877 -0.4309 -0.8019 554  THR A CG2 
4232  N  N   . PRO A  555 ? 3.2674 3.6548 3.0108 -0.1068 -0.4230 -0.7581 555  PRO A N   
4233  C  CA  . PRO A  555 ? 3.2027 3.5912 2.9546 -0.1034 -0.4371 -0.7327 555  PRO A CA  
4234  C  C   . PRO A  555 ? 3.1200 3.5203 2.9266 -0.0968 -0.4527 -0.7224 555  PRO A C   
4235  O  O   . PRO A  555 ? 3.1129 3.5219 2.9610 -0.0924 -0.4470 -0.7261 555  PRO A O   
4236  C  CB  . PRO A  555 ? 3.1552 3.5541 2.9052 -0.1002 -0.4206 -0.7191 555  PRO A CB  
4237  C  CG  . PRO A  555 ? 3.1429 3.5578 2.9129 -0.0995 -0.3992 -0.7342 555  PRO A CG  
4238  C  CD  . PRO A  555 ? 3.1567 3.5632 2.9015 -0.1055 -0.3985 -0.7600 555  PRO A CD  
4239  N  N   . ILE A  556 ? 3.1035 3.5065 2.9077 -0.0967 -0.4736 -0.7086 556  ILE A N   
4240  C  CA  . ILE A  556 ? 3.0885 3.5102 2.9395 -0.0964 -0.4915 -0.6972 556  ILE A CA  
4241  C  C   . ILE A  556 ? 3.1384 3.5893 3.0241 -0.0835 -0.4891 -0.6732 556  ILE A C   
4242  O  O   . ILE A  556 ? 3.2068 3.6672 3.0745 -0.0739 -0.4958 -0.6580 556  ILE A O   
4243  C  CB  . ILE A  556 ? 3.1165 3.5373 2.9488 -0.1034 -0.5157 -0.6949 556  ILE A CB  
4244  C  CG1 . ILE A  556 ? 3.2786 3.6666 3.0719 -0.1152 -0.5178 -0.7194 556  ILE A CG1 
4245  C  CG2 . ILE A  556 ? 3.0915 3.5402 2.9725 -0.1083 -0.5347 -0.6807 556  ILE A CG2 
4246  C  CD1 . ILE A  556 ? 3.4029 3.7876 3.1766 -0.1240 -0.5423 -0.7187 556  ILE A CD1 
4247  N  N   . THR A  557 ? 3.1414 3.6042 3.0733 -0.0809 -0.4802 -0.6706 557  THR A N   
4248  C  CA  . THR A  557 ? 3.0595 3.5508 3.0281 -0.0686 -0.4768 -0.6487 557  THR A CA  
4249  C  C   . THR A  557 ? 2.9823 3.5057 2.9903 -0.0716 -0.4978 -0.6322 557  THR A C   
4250  O  O   . THR A  557 ? 2.9034 3.4240 2.9359 -0.0854 -0.5070 -0.6376 557  THR A O   
4251  C  CB  . THR A  557 ? 3.0066 3.4967 3.0048 -0.0649 -0.4569 -0.6535 557  THR A CB  
4252  O  OG1 . THR A  557 ? 3.0480 3.5210 3.0096 -0.0637 -0.4371 -0.6656 557  THR A OG1 
4253  C  CG2 . THR A  557 ? 3.0022 3.5218 3.0415 -0.0529 -0.4548 -0.6306 557  THR A CG2 
4254  N  N   . ILE A  558 ? 3.1108 3.6649 3.1204 -0.0589 -0.5068 -0.6120 558  ILE A N   
4255  C  CA  . ILE A  558 ? 3.0713 3.6730 3.1215 -0.0602 -0.5250 -0.5929 558  ILE A CA  
4256  C  C   . ILE A  558 ? 3.1619 3.7882 3.2606 -0.0524 -0.5151 -0.5784 558  ILE A C   
4257  O  O   . ILE A  558 ? 3.1984 3.8292 3.2925 -0.0326 -0.5033 -0.5695 558  ILE A O   
4258  C  CB  . ILE A  558 ? 2.9487 3.5803 2.9761 -0.0447 -0.5401 -0.5793 558  ILE A CB  
4259  C  CG1 . ILE A  558 ? 2.9652 3.5746 2.9467 -0.0538 -0.5529 -0.5927 558  ILE A CG1 
4260  C  CG2 . ILE A  558 ? 2.8562 3.5538 2.9309 -0.0429 -0.5557 -0.5569 558  ILE A CG2 
4261  C  CD1 . ILE A  558 ? 2.9855 3.5449 2.9055 -0.0470 -0.5415 -0.6068 558  ILE A CD1 
4262  N  N   . PHE A  559 ? 3.1779 3.8160 3.3186 -0.0688 -0.5215 -0.5754 559  PHE A N   
4263  C  CA  . PHE A  559 ? 3.1472 3.8050 3.3342 -0.0645 -0.5130 -0.5626 559  PHE A CA  
4264  C  C   . PHE A  559 ? 3.0342 3.7546 3.2588 -0.0677 -0.5303 -0.5375 559  PHE A C   
4265  O  O   . PHE A  559 ? 3.2141 3.9523 3.4448 -0.0888 -0.5505 -0.5341 559  PHE A O   
4266  C  CB  . PHE A  559 ? 3.1578 3.7788 3.3600 -0.0799 -0.5080 -0.5774 559  PHE A CB  
4267  C  CG  . PHE A  559 ? 3.0500 3.6873 3.2982 -0.0773 -0.5014 -0.5645 559  PHE A CG  
4268  C  CD1 . PHE A  559 ? 2.9901 3.6243 3.2452 -0.0576 -0.4795 -0.5637 559  PHE A CD1 
4269  C  CD2 . PHE A  559 ? 3.0140 3.6691 3.2958 -0.0970 -0.5183 -0.5523 559  PHE A CD2 
4270  C  CE1 . PHE A  559 ? 2.9597 3.6082 3.2566 -0.0544 -0.4735 -0.5520 559  PHE A CE1 
4271  C  CE2 . PHE A  559 ? 3.0050 3.6732 3.3265 -0.0956 -0.5128 -0.5400 559  PHE A CE2 
4272  C  CZ  . PHE A  559 ? 3.0208 3.6860 3.3510 -0.0726 -0.4899 -0.5403 559  PHE A CZ  
4273  N  N   . MET A  560 ? 2.8423 3.5990 3.0904 -0.0475 -0.5229 -0.5195 560  MET A N   
4274  C  CA  . MET A  560 ? 2.8508 3.6784 3.1373 -0.0468 -0.5366 -0.4945 560  MET A CA  
4275  C  C   . MET A  560 ? 2.9638 3.8035 3.2961 -0.0482 -0.5269 -0.4832 560  MET A C   
4276  O  O   . MET A  560 ? 3.0850 3.9060 3.4169 -0.0279 -0.5082 -0.4844 560  MET A O   
4277  C  CB  . MET A  560 ? 2.8342 3.7022 3.1023 -0.0148 -0.5397 -0.4819 560  MET A CB  
4278  C  CG  . MET A  560 ? 2.8193 3.7706 3.1291 -0.0068 -0.5501 -0.4560 560  MET A CG  
4279  S  SD  . MET A  560 ? 2.9008 3.8931 3.1806 0.0413  -0.5541 -0.4442 560  MET A SD  
4280  C  CE  . MET A  560 ? 2.8212 3.9144 3.1615 0.0491  -0.5603 -0.4151 560  MET A CE  
4281  N  N   . GLU A  561 ? 2.9377 3.8080 3.3062 -0.0740 -0.5410 -0.4712 561  GLU A N   
4282  C  CA  . GLU A  561 ? 2.8923 3.7739 3.3033 -0.0802 -0.5355 -0.4591 561  GLU A CA  
4283  C  C   . GLU A  561 ? 2.8730 3.8420 3.3212 -0.0854 -0.5498 -0.4305 561  GLU A C   
4284  O  O   . GLU A  561 ? 3.0340 4.0464 3.4808 -0.1020 -0.5697 -0.4223 561  GLU A O   
4285  C  CB  . GLU A  561 ? 2.8707 3.6970 3.2841 -0.1109 -0.5409 -0.4721 561  GLU A CB  
4286  C  CG  . GLU A  561 ? 2.8387 3.6672 3.2904 -0.1203 -0.5384 -0.4606 561  GLU A CG  
4287  C  CD  . GLU A  561 ? 2.9113 3.6783 3.3544 -0.1497 -0.5499 -0.4737 561  GLU A CD  
4288  O  OE1 . GLU A  561 ? 2.9034 3.6354 3.3140 -0.1654 -0.5628 -0.4886 561  GLU A OE1 
4289  O  OE2 . GLU A  561 ? 2.9697 3.7194 3.4343 -0.1555 -0.5474 -0.4694 561  GLU A OE2 
4290  N  N   . TYR A  562 ? 2.7410 3.7414 3.2222 -0.0709 -0.5397 -0.4148 562  TYR A N   
4291  C  CA  . TYR A  562 ? 2.7230 3.8154 3.2411 -0.0733 -0.5512 -0.3869 562  TYR A CA  
4292  C  C   . TYR A  562 ? 2.7154 3.8142 3.2742 -0.0838 -0.5450 -0.3739 562  TYR A C   
4293  O  O   . TYR A  562 ? 2.7244 3.7705 3.2835 -0.0699 -0.5265 -0.3838 562  TYR A O   
4294  C  CB  . TYR A  562 ? 2.6783 3.8258 3.1867 -0.0301 -0.5474 -0.3772 562  TYR A CB  
4295  C  CG  . TYR A  562 ? 2.7336 3.8397 3.2270 0.0072  -0.5255 -0.3840 562  TYR A CG  
4296  C  CD1 . TYR A  562 ? 2.7920 3.9253 3.3170 0.0229  -0.5153 -0.3689 562  TYR A CD1 
4297  C  CD2 . TYR A  562 ? 2.7928 3.8331 3.2376 0.0241  -0.5161 -0.4044 562  TYR A CD2 
4298  C  CE1 . TYR A  562 ? 2.8373 3.9306 3.3454 0.0546  -0.4970 -0.3743 562  TYR A CE1 
4299  C  CE2 . TYR A  562 ? 2.8437 3.8456 3.2701 0.0527  -0.4982 -0.4089 562  TYR A CE2 
4300  C  CZ  . TYR A  562 ? 2.8516 3.8790 3.3095 0.0680  -0.4891 -0.3938 562  TYR A CZ  
4301  O  OH  . TYR A  562 ? 2.8305 3.8174 3.2672 0.0943  -0.4729 -0.3975 562  TYR A OH  
4302  N  N   . ARG A  563 ? 2.9029 4.0708 3.4948 -0.1099 -0.5613 -0.3507 563  ARG A N   
4303  C  CA  . ARG A  563 ? 2.9437 4.1247 3.5734 -0.1258 -0.5594 -0.3350 563  ARG A CA  
4304  C  C   . ARG A  563 ? 2.8931 4.1902 3.5579 -0.1317 -0.5715 -0.3040 563  ARG A C   
4305  O  O   . ARG A  563 ? 2.8846 4.2511 3.5442 -0.1252 -0.5827 -0.2962 563  ARG A O   
4306  C  CB  . ARG A  563 ? 3.1062 4.2211 3.7318 -0.1710 -0.5715 -0.3423 563  ARG A CB  
4307  C  CG  . ARG A  563 ? 3.2492 4.2552 3.8401 -0.1647 -0.5609 -0.3741 563  ARG A CG  
4308  C  CD  . ARG A  563 ? 3.4495 4.3902 4.0315 -0.2044 -0.5764 -0.3806 563  ARG A CD  
4309  N  NE  . ARG A  563 ? 3.5103 4.3548 4.0647 -0.1907 -0.5636 -0.4104 563  ARG A NE  
4310  C  CZ  . ARG A  563 ? 3.5229 4.2931 4.0576 -0.2139 -0.5757 -0.4232 563  ARG A CZ  
4311  N  NH1 . ARG A  563 ? 3.6463 4.4184 4.1821 -0.2566 -0.6025 -0.4076 563  ARG A NH1 
4312  N  NH2 . ARG A  563 ? 3.3909 4.0854 3.9006 -0.1944 -0.5625 -0.4515 563  ARG A NH2 
4313  N  N   . LEU A  564 ? 2.8080 4.1292 3.5078 -0.1430 -0.5689 -0.2866 564  LEU A N   
4314  C  CA  . LEU A  564 ? 2.7446 4.1803 3.4817 -0.1511 -0.5783 -0.2556 564  LEU A CA  
4315  C  C   . LEU A  564 ? 2.9199 4.3610 3.6738 -0.2124 -0.5983 -0.2400 564  LEU A C   
4316  O  O   . LEU A  564 ? 2.9603 4.3064 3.6999 -0.2384 -0.6007 -0.2528 564  LEU A O   
4317  C  CB  . LEU A  564 ? 2.5140 3.9792 3.2752 -0.1109 -0.5588 -0.2456 564  LEU A CB  
4318  C  CG  . LEU A  564 ? 2.4391 4.0304 3.2391 -0.1086 -0.5646 -0.2143 564  LEU A CG  
4319  C  CD1 . LEU A  564 ? 2.4934 4.1826 3.2873 -0.0953 -0.5779 -0.2059 564  LEU A CD1 
4320  C  CD2 . LEU A  564 ? 2.5223 4.1251 3.3374 -0.0625 -0.5442 -0.2091 564  LEU A CD2 
4321  N  N   . ASP A  565 ? 3.0030 4.5581 3.7836 -0.2351 -0.6140 -0.2116 565  ASP A N   
4322  C  CA  . ASP A  565 ? 2.9195 4.4935 3.7150 -0.2979 -0.6353 -0.1906 565  ASP A CA  
4323  C  C   . ASP A  565 ? 2.7632 4.3333 3.5869 -0.3036 -0.6266 -0.1763 565  ASP A C   
4324  O  O   . ASP A  565 ? 2.7088 4.2370 3.5298 -0.3541 -0.6420 -0.1681 565  ASP A O   
4325  C  CB  . ASP A  565 ? 2.8662 4.5778 3.6805 -0.3220 -0.6549 -0.1637 565  ASP A CB  
4326  C  CG  . ASP A  565 ? 2.8866 4.6063 3.7004 -0.3987 -0.6836 -0.1444 565  ASP A CG  
4327  O  OD1 . ASP A  565 ? 2.9244 4.6018 3.7076 -0.4327 -0.7029 -0.1533 565  ASP A OD1 
4328  O  OD2 . ASP A  565 ? 2.9133 4.6798 3.7540 -0.4267 -0.6883 -0.1196 565  ASP A OD2 
4329  N  N   . TYR A  566 ? 2.5489 4.1559 3.3948 -0.2533 -0.6043 -0.1730 566  TYR A N   
4330  C  CA  . TYR A  566 ? 2.4908 4.1132 3.3674 -0.2539 -0.5953 -0.1565 566  TYR A CA  
4331  C  C   . TYR A  566 ? 2.4696 4.1869 3.3743 -0.3060 -0.6152 -0.1221 566  TYR A C   
4332  O  O   . TYR A  566 ? 2.4995 4.3079 3.4378 -0.2907 -0.6078 -0.1004 566  TYR A O   
4333  C  CB  . TYR A  566 ? 2.5538 4.0429 3.4156 -0.2621 -0.5876 -0.1751 566  TYR A CB  
4334  C  CG  . TYR A  566 ? 2.6804 4.0764 3.5186 -0.2144 -0.5652 -0.2071 566  TYR A CG  
4335  C  CD1 . TYR A  566 ? 2.6879 4.1174 3.5237 -0.1599 -0.5481 -0.2139 566  TYR A CD1 
4336  C  CD2 . TYR A  566 ? 2.7035 3.9786 3.5184 -0.2238 -0.5623 -0.2299 566  TYR A CD2 
4337  C  CE1 . TYR A  566 ? 2.6030 3.9485 3.4138 -0.1226 -0.5289 -0.2409 566  TYR A CE1 
4338  C  CE2 . TYR A  566 ? 2.5889 3.7902 3.3836 -0.1833 -0.5414 -0.2578 566  TYR A CE2 
4339  C  CZ  . TYR A  566 ? 2.4968 3.7342 3.2898 -0.1360 -0.5247 -0.2622 566  TYR A CZ  
4340  O  OH  . TYR A  566 ? 2.4469 3.6130 3.2163 -0.1018 -0.5054 -0.2877 566  TYR A OH  
4341  N  N   . ARG A  567 ? 2.4535 4.1498 3.3416 -0.3689 -0.6414 -0.1159 567  ARG A N   
4342  C  CA  . ARG A  567 ? 2.3807 4.1597 3.2895 -0.4279 -0.6628 -0.0815 567  ARG A CA  
4343  C  C   . ARG A  567 ? 2.2093 4.1615 3.1506 -0.4173 -0.6651 -0.0560 567  ARG A C   
4344  O  O   . ARG A  567 ? 2.1462 4.1960 3.1206 -0.4316 -0.6665 -0.0273 567  ARG A O   
4345  C  CB  . ARG A  567 ? 2.5419 4.2575 3.4163 -0.4982 -0.6937 -0.0807 567  ARG A CB  
4346  C  CG  . ARG A  567 ? 2.6920 4.2382 3.5291 -0.5076 -0.6950 -0.1059 567  ARG A CG  
4347  C  CD  . ARG A  567 ? 2.8273 4.3148 3.6272 -0.5829 -0.7307 -0.0981 567  ARG A CD  
4348  N  NE  . ARG A  567 ? 2.8940 4.2158 3.6496 -0.5849 -0.7344 -0.1259 567  ARG A NE  
4349  C  CZ  . ARG A  567 ? 2.8498 4.0840 3.5613 -0.6431 -0.7658 -0.1239 567  ARG A CZ  
4350  N  NH1 . ARG A  567 ? 2.6894 3.9854 3.3958 -0.7105 -0.7965 -0.0933 567  ARG A NH1 
4351  N  NH2 . ARG A  567 ? 2.8997 3.9852 3.5684 -0.6339 -0.7679 -0.1523 567  ARG A NH2 
4352  N  N   . THR A  568 ? 2.2734 4.2692 3.2042 -0.3909 -0.6663 -0.0662 568  THR A N   
4353  C  CA  . THR A  568 ? 2.2498 4.4115 3.2067 -0.3710 -0.6688 -0.0457 568  THR A CA  
4354  C  C   . THR A  568 ? 2.2136 4.4197 3.1860 -0.2907 -0.6429 -0.0510 568  THR A C   
4355  O  O   . THR A  568 ? 2.1794 4.5240 3.1708 -0.2625 -0.6438 -0.0358 568  THR A O   
4356  C  CB  . THR A  568 ? 2.3147 4.5054 3.2495 -0.3761 -0.6839 -0.0542 568  THR A CB  
4357  O  OG1 . THR A  568 ? 2.4565 4.8229 3.4180 -0.3713 -0.6926 -0.0295 568  THR A OG1 
4358  C  CG2 . THR A  568 ? 2.2273 4.3378 3.1332 -0.3111 -0.6660 -0.0882 568  THR A CG2 
4359  N  N   . ALA A  569 ? 2.2645 4.3576 3.2256 -0.2522 -0.6214 -0.0725 569  ALA A N   
4360  C  CA  . ALA A  569 ? 2.3507 4.4693 3.3205 -0.1801 -0.5986 -0.0767 569  ALA A CA  
4361  C  C   . ALA A  569 ? 2.4774 4.5874 3.4744 -0.1811 -0.5863 -0.0638 569  ALA A C   
4362  O  O   . ALA A  569 ? 2.4766 4.5859 3.4777 -0.1239 -0.5669 -0.0684 569  ALA A O   
4363  C  CB  . ALA A  569 ? 2.3543 4.3575 3.2862 -0.1312 -0.5831 -0.1108 569  ALA A CB  
4364  N  N   . ALA A  570 ? 2.5641 4.6620 3.5748 -0.2454 -0.5989 -0.0475 570  ALA A N   
4365  C  CA  . ALA A  570 ? 2.4491 4.5392 3.4843 -0.2524 -0.5898 -0.0336 570  ALA A CA  
4366  C  C   . ALA A  570 ? 2.3052 4.5587 3.3780 -0.2403 -0.5895 -0.0025 570  ALA A C   
4367  O  O   . ALA A  570 ? 2.3127 4.6906 3.3936 -0.2361 -0.5996 0.0102  570  ALA A O   
4368  C  CB  . ALA A  570 ? 2.4898 4.5048 3.5179 -0.3265 -0.6071 -0.0267 570  ALA A CB  
4369  N  N   . ASP A  571 ? 2.1511 4.4081 3.2467 -0.2323 -0.5775 0.0093  571  ASP A N   
4370  C  CA  . ASP A  571 ? 2.1450 4.5539 3.2758 -0.2165 -0.5750 0.0379  571  ASP A CA  
4371  C  C   . ASP A  571 ? 2.0575 4.5280 3.2109 -0.2942 -0.5931 0.0703  571  ASP A C   
4372  O  O   . ASP A  571 ? 2.0883 4.4728 3.2251 -0.3582 -0.6091 0.0699  571  ASP A O   
4373  C  CB  . ASP A  571 ? 2.1418 4.5233 3.2809 -0.1528 -0.5501 0.0311  571  ASP A CB  
4374  C  CG  . ASP A  571 ? 2.1654 4.7019 3.3279 -0.1049 -0.5445 0.0502  571  ASP A CG  
4375  O  OD1 . ASP A  571 ? 1.9949 4.6417 3.1567 -0.0923 -0.5547 0.0563  571  ASP A OD1 
4376  O  OD2 . ASP A  571 ? 2.1503 4.6986 3.3300 -0.0771 -0.5303 0.0583  571  ASP A OD2 
4377  N  N   . THR A  572 ? 1.9293 4.5512 3.1168 -0.2882 -0.5921 0.0993  572  THR A N   
4378  C  CA  . THR A  572 ? 1.9056 4.5978 3.1144 -0.3626 -0.6086 0.1336  572  THR A CA  
4379  C  C   . THR A  572 ? 1.9963 4.5560 3.1989 -0.3932 -0.6054 0.1315  572  THR A C   
4380  O  O   . THR A  572 ? 2.0572 4.6070 3.2570 -0.4697 -0.6253 0.1520  572  THR A O   
4381  C  CB  . THR A  572 ? 1.8526 4.7355 3.0997 -0.3400 -0.6039 0.1630  572  THR A CB  
4382  O  OG1 . THR A  572 ? 1.7596 4.7104 3.0257 -0.4173 -0.6199 0.1980  572  THR A OG1 
4383  C  CG2 . THR A  572 ? 1.8430 4.7112 3.1007 -0.2607 -0.5769 0.1531  572  THR A CG2 
4384  N  N   . THR A  573 ? 1.8499 4.3063 3.0467 -0.3353 -0.5823 0.1075  573  THR A N   
4385  C  CA  . THR A  573 ? 1.7276 4.0525 2.9168 -0.3533 -0.5772 0.1009  573  THR A CA  
4386  C  C   . THR A  573 ? 1.9498 4.1045 3.0993 -0.3730 -0.5837 0.0714  573  THR A C   
4387  O  O   . THR A  573 ? 2.2916 4.3266 3.4295 -0.3812 -0.5797 0.0609  573  THR A O   
4388  C  CB  . THR A  573 ? 1.6227 3.9295 2.8263 -0.2813 -0.5490 0.0911  573  THR A CB  
4389  O  OG1 . THR A  573 ? 1.6330 3.8800 2.8165 -0.2169 -0.5337 0.0596  573  THR A OG1 
4390  C  CG2 . THR A  573 ? 1.5184 3.9918 2.7577 -0.2564 -0.5429 0.1191  573  THR A CG2 
4391  N  N   . GLY A  574 ? 1.8261 3.9687 2.9532 -0.3787 -0.5940 0.0572  574  GLY A N   
4392  C  CA  . GLY A  574 ? 1.8328 3.8205 2.9202 -0.3958 -0.6008 0.0288  574  GLY A CA  
4393  C  C   . GLY A  574 ? 1.8283 3.7104 2.9010 -0.3304 -0.5763 -0.0067 574  GLY A C   
4394  O  O   . GLY A  574 ? 1.9089 3.6553 2.9518 -0.3398 -0.5779 -0.0306 574  GLY A O   
4395  N  N   . LEU A  575 ? 1.7476 3.6883 2.8368 -0.2642 -0.5548 -0.0105 575  LEU A N   
4396  C  CA  . LEU A  575 ? 1.7672 3.6155 2.8405 -0.2037 -0.5318 -0.0409 575  LEU A CA  
4397  C  C   . LEU A  575 ? 1.9104 3.7363 2.9549 -0.1843 -0.5337 -0.0632 575  LEU A C   
4398  O  O   . LEU A  575 ? 1.9892 3.9114 3.0373 -0.1570 -0.5346 -0.0570 575  LEU A O   
4399  C  CB  . LEU A  575 ? 1.7178 3.6299 2.8135 -0.1440 -0.5112 -0.0333 575  LEU A CB  
4400  C  CG  . LEU A  575 ? 1.7327 3.5377 2.8153 -0.0958 -0.4883 -0.0578 575  LEU A CG  
4401  C  CD1 . LEU A  575 ? 2.0192 3.7143 3.0983 -0.1314 -0.4892 -0.0653 575  LEU A CD1 
4402  C  CD2 . LEU A  575 ? 1.6759 3.5482 2.7787 -0.0438 -0.4723 -0.0456 575  LEU A CD2 
4403  N  N   . GLN A  576 ? 1.9779 3.6781 2.9915 -0.1962 -0.5348 -0.0896 576  GLN A N   
4404  C  CA  . GLN A  576 ? 2.0098 3.6805 2.9931 -0.1824 -0.5373 -0.1115 576  GLN A CA  
4405  C  C   . GLN A  576 ? 2.0022 3.6332 2.9712 -0.1159 -0.5137 -0.1334 576  GLN A C   
4406  O  O   . GLN A  576 ? 2.0061 3.5623 2.9741 -0.0956 -0.4972 -0.1452 576  GLN A O   
4407  C  CB  . GLN A  576 ? 2.0814 3.6395 3.0337 -0.2240 -0.5503 -0.1303 576  GLN A CB  
4408  C  CG  . GLN A  576 ? 2.2370 3.7969 3.1919 -0.2932 -0.5753 -0.1107 576  GLN A CG  
4409  C  CD  . GLN A  576 ? 2.4153 3.8485 3.3301 -0.3269 -0.5896 -0.1325 576  GLN A CD  
4410  O  OE1 . GLN A  576 ? 2.3941 3.7412 3.2841 -0.2965 -0.5777 -0.1630 576  GLN A OE1 
4411  N  NE2 . GLN A  576 ? 2.6096 4.0311 3.5135 -0.3903 -0.6166 -0.1167 576  GLN A NE2 
4412  N  N   . PRO A  577 ? 2.1470 3.8248 3.1011 -0.0823 -0.5132 -0.1388 577  PRO A N   
4413  C  CA  . PRO A  577 ? 2.1692 3.8018 3.0996 -0.0227 -0.4943 -0.1585 577  PRO A CA  
4414  C  C   . PRO A  577 ? 2.3061 3.8074 3.2055 -0.0243 -0.4855 -0.1889 577  PRO A C   
4415  O  O   . PRO A  577 ? 2.4501 3.8919 3.3447 -0.0670 -0.4944 -0.1968 577  PRO A O   
4416  C  CB  . PRO A  577 ? 2.0940 3.8033 3.0083 0.0032  -0.5028 -0.1567 577  PRO A CB  
4417  C  CG  . PRO A  577 ? 2.1756 4.0056 3.1202 -0.0314 -0.5211 -0.1291 577  PRO A CG  
4418  C  CD  . PRO A  577 ? 2.2512 4.0323 3.2079 -0.0968 -0.5313 -0.1248 577  PRO A CD  
4419  N  N   . ILE A  578 ? 2.2472 3.7030 3.1211 0.0221  -0.4695 -0.2058 578  ILE A N   
4420  C  CA  . ILE A  578 ? 2.2416 3.5849 3.0858 0.0237  -0.4590 -0.2341 578  ILE A CA  
4421  C  C   . ILE A  578 ? 2.2572 3.5816 3.0631 0.0677  -0.4505 -0.2481 578  ILE A C   
4422  O  O   . ILE A  578 ? 2.2567 3.6292 3.0589 0.1071  -0.4470 -0.2375 578  ILE A O   
4423  C  CB  . ILE A  578 ? 2.0992 3.3800 2.9580 0.0236  -0.4441 -0.2388 578  ILE A CB  
4424  C  CG1 . ILE A  578 ? 2.1580 3.3336 2.9885 0.0184  -0.4359 -0.2683 578  ILE A CG1 
4425  C  CG2 . ILE A  578 ? 1.9849 3.2880 2.8506 0.0687  -0.4285 -0.2302 578  ILE A CG2 
4426  C  CD1 . ILE A  578 ? 2.1393 3.2819 2.9567 -0.0230 -0.4524 -0.2791 578  ILE A CD1 
4427  N  N   . LEU A  579 ? 2.2395 3.4906 3.0115 0.0609  -0.4488 -0.2721 579  LEU A N   
4428  C  CA  . LEU A  579 ? 2.1638 3.3841 2.8913 0.0949  -0.4427 -0.2866 579  LEU A CA  
4429  C  C   . LEU A  579 ? 2.0831 3.2486 2.7968 0.1246  -0.4232 -0.2940 579  LEU A C   
4430  O  O   . LEU A  579 ? 2.0472 3.1743 2.7810 0.1137  -0.4121 -0.2975 579  LEU A O   
4431  C  CB  . LEU A  579 ? 2.1478 3.3107 2.8436 0.0736  -0.4473 -0.3092 579  LEU A CB  
4432  C  CG  . LEU A  579 ? 2.1414 3.3485 2.8386 0.0457  -0.4681 -0.3050 579  LEU A CG  
4433  C  CD1 . LEU A  579 ? 2.1834 3.3198 2.8484 0.0250  -0.4706 -0.3296 579  LEU A CD1 
4434  C  CD2 . LEU A  579 ? 2.1572 3.4396 2.8420 0.0743  -0.4779 -0.2929 579  LEU A CD2 
4435  N  N   . ASN A  580 ? 2.0678 3.2298 2.7434 0.1626  -0.4210 -0.2956 580  ASN A N   
4436  C  CA  . ASN A  580 ? 2.0797 3.1815 2.7307 0.1867  -0.4050 -0.3033 580  ASN A CA  
4437  C  C   . ASN A  580 ? 2.1626 3.1853 2.7967 0.1636  -0.3948 -0.3271 580  ASN A C   
4438  O  O   . ASN A  580 ? 2.2331 3.2382 2.8501 0.1438  -0.4015 -0.3406 580  ASN A O   
4439  C  CB  . ASN A  580 ? 2.0971 3.1975 2.6966 0.2283  -0.4095 -0.3015 580  ASN A CB  
4440  C  CG  . ASN A  580 ? 2.1004 3.1401 2.6702 0.2511  -0.3959 -0.3053 580  ASN A CG  
4441  O  OD1 . ASN A  580 ? 2.1768 3.1500 2.7014 0.2492  -0.3909 -0.3210 580  ASN A OD1 
4442  N  ND2 . ASN A  580 ? 2.0527 3.1168 2.6470 0.2699  -0.3905 -0.2902 580  ASN A ND2 
4443  N  N   . GLN A  581 ? 2.1191 3.0973 2.7558 0.1682  -0.3786 -0.3325 581  GLN A N   
4444  C  CA  . GLN A  581 ? 2.1476 3.0694 2.7855 0.1441  -0.3681 -0.3529 581  GLN A CA  
4445  C  C   . GLN A  581 ? 2.0557 2.9253 2.6417 0.1444  -0.3631 -0.3730 581  GLN A C   
4446  O  O   . GLN A  581 ? 2.0830 2.9231 2.6634 0.1222  -0.3618 -0.3915 581  GLN A O   
4447  C  CB  . GLN A  581 ? 2.2862 3.1909 2.9508 0.1488  -0.3532 -0.3503 581  GLN A CB  
4448  C  CG  . GLN A  581 ? 2.2235 3.1214 2.8682 0.1804  -0.3446 -0.3410 581  GLN A CG  
4449  C  CD  . GLN A  581 ? 2.1070 2.9586 2.7514 0.1799  -0.3266 -0.3511 581  GLN A CD  
4450  O  OE1 . GLN A  581 ? 2.2632 3.0847 2.9125 0.1602  -0.3195 -0.3692 581  GLN A OE1 
4451  N  NE2 . GLN A  581 ? 1.9641 2.8134 2.6033 0.2030  -0.3201 -0.3393 581  GLN A NE2 
4452  N  N   . PHE A  582 ? 2.2360 3.0897 2.7791 0.1685  -0.3611 -0.3702 582  PHE A N   
4453  C  CA  . PHE A  582 ? 2.3534 3.1567 2.8437 0.1631  -0.3572 -0.3880 582  PHE A CA  
4454  C  C   . PHE A  582 ? 2.5871 3.3974 3.0456 0.1598  -0.3725 -0.3928 582  PHE A C   
4455  O  O   . PHE A  582 ? 2.7265 3.4968 3.1429 0.1502  -0.3704 -0.4086 582  PHE A O   
4456  C  CB  . PHE A  582 ? 2.3806 3.1480 2.8285 0.1827  -0.3495 -0.3847 582  PHE A CB  
4457  C  CG  . PHE A  582 ? 2.4758 3.2059 2.9245 0.1681  -0.3311 -0.3977 582  PHE A CG  
4458  C  CD1 . PHE A  582 ? 2.4868 3.2289 2.9870 0.1639  -0.3202 -0.3961 582  PHE A CD1 
4459  C  CD2 . PHE A  582 ? 2.5088 3.1965 2.9068 0.1573  -0.3253 -0.4118 582  PHE A CD2 
4460  C  CE1 . PHE A  582 ? 2.4653 3.1809 2.9677 0.1533  -0.3036 -0.4091 582  PHE A CE1 
4461  C  CE2 . PHE A  582 ? 2.4584 3.1252 2.8598 0.1434  -0.3079 -0.4237 582  PHE A CE2 
4462  C  CZ  . PHE A  582 ? 2.4117 3.0942 2.8661 0.1433  -0.2970 -0.4229 582  PHE A CZ  
4463  N  N   . THR A  583 ? 2.5319 3.3961 3.0076 0.1677  -0.3881 -0.3790 583  THR A N   
4464  C  CA  . THR A  583 ? 2.5825 3.4569 3.0268 0.1667  -0.4035 -0.3832 583  THR A CA  
4465  C  C   . THR A  583 ? 2.4317 3.3560 2.9151 0.1447  -0.4163 -0.3798 583  THR A C   
4466  O  O   . THR A  583 ? 2.4473 3.4176 2.9233 0.1549  -0.4320 -0.3707 583  THR A O   
4467  C  CB  . THR A  583 ? 2.6512 3.5448 3.0577 0.2040  -0.4151 -0.3701 583  THR A CB  
4468  O  OG1 . THR A  583 ? 2.6564 3.6223 3.1054 0.2195  -0.4220 -0.3498 583  THR A OG1 
4469  C  CG2 . THR A  583 ? 2.6430 3.4813 3.0033 0.2246  -0.4065 -0.3705 583  THR A CG2 
4470  N  N   . PRO A  584 ? 2.2737 3.1903 2.7946 0.1145  -0.4123 -0.3865 584  PRO A N   
4471  C  CA  . PRO A  584 ? 2.3521 3.3078 2.8999 0.0889  -0.4282 -0.3822 584  PRO A CA  
4472  C  C   . PRO A  584 ? 2.4766 3.4008 2.9950 0.0681  -0.4359 -0.4010 584  PRO A C   
4473  O  O   . PRO A  584 ? 2.5982 3.5576 3.1238 0.0518  -0.4528 -0.3962 584  PRO A O   
4474  C  CB  . PRO A  584 ? 2.3122 3.2627 2.9052 0.0681  -0.4230 -0.3797 584  PRO A CB  
4475  C  CG  . PRO A  584 ? 2.2727 3.1593 2.8499 0.0732  -0.4042 -0.3976 584  PRO A CG  
4476  C  CD  . PRO A  584 ? 2.2177 3.0970 2.7604 0.1045  -0.3960 -0.3947 584  PRO A CD  
4477  N  N   . ALA A  585 ? 2.2332 3.0952 2.7185 0.0671  -0.4238 -0.4220 585  ALA A N   
4478  C  CA  . ALA A  585 ? 2.2801 3.1058 2.7424 0.0450  -0.4280 -0.4427 585  ALA A CA  
4479  C  C   . ALA A  585 ? 2.5477 3.3917 2.9801 0.0441  -0.4445 -0.4428 585  ALA A C   
4480  O  O   . ALA A  585 ? 2.6365 3.5073 3.0489 0.0671  -0.4502 -0.4320 585  ALA A O   
4481  C  CB  . ALA A  585 ? 2.2807 3.0486 2.7103 0.0485  -0.4102 -0.4635 585  ALA A CB  
4482  N  N   . ASN A  586 ? 2.5763 3.4014 3.0025 0.0185  -0.4535 -0.4565 586  ASN A N   
4483  C  CA  . ASN A  586 ? 2.4879 3.3085 2.8783 0.0118  -0.4662 -0.4653 586  ASN A CA  
4484  C  C   . ASN A  586 ? 2.5685 3.3488 2.9053 0.0293  -0.4559 -0.4782 586  ASN A C   
4485  O  O   . ASN A  586 ? 2.7537 3.5048 3.0805 0.0404  -0.4386 -0.4826 586  ASN A O   
4486  C  CB  . ASN A  586 ? 2.4359 3.2255 2.8279 -0.0192 -0.4738 -0.4813 586  ASN A CB  
4487  C  CG  . ASN A  586 ? 2.7118 3.4486 3.1036 -0.0220 -0.4570 -0.4994 586  ASN A CG  
4488  O  OD1 . ASN A  586 ? 2.5157 3.2284 2.8858 -0.0058 -0.4394 -0.5083 586  ASN A OD1 
4489  N  ND2 . ASN A  586 ? 3.7202 4.4387 4.1326 -0.0420 -0.4631 -0.5047 586  ASN A ND2 
4490  N  N   . ILE A  587 ? 2.5613 3.3395 2.8604 0.0290  -0.4679 -0.4836 587  ILE A N   
4491  C  CA  . ILE A  587 ? 2.6208 3.3566 2.8612 0.0406  -0.4617 -0.4952 587  ILE A CA  
4492  C  C   . ILE A  587 ? 2.7025 3.4119 2.9103 0.0224  -0.4695 -0.5134 587  ILE A C   
4493  O  O   . ILE A  587 ? 2.7638 3.4956 2.9879 0.0066  -0.4849 -0.5130 587  ILE A O   
4494  C  CB  . ILE A  587 ? 2.7132 3.4676 2.9232 0.0714  -0.4698 -0.4803 587  ILE A CB  
4495  C  CG1 . ILE A  587 ? 2.6050 3.4226 2.8333 0.0773  -0.4909 -0.4663 587  ILE A CG1 
4496  C  CG2 . ILE A  587 ? 2.8572 3.6143 3.0798 0.0923  -0.4580 -0.4675 587  ILE A CG2 
4497  C  CD1 . ILE A  587 ? 2.6092 3.4474 2.8025 0.1143  -0.5013 -0.4539 587  ILE A CD1 
4498  N  N   . SER A  588 ? 2.7537 3.4153 2.9124 0.0226  -0.4593 -0.5286 588  SER A N   
4499  C  CA  . SER A  588 ? 2.7373 3.3689 2.8598 0.0062  -0.4636 -0.5478 588  SER A CA  
4500  C  C   . SER A  588 ? 2.6998 3.3002 2.7554 0.0161  -0.4642 -0.5514 588  SER A C   
4501  O  O   . SER A  588 ? 2.7334 3.3164 2.7643 0.0295  -0.4552 -0.5452 588  SER A O   
4502  C  CB  . SER A  588 ? 2.7913 3.3924 2.9217 -0.0111 -0.4487 -0.5683 588  SER A CB  
4503  O  OG  . SER A  588 ? 2.8545 3.4355 2.9718 -0.0046 -0.4283 -0.5719 588  SER A OG  
4504  N  N   . ARG A  589 ? 2.6608 3.2502 2.6830 0.0078  -0.4768 -0.5610 589  ARG A N   
4505  C  CA  . ARG A  589 ? 2.7219 3.2732 2.6735 0.0116  -0.4794 -0.5674 589  ARG A CA  
4506  C  C   . ARG A  589 ? 2.9919 3.5200 2.9220 -0.0106 -0.4808 -0.5884 589  ARG A C   
4507  O  O   . ARG A  589 ? 3.1756 3.7130 3.1426 -0.0258 -0.4797 -0.5979 589  ARG A O   
4508  C  CB  . ARG A  589 ? 2.7316 3.2984 2.6553 0.0357  -0.4993 -0.5525 589  ARG A CB  
4509  C  CG  . ARG A  589 ? 2.7874 3.3039 2.6316 0.0466  -0.5015 -0.5535 589  ARG A CG  
4510  C  CD  . ARG A  589 ? 2.8210 3.3479 2.6295 0.0747  -0.5247 -0.5424 589  ARG A CD  
4511  N  NE  . ARG A  589 ? 2.8668 3.3320 2.5874 0.0818  -0.5309 -0.5456 589  ARG A NE  
4512  C  CZ  . ARG A  589 ? 2.8955 3.3505 2.5631 0.1090  -0.5525 -0.5392 589  ARG A CZ  
4513  N  NH1 . ARG A  589 ? 2.9678 3.4813 2.6661 0.1335  -0.5686 -0.5294 589  ARG A NH1 
4514  N  NH2 . ARG A  589 ? 2.9455 3.3327 2.5259 0.1117  -0.5593 -0.5424 589  ARG A NH2 
4515  N  N   . GLN A  590 ? 3.0180 3.5113 2.8834 -0.0125 -0.4846 -0.5961 590  GLN A N   
4516  C  CA  . GLN A  590 ? 3.0321 3.5019 2.8731 -0.0331 -0.4835 -0.6171 590  GLN A CA  
4517  C  C   . GLN A  590 ? 3.1062 3.5474 2.8783 -0.0316 -0.4967 -0.6200 590  GLN A C   
4518  O  O   . GLN A  590 ? 3.2601 3.6815 2.9872 -0.0177 -0.5009 -0.6096 590  GLN A O   
4519  C  CB  . GLN A  590 ? 2.9415 3.3909 2.7774 -0.0468 -0.4600 -0.6323 590  GLN A CB  
4520  C  CG  . GLN A  590 ? 2.8929 3.3180 2.6837 -0.0445 -0.4483 -0.6266 590  GLN A CG  
4521  C  CD  . GLN A  590 ? 2.8268 3.2485 2.6211 -0.0585 -0.4244 -0.6397 590  GLN A CD  
4522  O  OE1 . GLN A  590 ? 2.8039 3.2417 2.6386 -0.0634 -0.4161 -0.6531 590  GLN A OE1 
4523  N  NE2 . GLN A  590 ? 2.8400 3.2409 2.5884 -0.0645 -0.4147 -0.6355 590  GLN A NE2 
4524  N  N   . ALA A  591 ? 2.9974 3.4310 2.7567 -0.0456 -0.5048 -0.6345 591  ALA A N   
4525  C  CA  . ALA A  591 ? 2.9558 3.3590 2.6489 -0.0477 -0.5169 -0.6406 591  ALA A CA  
4526  C  C   . ALA A  591 ? 2.9080 3.2826 2.5733 -0.0704 -0.5050 -0.6630 591  ALA A C   
4527  O  O   . ALA A  591 ? 2.8667 3.2517 2.5699 -0.0810 -0.4939 -0.6752 591  ALA A O   
4528  C  CB  . ALA A  591 ? 2.9446 3.3728 2.6458 -0.0407 -0.5416 -0.6356 591  ALA A CB  
4529  N  N   . HIS A  592 ? 2.9093 3.2472 2.5045 -0.0766 -0.5083 -0.6689 592  HIS A N   
4530  C  CA  . HIS A  592 ? 2.9386 3.2539 2.5006 -0.0978 -0.4942 -0.6886 592  HIS A CA  
4531  C  C   . HIS A  592 ? 3.1316 3.4212 2.6403 -0.1061 -0.5086 -0.6991 592  HIS A C   
4532  O  O   . HIS A  592 ? 3.2047 3.4807 2.6791 -0.0952 -0.5281 -0.6895 592  HIS A O   
4533  C  CB  . HIS A  592 ? 2.9097 3.2047 2.4315 -0.1058 -0.4773 -0.6852 592  HIS A CB  
4534  C  CG  . HIS A  592 ? 2.8910 3.2094 2.4609 -0.0986 -0.4623 -0.6755 592  HIS A CG  
4535  N  ND1 . HIS A  592 ? 2.9129 3.2558 2.5274 -0.1054 -0.4426 -0.6873 592  HIS A ND1 
4536  C  CD2 . HIS A  592 ? 2.9250 3.2451 2.5034 -0.0827 -0.4651 -0.6558 592  HIS A CD2 
4537  C  CE1 . HIS A  592 ? 2.9778 3.3370 2.6279 -0.0961 -0.4333 -0.6747 592  HIS A CE1 
4538  N  NE2 . HIS A  592 ? 2.9924 3.3381 2.6220 -0.0830 -0.4464 -0.6552 592  HIS A NE2 
4539  N  N   . ILE A  593 ? 3.1440 3.4273 2.6435 -0.1231 -0.4992 -0.7199 593  ILE A N   
4540  C  CA  . ILE A  593 ? 2.9924 3.2499 2.4393 -0.1340 -0.5092 -0.7329 593  ILE A CA  
4541  C  C   . ILE A  593 ? 2.9484 3.1826 2.3352 -0.1517 -0.4932 -0.7408 593  ILE A C   
4542  O  O   . ILE A  593 ? 2.9737 3.2243 2.3749 -0.1614 -0.4719 -0.7527 593  ILE A O   
4543  C  CB  . ILE A  593 ? 2.8721 3.1396 2.3491 -0.1397 -0.5131 -0.7511 593  ILE A CB  
4544  C  CG1 . ILE A  593 ? 2.8580 3.1539 2.4008 -0.1293 -0.5262 -0.7416 593  ILE A CG1 
4545  C  CG2 . ILE A  593 ? 2.9099 3.1510 2.3339 -0.1484 -0.5275 -0.7619 593  ILE A CG2 
4546  C  CD1 . ILE A  593 ? 2.8301 3.1461 2.4297 -0.1281 -0.5114 -0.7458 593  ILE A CD1 
4547  N  N   . LEU A  594 ? 2.8332 3.0311 2.1499 -0.1561 -0.5044 -0.7341 594  LEU A N   
4548  C  CA  . LEU A  594 ? 3.0092 3.1825 2.2600 -0.1782 -0.4923 -0.7374 594  LEU A CA  
4549  C  C   . LEU A  594 ? 3.7598 3.9072 2.9529 -0.1930 -0.5002 -0.7516 594  LEU A C   
4550  O  O   . LEU A  594 ? 2.8416 2.9889 2.0465 -0.1856 -0.5147 -0.7601 594  LEU A O   
4551  C  CB  . LEU A  594 ? 3.0339 3.1734 2.2345 -0.1763 -0.4992 -0.7166 594  LEU A CB  
4552  C  CG  . LEU A  594 ? 2.7577 2.9142 1.9928 -0.1698 -0.4867 -0.7023 594  LEU A CG  
4553  C  CD1 . LEU A  594 ? 2.7155 2.8884 2.0037 -0.1386 -0.5001 -0.6887 594  LEU A CD1 
4554  C  CD2 . LEU A  594 ? 2.8029 2.9165 1.9610 -0.1858 -0.4869 -0.6888 594  LEU A CD2 
4571  N  N   . ASP B  3   ? 1.6309 3.0616 6.0268 -0.3290 0.3905  -0.5534 113  ASP B N   
4572  C  CA  . ASP B  3   ? 1.6048 2.9713 6.0320 -0.2709 0.3488  -0.5389 113  ASP B CA  
4573  C  C   . ASP B  3   ? 1.5516 2.7936 5.7537 -0.2787 0.4001  -0.5243 113  ASP B C   
4574  O  O   . ASP B  3   ? 1.5744 2.7830 5.7261 -0.2962 0.4942  -0.5520 113  ASP B O   
4575  C  CB  . ASP B  3   ? 1.6730 3.0905 6.3543 -0.2236 0.3682  -0.5751 113  ASP B CB  
4576  C  CG  . ASP B  3   ? 1.6595 3.0169 6.3962 -0.1612 0.3137  -0.5565 113  ASP B CG  
4577  O  OD1 . ASP B  3   ? 1.6080 2.9167 6.2477 -0.1484 0.2318  -0.5145 113  ASP B OD1 
4578  O  OD2 . ASP B  3   ? 1.7067 3.0629 6.5823 -0.1250 0.3540  -0.5826 113  ASP B OD2 
4579  N  N   . TYR B  4   ? 1.6813 2.8553 5.7506 -0.2650 0.3363  -0.4818 114  TYR B N   
4580  C  CA  . TYR B  4   ? 1.6300 2.6974 5.4764 -0.2763 0.3789  -0.4658 114  TYR B CA  
4581  C  C   . TYR B  4   ? 1.6064 2.6110 5.4010 -0.2419 0.3039  -0.4234 114  TYR B C   
4582  O  O   . TYR B  4   ? 1.5605 2.5921 5.3731 -0.2325 0.2131  -0.3940 114  TYR B O   
4583  C  CB  . TYR B  4   ? 1.6004 2.6562 5.2160 -0.3337 0.4099  -0.4550 114  TYR B CB  
4584  C  CG  . TYR B  4   ? 1.7418 2.6969 5.1440 -0.3457 0.4605  -0.4495 114  TYR B CG  
4585  C  CD1 . TYR B  4   ? 1.8162 2.7298 5.2091 -0.3531 0.5546  -0.4899 114  TYR B CD1 
4586  C  CD2 . TYR B  4   ? 1.6435 2.5452 4.8616 -0.3498 0.4145  -0.4082 114  TYR B CD2 
4587  C  CE1 . TYR B  4   ? 1.9508 2.7732 5.1581 -0.3634 0.5969  -0.4912 114  TYR B CE1 
4588  C  CE2 . TYR B  4   ? 1.4764 2.2948 4.5137 -0.3597 0.4589  -0.4074 114  TYR B CE2 
4589  C  CZ  . TYR B  4   ? 1.8252 2.6049 4.8585 -0.3662 0.5480  -0.4500 114  TYR B CZ  
4590  O  OH  . TYR B  4   ? 1.6261 2.3260 4.4824 -0.3759 0.5874  -0.4536 114  TYR B OH  
4591  N  N   . PRO B  5   ? 1.7209 2.6408 5.4613 -0.2229 0.3382  -0.4200 115  PRO B N   
4592  C  CA  . PRO B  5   ? 1.7755 2.6322 5.4740 -0.1916 0.2731  -0.3772 115  PRO B CA  
4593  C  C   . PRO B  5   ? 1.4070 2.2398 4.8811 -0.2190 0.2296  -0.3355 115  PRO B C   
4594  O  O   . PRO B  5   ? 1.3827 2.2099 4.6673 -0.2635 0.2749  -0.3384 115  PRO B O   
4595  C  CB  . PRO B  5   ? 1.7744 2.5479 5.4383 -0.1821 0.3458  -0.3900 115  PRO B CB  
4596  C  CG  . PRO B  5   ? 1.8241 2.6292 5.6149 -0.1867 0.4261  -0.4438 115  PRO B CG  
4597  C  CD  . PRO B  5   ? 1.7559 2.6362 5.5045 -0.2269 0.4379  -0.4588 115  PRO B CD  
4598  N  N   . VAL B  6   ? 1.2359 2.0509 4.7313 -0.1896 0.1369  -0.2947 116  VAL B N   
4599  C  CA  . VAL B  6   ? 1.1802 1.9727 4.4836 -0.2097 0.0851  -0.2531 116  VAL B CA  
4600  C  C   . VAL B  6   ? 1.2940 2.0163 4.5862 -0.1725 0.0268  -0.2093 116  VAL B C   
4601  O  O   . VAL B  6   ? 1.2559 1.9731 4.7301 -0.1245 -0.0320 -0.1995 116  VAL B O   
4602  C  CB  . VAL B  6   ? 1.1949 2.0548 4.5386 -0.2210 0.0123  -0.2469 116  VAL B CB  
4603  C  CG1 . VAL B  6   ? 1.1509 1.9732 4.3409 -0.2251 -0.0628 -0.1998 116  VAL B CG1 
4604  C  CG2 . VAL B  6   ? 1.2074 2.1242 4.4928 -0.2733 0.0764  -0.2776 116  VAL B CG2 
4605  N  N   . ASP B  7   ? 1.1004 1.7707 4.1784 -0.1940 0.0408  -0.1814 117  ASP B N   
4606  C  CA  . ASP B  7   ? 1.0743 1.6803 4.1142 -0.1676 -0.0139 -0.1328 117  ASP B CA  
4607  C  C   . ASP B  7   ? 1.0379 1.6419 3.9238 -0.1840 -0.0829 -0.0951 117  ASP B C   
4608  O  O   . ASP B  7   ? 1.0107 1.6394 3.7306 -0.2285 -0.0505 -0.1054 117  ASP B O   
4609  C  CB  . ASP B  7   ? 1.5227 2.0686 4.4438 -0.1789 0.0637  -0.1315 117  ASP B CB  
4610  C  CG  . ASP B  7   ? 1.3656 1.8963 4.4302 -0.1625 0.1337  -0.1685 117  ASP B CG  
4611  O  OD1 . ASP B  7   ? 1.1854 1.7413 4.4724 -0.1285 0.1051  -0.1821 117  ASP B OD1 
4612  O  OD2 . ASP B  7   ? 1.0840 1.5772 4.0331 -0.1834 0.2139  -0.1855 117  ASP B OD2 
4613  N  N   . LEU B  8   ? 1.0469 1.6155 3.9846 -0.1470 -0.1827 -0.0496 118  LEU B N   
4614  C  CA  . LEU B  8   ? 1.0257 1.5784 3.8251 -0.1561 -0.2591 -0.0110 118  LEU B CA  
4615  C  C   . LEU B  8   ? 1.0642 1.5405 3.8237 -0.1268 -0.3152 0.0472  118  LEU B C   
4616  O  O   . LEU B  8   ? 1.3972 1.8427 4.2996 -0.0775 -0.3857 0.0719  118  LEU B O   
4617  C  CB  . LEU B  8   ? 1.3905 1.9821 4.2910 -0.1410 -0.3524 -0.0144 118  LEU B CB  
4618  C  CG  . LEU B  8   ? 1.3247 1.9020 4.0860 -0.1548 -0.4303 0.0141  118  LEU B CG  
4619  C  CD1 . LEU B  8   ? 1.3345 1.8353 4.0838 -0.1076 -0.5496 0.0700  118  LEU B CD1 
4620  C  CD2 . LEU B  8   ? 1.0227 1.5935 3.5562 -0.2055 -0.3600 0.0154  118  LEU B CD2 
4621  N  N   . TYR B  9   ? 1.2353 1.6824 3.7951 -0.1561 -0.2851 0.0701  119  TYR B N   
4622  C  CA  . TYR B  9   ? 1.0730 1.4525 3.5784 -0.1359 -0.3373 0.1321  119  TYR B CA  
4623  C  C   . TYR B  9   ? 0.9652 1.3199 3.3584 -0.1312 -0.4429 0.1727  119  TYR B C   
4624  O  O   . TYR B  9   ? 1.3197 1.7019 3.5781 -0.1673 -0.4249 0.1544  119  TYR B O   
4625  C  CB  . TYR B  9   ? 0.9027 1.2642 3.2524 -0.1710 -0.2387 0.1322  119  TYR B CB  
4626  C  CG  . TYR B  9   ? 0.9044 1.2016 3.2575 -0.1520 -0.2687 0.1950  119  TYR B CG  
4627  C  CD1 . TYR B  9   ? 1.0866 1.3544 3.5868 -0.1301 -0.2349 0.2016  119  TYR B CD1 
4628  C  CD2 . TYR B  9   ? 1.0231 1.2863 3.2366 -0.1578 -0.3298 0.2517  119  TYR B CD2 
4629  C  CE1 . TYR B  9   ? 0.9681 1.1744 3.4776 -0.1204 -0.2561 0.2665  119  TYR B CE1 
4630  C  CE2 . TYR B  9   ? 0.8989 1.1051 3.1158 -0.1468 -0.3569 0.3185  119  TYR B CE2 
4631  C  CZ  . TYR B  9   ? 0.9578 1.1057 3.2533 -0.1178 -0.3091 0.3225  119  TYR B CZ  
4632  O  OH  . TYR B  9   ? 1.0625 1.0735 3.1843 -0.0792 -0.3068 0.3805  119  TYR B OH  
4633  N  N   . TYR B  10  ? 1.0206 1.3143 3.4440 -0.0829 -0.5536 0.2272  120  TYR B N   
4634  C  CA  . TYR B  10  ? 1.0718 1.3170 3.3578 -0.0667 -0.6648 0.2634  120  TYR B CA  
4635  C  C   . TYR B  10  ? 1.0590 1.2384 3.1650 -0.0629 -0.6824 0.3254  120  TYR B C   
4636  O  O   . TYR B  10  ? 1.1213 1.2303 3.2019 -0.0118 -0.7120 0.3709  120  TYR B O   
4637  C  CB  . TYR B  10  ? 1.1953 1.4021 3.5502 -0.0060 -0.7727 0.2702  120  TYR B CB  
4638  C  CG  . TYR B  10  ? 1.2698 1.4379 3.4847 0.0009  -0.8663 0.2777  120  TYR B CG  
4639  C  CD1 . TYR B  10  ? 1.2514 1.4806 3.5070 -0.0348 -0.8626 0.2365  120  TYR B CD1 
4640  C  CD2 . TYR B  10  ? 1.3776 1.4422 3.3931 0.0450  -0.9433 0.3214  120  TYR B CD2 
4641  C  CE1 . TYR B  10  ? 1.5630 1.7526 3.7009 -0.0305 -0.9444 0.2420  120  TYR B CE1 
4642  C  CE2 . TYR B  10  ? 1.4570 1.4808 3.3336 0.0500  -1.0153 0.3199  120  TYR B CE2 
4643  C  CZ  . TYR B  10  ? 1.6747 1.7598 3.6281 0.0106  -1.0219 0.2821  120  TYR B CZ  
4644  O  OH  . TYR B  10  ? 1.9138 1.9534 3.7393 0.0145  -1.0919 0.2807  120  TYR B OH  
4645  N  N   . LEU B  11  ? 1.0011 1.1924 2.9466 -0.1089 -0.6543 0.3266  121  LEU B N   
4646  C  CA  . LEU B  11  ? 0.9851 1.1286 2.7475 -0.1118 -0.6628 0.3826  121  LEU B CA  
4647  C  C   . LEU B  11  ? 1.0882 1.1405 2.6307 -0.0808 -0.7572 0.4107  121  LEU B C   
4648  O  O   . LEU B  11  ? 1.0715 1.1374 2.5275 -0.1127 -0.7644 0.3901  121  LEU B O   
4649  C  CB  . LEU B  11  ? 0.8831 1.0853 2.5580 -0.1817 -0.5478 0.3516  121  LEU B CB  
4650  C  CG  . LEU B  11  ? 0.9205 1.0990 2.4591 -0.2003 -0.5266 0.4026  121  LEU B CG  
4651  C  CD1 . LEU B  11  ? 0.9115 1.0223 2.4769 -0.1635 -0.4842 0.4273  121  LEU B CD1 
4652  C  CD2 . LEU B  11  ? 1.3449 1.5665 2.7432 -0.2548 -0.3981 0.3495  121  LEU B CD2 
4653  N  N   . MET B  12  ? 1.5448 1.4938 2.9504 -0.0199 -0.8011 0.4445  122  MET B N   
4654  C  CA  . MET B  12  ? 1.4250 1.2917 2.5979 0.0113  -0.8567 0.4459  122  MET B CA  
4655  C  C   . MET B  12  ? 1.3660 1.1711 2.2695 0.0208  -0.8139 0.4748  122  MET B C   
4656  O  O   . MET B  12  ? 1.3739 1.1483 2.2284 0.0376  -0.7641 0.5065  122  MET B O   
4657  C  CB  . MET B  12  ? 1.5822 1.3888 2.7534 0.0783  -0.9131 0.4456  122  MET B CB  
4658  C  CG  . MET B  12  ? 1.6088 1.3579 2.6055 0.1080  -0.9713 0.4352  122  MET B CG  
4659  S  SD  . MET B  12  ? 2.3167 1.9675 3.1793 0.1997  -1.0019 0.4591  122  MET B SD  
4660  C  CE  . MET B  12  ? 2.2284 1.9199 3.3705 0.2223  -1.0497 0.4427  122  MET B CE  
4661  N  N   . ASP B  13  ? 1.3920 1.1750 2.1217 0.0153  -0.8249 0.4594  123  ASP B N   
4662  C  CA  . ASP B  13  ? 1.4274 1.1624 1.9028 0.0374  -0.7744 0.4705  123  ASP B CA  
4663  C  C   . ASP B  13  ? 1.5801 1.2376 1.9140 0.1120  -0.7904 0.4788  123  ASP B C   
4664  O  O   . ASP B  13  ? 2.1472 1.7854 2.4646 0.1317  -0.8455 0.4613  123  ASP B O   
4665  C  CB  . ASP B  13  ? 1.3845 1.1371 1.7567 0.0058  -0.7646 0.4441  123  ASP B CB  
4666  C  CG  . ASP B  13  ? 1.4252 1.1428 1.5613 0.0456  -0.7059 0.4433  123  ASP B CG  
4667  O  OD1 . ASP B  13  ? 1.4400 1.1405 1.4996 0.0748  -0.6530 0.4666  123  ASP B OD1 
4668  O  OD2 . ASP B  13  ? 1.4456 1.1557 1.4887 0.0515  -0.7086 0.4198  123  ASP B OD2 
4669  N  N   . LEU B  14  ? 1.6304 1.2436 1.8651 0.1518  -0.7396 0.5094  124  LEU B N   
4670  C  CA  . LEU B  14  ? 1.7770 1.3223 1.8812 0.2242  -0.7425 0.5274  124  LEU B CA  
4671  C  C   . LEU B  14  ? 1.8225 1.3439 1.7380 0.2396  -0.7056 0.5346  124  LEU B C   
4672  O  O   . LEU B  14  ? 2.1314 1.5845 1.9465 0.2847  -0.7138 0.5631  124  LEU B O   
4673  C  CB  . LEU B  14  ? 1.8453 1.3352 1.9672 0.2597  -0.7179 0.5644  124  LEU B CB  
4674  C  CG  . LEU B  14  ? 1.8746 1.3620 2.1912 0.2647  -0.7800 0.5613  124  LEU B CG  
4675  C  CD1 . LEU B  14  ? 2.0519 1.4647 2.3590 0.3075  -0.7453 0.5986  124  LEU B CD1 
4676  C  CD2 . LEU B  14  ? 1.9716 1.4500 2.2943 0.2973  -0.8591 0.5432  124  LEU B CD2 
4677  N  N   . SER B  15  ? 1.7309 1.2954 1.6101 0.1971  -0.6812 0.5115  125  SER B N   
4678  C  CA  . SER B  15  ? 1.7850 1.3237 1.5102 0.2062  -0.6528 0.5182  125  SER B CA  
4679  C  C   . SER B  15  ? 1.9390 1.4090 1.5880 0.2305  -0.7211 0.5146  125  SER B C   
4680  O  O   . SER B  15  ? 2.0029 1.4462 1.7134 0.2380  -0.7937 0.5042  125  SER B O   
4681  C  CB  . SER B  15  ? 1.6601 1.2578 1.3717 0.1591  -0.6138 0.4902  125  SER B CB  
4682  O  OG  . SER B  15  ? 1.6299 1.2412 1.3967 0.1238  -0.6644 0.4570  125  SER B OG  
4683  N  N   . ALA B  16  ? 2.0027 1.4433 1.5200 0.2421  -0.6990 0.5202  126  ALA B N   
4684  C  CA  . ALA B  16  ? 2.1728 1.5274 1.5955 0.2704  -0.7583 0.5194  126  ALA B CA  
4685  C  C   . ALA B  16  ? 2.1900 1.5232 1.6351 0.2437  -0.8273 0.4781  126  ALA B C   
4686  O  O   . ALA B  16  ? 2.3300 1.5894 1.7461 0.2653  -0.9012 0.4716  126  ALA B O   
4687  C  CB  . ALA B  16  ? 2.2331 1.5628 1.5203 0.2870  -0.7141 0.5335  126  ALA B CB  
4688  N  N   . SER B  17  ? 2.0590 1.4496 1.5555 0.1971  -0.8065 0.4514  127  SER B N   
4689  C  CA  . SER B  17  ? 2.0798 1.4433 1.5929 0.1682  -0.8649 0.4172  127  SER B CA  
4690  C  C   . SER B  17  ? 2.0730 1.4503 1.7259 0.1575  -0.9309 0.4086  127  SER B C   
4691  O  O   . SER B  17  ? 2.0770 1.4433 1.7728 0.1282  -0.9797 0.3830  127  SER B O   
4692  C  CB  . SER B  17  ? 2.0817 1.4958 1.5981 0.1229  -0.8169 0.3955  127  SER B CB  
4693  O  OG  . SER B  17  ? 1.7933 1.2985 1.4071 0.0976  -0.7636 0.4009  127  SER B OG  
4694  N  N   . MET B  18  ? 2.0735 1.4715 1.8016 0.1836  -0.9341 0.4306  128  MET B N   
4695  C  CA  . MET B  18  ? 2.0504 1.4819 1.9396 0.1775  -0.9877 0.4219  128  MET B CA  
4696  C  C   . MET B  18  ? 2.2215 1.5848 2.1044 0.2243  -1.0680 0.4285  128  MET B C   
4697  O  O   . MET B  18  ? 2.2204 1.6138 2.2451 0.2293  -1.1170 0.4212  128  MET B O   
4698  C  CB  . MET B  18  ? 1.9196 1.4282 1.9234 0.1735  -0.9328 0.4365  128  MET B CB  
4699  C  CG  . MET B  18  ? 1.7449 1.3297 1.7921 0.1217  -0.8695 0.4231  128  MET B CG  
4700  S  SD  . MET B  18  ? 1.6595 1.2990 1.8497 0.0667  -0.9101 0.3872  128  MET B SD  
4701  C  CE  . MET B  18  ? 1.6994 1.3533 2.1100 0.0763  -0.9858 0.3902  128  MET B CE  
4702  N  N   . ASP B  19  ? 2.3750 1.6483 2.1016 0.2603  -1.0845 0.4397  129  ASP B N   
4703  C  CA  . ASP B  19  ? 2.5547 1.7533 2.2610 0.3063  -1.1664 0.4444  129  ASP B CA  
4704  C  C   . ASP B  19  ? 2.6134 1.7918 2.3782 0.2871  -1.2565 0.4093  129  ASP B C   
4705  O  O   . ASP B  19  ? 2.9800 2.1421 2.8181 0.3138  -1.3324 0.4053  129  ASP B O   
4706  C  CB  . ASP B  19  ? 2.8952 1.9964 2.4126 0.3480  -1.1597 0.4637  129  ASP B CB  
4707  C  CG  . ASP B  19  ? 3.2402 2.2501 2.7162 0.3980  -1.2489 0.4671  129  ASP B CG  
4708  O  OD1 . ASP B  19  ? 2.9713 1.9764 2.4822 0.4381  -1.2543 0.4950  129  ASP B OD1 
4709  O  OD2 . ASP B  19  ? 3.3263 2.2625 2.7313 0.3995  -1.3150 0.4415  129  ASP B OD2 
4710  N  N   . ASP B  20  ? 2.5573 1.7364 2.2952 0.2425  -1.2491 0.3848  130  ASP B N   
4711  C  CA  . ASP B  20  ? 2.6722 1.8329 2.4706 0.2174  -1.3265 0.3545  130  ASP B CA  
4712  C  C   . ASP B  20  ? 2.4580 1.7245 2.4661 0.1820  -1.3328 0.3430  130  ASP B C   
4713  O  O   . ASP B  20  ? 2.4926 1.7616 2.5902 0.1651  -1.4013 0.3211  130  ASP B O   
4714  C  CB  . ASP B  20  ? 2.8558 1.9673 2.5404 0.1851  -1.3101 0.3363  130  ASP B CB  
4715  C  CG  . ASP B  20  ? 2.4284 1.6090 2.1072 0.1485  -1.2112 0.3408  130  ASP B CG  
4716  O  OD1 . ASP B  20  ? 2.3519 1.5826 2.0315 0.1623  -1.1454 0.3631  130  ASP B OD1 
4717  O  OD2 . ASP B  20  ? 2.3759 1.5576 2.0471 0.1074  -1.1999 0.3231  130  ASP B OD2 
4718  N  N   . ASP B  21  ? 2.3074 1.6616 2.3992 0.1712  -1.2623 0.3564  131  ASP B N   
4719  C  CA  . ASP B  21  ? 2.1668 1.6263 2.4580 0.1368  -1.2547 0.3431  131  ASP B CA  
4720  C  C   . ASP B  21  ? 2.1510 1.6623 2.5701 0.1719  -1.2557 0.3554  131  ASP B C   
4721  O  O   . ASP B  21  ? 2.0600 1.6448 2.6721 0.1441  -1.2608 0.3434  131  ASP B O   
4722  C  CB  . ASP B  21  ? 1.9950 1.5145 2.2841 0.0891  -1.1667 0.3425  131  ASP B CB  
4723  C  CG  . ASP B  21  ? 2.1441 1.5959 2.2463 0.0750  -1.1370 0.3419  131  ASP B CG  
4724  O  OD1 . ASP B  21  ? 2.1350 1.5128 2.1622 0.0719  -1.1892 0.3281  131  ASP B OD1 
4725  O  OD2 . ASP B  21  ? 2.2938 1.7659 2.3241 0.0704  -1.0593 0.3543  131  ASP B OD2 
4726  N  N   . LEU B  22  ? 2.2696 1.7179 2.5946 0.2271  -1.2651 0.3802  132  LEU B N   
4727  C  CA  . LEU B  22  ? 2.3269 1.8064 2.7490 0.2679  -1.2583 0.3978  132  LEU B CA  
4728  C  C   . LEU B  22  ? 2.4072 1.9265 3.0226 0.2769  -1.3412 0.3746  132  LEU B C   
4729  O  O   . LEU B  22  ? 2.4425 2.0204 3.2532 0.2637  -1.3452 0.3664  132  LEU B O   
4730  C  CB  . LEU B  22  ? 2.6466 2.0303 2.9093 0.3278  -1.2607 0.4316  132  LEU B CB  
4731  C  CG  . LEU B  22  ? 2.7537 2.1376 3.0792 0.3817  -1.2555 0.4577  132  LEU B CG  
4732  C  CD1 . LEU B  22  ? 2.3876 1.8404 2.7901 0.3640  -1.1630 0.4695  132  LEU B CD1 
4733  C  CD2 . LEU B  22  ? 2.8180 2.0915 2.9667 0.4397  -1.2645 0.4931  132  LEU B CD2 
4734  N  N   . ASN B  23  ? 2.4511 1.9244 3.0362 0.2944  -1.4248 0.3603  133  ASN B N   
4735  C  CA  . ASN B  23  ? 2.5165 2.0272 3.2841 0.3103  -1.5121 0.3373  133  ASN B CA  
4736  C  C   . ASN B  23  ? 2.3992 1.9980 3.3910 0.2484  -1.5250 0.3040  133  ASN B C   
4737  O  O   . ASN B  23  ? 2.4192 2.0770 3.6219 0.2568  -1.5775 0.2830  133  ASN B O   
4738  C  CB  . ASN B  23  ? 2.6978 2.1310 3.3804 0.3354  -1.6065 0.3264  133  ASN B CB  
4739  C  CG  . ASN B  23  ? 2.7465 2.1425 3.3439 0.2854  -1.6155 0.3086  133  ASN B CG  
4740  O  OD1 . ASN B  23  ? 2.6954 2.0863 3.2003 0.2492  -1.5407 0.3164  133  ASN B OD1 
4741  N  ND2 . ASN B  23  ? 2.8037 2.1725 3.4337 0.2850  -1.7081 0.2843  133  ASN B ND2 
4742  N  N   . THR B  24  ? 2.2852 1.9000 3.2395 0.1895  -1.4715 0.2991  134  THR B N   
4743  C  CA  . THR B  24  ? 2.1678 1.8695 3.3269 0.1304  -1.4659 0.2731  134  THR B CA  
4744  C  C   . THR B  24  ? 2.0457 1.8226 3.3689 0.1194  -1.4078 0.2763  134  THR B C   
4745  O  O   . THR B  24  ? 1.9841 1.8537 3.5403 0.0935  -1.4084 0.2500  134  THR B O   
4746  C  CB  . THR B  24  ? 2.0935 1.7801 3.1405 0.0760  -1.4225 0.2714  134  THR B CB  
4747  O  OG1 . THR B  24  ? 2.2109 1.8185 3.0950 0.0884  -1.4683 0.2685  134  THR B OG1 
4748  C  CG2 . THR B  24  ? 1.9998 1.7780 3.2474 0.0200  -1.4140 0.2463  134  THR B CG2 
4749  N  N   . ILE B  25  ? 2.0900 1.8331 3.2994 0.1409  -1.3505 0.3066  135  ILE B N   
4750  C  CA  . ILE B  25  ? 1.9037 1.7075 3.2585 0.1292  -1.2912 0.3122  135  ILE B CA  
4751  C  C   . ILE B  25  ? 1.9715 1.8005 3.4923 0.1785  -1.3294 0.3061  135  ILE B C   
4752  O  O   . ILE B  25  ? 1.9710 1.8842 3.7197 0.1622  -1.3029 0.2868  135  ILE B O   
4753  C  CB  . ILE B  25  ? 1.8568 1.6140 3.0270 0.1336  -1.2165 0.3478  135  ILE B CB  
4754  C  CG1 . ILE B  25  ? 1.7872 1.5323 2.8089 0.0861  -1.1760 0.3478  135  ILE B CG1 
4755  C  CG2 . ILE B  25  ? 1.8075 1.6190 3.1300 0.1221  -1.1582 0.3558  135  ILE B CG2 
4756  C  CD1 . ILE B  25  ? 1.6912 1.5083 2.8645 0.0242  -1.1724 0.3200  135  ILE B CD1 
4757  N  N   . LYS B  26  ? 2.1279 1.8865 3.5362 0.2428  -1.3852 0.3204  136  LYS B N   
4758  C  CA  . LYS B  26  ? 2.2653 2.0408 3.8160 0.2981  -1.4291 0.3152  136  LYS B CA  
4759  C  C   . LYS B  26  ? 2.3561 2.2178 4.1410 0.2836  -1.4912 0.2704  136  LYS B C   
4760  O  O   . LYS B  26  ? 2.4033 2.3329 4.4014 0.3027  -1.4953 0.2518  136  LYS B O   
4761  C  CB  . LYS B  26  ? 2.4981 2.1722 3.8496 0.3729  -1.4703 0.3448  136  LYS B CB  
4762  C  CG  . LYS B  26  ? 2.3991 1.9935 3.5192 0.3935  -1.3948 0.3904  136  LYS B CG  
4763  C  CD  . LYS B  26  ? 2.5971 2.0959 3.5337 0.4704  -1.4222 0.4223  136  LYS B CD  
4764  C  CE  . LYS B  26  ? 2.5880 2.0172 3.3006 0.4870  -1.3336 0.4673  136  LYS B CE  
4765  N  NZ  . LYS B  26  ? 2.7731 2.1103 3.3131 0.5587  -1.3501 0.5029  136  LYS B NZ  
4766  N  N   . GLU B  27  ? 2.3467 2.2092 4.0977 0.2511  -1.5335 0.2514  137  GLU B N   
4767  C  CA  . GLU B  27  ? 2.3437 2.2984 4.3178 0.2285  -1.5799 0.2083  137  GLU B CA  
4768  C  C   . GLU B  27  ? 2.0815 2.1436 4.2398 0.1641  -1.5005 0.1841  137  GLU B C   
4769  O  O   . GLU B  27  ? 2.0706 2.2350 4.4484 0.1476  -1.5108 0.1453  137  GLU B O   
4770  C  CB  . GLU B  27  ? 2.3531 2.2661 4.2223 0.2143  -1.6473 0.1983  137  GLU B CB  
4771  C  CG  . GLU B  27  ? 2.5265 2.3784 4.3253 0.2788  -1.7465 0.2005  137  GLU B CG  
4772  C  CD  . GLU B  27  ? 2.6660 2.5048 4.4440 0.2584  -1.8203 0.1784  137  GLU B CD  
4773  O  OE1 . GLU B  27  ? 2.8394 2.6076 4.5090 0.3055  -1.8979 0.1830  137  GLU B OE1 
4774  O  OE2 . GLU B  27  ? 2.5221 2.4194 4.3870 0.1962  -1.7977 0.1576  137  GLU B OE2 
4775  N  N   . LEU B  28  ? 1.9595 2.0060 4.0271 0.1284  -1.4153 0.2045  138  LEU B N   
4776  C  CA  . LEU B  28  ? 1.8069 1.9523 4.0307 0.0736  -1.3237 0.1833  138  LEU B CA  
4777  C  C   . LEU B  28  ? 1.7578 1.9507 4.1414 0.0951  -1.2712 0.1793  138  LEU B C   
4778  O  O   . LEU B  28  ? 1.6836 1.9813 4.2704 0.0678  -1.2109 0.1433  138  LEU B O   
4779  C  CB  . LEU B  28  ? 1.7060 1.8162 3.7557 0.0263  -1.2575 0.2050  138  LEU B CB  
4780  C  CG  . LEU B  28  ? 1.5561 1.7628 3.7215 -0.0282 -1.1482 0.1838  138  LEU B CG  
4781  C  CD1 . LEU B  28  ? 1.5504 1.8688 3.9033 -0.0586 -1.1345 0.1343  138  LEU B CD1 
4782  C  CD2 . LEU B  28  ? 1.4818 1.6512 3.4516 -0.0690 -1.0987 0.2044  138  LEU B CD2 
4783  N  N   . GLY B  29  ? 1.8087 1.9247 4.0911 0.1448  -1.2830 0.2143  139  GLY B N   
4784  C  CA  . GLY B  29  ? 1.7838 1.9295 4.2077 0.1726  -1.2387 0.2138  139  GLY B CA  
4785  C  C   . GLY B  29  ? 1.8567 2.0725 4.5034 0.2091  -1.2796 0.1779  139  GLY B C   
4786  O  O   . GLY B  29  ? 1.7840 2.0925 4.6426 0.1909  -1.2157 0.1445  139  GLY B O   
4787  N  N   . SER B  30  ? 2.0098 2.1834 4.6038 0.2628  -1.3811 0.1820  140  SER B N   
4788  C  CA  . SER B  30  ? 2.0961 2.3380 4.8960 0.3061  -1.4305 0.1496  140  SER B CA  
4789  C  C   . SER B  30  ? 2.0342 2.4051 5.0475 0.2541  -1.4130 0.0970  140  SER B C   
4790  O  O   . SER B  30  ? 2.0287 2.4961 5.2697 0.2645  -1.3887 0.0612  140  SER B O   
4791  C  CB  . SER B  30  ? 2.2821 2.4505 4.9602 0.3725  -1.5447 0.1650  140  SER B CB  
4792  O  OG  . SER B  30  ? 2.3129 2.4678 4.9021 0.3407  -1.5992 0.1567  140  SER B OG  
4793  N  N   . ARG B  31  ? 1.9960 2.3696 4.9288 0.1992  -1.4165 0.0917  141  ARG B N   
4794  C  CA  . ARG B  31  ? 1.9506 2.4444 5.0571 0.1478  -1.3896 0.0448  141  ARG B CA  
4795  C  C   . ARG B  31  ? 1.8087 2.3849 5.0339 0.1000  -1.2570 0.0222  141  ARG B C   
4796  O  O   . ARG B  31  ? 1.7943 2.4868 5.2223 0.0816  -1.2154 -0.0226 141  ARG B O   
4797  C  CB  . ARG B  31  ? 1.9570 2.4191 4.9187 0.1039  -1.4214 0.0499  141  ARG B CB  
4798  C  CG  . ARG B  31  ? 1.9546 2.5339 5.0734 0.0575  -1.4158 0.0045  141  ARG B CG  
4799  C  CD  . ARG B  31  ? 1.9897 2.5181 4.9490 0.0237  -1.4634 0.0140  141  ARG B CD  
4800  N  NE  . ARG B  31  ? 2.0086 2.6497 5.1164 -0.0208 -1.4669 -0.0283 141  ARG B NE  
4801  C  CZ  . ARG B  31  ? 2.0543 2.6735 5.0708 -0.0545 -1.5112 -0.0296 141  ARG B CZ  
4802  N  NH1 . ARG B  31  ? 2.0871 2.5704 4.8604 -0.0446 -1.5547 0.0082  141  ARG B NH1 
4803  N  NH2 . ARG B  31  ? 2.0756 2.8083 5.2414 -0.0994 -1.5088 -0.0697 141  ARG B NH2 
4804  N  N   . LEU B  32  ? 1.7133 2.2313 4.8051 0.0798  -1.1856 0.0510  142  LEU B N   
4805  C  CA  . LEU B  32  ? 1.5931 2.1748 4.7707 0.0400  -1.0550 0.0296  142  LEU B CA  
4806  C  C   . LEU B  32  ? 1.6113 2.2205 4.9600 0.0836  -1.0285 0.0163  142  LEU B C   
4807  O  O   . LEU B  32  ? 1.5524 2.2390 5.0357 0.0579  -0.9292 -0.0200 142  LEU B O   
4808  C  CB  . LEU B  32  ? 1.5614 2.0734 4.5402 0.0088  -0.9945 0.0646  142  LEU B CB  
4809  C  CG  . LEU B  32  ? 1.5177 2.0635 4.5063 -0.0305 -0.8581 0.0519  142  LEU B CG  
4810  C  CD1 . LEU B  32  ? 1.2989 1.8232 4.0859 -0.0836 -0.8073 0.0658  142  LEU B CD1 
4811  C  CD2 . LEU B  32  ? 1.4873 1.9771 4.4910 0.0083  -0.8423 0.0787  142  LEU B CD2 
4812  N  N   . SER B  33  ? 1.7089 2.2510 5.0365 0.1524  -1.1124 0.0439  143  SER B N   
4813  C  CA  . SER B  33  ? 1.7468 2.3058 5.2225 0.2035  -1.0952 0.0348  143  SER B CA  
4814  C  C   . SER B  33  ? 1.8322 2.4890 5.5202 0.2320  -1.1391 -0.0092 143  SER B C   
4815  O  O   . SER B  33  ? 1.9203 2.5778 5.7046 0.2981  -1.1736 -0.0111 143  SER B O   
4816  C  CB  . SER B  33  ? 1.8363 2.2769 5.1657 0.2719  -1.1580 0.0864  143  SER B CB  
4817  O  OG  . SER B  33  ? 1.8890 2.3378 5.3475 0.3279  -1.1407 0.0801  143  SER B OG  
4818  N  N   . LYS B  34  ? 1.8153 2.5575 5.5724 0.1846  -1.1362 -0.0438 144  LYS B N   
4819  C  CA  . LYS B  34  ? 1.8929 2.7459 5.8622 0.2026  -1.1734 -0.0882 144  LYS B CA  
4820  C  C   . LYS B  34  ? 1.8143 2.7836 5.9031 0.1320  -1.0705 -0.1348 144  LYS B C   
4821  O  O   . LYS B  34  ? 1.8228 2.8851 6.1068 0.1379  -1.0162 -0.1744 144  LYS B O   
4822  C  CB  . LYS B  34  ? 2.0090 2.8440 5.9255 0.2277  -1.3083 -0.0802 144  LYS B CB  
4823  C  CG  . LYS B  34  ? 2.0773 3.0448 6.2080 0.2257  -1.3454 -0.1292 144  LYS B CG  
4824  C  CD  . LYS B  34  ? 2.1489 3.1858 6.4895 0.2893  -1.3541 -0.1545 144  LYS B CD  
4825  C  CE  . LYS B  34  ? 2.2119 3.3984 6.7802 0.2823  -1.3826 -0.2058 144  LYS B CE  
4826  N  NZ  . LYS B  34  ? 2.2834 3.5475 7.0632 0.3467  -1.3860 -0.2327 144  LYS B NZ  
4827  N  N   . GLU B  35  ? 1.7476 2.7081 5.7026 0.0669  -1.0373 -0.1294 145  GLU B N   
4828  C  CA  . GLU B  35  ? 1.6962 2.7605 5.7236 -0.0011 -0.9424 -0.1701 145  GLU B CA  
4829  C  C   . GLU B  35  ? 1.6072 2.6843 5.6422 -0.0291 -0.7996 -0.1856 145  GLU B C   
4830  O  O   . GLU B  35  ? 1.5861 2.7503 5.6915 -0.0772 -0.7113 -0.2234 145  GLU B O   
4831  C  CB  . GLU B  35  ? 1.6676 2.7098 5.5242 -0.0583 -0.9528 -0.1567 145  GLU B CB  
4832  C  CG  . GLU B  35  ? 1.7630 2.7694 5.5741 -0.0340 -1.0939 -0.1396 145  GLU B CG  
4833  C  CD  . GLU B  35  ? 1.8603 2.9795 5.8823 -0.0255 -1.1533 -0.1793 145  GLU B CD  
4834  O  OE1 . GLU B  35  ? 1.8418 3.0790 6.0209 -0.0627 -1.0742 -0.2208 145  GLU B OE1 
4835  O  OE2 . GLU B  35  ? 1.9648 3.0541 5.9877 0.0182  -1.2789 -0.1694 145  GLU B OE2 
4836  N  N   . MET B  36  ? 1.5660 2.5554 5.5219 -0.0017 -0.7746 -0.1575 146  MET B N   
4837  C  CA  . MET B  36  ? 1.4918 2.4819 5.4402 -0.0276 -0.6409 -0.1734 146  MET B CA  
4838  C  C   . MET B  36  ? 1.5350 2.6025 5.7079 -0.0042 -0.5936 -0.2165 146  MET B C   
4839  O  O   . MET B  36  ? 1.5001 2.6075 5.6970 -0.0418 -0.4773 -0.2491 146  MET B O   
4840  C  CB  . MET B  36  ? 1.4460 2.3243 5.2645 -0.0048 -0.6332 -0.1313 146  MET B CB  
4841  C  CG  . MET B  36  ? 1.3750 2.1864 4.9540 -0.0440 -0.6236 -0.0965 146  MET B CG  
4842  S  SD  . MET B  36  ? 1.2968 2.1591 4.7598 -0.1264 -0.4878 -0.1280 146  MET B SD  
4843  C  CE  . MET B  36  ? 1.2669 2.1275 4.7918 -0.1249 -0.3605 -0.1557 146  MET B CE  
4844  N  N   . SER B  37  ? 1.6230 2.7096 5.9474 0.0606  -0.6833 -0.2177 147  SER B N   
4845  C  CA  . SER B  37  ? 1.6744 2.8368 6.2172 0.0921  -0.6455 -0.2576 147  SER B CA  
4846  C  C   . SER B  37  ? 1.7037 2.9985 6.3919 0.0558  -0.6134 -0.3061 147  SER B C   
4847  O  O   . SER B  37  ? 1.7433 3.1132 6.6133 0.0730  -0.5643 -0.3442 147  SER B O   
4848  C  CB  . SER B  37  ? 1.7751 2.9195 6.4147 0.1800  -0.7586 -0.2417 147  SER B CB  
4849  O  OG  . SER B  37  ? 1.8341 3.0565 6.6868 0.2181  -0.7266 -0.2800 147  SER B OG  
4850  N  N   . LYS B  38  ? 1.6921 3.0177 6.3055 0.0059  -0.6376 -0.3050 148  LYS B N   
4851  C  CA  . LYS B  38  ? 1.7290 3.1834 6.4790 -0.0337 -0.6116 -0.3473 148  LYS B CA  
4852  C  C   . LYS B  38  ? 1.6798 3.1679 6.4119 -0.0922 -0.4625 -0.3767 148  LYS B C   
4853  O  O   . LYS B  38  ? 1.7184 3.2854 6.6251 -0.0845 -0.4033 -0.4157 148  LYS B O   
4854  C  CB  . LYS B  38  ? 1.7410 3.2084 6.4044 -0.0721 -0.6846 -0.3345 148  LYS B CB  
4855  C  CG  . LYS B  38  ? 1.8224 3.2720 6.5212 -0.0158 -0.8403 -0.3149 148  LYS B CG  
4856  C  CD  . LYS B  38  ? 1.9246 3.4874 6.8840 0.0320  -0.8922 -0.3508 148  LYS B CD  
4857  C  CE  . LYS B  38  ? 2.0244 3.5640 6.9960 0.0917  -1.0525 -0.3325 148  LYS B CE  
4858  N  NZ  . LYS B  38  ? 2.0422 3.5785 6.9162 0.0471  -1.1184 -0.3236 148  LYS B NZ  
4859  N  N   . LEU B  39  ? 1.6051 3.0311 6.1172 -0.1474 -0.4026 -0.3582 149  LEU B N   
4860  C  CA  . LEU B  39  ? 1.5756 3.0273 6.0323 -0.2064 -0.2714 -0.3837 149  LEU B CA  
4861  C  C   . LEU B  39  ? 1.5475 2.9447 5.9873 -0.1890 -0.1765 -0.3937 149  LEU B C   
4862  O  O   . LEU B  39  ? 1.5383 2.9481 5.9317 -0.2310 -0.0682 -0.4175 149  LEU B O   
4863  C  CB  . LEU B  39  ? 1.5196 2.9254 5.7319 -0.2689 -0.2495 -0.3596 149  LEU B CB  
4864  C  CG  . LEU B  39  ? 1.5535 3.0466 5.7830 -0.3341 -0.2290 -0.3791 149  LEU B CG  
4865  C  CD1 . LEU B  39  ? 1.5021 2.9344 5.4725 -0.3898 -0.2132 -0.3506 149  LEU B CD1 
4866  C  CD2 . LEU B  39  ? 1.5870 3.1524 5.9298 -0.3599 -0.1201 -0.4212 149  LEU B CD2 
4867  N  N   . THR B  40  ? 1.5439 2.8764 6.0159 -0.1295 -0.2149 -0.3762 150  THR B N   
4868  C  CA  . THR B  40  ? 1.5267 2.8041 5.9936 -0.1141 -0.1271 -0.3873 150  THR B CA  
4869  C  C   . THR B  40  ? 1.5676 2.8213 6.1799 -0.0387 -0.1907 -0.3783 150  THR B C   
4870  O  O   . THR B  40  ? 1.5869 2.8214 6.2103 0.0008  -0.3059 -0.3470 150  THR B O   
4871  C  CB  . THR B  40  ? 1.4458 2.6165 5.6566 -0.1447 -0.0738 -0.3598 150  THR B CB  
4872  O  OG1 . THR B  40  ? 1.4412 2.5592 5.6581 -0.1312 0.0107  -0.3753 150  THR B OG1 
4873  C  CG2 . THR B  40  ? 1.4102 2.5064 5.5110 -0.1198 -0.1711 -0.3083 150  THR B CG2 
4874  N  N   . SER B  41  ? 1.5913 2.8395 6.3020 -0.0177 -0.1158 -0.4048 151  SER B N   
4875  C  CA  . SER B  41  ? 1.6375 2.8565 6.4744 0.0544  -0.1611 -0.3960 151  SER B CA  
4876  C  C   . SER B  41  ? 1.5887 2.6827 6.2915 0.0611  -0.1237 -0.3674 151  SER B C   
4877  O  O   . SER B  41  ? 1.6172 2.6604 6.3568 0.1188  -0.1892 -0.3380 151  SER B O   
4878  C  CB  . SER B  41  ? 1.7120 3.0115 6.7681 0.0813  -0.1074 -0.4443 151  SER B CB  
4879  O  OG  . SER B  41  ? 1.6900 2.9815 6.6951 0.0310  0.0267  -0.4775 151  SER B OG  
4880  N  N   . ASN B  42  ? 1.5271 2.5709 6.0680 0.0054  -0.0214 -0.3747 152  ASN B N   
4881  C  CA  . ASN B  42  ? 1.4801 2.4108 5.8847 0.0030  0.0215  -0.3507 152  ASN B CA  
4882  C  C   . ASN B  42  ? 1.5317 2.4087 5.7348 -0.0175 -0.0354 -0.3019 152  ASN B C   
4883  O  O   . ASN B  42  ? 1.5148 2.3708 5.5256 -0.0695 0.0168  -0.3000 152  ASN B O   
4884  C  CB  . ASN B  42  ? 1.4673 2.3715 5.7942 -0.0403 0.1562  -0.3879 152  ASN B CB  
4885  C  CG  . ASN B  42  ? 1.4572 2.2591 5.7370 -0.0280 0.2078  -0.3789 152  ASN B CG  
4886  O  OD1 . ASN B  42  ? 1.4640 2.2208 5.7940 0.0156  0.1478  -0.3438 152  ASN B OD1 
4887  N  ND2 . ASN B  42  ? 1.4572 2.2195 5.6355 -0.0656 0.3171  -0.4098 152  ASN B ND2 
4888  N  N   . PHE B  43  ? 1.7589 2.6132 5.9963 0.0287  -0.1489 -0.2606 153  PHE B N   
4889  C  CA  . PHE B  43  ? 1.6383 2.4458 5.7057 0.0177  -0.2210 -0.2119 153  PHE B CA  
4890  C  C   . PHE B  43  ? 1.6126 2.3241 5.6350 0.0558  -0.2595 -0.1633 153  PHE B C   
4891  O  O   . PHE B  43  ? 1.8289 2.5280 5.9712 0.1192  -0.3257 -0.1486 153  PHE B O   
4892  C  CB  . PHE B  43  ? 1.4798 2.3450 5.5982 0.0342  -0.3369 -0.2033 153  PHE B CB  
4893  C  CG  . PHE B  43  ? 1.6831 2.4806 5.6762 0.0550  -0.4451 -0.1470 153  PHE B CG  
4894  C  CD1 . PHE B  43  ? 1.8115 2.5633 5.5937 0.0107  -0.4311 -0.1196 153  PHE B CD1 
4895  C  CD2 . PHE B  43  ? 1.5650 2.3418 5.6302 0.1234  -0.5627 -0.1211 153  PHE B CD2 
4896  C  CE1 . PHE B  43  ? 1.8828 2.5684 5.5440 0.0303  -0.5295 -0.0672 153  PHE B CE1 
4897  C  CE2 . PHE B  43  ? 1.8901 2.5921 5.8095 0.1450  -0.6630 -0.0683 153  PHE B CE2 
4898  C  CZ  . PHE B  43  ? 2.0035 2.6600 5.7286 0.0963  -0.6455 -0.0413 153  PHE B CZ  
4899  N  N   . ARG B  44  ? 1.3019 1.9487 5.1387 0.0207  -0.2184 -0.1369 154  ARG B N   
4900  C  CA  . ARG B  44  ? 1.2903 1.8491 5.0630 0.0473  -0.2522 -0.0837 154  ARG B CA  
4901  C  C   . ARG B  44  ? 1.2293 1.7574 4.7972 0.0170  -0.2912 -0.0428 154  ARG B C   
4902  O  O   . ARG B  44  ? 1.1718 1.7213 4.5986 -0.0373 -0.2277 -0.0614 154  ARG B O   
4903  C  CB  . ARG B  44  ? 1.2693 1.7767 5.0412 0.0348  -0.1391 -0.0956 154  ARG B CB  
4904  C  CG  . ARG B  44  ? 1.3395 1.8643 5.3076 0.0691  -0.0994 -0.1328 154  ARG B CG  
4905  C  CD  . ARG B  44  ? 1.3323 1.7876 5.2926 0.0594  0.0047  -0.1397 154  ARG B CD  
4906  N  NE  . ARG B  44  ? 1.4044 1.8768 5.5388 0.0869  0.0551  -0.1819 154  ARG B NE  
4907  C  CZ  . ARG B  44  ? 1.4196 1.8371 5.5721 0.0762  0.1580  -0.2040 154  ARG B CZ  
4908  N  NH1 . ARG B  44  ? 1.4777 1.8220 5.4853 0.0376  0.2215  -0.1899 154  ARG B NH1 
4909  N  NH2 . ARG B  44  ? 1.4952 1.9316 5.8041 0.1052  0.1980  -0.2419 154  ARG B NH2 
4910  N  N   . LEU B  45  ? 1.2585 1.7344 4.7853 0.0575  -0.3987 0.0134  155  LEU B N   
4911  C  CA  . LEU B  45  ? 1.2327 1.6734 4.5673 0.0355  -0.4477 0.0567  155  LEU B CA  
4912  C  C   . LEU B  45  ? 1.2218 1.5736 4.4752 0.0671  -0.4779 0.1197  155  LEU B C   
4913  O  O   . LEU B  45  ? 1.4304 1.7338 4.7501 0.1292  -0.5088 0.1404  155  LEU B O   
4914  C  CB  . LEU B  45  ? 1.2707 1.7320 4.5838 0.0525  -0.5661 0.0642  155  LEU B CB  
4915  C  CG  . LEU B  45  ? 1.3849 1.7879 4.6856 0.1253  -0.6987 0.1057  155  LEU B CG  
4916  C  CD1 . LEU B  45  ? 1.4329 1.8543 4.6759 0.1238  -0.7958 0.1035  155  LEU B CD1 
4917  C  CD2 . LEU B  45  ? 1.4773 1.8890 4.9477 0.1874  -0.7101 0.0890  155  LEU B CD2 
4918  N  N   . GLY B  46  ? 1.1529 1.4777 4.2336 0.0299  -0.4650 0.1520  156  GLY B N   
4919  C  CA  . GLY B  46  ? 1.1610 1.4035 4.1414 0.0578  -0.4866 0.2176  156  GLY B CA  
4920  C  C   . GLY B  46  ? 1.1813 1.3729 3.9524 0.0656  -0.5794 0.2707  156  GLY B C   
4921  O  O   . GLY B  46  ? 1.1960 1.4149 3.9209 0.0531  -0.6419 0.2556  156  GLY B O   
4922  N  N   . PHE B  47  ? 1.2043 1.3036 3.8188 0.0882  -0.5806 0.3322  157  PHE B N   
4923  C  CA  . PHE B  47  ? 1.2603 1.2858 3.6192 0.0996  -0.6583 0.3808  157  PHE B CA  
4924  C  C   . PHE B  47  ? 1.2690 1.2088 3.4492 0.0933  -0.6050 0.4364  157  PHE B C   
4925  O  O   . PHE B  47  ? 1.2924 1.1603 3.4742 0.1048  -0.5315 0.4512  157  PHE B O   
4926  C  CB  . PHE B  47  ? 1.4452 1.3789 3.6753 0.1713  -0.7588 0.3988  157  PHE B CB  
4927  C  CG  . PHE B  47  ? 1.5247 1.3757 3.4620 0.1844  -0.8157 0.4370  157  PHE B CG  
4928  C  CD1 . PHE B  47  ? 1.4912 1.3849 3.3721 0.1518  -0.8665 0.4191  157  PHE B CD1 
4929  C  CD2 . PHE B  47  ? 1.6467 1.3704 3.3520 0.2288  -0.8043 0.4853  157  PHE B CD2 
4930  C  CE1 . PHE B  47  ? 1.5708 1.3874 3.1786 0.1659  -0.9042 0.4452  157  PHE B CE1 
4931  C  CE2 . PHE B  47  ? 1.7246 1.3804 3.1577 0.2434  -0.8368 0.5099  157  PHE B CE2 
4932  C  CZ  . PHE B  47  ? 1.6836 1.3886 3.0714 0.2132  -0.8857 0.4879  157  PHE B CZ  
4933  N  N   . GLY B  48  ? 1.5434 1.4782 3.5381 0.0662  -0.6319 0.4606  158  GLY B N   
4934  C  CA  . GLY B  48  ? 1.2387 1.0916 3.0047 0.0492  -0.5778 0.5069  158  GLY B CA  
4935  C  C   . GLY B  48  ? 1.2831 1.1026 2.7993 0.0547  -0.6452 0.5305  158  GLY B C   
4936  O  O   . GLY B  48  ? 1.2524 1.1321 2.7833 0.0382  -0.7039 0.5009  158  GLY B O   
4937  N  N   . SER B  49  ? 1.3703 1.0919 2.6364 0.0723  -0.6180 0.5704  159  SER B N   
4938  C  CA  . SER B  49  ? 1.4351 1.1182 2.4323 0.0859  -0.6527 0.5762  159  SER B CA  
4939  C  C   . SER B  49  ? 1.3904 1.0628 2.2231 0.0521  -0.5807 0.6042  159  SER B C   
4940  O  O   . SER B  49  ? 1.3671 1.0196 2.2370 0.0297  -0.5038 0.6308  159  SER B O   
4941  C  CB  . SER B  49  ? 1.6225 1.1995 2.4554 0.1632  -0.6895 0.5847  159  SER B CB  
4942  O  OG  . SER B  49  ? 1.8523 1.3435 2.6501 0.1918  -0.6351 0.6176  159  SER B OG  
4943  N  N   . PHE B  50  ? 1.3853 1.0698 2.0366 0.0457  -0.5958 0.5913  160  PHE B N   
4944  C  CA  . PHE B  50  ? 1.3476 1.0366 1.8310 0.0197  -0.5301 0.6057  160  PHE B CA  
4945  C  C   . PHE B  50  ? 1.4341 1.0796 1.6732 0.0670  -0.5395 0.5834  160  PHE B C   
4946  O  O   . PHE B  50  ? 1.4991 1.1269 1.7163 0.1025  -0.5964 0.5610  160  PHE B O   
4947  C  CB  . PHE B  50  ? 1.3191 1.1138 1.9054 -0.0569 -0.5062 0.6037  160  PHE B CB  
4948  C  CG  . PHE B  50  ? 1.6729 1.5215 2.2684 -0.0739 -0.5660 0.5653  160  PHE B CG  
4949  C  CD1 . PHE B  50  ? 1.3223 1.2201 2.1402 -0.0856 -0.6214 0.5451  160  PHE B CD1 
4950  C  CD2 . PHE B  50  ? 1.5389 1.3882 1.9319 -0.0768 -0.5531 0.5397  160  PHE B CD2 
4951  C  CE1 . PHE B  50  ? 1.0716 1.0066 1.8905 -0.1096 -0.6640 0.5071  160  PHE B CE1 
4952  C  CE2 . PHE B  50  ? 1.1164 0.9913 1.5092 -0.0956 -0.5935 0.5032  160  PHE B CE2 
4953  C  CZ  . PHE B  50  ? 1.0875 0.9989 1.6847 -0.1168 -0.6506 0.4917  160  PHE B CZ  
4954  N  N   . VAL B  51  ? 1.4397 1.0704 1.5112 0.0723  -0.4725 0.5899  161  VAL B N   
4955  C  CA  . VAL B  51  ? 1.4912 1.1050 1.3672 0.1234  -0.4541 0.5651  161  VAL B CA  
4956  C  C   . VAL B  51  ? 1.3989 1.0669 1.1938 0.0936  -0.3945 0.5449  161  VAL B C   
4957  O  O   . VAL B  51  ? 1.3260 1.0489 1.1191 0.0726  -0.4056 0.5097  161  VAL B O   
4958  C  CB  . VAL B  51  ? 1.6343 1.1657 1.3818 0.2012  -0.4233 0.5928  161  VAL B CB  
4959  C  CG1 . VAL B  51  ? 1.6958 1.2357 1.3218 0.2308  -0.4279 0.5916  161  VAL B CG1 
4960  C  CG2 . VAL B  51  ? 1.7360 1.2132 1.5564 0.2346  -0.4814 0.6103  161  VAL B CG2 
4961  N  N   . GLU B  52  ? 1.5194 1.1674 1.2522 0.0888  -0.3299 0.5644  162  GLU B N   
4962  C  CA  . GLU B  52  ? 1.3488 1.0360 0.9883 0.0766  -0.2689 0.5389  162  GLU B CA  
4963  C  C   . GLU B  52  ? 1.6023 1.2646 1.2260 0.0467  -0.2083 0.5704  162  GLU B C   
4964  O  O   . GLU B  52  ? 2.1645 1.7473 1.7901 0.0640  -0.2037 0.6088  162  GLU B O   
4965  C  CB  . GLU B  52  ? 1.4330 1.1062 0.9463 0.1340  -0.2741 0.5306  162  GLU B CB  
4966  C  CG  . GLU B  52  ? 1.8292 1.5427 1.2700 0.1217  -0.2358 0.5050  162  GLU B CG  
4967  C  CD  . GLU B  52  ? 1.7197 1.5089 1.2168 0.0745  -0.2496 0.4643  162  GLU B CD  
4968  O  OE1 . GLU B  52  ? 1.1927 1.0320 0.6994 0.0339  -0.2098 0.4438  162  GLU B OE1 
4969  O  OE2 . GLU B  52  ? 1.6343 1.4312 1.1664 0.0736  -0.2993 0.4538  162  GLU B OE2 
4970  N  N   . LYS B  53  ? 1.7240 1.4535 1.3289 0.0036  -0.1563 0.5493  163  LYS B N   
4971  C  CA  . LYS B  53  ? 1.8015 1.5313 1.3981 -0.0345 -0.0860 0.5703  163  LYS B CA  
4972  C  C   . LYS B  53  ? 1.5099 1.1046 0.9318 0.0276  -0.0693 0.5697  163  LYS B C   
4973  O  O   . LYS B  53  ? 2.1011 1.6837 1.4230 0.0667  -0.0879 0.5501  163  LYS B O   
4974  C  CB  . LYS B  53  ? 1.5237 1.3721 1.1481 -0.0876 -0.0346 0.5332  163  LYS B CB  
4975  C  CG  . LYS B  53  ? 1.3823 1.3533 1.1623 -0.1598 -0.0292 0.5284  163  LYS B CG  
4976  C  CD  . LYS B  53  ? 1.7015 1.7708 1.4873 -0.1953 0.0294  0.4722  163  LYS B CD  
4977  C  CE  . LYS B  53  ? 0.8438 1.0080 0.7563 -0.2561 0.0498  0.4349  163  LYS B CE  
4978  N  NZ  . LYS B  53  ? 0.8553 1.0046 0.8957 -0.2981 0.0988  0.4319  163  LYS B NZ  
4979  N  N   . PRO B  54  ? 1.9170 1.4291 1.3249 0.0202  -0.0465 0.6124  164  PRO B N   
4980  C  CA  . PRO B  54  ? 2.2318 1.6145 1.4839 0.0607  -0.0509 0.6060  164  PRO B CA  
4981  C  C   . PRO B  54  ? 2.4861 1.9043 1.6778 0.0116  -0.0143 0.5990  164  PRO B C   
4982  O  O   . PRO B  54  ? 1.8306 1.2069 0.9887 -0.0279 0.0112  0.6254  164  PRO B O   
4983  C  CB  . PRO B  54  ? 2.5421 1.8321 1.8190 0.0503  -0.0434 0.6608  164  PRO B CB  
4984  C  CG  . PRO B  54  ? 2.5108 1.9119 1.9714 -0.0237 0.0081  0.6865  164  PRO B CG  
4985  C  CD  . PRO B  54  ? 1.5519 1.0899 1.1140 -0.0360 -0.0195 0.6562  164  PRO B CD  
4986  N  N   . VAL B  55  ? 2.8481 2.3611 2.0420 0.0109  -0.0119 0.5699  165  VAL B N   
4987  C  CA  . VAL B  55  ? 2.0458 1.6146 1.2018 -0.0213 0.0258  0.5648  165  VAL B CA  
4988  C  C   . VAL B  55  ? 1.9492 1.5437 1.0580 0.0063  -0.0220 0.5410  165  VAL B C   
4989  O  O   . VAL B  55  ? 1.8162 1.4223 0.9465 0.0368  -0.0607 0.5141  165  VAL B O   
4990  C  CB  . VAL B  55  ? 1.7117 1.4049 0.9711 -0.0698 0.1025  0.5435  165  VAL B CB  
4991  C  CG1 . VAL B  55  ? 1.3934 1.1928 0.7521 -0.0693 0.0811  0.5087  165  VAL B CG1 
4992  C  CG2 . VAL B  55  ? 1.5852 1.3451 0.8214 -0.0876 0.1459  0.5341  165  VAL B CG2 
4993  N  N   . SER B  56  ? 2.0223 1.6346 1.0767 -0.0066 -0.0137 0.5562  166  SER B N   
4994  C  CA  . SER B  56  ? 2.4637 2.1202 1.4889 0.0090  -0.0433 0.5418  166  SER B CA  
4995  C  C   . SER B  56  ? 2.0020 1.7488 1.0829 0.0122  -0.0180 0.4966  166  SER B C   
4996  O  O   . SER B  56  ? 1.4821 1.3158 0.6482 -0.0097 0.0360  0.4841  166  SER B O   
4997  C  CB  . SER B  56  ? 1.8026 1.4856 0.7720 0.0087  -0.0118 0.5753  166  SER B CB  
4998  O  OG  . SER B  56  ? 1.8450 1.5501 0.7814 0.0412  -0.0453 0.5796  166  SER B OG  
4999  N  N   . PRO B  57  ? 1.8117 1.5670 0.8815 0.0289  -0.0610 0.4722  167  PRO B N   
5000  C  CA  . PRO B  57  ? 2.5062 2.2251 1.5399 0.0355  -0.1243 0.4854  167  PRO B CA  
5001  C  C   . PRO B  57  ? 1.9847 1.6598 1.0595 0.0255  -0.1901 0.4853  167  PRO B C   
5002  O  O   . PRO B  57  ? 2.0959 1.8677 1.2276 0.0342  -0.2253 0.5279  167  PRO B O   
5003  C  CB  . PRO B  57  ? 2.2002 1.9796 1.2304 0.0460  -0.1213 0.4591  167  PRO B CB  
5004  C  CG  . PRO B  57  ? 1.7309 1.5542 0.8191 0.0429  -0.0915 0.4201  167  PRO B CG  
5005  C  CD  . PRO B  57  ? 1.4758 1.3366 0.6196 0.0285  -0.0417 0.4326  167  PRO B CD  
5006  N  N   . PHE B  58  ? 1.6861 1.2869 0.7589 0.0636  -0.1662 0.4534  168  PHE B N   
5007  C  CA  . PHE B  58  ? 1.6798 1.2807 0.7798 0.1732  -0.1592 0.4421  168  PHE B CA  
5008  C  C   . PHE B  58  ? 1.7915 1.7111 1.1460 0.1568  -0.1635 0.5934  168  PHE B C   
5009  O  O   . PHE B  58  ? 1.7581 1.6064 1.0714 0.1841  -0.2132 0.5907  168  PHE B O   
5010  C  CB  . PHE B  58  ? 1.8955 1.5770 1.1089 0.1342  -0.1491 0.4588  168  PHE B CB  
5011  C  CG  . PHE B  58  ? 2.5048 2.2688 1.7636 0.0796  -0.1320 0.4357  168  PHE B CG  
5012  C  CD1 . PHE B  58  ? 2.3951 2.1848 1.6352 0.0874  -0.1444 0.4023  168  PHE B CD1 
5013  C  CD2 . PHE B  58  ? 2.4194 2.2636 1.7751 0.0204  -0.0922 0.4389  168  PHE B CD2 
5014  C  CE1 . PHE B  58  ? 1.7481 1.6327 1.0508 0.0423  -0.1234 0.3783  168  PHE B CE1 
5015  C  CE2 . PHE B  58  ? 1.1818 1.1418 0.6137 -0.0238 -0.0693 0.4083  168  PHE B CE2 
5016  C  CZ  . PHE B  58  ? 1.1693 1.1512 0.5767 -0.0118 -0.0866 0.3787  168  PHE B CZ  
5017  N  N   . VAL B  59  ? 2.0158 1.7827 1.2996 0.0263  -0.2382 0.6145  169  VAL B N   
5018  C  CA  . VAL B  59  ? 2.2244 1.9671 1.4879 0.0961  -0.2341 0.6759  169  VAL B CA  
5019  C  C   . VAL B  59  ? 2.4621 2.1111 1.5757 0.0918  -0.2264 0.6833  169  VAL B C   
5020  O  O   . VAL B  59  ? 1.9132 1.5358 0.9678 0.0553  -0.1894 0.6557  169  VAL B O   
5021  C  CB  . VAL B  59  ? 2.2771 2.0117 1.6226 0.1026  -0.2176 0.7122  169  VAL B CB  
5022  C  CG1 . VAL B  59  ? 2.5384 2.1720 1.8224 0.1667  -0.2435 0.7565  169  VAL B CG1 
5023  C  CG2 . VAL B  59  ? 1.7267 1.3961 1.0237 0.2465  -0.1241 0.6356  169  VAL B CG2 
5024  N  N   . LYS B  60  ? 2.6975 2.2892 1.7297 0.1509  -0.2446 0.7178  170  LYS B N   
5025  C  CA  . LYS B  60  ? 2.5917 2.1175 1.5000 0.1707  -0.2156 0.7312  170  LYS B CA  
5026  C  C   . LYS B  60  ? 2.6083 2.0870 1.5036 0.1492  -0.1811 0.7680  170  LYS B C   
5027  O  O   . LYS B  60  ? 2.3095 1.7580 1.2588 0.1463  -0.2000 0.8007  170  LYS B O   
5028  C  CB  . LYS B  60  ? 2.4071 1.8480 1.2195 0.2401  -0.2414 0.7344  170  LYS B CB  
5029  C  CG  . LYS B  60  ? 2.4078 1.8604 1.1752 0.2634  -0.2525 0.6902  170  LYS B CG  
5030  C  CD  . LYS B  60  ? 2.6017 1.9411 1.2396 0.3284  -0.2721 0.6879  170  LYS B CD  
5031  C  CE  . LYS B  60  ? 2.6167 1.9532 1.2009 0.3523  -0.2772 0.6438  170  LYS B CE  
5032  N  NZ  . LYS B  60  ? 2.5020 1.8869 1.1625 0.3304  -0.3126 0.6109  170  LYS B NZ  
5033  N  N   . THR B  61  ? 2.9513 2.4256 1.7796 0.1401  -0.1233 0.7634  171  THR B N   
5034  C  CA  . THR B  61  ? 3.0536 2.4923 1.8641 0.1133  -0.0705 0.7924  171  THR B CA  
5035  C  C   . THR B  61  ? 2.7186 2.0724 1.4300 0.1613  -0.0465 0.8335  171  THR B C   
5036  O  O   . THR B  61  ? 2.6805 2.0194 1.3549 0.1443  0.0166  0.8536  171  THR B O   
5037  C  CB  . THR B  61  ? 2.8913 2.3963 1.7073 0.0685  -0.0070 0.7592  171  THR B CB  
5038  O  OG1 . THR B  61  ? 2.6537 2.2093 1.4344 0.0977  0.0015  0.7300  171  THR B OG1 
5039  C  CG2 . THR B  61  ? 2.5148 2.0514 1.4039 0.0168  -0.0113 0.7200  171  THR B CG2 
5040  N  N   . THR B  62  ? 2.6260 1.9164 1.2861 0.2194  -0.0908 0.8435  172  THR B N   
5041  C  CA  . THR B  62  ? 2.9537 2.1347 1.5004 0.2676  -0.0721 0.8795  172  THR B CA  
5042  C  C   . THR B  62  ? 3.2915 2.3907 1.8578 0.2684  -0.0887 0.9222  172  THR B C   
5043  O  O   . THR B  62  ? 3.3899 2.5014 2.0423 0.2642  -0.1418 0.9208  172  THR B O   
5044  C  CB  . THR B  62  ? 3.2039 2.3287 1.6586 0.3337  -0.1103 0.8627  172  THR B CB  
5045  O  OG1 . THR B  62  ? 2.9878 2.1096 1.4963 0.3450  -0.1813 0.8480  172  THR B OG1 
5046  C  CG2 . THR B  62  ? 3.0555 2.2470 1.4869 0.3403  -0.0886 0.8237  172  THR B CG2 
5047  N  N   . PRO B  63  ? 3.0528 2.0688 1.5460 0.2755  -0.0404 0.9617  173  PRO B N   
5048  C  CA  . PRO B  63  ? 3.1296 2.0605 1.6457 0.2729  -0.0484 1.0031  173  PRO B CA  
5049  C  C   . PRO B  63  ? 3.1941 2.0613 1.7174 0.3228  -0.1266 1.0098  173  PRO B C   
5050  O  O   . PRO B  63  ? 3.1818 2.0214 1.7838 0.3141  -0.1498 1.0324  173  PRO B O   
5051  C  CB  . PRO B  63  ? 3.6602 2.4939 2.0570 0.2888  0.0173  1.0410  173  PRO B CB  
5052  C  CG  . PRO B  63  ? 3.6307 2.4814 1.9303 0.3214  0.0396  1.0213  173  PRO B CG  
5053  C  CD  . PRO B  63  ? 3.1708 2.1604 1.5565 0.2905  0.0257  0.9727  173  PRO B CD  
5054  N  N   . GLU B  64  ? 3.2719 2.1105 1.7158 0.3759  -0.1667 0.9882  174  GLU B N   
5055  C  CA  . GLU B  64  ? 3.3488 2.1255 1.7903 0.4228  -0.2408 0.9879  174  GLU B CA  
5056  C  C   . GLU B  64  ? 3.1579 2.0409 1.7399 0.4020  -0.2895 0.9572  174  GLU B C   
5057  O  O   . GLU B  64  ? 3.1573 2.0234 1.8107 0.4178  -0.3348 0.9677  174  GLU B O   
5058  C  CB  . GLU B  64  ? 3.5340 2.2181 1.8172 0.4858  -0.2646 0.9719  174  GLU B CB  
5059  C  CG  . GLU B  64  ? 3.7142 2.3291 1.9767 0.5332  -0.3473 0.9607  174  GLU B CG  
5060  C  CD  . GLU B  64  ? 3.8685 2.3778 1.9604 0.5921  -0.3730 0.9395  174  GLU B CD  
5061  O  OE1 . GLU B  64  ? 3.9111 2.3876 1.8961 0.6047  -0.3201 0.9432  174  GLU B OE1 
5062  O  OE2 . GLU B  64  ? 3.9039 2.3605 1.9681 0.6266  -0.4461 0.9174  174  GLU B OE2 
5063  N  N   . GLU B  65  ? 3.5551 2.5461 2.1777 0.3707  -0.2772 0.9194  175  GLU B N   
5064  C  CA  . GLU B  65  ? 3.0728 2.1633 1.8138 0.3525  -0.3141 0.8875  175  GLU B CA  
5065  C  C   . GLU B  65  ? 2.6816 1.8635 1.5762 0.2974  -0.2933 0.9014  175  GLU B C   
5066  O  O   . GLU B  65  ? 2.5177 1.7933 1.5177 0.2820  -0.3091 0.8780  175  GLU B O   
5067  C  CB  . GLU B  65  ? 2.7890 1.9400 1.4954 0.3463  -0.3091 0.8403  175  GLU B CB  
5068  C  CG  . GLU B  65  ? 3.3594 2.5626 2.1287 0.3500  -0.3570 0.8005  175  GLU B CG  
5069  C  CD  . GLU B  65  ? 3.3809 2.5917 2.0772 0.3601  -0.3595 0.7553  175  GLU B CD  
5070  O  OE1 . GLU B  65  ? 3.2998 2.4334 1.8681 0.3939  -0.3463 0.7553  175  GLU B OE1 
5071  O  OE2 . GLU B  65  ? 3.2313 2.5189 1.9952 0.3381  -0.3706 0.7208  175  GLU B OE2 
5072  N  N   . ILE B  66  ? 2.6776 1.8244 1.5771 0.2681  -0.2538 0.9357  176  ILE B N   
5073  C  CA  . ILE B  66  ? 2.5438 1.7388 1.5759 0.2167  -0.2405 0.9464  176  ILE B CA  
5074  C  C   . ILE B  66  ? 2.6382 1.7833 1.7513 0.2540  -0.2696 0.9740  176  ILE B C   
5075  O  O   . ILE B  66  ? 2.8681 2.0850 2.1184 0.2544  -0.2736 0.9525  176  ILE B O   
5076  C  CB  . ILE B  66  ? 2.5735 1.7321 1.5532 0.1626  -0.1786 0.9571  176  ILE B CB  
5077  C  CG1 . ILE B  66  ? 2.5195 1.7436 1.4328 0.1360  -0.1373 0.9186  176  ILE B CG1 
5078  C  CG2 . ILE B  66  ? 2.4739 1.6400 1.5601 0.1079  -0.1631 0.9393  176  ILE B CG2 
5079  C  CD1 . ILE B  66  ? 2.5659 1.7724 1.4262 0.0947  -0.0563 0.9240  176  ILE B CD1 
5080  N  N   . ALA B  67  ? 2.7905 1.8097 1.8128 0.2963  -0.2795 1.0130  177  ALA B N   
5081  C  CA  . ALA B  67  ? 2.8721 1.8244 1.9503 0.3423  -0.3124 1.0411  177  ALA B CA  
5082  C  C   . ALA B  67  ? 2.9126 1.8643 1.9748 0.4039  -0.3723 1.0143  177  ALA B C   
5083  O  O   . ALA B  67  ? 2.9411 1.8660 2.0708 0.4427  -0.4027 1.0212  177  ALA B O   
5084  C  CB  . ALA B  67  ? 3.0936 1.8975 2.0601 0.3638  -0.2994 1.0804  177  ALA B CB  
5085  N  N   . ASN B  68  ? 2.9329 1.8988 1.8971 0.4127  -0.3919 0.9773  178  ASN B N   
5086  C  CA  . ASN B  68  ? 2.9875 1.9340 1.9155 0.4561  -0.4587 0.9393  178  ASN B CA  
5087  C  C   . ASN B  68  ? 2.8742 1.9038 1.7870 0.4318  -0.4577 0.8902  178  ASN B C   
5088  O  O   . ASN B  68  ? 2.9701 1.9553 1.7563 0.4434  -0.4623 0.8723  178  ASN B O   
5089  C  CB  . ASN B  68  ? 3.2399 2.0423 2.0109 0.5095  -0.5011 0.9479  178  ASN B CB  
5090  C  CG  . ASN B  68  ? 3.3125 2.0810 2.0426 0.5458  -0.5817 0.9047  178  ASN B CG  
5091  O  OD1 . ASN B  68  ? 3.2173 2.0397 2.0539 0.5431  -0.6180 0.8811  178  ASN B OD1 
5092  N  ND2 . ASN B  68  ? 3.4893 2.1615 2.0595 0.5786  -0.6098 0.8900  178  ASN B ND2 
5093  N  N   . PRO B  69  ? 2.6813 1.8222 1.7145 0.4040  -0.4478 0.8649  179  PRO B N   
5094  C  CA  . PRO B  69  ? 2.7214 1.9358 1.7412 0.3797  -0.4456 0.8175  179  PRO B CA  
5095  C  C   . PRO B  69  ? 2.8487 2.0028 1.7904 0.4081  -0.5146 0.7728  179  PRO B C   
5096  O  O   . PRO B  69  ? 2.6237 1.8136 1.5380 0.3916  -0.5148 0.7336  179  PRO B O   
5097  C  CB  . PRO B  69  ? 2.4884 1.8158 1.6478 0.3514  -0.4146 0.8032  179  PRO B CB  
5098  C  CG  . PRO B  69  ? 2.3960 1.6841 1.6279 0.3791  -0.4270 0.8227  179  PRO B CG  
5099  C  CD  . PRO B  69  ? 2.5585 1.7528 1.7350 0.3983  -0.4263 0.8767  179  PRO B CD  
5100  N  N   . CYS B  70  ? 2.8281 1.8870 1.7350 0.4484  -0.5761 0.7764  180  CYS B N   
5101  C  CA  . CYS B  70  ? 2.9553 1.9370 1.7748 0.4735  -0.6496 0.7363  180  CYS B CA  
5102  C  C   . CYS B  70  ? 3.1599 2.0273 1.8124 0.5102  -0.6566 0.7458  180  CYS B C   
5103  O  O   . CYS B  70  ? 3.3228 2.0906 1.8859 0.5451  -0.7241 0.7244  180  CYS B O   
5104  C  CB  . CYS B  70  ? 3.0157 1.9565 1.8894 0.4963  -0.7245 0.7277  180  CYS B CB  
5105  S  SG  . CYS B  70  ? 3.4458 2.4998 2.5016 0.4601  -0.7255 0.7036  180  CYS B SG  
5106  N  N   . SER B  71  ? 3.1645 2.0379 1.7683 0.5036  -0.5898 0.7746  181  SER B N   
5107  C  CA  . SER B  71  ? 3.3623 2.1242 1.7981 0.5418  -0.5859 0.7802  181  SER B CA  
5108  C  C   . SER B  71  ? 3.3861 2.1322 1.7415 0.5484  -0.6029 0.7297  181  SER B C   
5109  O  O   . SER B  71  ? 3.2437 2.0677 1.6756 0.5175  -0.6122 0.6943  181  SER B O   
5110  C  CB  . SER B  71  ? 3.3557 2.1316 1.7681 0.5282  -0.5066 0.8204  181  SER B CB  
5111  O  OG  . SER B  71  ? 3.5579 2.2208 1.8008 0.5707  -0.4954 0.8256  181  SER B OG  
5112  N  N   . SER B  72  ? 3.8959 2.5276 2.0885 0.5928  -0.6065 0.7263  182  SER B N   
5113  C  CA  . SER B  72  ? 4.0714 2.6532 2.1573 0.6137  -0.6198 0.6825  182  SER B CA  
5114  C  C   . SER B  72  ? 4.0246 2.5583 2.1057 0.6208  -0.7056 0.6386  182  SER B C   
5115  O  O   . SER B  72  ? 4.0196 2.4961 2.0106 0.6382  -0.7244 0.6000  182  SER B O   
5116  C  CB  . SER B  72  ? 3.7266 2.4159 1.8612 0.5797  -0.5587 0.6647  182  SER B CB  
5117  O  OG  . SER B  72  ? 3.7921 2.4266 1.8340 0.6030  -0.5775 0.6205  182  SER B OG  
5118  N  N   . ILE B  73  ? 3.7975 2.3446 1.9699 0.6102  -0.7595 0.6426  183  ILE B N   
5119  C  CA  . ILE B  73  ? 3.7230 2.2230 1.8987 0.6131  -0.8467 0.6011  183  ILE B CA  
5120  C  C   . ILE B  73  ? 3.9840 2.3285 2.0235 0.6694  -0.9173 0.6007  183  ILE B C   
5121  O  O   . ILE B  73  ? 4.1160 2.3664 2.0511 0.6913  -0.9672 0.5630  183  ILE B O   
5122  C  CB  . ILE B  73  ? 3.5974 2.1959 1.9501 0.5738  -0.8727 0.6000  183  ILE B CB  
5123  C  CG1 . ILE B  73  ? 3.5833 2.3275 2.0573 0.5215  -0.8011 0.6002  183  ILE B CG1 
5124  C  CG2 . ILE B  73  ? 3.6198 2.1697 1.9820 0.5716  -0.9656 0.5555  183  ILE B CG2 
5125  C  CD1 . ILE B  73  ? 3.5141 2.3535 2.1560 0.4871  -0.8133 0.6012  183  ILE B CD1 
5126  N  N   . PRO B  74  ? 4.0728 2.3797 2.1060 0.6955  -0.9236 0.6423  184  PRO B N   
5127  C  CA  . PRO B  74  ? 3.9687 2.3507 2.1109 0.6801  -0.8777 0.6915  184  PRO B CA  
5128  C  C   . PRO B  74  ? 3.9031 2.3282 2.1863 0.6697  -0.9348 0.6927  184  PRO B C   
5129  O  O   . PRO B  74  ? 3.9994 2.3668 2.2684 0.6864  -1.0222 0.6619  184  PRO B O   
5130  C  CB  . PRO B  74  ? 4.1835 2.4459 2.1847 0.7305  -0.8640 0.7301  184  PRO B CB  
5131  C  CG  . PRO B  74  ? 4.4136 2.5349 2.2756 0.7788  -0.9495 0.6994  184  PRO B CG  
5132  C  CD  . PRO B  74  ? 4.3488 2.4929 2.2133 0.7566  -0.9769 0.6431  184  PRO B CD  
5133  N  N   . TYR B  75  ? 3.7476 2.2697 2.1667 0.6440  -0.8870 0.7263  185  TYR B N   
5134  C  CA  . TYR B  75  ? 3.6916 2.2526 2.2486 0.6423  -0.9314 0.7308  185  TYR B CA  
5135  C  C   . TYR B  75  ? 3.5803 2.2070 2.2382 0.6296  -0.8599 0.7809  185  TYR B C   
5136  O  O   . TYR B  75  ? 3.4704 2.1567 2.1369 0.6001  -0.7782 0.7997  185  TYR B O   
5137  C  CB  . TYR B  75  ? 3.5349 2.1822 2.2080 0.6022  -0.9659 0.6829  185  TYR B CB  
5138  C  CG  . TYR B  75  ? 3.4968 2.1770 2.3105 0.6047  -1.0217 0.6790  185  TYR B CG  
5139  C  CD1 . TYR B  75  ? 3.6759 2.2675 2.4607 0.6456  -1.1170 0.6696  185  TYR B CD1 
5140  C  CD2 . TYR B  75  ? 3.2962 2.0936 2.2712 0.5693  -0.9813 0.6814  185  TYR B CD2 
5141  C  CE1 . TYR B  75  ? 3.6449 2.2728 2.5697 0.6509  -1.1710 0.6635  185  TYR B CE1 
5142  C  CE2 . TYR B  75  ? 3.2804 2.1065 2.3885 0.5752  -1.0313 0.6736  185  TYR B CE2 
5143  C  CZ  . TYR B  75  ? 3.4358 2.1819 2.5245 0.6157  -1.1262 0.6652  185  TYR B CZ  
5144  O  OH  . TYR B  75  ? 3.4086 2.1914 2.6427 0.6237  -1.1779 0.6555  185  TYR B OH  
5145  N  N   . PHE B  76  ? 3.6192 2.2292 2.3545 0.6536  -0.8937 0.8015  186  PHE B N   
5146  C  CA  . PHE B  76  ? 3.5350 2.1873 2.3720 0.6480  -0.8319 0.8485  186  PHE B CA  
5147  C  C   . PHE B  76  ? 3.3187 2.0921 2.3329 0.6144  -0.8211 0.8267  186  PHE B C   
5148  O  O   . PHE B  76  ? 3.3217 2.1032 2.4075 0.6242  -0.8919 0.7953  186  PHE B O   
5149  C  CB  . PHE B  76  ? 3.7251 2.2722 2.5355 0.7022  -0.8686 0.8852  186  PHE B CB  
5150  C  CG  . PHE B  76  ? 3.6610 2.2300 2.5725 0.6993  -0.8039 0.9348  186  PHE B CG  
5151  C  CD1 . PHE B  76  ? 3.6863 2.2235 2.5422 0.6861  -0.7271 0.9813  186  PHE B CD1 
5152  C  CD2 . PHE B  76  ? 3.5848 2.1980 2.6472 0.7089  -0.8198 0.9317  186  PHE B CD2 
5153  C  CE1 . PHE B  76  ? 3.6372 2.1808 2.5885 0.6777  -0.6685 1.0264  186  PHE B CE1 
5154  C  CE2 . PHE B  76  ? 3.5379 2.1556 2.6900 0.7100  -0.7548 0.9749  186  PHE B CE2 
5155  C  CZ  . PHE B  76  ? 3.5639 2.1445 2.6631 0.6921  -0.6792 1.0242  186  PHE B CZ  
5156  N  N   . CYS B  77  ? 3.1405 2.0033 2.2232 0.5750  -0.7353 0.8405  187  CYS B N   
5157  C  CA  . CYS B  77  ? 2.9668 1.9302 2.2000 0.5471  -0.7150 0.8178  187  CYS B CA  
5158  C  C   . CYS B  77  ? 2.8379 1.8419 2.1363 0.5314  -0.6180 0.8579  187  CYS B C   
5159  O  O   . CYS B  77  ? 2.8835 1.8604 2.1219 0.5255  -0.5658 0.9019  187  CYS B O   
5160  C  CB  . CYS B  77  ? 2.8849 1.9251 2.1280 0.5042  -0.7249 0.7638  187  CYS B CB  
5161  S  SG  . CYS B  77  ? 2.8005 1.8867 1.9578 0.4686  -0.6502 0.7681  187  CYS B SG  
5162  N  N   . LEU B  78  ? 2.7515 1.8109 2.1722 0.5209  -0.5985 0.8371  188  LEU B N   
5163  C  CA  . LEU B  78  ? 2.6354 1.7142 2.1155 0.5094  -0.5060 0.8614  188  LEU B CA  
5164  C  C   . LEU B  78  ? 2.8312 1.9817 2.2773 0.4650  -0.4340 0.8636  188  LEU B C   
5165  O  O   . LEU B  78  ? 2.9600 2.1681 2.3718 0.4393  -0.4567 0.8272  188  LEU B O   
5166  C  CB  . LEU B  78  ? 2.6945 1.7981 2.2907 0.5041  -0.5153 0.8160  188  LEU B CB  
5167  C  CG  . LEU B  78  ? 2.8930 1.9616 2.5650 0.5401  -0.5978 0.8024  188  LEU B CG  
5168  C  CD1 . LEU B  78  ? 2.6127 1.7262 2.4290 0.5189  -0.6016 0.7574  188  LEU B CD1 
5169  C  CD2 . LEU B  78  ? 3.0386 2.0047 2.6765 0.5948  -0.5918 0.8590  188  LEU B CD2 
5170  N  N   . PRO B  79  ? 2.5494 1.6984 2.0119 0.4466  -0.3485 0.8946  189  PRO B N   
5171  C  CA  . PRO B  79  ? 2.3924 1.6261 1.8446 0.3926  -0.2843 0.8794  189  PRO B CA  
5172  C  C   . PRO B  79  ? 2.1798 1.4514 1.6388 0.3789  -0.2677 0.8075  189  PRO B C   
5173  O  O   . PRO B  79  ? 2.1579 1.3978 1.6635 0.3903  -0.3098 0.7787  189  PRO B O   
5174  C  CB  . PRO B  79  ? 2.4319 1.6498 1.9369 0.3607  -0.2149 0.9183  189  PRO B CB  
5175  C  CG  . PRO B  79  ? 2.4251 1.5355 1.9543 0.4126  -0.2098 0.9201  189  PRO B CG  
5176  C  CD  . PRO B  79  ? 2.5336 1.6061 2.0371 0.4618  -0.3099 0.9304  189  PRO B CD  
5177  N  N   . THR B  80  ? 2.0806 1.4238 1.5080 0.3428  -0.2233 0.7829  190  THR B N   
5178  C  CA  . THR B  80  ? 2.5123 1.8718 1.9315 0.3121  -0.2253 0.7160  190  THR B CA  
5179  C  C   . THR B  80  ? 2.3667 1.6359 1.7920 0.2648  -0.1950 0.6965  190  THR B C   
5180  O  O   . THR B  80  ? 2.6690 1.8571 2.0220 0.2339  -0.1464 0.7023  190  THR B O   
5181  C  CB  . THR B  80  ? 2.0590 1.5073 1.4324 0.2893  -0.2000 0.6941  190  THR B CB  
5182  O  OG1 . THR B  80  ? 2.4328 1.9444 1.8094 0.2973  -0.2534 0.7276  190  THR B OG1 
5183  C  CG2 . THR B  80  ? 1.7548 1.2316 1.1447 0.2460  -0.2174 0.6379  190  THR B CG2 
5184  N  N   . PHE B  81  ? 1.8501 1.1583 1.4195 0.2173  -0.2514 0.6909  191  PHE B N   
5185  C  CA  . PHE B  81  ? 1.7805 1.1067 1.4976 0.1326  -0.2324 0.7076  191  PHE B CA  
5186  C  C   . PHE B  81  ? 1.5960 1.0632 1.4613 0.0655  -0.2533 0.6849  191  PHE B C   
5187  O  O   . PHE B  81  ? 1.5541 1.0673 1.4353 0.0828  -0.3137 0.6555  191  PHE B O   
5188  C  CB  . PHE B  81  ? 1.8613 1.1155 1.6950 0.1497  -0.2590 0.7329  191  PHE B CB  
5189  C  CG  . PHE B  81  ? 1.8504 1.1368 1.7858 0.1845  -0.3470 0.7130  191  PHE B CG  
5190  C  CD1 . PHE B  81  ? 1.9694 1.2091 1.7973 0.2664  -0.3853 0.7113  191  PHE B CD1 
5191  C  CD2 . PHE B  81  ? 1.7172 1.0965 1.8755 0.1320  -0.3815 0.6983  191  PHE B CD2 
5192  C  CE1 . PHE B  81  ? 1.9647 1.2426 1.8923 0.2853  -0.4664 0.6898  191  PHE B CE1 
5193  C  CE2 . PHE B  81  ? 1.7145 1.1240 1.9743 0.1571  -0.4644 0.6737  191  PHE B CE2 
5194  C  CZ  . PHE B  81  ? 1.8428 1.1986 1.9796 0.2300  -0.5106 0.6668  191  PHE B CZ  
5195  N  N   . GLY B  82  ? 1.7087 1.2466 1.6807 -0.0137 -0.1906 0.6972  192  GLY B N   
5196  C  CA  . GLY B  82  ? 1.3266 0.9954 1.4351 -0.0800 -0.1903 0.6801  192  GLY B CA  
5197  C  C   . GLY B  82  ? 1.2822 0.9685 1.5976 -0.0867 -0.2501 0.6803  192  GLY B C   
5198  O  O   . GLY B  82  ? 1.2528 0.9848 1.5903 -0.0804 -0.3193 0.6586  192  GLY B O   
5199  N  N   . PHE B  83  ? 1.3044 0.9519 1.7795 -0.0984 -0.2184 0.6924  193  PHE B N   
5200  C  CA  . PHE B  83  ? 1.2642 0.9359 1.9612 -0.0970 -0.2615 0.6680  193  PHE B CA  
5201  C  C   . PHE B  83  ? 1.3565 0.9398 2.1564 -0.0710 -0.2345 0.6782  193  PHE B C   
5202  O  O   . PHE B  83  ? 1.3723 0.9338 2.1670 -0.1090 -0.1364 0.6767  193  PHE B O   
5203  C  CB  . PHE B  83  ? 1.1005 0.9250 1.9395 -0.1792 -0.1994 0.5909  193  PHE B CB  
5204  C  CG  . PHE B  83  ? 1.0643 0.9290 2.1434 -0.1889 -0.1907 0.5412  193  PHE B CG  
5205  C  CD1 . PHE B  83  ? 1.0773 0.9479 2.2652 -0.1447 -0.2880 0.5348  193  PHE B CD1 
5206  C  CD2 . PHE B  83  ? 1.1588 1.0572 2.3577 -0.2416 -0.0853 0.4987  193  PHE B CD2 
5207  C  CE1 . PHE B  83  ? 1.0455 0.9647 2.4657 -0.1502 -0.2764 0.4877  193  PHE B CE1 
5208  C  CE2 . PHE B  83  ? 1.4107 1.3443 2.8274 -0.2453 -0.0724 0.4522  193  PHE B CE2 
5209  C  CZ  . PHE B  83  ? 1.1361 1.0849 2.6682 -0.1980 -0.1663 0.4471  193  PHE B CZ  
5210  N  N   . LYS B  84  ? 1.4258 0.9669 2.3064 -0.0060 -0.3201 0.6766  194  LYS B N   
5211  C  CA  . LYS B  84  ? 1.5277 0.9884 2.5004 0.0323  -0.3075 0.6770  194  LYS B CA  
5212  C  C   . LYS B  84  ? 1.4528 0.9827 2.7013 0.0309  -0.3354 0.6351  194  LYS B C   
5213  O  O   . LYS B  84  ? 1.4325 1.0162 2.7358 0.0606  -0.4298 0.6180  194  LYS B O   
5214  C  CB  . LYS B  84  ? 1.9499 1.2988 2.7310 0.1198  -0.3726 0.6967  194  LYS B CB  
5215  C  CG  . LYS B  84  ? 1.8182 1.0764 2.3376 0.1296  -0.3245 0.7302  194  LYS B CG  
5216  C  CD  . LYS B  84  ? 2.0196 1.1530 2.3545 0.2207  -0.3709 0.7440  194  LYS B CD  
5217  C  CE  . LYS B  84  ? 2.1324 1.1662 2.2188 0.2345  -0.3107 0.7735  194  LYS B CE  
5218  N  NZ  . LYS B  84  ? 2.6840 1.5947 2.5965 0.3308  -0.3331 0.7931  194  LYS B NZ  
5219  N  N   . HIS B  85  ? 1.4209 0.9762 2.8148 -0.0086 -0.2417 0.5930  195  HIS B N   
5220  C  CA  . HIS B  85  ? 1.3912 1.0197 3.0335 -0.0038 -0.2482 0.5368  195  HIS B CA  
5221  C  C   . HIS B  85  ? 1.8101 1.3136 3.5004 0.0924  -0.3147 0.5719  195  HIS B C   
5222  O  O   . HIS B  85  ? 1.6363 1.0411 3.2778 0.1052  -0.2560 0.5845  195  HIS B O   
5223  C  CB  . HIS B  85  ? 1.5153 1.2171 3.2800 -0.0837 -0.1176 0.4740  195  HIS B CB  
5224  C  CG  . HIS B  85  ? 1.3849 1.1485 3.4007 -0.0731 -0.1101 0.4181  195  HIS B CG  
5225  N  ND1 . HIS B  85  ? 1.1737 1.0527 3.3395 -0.0671 -0.1714 0.3818  195  HIS B ND1 
5226  C  CD2 . HIS B  85  ? 1.6408 1.3650 3.7852 -0.0657 -0.0463 0.3919  195  HIS B CD2 
5227  C  CE1 . HIS B  85  ? 1.1683 1.0875 3.5522 -0.0559 -0.1427 0.3352  195  HIS B CE1 
5228  N  NE2 . HIS B  85  ? 1.2470 1.0704 3.6181 -0.0516 -0.0680 0.3402  195  HIS B NE2 
5229  N  N   . ILE B  86  ? 1.8179 1.3619 3.5449 0.1469  -0.4261 0.5611  196  ILE B N   
5230  C  CA  . ILE B  86  ? 1.7340 1.1975 3.4139 0.2278  -0.4866 0.5681  196  ILE B CA  
5231  C  C   . ILE B  86  ? 1.7178 1.2355 3.6671 0.2449  -0.4781 0.5221  196  ILE B C   
5232  O  O   . ILE B  86  ? 1.8779 1.3089 3.8390 0.2782  -0.4379 0.5262  196  ILE B O   
5233  C  CB  . ILE B  86  ? 1.8612 1.3239 3.3925 0.2723  -0.6003 0.5745  196  ILE B CB  
5234  C  CG1 . ILE B  86  ? 1.8331 1.2425 3.0885 0.2590  -0.5920 0.6114  196  ILE B CG1 
5235  C  CG2 . ILE B  86  ? 2.1577 1.5284 3.6291 0.3582  -0.6550 0.5822  196  ILE B CG2 
5236  C  CD1 . ILE B  86  ? 1.9314 1.3185 3.0048 0.3047  -0.6785 0.6125  196  ILE B CD1 
5237  N  N   . LEU B  87  ? 1.5904 1.2501 3.7512 0.2217  -0.5092 0.4752  197  LEU B N   
5238  C  CA  . LEU B  87  ? 1.5826 1.3138 3.9988 0.2420  -0.5073 0.4236  197  LEU B CA  
5239  C  C   . LEU B  87  ? 1.4055 1.2547 4.0678 0.1776  -0.4069 0.3697  197  LEU B C   
5240  O  O   . LEU B  87  ? 1.2678 1.2446 3.9871 0.1196  -0.4069 0.3387  197  LEU B O   
5241  C  CB  . LEU B  87  ? 1.6195 1.4195 4.0818 0.2732  -0.6226 0.4010  197  LEU B CB  
5242  C  CG  . LEU B  87  ? 1.6253 1.5081 4.3436 0.2935  -0.6246 0.3458  197  LEU B CG  
5243  C  CD1 . LEU B  87  ? 1.7829 1.5570 4.4838 0.3623  -0.6072 0.3607  197  LEU B CD1 
5244  C  CD2 . LEU B  87  ? 1.6629 1.6117 4.4153 0.3103  -0.7323 0.3223  197  LEU B CD2 
5245  N  N   . PRO B  88  ? 1.5822 1.3963 4.3444 0.1720  -0.3068 0.3460  198  PRO B N   
5246  C  CA  . PRO B  88  ? 1.2922 1.2433 4.2365 0.0974  -0.2012 0.2674  198  PRO B CA  
5247  C  C   . PRO B  88  ? 1.2460 1.3316 4.4486 0.1269  -0.2564 0.2204  198  PRO B C   
5248  O  O   . PRO B  88  ? 1.3764 1.4211 4.5833 0.1915  -0.3380 0.2292  198  PRO B O   
5249  C  CB  . PRO B  88  ? 1.3728 1.2239 4.3329 0.1017  -0.0998 0.2573  198  PRO B CB  
5250  C  CG  . PRO B  88  ? 1.6566 1.3259 4.3839 0.1394  -0.1233 0.3330  198  PRO B CG  
5251  C  CD  . PRO B  88  ? 1.8849 1.5397 4.5175 0.2077  -0.2678 0.3797  198  PRO B CD  
5252  N  N   . LEU B  89  ? 1.1272 1.3429 4.3967 0.0425  -0.1948 0.1584  199  LEU B N   
5253  C  CA  . LEU B  89  ? 1.3059 1.5866 4.6551 0.0435  -0.2300 0.1091  199  LEU B CA  
5254  C  C   . LEU B  89  ? 1.2651 1.5465 4.8005 0.0878  -0.2058 0.0752  199  LEU B C   
5255  O  O   . LEU B  89  ? 1.2253 1.4930 4.8215 0.0679  -0.0961 0.0430  199  LEU B O   
5256  C  CB  . LEU B  89  ? 1.0921 1.4288 4.3244 -0.0285 -0.1510 0.0547  199  LEU B CB  
5257  C  CG  . LEU B  89  ? 1.0710 1.4029 4.2239 -0.0722 -0.0101 0.0046  199  LEU B CG  
5258  C  CD1 . LEU B  89  ? 1.1505 1.5236 4.4432 -0.0666 0.0378  -0.0576 199  LEU B CD1 
5259  C  CD2 . LEU B  89  ? 1.0167 1.3698 3.9045 -0.1259 0.0284  -0.0069 199  LEU B CD2 
5260  N  N   . THR B  90  ? 1.3613 1.6540 4.9636 0.1482  -0.3088 0.0798  200  THR B N   
5261  C  CA  . THR B  90  ? 1.5582 1.8555 5.3166 0.2018  -0.3036 0.0516  200  THR B CA  
5262  C  C   . THR B  90  ? 1.5344 1.9144 5.3848 0.2215  -0.3859 0.0224  200  THR B C   
5263  O  O   . THR B  90  ? 1.4563 1.8643 5.2306 0.2050  -0.4604 0.0334  200  THR B O   
5264  C  CB  . THR B  90  ? 1.7377 1.9096 5.4215 0.2892  -0.3498 0.1046  200  THR B CB  
5265  O  OG1 . THR B  90  ? 1.7849 1.8999 5.3004 0.3327  -0.4752 0.1588  200  THR B OG1 
5266  C  CG2 . THR B  90  ? 1.7471 1.8185 5.3441 0.2723  -0.2512 0.1290  200  THR B CG2 
5267  N  N   . ASN B  91  ? 1.5495 1.9668 5.5648 0.2590  -0.3694 -0.0159 201  ASN B N   
5268  C  CA  . ASN B  91  ? 1.6077 2.1122 5.7343 0.2829  -0.4431 -0.0458 201  ASN B CA  
5269  C  C   . ASN B  91  ? 1.7296 2.1878 5.7852 0.3625  -0.5877 -0.0010 201  ASN B C   
5270  O  O   . ASN B  91  ? 1.7647 2.2837 5.8471 0.3673  -0.6709 -0.0126 201  ASN B O   
5271  C  CB  . ASN B  91  ? 1.6564 2.2219 5.9801 0.3015  -0.3791 -0.1009 201  ASN B CB  
5272  C  CG  . ASN B  91  ? 1.7562 2.2414 6.1078 0.3742  -0.3643 -0.0833 201  ASN B CG  
5273  O  OD1 . ASN B  91  ? 2.0167 2.4201 6.2774 0.4494  -0.4538 -0.0348 201  ASN B OD1 
5274  N  ND2 . ASN B  91  ? 1.7443 2.2354 6.1909 0.3551  -0.2472 -0.1230 201  ASN B ND2 
5275  N  N   . ASP B  92  ? 1.8221 2.1602 5.7622 0.4268  -0.6140 0.0491  202  ASP B N   
5276  C  CA  . ASP B  92  ? 1.9732 2.2362 5.7821 0.5080  -0.7424 0.0939  202  ASP B CA  
5277  C  C   . ASP B  92  ? 1.9308 2.2000 5.6010 0.4720  -0.8196 0.1158  202  ASP B C   
5278  O  O   . ASP B  92  ? 1.8757 2.0752 5.3704 0.4404  -0.8045 0.1558  202  ASP B O   
5279  C  CB  . ASP B  92  ? 2.0887 2.1867 5.7177 0.5701  -0.7349 0.1509  202  ASP B CB  
5280  C  CG  . ASP B  92  ? 2.2093 2.2730 5.9448 0.6298  -0.6840 0.1340  202  ASP B CG  
5281  O  OD1 . ASP B  92  ? 2.2002 2.3269 6.0967 0.5849  -0.5779 0.0894  202  ASP B OD1 
5282  O  OD2 . ASP B  92  ? 2.3769 2.3408 6.0178 0.7237  -0.7465 0.1651  202  ASP B OD2 
5283  N  N   . ALA B  93  ? 1.9655 2.3155 5.7099 0.4773  -0.9004 0.0892  203  ALA B N   
5284  C  CA  . ALA B  93  ? 1.9219 2.2875 5.5573 0.4326  -0.9612 0.0978  203  ALA B CA  
5285  C  C   . ALA B  93  ? 2.0658 2.3334 5.4964 0.4946  -1.0810 0.1448  203  ALA B C   
5286  O  O   . ALA B  93  ? 2.0363 2.2693 5.3014 0.4606  -1.1161 0.1679  203  ALA B O   
5287  C  CB  . ALA B  93  ? 1.8853 2.3869 5.7005 0.3929  -0.9696 0.0397  203  ALA B CB  
5288  N  N   . GLU B  94  ? 2.2330 2.4465 5.6499 0.5867  -1.1386 0.1596  204  GLU B N   
5289  C  CA  . GLU B  94  ? 2.3885 2.4911 5.5738 0.6474  -1.2369 0.2058  204  GLU B CA  
5290  C  C   . GLU B  94  ? 2.4229 2.3748 5.3532 0.6638  -1.1983 0.2669  204  GLU B C   
5291  O  O   . GLU B  94  ? 2.5262 2.3809 5.2204 0.6932  -1.2555 0.3076  204  GLU B O   
5292  C  CB  . GLU B  94  ? 2.5766 2.6711 5.8190 0.7447  -1.3157 0.2010  204  GLU B CB  
5293  C  CG  . GLU B  94  ? 2.5775 2.8123 6.0301 0.7347  -1.3780 0.1467  204  GLU B CG  
5294  C  CD  . GLU B  94  ? 2.7846 2.9918 6.2125 0.8298  -1.4893 0.1543  204  GLU B CD  
5295  O  OE1 . GLU B  94  ? 2.9311 3.0111 6.1988 0.9098  -1.5038 0.1994  204  GLU B OE1 
5296  O  OE2 . GLU B  94  ? 2.8100 3.1198 6.3764 0.8253  -1.5583 0.1156  204  GLU B OE2 
5297  N  N   . ARG B  95  ? 2.3463 2.2755 5.3160 0.6433  -1.0954 0.2723  205  ARG B N   
5298  C  CA  . ARG B  95  ? 2.3591 2.1548 5.0939 0.6409  -1.0456 0.3273  205  ARG B CA  
5299  C  C   . ARG B  95  ? 2.2201 2.0401 4.8508 0.5606  -1.0335 0.3361  205  ARG B C   
5300  O  O   . ARG B  95  ? 2.2674 1.9797 4.6468 0.5667  -1.0326 0.3844  205  ARG B O   
5301  C  CB  . ARG B  95  ? 2.3176 2.0836 5.1379 0.6342  -0.9349 0.3256  205  ARG B CB  
5302  C  CG  . ARG B  95  ? 2.3649 1.9769 4.9474 0.6382  -0.8768 0.3826  205  ARG B CG  
5303  C  CD  . ARG B  95  ? 2.5949 2.0534 4.9314 0.7283  -0.9376 0.4337  205  ARG B CD  
5304  N  NE  . ARG B  95  ? 2.6893 1.9940 4.7861 0.7281  -0.8726 0.4876  205  ARG B NE  
5305  C  CZ  . ARG B  95  ? 2.7432 1.9338 4.8077 0.7545  -0.7993 0.5056  205  ARG B CZ  
5306  N  NH1 . ARG B  95  ? 2.7806 1.9947 5.0335 0.7884  -0.7823 0.4737  205  ARG B NH1 
5307  N  NH2 . ARG B  95  ? 2.8042 1.8530 4.6436 0.7453  -0.7391 0.5534  205  ARG B NH2 
5308  N  N   . PHE B  96  ? 2.0609 2.0170 4.8715 0.4873  -1.0176 0.2895  206  PHE B N   
5309  C  CA  . PHE B  96  ? 1.9418 1.9216 4.6531 0.4151  -1.0128 0.2953  206  PHE B CA  
5310  C  C   . PHE B  96  ? 2.0509 1.9760 4.5614 0.4408  -1.1136 0.3166  206  PHE B C   
5311  O  O   . PHE B  96  ? 2.0501 1.9031 4.3336 0.4258  -1.1118 0.3530  206  PHE B O   
5312  C  CB  . PHE B  96  ? 1.7839 1.9084 4.7173 0.3389  -0.9711 0.2381  206  PHE B CB  
5313  C  CG  . PHE B  96  ? 1.7694 1.9169 4.5978 0.2722  -0.9794 0.2394  206  PHE B CG  
5314  C  CD1 . PHE B  96  ? 1.6258 1.7561 4.3579 0.2206  -0.9084 0.2616  206  PHE B CD1 
5315  C  CD2 . PHE B  96  ? 1.9808 2.1650 4.8060 0.2630  -1.0560 0.2180  206  PHE B CD2 
5316  C  CE1 . PHE B  96  ? 1.4998 1.6465 4.1209 0.1653  -0.9152 0.2633  206  PHE B CE1 
5317  C  CE2 . PHE B  96  ? 2.0115 2.2028 4.7243 0.2055  -1.0587 0.2196  206  PHE B CE2 
5318  C  CZ  . PHE B  96  ? 1.5516 1.7227 4.1561 0.1587  -0.9886 0.2425  206  PHE B CZ  
5319  N  N   . ASN B  97  ? 2.1535 2.1131 4.7442 0.4808  -1.1977 0.2920  207  ASN B N   
5320  C  CA  . ASN B  97  ? 2.2629 2.1756 4.6813 0.5023  -1.2909 0.3050  207  ASN B CA  
5321  C  C   . ASN B  97  ? 2.4159 2.1790 4.5535 0.5675  -1.3045 0.3623  207  ASN B C   
5322  O  O   . ASN B  97  ? 2.4493 2.1512 4.3673 0.5590  -1.3248 0.3862  207  ASN B O   
5323  C  CB  . ASN B  97  ? 2.3530 2.3362 4.9365 0.5360  -1.3756 0.2661  207  ASN B CB  
5324  C  CG  . ASN B  97  ? 2.2191 2.3462 5.0481 0.4671  -1.3559 0.2094  207  ASN B CG  
5325  O  OD1 . ASN B  97  ? 2.0769 2.2375 4.8980 0.3913  -1.3012 0.2018  207  ASN B OD1 
5326  N  ND2 . ASN B  97  ? 2.2743 2.4869 5.3153 0.4957  -1.3935 0.1696  207  ASN B ND2 
5327  N  N   . GLU B  98  ? 2.5192 2.2166 4.6526 0.6339  -1.2829 0.3846  208  GLU B N   
5328  C  CA  . GLU B  98  ? 2.6887 2.2345 4.5548 0.7016  -1.2835 0.4413  208  GLU B CA  
5329  C  C   . GLU B  98  ? 2.6267 2.0997 4.2789 0.6629  -1.2087 0.4798  208  GLU B C   
5330  O  O   . GLU B  98  ? 2.7564 2.1138 4.1605 0.7054  -1.2040 0.5253  208  GLU B O   
5331  C  CB  . GLU B  98  ? 2.8083 2.2908 4.7231 0.7752  -1.2599 0.4570  208  GLU B CB  
5332  C  CG  . GLU B  98  ? 2.9187 2.4538 5.0006 0.8361  -1.3407 0.4274  208  GLU B CG  
5333  C  CD  . GLU B  98  ? 2.9900 2.4936 5.1837 0.8934  -1.3008 0.4286  208  GLU B CD  
5334  O  OE1 . GLU B  98  ? 2.9898 2.3989 5.0896 0.8941  -1.2149 0.4602  208  GLU B OE1 
5335  O  OE2 . GLU B  98  ? 3.0517 2.6235 5.4288 0.9372  -1.3526 0.3961  208  GLU B OE2 
5336  N  N   . ILE B  99  ? 2.5050 2.0473 4.2533 0.5844  -1.1446 0.4631  209  ILE B N   
5337  C  CA  . ILE B  99  ? 2.3725 1.8588 3.9312 0.5455  -1.0756 0.4966  209  ILE B CA  
5338  C  C   . ILE B  99  ? 2.3310 1.8414 3.7576 0.5068  -1.1107 0.4917  209  ILE B C   
5339  O  O   . ILE B  99  ? 2.3870 1.8167 3.5677 0.5178  -1.0876 0.5267  209  ILE B O   
5340  C  CB  . ILE B  99  ? 2.1964 1.7432 3.9172 0.4812  -0.9879 0.4838  209  ILE B CB  
5341  C  CG1 . ILE B  99  ? 2.2605 1.7586 4.0819 0.5230  -0.9400 0.4900  209  ILE B CG1 
5342  C  CG2 . ILE B  99  ? 2.1214 1.6282 3.6612 0.4348  -0.9235 0.5151  209  ILE B CG2 
5343  C  CD1 . ILE B  99  ? 2.0949 1.6623 4.1164 0.4618  -0.8479 0.4681  209  ILE B CD1 
5344  N  N   . VAL B  100 ? 2.2434 1.8613 3.8300 0.4624  -1.1593 0.4468  210  VAL B N   
5345  C  CA  . VAL B  100 ? 2.2619 1.8943 3.7297 0.4222  -1.1893 0.4380  210  VAL B CA  
5346  C  C   . VAL B  100 ? 2.3888 1.9389 3.6566 0.4811  -1.2513 0.4561  210  VAL B C   
5347  O  O   . VAL B  100 ? 2.4000 1.9133 3.4736 0.4672  -1.2456 0.4678  210  VAL B O   
5348  C  CB  . VAL B  100 ? 2.2280 1.9815 3.9220 0.3633  -1.2215 0.3864  210  VAL B CB  
5349  C  CG1 . VAL B  100 ? 2.1729 1.9293 3.7380 0.3131  -1.2341 0.3794  210  VAL B CG1 
5350  C  CG2 . VAL B  100 ? 2.0970 1.9387 4.0183 0.3151  -1.1490 0.3668  210  VAL B CG2 
5351  N  N   . LYS B  101 ? 2.5338 2.0560 3.8485 0.5493  -1.3064 0.4583  211  LYS B N   
5352  C  CA  . LYS B  101 ? 2.7124 2.1618 3.8587 0.6062  -1.3682 0.4757  211  LYS B CA  
5353  C  C   . LYS B  101 ? 2.7959 2.1334 3.6710 0.6402  -1.3065 0.5303  211  LYS B C   
5354  O  O   . LYS B  101 ? 2.8640 2.1610 3.5636 0.6478  -1.3208 0.5428  211  LYS B O   
5355  C  CB  . LYS B  101 ? 2.8548 2.3010 4.1214 0.6758  -1.4376 0.4689  211  LYS B CB  
5356  C  CG  . LYS B  101 ? 2.7849 2.3544 4.3391 0.6484  -1.4943 0.4126  211  LYS B CG  
5357  C  CD  . LYS B  101 ? 2.8954 2.4711 4.5951 0.7195  -1.5278 0.4085  211  LYS B CD  
5358  C  CE  . LYS B  101 ? 2.8155 2.5305 4.8258 0.6926  -1.5635 0.3503  211  LYS B CE  
5359  N  NZ  . LYS B  101 ? 2.9248 2.6504 5.0774 0.7672  -1.5882 0.3448  211  LYS B NZ  
5360  N  N   . ASN B  102 ? 2.7956 2.0826 3.6422 0.6596  -1.2317 0.5628  212  ASN B N   
5361  C  CA  . ASN B  102 ? 2.8921 2.0708 3.5033 0.6970  -1.1647 0.6188  212  ASN B CA  
5362  C  C   . ASN B  102 ? 2.7700 1.9580 3.2528 0.6415  -1.0878 0.6279  212  ASN B C   
5363  O  O   . ASN B  102 ? 2.8327 1.9466 3.1363 0.6654  -1.0204 0.6736  212  ASN B O   
5364  C  CB  . ASN B  102 ? 2.9630 2.0672 3.5940 0.7414  -1.1127 0.6510  212  ASN B CB  
5365  C  CG  . ASN B  102 ? 3.0801 2.1806 3.8515 0.8007  -1.1816 0.6396  212  ASN B CG  
5366  O  OD1 . ASN B  102 ? 3.0722 2.2512 3.9777 0.7966  -1.2681 0.5988  212  ASN B OD1 
5367  N  ND2 . ASN B  102 ? 3.1970 2.2036 3.9413 0.8568  -1.1416 0.6750  212  ASN B ND2 
5368  N  N   . GLN B  103 ? 2.6022 1.8818 3.1801 0.5693  -1.0927 0.5878  213  GLN B N   
5369  C  CA  . GLN B  103 ? 2.4837 1.7782 2.9503 0.5183  -1.0202 0.5936  213  GLN B CA  
5370  C  C   . GLN B  103 ? 2.5498 1.8143 2.8085 0.5343  -1.0129 0.6096  213  GLN B C   
5371  O  O   . GLN B  103 ? 2.6024 1.8770 2.8620 0.5323  -1.0898 0.5858  213  GLN B O   
5372  C  CB  . GLN B  103 ? 2.3012 1.6997 2.9285 0.4391  -1.0322 0.5493  213  GLN B CB  
5373  C  CG  . GLN B  103 ? 2.1968 1.6434 3.0432 0.4096  -1.0083 0.5388  213  GLN B CG  
5374  C  CD  . GLN B  103 ? 2.1711 1.5656 2.9431 0.4057  -0.9158 0.5741  213  GLN B CD  
5375  O  OE1 . GLN B  103 ? 2.1760 1.5293 2.7513 0.4023  -0.8628 0.5980  213  GLN B OE1 
5376  N  NE2 . GLN B  103 ? 2.1459 1.5443 3.0858 0.4054  -0.8903 0.5750  213  GLN B NE2 
5377  N  N   . LYS B  104 ? 2.5724 1.7844 2.6748 0.5421  -0.9376 0.6477  214  LYS B N   
5378  C  CA  . LYS B  104 ? 2.6606 1.8236 2.5923 0.5414  -0.9487 0.6609  214  LYS B CA  
5379  C  C   . LYS B  104 ? 2.5090 1.7293 2.3965 0.4827  -0.8920 0.6441  214  LYS B C   
5380  O  O   . LYS B  104 ? 2.3497 1.6327 2.3146 0.4474  -0.8336 0.6326  214  LYS B O   
5381  C  CB  . LYS B  104 ? 2.8184 1.8807 2.6150 0.5916  -0.9117 0.7187  214  LYS B CB  
5382  C  CG  . LYS B  104 ? 2.9975 1.9860 2.8124 0.6561  -0.9681 0.7407  214  LYS B CG  
5383  C  CD  . LYS B  104 ? 3.1634 2.0444 2.8331 0.6978  -0.9314 0.8011  214  LYS B CD  
5384  C  CE  . LYS B  104 ? 3.3477 2.1464 3.0337 0.7648  -0.9794 0.8275  214  LYS B CE  
5385  N  NZ  . LYS B  104 ? 3.2870 2.1058 3.1141 0.7820  -0.9426 0.8305  214  LYS B NZ  
5386  N  N   . ILE B  105 ? 2.5713 1.7626 2.3303 0.4745  -0.9120 0.6400  215  ILE B N   
5387  C  CA  . ILE B  105 ? 2.4541 1.6926 2.1580 0.4259  -0.8658 0.6223  215  ILE B CA  
5388  C  C   . ILE B  105 ? 2.4376 1.6656 2.0502 0.4324  -0.7706 0.6627  215  ILE B C   
5389  O  O   . ILE B  105 ? 2.5628 1.7235 2.1087 0.4739  -0.7533 0.7073  215  ILE B O   
5390  C  CB  . ILE B  105 ? 2.5608 1.7604 2.1663 0.4183  -0.9259 0.5973  215  ILE B CB  
5391  C  CG1 . ILE B  105 ? 2.8252 2.0030 2.5034 0.4289  -1.0308 0.5695  215  ILE B CG1 
5392  C  CG2 . ILE B  105 ? 2.4078 1.6660 1.9995 0.3640  -0.8922 0.5662  215  ILE B CG2 
5393  C  CD1 . ILE B  105 ? 2.8506 1.9249 2.4407 0.4878  -1.0926 0.5900  215  ILE B CD1 
5394  N  N   . SER B  106 ? 2.2850 1.5806 1.9022 0.3897  -0.7085 0.6483  216  SER B N   
5395  C  CA  . SER B  106 ? 2.2580 1.5607 1.7903 0.3874  -0.6223 0.6789  216  SER B CA  
5396  C  C   . SER B  106 ? 2.2424 1.5693 1.6853 0.3630  -0.6217 0.6578  216  SER B C   
5397  O  O   . SER B  106 ? 2.3045 1.6051 1.7188 0.3598  -0.6895 0.6283  216  SER B O   
5398  C  CB  . SER B  106 ? 2.1100 1.4602 1.7151 0.3627  -0.5504 0.6753  216  SER B CB  
5399  O  OG  . SER B  106 ? 2.1390 1.4490 1.8246 0.3861  -0.5500 0.6895  216  SER B OG  
5400  N  N   . ALA B  107 ? 2.1650 1.5376 1.5675 0.3465  -0.5458 0.6701  217  ALA B N   
5401  C  CA  . ALA B  107 ? 2.1516 1.5493 1.4772 0.3267  -0.5405 0.6494  217  ALA B CA  
5402  C  C   . ALA B  107 ? 2.0382 1.5171 1.3684 0.3024  -0.4564 0.6543  217  ALA B C   
5403  O  O   . ALA B  107 ? 2.1096 1.6061 1.4778 0.3049  -0.3993 0.6782  217  ALA B O   
5404  C  CB  . ALA B  107 ? 2.3256 1.6449 1.5319 0.3553  -0.5665 0.6706  217  ALA B CB  
5405  N  N   . ASN B  108 ? 1.9805 1.4970 1.2666 0.2814  -0.4507 0.6272  218  ASN B N   
5406  C  CA  . ASN B  108 ? 1.8779 1.4761 1.1562 0.2612  -0.3819 0.6293  218  ASN B CA  
5407  C  C   . ASN B  108 ? 2.1575 1.7515 1.3624 0.2518  -0.4028 0.6046  218  ASN B C   
5408  O  O   . ASN B  108 ? 2.1087 1.6153 1.2442 0.2712  -0.4577 0.5967  218  ASN B O   
5409  C  CB  . ASN B  108 ? 1.7882 1.4369 1.1331 0.2393  -0.3463 0.5944  218  ASN B CB  
5410  C  CG  . ASN B  108 ? 1.7007 1.3571 1.0812 0.2080  -0.3941 0.5427  218  ASN B CG  
5411  O  OD1 . ASN B  108 ? 1.6008 1.3028 0.9675 0.1864  -0.3753 0.5133  218  ASN B OD1 
5412  N  ND2 . ASN B  108 ? 1.9480 1.5632 1.3844 0.2042  -0.4559 0.5345  218  ASN B ND2 
5413  N  N   . ILE B  109 ? 2.2585 1.9322 1.4696 0.2280  -0.3605 0.5881  219  ILE B N   
5414  C  CA  . ILE B  109 ? 1.8607 1.5190 0.9998 0.2221  -0.3736 0.5635  219  ILE B CA  
5415  C  C   . ILE B  109 ? 1.7782 1.4618 0.9438 0.2032  -0.3834 0.5147  219  ILE B C   
5416  O  O   . ILE B  109 ? 1.8587 1.4697 0.9738 0.2078  -0.4299 0.4864  219  ILE B O   
5417  C  CB  . ILE B  109 ? 1.8470 1.5530 0.9566 0.2034  -0.3297 0.5830  219  ILE B CB  
5418  C  CG1 . ILE B  109 ? 2.6870 2.3557 1.7713 0.2073  -0.3186 0.6304  219  ILE B CG1 
5419  C  CG2 . ILE B  109 ? 1.9466 1.5901 0.9532 0.2193  -0.3454 0.5534  219  ILE B CG2 
5420  C  CD1 . ILE B  109 ? 1.9382 1.6170 0.9729 0.1781  -0.2844 0.6351  219  ILE B CD1 
5421  N  N   . ASP B  110 ? 2.0456 1.8138 1.2801 0.1843  -0.3414 0.5010  220  ASP B N   
5422  C  CA  . ASP B  110 ? 1.8191 1.6131 1.0673 0.1620  -0.3397 0.4568  220  ASP B CA  
5423  C  C   . ASP B  110 ? 1.5321 1.2841 0.8327 0.1385  -0.3836 0.4294  220  ASP B C   
5424  O  O   . ASP B  110 ? 1.4911 1.2443 0.8519 0.1310  -0.3853 0.4365  220  ASP B O   
5425  C  CB  . ASP B  110 ? 1.4385 1.3204 0.7164 0.1558  -0.2735 0.4413  220  ASP B CB  
5426  C  CG  . ASP B  110 ? 1.3713 1.2301 0.6845 0.1476  -0.2539 0.4245  220  ASP B CG  
5427  O  OD1 . ASP B  110 ? 1.6123 1.4334 0.9520 0.1487  -0.2750 0.4475  220  ASP B OD1 
5428  O  OD2 . ASP B  110 ? 1.2994 1.1653 0.6157 0.1234  -0.2259 0.3909  220  ASP B OD2 
5429  N  N   . THR B  111 ? 1.5697 1.2774 0.8507 0.1224  -0.4246 0.4020  221  THR B N   
5430  C  CA  . THR B  111 ? 1.5670 1.2340 0.9031 0.0932  -0.4798 0.3836  221  THR B CA  
5431  C  C   . THR B  111 ? 1.4331 1.1572 0.8717 0.0548  -0.4630 0.3749  221  THR B C   
5432  O  O   . THR B  111 ? 1.4309 1.1411 0.9436 0.0428  -0.5029 0.3812  221  THR B O   
5433  C  CB  . THR B  111 ? 1.8683 1.4823 1.1594 0.0785  -0.5120 0.3554  221  THR B CB  
5434  O  OG1 . THR B  111 ? 2.5130 2.0624 1.7017 0.1140  -0.5259 0.3603  221  THR B OG1 
5435  C  CG2 . THR B  111 ? 1.6488 1.2113 0.9918 0.0527  -0.5800 0.3441  221  THR B CG2 
5436  N  N   . PRO B  112 ? 2.3648 2.1500 1.8187 0.0328  -0.4112 0.3593  222  PRO B N   
5437  C  CA  . PRO B  112 ? 1.2108 1.0433 0.7619 -0.0110 -0.3975 0.3532  222  PRO B CA  
5438  C  C   . PRO B  112 ? 1.1924 1.0385 0.7768 0.0023  -0.3771 0.3785  222  PRO B C   
5439  O  O   . PRO B  112 ? 1.2414 1.0776 0.7604 0.0408  -0.3463 0.3951  222  PRO B O   
5440  C  CB  . PRO B  112 ? 1.1302 1.0111 0.6665 -0.0347 -0.3483 0.3289  222  PRO B CB  
5441  C  CG  . PRO B  112 ? 1.1962 1.0702 0.6374 0.0146  -0.3220 0.3310  222  PRO B CG  
5442  C  CD  . PRO B  112 ? 1.3162 1.1307 0.7081 0.0444  -0.3676 0.3455  222  PRO B CD  
5443  N  N   . GLU B  113 ? 1.1153 0.9858 0.8069 -0.0309 -0.3896 0.3835  223  GLU B N   
5444  C  CA  . GLU B  113 ? 1.2473 1.1108 0.9835 -0.0158 -0.3808 0.4121  223  GLU B CA  
5445  C  C   . GLU B  113 ? 1.0056 0.9339 0.8324 -0.0793 -0.3498 0.4245  223  GLU B C   
5446  O  O   . GLU B  113 ? 2.0721 2.0614 1.9187 -0.1293 -0.3297 0.4066  223  GLU B O   
5447  C  CB  . GLU B  113 ? 1.1750 1.0017 0.9848 0.0016  -0.4436 0.4256  223  GLU B CB  
5448  C  CG  . GLU B  113 ? 1.3029 1.0703 1.0478 0.0321  -0.4990 0.4225  223  GLU B CG  
5449  C  CD  . GLU B  113 ? 1.8297 1.5478 1.4512 0.0852  -0.4854 0.4445  223  GLU B CD  
5450  O  OE1 . GLU B  113 ? 1.7251 1.4561 1.2994 0.1015  -0.4280 0.4604  223  GLU B OE1 
5451  O  OE2 . GLU B  113 ? 1.6484 1.3120 1.2223 0.1089  -0.5338 0.4472  223  GLU B OE2 
5452  N  N   . GLY B  114 ? 1.5232 1.4436 1.4183 -0.0918 -0.3520 0.4718  224  GLY B N   
5453  C  CA  . GLY B  114 ? 0.9413 0.9405 0.9579 -0.1673 -0.3239 0.5118  224  GLY B CA  
5454  C  C   . GLY B  114 ? 1.5081 1.5368 1.7302 -0.2124 -0.3800 0.5463  224  GLY B C   
5455  O  O   . GLY B  114 ? 0.9006 0.9208 1.2715 -0.2228 -0.3582 0.5672  224  GLY B O   
5456  N  N   . GLY B  115 ? 0.8694 0.9214 1.1168 -0.2288 -0.4288 0.5174  225  GLY B N   
5457  C  CA  . GLY B  115 ? 0.8195 0.9212 1.2944 -0.2618 -0.4611 0.5011  225  GLY B CA  
5458  C  C   . GLY B  115 ? 0.7123 0.9154 1.3358 -0.3347 -0.3465 0.4434  225  GLY B C   
5459  O  O   . GLY B  115 ? 0.7058 0.9238 1.4960 -0.3301 -0.3125 0.4050  225  GLY B O   
5460  N  N   . PHE B  116 ? 0.6687 0.9114 1.1606 -0.3556 -0.2695 0.4102  226  PHE B N   
5461  C  CA  . PHE B  116 ? 0.6239 0.9083 1.1474 -0.3628 -0.1491 0.3065  226  PHE B CA  
5462  C  C   . PHE B  116 ? 0.6353 0.9137 1.2234 -0.3640 -0.0821 0.2922  226  PHE B C   
5463  O  O   . PHE B  116 ? 0.6290 0.9235 1.2867 -0.3770 -0.0126 0.2131  226  PHE B O   
5464  C  CB  . PHE B  116 ? 0.5889 0.8938 0.9601 -0.3669 -0.1046 0.2690  226  PHE B CB  
5465  C  CG  . PHE B  116 ? 0.5868 0.8895 0.8920 -0.3707 -0.1506 0.2677  226  PHE B CG  
5466  C  CD1 . PHE B  116 ? 1.0513 1.3390 1.4513 -0.3709 -0.2012 0.2666  226  PHE B CD1 
5467  C  CD2 . PHE B  116 ? 1.0141 1.3268 1.1608 -0.3721 -0.1429 0.2627  226  PHE B CD2 
5468  C  CE1 . PHE B  116 ? 0.9905 1.2625 1.3260 -0.3755 -0.2355 0.2602  226  PHE B CE1 
5469  C  CE2 . PHE B  116 ? 0.5858 0.8822 0.6585 -0.3806 -0.1798 0.2651  226  PHE B CE2 
5470  C  CZ  . PHE B  116 ? 0.8312 1.1010 0.9994 -0.3826 -0.2214 0.2625  226  PHE B CZ  
5471  N  N   . ASP B  117 ? 0.6704 0.9174 1.2128 -0.3567 -0.1017 0.3694  227  ASP B N   
5472  C  CA  . ASP B  117 ? 0.7024 0.9243 1.2966 -0.3576 -0.0393 0.3638  227  ASP B CA  
5473  C  C   . ASP B  117 ? 0.7275 0.9282 1.5100 -0.3500 -0.0530 0.3607  227  ASP B C   
5474  O  O   . ASP B  117 ? 0.7418 0.9420 1.5764 -0.3605 0.0163  0.3107  227  ASP B O   
5475  C  CB  . ASP B  117 ? 1.4902 1.6532 1.9839 -0.3399 -0.0614 0.4583  227  ASP B CB  
5476  C  CG  . ASP B  117 ? 1.6157 1.8096 1.9517 -0.3417 -0.0004 0.4244  227  ASP B CG  
5477  O  OD1 . ASP B  117 ? 1.0895 1.3365 1.3770 -0.3489 0.0211  0.3581  227  ASP B OD1 
5478  O  OD2 . ASP B  117 ? 1.2335 1.3836 1.5009 -0.3272 0.0262  0.4577  227  ASP B OD2 
5479  N  N   . ALA B  118 ? 0.7485 0.9206 1.6285 -0.3300 -0.1544 0.4189  228  ALA B N   
5480  C  CA  . ALA B  118 ? 1.0466 1.2040 2.1308 -0.3110 -0.1825 0.4111  228  ALA B CA  
5481  C  C   . ALA B  118 ? 0.8121 1.0395 1.9511 -0.3204 -0.1280 0.3096  228  ALA B C   
5482  O  O   . ALA B  118 ? 0.8183 1.0499 2.0845 -0.3135 -0.0919 0.2762  228  ALA B O   
5483  C  CB  . ALA B  118 ? 1.2698 1.3597 2.3525 -0.2510 -0.3145 0.4650  228  ALA B CB  
5484  N  N   . ILE B  119 ? 0.7572 1.0255 1.7907 -0.3370 -0.1229 0.2676  229  ILE B N   
5485  C  CA  . ILE B  119 ? 0.6799 0.9978 1.7200 -0.3571 -0.0662 0.1827  229  ILE B CA  
5486  C  C   . ILE B  119 ? 0.6805 1.0171 1.6500 -0.3869 0.0273  0.1298  229  ILE B C   
5487  O  O   . ILE B  119 ? 0.7887 1.1432 1.8356 -0.3902 0.0566  0.1002  229  ILE B O   
5488  C  CB  . ILE B  119 ? 0.6522 0.9927 1.5735 -0.3738 -0.0751 0.1557  229  ILE B CB  
5489  C  CG1 . ILE B  119 ? 0.6713 0.9846 1.6405 -0.3472 -0.1879 0.2162  229  ILE B CG1 
5490  C  CG2 . ILE B  119 ? 0.6507 1.0400 1.5530 -0.4060 -0.0208 0.0843  229  ILE B CG2 
5491  C  CD1 . ILE B  119 ? 0.6723 0.9937 1.5248 -0.3616 -0.1972 0.1946  229  ILE B CD1 
5492  N  N   . MET B  120 ? 0.6688 0.9976 1.4976 -0.4051 0.0629  0.1266  230  MET B N   
5493  C  CA  . MET B  120 ? 0.6792 1.0326 1.4249 -0.4380 0.1188  0.0953  230  MET B CA  
5494  C  C   . MET B  120 ? 0.7201 1.0410 1.5766 -0.4239 0.1392  0.1086  230  MET B C   
5495  O  O   . MET B  120 ? 0.7413 1.0745 1.6407 -0.4284 0.1733  0.0854  230  MET B O   
5496  C  CB  . MET B  120 ? 1.0336 1.3833 1.6328 -0.4499 0.1403  0.0893  230  MET B CB  
5497  C  CG  . MET B  120 ? 1.0256 1.4084 1.6023 -0.4549 0.1513  0.1162  230  MET B CG  
5498  S  SD  . MET B  120 ? 0.6700 1.0840 1.3336 -0.4462 0.1720  0.1042  230  MET B SD  
5499  C  CE  . MET B  120 ? 0.6138 1.0151 1.2319 -0.4042 0.1543  0.1180  230  MET B CE  
5500  N  N   . GLN B  121 ? 0.7478 1.0113 1.6978 -0.3953 0.1215  0.1595  231  GLN B N   
5501  C  CA  . GLN B  121 ? 0.8007 1.0187 1.8670 -0.3820 0.1491  0.1727  231  GLN B CA  
5502  C  C   . GLN B  121 ? 0.8149 1.0360 2.0730 -0.3558 0.1393  0.1567  231  GLN B C   
5503  O  O   . GLN B  121 ? 0.8489 1.0573 2.1757 -0.3550 0.1854  0.1285  231  GLN B O   
5504  C  CB  . GLN B  121 ? 1.1531 1.2969 2.2535 -0.3600 0.1262  0.2523  231  GLN B CB  
5505  C  CG  . GLN B  121 ? 1.1077 1.2451 2.0241 -0.3853 0.1565  0.2612  231  GLN B CG  
5506  C  CD  . GLN B  121 ? 0.8578 1.0259 1.6849 -0.4251 0.2169  0.2002  231  GLN B CD  
5507  O  OE1 . GLN B  121 ? 0.9046 1.0418 1.8171 -0.4224 0.2479  0.1911  231  GLN B OE1 
5508  N  NE2 . GLN B  121 ? 1.1026 1.3349 1.7683 -0.4590 0.2186  0.1700  231  GLN B NE2 
5509  N  N   . ALA B  122 ? 1.0747 1.3146 2.4238 -0.3340 0.0769  0.1715  232  ALA B N   
5510  C  CA  . ALA B  122 ? 0.8097 1.0633 2.3530 -0.3081 0.0615  0.1522  232  ALA B CA  
5511  C  C   . ALA B  122 ? 0.8018 1.1048 2.2926 -0.3322 0.1178  0.0830  232  ALA B C   
5512  O  O   . ALA B  122 ? 0.8299 1.1359 2.4647 -0.3164 0.1415  0.0558  232  ALA B O   
5513  C  CB  . ALA B  122 ? 0.7990 1.0634 2.4399 -0.2820 -0.0354 0.1862  232  ALA B CB  
5514  N  N   . ALA B  123 ? 0.8230 1.1595 2.1135 -0.3689 0.1356  0.0620  233  ALA B N   
5515  C  CA  . ALA B  123 ? 0.8267 1.1978 2.0797 -0.3877 0.1749  0.0185  233  ALA B CA  
5516  C  C   . ALA B  123 ? 0.8619 1.2087 2.1234 -0.3906 0.2369  -0.0068 233  ALA B C   
5517  O  O   . ALA B  123 ? 0.8944 1.2379 2.2614 -0.3810 0.2742  -0.0424 233  ALA B O   
5518  C  CB  . ALA B  123 ? 0.8008 1.1983 1.9144 -0.4125 0.1678  0.0174  233  ALA B CB  
5519  N  N   . VAL B  124 ? 1.1033 1.4316 2.2587 -0.4041 0.2494  0.0082  234  VAL B N   
5520  C  CA  . VAL B  124 ? 1.1317 1.4367 2.2796 -0.4103 0.3066  -0.0222 234  VAL B CA  
5521  C  C   . VAL B  124 ? 0.8892 1.1533 2.1549 -0.3953 0.3309  -0.0250 234  VAL B C   
5522  O  O   . VAL B  124 ? 0.9300 1.1763 2.2551 -0.3930 0.3819  -0.0669 234  VAL B O   
5523  C  CB  . VAL B  124 ? 0.8385 1.1429 1.8508 -0.4284 0.3072  -0.0041 234  VAL B CB  
5524  C  CG1 . VAL B  124 ? 1.6959 1.9764 2.7005 -0.4359 0.3645  -0.0459 234  VAL B CG1 
5525  C  CG2 . VAL B  124 ? 0.7928 1.1368 1.7019 -0.4371 0.2768  0.0065  234  VAL B CG2 
5526  N  N   . CYS B  125 ? 0.8923 1.1276 2.2127 -0.3817 0.3027  0.0162  235  CYS B N   
5527  C  CA  . CYS B  125 ? 1.0194 1.1958 2.5099 -0.3578 0.3359  0.0174  235  CYS B CA  
5528  C  C   . CYS B  125 ? 0.9670 1.1552 2.6480 -0.3301 0.3462  -0.0142 235  CYS B C   
5529  O  O   . CYS B  125 ? 0.9627 1.1530 2.8060 -0.2984 0.3038  0.0094  235  CYS B O   
5530  C  CB  . CYS B  125 ? 1.1792 1.3024 2.7436 -0.3369 0.3035  0.0803  235  CYS B CB  
5531  S  SG  . CYS B  125 ? 0.9803 1.0737 2.3401 -0.3673 0.3037  0.1217  235  CYS B SG  
5532  N  N   . LYS B  126 ? 1.0063 1.2010 2.6828 -0.3394 0.3971  -0.0653 236  LYS B N   
5533  C  CA  . LYS B  126 ? 1.2937 1.4963 3.1559 -0.3147 0.4184  -0.1006 236  LYS B CA  
5534  C  C   . LYS B  126 ? 1.0721 1.2174 3.1438 -0.2829 0.4478  -0.0966 236  LYS B C   
5535  O  O   . LYS B  126 ? 1.0959 1.2470 3.3626 -0.2553 0.4600  -0.1212 236  LYS B O   
5536  C  CB  . LYS B  126 ? 1.4222 1.6406 3.2102 -0.3347 0.4667  -0.1550 236  LYS B CB  
5537  C  CG  . LYS B  126 ? 0.9918 1.2563 2.6551 -0.3550 0.4493  -0.1658 236  LYS B CG  
5538  C  CD  . LYS B  126 ? 1.0363 1.2871 2.6842 -0.3675 0.5156  -0.2293 236  LYS B CD  
5539  C  CE  . LYS B  126 ? 1.0200 1.3014 2.5801 -0.3843 0.5100  -0.2467 236  LYS B CE  
5540  N  NZ  . LYS B  126 ? 1.0701 1.3287 2.6013 -0.3986 0.5743  -0.3110 236  LYS B NZ  
5541  N  N   . GLU B  127 ? 1.1027 1.1903 3.1415 -0.2870 0.4598  -0.0639 237  GLU B N   
5542  C  CA  . GLU B  127 ? 1.5248 1.5413 3.7425 -0.2609 0.4944  -0.0526 237  GLU B CA  
5543  C  C   . GLU B  127 ? 1.6007 1.5785 3.9422 -0.2299 0.4330  0.0208  237  GLU B C   
5544  O  O   . GLU B  127 ? 1.8350 1.7995 4.4181 -0.1884 0.4087  0.0338  237  GLU B O   
5545  C  CB  . GLU B  127 ? 1.8708 1.8284 3.9558 -0.2918 0.5561  -0.0649 237  GLU B CB  
5546  C  CG  . GLU B  127 ? 1.7623 1.7489 3.7228 -0.3220 0.6012  -0.1295 237  GLU B CG  
5547  C  CD  . GLU B  127 ? 1.9043 1.8474 3.7151 -0.3571 0.6384  -0.1359 237  GLU B CD  
5548  O  OE1 . GLU B  127 ? 2.0058 1.9620 3.7337 -0.3789 0.6706  -0.1846 237  GLU B OE1 
5549  O  OE2 . GLU B  127 ? 1.7587 1.6495 3.5385 -0.3632 0.6335  -0.0907 237  GLU B OE2 
5550  N  N   . LYS B  128 ? 1.4549 1.4075 3.6388 -0.2477 0.3998  0.0726  238  LYS B N   
5551  C  CA  . LYS B  128 ? 1.2096 1.0919 3.4735 -0.2179 0.3331  0.1540  238  LYS B CA  
5552  C  C   . LYS B  128 ? 1.2589 1.2039 3.6586 -0.1897 0.2399  0.1727  238  LYS B C   
5553  O  O   . LYS B  128 ? 1.5050 1.3693 4.0185 -0.1500 0.1602  0.2366  238  LYS B O   
5554  C  CB  . LYS B  128 ? 1.2305 1.0611 3.2671 -0.2447 0.3283  0.2027  238  LYS B CB  
5555  C  CG  . LYS B  128 ? 1.4350 1.2275 3.3235 -0.2823 0.4114  0.1740  238  LYS B CG  
5556  C  CD  . LYS B  128 ? 1.6668 1.3943 3.3667 -0.3022 0.4069  0.2286  238  LYS B CD  
5557  C  CE  . LYS B  128 ? 1.5262 1.0956 3.2610 -0.2578 0.3796  0.3095  238  LYS B CE  
5558  N  NZ  . LYS B  128 ? 1.5333 1.0283 3.0608 -0.2762 0.3905  0.3586  238  LYS B NZ  
5559  N  N   . ILE B  129 ? 1.0678 1.1190 3.4147 -0.2049 0.2373  0.1209  239  ILE B N   
5560  C  CA  . ILE B  129 ? 1.0253 1.1412 3.5035 -0.1795 0.1566  0.1226  239  ILE B CA  
5561  C  C   . ILE B  129 ? 1.0433 1.1950 3.7213 -0.1550 0.1808  0.0680  239  ILE B C   
5562  O  O   . ILE B  129 ? 1.1836 1.3573 4.0775 -0.1147 0.1090  0.0812  239  ILE B O   
5563  C  CB  . ILE B  129 ? 0.9630 1.1427 3.2319 -0.2110 0.1383  0.1055  239  ILE B CB  
5564  C  CG1 . ILE B  129 ? 0.9442 1.0979 3.1189 -0.2134 0.0669  0.1751  239  ILE B CG1 
5565  C  CG2 . ILE B  129 ? 0.9448 1.1923 3.3013 -0.2000 0.1058  0.0685  239  ILE B CG2 
5566  C  CD1 . ILE B  129 ? 0.9698 1.0601 2.9785 -0.2383 0.1142  0.2041  239  ILE B CD1 
5567  N  N   . GLY B  130 ? 1.0598 1.2159 3.6666 -0.1777 0.2733  0.0064  240  GLY B N   
5568  C  CA  . GLY B  130 ? 1.1087 1.2812 3.8985 -0.1570 0.3099  -0.0450 240  GLY B CA  
5569  C  C   . GLY B  130 ? 1.0709 1.3170 3.8319 -0.1684 0.2970  -0.0867 240  GLY B C   
5570  O  O   . GLY B  130 ? 1.0829 1.3645 4.0245 -0.1400 0.2476  -0.0903 240  GLY B O   
5571  N  N   . TRP B  131 ? 1.0463 1.3157 3.5785 -0.2114 0.3361  -0.1152 241  TRP B N   
5572  C  CA  . TRP B  131 ? 1.0349 1.3655 3.5286 -0.2286 0.3351  -0.1497 241  TRP B CA  
5573  C  C   . TRP B  131 ? 1.2592 1.5907 3.8705 -0.2244 0.4024  -0.2067 241  TRP B C   
5574  O  O   . TRP B  131 ? 1.1190 1.4054 3.6989 -0.2320 0.4704  -0.2337 241  TRP B O   
5575  C  CB  . TRP B  131 ? 1.0618 1.4124 3.2815 -0.2734 0.3435  -0.1503 241  TRP B CB  
5576  C  CG  . TRP B  131 ? 1.1308 1.4883 3.2363 -0.2803 0.2785  -0.1006 241  TRP B CG  
5577  C  CD1 . TRP B  131 ? 0.9245 1.2507 2.8798 -0.2947 0.2753  -0.0701 241  TRP B CD1 
5578  C  CD2 . TRP B  131 ? 1.4720 1.8675 3.6111 -0.2734 0.2065  -0.0771 241  TRP B CD2 
5579  N  NE1 . TRP B  131 ? 0.8863 1.2262 2.7801 -0.2961 0.2095  -0.0292 241  TRP B NE1 
5580  C  CE2 . TRP B  131 ? 0.8840 1.2632 2.8872 -0.2824 0.1641  -0.0328 241  TRP B CE2 
5581  C  CE3 . TRP B  131 ? 0.9342 1.3759 3.2051 -0.2623 0.1734  -0.0912 241  TRP B CE3 
5582  C  CZ2 . TRP B  131 ? 0.8600 1.2592 2.8544 -0.2780 0.0882  -0.0024 241  TRP B CZ2 
5583  C  CZ3 . TRP B  131 ? 0.9124 1.3778 3.1698 -0.2604 0.0961  -0.0616 241  TRP B CZ3 
5584  C  CH2 . TRP B  131 ? 0.8758 1.3157 2.9950 -0.2669 0.0532  -0.0177 241  TRP B CH2 
5585  N  N   . ARG B  132 ? 1.4416 1.8245 4.1854 -0.2146 0.3831  -0.2265 242  ARG B N   
5586  C  CA  . ARG B  132 ? 1.1578 1.5483 4.0243 -0.2120 0.4455  -0.2808 242  ARG B CA  
5587  C  C   . ARG B  132 ? 1.1612 1.5481 3.8340 -0.2528 0.5106  -0.3162 242  ARG B C   
5588  O  O   . ARG B  132 ? 1.1173 1.5183 3.5782 -0.2827 0.4933  -0.2983 242  ARG B O   
5589  C  CB  . ARG B  132 ? 1.1756 1.6356 4.2080 -0.1988 0.4052  -0.2914 242  ARG B CB  
5590  C  CG  . ARG B  132 ? 1.2304 1.6923 4.5321 -0.1499 0.3612  -0.2821 242  ARG B CG  
5591  C  CD  . ARG B  132 ? 1.3821 1.9285 4.8207 -0.1415 0.3137  -0.2952 242  ARG B CD  
5592  N  NE  . ARG B  132 ? 1.2867 1.8479 4.9741 -0.0903 0.2533  -0.2855 242  ARG B NE  
5593  C  CZ  . ARG B  132 ? 1.2950 1.9246 5.0969 -0.0699 0.1686  -0.2766 242  ARG B CZ  
5594  N  NH1 . ARG B  132 ? 1.2678 1.9517 4.9693 -0.1013 0.1437  -0.2764 242  ARG B NH1 
5595  N  NH2 . ARG B  132 ? 1.3478 1.9924 5.3558 -0.0163 0.1052  -0.2677 242  ARG B NH2 
5596  N  N   . ASN B  133 ? 1.3071 1.6732 4.0655 -0.2521 0.5817  -0.3662 243  ASN B N   
5597  C  CA  . ASN B  133 ? 1.3338 1.6855 3.9323 -0.2860 0.6416  -0.4024 243  ASN B CA  
5598  C  C   . ASN B  133 ? 1.2677 1.6813 3.7961 -0.3111 0.6277  -0.4068 243  ASN B C   
5599  O  O   . ASN B  133 ? 1.2529 1.6567 3.6240 -0.3367 0.6313  -0.4083 243  ASN B O   
5600  C  CB  . ASN B  133 ? 1.3584 1.6636 4.0857 -0.2776 0.7218  -0.4566 243  ASN B CB  
5601  C  CG  . ASN B  133 ? 1.4430 1.6706 4.1372 -0.2716 0.7556  -0.4581 243  ASN B CG  
5602  O  OD1 . ASN B  133 ? 1.3298 1.5446 3.8771 -0.2794 0.7229  -0.4208 243  ASN B OD1 
5603  N  ND2 . ASN B  133 ? 1.7164 1.8925 4.5512 -0.2596 0.8225  -0.5003 243  ASN B ND2 
5604  N  N   . ASP B  134 ? 1.4217 1.8840 4.1273 -0.3016 0.6289  -0.4260 244  ASP B N   
5605  C  CA  . ASP B  134 ? 1.5910 2.1065 4.2818 -0.3263 0.6299  -0.4393 244  ASP B CA  
5606  C  C   . ASP B  134 ? 1.3489 1.9370 4.1457 -0.3123 0.5519  -0.4042 244  ASP B C   
5607  O  O   . ASP B  134 ? 1.3911 2.0209 4.4010 -0.2932 0.5517  -0.4244 244  ASP B O   
5608  C  CB  . ASP B  134 ? 1.6649 2.1820 4.4504 -0.3366 0.7082  -0.4975 244  ASP B CB  
5609  C  CG  . ASP B  134 ? 2.0964 2.5341 4.7894 -0.3473 0.7810  -0.5355 244  ASP B CG  
5610  O  OD1 . ASP B  134 ? 2.4022 2.8059 5.1641 -0.3271 0.8020  -0.5423 244  ASP B OD1 
5611  O  OD2 . ASP B  134 ? 2.0883 2.4959 4.6378 -0.3765 0.8151  -0.5592 244  ASP B OD2 
5612  N  N   . SER B  135 ? 1.4533 2.0475 4.1360 -0.3196 0.4901  -0.3620 245  SER B N   
5613  C  CA  . SER B  135 ? 1.3393 1.9930 4.1065 -0.3096 0.4115  -0.3318 245  SER B CA  
5614  C  C   . SER B  135 ? 1.4259 2.0812 4.0220 -0.3366 0.3721  -0.3017 245  SER B C   
5615  O  O   . SER B  135 ? 1.3160 1.9287 3.7449 -0.3580 0.4041  -0.3040 245  SER B O   
5616  C  CB  . SER B  135 ? 1.2113 1.8451 4.1352 -0.2639 0.3591  -0.3101 245  SER B CB  
5617  O  OG  . SER B  135 ? 1.1624 1.7430 3.9410 -0.2617 0.3335  -0.2714 245  SER B OG  
5618  N  N   . LEU B  136 ? 1.4003 2.1054 4.0485 -0.3345 0.3005  -0.2767 246  LEU B N   
5619  C  CA  . LEU B  136 ? 1.0688 1.7759 3.5757 -0.3586 0.2545  -0.2466 246  LEU B CA  
5620  C  C   . LEU B  136 ? 1.0145 1.6862 3.4354 -0.3378 0.1928  -0.1989 246  LEU B C   
5621  O  O   . LEU B  136 ? 1.0192 1.6981 3.5775 -0.3051 0.1274  -0.1815 246  LEU B O   
5622  C  CB  . LEU B  136 ? 1.1388 1.9128 3.7463 -0.3706 0.2097  -0.2481 246  LEU B CB  
5623  C  CG  . LEU B  136 ? 1.1536 1.9716 3.8655 -0.3941 0.2716  -0.2946 246  LEU B CG  
5624  C  CD1 . LEU B  136 ? 1.2011 2.0886 4.0040 -0.4119 0.2220  -0.2924 246  LEU B CD1 
5625  C  CD2 . LEU B  136 ? 1.3648 2.1423 3.9280 -0.4279 0.3468  -0.3163 246  LEU B CD2 
5626  N  N   . HIS B  137 ? 1.0663 1.6877 3.3143 -0.3501 0.2167  -0.1865 247  HIS B N   
5627  C  CA  . HIS B  137 ? 1.3510 1.9367 3.5034 -0.3361 0.1697  -0.1424 247  HIS B CA  
5628  C  C   . HIS B  137 ? 1.3248 1.9228 3.3813 -0.3504 0.1032  -0.1104 247  HIS B C   
5629  O  O   . HIS B  137 ? 1.2481 1.8326 3.1464 -0.3787 0.1152  -0.1042 247  HIS B O   
5630  C  CB  . HIS B  137 ? 0.9256 1.4612 2.9395 -0.3466 0.2236  -0.1460 247  HIS B CB  
5631  C  CG  . HIS B  137 ? 0.9651 1.4799 3.0552 -0.3382 0.2950  -0.1854 247  HIS B CG  
5632  N  ND1 . HIS B  137 ? 1.2671 1.7470 3.2532 -0.3559 0.3602  -0.2141 247  HIS B ND1 
5633  C  CD2 . HIS B  137 ? 0.9989 1.5180 3.2686 -0.3123 0.3113  -0.2050 247  HIS B CD2 
5634  C  CE1 . HIS B  137 ? 1.5043 1.9652 3.5885 -0.3442 0.4142  -0.2495 247  HIS B CE1 
5635  N  NE2 . HIS B  137 ? 1.4705 1.9568 3.7225 -0.3185 0.3867  -0.2423 247  HIS B NE2 
5636  N  N   . LEU B  138 ? 1.3480 1.9586 3.5449 -0.3230 0.0296  -0.0941 248  LEU B N   
5637  C  CA  . LEU B  138 ? 1.0220 1.6381 3.1501 -0.3321 -0.0421 -0.0673 248  LEU B CA  
5638  C  C   . LEU B  138 ? 0.9164 1.4771 3.0254 -0.3004 -0.1075 -0.0210 248  LEU B C   
5639  O  O   . LEU B  138 ? 1.0778 1.6124 3.3419 -0.2572 -0.1425 -0.0043 248  LEU B O   
5640  C  CB  . LEU B  138 ? 1.1379 1.8019 3.4357 -0.3231 -0.0941 -0.0796 248  LEU B CB  
5641  C  CG  . LEU B  138 ? 1.2452 1.9697 3.6260 -0.3475 -0.0354 -0.1232 248  LEU B CG  
5642  C  CD1 . LEU B  138 ? 1.0639 1.8410 3.6136 -0.3394 -0.0984 -0.1318 248  LEU B CD1 
5643  C  CD2 . LEU B  138 ? 1.1741 1.8998 3.3957 -0.3981 0.0259  -0.1366 248  LEU B CD2 
5644  N  N   . LEU B  139 ? 0.8526 1.3921 2.7783 -0.3209 -0.1282 0.0029  249  LEU B N   
5645  C  CA  . LEU B  139 ? 0.9996 1.4818 2.8788 -0.2955 -0.1868 0.0529  249  LEU B CA  
5646  C  C   . LEU B  139 ? 0.8440 1.3110 2.6641 -0.2936 -0.2752 0.0808  249  LEU B C   
5647  O  O   . LEU B  139 ? 0.8191 1.2901 2.4694 -0.3280 -0.2548 0.0740  249  LEU B O   
5648  C  CB  . LEU B  139 ? 0.7939 1.2543 2.4932 -0.3195 -0.1204 0.0554  249  LEU B CB  
5649  C  CG  . LEU B  139 ? 0.7865 1.1931 2.4950 -0.2938 -0.1374 0.0993  249  LEU B CG  
5650  C  CD1 . LEU B  139 ? 0.9558 1.3602 2.4968 -0.3267 -0.0496 0.0794  249  LEU B CD1 
5651  C  CD2 . LEU B  139 ? 0.7858 1.1506 2.4501 -0.2754 -0.2349 0.1594  249  LEU B CD2 
5652  N  N   . VAL B  140 ? 0.8912 1.3339 2.8446 -0.2523 -0.3781 0.1101  250  VAL B N   
5653  C  CA  . VAL B  140 ? 0.9241 1.3332 2.8123 -0.2441 -0.4780 0.1395  250  VAL B CA  
5654  C  C   . VAL B  140 ? 0.9134 1.2472 2.6541 -0.2305 -0.5263 0.1981  250  VAL B C   
5655  O  O   . VAL B  140 ? 0.9312 1.2186 2.7199 -0.1962 -0.5680 0.2397  250  VAL B O   
5656  C  CB  . VAL B  140 ? 1.0031 1.4040 3.0578 -0.2036 -0.5784 0.1457  250  VAL B CB  
5657  C  CG1 . VAL B  140 ? 1.0638 1.3943 3.0116 -0.1847 -0.6947 0.1847  250  VAL B CG1 
5658  C  CG2 . VAL B  140 ? 1.0188 1.5038 3.1963 -0.2268 -0.5369 0.0898  250  VAL B CG2 
5659  N  N   . PHE B  141 ? 0.8942 1.2132 2.4547 -0.2567 -0.5245 0.2041  251  PHE B N   
5660  C  CA  . PHE B  141 ? 1.4524 1.7018 2.8481 -0.2477 -0.5681 0.2601  251  PHE B CA  
5661  C  C   . PHE B  141 ? 0.9737 1.1478 2.2737 -0.2258 -0.6800 0.2910  251  PHE B C   
5662  O  O   . PHE B  141 ? 0.9833 1.1706 2.2329 -0.2483 -0.6791 0.2650  251  PHE B O   
5663  C  CB  . PHE B  141 ? 1.4594 1.7367 2.6957 -0.2897 -0.4744 0.2393  251  PHE B CB  
5664  C  CG  . PHE B  141 ? 1.1258 1.3409 2.1899 -0.2830 -0.5166 0.2982  251  PHE B CG  
5665  C  CD1 . PHE B  141 ? 0.8092 1.0065 1.8689 -0.2729 -0.5125 0.3414  251  PHE B CD1 
5666  C  CD2 . PHE B  141 ? 1.0740 1.2447 1.9743 -0.2879 -0.5585 0.3125  251  PHE B CD2 
5667  C  CE1 . PHE B  141 ? 0.8219 0.9706 1.7097 -0.2681 -0.5505 0.3989  251  PHE B CE1 
5668  C  CE2 . PHE B  141 ? 1.1381 1.2442 1.8532 -0.2781 -0.5897 0.3636  251  PHE B CE2 
5669  C  CZ  . PHE B  141 ? 0.8586 0.9581 1.5594 -0.2663 -0.5840 0.4055  251  PHE B CZ  
5670  N  N   . VAL B  142 ? 1.0497 1.1353 2.2899 -0.1822 -0.7623 0.3395  252  VAL B N   
5671  C  CA  . VAL B  142 ? 1.1645 1.1591 2.2662 -0.1537 -0.8460 0.3506  252  VAL B CA  
5672  C  C   . VAL B  142 ? 1.2045 1.1181 2.0583 -0.1324 -0.8398 0.3828  252  VAL B C   
5673  O  O   . VAL B  142 ? 1.2186 1.1114 2.0424 -0.1030 -0.8244 0.4084  252  VAL B O   
5674  C  CB  . VAL B  142 ? 1.2670 1.2343 2.4758 -0.1081 -0.9189 0.3450  252  VAL B CB  
5675  C  CG1 . VAL B  142 ? 1.3947 1.2713 2.4226 -0.0773 -0.9832 0.3478  252  VAL B CG1 
5676  C  CG2 . VAL B  142 ? 1.2417 1.2976 2.6875 -0.1246 -0.9159 0.3028  252  VAL B CG2 
5677  N  N   . SER B  143 ? 1.2299 1.1027 1.9031 -0.1412 -0.8358 0.3743  253  SER B N   
5678  C  CA  . SER B  143 ? 1.2810 1.0917 1.7135 -0.1063 -0.8065 0.3812  253  SER B CA  
5679  C  C   . SER B  143 ? 1.3273 1.0990 1.6335 -0.1080 -0.8163 0.3578  253  SER B C   
5680  O  O   . SER B  143 ? 1.3110 1.1050 1.6676 -0.1530 -0.8202 0.3460  253  SER B O   
5681  C  CB  . SER B  143 ? 1.1935 1.0353 1.5478 -0.1229 -0.7295 0.3963  253  SER B CB  
5682  O  OG  . SER B  143 ? 1.7161 1.5979 2.0619 -0.1755 -0.6973 0.3850  253  SER B OG  
5683  N  N   . ASP B  144 ? 1.4136 1.1334 1.5596 -0.0554 -0.8105 0.3528  254  ASP B N   
5684  C  CA  . ASP B  144 ? 1.7190 1.3792 1.7661 -0.0619 -0.8374 0.3374  254  ASP B CA  
5685  C  C   . ASP B  144 ? 1.9352 1.5700 1.8282 -0.0661 -0.7812 0.3351  254  ASP B C   
5686  O  O   . ASP B  144 ? 2.3011 1.8611 2.0816 -0.0557 -0.8030 0.3272  254  ASP B O   
5687  C  CB  . ASP B  144 ? 1.6549 1.2334 1.6594 -0.0235 -0.9113 0.3398  254  ASP B CB  
5688  C  CG  . ASP B  144 ? 1.7423 1.2702 1.6133 0.0236  -0.8920 0.3574  254  ASP B CG  
5689  O  OD1 . ASP B  144 ? 1.6697 1.2404 1.5280 0.0332  -0.8282 0.3733  254  ASP B OD1 
5690  O  OD2 . ASP B  144 ? 1.8903 1.3340 1.6702 0.0514  -0.9411 0.3556  254  ASP B OD2 
5691  N  N   . ALA B  145 ? 1.3717 1.0689 1.2650 -0.0793 -0.7103 0.3389  255  ALA B N   
5692  C  CA  . ALA B  145 ? 1.3597 1.0506 1.1293 -0.0796 -0.6535 0.3329  255  ALA B CA  
5693  C  C   . ALA B  145 ? 1.2388 1.0101 1.0549 -0.1158 -0.5911 0.3280  255  ALA B C   
5694  O  O   . ALA B  145 ? 1.1248 0.9547 1.0652 -0.1405 -0.5912 0.3303  255  ALA B O   
5695  C  CB  . ALA B  145 ? 1.4313 1.0962 1.1033 -0.0294 -0.6316 0.3482  255  ALA B CB  
5696  N  N   . ASP B  146 ? 1.1981 0.9760 0.9198 -0.1150 -0.5379 0.3190  256  ASP B N   
5697  C  CA  . ASP B  146 ? 1.0757 0.9233 0.8209 -0.1469 -0.4777 0.3113  256  ASP B CA  
5698  C  C   . ASP B  146 ? 1.0124 0.9106 0.8070 -0.1376 -0.4471 0.3278  256  ASP B C   
5699  O  O   . ASP B  146 ? 1.7501 1.6247 1.5546 -0.1025 -0.4690 0.3471  256  ASP B O   
5700  C  CB  . ASP B  146 ? 1.0931 0.9316 0.7314 -0.1374 -0.4358 0.2947  256  ASP B CB  
5701  C  CG  . ASP B  146 ? 2.4377 2.3325 2.0963 -0.1797 -0.3865 0.2789  256  ASP B CG  
5702  O  OD1 . ASP B  146 ? 1.9002 1.8568 1.6387 -0.2118 -0.3646 0.2837  256  ASP B OD1 
5703  O  OD2 . ASP B  146 ? 2.1074 1.9836 1.7005 -0.1788 -0.3696 0.2619  256  ASP B OD2 
5704  N  N   . SER B  147 ? 1.7041 1.6672 1.5266 -0.1705 -0.3955 0.3215  257  SER B N   
5705  C  CA  . SER B  147 ? 0.8660 0.8699 0.7331 -0.1831 -0.3734 0.3485  257  SER B CA  
5706  C  C   . SER B  147 ? 0.8731 0.9291 0.6909 -0.1940 -0.3010 0.3264  257  SER B C   
5707  O  O   . SER B  147 ? 0.7548 0.8312 0.5508 -0.2167 -0.2774 0.2988  257  SER B O   
5708  C  CB  . SER B  147 ? 0.8373 0.8852 0.8806 -0.2539 -0.4256 0.4000  257  SER B CB  
5709  O  OG  . SER B  147 ? 0.7795 0.8799 0.8913 -0.3179 -0.4250 0.3967  257  SER B OG  
5710  N  N   . HIS B  148 ? 1.4677 1.5346 1.2662 -0.1734 -0.2688 0.3389  258  HIS B N   
5711  C  CA  . HIS B  148 ? 0.7406 0.8613 0.5127 -0.1852 -0.2095 0.3198  258  HIS B CA  
5712  C  C   . HIS B  148 ? 0.6447 0.8801 0.5122 -0.2760 -0.1916 0.3305  258  HIS B C   
5713  O  O   . HIS B  148 ? 0.6368 0.9172 0.5999 -0.3296 -0.2185 0.3814  258  HIS B O   
5714  C  CB  . HIS B  148 ? 1.3567 1.4571 1.0864 -0.1496 -0.1879 0.3397  258  HIS B CB  
5715  C  CG  . HIS B  148 ? 0.9098 0.9431 0.5353 -0.0898 -0.2032 0.3419  258  HIS B CG  
5716  N  ND1 . HIS B  148 ? 0.9303 0.9703 0.4932 -0.0729 -0.1846 0.3200  258  HIS B ND1 
5717  C  CD2 . HIS B  148 ? 1.0200 0.9792 0.5922 -0.0380 -0.2345 0.3643  258  HIS B CD2 
5718  C  CE1 . HIS B  148 ? 1.0464 1.0182 0.5166 -0.0120 -0.2008 0.3300  258  HIS B CE1 
5719  N  NE2 . HIS B  148 ? 1.7806 1.7099 1.2546 0.0087  -0.2296 0.3566  258  HIS B NE2 
5720  N  N   . PHE B  149 ? 0.5835 0.8627 0.4324 -0.2810 -0.1490 0.2808  259  PHE B N   
5721  C  CA  . PHE B  149 ? 1.5269 1.9060 1.4202 -0.3340 -0.1318 0.2562  259  PHE B CA  
5722  C  C   . PHE B  149 ? 1.7411 2.1294 1.6133 -0.3012 -0.0849 0.2215  259  PHE B C   
5723  O  O   . PHE B  149 ? 0.5399 0.9051 0.3846 -0.2695 -0.0767 0.2436  259  PHE B O   
5724  C  CB  . PHE B  149 ? 0.4990 0.8750 0.3744 -0.3472 -0.1308 0.2142  259  PHE B CB  
5725  C  CG  . PHE B  149 ? 0.8405 1.1790 0.6945 -0.3316 -0.1205 0.2014  259  PHE B CG  
5726  C  CD1 . PHE B  149 ? 0.5722 0.8231 0.3783 -0.3066 -0.1494 0.2238  259  PHE B CD1 
5727  C  CD2 . PHE B  149 ? 1.4439 1.8248 1.2880 -0.3323 -0.0973 0.1723  259  PHE B CD2 
5728  C  CE1 . PHE B  149 ? 0.6370 0.8418 0.3734 -0.2784 -0.1536 0.2130  259  PHE B CE1 
5729  C  CE2 . PHE B  149 ? 2.1672 2.5034 1.9525 -0.3039 -0.0959 0.1723  259  PHE B CE2 
5730  C  CZ  . PHE B  149 ? 1.8901 2.1349 1.6140 -0.2749 -0.1242 0.1902  259  PHE B CZ  
5731  N  N   . GLY B  150 ? 2.0150 2.4406 1.8816 -0.3190 -0.0652 0.1758  260  GLY B N   
5732  C  CA  . GLY B  150 ? 0.4836 0.9499 0.3408 -0.3204 -0.0438 0.1521  260  GLY B CA  
5733  C  C   . GLY B  150 ? 0.4745 0.9775 0.3331 -0.3045 -0.0527 0.1608  260  GLY B C   
5734  O  O   . GLY B  150 ? 0.4805 0.9646 0.3300 -0.2924 -0.0606 0.1696  260  GLY B O   
5735  N  N   . MET B  151 ? 0.5194 1.0493 0.3709 -0.2954 -0.0346 0.1624  261  MET B N   
5736  C  CA  . MET B  151 ? 0.5316 1.1006 0.3743 -0.2731 -0.0289 0.1672  261  MET B CA  
5737  C  C   . MET B  151 ? 1.3840 1.8876 1.1756 -0.2246 -0.0293 0.2051  261  MET B C   
5738  O  O   . MET B  151 ? 1.7278 2.2413 1.4861 -0.1926 -0.0212 0.2121  261  MET B O   
5739  C  CB  . MET B  151 ? 0.5793 1.2039 0.4426 -0.2865 -0.0348 0.1361  261  MET B CB  
5740  C  CG  . MET B  151 ? 0.4722 1.1449 0.3520 -0.3252 -0.0375 0.0915  261  MET B CG  
5741  S  SD  . MET B  151 ? 0.4637 1.1090 0.3463 -0.3202 -0.0300 0.0625  261  MET B SD  
5742  C  CE  . MET B  151 ? 1.9989 2.6784 1.8801 -0.3295 -0.0189 0.0260  261  MET B CE  
5743  N  N   . ASP B  152 ? 1.3684 1.7954 1.1377 -0.2142 -0.0432 0.2273  262  ASP B N   
5744  C  CA  . ASP B  152 ? 0.6961 1.0313 0.3847 -0.1628 -0.0553 0.2564  262  ASP B CA  
5745  C  C   . ASP B  152 ? 0.7508 1.0644 0.4106 -0.1431 -0.0382 0.2837  262  ASP B C   
5746  O  O   . ASP B  152 ? 0.8465 1.0952 0.4249 -0.0982 -0.0429 0.3005  262  ASP B O   
5747  C  CB  . ASP B  152 ? 0.7232 0.9824 0.3973 -0.1585 -0.0869 0.2701  262  ASP B CB  
5748  C  CG  . ASP B  152 ? 0.7194 0.9612 0.3825 -0.1633 -0.1053 0.2499  262  ASP B CG  
5749  O  OD1 . ASP B  152 ? 0.7465 0.9870 0.3689 -0.1423 -0.0993 0.2347  262  ASP B OD1 
5750  O  OD2 . ASP B  152 ? 0.7004 0.9218 0.3918 -0.1859 -0.1268 0.2530  262  ASP B OD2 
5751  N  N   . SER B  153 ? 0.7702 1.1239 0.4827 -0.1761 -0.0153 0.2857  263  SER B N   
5752  C  CA  . SER B  153 ? 2.0258 2.3495 1.7126 -0.1659 0.0142  0.3129  263  SER B CA  
5753  C  C   . SER B  153 ? 2.7764 3.1619 2.4545 -0.1632 0.0369  0.3021  263  SER B C   
5754  O  O   . SER B  153 ? 0.9122 1.2671 0.5553 -0.1532 0.0659  0.3261  263  SER B O   
5755  C  CB  . SER B  153 ? 0.8074 1.1273 0.5537 -0.2035 0.0436  0.3159  263  SER B CB  
5756  O  OG  . SER B  153 ? 0.7336 1.1307 0.5380 -0.2426 0.0512  0.2708  263  SER B OG  
5757  N  N   . LYS B  154 ? 2.5452 3.0100 2.2506 -0.1699 0.0243  0.2704  264  LYS B N   
5758  C  CA  . LYS B  154 ? 2.0308 2.5673 1.7369 -0.1650 0.0384  0.2618  264  LYS B CA  
5759  C  C   . LYS B  154 ? 0.8389 1.3214 0.4667 -0.1167 0.0467  0.2921  264  LYS B C   
5760  O  O   . LYS B  154 ? 0.8732 1.3934 0.4920 -0.1143 0.0704  0.3003  264  LYS B O   
5761  C  CB  . LYS B  154 ? 1.3083 1.9244 1.0524 -0.1722 0.0202  0.2284  264  LYS B CB  
5762  C  CG  . LYS B  154 ? 1.3733 2.0798 1.1283 -0.1655 0.0286  0.2195  264  LYS B CG  
5763  C  CD  . LYS B  154 ? 1.0435 1.8218 0.8390 -0.1739 0.0130  0.1884  264  LYS B CD  
5764  C  CE  . LYS B  154 ? 0.6327 1.5012 0.4348 -0.1531 0.0181  0.1850  264  LYS B CE  
5765  N  NZ  . LYS B  154 ? 0.6372 1.5698 0.4577 -0.1837 0.0275  0.1798  264  LYS B NZ  
5766  N  N   . LEU B  155 ? 0.8921 1.2784 0.4523 -0.0802 0.0252  0.3055  265  LEU B N   
5767  C  CA  . LEU B  155 ? 1.5137 1.8212 0.9756 -0.0362 0.0253  0.3301  265  LEU B CA  
5768  C  C   . LEU B  155 ? 2.2538 2.5052 1.6796 -0.0397 0.0495  0.3629  265  LEU B C   
5769  O  O   . LEU B  155 ? 2.0949 2.3296 1.4651 -0.0220 0.0679  0.3822  265  LEU B O   
5770  C  CB  . LEU B  155 ? 1.5192 1.7113 0.9008 -0.0051 -0.0137 0.3307  265  LEU B CB  
5771  C  CG  . LEU B  155 ? 1.4196 1.6367 0.8235 -0.0056 -0.0317 0.3005  265  LEU B CG  
5772  C  CD1 . LEU B  155 ? 1.9244 2.0056 1.2356 0.0199  -0.0733 0.3019  265  LEU B CD1 
5773  C  CD2 . LEU B  155 ? 1.5885 1.8772 0.9959 0.0104  -0.0185 0.2890  265  LEU B CD2 
5774  N  N   . ALA B  156 ? 1.7570 1.9743 1.2117 -0.0631 0.0532  0.3721  266  ALA B N   
5775  C  CA  . ALA B  156 ? 1.8867 2.0317 1.3039 -0.0682 0.0831  0.4059  266  ALA B CA  
5776  C  C   . ALA B  156 ? 1.5209 1.7381 0.9882 -0.1046 0.1385  0.4025  266  ALA B C   
5777  O  O   . ALA B  156 ? 1.2201 1.3724 0.6461 -0.1121 0.1782  0.4301  266  ALA B O   
5778  C  CB  . ALA B  156 ? 1.6553 1.7355 1.0940 -0.0785 0.0716  0.4193  266  ALA B CB  
5779  N  N   . GLY B  157 ? 1.6895 2.0277 1.2366 -0.1302 0.1402  0.3672  267  GLY B N   
5780  C  CA  . GLY B  157 ? 1.6746 2.0797 1.2720 -0.1689 0.1846  0.3534  267  GLY B CA  
5781  C  C   . GLY B  157 ? 0.9660 1.3789 0.6402 -0.2148 0.2064  0.3322  267  GLY B C   
5782  O  O   . GLY B  157 ? 0.9970 1.4223 0.7091 -0.2478 0.2580  0.3245  267  GLY B O   
5783  N  N   . ILE B  158 ? 1.1704 1.5768 0.8751 -0.2191 0.1729  0.3188  268  ILE B N   
5784  C  CA  . ILE B  158 ? 1.2459 1.6512 1.0252 -0.2586 0.1946  0.2952  268  ILE B CA  
5785  C  C   . ILE B  158 ? 0.7745 1.2691 0.5836 -0.2779 0.1566  0.2456  268  ILE B C   
5786  O  O   . ILE B  158 ? 0.7210 1.2327 0.5179 -0.2632 0.1083  0.2388  268  ILE B O   
5787  C  CB  . ILE B  158 ? 1.1389 1.4586 0.9277 -0.2518 0.1908  0.3196  268  ILE B CB  
5788  C  CG1 . ILE B  158 ? 1.2652 1.4790 0.9785 -0.2225 0.2036  0.3722  268  ILE B CG1 
5789  C  CG2 . ILE B  158 ? 0.8511 1.1605 0.7405 -0.2909 0.2363  0.2966  268  ILE B CG2 
5790  C  CD1 . ILE B  158 ? 0.9929 1.1154 0.6966 -0.2090 0.1793  0.4020  268  ILE B CD1 
5791  N  N   . VAL B  159 ? 0.7764 1.3200 0.6196 -0.3122 0.1799  0.2095  269  VAL B N   
5792  C  CA  . VAL B  159 ? 1.8658 2.4838 1.7124 -0.3339 0.1447  0.1584  269  VAL B CA  
5793  C  C   . VAL B  159 ? 1.9338 2.5342 1.8220 -0.3703 0.1716  0.1180  269  VAL B C   
5794  O  O   . VAL B  159 ? 0.7032 1.3454 0.5768 -0.3905 0.1466  0.0707  269  VAL B O   
5795  C  CB  . VAL B  159 ? 1.1649 1.8701 0.9964 -0.3387 0.1368  0.1445  269  VAL B CB  
5796  C  CG1 . VAL B  159 ? 0.7185 1.4537 0.5230 -0.2951 0.1069  0.1762  269  VAL B CG1 
5797  C  CG2 . VAL B  159 ? 0.8074 1.5002 0.6570 -0.3570 0.1965  0.1540  269  VAL B CG2 
5798  N  N   . CYS B  160 ? 1.8738 2.4099 1.8208 -0.3765 0.2227  0.1361  270  CYS B N   
5799  C  CA  . CYS B  160 ? 0.7787 1.2972 0.7895 -0.4043 0.2514  0.1020  270  CYS B CA  
5800  C  C   . CYS B  160 ? 0.7366 1.2206 0.7650 -0.3930 0.2324  0.1001  270  CYS B C   
5801  O  O   . CYS B  160 ? 0.7276 1.1654 0.7792 -0.3706 0.2332  0.1429  270  CYS B O   
5802  C  CB  . CYS B  160 ? 1.6586 2.1366 1.7556 -0.4151 0.3105  0.1287  270  CYS B CB  
5803  S  SG  . CYS B  160 ? 2.8194 3.3291 2.9160 -0.4349 0.3501  0.1383  270  CYS B SG  
5804  N  N   . PRO B  161 ? 1.7125 2.2151 1.7218 -0.4087 0.2152  0.0505  271  PRO B N   
5805  C  CA  . PRO B  161 ? 0.8527 1.3274 0.8758 -0.3991 0.1997  0.0474  271  PRO B CA  
5806  C  C   . PRO B  161 ? 0.6948 1.1223 0.8380 -0.3968 0.2366  0.0699  271  PRO B C   
5807  O  O   . PRO B  161 ? 0.7316 1.1489 0.9471 -0.4089 0.2733  0.0781  271  PRO B O   
5808  C  CB  . PRO B  161 ? 0.6854 1.1853 0.6592 -0.4222 0.1887  -0.0162 271  PRO B CB  
5809  C  CG  . PRO B  161 ? 0.6986 1.2538 0.6136 -0.4385 0.1741  -0.0402 271  PRO B CG  
5810  C  CD  . PRO B  161 ? 1.1398 1.6897 1.1048 -0.4378 0.2097  -0.0070 271  PRO B CD  
5811  N  N   . ASN B  162 ? 0.6634 1.0697 0.8382 -0.3845 0.2216  0.0807  272  ASN B N   
5812  C  CA  . ASN B  162 ? 1.3917 1.7694 1.7062 -0.3835 0.2448  0.1046  272  ASN B CA  
5813  C  C   . ASN B  162 ? 1.7736 2.1640 2.1198 -0.4075 0.2627  0.0590  272  ASN B C   
5814  O  O   . ASN B  162 ? 1.8066 2.2034 2.0997 -0.4131 0.2543  0.0154  272  ASN B O   
5815  C  CB  . ASN B  162 ? 0.6296 0.9823 0.9872 -0.3669 0.2224  0.1259  272  ASN B CB  
5816  C  CG  . ASN B  162 ? 0.6363 0.9609 1.1453 -0.3605 0.2307  0.1576  272  ASN B CG  
5817  O  OD1 . ASN B  162 ? 0.6469 1.0114 1.2048 -0.3826 0.2130  0.1627  272  ASN B OD1 
5818  N  ND2 . ASN B  162 ? 0.6663 0.9193 1.1552 -0.3553 0.2508  0.1481  272  ASN B ND2 
5819  N  N   . ASP B  163 ? 1.8799 2.2663 2.2943 -0.4253 0.2897  0.0622  273  ASP B N   
5820  C  CA  . ASP B  163 ? 1.3841 1.7639 1.8120 -0.4487 0.3167  0.0021  273  ASP B CA  
5821  C  C   . ASP B  163 ? 1.1330 1.5037 1.6333 -0.4465 0.3113  0.0018  273  ASP B C   
5822  O  O   . ASP B  163 ? 1.0441 1.4017 1.5483 -0.4585 0.3390  -0.0566 273  ASP B O   
5823  C  CB  . ASP B  163 ? 0.8501 1.2158 1.3136 -0.4719 0.3528  -0.0096 273  ASP B CB  
5824  C  CG  . ASP B  163 ? 0.8891 1.2425 1.4248 -0.4718 0.3468  0.0549  273  ASP B CG  
5825  O  OD1 . ASP B  163 ? 0.8167 1.1775 1.3783 -0.4580 0.3104  0.1067  273  ASP B OD1 
5826  O  OD2 . ASP B  163 ? 1.3779 1.7104 1.9345 -0.4919 0.3768  0.0498  273  ASP B OD2 
5827  N  N   . GLY B  164 ? 0.7315 1.1097 1.2862 -0.4349 0.2762  0.0616  274  GLY B N   
5828  C  CA  . GLY B  164 ? 1.0907 1.4669 1.7091 -0.4406 0.2692  0.0518  274  GLY B CA  
5829  C  C   . GLY B  164 ? 1.2339 1.5808 1.9228 -0.4540 0.3076  0.0207  274  GLY B C   
5830  O  O   . GLY B  164 ? 1.7716 2.1035 2.4991 -0.4551 0.3402  -0.0325 274  GLY B O   
5831  N  N   . LEU B  165 ? 0.8596 1.1888 1.5654 -0.4621 0.3105  0.0505  275  LEU B N   
5832  C  CA  . LEU B  165 ? 0.9211 1.2055 1.7031 -0.4679 0.3507  0.0251  275  LEU B CA  
5833  C  C   . LEU B  165 ? 0.9993 1.2523 1.8288 -0.4649 0.3301  0.0667  275  LEU B C   
5834  O  O   . LEU B  165 ? 1.1059 1.3683 1.8933 -0.4643 0.2877  0.1054  275  LEU B O   
5835  C  CB  . LEU B  165 ? 0.9695 1.2362 1.7209 -0.4830 0.3904  0.0045  275  LEU B CB  
5836  C  CG  . LEU B  165 ? 0.9779 1.2567 1.6772 -0.4889 0.4169  -0.0568 275  LEU B CG  
5837  C  CD1 . LEU B  165 ? 1.0327 1.2959 1.7004 -0.5104 0.4521  -0.0814 275  LEU B CD1 
5838  C  CD2 . LEU B  165 ? 1.3773 1.6379 2.1298 -0.4856 0.4458  -0.1127 275  LEU B CD2 
5839  N  N   . CYS B  166 ? 1.2764 1.4788 2.1917 -0.4614 0.3635  0.0526  276  CYS B N   
5840  C  CA  . CYS B  166 ? 1.5055 1.6552 2.4800 -0.4505 0.3482  0.0887  276  CYS B CA  
5841  C  C   . CYS B  166 ? 1.3044 1.4043 2.2230 -0.4640 0.3601  0.1285  276  CYS B C   
5842  O  O   . CYS B  166 ? 1.2298 1.3020 2.1382 -0.4796 0.3962  0.1191  276  CYS B O   
5843  C  CB  . CYS B  166 ? 1.5586 1.6648 2.6854 -0.4324 0.3894  0.0576  276  CYS B CB  
5844  S  SG  . CYS B  166 ? 1.9815 2.0106 3.3151 -0.3892 0.3846  0.0986  276  CYS B SG  
5845  N  N   . HIS B  167 ? 1.0173 1.0960 1.9029 -0.4560 0.3337  0.1743  277  HIS B N   
5846  C  CA  . HIS B  167 ? 1.2835 1.3023 2.1037 -0.4647 0.3490  0.2202  277  HIS B CA  
5847  C  C   . HIS B  167 ? 1.2478 1.1553 2.1619 -0.4228 0.3407  0.2882  277  HIS B C   
5848  O  O   . HIS B  167 ? 1.3413 1.2142 2.1881 -0.4068 0.3135  0.3473  277  HIS B O   
5849  C  CB  . HIS B  167 ? 1.4052 1.4896 2.0691 -0.4869 0.3225  0.2309  277  HIS B CB  
5850  C  CG  . HIS B  167 ? 1.5405 1.7252 2.1583 -0.5073 0.3212  0.2014  277  HIS B CG  
5851  N  ND1 . HIS B  167 ? 1.4579 1.6346 2.0934 -0.5194 0.3624  0.1900  277  HIS B ND1 
5852  C  CD2 . HIS B  167 ? 1.3163 1.5801 1.9206 -0.4988 0.3029  0.1839  277  HIS B CD2 
5853  C  CE1 . HIS B  167 ? 1.3273 1.5648 1.9579 -0.5162 0.3725  0.1564  277  HIS B CE1 
5854  N  NE2 . HIS B  167 ? 1.8023 2.0872 2.4164 -0.4989 0.3375  0.1557  277  HIS B NE2 
5855  N  N   . LEU B  168 ? 1.2048 1.0490 2.2714 -0.3970 0.3547  0.2913  278  LEU B N   
5856  C  CA  . LEU B  168 ? 1.2920 1.0147 2.4520 -0.3472 0.3257  0.3695  278  LEU B CA  
5857  C  C   . LEU B  168 ? 1.8328 1.4350 2.9705 -0.3475 0.3769  0.3900  278  LEU B C   
5858  O  O   . LEU B  168 ? 2.1504 1.7541 3.3554 -0.3639 0.4258  0.3386  278  LEU B O   
5859  C  CB  . LEU B  168 ? 1.2607 0.9968 2.6242 -0.3099 0.2848  0.3616  278  LEU B CB  
5860  C  CG  . LEU B  168 ? 1.3119 1.1597 2.7036 -0.3096 0.2284  0.3419  278  LEU B CG  
5861  C  CD1 . LEU B  168 ? 1.3339 1.2043 2.9469 -0.2772 0.1906  0.3251  278  LEU B CD1 
5862  C  CD2 . LEU B  168 ? 1.1403 0.9572 2.4332 -0.2928 0.1599  0.4183  278  LEU B CD2 
5863  N  N   . ASP B  169 ? 1.5364 1.0263 2.5588 -0.3260 0.3646  0.4650  279  ASP B N   
5864  C  CA  . ASP B  169 ? 1.6914 1.0522 2.6523 -0.3266 0.4112  0.4888  279  ASP B CA  
5865  C  C   . ASP B  169 ? 1.8153 1.0372 2.8820 -0.2642 0.3909  0.5204  279  ASP B C   
5866  O  O   . ASP B  169 ? 1.7622 1.0140 2.9860 -0.2286 0.3475  0.5079  279  ASP B O   
5867  C  CB  . ASP B  169 ? 2.3798 1.6686 3.1487 -0.3199 0.4034  0.5537  279  ASP B CB  
5868  C  CG  . ASP B  169 ? 2.2514 1.4875 2.9625 -0.2500 0.3166  0.6258  279  ASP B CG  
5869  O  OD1 . ASP B  169 ? 1.7876 1.0065 2.6143 -0.1969 0.2517  0.6373  279  ASP B OD1 
5870  O  OD2 . ASP B  169 ? 2.4469 1.6652 2.9901 -0.2441 0.3047  0.6654  279  ASP B OD2 
5871  N  N   . SER B  170 ? 1.9912 1.0612 2.9656 -0.2469 0.4153  0.5588  280  SER B N   
5872  C  CA  . SER B  170 ? 2.1393 1.0627 3.1735 -0.1756 0.3868  0.5865  280  SER B CA  
5873  C  C   . SER B  170 ? 2.4331 1.2964 3.4388 -0.0817 0.2747  0.6447  280  SER B C   
5874  O  O   . SER B  170 ? 2.7190 1.5139 3.8083 -0.0102 0.2228  0.6497  280  SER B O   
5875  C  CB  . SER B  170 ? 2.3344 1.1030 3.2396 -0.1810 0.4361  0.6123  280  SER B CB  
5876  O  OG  . SER B  170 ? 2.4009 1.1218 3.1087 -0.1845 0.4259  0.6653  280  SER B OG  
5877  N  N   . LYS B  171 ? 2.4789 1.3760 3.3582 -0.0756 0.2291  0.6809  281  LYS B N   
5878  C  CA  . LYS B  171 ? 2.2025 1.0653 3.0284 0.0126  0.1112  0.7219  281  LYS B CA  
5879  C  C   . LYS B  171 ? 2.0265 1.0364 3.0287 0.0145  0.0525  0.6902  281  LYS B C   
5880  O  O   . LYS B  171 ? 2.0473 1.0607 3.0123 0.0795  -0.0531 0.7101  281  LYS B O   
5881  C  CB  . LYS B  171 ? 2.3527 1.1744 2.9355 0.0226  0.0884  0.7690  281  LYS B CB  
5882  C  CG  . LYS B  171 ? 2.6568 1.3188 3.0514 0.0264  0.1311  0.8044  281  LYS B CG  
5883  C  CD  . LYS B  171 ? 2.5993 1.2318 2.7631 0.0326  0.1106  0.8411  281  LYS B CD  
5884  C  CE  . LYS B  171 ? 2.9064 1.3896 2.9086 0.0252  0.1480  0.8752  281  LYS B CE  
5885  N  NZ  . LYS B  171 ? 2.9218 1.3904 2.7227 0.0237  0.1255  0.9061  281  LYS B NZ  
5886  N  N   . ASN B  172 ? 1.8598 0.9925 3.0386 -0.0578 0.1186  0.6310  282  ASN B N   
5887  C  CA  . ASN B  172 ? 1.6902 0.9665 3.0359 -0.0745 0.0790  0.5931  282  ASN B CA  
5888  C  C   . ASN B  172 ? 1.6109 0.9508 2.8376 -0.0829 0.0245  0.6211  282  ASN B C   
5889  O  O   . ASN B  172 ? 1.5465 0.9474 2.8413 -0.0548 -0.0621 0.6183  282  ASN B O   
5890  C  CB  . ASN B  172 ? 1.7251 0.9883 3.2359 0.0027  -0.0068 0.5857  282  ASN B CB  
5891  C  CG  . ASN B  172 ? 2.1028 1.3688 3.8022 -0.0081 0.0590  0.5325  282  ASN B CG  
5892  O  OD1 . ASN B  172 ? 1.9856 1.3314 3.7497 -0.0881 0.1577  0.4762  282  ASN B OD1 
5893  N  ND2 . ASN B  172 ? 2.4204 1.6150 4.1858 0.0760  0.0016  0.5401  282  ASN B ND2 
5894  N  N   . GLU B  173 ? 1.7447 1.0762 2.7859 -0.1199 0.0737  0.6419  283  GLU B N   
5895  C  CA  . GLU B  173 ? 1.6832 1.0714 2.5851 -0.1269 0.0349  0.6663  283  GLU B CA  
5896  C  C   . GLU B  173 ? 1.6257 1.1566 2.5208 -0.2194 0.1203  0.6100  283  GLU B C   
5897  O  O   . GLU B  173 ? 1.7505 1.3198 2.6863 -0.2705 0.2066  0.5514  283  GLU B O   
5898  C  CB  . GLU B  173 ? 1.7138 0.9848 2.3704 -0.0779 0.0147  0.7238  283  GLU B CB  
5899  C  CG  . GLU B  173 ? 2.2642 1.3916 2.8637 0.0163  -0.0576 0.7540  283  GLU B CG  
5900  C  CD  . GLU B  173 ? 2.5629 1.5659 2.8955 0.0581  -0.0629 0.7935  283  GLU B CD  
5901  O  OE1 . GLU B  173 ? 2.5777 1.6215 2.7763 0.0282  -0.0368 0.7998  283  GLU B OE1 
5902  O  OE2 . GLU B  173 ? 2.6421 1.5032 2.8927 0.1226  -0.0914 0.8126  283  GLU B OE2 
5903  N  N   . TYR B  174 ? 1.3981 1.0101 2.2120 -0.2304 0.0847  0.6155  284  TYR B N   
5904  C  CA  . TYR B  174 ? 1.2196 0.9625 1.9675 -0.2969 0.1503  0.5519  284  TYR B CA  
5905  C  C   . TYR B  174 ? 1.3421 1.0437 1.9220 -0.3117 0.2073  0.5648  284  TYR B C   
5906  O  O   . TYR B  174 ? 1.3345 1.0078 1.7607 -0.2840 0.1795  0.6127  284  TYR B O   
5907  C  CB  . TYR B  174 ? 1.2878 1.1141 1.9838 -0.2960 0.0926  0.5555  284  TYR B CB  
5908  C  CG  . TYR B  174 ? 1.0144 0.9702 1.6502 -0.3480 0.1461  0.4659  284  TYR B CG  
5909  C  CD1 . TYR B  174 ? 1.0094 1.0004 1.6275 -0.3931 0.2221  0.3844  284  TYR B CD1 
5910  C  CD2 . TYR B  174 ? 0.9405 0.9626 1.5030 -0.3460 0.1060  0.4619  284  TYR B CD2 
5911  C  CE1 . TYR B  174 ? 0.9401 1.0209 1.4615 -0.4337 0.2485  0.3000  284  TYR B CE1 
5912  C  CE2 . TYR B  174 ? 0.8661 0.9707 1.3535 -0.3767 0.1513  0.3735  284  TYR B CE2 
5913  C  CZ  . TYR B  174 ? 0.8709 0.9938 1.3352 -0.4191 0.2243  0.2875  284  TYR B CZ  
5914  O  OH  . TYR B  174 ? 0.8165 0.9845 1.2036 -0.4327 0.2614  0.1936  284  TYR B OH  
5915  N  N   . SER B  175 ? 1.7342 1.4327 2.3332 -0.3532 0.2801  0.5168  285  SER B N   
5916  C  CA  . SER B  175 ? 1.6233 1.2850 2.0837 -0.3771 0.3274  0.5256  285  SER B CA  
5917  C  C   . SER B  175 ? 1.6926 1.4739 2.0397 -0.4203 0.3409  0.4752  285  SER B C   
5918  O  O   . SER B  175 ? 1.3806 1.1393 1.5984 -0.4228 0.3546  0.4993  285  SER B O   
5919  C  CB  . SER B  175 ? 1.8679 1.4972 2.3875 -0.4119 0.3833  0.4911  285  SER B CB  
5920  O  OG  . SER B  175 ? 1.3712 1.1224 1.9577 -0.4563 0.3982  0.4048  285  SER B OG  
5921  N  N   . MET B  176 ? 1.2782 1.1788 1.6599 -0.4510 0.3337  0.4007  286  MET B N   
5922  C  CA  . MET B  176 ? 1.1289 1.1307 1.3972 -0.4882 0.3391  0.3411  286  MET B CA  
5923  C  C   . MET B  176 ? 1.0668 1.0705 1.3030 -0.4360 0.3168  0.3504  286  MET B C   
5924  O  O   . MET B  176 ? 1.2170 1.2804 1.4481 -0.4283 0.3260  0.2802  286  MET B O   
5925  C  CB  . MET B  176 ? 1.0410 1.1809 1.3582 -0.5136 0.3082  0.2846  286  MET B CB  
5926  C  CG  . MET B  176 ? 1.0888 1.2219 1.4978 -0.5374 0.3356  0.3012  286  MET B CG  
5927  S  SD  . MET B  176 ? 3.1902 3.3304 3.5660 -0.5493 0.3668  0.3378  286  MET B SD  
5928  C  CE  . MET B  176 ? 2.1199 2.3958 2.5519 -0.5159 0.3718  0.3200  286  MET B CE  
5929  N  N   . SER B  177 ? 1.1199 1.0575 1.3321 -0.3789 0.2692  0.4508  287  SER B N   
5930  C  CA  . SER B  177 ? 1.0729 1.0382 1.2292 -0.3330 0.2027  0.4892  287  SER B CA  
5931  C  C   . SER B  177 ? 1.0805 1.0618 1.0879 -0.3099 0.2134  0.4818  287  SER B C   
5932  O  O   . SER B  177 ? 1.7639 1.8119 1.7320 -0.2928 0.1836  0.4572  287  SER B O   
5933  C  CB  . SER B  177 ? 1.1580 1.0252 1.3095 -0.2765 0.1237  0.5840  287  SER B CB  
5934  O  OG  . SER B  177 ? 1.9302 1.8150 1.9979 -0.2349 0.0455  0.6030  287  SER B OG  
5935  N  N   . THR B  178 ? 1.4245 1.3403 1.3539 -0.3087 0.2546  0.4978  288  THR B N   
5936  C  CA  . THR B  178 ? 1.2014 1.1234 1.0138 -0.2878 0.2760  0.4811  288  THR B CA  
5937  C  C   . THR B  178 ? 1.1516 1.1368 1.0240 -0.3222 0.3498  0.4013  288  THR B C   
5938  O  O   . THR B  178 ? 1.1571 1.1641 0.9782 -0.3069 0.3710  0.3959  288  THR B O   
5939  C  CB  . THR B  178 ? 1.5286 1.3342 1.2280 -0.2715 0.2849  0.5333  288  THR B CB  
5940  O  OG1 . THR B  178 ? 1.8478 1.6248 1.5954 -0.3355 0.3466  0.5215  288  THR B OG1 
5941  C  CG2 . THR B  178 ? 1.9140 1.6163 1.5647 -0.2125 0.2093  0.6029  288  THR B CG2 
5942  N  N   . VAL B  179 ? 1.2352 1.2535 1.2355 -0.3542 0.3784  0.3457  289  VAL B N   
5943  C  CA  . VAL B  179 ? 1.0248 1.1318 1.1394 -0.3528 0.4131  0.3086  289  VAL B CA  
5944  C  C   . VAL B  179 ? 0.9134 1.1216 1.0773 -0.3520 0.3772  0.2831  289  VAL B C   
5945  O  O   . VAL B  179 ? 0.8888 1.1817 1.0443 -0.3595 0.3641  0.2602  289  VAL B O   
5946  C  CB  . VAL B  179 ? 1.0506 1.1454 1.3121 -0.3541 0.4474  0.3112  289  VAL B CB  
5947  C  CG1 . VAL B  179 ? 1.5075 1.7700 1.8451 -0.3791 0.4244  0.3479  289  VAL B CG1 
5948  C  CG2 . VAL B  179 ? 1.2301 1.2250 1.2294 -0.4842 0.4131  0.2827  289  VAL B CG2 
5949  N  N   . LEU B  180 ? 0.8682 1.0607 1.0495 -0.3508 0.3458  0.2699  290  LEU B N   
5950  C  CA  . LEU B  180 ? 0.8137 1.0811 1.0190 -0.3505 0.3048  0.2355  290  LEU B CA  
5951  C  C   . LEU B  180 ? 0.8353 1.1146 0.9380 -0.3301 0.2404  0.2458  290  LEU B C   
5952  O  O   . LEU B  180 ? 1.0803 1.3053 1.1357 -0.3133 0.2170  0.2868  290  LEU B O   
5953  C  CB  . LEU B  180 ? 0.7637 1.0235 1.1073 -0.3591 0.3156  0.2181  290  LEU B CB  
5954  C  CG  . LEU B  180 ? 0.7951 1.0814 1.2426 -0.3675 0.3227  0.2462  290  LEU B CG  
5955  C  CD1 . LEU B  180 ? 0.7786 1.1146 1.2840 -0.3982 0.2731  0.2529  290  LEU B CD1 
5956  C  CD2 . LEU B  180 ? 1.1371 1.4868 1.5467 -0.4016 0.3427  0.2196  290  LEU B CD2 
5957  N  N   . GLU B  181 ? 0.8593 1.2049 0.9208 -0.3313 0.2040  0.2130  291  GLU B N   
5958  C  CA  . GLU B  181 ? 1.0312 1.3941 1.0179 -0.3131 0.1422  0.2219  291  GLU B CA  
5959  C  C   . GLU B  181 ? 0.8637 1.1915 0.9110 -0.3159 0.1314  0.2276  291  GLU B C   
5960  O  O   . GLU B  181 ? 0.6420 0.9461 0.8028 -0.3329 0.1707  0.2091  291  GLU B O   
5961  C  CB  . GLU B  181 ? 0.6215 1.0531 0.5567 -0.3220 0.1101  0.1773  291  GLU B CB  
5962  C  CG  . GLU B  181 ? 1.3884 1.8734 1.2801 -0.3235 0.1070  0.1652  291  GLU B CG  
5963  C  CD  . GLU B  181 ? 0.9994 1.5493 0.8594 -0.3390 0.0709  0.1174  291  GLU B CD  
5964  O  OE1 . GLU B  181 ? 0.5749 1.1141 0.4339 -0.3501 0.0587  0.0915  291  GLU B OE1 
5965  O  OE2 . GLU B  181 ? 0.5957 1.2064 0.4386 -0.3415 0.0585  0.1063  291  GLU B OE2 
5966  N  N   . TYR B  182 ? 0.8329 1.1604 0.8196 -0.2991 0.0754  0.2500  292  TYR B N   
5967  C  CA  . TYR B  182 ? 1.1780 1.5042 1.2191 -0.3166 0.0489  0.2559  292  TYR B CA  
5968  C  C   . TYR B  182 ? 1.5047 1.8499 1.5836 -0.3269 0.0734  0.1915  292  TYR B C   
5969  O  O   . TYR B  182 ? 0.5547 0.9393 0.5628 -0.3309 0.0709  0.1617  292  TYR B O   
5970  C  CB  . TYR B  182 ? 0.5964 0.9375 0.5596 -0.3098 -0.0324 0.3040  292  TYR B CB  
5971  C  CG  . TYR B  182 ? 0.7372 1.0286 0.6438 -0.2752 -0.0662 0.3619  292  TYR B CG  
5972  C  CD1 . TYR B  182 ? 0.6821 0.9386 0.4950 -0.2218 -0.0548 0.3369  292  TYR B CD1 
5973  C  CD2 . TYR B  182 ? 1.6631 1.8984 1.6103 -0.2729 -0.1061 0.4258  292  TYR B CD2 
5974  C  CE1 . TYR B  182 ? 0.7793 0.9411 0.5115 -0.1643 -0.0698 0.3617  292  TYR B CE1 
5975  C  CE2 . TYR B  182 ? 2.0446 2.1839 1.9061 -0.2082 -0.1332 0.4480  292  TYR B CE2 
5976  C  CZ  . TYR B  182 ? 1.5510 1.6478 1.2921 -0.1512 -0.1058 0.4081  292  TYR B CZ  
5977  O  OH  . TYR B  182 ? 0.9667 0.9560 0.6107 -0.0828 -0.1226 0.4204  292  TYR B OH  
5978  N  N   . PRO B  183 ? 2.0360 2.3645 2.2277 -0.3389 0.0895  0.1712  293  PRO B N   
5979  C  CA  . PRO B  183 ? 1.0099 1.3590 1.2227 -0.3505 0.1051  0.1262  293  PRO B CA  
5980  C  C   . PRO B  183 ? 0.5309 0.8902 0.6442 -0.3500 0.0607  0.1246  293  PRO B C   
5981  O  O   . PRO B  183 ? 0.5183 0.8643 0.5994 -0.3421 0.0153  0.1598  293  PRO B O   
5982  C  CB  . PRO B  183 ? 0.5534 0.8829 0.9498 -0.3577 0.1363  0.1113  293  PRO B CB  
5983  C  CG  . PRO B  183 ? 0.5574 0.8598 0.9760 -0.3589 0.1123  0.1306  293  PRO B CG  
5984  C  CD  . PRO B  183 ? 0.5698 0.8664 0.8761 -0.3479 0.0900  0.1841  293  PRO B CD  
5985  N  N   . THR B  184 ? 0.6392 1.0173 0.6916 -0.3613 0.0708  0.0834  294  THR B N   
5986  C  CA  . THR B  184 ? 0.9885 1.3702 0.9453 -0.3667 0.0387  0.0723  294  THR B CA  
5987  C  C   . THR B  184 ? 0.8662 1.2294 0.9243 -0.3771 0.0601  0.0584  294  THR B C   
5988  O  O   . THR B  184 ? 1.7734 2.1322 1.9812 -0.3795 0.0933  0.0519  294  THR B O   
5989  C  CB  . THR B  184 ? 1.4432 1.8521 1.2902 -0.3797 0.0325  0.0257  294  THR B CB  
5990  O  OG1 . THR B  184 ? 0.5717 0.9728 0.4610 -0.3958 0.0818  -0.0193 294  THR B OG1 
5991  C  CG2 . THR B  184 ? 0.5264 0.9707 0.3452 -0.3754 0.0164  0.0277  294  THR B CG2 
5992  N  N   . ILE B  185 ? 0.6770 1.0327 0.6648 -0.3844 0.0362  0.0554  295  ILE B N   
5993  C  CA  . ILE B  185 ? 0.5686 0.9133 0.6538 -0.3980 0.0565  0.0369  295  ILE B CA  
5994  C  C   . ILE B  185 ? 0.9378 1.2921 1.0432 -0.4119 0.1070  -0.0109 295  ILE B C   
5995  O  O   . ILE B  185 ? 0.6157 0.9720 0.8511 -0.4204 0.1324  -0.0204 295  ILE B O   
5996  C  CB  . ILE B  185 ? 1.4420 1.7703 1.4281 -0.4069 0.0231  0.0447  295  ILE B CB  
5997  C  CG1 . ILE B  185 ? 0.6159 0.9255 0.5897 -0.3949 -0.0339 0.0960  295  ILE B CG1 
5998  C  CG2 . ILE B  185 ? 2.1205 2.4418 2.2051 -0.4257 0.0476  0.0204  295  ILE B CG2 
5999  C  CD1 . ILE B  185 ? 0.5850 0.8641 0.4819 -0.4054 -0.0707 0.1121  295  ILE B CD1 
6000  N  N   . GLY B  186 ? 1.1907 1.5527 1.1654 -0.4174 0.1132  -0.0441 296  GLY B N   
6001  C  CA  . GLY B  186 ? 0.6447 1.0072 0.6259 -0.4332 0.1567  -0.0966 296  GLY B CA  
6002  C  C   . GLY B  186 ? 1.2158 1.5839 1.3267 -0.4287 0.1881  -0.0920 296  GLY B C   
6003  O  O   . GLY B  186 ? 1.6559 2.0198 1.8404 -0.4402 0.2246  -0.1199 296  GLY B O   
6004  N  N   . GLN B  187 ? 0.6257 1.0017 0.7599 -0.4140 0.1743  -0.0575 297  GLN B N   
6005  C  CA  . GLN B  187 ? 0.8129 1.1917 1.0676 -0.4124 0.2000  -0.0464 297  GLN B CA  
6006  C  C   . GLN B  187 ? 0.8133 1.1950 1.2274 -0.4111 0.1962  -0.0133 297  GLN B C   
6007  O  O   . GLN B  187 ? 1.3453 1.7325 1.8350 -0.4230 0.2231  -0.0302 297  GLN B O   
6008  C  CB  . GLN B  187 ? 1.2319 1.6147 1.4777 -0.3989 0.1866  -0.0110 297  GLN B CB  
6009  C  CG  . GLN B  187 ? 1.5675 1.9643 1.6720 -0.4046 0.1792  -0.0376 297  GLN B CG  
6010  C  CD  . GLN B  187 ? 0.6139 1.0177 0.7255 -0.3938 0.1739  -0.0019 297  GLN B CD  
6011  O  OE1 . GLN B  187 ? 0.6205 1.0127 0.8432 -0.3897 0.1963  0.0262  297  GLN B OE1 
6012  N  NE2 . GLN B  187 ? 1.1805 1.6067 1.1789 -0.3904 0.1401  0.0001  297  GLN B NE2 
6013  N  N   . LEU B  188 ? 0.5961 0.9740 1.0547 -0.4004 0.1585  0.0265  298  LEU B N   
6014  C  CA  . LEU B  188 ? 0.5928 0.9868 1.1990 -0.4080 0.1315  0.0647  298  LEU B CA  
6015  C  C   . LEU B  188 ? 0.6368 1.0432 1.2515 -0.4306 0.1570  0.0231  298  LEU B C   
6016  O  O   . LEU B  188 ? 1.4724 1.8985 2.1672 -0.4471 0.1695  0.0117  298  LEU B O   
6017  C  CB  . LEU B  188 ? 0.5632 0.9194 1.1968 -0.3818 0.0956  0.0740  298  LEU B CB  
6018  C  CG  . LEU B  188 ? 0.5495 0.8774 1.1518 -0.3708 0.1028  0.0543  298  LEU B CG  
6019  C  CD1 . LEU B  188 ? 0.5401 0.8670 1.0503 -0.3792 0.0483  0.0696  298  LEU B CD1 
6020  C  CD2 . LEU B  188 ? 0.6052 0.9483 1.1908 -0.4082 0.1287  0.0004  298  LEU B CD2 
6021  N  N   . ILE B  189 ? 0.6480 1.0367 1.1660 -0.4327 0.1749  -0.0163 299  ILE B N   
6022  C  CA  . ILE B  189 ? 1.0015 1.3911 1.5301 -0.4523 0.2103  -0.0616 299  ILE B CA  
6023  C  C   . ILE B  189 ? 0.7814 1.1649 1.3181 -0.4590 0.2651  -0.1137 299  ILE B C   
6024  O  O   . ILE B  189 ? 1.0607 1.4463 1.6739 -0.4701 0.2982  -0.1447 299  ILE B O   
6025  C  CB  . ILE B  189 ? 1.6507 2.0194 2.0455 -0.4596 0.2157  -0.0913 299  ILE B CB  
6026  C  CG1 . ILE B  189 ? 1.3500 1.7155 1.7606 -0.4573 0.1684  -0.0504 299  ILE B CG1 
6027  C  CG2 . ILE B  189 ? 2.0477 2.4071 2.4322 -0.4814 0.2653  -0.1484 299  ILE B CG2 
6028  C  CD1 . ILE B  189 ? 0.6995 1.0423 0.9548 -0.4684 0.1696  -0.0755 299  ILE B CD1 
6029  N  N   . ASP B  190 ? 1.0371 1.4098 1.5013 -0.4532 0.2767  -0.1283 300  ASP B N   
6030  C  CA  . ASP B  190 ? 1.3595 1.7171 1.8275 -0.4626 0.3262  -0.1819 300  ASP B CA  
6031  C  C   . ASP B  190 ? 1.5428 1.9067 2.1428 -0.4585 0.3380  -0.1682 300  ASP B C   
6032  O  O   . ASP B  190 ? 1.6331 1.9781 2.2652 -0.4660 0.3853  -0.2173 300  ASP B O   
6033  C  CB  . ASP B  190 ? 0.7938 1.1418 1.1444 -0.4645 0.3285  -0.2038 300  ASP B CB  
6034  C  CG  . ASP B  190 ? 1.7691 2.0961 2.1105 -0.4809 0.3767  -0.2664 300  ASP B CG  
6035  O  OD1 . ASP B  190 ? 2.1582 2.4675 2.5176 -0.4937 0.4129  -0.3120 300  ASP B OD1 
6036  O  OD2 . ASP B  190 ? 0.8545 1.1810 1.1773 -0.4825 0.3801  -0.2696 300  ASP B OD2 
6037  N  N   . LYS B  191 ? 1.5877 1.9731 2.2591 -0.4493 0.2960  -0.1073 301  LYS B N   
6038  C  CA  . LYS B  191 ? 1.1788 1.5654 1.9584 -0.4471 0.3042  -0.0994 301  LYS B CA  
6039  C  C   . LYS B  191 ? 0.8520 1.2564 1.7449 -0.4473 0.2886  -0.0902 301  LYS B C   
6040  O  O   . LYS B  191 ? 0.8332 1.2304 1.8314 -0.4402 0.3076  -0.1033 301  LYS B O   
6041  C  CB  . LYS B  191 ? 1.1514 1.5432 1.9150 -0.4420 0.2719  -0.0478 301  LYS B CB  
6042  C  CG  . LYS B  191 ? 0.7837 1.1577 1.4785 -0.4424 0.2997  -0.0661 301  LYS B CG  
6043  C  CD  . LYS B  191 ? 0.8476 1.1936 1.5906 -0.4491 0.3564  -0.1211 301  LYS B CD  
6044  C  CE  . LYS B  191 ? 0.8647 1.1957 1.5263 -0.4579 0.3804  -0.1476 301  LYS B CE  
6045  N  NZ  . LYS B  191 ? 0.9275 1.2264 1.6323 -0.4683 0.4344  -0.2005 301  LYS B NZ  
6046  N  N   . LEU B  192 ? 0.8530 1.2771 1.7330 -0.4539 0.2563  -0.0726 302  LEU B N   
6047  C  CA  . LEU B  192 ? 0.8145 1.2594 1.8028 -0.4573 0.2416  -0.0735 302  LEU B CA  
6048  C  C   . LEU B  192 ? 1.2928 1.7333 2.3426 -0.4620 0.2963  -0.1289 302  LEU B C   
6049  O  O   . LEU B  192 ? 1.3418 1.8022 2.5068 -0.4624 0.2954  -0.1387 302  LEU B O   
6050  C  CB  . LEU B  192 ? 0.7831 1.2485 1.7235 -0.4700 0.1818  -0.0330 302  LEU B CB  
6051  C  CG  . LEU B  192 ? 0.7996 1.2704 1.6979 -0.4711 0.1255  0.0107  302  LEU B CG  
6052  C  CD1 . LEU B  192 ? 0.9376 1.4205 1.7737 -0.4909 0.0767  0.0296  302  LEU B CD1 
6053  C  CD2 . LEU B  192 ? 0.9903 1.4567 2.0147 -0.4519 0.1211  0.0021  302  LEU B CD2 
6054  N  N   . VAL B  193 ? 0.8838 1.2976 1.8581 -0.4665 0.3446  -0.1706 303  VAL B N   
6055  C  CA  . VAL B  193 ? 0.9106 1.3108 1.9240 -0.4752 0.4044  -0.2305 303  VAL B CA  
6056  C  C   . VAL B  193 ? 1.2417 1.6131 2.2988 -0.4684 0.4561  -0.2724 303  VAL B C   
6057  O  O   . VAL B  193 ? 1.5163 1.8828 2.6769 -0.4681 0.4977  -0.3095 303  VAL B O   
6058  C  CB  . VAL B  193 ? 1.0908 1.4721 1.9747 -0.4911 0.4236  -0.2588 303  VAL B CB  
6059  C  CG1 . VAL B  193 ? 1.6180 1.9814 2.5367 -0.5058 0.4875  -0.3220 303  VAL B CG1 
6060  C  CG2 . VAL B  193 ? 0.8886 1.2901 1.7280 -0.4972 0.3725  -0.2149 303  VAL B CG2 
6061  N  N   . GLN B  194 ? 1.0867 1.4384 2.0716 -0.4640 0.4546  -0.2670 304  GLN B N   
6062  C  CA  . GLN B  194 ? 1.3370 1.6587 2.3676 -0.4599 0.4987  -0.3008 304  GLN B CA  
6063  C  C   . GLN B  194 ? 1.5306 1.8611 2.7164 -0.4432 0.4950  -0.2839 304  GLN B C   
6064  O  O   . GLN B  194 ? 1.4514 1.7564 2.7153 -0.4387 0.5417  -0.3209 304  GLN B O   
6065  C  CB  . GLN B  194 ? 1.1089 1.4160 2.0461 -0.4608 0.4887  -0.2881 304  GLN B CB  
6066  C  CG  . GLN B  194 ? 1.4958 1.7874 2.2888 -0.4764 0.5014  -0.3227 304  GLN B CG  
6067  C  CD  . GLN B  194 ? 1.5497 1.8354 2.2695 -0.4780 0.4895  -0.3102 304  GLN B CD  
6068  O  OE1 . GLN B  194 ? 1.1414 1.4268 1.9210 -0.4699 0.4827  -0.2803 304  GLN B OE1 
6069  N  NE2 . GLN B  194 ? 1.5140 1.7951 2.1041 -0.4903 0.4865  -0.3345 304  GLN B NE2 
6070  N  N   . ASN B  195 ? 1.4823 1.8449 2.7125 -0.4339 0.4389  -0.2308 305  ASN B N   
6071  C  CA  . ASN B  195 ? 1.3285 1.7016 2.7106 -0.4158 0.4267  -0.2171 305  ASN B CA  
6072  C  C   . ASN B  195 ? 0.9477 1.3564 2.4252 -0.4158 0.4133  -0.2218 305  ASN B C   
6073  O  O   . ASN B  195 ? 0.9605 1.3822 2.5854 -0.3987 0.4074  -0.2218 305  ASN B O   
6074  C  CB  . ASN B  195 ? 1.1218 1.4992 2.4941 -0.4054 0.3711  -0.1597 305  ASN B CB  
6075  C  CG  . ASN B  195 ? 1.3016 1.6537 2.5572 -0.4128 0.3777  -0.1476 305  ASN B CG  
6076  O  OD1 . ASN B  195 ? 1.3992 1.7211 2.6411 -0.4166 0.4279  -0.1845 305  ASN B OD1 
6077  N  ND2 . ASN B  195 ? 1.4027 1.7671 2.5729 -0.4172 0.3281  -0.0990 305  ASN B ND2 
6078  N  N   . ASN B  196 ? 0.9450 1.3692 2.3479 -0.4348 0.4103  -0.2281 306  ASN B N   
6079  C  CA  . ASN B  196 ? 0.9581 1.4182 2.4403 -0.4425 0.3988  -0.2323 306  ASN B CA  
6080  C  C   . ASN B  196 ? 0.9256 1.4181 2.4865 -0.4304 0.3305  -0.1879 306  ASN B C   
6081  O  O   . ASN B  196 ? 0.9436 1.4517 2.6584 -0.4122 0.3270  -0.1949 306  ASN B O   
6082  C  CB  . ASN B  196 ? 1.3741 1.8329 2.9829 -0.4407 0.4597  -0.2855 306  ASN B CB  
6083  C  CG  . ASN B  196 ? 1.1305 1.6301 2.8181 -0.4549 0.4568  -0.2951 306  ASN B CG  
6084  O  OD1 . ASN B  196 ? 1.2301 1.7445 2.8367 -0.4745 0.4297  -0.2766 306  ASN B OD1 
6085  N  ND2 . ASN B  196 ? 1.1043 1.6232 2.9556 -0.4463 0.4849  -0.3237 306  ASN B ND2 
6086  N  N   . VAL B  197 ? 0.8817 1.3814 2.3393 -0.4390 0.2746  -0.1449 307  VAL B N   
6087  C  CA  . VAL B  197 ? 0.8547 1.3737 2.3608 -0.4284 0.2050  -0.1071 307  VAL B CA  
6088  C  C   . VAL B  197 ? 0.8487 1.3920 2.3029 -0.4525 0.1670  -0.0939 307  VAL B C   
6089  O  O   . VAL B  197 ? 0.8346 1.3675 2.1478 -0.4743 0.1708  -0.0849 307  VAL B O   
6090  C  CB  . VAL B  197 ? 1.2110 1.7035 2.6347 -0.4171 0.1738  -0.0697 307  VAL B CB  
6091  C  CG1 . VAL B  197 ? 1.1658 1.6646 2.6411 -0.3999 0.1024  -0.0372 307  VAL B CG1 
6092  C  CG2 . VAL B  197 ? 0.9894 1.4526 2.4568 -0.3999 0.2169  -0.0830 307  VAL B CG2 
6093  N  N   . LEU B  198 ? 1.3021 1.8769 2.8783 -0.4481 0.1304  -0.0946 308  LEU B N   
6094  C  CA  . LEU B  198 ? 0.8692 1.4648 2.4111 -0.4726 0.0875  -0.0835 308  LEU B CA  
6095  C  C   . LEU B  198 ? 0.9458 1.5284 2.4488 -0.4577 0.0113  -0.0490 308  LEU B C   
6096  O  O   . LEU B  198 ? 0.8410 1.4291 2.4649 -0.4255 -0.0315 -0.0411 308  LEU B O   
6097  C  CB  . LEU B  198 ? 0.9175 1.5569 2.6197 -0.4789 0.0920  -0.1102 308  LEU B CB  
6098  C  CG  . LEU B  198 ? 1.2896 1.9390 3.0342 -0.4957 0.1702  -0.1510 308  LEU B CG  
6099  C  CD1 . LEU B  198 ? 1.3298 2.0312 3.2385 -0.5055 0.1671  -0.1737 308  LEU B CD1 
6100  C  CD2 . LEU B  198 ? 1.3327 1.9562 2.9119 -0.5269 0.1996  -0.1500 308  LEU B CD2 
6101  N  N   . LEU B  199 ? 1.3198 1.8807 2.6575 -0.4775 -0.0076 -0.0302 309  LEU B N   
6102  C  CA  . LEU B  199 ? 1.2178 1.7498 2.4959 -0.4571 -0.0702 -0.0034 309  LEU B CA  
6103  C  C   . LEU B  199 ? 0.8038 1.3401 2.0982 -0.4631 -0.1300 -0.0018 309  LEU B C   
6104  O  O   . LEU B  199 ? 0.8159 1.3544 2.0235 -0.5003 -0.1176 -0.0135 309  LEU B O   
6105  C  CB  . LEU B  199 ? 0.7428 1.2442 1.8391 -0.4686 -0.0512 0.0072  309  LEU B CB  
6106  C  CG  . LEU B  199 ? 0.7118 1.1710 1.7561 -0.4351 -0.1067 0.0352  309  LEU B CG  
6107  C  CD1 . LEU B  199 ? 0.7207 1.1616 1.9070 -0.3925 -0.1400 0.0677  309  LEU B CD1 
6108  C  CD2 . LEU B  199 ? 0.6762 1.1112 1.5639 -0.4444 -0.0746 0.0325  309  LEU B CD2 
6109  N  N   . ILE B  200 ? 0.8202 1.3526 2.2343 -0.4258 -0.2000 0.0146  310  ILE B N   
6110  C  CA  . ILE B  200 ? 1.1195 1.6438 2.5703 -0.4217 -0.2778 0.0239  310  ILE B CA  
6111  C  C   . ILE B  200 ? 0.8554 1.3052 2.2159 -0.3888 -0.3586 0.0729  310  ILE B C   
6112  O  O   . ILE B  200 ? 0.8582 1.2675 2.2656 -0.3463 -0.4092 0.1139  310  ILE B O   
6113  C  CB  . ILE B  200 ? 0.9102 1.4631 2.5801 -0.3939 -0.3307 0.0218  310  ILE B CB  
6114  C  CG1 . ILE B  200 ? 0.9233 1.5476 2.6830 -0.4253 -0.2535 -0.0213 310  ILE B CG1 
6115  C  CG2 . ILE B  200 ? 0.9639 1.4996 2.6567 -0.3876 -0.4255 0.0347  310  ILE B CG2 
6116  C  CD1 . ILE B  200 ? 0.9723 1.6332 2.9648 -0.3949 -0.2955 -0.0310 310  ILE B CD1 
6117  N  N   . PHE B  201 ? 0.8595 1.2822 2.0843 -0.4083 -0.3738 0.0741  311  PHE B N   
6118  C  CA  . PHE B  201 ? 0.8809 1.2191 1.9986 -0.3764 -0.4655 0.1304  311  PHE B CA  
6119  C  C   . PHE B  201 ? 1.2019 1.5057 2.3891 -0.3538 -0.5739 0.1507  311  PHE B C   
6120  O  O   . PHE B  201 ? 1.1608 1.4957 2.3793 -0.3826 -0.5714 0.1184  311  PHE B O   
6121  C  CB  . PHE B  201 ? 0.8590 1.1705 1.7925 -0.4012 -0.4340 0.1241  311  PHE B CB  
6122  C  CG  . PHE B  201 ? 1.3017 1.6255 2.1437 -0.4108 -0.3490 0.1110  311  PHE B CG  
6123  C  CD1 . PHE B  201 ? 1.0798 1.3921 1.9326 -0.3857 -0.3529 0.1452  311  PHE B CD1 
6124  C  CD2 . PHE B  201 ? 1.1905 1.5314 1.9447 -0.4434 -0.2654 0.0603  311  PHE B CD2 
6125  C  CE1 . PHE B  201 ? 0.7102 1.0360 1.4832 -0.3960 -0.2742 0.1277  311  PHE B CE1 
6126  C  CE2 . PHE B  201 ? 0.7030 1.0465 1.3874 -0.4435 -0.1925 0.0409  311  PHE B CE2 
6127  C  CZ  . PHE B  201 ? 0.6792 1.0199 1.3679 -0.4220 -0.1952 0.0722  311  PHE B CZ  
6128  N  N   . ALA B  202 ? 1.1792 1.4142 2.3814 -0.3052 -0.6668 0.2001  312  ALA B N   
6129  C  CA  . ALA B  202 ? 1.1149 1.2973 2.3544 -0.2772 -0.7743 0.2149  312  ALA B CA  
6130  C  C   . ALA B  202 ? 1.1828 1.2368 2.2213 -0.2452 -0.8468 0.2653  312  ALA B C   
6131  O  O   . ALA B  202 ? 1.2288 1.2233 2.2470 -0.2048 -0.8901 0.2943  312  ALA B O   
6132  C  CB  . ALA B  202 ? 1.1466 1.3566 2.5861 -0.2451 -0.8087 0.2092  312  ALA B CB  
6133  N  N   . VAL B  203 ? 1.4026 1.4093 2.2802 -0.2629 -0.8503 0.2677  313  VAL B N   
6134  C  CA  . VAL B  203 ? 1.7484 1.6363 2.4030 -0.2366 -0.8803 0.2989  313  VAL B CA  
6135  C  C   . VAL B  203 ? 1.4543 1.2720 2.0489 -0.2267 -0.9474 0.2907  313  VAL B C   
6136  O  O   . VAL B  203 ? 1.4223 1.2798 2.1624 -0.2366 -0.9904 0.2707  313  VAL B O   
6137  C  CB  . VAL B  203 ? 1.6040 1.4848 2.0954 -0.2592 -0.8097 0.3059  313  VAL B CB  
6138  C  CG1 . VAL B  203 ? 1.1038 1.0527 1.6454 -0.2693 -0.7466 0.3142  313  VAL B CG1 
6139  C  CG2 . VAL B  203 ? 1.3048 1.2214 1.7911 -0.3018 -0.7834 0.2808  313  VAL B CG2 
6140  N  N   . THR B  204 ? 1.8560 1.5826 2.2451 -0.2047 -0.9462 0.2978  314  THR B N   
6141  C  CA  . THR B  204 ? 2.0363 1.6898 2.3423 -0.1944 -0.9971 0.2875  314  THR B CA  
6142  C  C   . THR B  204 ? 1.8578 1.4998 2.0968 -0.2346 -0.9741 0.2802  314  THR B C   
6143  O  O   . THR B  204 ? 1.6813 1.3660 1.9015 -0.2638 -0.9110 0.2821  314  THR B O   
6144  C  CB  . THR B  204 ? 2.0924 1.6681 2.2249 -0.1455 -0.9925 0.2905  314  THR B CB  
6145  O  OG1 . THR B  204 ? 1.8871 1.4590 1.8986 -0.1457 -0.9173 0.2972  314  THR B OG1 
6146  C  CG2 . THR B  204 ? 1.6823 1.2630 1.8728 -0.1025 -1.0270 0.2980  314  THR B CG2 
6147  N  N   . GLN B  205 ? 1.6483 1.2292 1.8460 -0.2356 -1.0276 0.2716  315  GLN B N   
6148  C  CA  . GLN B  205 ? 1.6578 1.2193 1.7964 -0.2744 -1.0152 0.2661  315  GLN B CA  
6149  C  C   . GLN B  205 ? 1.8409 1.3666 1.8112 -0.2754 -0.9368 0.2707  315  GLN B C   
6150  O  O   . GLN B  205 ? 2.1530 1.7230 2.1187 -0.3103 -0.8863 0.2685  315  GLN B O   
6151  C  CB  . GLN B  205 ? 1.9613 1.4408 2.0525 -0.2689 -1.0862 0.2590  315  GLN B CB  
6152  C  CG  . GLN B  205 ? 2.2673 1.7878 2.5379 -0.2736 -1.1703 0.2489  315  GLN B CG  
6153  C  CD  . GLN B  205 ? 2.2342 1.6877 2.4690 -0.2852 -1.2387 0.2402  315  GLN B CD  
6154  O  OE1 . GLN B  205 ? 2.1938 1.5830 2.2953 -0.3042 -1.2189 0.2429  315  GLN B OE1 
6155  N  NE2 . GLN B  205 ? 2.5477 2.0137 2.9027 -0.2730 -1.3212 0.2287  315  GLN B NE2 
6156  N  N   . GLU B  206 ? 2.0543 1.4931 1.8929 -0.2422 -0.9344 0.2751  316  GLU B N   
6157  C  CA  . GLU B  206 ? 2.0174 1.4191 1.7142 -0.2424 -0.8708 0.2722  316  GLU B CA  
6158  C  C   . GLU B  206 ? 1.6540 1.1533 1.3836 -0.2503 -0.7920 0.2754  316  GLU B C   
6159  O  O   . GLU B  206 ? 1.7101 1.2025 1.3491 -0.2559 -0.7351 0.2695  316  GLU B O   
6160  C  CB  . GLU B  206 ? 2.1457 1.4643 1.7187 -0.1973 -0.8814 0.2658  316  GLU B CB  
6161  C  CG  . GLU B  206 ? 2.0711 1.4324 1.6774 -0.1594 -0.8752 0.2735  316  GLU B CG  
6162  C  CD  . GLU B  206 ? 2.4261 1.7718 2.1155 -0.1438 -0.9535 0.2778  316  GLU B CD  
6163  O  OE1 . GLU B  206 ? 2.3947 1.7026 2.1220 -0.1621 -1.0144 0.2729  316  GLU B OE1 
6164  O  OE2 . GLU B  206 ? 2.8081 2.1807 2.5271 -0.1117 -0.9554 0.2863  316  GLU B OE2 
6165  N  N   . GLN B  207 ? 1.4324 1.0218 1.2945 -0.2488 -0.7893 0.2810  317  GLN B N   
6166  C  CA  . GLN B  207 ? 1.8868 1.5656 1.7852 -0.2566 -0.7199 0.2827  317  GLN B CA  
6167  C  C   . GLN B  207 ? 1.8361 1.5849 1.8469 -0.3102 -0.7137 0.2842  317  GLN B C   
6168  O  O   . GLN B  207 ? 1.1485 0.9647 1.1896 -0.3297 -0.6614 0.2861  317  GLN B O   
6169  C  CB  . GLN B  207 ? 1.2769 0.9913 1.2392 -0.2228 -0.7247 0.2917  317  GLN B CB  
6170  C  CG  . GLN B  207 ? 1.2191 0.9579 1.1103 -0.2081 -0.6587 0.2963  317  GLN B CG  
6171  C  CD  . GLN B  207 ? 1.6332 1.2995 1.3700 -0.1811 -0.6469 0.2914  317  GLN B CD  
6172  O  OE1 . GLN B  207 ? 2.1403 1.7268 1.8215 -0.1624 -0.6971 0.2886  317  GLN B OE1 
6173  N  NE2 . GLN B  207 ? 1.2544 0.9524 0.9287 -0.1769 -0.5812 0.2865  317  GLN B NE2 
6174  N  N   . VAL B  208 ? 1.9483 1.6942 2.0184 -0.3359 -0.7579 0.2754  318  VAL B N   
6175  C  CA  . VAL B  208 ? 1.2330 1.0857 1.4351 -0.3834 -0.7277 0.2479  318  VAL B CA  
6176  C  C   . VAL B  208 ? 1.1954 1.0478 1.2788 -0.4131 -0.6600 0.2394  318  VAL B C   
6177  O  O   . VAL B  208 ? 1.1087 1.0486 1.2479 -0.4372 -0.5884 0.2119  318  VAL B O   
6178  C  CB  . VAL B  208 ? 1.3011 1.1757 1.6237 -0.4035 -0.7796 0.2227  318  VAL B CB  
6179  C  CG1 . VAL B  208 ? 1.2428 1.2357 1.6960 -0.4590 -0.7059 0.1646  318  VAL B CG1 
6180  C  CG2 . VAL B  208 ? 1.3362 1.2235 1.7975 -0.3727 -0.8434 0.2277  318  VAL B CG2 
6181  N  N   . HIS B  209 ? 1.9172 1.6647 1.8371 -0.4082 -0.6714 0.2548  319  HIS B N   
6182  C  CA  . HIS B  209 ? 1.9772 1.7078 1.7801 -0.4344 -0.6118 0.2502  319  HIS B CA  
6183  C  C   . HIS B  209 ? 1.7228 1.4922 1.4835 -0.4261 -0.5405 0.2534  319  HIS B C   
6184  O  O   . HIS B  209 ? 1.1193 0.9167 0.8344 -0.4554 -0.4830 0.2433  319  HIS B O   
6185  C  CB  . HIS B  209 ? 2.2805 1.8896 1.9366 -0.4166 -0.6232 0.2557  319  HIS B CB  
6186  C  CG  . HIS B  209 ? 2.2250 1.7959 1.7739 -0.4491 -0.5758 0.2531  319  HIS B CG  
6187  N  ND1 . HIS B  209 ? 2.4886 2.0454 1.9592 -0.4451 -0.5127 0.2488  319  HIS B ND1 
6188  C  CD2 . HIS B  209 ? 1.7186 1.2593 1.2306 -0.4891 -0.5861 0.2499  319  HIS B CD2 
6189  C  CE1 . HIS B  209 ? 1.8249 1.3387 1.2180 -0.4777 -0.4842 0.2442  319  HIS B CE1 
6190  N  NE2 . HIS B  209 ? 1.5939 1.0924 0.9961 -0.5040 -0.5242 0.2493  319  HIS B NE2 
6191  N  N   . LEU B  210 ? 1.3672 1.1435 1.1454 -0.3872 -0.5409 0.2620  320  LEU B N   
6192  C  CA  . LEU B  210 ? 1.6162 1.4449 1.3790 -0.3811 -0.4770 0.2609  320  LEU B CA  
6193  C  C   . LEU B  210 ? 1.4743 1.4106 1.3640 -0.4138 -0.4594 0.2548  320  LEU B C   
6194  O  O   . LEU B  210 ? 0.9114 0.9011 0.7848 -0.4379 -0.3949 0.2335  320  LEU B O   
6195  C  CB  . LEU B  210 ? 1.9201 1.7309 1.6644 -0.3279 -0.4826 0.2622  320  LEU B CB  
6196  C  CG  . LEU B  210 ? 1.6761 1.5259 1.3866 -0.3095 -0.4270 0.2580  320  LEU B CG  
6197  C  CD1 . LEU B  210 ? 1.6489 1.4556 1.3102 -0.2570 -0.4504 0.2613  320  LEU B CD1 
6198  C  CD2 . LEU B  210 ? 1.6040 1.5373 1.4070 -0.3306 -0.4050 0.2697  320  LEU B CD2 
6199  N  N   . TYR B  211 ? 0.9620 0.9406 1.0047 -0.4039 -0.4988 0.2493  321  TYR B N   
6200  C  CA  . TYR B  211 ? 0.8818 0.9712 1.0960 -0.4170 -0.4443 0.2070  321  TYR B CA  
6201  C  C   . TYR B  211 ? 0.8585 1.0128 1.1824 -0.4523 -0.3743 0.1335  321  TYR B C   
6202  O  O   . TYR B  211 ? 0.7957 1.0168 1.2243 -0.4616 -0.2876 0.0794  321  TYR B O   
6203  C  CB  . TYR B  211 ? 0.8985 1.0016 1.2551 -0.3944 -0.4965 0.2191  321  TYR B CB  
6204  C  CG  . TYR B  211 ? 0.9008 0.9596 1.1944 -0.3618 -0.5278 0.2726  321  TYR B CG  
6205  C  CD1 . TYR B  211 ? 0.9663 0.9201 1.0934 -0.3330 -0.5639 0.3064  321  TYR B CD1 
6206  C  CD2 . TYR B  211 ? 1.4741 1.5930 1.8826 -0.3575 -0.4980 0.2697  321  TYR B CD2 
6207  C  CE1 . TYR B  211 ? 0.9712 0.8986 1.0457 -0.2977 -0.5603 0.3237  321  TYR B CE1 
6208  C  CE2 . TYR B  211 ? 1.7124 1.7906 2.0659 -0.3322 -0.5262 0.3198  321  TYR B CE2 
6209  C  CZ  . TYR B  211 ? 1.6509 1.6336 1.8304 -0.3025 -0.5536 0.3433  321  TYR B CZ  
6210  O  OH  . TYR B  211 ? 1.3561 1.3153 1.4762 -0.2646 -0.5457 0.3581  321  TYR B OH  
6211  N  N   . GLU B  212 ? 1.4900 1.6130 1.7910 -0.4717 -0.4010 0.1250  322  GLU B N   
6212  C  CA  . GLU B  212 ? 1.0746 1.2481 1.4799 -0.5094 -0.3260 0.0538  322  GLU B CA  
6213  C  C   . GLU B  212 ? 0.8811 1.0416 1.1930 -0.5195 -0.2594 0.0487  322  GLU B C   
6214  O  O   . GLU B  212 ? 0.8741 1.0712 1.2903 -0.5451 -0.1894 0.0057  322  GLU B O   
6215  C  CB  . GLU B  212 ? 0.9937 1.1306 1.3869 -0.5334 -0.3744 0.0524  322  GLU B CB  
6216  C  CG  . GLU B  212 ? 1.1539 1.3367 1.6697 -0.5863 -0.3046 -0.0090 322  GLU B CG  
6217  C  CD  . GLU B  212 ? 1.5370 1.6848 2.0439 -0.6167 -0.3480 -0.0136 322  GLU B CD  
6218  O  OE1 . GLU B  212 ? 2.1637 2.2468 2.5670 -0.5923 -0.4365 0.0306  322  GLU B OE1 
6219  O  OE2 . GLU B  212 ? 1.6034 1.7804 2.2102 -0.6642 -0.2918 -0.0620 322  GLU B OE2 
6220  N  N   . ASN B  213 ? 0.8849 0.9852 0.9866 -0.5020 -0.2850 0.1007  323  ASN B N   
6221  C  CA  . ASN B  213 ? 1.3972 1.4943 1.3808 -0.5071 -0.2242 0.0988  323  ASN B CA  
6222  C  C   . ASN B  213 ? 1.6854 1.8398 1.7332 -0.4912 -0.1737 0.0849  323  ASN B C   
6223  O  O   . ASN B  213 ? 1.4424 1.6157 1.4539 -0.5016 -0.1139 0.0647  323  ASN B O   
6224  C  CB  . ASN B  213 ? 1.8961 1.9081 1.6223 -0.5101 -0.2587 0.1651  323  ASN B CB  
6225  C  CG  . ASN B  213 ? 1.8867 1.8159 1.5365 -0.5302 -0.2987 0.1803  323  ASN B CG  
6226  O  OD1 . ASN B  213 ? 1.5836 1.4212 1.1591 -0.5134 -0.3451 0.2212  323  ASN B OD1 
6227  N  ND2 . ASN B  213 ? 1.9775 1.9273 1.6787 -0.5610 -0.2667 0.1347  323  ASN B ND2 
6228  N  N   . TYR B  214 ? 1.6159 1.7920 1.7478 -0.4665 -0.1986 0.0947  324  TYR B N   
6229  C  CA  . TYR B  214 ? 0.6998 0.9246 0.9213 -0.4559 -0.1471 0.0759  324  TYR B CA  
6230  C  C   . TYR B  214 ? 1.0535 1.3208 1.4817 -0.4748 -0.0903 0.0223  324  TYR B C   
6231  O  O   . TYR B  214 ? 1.7545 2.0394 2.2149 -0.4747 -0.0355 0.0119  324  TYR B O   
6232  C  CB  . TYR B  214 ? 0.6783 0.9082 0.9321 -0.4305 -0.1885 0.1034  324  TYR B CB  
6233  C  CG  . TYR B  214 ? 0.6947 0.8874 0.7520 -0.4227 -0.2369 0.1775  324  TYR B CG  
6234  C  CD1 . TYR B  214 ? 1.4268 1.5898 1.2930 -0.4339 -0.2222 0.2000  324  TYR B CD1 
6235  C  CD2 . TYR B  214 ? 0.7060 0.8849 0.7697 -0.4068 -0.2890 0.2279  324  TYR B CD2 
6236  C  CE1 . TYR B  214 ? 2.1096 2.2276 1.8597 -0.4348 -0.2220 0.2545  324  TYR B CE1 
6237  C  CE2 . TYR B  214 ? 0.7260 0.8557 0.6387 -0.4008 -0.3067 0.2860  324  TYR B CE2 
6238  C  CZ  . TYR B  214 ? 1.6830 1.7898 1.4845 -0.4125 -0.2565 0.2757  324  TYR B CZ  
6239  O  OH  . TYR B  214 ? 1.0319 1.1214 0.8068 -0.3502 -0.2405 0.2404  324  TYR B OH  
6240  N  N   . ALA B  215 ? 0.7333 1.0187 1.2894 -0.4929 -0.1064 -0.0078 325  ALA B N   
6241  C  CA  . ALA B  215 ? 1.0247 1.3520 1.7554 -0.5105 -0.0451 -0.0640 325  ALA B CA  
6242  C  C   . ALA B  215 ? 1.1007 1.4011 1.8455 -0.5186 -0.0299 -0.0281 325  ALA B C   
6243  O  O   . ALA B  215 ? 1.4652 1.7956 2.2770 -0.5338 -0.0249 0.0171  325  ALA B O   
6244  C  CB  . ALA B  215 ? 1.0988 1.4766 1.8620 -0.5571 -0.0769 -0.0866 325  ALA B CB  
6245  N  N   . LYS B  216 ? 1.4175 1.6813 1.9791 -0.5377 -0.0409 -0.0178 326  LYS B N   
6246  C  CA  . LYS B  216 ? 1.7054 1.9574 2.1693 -0.5643 0.0018  -0.0193 326  LYS B CA  
6247  C  C   . LYS B  216 ? 1.5946 1.8606 1.9537 -0.5530 0.0529  -0.0281 326  LYS B C   
6248  O  O   . LYS B  216 ? 2.3170 2.5935 2.6632 -0.5719 0.1070  -0.0551 326  LYS B O   
6249  C  CB  . LYS B  216 ? 1.6438 1.8407 1.9099 -0.5802 -0.0201 -0.0135 326  LYS B CB  
6250  C  CG  . LYS B  216 ? 0.9288 1.1058 1.2779 -0.5999 -0.0659 -0.0165 326  LYS B CG  
6251  C  CD  . LYS B  216 ? 0.9892 1.0964 1.1174 -0.6170 -0.0903 0.0018  326  LYS B CD  
6252  C  CE  . LYS B  216 ? 1.0497 1.1308 1.2436 -0.6384 -0.1406 -0.0024 326  LYS B CE  
6253  N  NZ  . LYS B  216 ? 1.1258 1.1219 1.1010 -0.6564 -0.1650 0.0214  326  LYS B NZ  
6254  N  N   . LEU B  217 ? 0.8026 1.0672 1.0761 -0.5241 0.0382  -0.0152 327  LEU B N   
6255  C  CA  . LEU B  217 ? 1.0885 1.3688 1.2825 -0.5134 0.0814  -0.0336 327  LEU B CA  
6256  C  C   . LEU B  217 ? 1.6577 1.9754 2.0277 -0.5085 0.1075  -0.0380 327  LEU B C   
6257  O  O   . LEU B  217 ? 1.9224 2.2499 2.2760 -0.5197 0.1597  -0.0738 327  LEU B O   
6258  C  CB  . LEU B  217 ? 0.7460 1.0196 0.8011 -0.4888 0.0536  -0.0134 327  LEU B CB  
6259  C  CG  . LEU B  217 ? 0.7583 0.9965 0.6119 -0.4920 0.0156  0.0070  327  LEU B CG  
6260  C  CD1 . LEU B  217 ? 0.7171 0.9623 0.4464 -0.4679 -0.0125 0.0300  327  LEU B CD1 
6261  C  CD2 . LEU B  217 ? 1.7301 1.9463 1.4537 -0.5173 0.0443  -0.0284 327  LEU B CD2 
6262  N  N   . ILE B  218 ? 1.2021 1.5355 1.7270 -0.4930 0.0691  -0.0053 328  ILE B N   
6263  C  CA  . ILE B  218 ? 0.8078 1.1829 1.4680 -0.4957 0.0756  0.0121  328  ILE B CA  
6264  C  C   . ILE B  218 ? 0.9274 1.3366 1.6641 -0.5331 0.0947  -0.0012 328  ILE B C   
6265  O  O   . ILE B  218 ? 1.4879 1.9119 2.2922 -0.5584 0.0491  0.0243  328  ILE B O   
6266  C  CB  . ILE B  218 ? 0.9200 1.2924 1.6645 -0.4662 0.0166  0.0548  328  ILE B CB  
6267  C  CG1 . ILE B  218 ? 0.7078 1.0443 1.3689 -0.4387 0.0295  0.0218  328  ILE B CG1 
6268  C  CG2 . ILE B  218 ? 1.5012 1.9375 2.2493 -0.4980 0.0288  0.0644  328  ILE B CG2 
6269  C  CD1 . ILE B  218 ? 0.6831 1.0195 1.3594 -0.4251 0.0211  -0.0122 328  ILE B CD1 
6270  N  N   . PRO B  219 ? 1.2137 1.6314 1.9396 -0.5388 0.1652  -0.0529 329  PRO B N   
6271  C  CA  . PRO B  219 ? 1.3055 1.7459 2.1179 -0.5658 0.2024  -0.0862 329  PRO B CA  
6272  C  C   . PRO B  219 ? 1.2895 1.7791 2.2473 -0.5732 0.1789  -0.0746 329  PRO B C   
6273  O  O   . PRO B  219 ? 1.1642 1.6657 2.1575 -0.5542 0.1758  -0.0716 329  PRO B O   
6274  C  CB  . PRO B  219 ? 1.6633 2.0840 2.4274 -0.5610 0.2827  -0.1499 329  PRO B CB  
6275  C  CG  . PRO B  219 ? 1.2874 1.6963 1.9902 -0.5343 0.2775  -0.1436 329  PRO B CG  
6276  C  CD  . PRO B  219 ? 0.8025 1.2015 1.4385 -0.5214 0.2151  -0.0916 329  PRO B CD  
6277  N  N   . GLY B  220 ? 0.9195 1.4351 1.9584 -0.6005 0.1675  -0.0782 330  GLY B N   
6278  C  CA  . GLY B  220 ? 1.2576 1.8207 2.4435 -0.6022 0.1547  -0.0890 330  GLY B CA  
6279  C  C   . GLY B  220 ? 1.0655 1.6428 2.2475 -0.6025 0.0783  -0.0572 330  GLY B C   
6280  O  O   . GLY B  220 ? 1.6528 2.2646 2.9600 -0.6026 0.0550  -0.0709 330  GLY B O   
6281  N  N   . ALA B  221 ? 0.8652 1.4140 1.9101 -0.5981 0.0423  -0.0235 331  ALA B N   
6282  C  CA  . ALA B  221 ? 0.8465 1.3964 1.8672 -0.5932 -0.0116 -0.0219 331  ALA B CA  
6283  C  C   . ALA B  221 ? 1.2178 1.7654 2.2132 -0.6239 -0.0472 -0.0325 331  ALA B C   
6284  O  O   . ALA B  221 ? 0.9010 1.4105 1.7617 -0.6433 -0.0442 -0.0213 331  ALA B O   
6285  C  CB  . ALA B  221 ? 0.8976 1.4140 1.7708 -0.5778 -0.0168 -0.0098 331  ALA B CB  
6286  N  N   . THR B  222 ? 1.5868 2.1490 2.7098 -0.6002 -0.0919 -0.0440 332  THR B N   
6287  C  CA  . THR B  222 ? 0.9340 1.4920 2.0766 -0.6153 -0.1389 -0.0539 332  THR B CA  
6288  C  C   . THR B  222 ? 1.2517 1.7637 2.3760 -0.5622 -0.2167 -0.0349 332  THR B C   
6289  O  O   . THR B  222 ? 1.4403 1.9273 2.5343 -0.5205 -0.2285 -0.0131 332  THR B O   
6290  C  CB  . THR B  222 ? 0.9874 1.6006 2.3185 -0.6241 -0.1493 -0.0638 332  THR B CB  
6291  O  OG1 . THR B  222 ? 0.9739 1.6018 2.4435 -0.5694 -0.1920 -0.0556 332  THR B OG1 
6292  C  CG2 . THR B  222 ? 1.0084 1.6536 2.3888 -0.6505 -0.0761 -0.0728 332  THR B CG2 
6293  N  N   . VAL B  223 ? 1.2339 1.7260 2.3647 -0.5645 -0.2775 -0.0331 333  VAL B N   
6294  C  CA  . VAL B  223 ? 1.1981 1.6292 2.2854 -0.5133 -0.3736 0.0045  333  VAL B CA  
6295  C  C   . VAL B  223 ? 1.0247 1.4730 2.2645 -0.5004 -0.4565 0.0141  333  VAL B C   
6296  O  O   . VAL B  223 ? 1.0550 1.5723 2.4121 -0.5361 -0.4267 -0.0193 333  VAL B O   
6297  C  CB  . VAL B  223 ? 1.0053 1.3627 1.9281 -0.5155 -0.3959 0.0162  333  VAL B CB  
6298  C  CG1 . VAL B  223 ? 0.9005 1.2241 1.6920 -0.4985 -0.3511 0.0273  333  VAL B CG1 
6299  C  CG2 . VAL B  223 ? 1.0090 1.3852 1.9363 -0.5754 -0.3509 -0.0268 333  VAL B CG2 
6300  N  N   . GLY B  224 ? 1.0922 1.4697 2.3256 -0.4479 -0.5669 0.0643  334  GLY B N   
6301  C  CA  . GLY B  224 ? 1.1718 1.5485 2.5353 -0.4270 -0.6598 0.0722  334  GLY B CA  
6302  C  C   . GLY B  224 ? 1.2426 1.5031 2.4909 -0.3842 -0.7753 0.1236  334  GLY B C   
6303  O  O   . GLY B  224 ? 1.6788 1.8594 2.7704 -0.3588 -0.7877 0.1637  334  GLY B O   
6304  N  N   . LEU B  225 ? 1.3058 1.5527 2.6203 -0.3784 -0.8569 0.1203  335  LEU B N   
6305  C  CA  . LEU B  225 ? 1.4047 1.5278 2.5936 -0.3402 -0.9641 0.1603  335  LEU B CA  
6306  C  C   . LEU B  225 ? 1.5268 1.6201 2.8133 -0.2869 -1.0480 0.1755  335  LEU B C   
6307  O  O   . LEU B  225 ? 1.9847 2.1632 3.4757 -0.2874 -1.0560 0.1471  335  LEU B O   
6308  C  CB  . LEU B  225 ? 1.4829 1.5914 2.6416 -0.3732 -1.0008 0.1426  335  LEU B CB  
6309  C  CG  . LEU B  225 ? 1.9925 1.9548 2.9832 -0.3356 -1.0968 0.1796  335  LEU B CG  
6310  C  CD1 . LEU B  225 ? 1.5750 1.4321 2.3294 -0.3163 -1.0675 0.2171  335  LEU B CD1 
6311  C  CD2 . LEU B  225 ? 2.1285 2.0766 3.1146 -0.3677 -1.1435 0.1603  335  LEU B CD2 
6312  N  N   . LEU B  226 ? 1.5477 1.5160 2.6744 -0.2424 -1.1053 0.2142  336  LEU B N   
6313  C  CA  . LEU B  226 ? 1.7826 1.7025 2.9491 -0.1900 -1.1803 0.2249  336  LEU B CA  
6314  C  C   . LEU B  226 ? 1.7757 1.6307 2.8992 -0.1771 -1.2712 0.2181  336  LEU B C   
6315  O  O   . LEU B  226 ? 1.8277 1.5940 2.7648 -0.1819 -1.2820 0.2286  336  LEU B O   
6316  C  CB  . LEU B  226 ? 1.6375 1.4715 2.6356 -0.1527 -1.1659 0.2584  336  LEU B CB  
6317  C  CG  . LEU B  226 ? 1.6063 1.4727 2.7130 -0.1221 -1.1552 0.2670  336  LEU B CG  
6318  C  CD1 . LEU B  226 ? 2.0294 1.9550 3.3587 -0.1053 -1.2099 0.2431  336  LEU B CD1 
6319  C  CD2 . LEU B  226 ? 1.4644 1.4046 2.6305 -0.1516 -1.0649 0.2700  336  LEU B CD2 
6320  N  N   . GLN B  227 ? 1.8349 1.7348 3.1323 -0.1595 -1.3341 0.1979  337  GLN B N   
6321  C  CA  . GLN B  227 ? 1.9799 1.8228 3.2510 -0.1427 -1.4294 0.1893  337  GLN B CA  
6322  C  C   . GLN B  227 ? 2.0662 1.8990 3.4170 -0.0871 -1.4953 0.1876  337  GLN B C   
6323  O  O   . GLN B  227 ? 2.0091 1.8873 3.4570 -0.0667 -1.4656 0.1915  337  GLN B O   
6324  C  CB  . GLN B  227 ? 2.1604 2.0928 3.5803 -0.1902 -1.4459 0.1552  337  GLN B CB  
6325  C  CG  . GLN B  227 ? 2.0574 1.9871 3.3696 -0.2446 -1.3895 0.1545  337  GLN B CG  
6326  C  CD  . GLN B  227 ? 2.2617 2.2754 3.7023 -0.2962 -1.4066 0.1168  337  GLN B CD  
6327  O  OE1 . GLN B  227 ? 2.3324 2.4245 3.9658 -0.2939 -1.4536 0.0890  337  GLN B OE1 
6328  N  NE2 . GLN B  227 ? 2.0442 2.0484 3.3828 -0.3462 -1.3637 0.1124  337  GLN B NE2 
6329  N  N   . LYS B  228 ? 2.2139 1.9844 3.5186 -0.0611 -1.5858 0.1810  338  LYS B N   
6330  C  CA  . LYS B  228 ? 2.3539 2.1193 3.7317 -0.0056 -1.6563 0.1758  338  LYS B CA  
6331  C  C   . LYS B  228 ? 2.2733 2.1764 3.9425 -0.0106 -1.6616 0.1480  338  LYS B C   
6332  O  O   . LYS B  228 ? 2.2940 2.2187 4.0455 0.0310  -1.6665 0.1508  338  LYS B O   
6333  C  CB  . LYS B  228 ? 2.4888 2.1757 3.7803 0.0177  -1.7539 0.1677  338  LYS B CB  
6334  C  CG  . LYS B  228 ? 2.5531 2.1043 3.5559 0.0362  -1.7421 0.1903  338  LYS B CG  
6335  C  CD  . LYS B  228 ? 2.7329 2.2091 3.6659 0.0612  -1.8392 0.1786  338  LYS B CD  
6336  C  CE  . LYS B  228 ? 2.8281 2.1510 3.4900 0.0791  -1.8340 0.1958  338  LYS B CE  
6337  N  NZ  . LYS B  228 ? 3.0825 2.3053 3.6804 0.1020  -1.9440 0.1819  338  LYS B NZ  
6338  N  N   . ASP B  229 ? 2.2371 2.2401 4.0630 -0.0608 -1.6534 0.1182  339  ASP B N   
6339  C  CA  . ASP B  229 ? 2.1744 2.3308 4.2777 -0.0766 -1.6233 0.0845  339  ASP B CA  
6340  C  C   . ASP B  229 ? 2.0088 2.2222 4.1305 -0.1126 -1.5006 0.0888  339  ASP B C   
6341  O  O   . ASP B  229 ? 1.9347 2.2090 4.0681 -0.1720 -1.4345 0.0733  339  ASP B O   
6342  C  CB  . ASP B  229 ? 2.2221 2.4738 4.4778 -0.1186 -1.6570 0.0450  339  ASP B CB  
6343  C  CG  . ASP B  229 ? 2.3901 2.6086 4.6753 -0.0786 -1.7827 0.0342  339  ASP B CG  
6344  O  OD1 . ASP B  229 ? 2.4567 2.6386 4.7513 -0.0154 -1.8327 0.0430  339  ASP B OD1 
6345  O  OD2 . ASP B  229 ? 2.5850 2.8134 4.8776 -0.1106 -1.8315 0.0160  339  ASP B OD2 
6346  N  N   . SER B  230 ? 1.9599 2.1533 4.0768 -0.0772 -1.4675 0.1082  340  SER B N   
6347  C  CA  . SER B  230 ? 1.9354 2.1674 4.0487 -0.1055 -1.3548 0.1152  340  SER B CA  
6348  C  C   . SER B  230 ? 1.9763 2.3607 4.3288 -0.1399 -1.2791 0.0724  340  SER B C   
6349  O  O   . SER B  230 ? 1.9968 2.4231 4.3785 -0.1558 -1.1821 0.0703  340  SER B O   
6350  C  CB  . SER B  230 ? 1.9282 2.0878 3.9599 -0.0584 -1.3466 0.1492  340  SER B CB  
6351  O  OG  . SER B  230 ? 2.1204 2.2967 4.2889 -0.0065 -1.4001 0.1411  340  SER B OG  
6352  N  N   . GLY B  231 ? 1.7975 2.2672 4.3137 -0.1547 -1.3153 0.0354  341  GLY B N   
6353  C  CA  . GLY B  231 ? 1.7384 2.3543 4.4582 -0.1963 -1.2303 -0.0093 341  GLY B CA  
6354  C  C   . GLY B  231 ? 1.6495 2.3074 4.2891 -0.2693 -1.1233 -0.0224 341  GLY B C   
6355  O  O   . GLY B  231 ? 1.5964 2.3605 4.3576 -0.3079 -1.0276 -0.0570 341  GLY B O   
6356  N  N   . ASN B  232 ? 1.6465 2.2146 4.0692 -0.2866 -1.1374 0.0040  342  ASN B N   
6357  C  CA  . ASN B  232 ? 1.5722 2.1601 3.8777 -0.3516 -1.0409 -0.0056 342  ASN B CA  
6358  C  C   . ASN B  232 ? 1.4583 2.0748 3.7474 -0.3596 -0.9251 -0.0069 342  ASN B C   
6359  O  O   . ASN B  232 ? 1.4106 2.1085 3.7319 -0.4145 -0.8217 -0.0400 342  ASN B O   
6360  C  CB  . ASN B  232 ? 1.5989 2.0619 3.6619 -0.3499 -1.0893 0.0300  342  ASN B CB  
6361  C  CG  . ASN B  232 ? 1.7688 2.2056 3.8206 -0.3646 -1.1842 0.0215  342  ASN B CG  
6362  O  OD1 . ASN B  232 ? 2.0612 2.5967 4.2843 -0.3981 -1.1940 -0.0178 342  ASN B OD1 
6363  N  ND2 . ASN B  232 ? 1.7990 2.0987 3.6405 -0.3413 -1.2495 0.0583  342  ASN B ND2 
6364  N  N   . ILE B  233 ? 1.4280 1.9760 3.6672 -0.3070 -0.9407 0.0275  343  ILE B N   
6365  C  CA  . ILE B  233 ? 1.4709 2.0408 3.6960 -0.3122 -0.8367 0.0264  343  ILE B CA  
6366  C  C   . ILE B  233 ? 1.3719 2.0426 3.8129 -0.3135 -0.7796 -0.0111 343  ILE B C   
6367  O  O   . ILE B  233 ? 1.4856 2.2013 3.9250 -0.3417 -0.6692 -0.0310 343  ILE B O   
6368  C  CB  . ILE B  233 ? 1.3209 1.7886 3.4429 -0.2589 -0.8778 0.0752  343  ILE B CB  
6369  C  CG1 . ILE B  233 ? 1.6842 2.0420 3.6016 -0.2494 -0.9548 0.1129  343  ILE B CG1 
6370  C  CG2 . ILE B  233 ? 1.2108 1.6914 3.2692 -0.2753 -0.7691 0.0764  343  ILE B CG2 
6371  C  CD1 . ILE B  233 ? 1.7327 1.9808 3.5163 -0.2030 -0.9960 0.1629  343  ILE B CD1 
6372  N  N   . LEU B  234 ? 1.3954 2.0981 4.0150 -0.2811 -0.8541 -0.0226 344  LEU B N   
6373  C  CA  . LEU B  234 ? 1.3979 2.1984 4.2318 -0.2799 -0.8030 -0.0604 344  LEU B CA  
6374  C  C   . LEU B  234 ? 1.3861 2.2828 4.2541 -0.3509 -0.7133 -0.1014 344  LEU B C   
6375  O  O   . LEU B  234 ? 1.3561 2.3139 4.3075 -0.3668 -0.6195 -0.1280 344  LEU B O   
6376  C  CB  . LEU B  234 ? 1.4957 2.3140 4.5071 -0.2297 -0.9116 -0.0662 344  LEU B CB  
6377  C  CG  . LEU B  234 ? 1.5344 2.2476 4.4973 -0.1585 -1.0051 -0.0249 344  LEU B CG  
6378  C  CD1 . LEU B  234 ? 1.6439 2.3833 4.7803 -0.1075 -1.1039 -0.0380 344  LEU B CD1 
6379  C  CD2 . LEU B  234 ? 1.4584 2.1365 4.3941 -0.1390 -0.9352 -0.0079 344  LEU B CD2 
6380  N  N   . GLN B  235 ? 1.4195 2.3197 4.2092 -0.3959 -0.7393 -0.1053 345  GLN B N   
6381  C  CA  . GLN B  235 ? 1.6289 2.6096 4.4297 -0.4718 -0.6562 -0.1398 345  GLN B CA  
6382  C  C   . GLN B  235 ? 1.6830 2.6487 4.3274 -0.5105 -0.5356 -0.1402 345  GLN B C   
6383  O  O   . GLN B  235 ? 2.0761 3.1040 4.7663 -0.5583 -0.4499 -0.1673 345  GLN B O   
6384  C  CB  . GLN B  235 ? 1.5806 2.5500 4.3085 -0.5147 -0.7124 -0.1409 345  GLN B CB  
6385  C  CG  . GLN B  235 ? 1.5796 2.5934 4.4821 -0.4974 -0.8179 -0.1543 345  GLN B CG  
6386  C  CD  . GLN B  235 ? 1.6447 2.6502 4.4750 -0.5514 -0.8610 -0.1611 345  GLN B CD  
6387  O  OE1 . GLN B  235 ? 1.6176 2.5896 4.2777 -0.6063 -0.8035 -0.1594 345  GLN B OE1 
6388  N  NE2 . GLN B  235 ? 1.7724 2.8042 4.7287 -0.5359 -0.9647 -0.1708 345  GLN B NE2 
6389  N  N   . LEU B  236 ? 1.4068 2.2851 3.8738 -0.4887 -0.5329 -0.1093 346  LEU B N   
6390  C  CA  . LEU B  236 ? 1.6184 2.4814 3.9373 -0.5180 -0.4259 -0.1104 346  LEU B CA  
6391  C  C   . LEU B  236 ? 1.4167 2.3235 3.8643 -0.5003 -0.3558 -0.1285 346  LEU B C   
6392  O  O   . LEU B  236 ? 1.3266 2.2620 3.7882 -0.5379 -0.2685 -0.1512 346  LEU B O   
6393  C  CB  . LEU B  236 ? 1.3839 2.1534 3.5199 -0.4891 -0.4465 -0.0748 346  LEU B CB  
6394  C  CG  . LEU B  236 ? 1.2945 2.0031 3.2578 -0.5096 -0.4906 -0.0586 346  LEU B CG  
6395  C  CD1 . LEU B  236 ? 1.2550 1.8724 3.0903 -0.4618 -0.5322 -0.0172 346  LEU B CD1 
6396  C  CD2 . LEU B  236 ? 1.2895 2.0055 3.1361 -0.5788 -0.4073 -0.0786 346  LEU B CD2 
6397  N  N   . ILE B  237 ? 1.1961 2.0907 3.7654 -0.4368 -0.3994 -0.1190 347  ILE B N   
6398  C  CA  . ILE B  237 ? 1.1786 2.0959 3.8529 -0.4139 -0.3333 -0.1356 347  ILE B CA  
6399  C  C   . ILE B  237 ? 1.2300 2.2410 4.0879 -0.4348 -0.2931 -0.1759 347  ILE B C   
6400  O  O   . ILE B  237 ? 1.2224 2.2554 4.1003 -0.4495 -0.2013 -0.1981 347  ILE B O   
6401  C  CB  . ILE B  237 ? 1.1788 2.0497 3.9491 -0.3419 -0.4005 -0.1131 347  ILE B CB  
6402  C  CG1 . ILE B  237 ? 1.1485 1.9282 3.7461 -0.3238 -0.4618 -0.0675 347  ILE B CG1 
6403  C  CG2 . ILE B  237 ? 1.1500 2.0165 3.9718 -0.3222 -0.3225 -0.1253 347  ILE B CG2 
6404  C  CD1 . ILE B  237 ? 1.1624 1.8804 3.8287 -0.2568 -0.5379 -0.0349 347  ILE B CD1 
6405  N  N   . ILE B  238 ? 1.3102 2.3746 4.3111 -0.4349 -0.3637 -0.1870 348  ILE B N   
6406  C  CA  . ILE B  238 ? 1.3978 2.5631 4.5913 -0.4563 -0.3303 -0.2261 348  ILE B CA  
6407  C  C   . ILE B  238 ? 1.4144 2.6015 4.5381 -0.5274 -0.2399 -0.2445 348  ILE B C   
6408  O  O   . ILE B  238 ? 1.3883 2.6254 4.6267 -0.5415 -0.1626 -0.2763 348  ILE B O   
6409  C  CB  . ILE B  238 ? 1.4229 2.6413 4.7772 -0.4445 -0.4347 -0.2338 348  ILE B CB  
6410  C  CG1 . ILE B  238 ? 1.4386 2.6158 4.8855 -0.3649 -0.5347 -0.2155 348  ILE B CG1 
6411  C  CG2 . ILE B  238 ? 1.4843 2.8198 5.0485 -0.4700 -0.3975 -0.2758 348  ILE B CG2 
6412  C  CD1 . ILE B  238 ? 1.5248 2.7464 5.1189 -0.3448 -0.6501 -0.2226 348  ILE B CD1 
6413  N  N   . SER B  239 ? 1.8354 2.9774 4.7860 -0.5701 -0.2506 -0.2271 349  SER B N   
6414  C  CA  . SER B  239 ? 1.7194 2.8600 4.5892 -0.6347 -0.1701 -0.2395 349  SER B CA  
6415  C  C   . SER B  239 ? 1.3996 2.4729 4.1108 -0.6314 -0.0912 -0.2311 349  SER B C   
6416  O  O   . SER B  239 ? 1.3322 2.3845 3.9388 -0.6785 -0.0301 -0.2352 349  SER B O   
6417  C  CB  . SER B  239 ? 1.7710 2.8884 4.5207 -0.6852 -0.2171 -0.2253 349  SER B CB  
6418  O  OG  . SER B  239 ? 1.6636 2.7005 4.2382 -0.6595 -0.2746 -0.1920 349  SER B OG  
6419  N  N   . ALA B  240 ? 1.2636 2.3001 3.9546 -0.5770 -0.0947 -0.2189 350  ALA B N   
6420  C  CA  . ALA B  240 ? 1.2220 2.2054 3.7988 -0.5692 -0.0187 -0.2183 350  ALA B CA  
6421  C  C   . ALA B  240 ? 1.2389 2.2517 3.9678 -0.5421 0.0441  -0.2503 350  ALA B C   
6422  O  O   . ALA B  240 ? 1.2230 2.1949 3.8775 -0.5393 0.1168  -0.2606 350  ALA B O   
6423  C  CB  . ALA B  240 ? 1.1533 2.0668 3.5801 -0.5348 -0.0592 -0.1822 350  ALA B CB  
6424  N  N   . TYR B  241 ? 1.3205 2.4024 4.2597 -0.5227 0.0167  -0.2690 351  TYR B N   
6425  C  CA  . TYR B  241 ? 1.5471 2.6663 4.6516 -0.5007 0.0759  -0.3041 351  TYR B CA  
6426  C  C   . TYR B  241 ? 1.5573 2.7234 4.7334 -0.5467 0.1546  -0.3424 351  TYR B C   
6427  O  O   . TYR B  241 ? 1.4139 2.6256 4.7526 -0.5346 0.2040  -0.3773 351  TYR B O   
6428  C  CB  . TYR B  241 ? 1.6540 2.8319 4.9569 -0.4559 0.0048  -0.3061 351  TYR B CB  
6429  C  CG  . TYR B  241 ? 1.6603 2.8592 5.1150 -0.4162 0.0489  -0.3322 351  TYR B CG  
6430  C  CD1 . TYR B  241 ? 1.3087 2.4374 4.6992 -0.3784 0.0674  -0.3202 351  TYR B CD1 
6431  C  CD2 . TYR B  241 ? 1.4089 2.6990 5.0817 -0.4167 0.0701  -0.3696 351  TYR B CD2 
6432  C  CE1 . TYR B  241 ? 1.3479 2.4834 4.8995 -0.3419 0.1081  -0.3488 351  TYR B CE1 
6433  C  CE2 . TYR B  241 ? 1.4329 2.7386 5.2573 -0.3780 0.1102  -0.3964 351  TYR B CE2 
6434  C  CZ  . TYR B  241 ? 1.5436 2.7660 5.3097 -0.3404 0.1290  -0.3870 351  TYR B CZ  
6435  O  OH  . TYR B  241 ? 1.5090 2.7365 5.4358 -0.3031 0.1706  -0.4166 351  TYR B OH  
6436  N  N   . GLU B  242 ? 1.3872 2.5412 4.4457 -0.5998 0.1671  -0.3360 352  GLU B N   
6437  C  CA  . GLU B  242 ? 1.4550 2.6429 4.5634 -0.6475 0.2449  -0.3694 352  GLU B CA  
6438  C  C   . GLU B  242 ? 1.4636 2.6067 4.5311 -0.6393 0.3472  -0.3980 352  GLU B C   
6439  O  O   . GLU B  242 ? 1.6149 2.7982 4.8058 -0.6538 0.4174  -0.4380 352  GLU B O   
6440  C  CB  . GLU B  242 ? 1.4677 2.6313 4.4274 -0.7045 0.2338  -0.3499 352  GLU B CB  
6441  C  CG  . GLU B  242 ? 1.7270 2.9266 4.7162 -0.7202 0.1344  -0.3267 352  GLU B CG  
6442  C  CD  . GLU B  242 ? 1.9494 3.1030 4.7575 -0.7749 0.1194  -0.3022 352  GLU B CD  
6443  O  OE1 . GLU B  242 ? 1.9618 3.0513 4.6107 -0.7918 0.1788  -0.2972 352  GLU B OE1 
6444  O  OE2 . GLU B  242 ? 2.0653 3.2425 4.8888 -0.7997 0.0458  -0.2893 352  GLU B OE2 
6445  N  N   . GLU B  243 ? 1.7688 2.8287 4.6637 -0.6177 0.3568  -0.3806 353  GLU B N   
6446  C  CA  . GLU B  243 ? 1.8312 2.8357 4.6622 -0.6086 0.4453  -0.4088 353  GLU B CA  
6447  C  C   . GLU B  243 ? 1.9552 2.9506 4.7404 -0.6558 0.5254  -0.4390 353  GLU B C   
6448  O  O   . GLU B  243 ? 2.0738 3.0352 4.7055 -0.6888 0.5191  -0.4205 353  GLU B O   
6449  C  CB  . GLU B  243 ? 1.6798 2.7091 4.6836 -0.5689 0.4738  -0.4378 353  GLU B CB  
6450  C  CG  . GLU B  243 ? 1.5669 2.6019 4.6287 -0.5200 0.3959  -0.4090 353  GLU B CG  
6451  C  CD  . GLU B  243 ? 1.5963 2.6380 4.8015 -0.4798 0.4297  -0.4352 353  GLU B CD  
6452  O  OE1 . GLU B  243 ? 1.6688 2.7776 5.0610 -0.4549 0.3877  -0.4380 353  GLU B OE1 
6453  O  OE2 . GLU B  243 ? 1.7335 2.7133 4.8656 -0.4734 0.4971  -0.4549 353  GLU B OE2 
6454  N  N   . LEU B  244 ? 1.8505 2.8723 4.7663 -0.6590 0.6013  -0.4854 354  LEU B N   
6455  C  CA  . LEU B  244 ? 1.7837 2.7927 4.6687 -0.7022 0.6879  -0.5206 354  LEU B CA  
6456  C  C   . LEU B  244 ? 1.8755 2.7849 4.5263 -0.7103 0.7275  -0.5220 354  LEU B C   
6457  O  O   . LEU B  244 ? 1.7528 2.6359 4.3259 -0.7492 0.7821  -0.5408 354  LEU B O   
6458  C  CB  . LEU B  244 ? 1.7201 2.7887 4.6581 -0.7522 0.6667  -0.5112 354  LEU B CB  
6459  C  CG  . LEU B  244 ? 1.7565 2.9365 4.9424 -0.7546 0.6376  -0.5210 354  LEU B CG  
6460  C  CD1 . LEU B  244 ? 1.8081 3.0390 5.0262 -0.8132 0.6193  -0.5127 354  LEU B CD1 
6461  C  CD2 . LEU B  244 ? 1.8284 3.0430 5.1785 -0.7426 0.7196  -0.5711 354  LEU B CD2 
6462  N  N   . ASP C  10  ? 3.0031 4.3277 2.7580 1.1819  -0.5462 0.5070  8    ASP C N   
6463  C  CA  . ASP C  10  ? 2.9981 4.1592 2.7859 1.1871  -0.5054 0.4732  8    ASP C CA  
6464  C  C   . ASP C  10  ? 3.0229 4.0898 2.8006 1.0825  -0.5118 0.4093  8    ASP C C   
6465  O  O   . ASP C  10  ? 2.9478 3.8500 2.7299 1.0749  -0.4777 0.3791  8    ASP C O   
6466  C  CB  . ASP C  10  ? 2.8280 4.0809 2.6884 1.2321  -0.4989 0.4782  8    ASP C CB  
6467  C  CG  . ASP C  10  ? 2.8691 4.1619 2.7349 1.3543  -0.4763 0.5407  8    ASP C CG  
6468  O  OD1 . ASP C  10  ? 3.0552 4.2134 2.8721 1.4089  -0.4435 0.5686  8    ASP C OD1 
6469  O  OD2 . ASP C  10  ? 2.7617 4.2185 2.6755 1.3971  -0.4893 0.5623  8    ASP C OD2 
6470  N  N   . MET C  11  ? 3.2062 4.3793 2.9642 1.0020  -0.5537 0.3889  9    MET C N   
6471  C  CA  . MET C  11  ? 3.2476 4.3299 2.9803 0.9059  -0.5596 0.3316  9    MET C CA  
6472  C  C   . MET C  11  ? 3.2923 4.2597 2.9515 0.8755  -0.5556 0.3262  9    MET C C   
6473  O  O   . MET C  11  ? 3.1840 4.0264 2.8195 0.8195  -0.5456 0.2820  9    MET C O   
6474  C  CB  . MET C  11  ? 3.2871 4.5196 3.0204 0.8269  -0.6007 0.3079  9    MET C CB  
6475  C  CG  . MET C  11  ? 3.2877 4.4228 2.9926 0.7334  -0.6031 0.2482  9    MET C CG  
6476  S  SD  . MET C  11  ? 3.2355 4.2338 2.9990 0.7460  -0.5676 0.2102  9    MET C SD  
6477  C  CE  . MET C  11  ? 3.1190 4.2946 2.9596 0.7676  -0.5819 0.2201  9    MET C CE  
6478  N  N   . GLU C  12  ? 3.5125 4.5219 3.1335 0.9142  -0.5623 0.3709  10   GLU C N   
6479  C  CA  . GLU C  12  ? 3.5945 4.4903 3.1460 0.8943  -0.5543 0.3699  10   GLU C CA  
6480  C  C   . GLU C  12  ? 3.6883 4.4200 3.2364 0.9586  -0.5076 0.3832  10   GLU C C   
6481  O  O   . GLU C  12  ? 3.7488 4.3567 3.2464 0.9354  -0.4928 0.3699  10   GLU C O   
6482  C  CB  . GLU C  12  ? 3.6384 4.6612 3.1418 0.8957  -0.5855 0.4102  10   GLU C CB  
6483  C  CG  . GLU C  12  ? 3.5938 4.7602 3.0748 0.8081  -0.6295 0.3897  10   GLU C CG  
6484  C  CD  . GLU C  12  ? 3.6585 4.7170 3.0719 0.7152  -0.6326 0.3434  10   GLU C CD  
6485  O  OE1 . GLU C  12  ? 3.7936 4.6944 3.1729 0.7244  -0.6068 0.3368  10   GLU C OE1 
6486  O  OE2 . GLU C  12  ? 3.6205 4.7503 3.0094 0.6324  -0.6586 0.3130  10   GLU C OE2 
6487  N  N   . LEU C  13  ? 3.5534 4.2795 3.1482 1.0362  -0.4816 0.4078  11   LEU C N   
6488  C  CA  . LEU C  13  ? 3.3862 3.9451 2.9702 1.0889  -0.4313 0.4155  11   LEU C CA  
6489  C  C   . LEU C  13  ? 3.2078 3.6351 2.8167 1.0469  -0.4043 0.3603  11   LEU C C   
6490  O  O   . LEU C  13  ? 3.1956 3.4730 2.7787 1.0543  -0.3664 0.3500  11   LEU C O   
6491  C  CB  . LEU C  13  ? 3.2869 3.8762 2.8984 1.1884  -0.4083 0.4628  11   LEU C CB  
6492  C  CG  . LEU C  13  ? 3.1617 3.8994 2.7539 1.2476  -0.4334 0.5241  11   LEU C CG  
6493  C  CD1 . LEU C  13  ? 3.0876 3.8365 2.7042 1.3544  -0.4036 0.5686  11   LEU C CD1 
6494  C  CD2 . LEU C  13  ? 3.2887 3.9718 2.8031 1.2485  -0.4341 0.5485  11   LEU C CD2 
6495  N  N   . VAL C  14  ? 3.2278 3.7141 2.8837 1.0016  -0.4226 0.3245  12   VAL C N   
6496  C  CA  . VAL C  14  ? 3.2670 3.6433 2.9460 0.9617  -0.4007 0.2727  12   VAL C CA  
6497  C  C   . VAL C  14  ? 3.4459 3.7336 3.0720 0.8993  -0.4034 0.2396  12   VAL C C   
6498  O  O   . VAL C  14  ? 3.4992 3.6601 3.1213 0.8897  -0.3715 0.2113  12   VAL C O   
6499  C  CB  . VAL C  14  ? 3.1876 3.6535 2.9224 0.9295  -0.4216 0.2456  12   VAL C CB  
6500  C  CG1 . VAL C  14  ? 3.1973 3.5548 2.9514 0.8891  -0.4011 0.1935  12   VAL C CG1 
6501  C  CG2 . VAL C  14  ? 3.1143 3.6659 2.9036 0.9960  -0.4147 0.2773  12   VAL C CG2 
6502  N  N   . LYS C  15  ? 3.5284 3.8851 3.1098 0.8559  -0.4395 0.2424  13   LYS C N   
6503  C  CA  . LYS C  15  ? 3.6251 3.9021 3.1517 0.7944  -0.4429 0.2085  13   LYS C CA  
6504  C  C   . LYS C  15  ? 3.6536 3.8230 3.1329 0.8167  -0.4162 0.2221  13   LYS C C   
6505  O  O   . LYS C  15  ? 3.6074 3.6752 3.0572 0.7826  -0.4012 0.1889  13   LYS C O   
6506  C  CB  . LYS C  15  ? 3.6653 4.0437 3.1489 0.7363  -0.4861 0.2064  13   LYS C CB  
6507  C  CG  . LYS C  15  ? 3.5941 4.0864 3.1155 0.7059  -0.5125 0.1924  13   LYS C CG  
6508  C  CD  . LYS C  15  ? 3.5090 4.1048 2.9771 0.6415  -0.5518 0.1905  13   LYS C CD  
6509  C  CE  . LYS C  15  ? 3.3630 4.0650 2.8620 0.6020  -0.5746 0.1715  13   LYS C CE  
6510  N  NZ  . LYS C  15  ? 3.3692 4.1700 2.8069 0.5276  -0.6095 0.1650  13   LYS C NZ  
6511  N  N   . ARG C  16  ? 3.6795 3.8692 3.1474 0.8757  -0.4084 0.2707  14   ARG C N   
6512  C  CA  . ARG C  16  ? 3.6605 3.7510 3.0730 0.8930  -0.3843 0.2862  14   ARG C CA  
6513  C  C   . ARG C  16  ? 3.6631 3.6104 3.0868 0.9118  -0.3339 0.2664  14   ARG C C   
6514  O  O   . ARG C  16  ? 3.6690 3.5194 3.0454 0.9027  -0.3118 0.2604  14   ARG C O   
6515  C  CB  . ARG C  16  ? 3.5996 3.7515 2.9883 0.9544  -0.3896 0.3471  14   ARG C CB  
6516  C  CG  . ARG C  16  ? 3.5113 3.8086 2.8732 0.9306  -0.4382 0.3692  14   ARG C CG  
6517  C  CD  . ARG C  16  ? 3.4862 3.7422 2.7832 0.8632  -0.4513 0.3453  14   ARG C CD  
6518  N  NE  . ARG C  16  ? 3.5301 3.6586 2.7786 0.8828  -0.4192 0.3543  14   ARG C NE  
6519  C  CZ  . ARG C  16  ? 3.5777 3.6489 2.7657 0.8359  -0.4212 0.3369  14   ARG C CZ  
6520  N  NH1 . ARG C  16  ? 3.5933 3.7136 2.7561 0.7679  -0.4521 0.3099  14   ARG C NH1 
6521  N  NH2 . ARG C  16  ? 3.6242 3.5838 2.7707 0.8552  -0.3897 0.3455  14   ARG C NH2 
6522  N  N   . LYS C  17  ? 3.6669 3.6027 3.1491 0.9337  -0.3140 0.2547  15   LYS C N   
6523  C  CA  . LYS C  17  ? 3.6431 3.4506 3.1326 0.9453  -0.2638 0.2344  15   LYS C CA  
6524  C  C   . LYS C  17  ? 3.5539 3.3014 3.0447 0.8852  -0.2578 0.1790  15   LYS C C   
6525  O  O   . LYS C  17  ? 3.5944 3.2401 3.0617 0.8784  -0.2221 0.1620  15   LYS C O   
6526  C  CB  . LYS C  17  ? 3.6332 3.4486 3.1798 0.9865  -0.2426 0.2398  15   LYS C CB  
6527  C  CG  . LYS C  17  ? 3.5869 3.2769 3.1414 0.9868  -0.1897 0.2123  15   LYS C CG  
6528  C  CD  . LYS C  17  ? 3.5636 3.2473 3.1576 1.0359  -0.1622 0.2265  15   LYS C CD  
6529  C  CE  . LYS C  17  ? 3.6277 3.2986 3.1827 1.1090  -0.1456 0.2846  15   LYS C CE  
6530  N  NZ  . LYS C  17  ? 3.5507 3.1936 3.1322 1.1621  -0.1101 0.2985  15   LYS C NZ  
6531  N  N   . ARG C  18  ? 3.4542 3.2646 2.9674 0.8422  -0.2905 0.1507  16   ARG C N   
6532  C  CA  . ARG C  18  ? 3.4734 3.2298 2.9821 0.7937  -0.2853 0.1011  16   ARG C CA  
6533  C  C   . ARG C  18  ? 3.5867 3.2918 3.0284 0.7679  -0.2851 0.0951  16   ARG C C   
6534  O  O   . ARG C  18  ? 3.6518 3.2847 3.0827 0.7479  -0.2622 0.0619  16   ARG C O   
6535  C  CB  . ARG C  18  ? 3.4383 3.2637 2.9698 0.7562  -0.3192 0.0767  16   ARG C CB  
6536  C  CG  . ARG C  18  ? 3.4334 3.2025 2.9546 0.7148  -0.3136 0.0283  16   ARG C CG  
6537  C  CD  . ARG C  18  ? 3.4437 3.2667 2.9680 0.6768  -0.3459 0.0073  16   ARG C CD  
6538  N  NE  . ARG C  18  ? 3.4039 3.1700 2.9265 0.6520  -0.3348 -0.0363 16   ARG C NE  
6539  C  CZ  . ARG C  18  ? 3.4619 3.1757 2.9257 0.6250  -0.3355 -0.0577 16   ARG C CZ  
6540  N  NH1 . ARG C  18  ? 3.6757 3.3829 3.0777 0.6129  -0.3464 -0.0418 16   ARG C NH1 
6541  N  NH2 . ARG C  18  ? 3.4370 3.1064 2.9009 0.6129  -0.3241 -0.0940 16   ARG C NH2 
6542  N  N   . ILE C  19  ? 3.6081 3.3567 3.0041 0.7679  -0.3101 0.1262  17   ILE C N   
6543  C  CA  . ILE C  19  ? 3.6545 3.3580 2.9827 0.7398  -0.3119 0.1201  17   ILE C CA  
6544  C  C   . ILE C  19  ? 3.7124 3.3160 3.0202 0.7588  -0.2688 0.1202  17   ILE C C   
6545  O  O   . ILE C  19  ? 3.6727 3.2148 2.9496 0.7313  -0.2544 0.0910  17   ILE C O   
6546  C  CB  . ILE C  19  ? 3.8085 3.5873 3.0920 0.7366  -0.3461 0.1569  17   ILE C CB  
6547  C  CG1 . ILE C  19  ? 3.8104 3.6915 3.1068 0.7041  -0.3866 0.1500  17   ILE C CG1 
6548  C  CG2 . ILE C  19  ? 3.9785 3.7050 3.1879 0.7075  -0.3452 0.1514  17   ILE C CG2 
6549  C  CD1 . ILE C  19  ? 3.8906 3.8669 3.1434 0.6915  -0.4221 0.1825  17   ILE C CD1 
6550  N  N   . GLU C  20  ? 3.9181 3.5018 3.2372 0.8061  -0.2450 0.1523  18   GLU C N   
6551  C  CA  . GLU C  20  ? 4.0237 3.5039 3.3142 0.8187  -0.1992 0.1515  18   GLU C CA  
6552  C  C   . GLU C  20  ? 4.0747 3.4983 3.4005 0.7996  -0.1655 0.1055  18   GLU C C   
6553  O  O   . GLU C  20  ? 4.1077 3.4533 3.4048 0.7894  -0.1294 0.0903  18   GLU C O   
6554  C  CB  . GLU C  20  ? 4.0145 3.4736 3.2947 0.8760  -0.1779 0.1990  18   GLU C CB  
6555  C  CG  . GLU C  20  ? 3.9702 3.4707 3.1990 0.8998  -0.2021 0.2481  18   GLU C CG  
6556  C  CD  . GLU C  20  ? 3.9707 3.4114 3.1301 0.8730  -0.1947 0.2444  18   GLU C CD  
6557  O  OE1 . GLU C  20  ? 3.8743 3.2182 3.0164 0.8569  -0.1552 0.2181  18   GLU C OE1 
6558  O  OE2 . GLU C  20  ? 4.0461 3.5423 3.1671 0.8648  -0.2279 0.2666  18   GLU C OE2 
6559  N  N   . ALA C  21  ? 4.0079 3.4752 3.3933 0.7925  -0.1761 0.0828  19   ALA C N   
6560  C  CA  . ALA C  21  ? 3.8881 3.3199 3.3061 0.7696  -0.1503 0.0367  19   ALA C CA  
6561  C  C   . ALA C  21  ? 3.9301 3.3651 3.3281 0.7299  -0.1654 0.0009  19   ALA C C   
6562  O  O   . ALA C  21  ? 3.9454 3.3435 3.3478 0.7129  -0.1387 -0.0339 19   ALA C O   
6563  C  CB  . ALA C  21  ? 3.7142 3.1890 3.2002 0.7786  -0.1546 0.0268  19   ALA C CB  
6564  N  N   . ILE C  22  ? 3.8974 3.3776 3.2686 0.7151  -0.2055 0.0088  20   ILE C N   
6565  C  CA  . ILE C  22  ? 3.8217 3.2878 3.1552 0.6816  -0.2158 -0.0213 20   ILE C CA  
6566  C  C   . ILE C  22  ? 3.8150 3.2240 3.0925 0.6760  -0.1946 -0.0202 20   ILE C C   
6567  O  O   . ILE C  22  ? 3.7420 3.1185 3.0024 0.6588  -0.1788 -0.0529 20   ILE C O   
6568  C  CB  . ILE C  22  ? 3.7654 3.2846 3.0723 0.6608  -0.2600 -0.0136 20   ILE C CB  
6569  C  CG1 . ILE C  22  ? 3.7467 3.3184 3.1056 0.6577  -0.2782 -0.0242 20   ILE C CG1 
6570  C  CG2 . ILE C  22  ? 3.7691 3.2533 3.0148 0.6291  -0.2656 -0.0391 20   ILE C CG2 
6571  C  CD1 . ILE C  22  ? 3.6788 3.2236 3.0594 0.6452  -0.2657 -0.0674 20   ILE C CD1 
6572  N  N   . ARG C  23  ? 3.8496 3.2491 3.0958 0.6931  -0.1931 0.0183  21   ARG C N   
6573  C  CA  . ARG C  23  ? 3.8834 3.2250 3.0729 0.6874  -0.1711 0.0221  21   ARG C CA  
6574  C  C   . ARG C  23  ? 3.9250 3.2100 3.1293 0.6850  -0.1241 -0.0058 21   ARG C C   
6575  O  O   . ARG C  23  ? 3.9841 3.2393 3.1590 0.6640  -0.1077 -0.0322 21   ARG C O   
6576  C  CB  . ARG C  23  ? 3.8826 3.2225 3.0386 0.7136  -0.1749 0.0724  21   ARG C CB  
6577  C  CG  . ARG C  23  ? 3.9240 3.1929 3.0210 0.7113  -0.1455 0.0800  21   ARG C CG  
6578  C  CD  . ARG C  23  ? 3.9428 3.2053 3.0054 0.7461  -0.1464 0.1337  21   ARG C CD  
6579  N  NE  . ARG C  23  ? 3.9108 3.2473 2.9499 0.7449  -0.1927 0.1621  21   ARG C NE  
6580  C  CZ  . ARG C  23  ? 3.9818 3.3148 2.9578 0.7243  -0.2063 0.1709  21   ARG C CZ  
6581  N  NH1 . ARG C  23  ? 4.0962 3.3538 3.0284 0.7067  -0.1773 0.1541  21   ARG C NH1 
6582  N  NH2 . ARG C  23  ? 3.9179 3.3281 2.8728 0.7178  -0.2480 0.1950  21   ARG C NH2 
6583  N  N   . GLY C  24  ? 3.7893 3.0627 3.0362 0.7044  -0.0999 -0.0017 22   GLY C N   
6584  C  CA  . GLY C  24  ? 3.7199 2.9477 2.9800 0.6933  -0.0535 -0.0318 22   GLY C CA  
6585  C  C   . GLY C  24  ? 3.6313 2.8918 2.9311 0.6714  -0.0528 -0.0793 22   GLY C C   
6586  O  O   . GLY C  24  ? 3.6232 2.8635 2.9253 0.6540  -0.0176 -0.1100 22   GLY C O   
6587  N  N   . GLN C  25  ? 3.6580 2.9714 2.9847 0.6712  -0.0899 -0.0859 23   GLN C N   
6588  C  CA  . GLN C  25  ? 3.7322 3.0736 3.0885 0.6571  -0.0908 -0.1274 23   GLN C CA  
6589  C  C   . GLN C  25  ? 3.6943 3.0262 3.0017 0.6422  -0.0946 -0.1474 23   GLN C C   
6590  O  O   . GLN C  25  ? 3.6466 2.9801 2.9591 0.6339  -0.0699 -0.1802 23   GLN C O   
6591  C  CB  . GLN C  25  ? 3.7835 3.1725 3.1771 0.6621  -0.1255 -0.1265 23   GLN C CB  
6592  C  CG  . GLN C  25  ? 3.7407 3.1545 3.1629 0.6537  -0.1260 -0.1657 23   GLN C CG  
6593  C  CD  . GLN C  25  ? 3.6673 3.1167 3.1070 0.6532  -0.1620 -0.1643 23   GLN C CD  
6594  O  OE1 . GLN C  25  ? 3.5480 3.0092 2.9646 0.6511  -0.1915 -0.1388 23   GLN C OE1 
6595  N  NE2 . GLN C  25  ? 3.6524 3.1239 3.1302 0.6525  -0.1593 -0.1923 23   GLN C NE2 
6596  N  N   . ILE C  26  ? 3.5342 2.8610 2.7916 0.6384  -0.1240 -0.1282 24   ILE C N   
6597  C  CA  . ILE C  26  ? 3.5266 2.8355 2.7284 0.6252  -0.1270 -0.1462 24   ILE C CA  
6598  C  C   . ILE C  26  ? 3.6159 2.8934 2.7927 0.6196  -0.0905 -0.1568 24   ILE C C   
6599  O  O   . ILE C  26  ? 3.5813 2.8599 2.7454 0.6148  -0.0747 -0.1881 24   ILE C O   
6600  C  CB  . ILE C  26  ? 3.5741 2.8787 2.7189 0.6153  -0.1615 -0.1212 24   ILE C CB  
6601  C  CG1 . ILE C  26  ? 3.5289 2.8714 2.6939 0.6125  -0.1958 -0.1157 24   ILE C CG1 
6602  C  CG2 . ILE C  26  ? 3.7046 2.9770 2.7820 0.6011  -0.1595 -0.1398 24   ILE C CG2 
6603  C  CD1 . ILE C  26  ? 3.5943 2.9449 2.7011 0.5936  -0.2292 -0.0940 24   ILE C CD1 
6604  N  N   . LEU C  27  ? 3.8933 3.1431 3.0585 0.6217  -0.0751 -0.1304 25   LEU C N   
6605  C  CA  . LEU C  27  ? 4.0189 3.2330 3.1537 0.6105  -0.0375 -0.1401 25   LEU C CA  
6606  C  C   . LEU C  27  ? 3.9193 3.1503 3.0974 0.6027  -0.0008 -0.1769 25   LEU C C   
6607  O  O   . LEU C  27  ? 3.9614 3.1905 3.1189 0.5876  0.0265  -0.2021 25   LEU C O   
6608  C  CB  . LEU C  27  ? 4.1339 3.3036 3.2398 0.6170  -0.0263 -0.1012 25   LEU C CB  
6609  C  CG  . LEU C  27  ? 4.1109 3.2749 3.1676 0.6236  -0.0598 -0.0621 25   LEU C CG  
6610  C  CD1 . LEU C  27  ? 4.1128 3.2333 3.1406 0.6391  -0.0443 -0.0217 25   LEU C CD1 
6611  C  CD2 . LEU C  27  ? 4.1152 3.2692 3.1141 0.6040  -0.0673 -0.0755 25   LEU C CD2 
6612  N  N   . SER C  28  ? 3.7733 3.0286 3.0106 0.6102  0.0009  -0.1815 26   SER C N   
6613  C  CA  . SER C  28  ? 3.7130 2.9972 2.9928 0.5983  0.0333  -0.2185 26   SER C CA  
6614  C  C   . SER C  28  ? 3.7168 3.0571 3.0160 0.6017  0.0209  -0.2520 26   SER C C   
6615  O  O   . SER C  28  ? 3.7434 3.1199 3.0571 0.5909  0.0486  -0.2858 26   SER C O   
6616  C  CB  . SER C  28  ? 3.7040 2.9908 3.0358 0.6041  0.0413  -0.2118 26   SER C CB  
6617  O  OG  . SER C  28  ? 3.6882 3.0084 3.0545 0.6220  0.0023  -0.2026 26   SER C OG  
6618  N  N   . LYS C  29  ? 3.6437 2.9933 2.9381 0.6167  -0.0183 -0.2433 27   LYS C N   
6619  C  CA  . LYS C  29  ? 3.6328 3.0185 2.9305 0.6261  -0.0278 -0.2718 27   LYS C CA  
6620  C  C   . LYS C  29  ? 3.7157 3.0897 2.9560 0.6255  -0.0185 -0.2849 27   LYS C C   
6621  O  O   . LYS C  29  ? 3.7492 3.1609 2.9936 0.6351  -0.0055 -0.3149 27   LYS C O   
6622  C  CB  . LYS C  29  ? 3.6561 3.0400 2.9526 0.6371  -0.0680 -0.2593 27   LYS C CB  
6623  C  CG  . LYS C  29  ? 3.5440 2.9508 2.9020 0.6399  -0.0773 -0.2507 27   LYS C CG  
6624  C  CD  . LYS C  29  ? 3.5889 2.9958 2.9382 0.6439  -0.1168 -0.2380 27   LYS C CD  
6625  C  CE  . LYS C  29  ? 3.6543 3.0717 2.9917 0.6528  -0.1244 -0.2650 27   LYS C CE  
6626  N  NZ  . LYS C  29  ? 3.4905 2.9541 2.8923 0.6610  -0.1103 -0.2879 27   LYS C NZ  
6627  N  N   . LEU C  30  ? 3.5869 2.9135 2.7723 0.6167  -0.0241 -0.2620 28   LEU C N   
6628  C  CA  . LEU C  30  ? 3.5302 2.8392 2.6564 0.6134  -0.0130 -0.2726 28   LEU C CA  
6629  C  C   . LEU C  30  ? 3.5846 2.8982 2.7087 0.5965  0.0270  -0.2844 28   LEU C C   
6630  O  O   . LEU C  30  ? 3.6021 2.9088 2.6808 0.5922  0.0408  -0.2960 28   LEU C O   
6631  C  CB  . LEU C  30  ? 3.6049 2.8624 2.6666 0.6071  -0.0393 -0.2433 28   LEU C CB  
6632  C  CG  . LEU C  30  ? 3.6146 2.8629 2.6578 0.6129  -0.0767 -0.2349 28   LEU C CG  
6633  C  CD1 . LEU C  30  ? 3.7268 2.9355 2.7043 0.5973  -0.0994 -0.2067 28   LEU C CD1 
6634  C  CD2 . LEU C  30  ? 3.7051 2.9573 2.7276 0.6289  -0.0734 -0.2657 28   LEU C CD2 
6635  N  N   . ARG C  31  ? 3.7793 3.1001 2.9450 0.5842  0.0486  -0.2829 29   ARG C N   
6636  C  CA  . ARG C  31  ? 3.8048 3.1170 2.9584 0.5591  0.0907  -0.2933 29   ARG C CA  
6637  C  C   . ARG C  31  ? 3.9202 3.1705 3.0043 0.5492  0.0923  -0.2696 29   ARG C C   
6638  O  O   . ARG C  31  ? 3.9234 3.1729 2.9737 0.5316  0.1197  -0.2862 29   ARG C O   
6639  C  CB  . ARG C  31  ? 3.6465 3.0288 2.8173 0.5518  0.1192  -0.3373 29   ARG C CB  
6640  C  CG  . ARG C  31  ? 3.5366 2.9884 2.7760 0.5566  0.1242  -0.3616 29   ARG C CG  
6641  C  CD  . ARG C  31  ? 3.5803 3.1113 2.8362 0.5386  0.1622  -0.4027 29   ARG C CD  
6642  N  NE  . ARG C  31  ? 3.6646 3.2825 2.9776 0.5546  0.1583  -0.4280 29   ARG C NE  
6643  C  CZ  . ARG C  31  ? 3.6275 3.2842 2.9919 0.5357  0.1748  -0.4416 29   ARG C CZ  
6644  N  NH1 . ARG C  31  ? 3.6032 3.2087 2.9640 0.5009  0.1994  -0.4329 29   ARG C NH1 
6645  N  NH2 . ARG C  31  ? 3.5532 3.2945 2.9660 0.5525  0.1687  -0.4635 29   ARG C NH2 
6646  N  N   . LEU C  32  ? 3.9455 3.1518 3.0078 0.5598  0.0622  -0.2306 30   LEU C N   
6647  C  CA  . LEU C  32  ? 3.9663 3.1173 2.9624 0.5528  0.0589  -0.2019 30   LEU C CA  
6648  C  C   . LEU C  32  ? 4.0151 3.1185 3.0066 0.5546  0.0680  -0.1663 30   LEU C C   
6649  O  O   . LEU C  32  ? 4.0480 3.1600 3.0825 0.5704  0.0562  -0.1518 30   LEU C O   
6650  C  CB  . LEU C  32  ? 4.0376 3.1834 2.9988 0.5633  0.0160  -0.1834 30   LEU C CB  
6651  C  CG  . LEU C  32  ? 4.1187 3.2812 3.0525 0.5641  0.0103  -0.2118 30   LEU C CG  
6652  C  CD1 . LEU C  32  ? 4.1488 3.2897 3.0345 0.5655  -0.0284 -0.1911 30   LEU C CD1 
6653  C  CD2 . LEU C  32  ? 4.2231 3.3753 3.1172 0.5489  0.0439  -0.2311 30   LEU C CD2 
6654  N  N   . ALA C  33  ? 4.0333 3.0829 2.9679 0.5412  0.0910  -0.1518 31   ALA C N   
6655  C  CA  . ALA C  33  ? 4.1157 3.1061 3.0264 0.5516  0.0990  -0.1108 31   ALA C CA  
6656  C  C   . ALA C  33  ? 4.1052 3.0837 2.9760 0.5704  0.0597  -0.0664 31   ALA C C   
6657  O  O   . ALA C  33  ? 4.1628 3.1260 3.0360 0.5955  0.0479  -0.0274 31   ALA C O   
6658  C  CB  . ALA C  33  ? 4.2525 3.1800 3.1129 0.5263  0.1499  -0.1164 31   ALA C CB  
6659  N  N   . SER C  34  ? 4.1491 3.1400 2.9818 0.5595  0.0399  -0.0718 32   SER C N   
6660  C  CA  . SER C  34  ? 4.2856 3.2736 3.0739 0.5682  0.0035  -0.0333 32   SER C CA  
6661  C  C   . SER C  34  ? 4.3208 3.3390 3.0899 0.5539  -0.0222 -0.0548 32   SER C C   
6662  O  O   . SER C  34  ? 4.3389 3.3599 3.1055 0.5396  -0.0022 -0.0937 32   SER C O   
6663  C  CB  . SER C  34  ? 4.4632 3.3898 3.1802 0.5636  0.0229  -0.0047 32   SER C CB  
6664  O  OG  . SER C  34  ? 4.5948 3.5316 3.2669 0.5692  -0.0137 0.0309  32   SER C OG  
6665  N  N   . PRO C  35  ? 4.2476 3.2899 2.9986 0.5571  -0.0641 -0.0312 33   PRO C N   
6666  C  CA  . PRO C  35  ? 4.1817 3.2344 2.8968 0.5390  -0.0839 -0.0517 33   PRO C CA  
6667  C  C   . PRO C  35  ? 4.2428 3.2556 2.8859 0.5189  -0.0674 -0.0573 33   PRO C C   
6668  O  O   . PRO C  35  ? 4.2613 3.2450 2.8678 0.5168  -0.0579 -0.0295 33   PRO C O   
6669  C  CB  . PRO C  35  ? 4.1249 3.2125 2.8290 0.5391  -0.1291 -0.0204 33   PRO C CB  
6670  C  CG  . PRO C  35  ? 4.1276 3.2268 2.8539 0.5623  -0.1330 0.0222  33   PRO C CG  
6671  C  CD  . PRO C  35  ? 4.1439 3.2149 2.9146 0.5777  -0.0934 0.0099  33   PRO C CD  
6672  N  N   . PRO C  36  ? 4.2125 3.2192 2.8284 0.5065  -0.0625 -0.0915 34   PRO C N   
6673  C  CA  . PRO C  36  ? 4.2781 3.2490 2.8290 0.4884  -0.0415 -0.1032 34   PRO C CA  
6674  C  C   . PRO C  36  ? 4.2538 3.2066 2.7288 0.4688  -0.0678 -0.0780 34   PRO C C   
6675  O  O   . PRO C  36  ? 4.1570 3.1328 2.6277 0.4666  -0.1032 -0.0531 34   PRO C O   
6676  C  CB  . PRO C  36  ? 4.3350 3.3136 2.8910 0.4921  -0.0260 -0.1495 34   PRO C CB  
6677  C  CG  . PRO C  36  ? 4.2436 3.2466 2.8316 0.5039  -0.0544 -0.1528 34   PRO C CG  
6678  C  CD  . PRO C  36  ? 4.1618 3.1915 2.8081 0.5141  -0.0694 -0.1236 34   PRO C CD  
6679  N  N   . SER C  37  ? 4.2790 3.1966 2.6917 0.4511  -0.0487 -0.0869 35   SER C N   
6680  C  CA  . SER C  37  ? 4.3997 3.2972 2.7323 0.4273  -0.0682 -0.0646 35   SER C CA  
6681  C  C   . SER C  37  ? 4.4700 3.3285 2.7428 0.4102  -0.0400 -0.0934 35   SER C C   
6682  O  O   . SER C  37  ? 4.5077 3.3455 2.7662 0.4051  -0.0125 -0.0919 35   SER C O   
6683  C  CB  . SER C  37  ? 4.3933 3.2914 2.7143 0.4298  -0.0774 -0.0169 35   SER C CB  
6684  O  OG  . SER C  37  ? 4.3691 3.2324 2.6869 0.4325  -0.0397 -0.0183 35   SER C OG  
6685  N  N   . GLN C  38  ? 4.4589 3.3027 2.6909 0.4012  -0.0444 -0.1193 36   GLN C N   
6686  C  CA  . GLN C  38  ? 4.4488 3.2566 2.6232 0.3911  -0.0154 -0.1486 36   GLN C CA  
6687  C  C   . GLN C  38  ? 4.3722 3.1413 2.4530 0.3635  -0.0306 -0.1487 36   GLN C C   
6688  O  O   . GLN C  38  ? 4.3336 3.1104 2.3906 0.3447  -0.0649 -0.1231 36   GLN C O   
6689  C  CB  . GLN C  38  ? 4.4207 3.2414 2.6345 0.4178  0.0115  -0.1917 36   GLN C CB  
6690  C  CG  . GLN C  38  ? 4.3703 3.2299 2.6612 0.4345  0.0377  -0.2016 36   GLN C CG  
6691  C  CD  . GLN C  38  ? 4.4718 3.3176 2.7365 0.4163  0.0673  -0.2002 36   GLN C CD  
6692  O  OE1 . GLN C  38  ? 4.5407 3.3517 2.7322 0.3967  0.0729  -0.2000 36   GLN C OE1 
6693  N  NE2 . GLN C  38  ? 4.4556 3.3235 2.7738 0.4188  0.0887  -0.2006 36   GLN C NE2 
6694  N  N   . GLY C  39  ? 4.1640 2.8951 2.1883 0.3589  -0.0030 -0.1785 37   GLY C N   
6695  C  CA  . GLY C  39  ? 4.1922 2.8727 2.1184 0.3322  -0.0099 -0.1854 37   GLY C CA  
6696  C  C   . GLY C  39  ? 4.1141 2.7809 2.0306 0.3363  -0.0274 -0.1968 37   GLY C C   
6697  O  O   . GLY C  39  ? 4.0712 2.7581 2.0496 0.3699  -0.0219 -0.2133 37   GLY C O   
6698  N  N   . GLU C  40  ? 4.2024 2.8339 2.0342 0.2976  -0.0471 -0.1887 38   GLU C N   
6699  C  CA  . GLU C  40  ? 4.1778 2.8038 1.9952 0.2850  -0.0723 -0.1885 38   GLU C CA  
6700  C  C   . GLU C  40  ? 4.2866 2.8245 1.9943 0.2683  -0.0552 -0.2188 38   GLU C C   
6701  O  O   . GLU C  40  ? 4.3223 2.8120 1.9357 0.2340  -0.0463 -0.2217 38   GLU C O   
6702  C  CB  . GLU C  40  ? 3.9593 2.6339 1.7710 0.2458  -0.1142 -0.1497 38   GLU C CB  
6703  C  CG  . GLU C  40  ? 3.9258 2.6279 1.7598 0.2370  -0.1439 -0.1462 38   GLU C CG  
6704  C  CD  . GLU C  40  ? 3.9400 2.7091 1.7582 0.1920  -0.1881 -0.1092 38   GLU C CD  
6705  O  OE1 . GLU C  40  ? 3.9525 2.7674 1.7709 0.1811  -0.2020 -0.0758 38   GLU C OE1 
6706  O  OE2 . GLU C  40  ? 3.9423 2.7227 1.7456 0.1682  -0.2083 -0.1138 38   GLU C OE2 
6707  N  N   . VAL C  41  ? 4.6957 3.2064 2.4101 0.2936  -0.0483 -0.2407 39   VAL C N   
6708  C  CA  . VAL C  41  ? 4.8123 3.2248 2.4161 0.2829  -0.0306 -0.2679 39   VAL C CA  
6709  C  C   . VAL C  41  ? 4.8761 3.2923 2.5049 0.2875  -0.0492 -0.2697 39   VAL C C   
6710  O  O   . VAL C  41  ? 4.6699 3.1506 2.4074 0.3255  -0.0573 -0.2646 39   VAL C O   
6711  C  CB  . VAL C  41  ? 4.7885 3.1472 2.3647 0.3316  0.0153  -0.3003 39   VAL C CB  
6712  C  CG1 . VAL C  41  ? 4.9660 3.2104 2.4241 0.3323  0.0373  -0.3265 39   VAL C CG1 
6713  C  CG2 . VAL C  41  ? 4.7507 3.1082 2.2990 0.3219  0.0347  -0.3001 39   VAL C CG2 
6714  N  N   . PRO C  42  ? 5.2768 3.6241 2.8030 0.2439  -0.0551 -0.2775 40   PRO C N   
6715  C  CA  . PRO C  42  ? 5.4908 3.7625 2.8785 0.1821  -0.0502 -0.2828 40   PRO C CA  
6716  C  C   . PRO C  42  ? 5.6013 3.9289 2.9737 0.1122  -0.0919 -0.2581 40   PRO C C   
6717  O  O   . PRO C  42  ? 5.5822 3.9786 3.0286 0.1133  -0.1206 -0.2442 40   PRO C O   
6718  C  CB  . PRO C  42  ? 5.4494 3.5942 2.7320 0.1928  -0.0186 -0.3159 40   PRO C CB  
6719  C  CG  . PRO C  42  ? 5.2848 3.4647 2.6574 0.2384  -0.0279 -0.3176 40   PRO C CG  
6720  C  CD  . PRO C  42  ? 5.1979 3.5162 2.7283 0.2621  -0.0561 -0.2912 40   PRO C CD  
6721  N  N   . PRO C  43  ? 5.7796 4.0866 3.0572 0.0517  -0.0952 -0.2529 41   PRO C N   
6722  C  CA  . PRO C  43  ? 5.7078 4.0814 2.9622 -0.0185 -0.1345 -0.2308 41   PRO C CA  
6723  C  C   . PRO C  43  ? 5.6678 3.9902 2.8479 -0.0614 -0.1378 -0.2494 41   PRO C C   
6724  O  O   . PRO C  43  ? 5.7465 4.1490 2.9325 -0.1132 -0.1732 -0.2322 41   PRO C O   
6725  C  CB  . PRO C  43  ? 5.8027 4.1530 2.9585 -0.0714 -0.1292 -0.2271 41   PRO C CB  
6726  C  CG  . PRO C  43  ? 5.9135 4.1334 2.9895 -0.0454 -0.0795 -0.2606 41   PRO C CG  
6727  C  CD  . PRO C  43  ? 5.8305 4.0592 3.0150 0.0425  -0.0627 -0.2678 41   PRO C CD  
6728  N  N   . GLY C  44  ? 5.7453 4.8994 2.6907 0.8467  -0.9743 -0.6258 42   GLY C N   
6729  C  CA  . GLY C  44  ? 5.5015 4.6027 2.5421 0.7654  -1.0560 -0.6788 42   GLY C CA  
6730  C  C   . GLY C  44  ? 5.1307 4.2470 2.2885 0.7049  -1.0176 -0.6594 42   GLY C C   
6731  O  O   . GLY C  44  ? 4.9357 4.1149 2.1160 0.7132  -0.9456 -0.6015 42   GLY C O   
6732  N  N   . PRO C  45  ? 4.8721 3.9297 2.1076 0.6444  -1.0641 -0.7059 43   PRO C N   
6733  C  CA  . PRO C  45  ? 4.7052 3.7760 2.0577 0.5833  -1.0348 -0.6901 43   PRO C CA  
6734  C  C   . PRO C  45  ? 4.8448 3.9115 2.1526 0.6259  -0.9274 -0.6715 43   PRO C C   
6735  O  O   . PRO C  45  ? 4.9253 3.9404 2.1481 0.6767  -0.8983 -0.6980 43   PRO C O   
6736  C  CB  . PRO C  45  ? 4.6935 3.6979 2.1307 0.5177  -1.1141 -0.7451 43   PRO C CB  
6737  C  CG  . PRO C  45  ? 4.9382 3.8732 2.2695 0.5651  -1.1519 -0.7956 43   PRO C CG  
6738  C  CD  . PRO C  45  ? 5.0387 4.0160 2.2642 0.6282  -1.1484 -0.7726 43   PRO C CD  
6739  N  N   . LEU C  46  ? 4.6514 3.8003 2.0998 0.5873  -0.8429 -0.6046 44   LEU C N   
6740  C  CA  . LEU C  46  ? 4.5322 3.7092 2.0029 0.6094  -0.7272 -0.5647 44   LEU C CA  
6741  C  C   . LEU C  46  ? 4.5649 3.6656 2.0034 0.6150  -0.7194 -0.6128 44   LEU C C   
6742  O  O   . LEU C  46  ? 4.4544 3.4932 1.9206 0.5715  -0.7954 -0.6667 44   LEU C O   
6743  C  CB  . LEU C  46  ? 4.1803 3.4429 1.8417 0.5405  -0.6692 -0.5019 44   LEU C CB  
6744  C  CG  . LEU C  46  ? 4.1553 3.4809 1.8849 0.5099  -0.7043 -0.4664 44   LEU C CG  
6745  C  CD1 . LEU C  46  ? 4.0805 3.4098 1.9540 0.4219  -0.7686 -0.4803 44   LEU C CD1 
6746  C  CD2 . LEU C  46  ? 4.1157 3.5259 1.9141 0.5175  -0.6078 -0.3891 44   LEU C CD2 
6747  N  N   . PRO C  47  ? 4.7644 3.8694 2.1535 0.6671  -0.6283 -0.5907 45   PRO C N   
6748  C  CA  . PRO C  47  ? 4.8178 3.8512 2.1692 0.6801  -0.6178 -0.6339 45   PRO C CA  
6749  C  C   . PRO C  47  ? 4.4872 3.5239 2.0067 0.5902  -0.6252 -0.6389 45   PRO C C   
6750  O  O   . PRO C  47  ? 4.3110 3.4245 1.9795 0.5345  -0.5830 -0.5880 45   PRO C O   
6751  C  CB  . PRO C  47  ? 4.8467 3.9168 2.1521 0.7455  -0.5047 -0.5851 45   PRO C CB  
6752  C  CG  . PRO C  47  ? 4.6384 3.8106 2.0367 0.7292  -0.4477 -0.5084 45   PRO C CG  
6753  C  CD  . PRO C  47  ? 4.7415 3.9208 2.1202 0.7150  -0.5285 -0.5195 45   PRO C CD  
6754  N  N   . GLU C  48  ? 4.5014 3.4510 1.9921 0.5801  -0.6795 -0.7012 46   GLU C N   
6755  C  CA  . GLU C  48  ? 4.3225 3.2665 1.9628 0.4987  -0.6989 -0.7105 46   GLU C CA  
6756  C  C   . GLU C  48  ? 4.0761 3.0531 1.7933 0.4900  -0.6054 -0.6777 46   GLU C C   
6757  O  O   . GLU C  48  ? 3.9505 2.9258 1.7860 0.4291  -0.6131 -0.6825 46   GLU C O   
6758  C  CB  . GLU C  48  ? 4.3404 3.1748 1.9267 0.4915  -0.7939 -0.7871 46   GLU C CB  
6759  C  CG  . GLU C  48  ? 4.3611 3.1704 1.9213 0.4770  -0.8987 -0.8176 46   GLU C CG  
6760  C  CD  . GLU C  48  ? 4.3822 3.1158 1.9910 0.4386  -0.9776 -0.8682 46   GLU C CD  
6761  O  OE1 . GLU C  48  ? 4.3237 3.0027 1.9288 0.4469  -0.9548 -0.8916 46   GLU C OE1 
6762  O  OE2 . GLU C  48  ? 4.5027 3.2329 2.1579 0.4003  -1.0619 -0.8814 46   GLU C OE2 
6763  N  N   . ALA C  49  ? 4.1423 3.1521 1.7993 0.5499  -0.5187 -0.6417 47   ALA C N   
6764  C  CA  . ALA C  49  ? 4.1264 3.1839 1.8777 0.5347  -0.4309 -0.6016 47   ALA C CA  
6765  C  C   . ALA C  49  ? 4.0596 3.2095 1.9770 0.4665  -0.3999 -0.5475 47   ALA C C   
6766  O  O   . ALA C  49  ? 3.7552 2.9313 1.7934 0.4159  -0.3731 -0.5346 47   ALA C O   
6767  C  CB  . ALA C  49  ? 4.1743 3.2468 1.8267 0.6173  -0.3480 -0.5713 47   ALA C CB  
6768  N  N   . VAL C  50  ? 4.2754 3.4740 2.1965 0.4680  -0.4033 -0.5158 48   VAL C N   
6769  C  CA  . VAL C  50  ? 3.9165 3.1941 1.9872 0.4068  -0.3802 -0.4686 48   VAL C CA  
6770  C  C   . VAL C  50  ? 3.8308 3.1013 1.9821 0.3409  -0.4603 -0.4906 48   VAL C C   
6771  O  O   . VAL C  50  ? 3.8392 3.1643 2.1266 0.2834  -0.4453 -0.4603 48   VAL C O   
6772  C  CB  . VAL C  50  ? 3.9129 3.2501 1.9642 0.4390  -0.3386 -0.4162 48   VAL C CB  
6773  C  CG1 . VAL C  50  ? 4.0377 3.3883 2.0210 0.5055  -0.2558 -0.3852 48   VAL C CG1 
6774  C  CG2 . VAL C  50  ? 4.0327 3.3476 1.9881 0.4648  -0.4092 -0.4361 48   VAL C CG2 
6775  N  N   . LEU C  51  ? 3.8079 3.0125 1.8802 0.3495  -0.5464 -0.5414 49   LEU C N   
6776  C  CA  . LEU C  51  ? 3.7318 2.9287 1.8945 0.2845  -0.6249 -0.5597 49   LEU C CA  
6777  C  C   . LEU C  51  ? 3.9266 3.1014 2.1824 0.2372  -0.6261 -0.5764 49   LEU C C   
6778  O  O   . LEU C  51  ? 3.9090 3.1085 2.2882 0.1745  -0.6588 -0.5670 49   LEU C O   
6779  C  CB  . LEU C  51  ? 3.7430 2.8730 1.8004 0.3053  -0.7229 -0.6101 49   LEU C CB  
6780  C  CG  . LEU C  51  ? 3.9070 3.0664 1.8877 0.3423  -0.7413 -0.5927 49   LEU C CG  
6781  C  CD1 . LEU C  51  ? 4.1746 3.2631 2.0559 0.3576  -0.8505 -0.6499 49   LEU C CD1 
6782  C  CD2 . LEU C  51  ? 3.7389 2.9898 1.8521 0.2948  -0.7242 -0.5348 49   LEU C CD2 
6783  N  N   . ALA C  52  ? 4.0476 3.1800 2.2477 0.2694  -0.5886 -0.5967 50   ALA C N   
6784  C  CA  . ALA C  52  ? 3.8619 2.9826 2.1531 0.2289  -0.5782 -0.6046 50   ALA C CA  
6785  C  C   . ALA C  52  ? 3.5381 2.7464 1.9620 0.1899  -0.5082 -0.5513 50   ALA C C   
6786  O  O   . ALA C  52  ? 3.3946 2.6209 1.9340 0.1362  -0.5168 -0.5453 50   ALA C O   
6787  C  CB  . ALA C  52  ? 4.0086 3.0636 2.2015 0.2795  -0.5530 -0.6370 50   ALA C CB  
6788  N  N   . LEU C  53  ? 3.5710 2.8329 1.9800 0.2183  -0.4394 -0.5118 51   LEU C N   
6789  C  CA  . LEU C  53  ? 3.4774 2.8183 2.0090 0.1814  -0.3811 -0.4641 51   LEU C CA  
6790  C  C   . LEU C  53  ? 3.4275 2.8101 2.0526 0.1316  -0.4175 -0.4450 51   LEU C C   
6791  O  O   . LEU C  53  ? 3.4883 2.9087 2.2302 0.0834  -0.4072 -0.4280 51   LEU C O   
6792  C  CB  . LEU C  53  ? 3.5930 2.9759 2.0907 0.2232  -0.3064 -0.4250 51   LEU C CB  
6793  C  CG  . LEU C  53  ? 3.6808 3.0656 2.1613 0.2535  -0.2386 -0.4157 51   LEU C CG  
6794  C  CD1 . LEU C  53  ? 3.9039 3.2160 2.2507 0.3102  -0.2546 -0.4546 51   LEU C CD1 
6795  C  CD2 . LEU C  53  ? 3.6107 3.0545 2.1061 0.2770  -0.1665 -0.3635 51   LEU C CD2 
6796  N  N   . TYR C  54  ? 3.3465 2.7256 1.9196 0.1465  -0.4596 -0.4453 52   TYR C N   
6797  C  CA  . TYR C  54  ? 3.3199 2.7451 1.9820 0.1045  -0.4905 -0.4205 52   TYR C CA  
6798  C  C   . TYR C  54  ? 3.3388 2.7447 2.0778 0.0540  -0.5560 -0.4411 52   TYR C C   
6799  O  O   . TYR C  54  ? 3.4411 2.8970 2.2958 0.0094  -0.5578 -0.4123 52   TYR C O   
6800  C  CB  . TYR C  54  ? 3.4898 2.9170 2.0737 0.1361  -0.5231 -0.4151 52   TYR C CB  
6801  C  CG  . TYR C  54  ? 3.5249 3.0041 2.1983 0.0983  -0.5529 -0.3844 52   TYR C CG  
6802  C  CD1 . TYR C  54  ? 3.3818 2.9283 2.1379 0.0842  -0.4948 -0.3350 52   TYR C CD1 
6803  C  CD2 . TYR C  54  ? 3.7380 3.1979 2.4160 0.0780  -0.6406 -0.4038 52   TYR C CD2 
6804  C  CE1 . TYR C  54  ? 3.4344 3.0281 2.2698 0.0551  -0.5182 -0.3047 52   TYR C CE1 
6805  C  CE2 . TYR C  54  ? 3.7356 3.2494 2.5010 0.0459  -0.6660 -0.3699 52   TYR C CE2 
6806  C  CZ  . TYR C  54  ? 3.6020 3.1831 2.4432 0.0367  -0.6021 -0.3197 52   TYR C CZ  
6807  O  OH  . TYR C  54  ? 3.5748 3.2089 2.5010 0.0096  -0.6242 -0.2840 52   TYR C OH  
6808  N  N   . ASN C  55  ? 3.3909 2.7234 2.0693 0.0625  -0.6090 -0.4885 53   ASN C N   
6809  C  CA  . ASN C  55  ? 3.5113 2.8211 2.2720 0.0140  -0.6700 -0.5051 53   ASN C CA  
6810  C  C   . ASN C  55  ? 3.6204 2.9494 2.4749 -0.0156 -0.6253 -0.4931 53   ASN C C   
6811  O  O   . ASN C  55  ? 3.5588 2.8974 2.5163 -0.0613 -0.6579 -0.4861 53   ASN C O   
6812  C  CB  . ASN C  55  ? 3.6598 2.8757 2.3253 0.0334  -0.7447 -0.5624 53   ASN C CB  
6813  C  CG  . ASN C  55  ? 3.9241 3.1255 2.5344 0.0426  -0.8190 -0.5754 53   ASN C CG  
6814  O  OD1 . ASN C  55  ? 3.7574 3.0213 2.3897 0.0416  -0.8071 -0.5385 53   ASN C OD1 
6815  N  ND2 . ASN C  55  ? 4.9528 4.0700 3.4907 0.0528  -0.8983 -0.6287 53   ASN C ND2 
6816  N  N   . SER C  56  ? 3.7657 3.1049 2.5910 0.0106  -0.5517 -0.4867 54   SER C N   
6817  C  CA  . SER C  56  ? 3.5618 2.9282 2.4728 -0.0142 -0.5062 -0.4726 54   SER C CA  
6818  C  C   . SER C  56  ? 3.3505 2.8003 2.3593 -0.0401 -0.4571 -0.4264 54   SER C C   
6819  O  O   . SER C  56  ? 3.3110 2.7908 2.4071 -0.0686 -0.4343 -0.4127 54   SER C O   
6820  C  CB  . SER C  56  ? 3.5024 2.8414 2.3415 0.0257  -0.4541 -0.4874 54   SER C CB  
6821  O  OG  . SER C  56  ? 3.6276 2.8825 2.3669 0.0565  -0.4954 -0.5328 54   SER C OG  
6822  N  N   . THR C  57  ? 3.1895 2.6748 2.1824 -0.0276 -0.4406 -0.4025 55   THR C N   
6823  C  CA  . THR C  57  ? 3.0746 2.6298 2.1550 -0.0488 -0.3958 -0.3619 55   THR C CA  
6824  C  C   . THR C  57  ? 3.1310 2.7195 2.3008 -0.0869 -0.4362 -0.3416 55   THR C C   
6825  O  O   . THR C  57  ? 3.2796 2.9163 2.5404 -0.1122 -0.4083 -0.3157 55   THR C O   
6826  C  CB  . THR C  57  ? 3.1180 2.6957 2.1500 -0.0169 -0.3533 -0.3402 55   THR C CB  
6827  O  OG1 . THR C  57  ? 3.3311 2.8767 2.2731 0.0248  -0.3220 -0.3554 55   THR C OG1 
6828  C  CG2 . THR C  57  ? 3.0863 2.7229 2.2035 -0.0349 -0.2977 -0.3052 55   THR C CG2 
6829  N  N   . ARG C  58  ? 3.0959 2.6613 2.2416 -0.0891 -0.5022 -0.3515 56   ARG C N   
6830  C  CA  . ARG C  58  ? 3.0738 2.6725 2.3148 -0.1264 -0.5459 -0.3287 56   ARG C CA  
6831  C  C   . ARG C  58  ? 3.0498 2.6372 2.3675 -0.1601 -0.5733 -0.3353 56   ARG C C   
6832  O  O   . ARG C  58  ? 2.9931 2.6195 2.4108 -0.1922 -0.5971 -0.3065 56   ARG C O   
6833  C  CB  . ARG C  58  ? 3.1701 2.7497 2.3674 -0.1201 -0.6147 -0.3365 56   ARG C CB  
6834  C  CG  . ARG C  58  ? 3.1595 2.7550 2.2822 -0.0839 -0.5916 -0.3240 56   ARG C CG  
6835  C  CD  . ARG C  58  ? 3.1780 2.7766 2.2861 -0.0845 -0.6611 -0.3199 56   ARG C CD  
6836  N  NE  . ARG C  58  ? 3.2263 2.7540 2.2513 -0.0732 -0.7333 -0.3680 56   ARG C NE  
6837  C  CZ  . ARG C  58  ? 3.3163 2.8174 2.3926 -0.1072 -0.8068 -0.3851 56   ARG C CZ  
6838  N  NH1 . ARG C  58  ? 3.1656 2.7133 2.3798 -0.1530 -0.8132 -0.3516 56   ARG C NH1 
6839  N  NH2 . ARG C  58  ? 3.5925 3.0191 2.5832 -0.0933 -0.8741 -0.4347 56   ARG C NH2 
6840  N  N   . ASP C  59  ? 3.3228 2.8608 2.5999 -0.1510 -0.5674 -0.3676 57   ASP C N   
6841  C  CA  . ASP C  59  ? 3.3979 2.9137 2.7387 -0.1789 -0.5983 -0.3763 57   ASP C CA  
6842  C  C   . ASP C  59  ? 3.1755 2.7464 2.6036 -0.1954 -0.5412 -0.3468 57   ASP C C   
6843  O  O   . ASP C  59  ? 3.2391 2.8000 2.6464 -0.1834 -0.4990 -0.3588 57   ASP C O   
6844  C  CB  . ASP C  59  ? 3.5621 2.9952 2.8132 -0.1563 -0.6179 -0.4247 57   ASP C CB  
6845  C  CG  . ASP C  59  ? 3.5515 2.9498 2.8671 -0.1843 -0.6580 -0.4352 57   ASP C CG  
6846  O  OD1 . ASP C  59  ? 3.5278 2.9749 2.9625 -0.2197 -0.6596 -0.3997 57   ASP C OD1 
6847  O  OD2 . ASP C  59  ? 3.5418 2.8624 2.7880 -0.1674 -0.6859 -0.4773 57   ASP C OD2 
6848  N  N   . ARG C  60  ? 2.9914 2.6235 2.5181 -0.2207 -0.5412 -0.3063 58   ARG C N   
6849  C  CA  . ARG C  60  ? 3.0518 2.7372 2.6622 -0.2343 -0.4956 -0.2774 58   ARG C CA  
6850  C  C   . ARG C  60  ? 2.9508 2.6332 2.6486 -0.2630 -0.5353 -0.2653 58   ARG C C   
6851  O  O   . ARG C  60  ? 2.9009 2.5923 2.6581 -0.2845 -0.5866 -0.2460 58   ARG C O   
6852  C  CB  . ARG C  60  ? 3.2859 3.0398 2.9438 -0.2357 -0.4615 -0.2386 58   ARG C CB  
6853  C  CG  . ARG C  60  ? 3.4101 3.1979 3.1371 -0.2543 -0.5036 -0.2046 58   ARG C CG  
6854  C  CD  . ARG C  60  ? 3.2148 3.0601 3.0579 -0.2744 -0.4928 -0.1618 58   ARG C CD  
6855  N  NE  . ARG C  60  ? 2.9881 2.8544 2.9127 -0.2980 -0.5485 -0.1303 58   ARG C NE  
6856  C  CZ  . ARG C  60  ? 2.7965 2.7085 2.8317 -0.3168 -0.5526 -0.0881 58   ARG C CZ  
6857  N  NH1 . ARG C  60  ? 2.7435 2.6833 2.8103 -0.3116 -0.5040 -0.0753 58   ARG C NH1 
6858  N  NH2 . ARG C  60  ? 2.8004 2.7338 2.9170 -0.3394 -0.6057 -0.0556 58   ARG C NH2 
6859  N  N   . VAL C  61  ? 2.9529 2.6218 2.6613 -0.2628 -0.5137 -0.2747 59   VAL C N   
6860  C  CA  . VAL C  61  ? 3.0501 2.7283 2.8554 -0.2876 -0.5358 -0.2528 59   VAL C CA  
6861  C  C   . VAL C  61  ? 3.1525 2.8763 2.9911 -0.2811 -0.4741 -0.2352 59   VAL C C   
6862  O  O   . VAL C  61  ? 3.2423 3.0345 3.1478 -0.2857 -0.4457 -0.1958 59   VAL C O   
6863  C  CB  . VAL C  61  ? 3.0698 2.6662 2.8518 -0.2937 -0.5902 -0.2873 59   VAL C CB  
6864  C  CG1 . VAL C  61  ? 3.0879 2.6973 2.9898 -0.3238 -0.6191 -0.2553 59   VAL C CG1 
6865  C  CG2 . VAL C  61  ? 3.0328 2.5744 2.7501 -0.2913 -0.6516 -0.3176 59   VAL C CG2 
6866  N  N   . ALA C  62  ? 3.2088 2.8955 2.9971 -0.2668 -0.4538 -0.2641 60   ALA C N   
6867  C  CA  . ALA C  62  ? 3.1159 2.8426 2.9199 -0.2568 -0.3971 -0.2540 60   ALA C CA  
6868  C  C   . ALA C  62  ? 3.0249 2.8026 2.9359 -0.2724 -0.3923 -0.2113 60   ALA C C   
6869  O  O   . ALA C  62  ? 3.0289 2.8143 3.0144 -0.2932 -0.4309 -0.1841 60   ALA C O   
6870  C  CB  . ALA C  62  ? 3.0162 2.7863 2.7864 -0.2415 -0.3477 -0.2514 60   ALA C CB  
6871  N  N   . ALA C  74  ? 2.9051 2.6569 2.7688 -0.1353 0.1281  -0.2166 72   ALA C N   
6872  C  CA  . ALA C  74  ? 2.8478 2.6171 2.7105 -0.1508 0.1236  -0.2215 72   ALA C CA  
6873  C  C   . ALA C  74  ? 2.9331 2.7100 2.7829 -0.1441 0.1371  -0.1847 72   ALA C C   
6874  O  O   . ALA C  74  ? 2.9870 2.7459 2.8574 -0.1362 0.1575  -0.1574 72   ALA C O   
6875  C  CB  . ALA C  74  ? 2.7349 2.5360 2.5653 -0.1537 0.1015  -0.2413 72   ALA C CB  
6876  N  N   . ASP C  75  ? 3.0509 2.8526 2.8632 -0.1436 0.1260  -0.1837 73   ASP C N   
6877  C  CA  . ASP C  75  ? 3.0430 2.8509 2.8282 -0.1315 0.1368  -0.1545 73   ASP C CA  
6878  C  C   . ASP C  75  ? 3.0457 2.8594 2.7886 -0.1138 0.1258  -0.1348 73   ASP C C   
6879  O  O   . ASP C  75  ? 2.9872 2.8156 2.6920 -0.1127 0.1000  -0.1443 73   ASP C O   
6880  C  CB  . ASP C  75  ? 3.1335 2.9580 2.8931 -0.1352 0.1291  -0.1662 73   ASP C CB  
6881  C  CG  . ASP C  75  ? 3.2862 3.1124 3.0940 -0.1520 0.1400  -0.1785 73   ASP C CG  
6882  O  OD1 . ASP C  75  ? 3.3723 3.2037 3.1972 -0.1671 0.1243  -0.2095 73   ASP C OD1 
6883  O  OD2 . ASP C  75  ? 3.2771 3.1033 3.1085 -0.1485 0.1640  -0.1543 73   ASP C OD2 
6884  N  N   . TYR C  76  ? 3.1526 2.9553 2.9075 -0.1007 0.1435  -0.1054 74   TYR C N   
6885  C  CA  . TYR C  76  ? 3.2456 3.0579 2.9652 -0.0825 0.1327  -0.0817 74   TYR C CA  
6886  C  C   . TYR C  76  ? 3.1791 2.9975 2.8522 -0.0625 0.1377  -0.0560 74   TYR C C   
6887  O  O   . TYR C  76  ? 3.1837 3.0127 2.8157 -0.0474 0.1190  -0.0416 74   TYR C O   
6888  C  CB  . TYR C  76  ? 3.4990 3.2986 3.2538 -0.0740 0.1492  -0.0611 74   TYR C CB  
6889  C  CG  . TYR C  76  ? 3.6551 3.4528 3.4323 -0.0810 0.1385  -0.0823 74   TYR C CG  
6890  C  CD1 . TYR C  76  ? 3.5570 3.3789 3.3150 -0.0753 0.1147  -0.0781 74   TYR C CD1 
6891  C  CD2 . TYR C  76  ? 3.6483 3.4208 3.4666 -0.0910 0.1513  -0.1051 74   TYR C CD2 
6892  C  CE1 . TYR C  76  ? 3.3907 3.2166 3.1687 -0.0752 0.1104  -0.0907 74   TYR C CE1 
6893  C  CE2 . TYR C  76  ? 3.5176 3.2876 3.3445 -0.0892 0.1436  -0.1249 74   TYR C CE2 
6894  C  CZ  . TYR C  76  ? 3.3968 3.1960 3.2030 -0.0792 0.1265  -0.1149 74   TYR C CZ  
6895  O  OH  . TYR C  76  ? 3.3855 3.1878 3.2001 -0.0713 0.1241  -0.1280 74   TYR C OH  
6896  N  N   . TYR C  77  ? 3.1146 2.9289 2.7925 -0.0594 0.1614  -0.0483 75   TYR C N   
6897  C  CA  . TYR C  77  ? 3.2139 3.0347 2.8414 -0.0317 0.1726  -0.0201 75   TYR C CA  
6898  C  C   . TYR C  77  ? 3.3171 3.1436 2.8711 -0.0245 0.1404  -0.0426 75   TYR C C   
6899  O  O   . TYR C  77  ? 3.3477 3.1751 2.9004 -0.0439 0.1122  -0.0760 75   TYR C O   
6900  C  CB  . TYR C  77  ? 3.2683 3.0876 2.9326 -0.0275 0.2126  0.0023  75   TYR C CB  
6901  C  CG  . TYR C  77  ? 3.3594 3.1665 3.0994 -0.0325 0.2434  0.0299  75   TYR C CG  
6902  C  CD1 . TYR C  77  ? 3.3724 3.1813 3.1093 -0.0059 0.2676  0.0767  75   TYR C CD1 
6903  C  CD2 . TYR C  77  ? 3.4133 3.2043 3.2271 -0.0622 0.2463  0.0087  75   TYR C CD2 
6904  C  CE1 . TYR C  77  ? 3.3622 3.1547 3.1745 -0.0105 0.2963  0.1037  75   TYR C CE1 
6905  C  CE2 . TYR C  77  ? 3.4033 3.1733 3.2880 -0.0675 0.2704  0.0299  75   TYR C CE2 
6906  C  CZ  . TYR C  77  ? 3.3290 3.0986 3.2161 -0.0425 0.2966  0.0786  75   TYR C CZ  
6907  O  OH  . TYR C  77  ? 3.2814 3.0253 3.2451 -0.0478 0.3211  0.1015  75   TYR C OH  
6908  N  N   . ALA C  78  ? 3.3201 3.1485 2.8106 0.0068  0.1450  -0.0232 76   ALA C N   
6909  C  CA  . ALA C  78  ? 3.2494 3.0731 2.6588 0.0202  0.1114  -0.0452 76   ALA C CA  
6910  C  C   . ALA C  78  ? 3.1844 3.0033 2.5799 0.0214  0.1233  -0.0622 76   ALA C C   
6911  O  O   . ALA C  78  ? 3.2667 3.0928 2.7053 0.0214  0.1625  -0.0449 76   ALA C O   
6912  C  CB  . ALA C  78  ? 3.2499 3.0741 2.5836 0.0601  0.1073  -0.0202 76   ALA C CB  
6913  N  N   . LYS C  79  ? 3.0556 2.8626 2.3956 0.0224  0.0880  -0.0941 77   LYS C N   
6914  C  CA  . LYS C  79  ? 3.0178 2.8180 2.3366 0.0271  0.0956  -0.1121 77   LYS C CA  
6915  C  C   . LYS C  79  ? 3.2091 2.9880 2.4225 0.0644  0.0760  -0.1212 77   LYS C C   
6916  O  O   . LYS C  79  ? 3.3064 3.0691 2.4750 0.0640  0.0293  -0.1413 77   LYS C O   
6917  C  CB  . LYS C  79  ? 2.9606 2.7607 2.3190 -0.0084 0.0716  -0.1472 77   LYS C CB  
6918  C  CG  . LYS C  79  ? 2.9450 2.7611 2.3905 -0.0415 0.0787  -0.1465 77   LYS C CG  
6919  C  CD  . LYS C  79  ? 3.0122 2.8398 2.5176 -0.0458 0.1224  -0.1268 77   LYS C CD  
6920  C  CE  . LYS C  79  ? 2.9591 2.7928 2.5412 -0.0760 0.1235  -0.1345 77   LYS C CE  
6921  N  NZ  . LYS C  79  ? 2.9949 2.8336 2.6436 -0.0846 0.1580  -0.1187 77   LYS C NZ  
6922  N  N   . GLU C  80  ? 3.3013 3.0794 2.4763 0.0983  0.1104  -0.1057 78   GLU C N   
6923  C  CA  . GLU C  80  ? 3.3344 3.0869 2.3963 0.1430  0.0960  -0.1163 78   GLU C CA  
6924  C  C   . GLU C  80  ? 3.3911 3.1172 2.4255 0.1339  0.0671  -0.1598 78   GLU C C   
6925  O  O   . GLU C  80  ? 3.3970 3.1331 2.4729 0.1238  0.0925  -0.1616 78   GLU C O   
6926  C  CB  . GLU C  80  ? 3.2704 3.0360 2.3007 0.1903  0.1505  -0.0765 78   GLU C CB  
6927  C  CG  . GLU C  80  ? 3.2616 2.9986 2.1602 0.2477  0.1407  -0.0871 78   GLU C CG  
6928  C  CD  . GLU C  80  ? 3.2719 3.0298 2.1388 0.3022  0.2007  -0.0375 78   GLU C CD  
6929  O  OE1 . GLU C  80  ? 3.2762 3.0708 2.2271 0.2934  0.2453  0.0097  78   GLU C OE1 
6930  O  OE2 . GLU C  80  ? 3.2923 3.0285 2.0510 0.3561  0.2037  -0.0443 78   GLU C OE2 
6931  N  N   . VAL C  81  ? 3.3954 3.0879 2.3645 0.1373  0.0122  -0.1930 79   VAL C N   
6932  C  CA  . VAL C  81  ? 3.3693 3.0312 2.3229 0.1232  -0.0231 -0.2346 79   VAL C CA  
6933  C  C   . VAL C  81  ? 3.5521 3.1742 2.3942 0.1742  -0.0234 -0.2510 79   VAL C C   
6934  O  O   . VAL C  81  ? 3.7004 3.2986 2.4493 0.2124  -0.0428 -0.2543 79   VAL C O   
6935  C  CB  . VAL C  81  ? 3.3841 3.0310 2.3501 0.0914  -0.0868 -0.2596 79   VAL C CB  
6936  C  CG1 . VAL C  81  ? 3.3982 3.0094 2.3511 0.0790  -0.1232 -0.2987 79   VAL C CG1 
6937  C  CG2 . VAL C  81  ? 3.2536 2.9408 2.3257 0.0480  -0.0807 -0.2416 79   VAL C CG2 
6938  N  N   . THR C  82  ? 3.5430 3.1577 2.3905 0.1783  -0.0025 -0.2617 80   THR C N   
6939  C  CA  . THR C  82  ? 3.5713 3.1437 2.3152 0.2283  -0.0005 -0.2804 80   THR C CA  
6940  C  C   . THR C  82  ? 3.4149 2.9612 2.1789 0.2068  -0.0212 -0.3146 80   THR C C   
6941  O  O   . THR C  82  ? 3.2944 2.8704 2.1579 0.1601  -0.0181 -0.3123 80   THR C O   
6942  C  CB  . THR C  82  ? 3.6297 3.2293 2.3557 0.2737  0.0687  -0.2402 80   THR C CB  
6943  O  OG1 . THR C  82  ? 3.3954 3.0452 2.2387 0.2391  0.1102  -0.2135 80   THR C OG1 
6944  C  CG2 . THR C  82  ? 3.7168 3.3343 2.4027 0.3075  0.0883  -0.2047 80   THR C CG2 
6945  N  N   . ARG C  83  ? 3.4514 2.9399 2.1164 0.2448  -0.0425 -0.3466 81   ARG C N   
6946  C  CA  . ARG C  83  ? 3.3487 2.8029 2.0250 0.2294  -0.0652 -0.3796 81   ARG C CA  
6947  C  C   . ARG C  83  ? 3.4072 2.8305 2.0024 0.2861  -0.0324 -0.3851 81   ARG C C   
6948  O  O   . ARG C  83  ? 3.6385 3.0541 2.1455 0.3431  -0.0047 -0.3714 81   ARG C O   
6949  C  CB  . ARG C  83  ? 3.3558 2.7534 2.0030 0.2098  -0.1428 -0.4229 81   ARG C CB  
6950  C  CG  . ARG C  83  ? 3.6185 2.9421 2.1244 0.2638  -0.1766 -0.4574 81   ARG C CG  
6951  C  CD  . ARG C  83  ? 3.6565 2.9178 2.1496 0.2386  -0.2584 -0.5034 81   ARG C CD  
6952  N  NE  . ARG C  83  ? 3.7381 2.9174 2.0893 0.2926  -0.2951 -0.5448 81   ARG C NE  
6953  C  CZ  . ARG C  83  ? 3.7751 2.8825 2.0928 0.2819  -0.3714 -0.5918 81   ARG C CZ  
6954  N  NH1 . ARG C  83  ? 3.6022 2.7164 2.0273 0.2182  -0.4154 -0.5964 81   ARG C NH1 
6955  N  NH2 . ARG C  83  ? 3.9952 3.0231 2.1730 0.3367  -0.4046 -0.6332 81   ARG C NH2 
6956  N  N   . VAL C  84  ? 3.3117 2.7192 1.9368 0.2738  -0.0335 -0.4022 82   VAL C N   
6957  C  CA  . VAL C  84  ? 3.4460 2.8211 2.0016 0.3262  -0.0039 -0.4091 82   VAL C CA  
6958  C  C   . VAL C  84  ? 3.5051 2.8213 2.0573 0.3111  -0.0473 -0.4518 82   VAL C C   
6959  O  O   . VAL C  84  ? 3.3324 2.6745 1.9870 0.2575  -0.0599 -0.4510 82   VAL C O   
6960  C  CB  . VAL C  84  ? 3.3988 2.8430 2.0243 0.3322  0.0690  -0.3625 82   VAL C CB  
6961  C  CG1 . VAL C  84  ? 3.5517 3.0334 2.1462 0.3733  0.1189  -0.3194 82   VAL C CG1 
6962  C  CG2 . VAL C  84  ? 3.2584 2.7642 2.0258 0.2636  0.0710  -0.3462 82   VAL C CG2 
6963  N  N   . LEU C  85  ? 3.9157 3.1511 2.3492 0.3615  -0.0694 -0.4881 83   LEU C N   
6964  C  CA  . LEU C  85  ? 3.8993 3.0660 2.3229 0.3533  -0.1112 -0.5298 83   LEU C CA  
6965  C  C   . LEU C  85  ? 3.8486 3.0337 2.3071 0.3682  -0.0594 -0.5131 83   LEU C C   
6966  O  O   . LEU C  85  ? 3.9437 3.1875 2.4178 0.3929  0.0060  -0.4724 83   LEU C O   
6967  C  CB  . LEU C  85  ? 3.9701 3.0337 2.2481 0.4040  -0.1588 -0.5800 83   LEU C CB  
6968  C  CG  . LEU C  85  ? 3.9034 2.9412 2.1355 0.3937  -0.2207 -0.6019 83   LEU C CG  
6969  C  CD1 . LEU C  85  ? 4.1820 3.1187 2.2507 0.4577  -0.2609 -0.6519 83   LEU C CD1 
6970  C  CD2 . LEU C  85  ? 3.6758 2.7151 2.0135 0.3180  -0.2828 -0.6145 83   LEU C CD2 
6971  N  N   . MET C  86  ? 3.6190 2.7547 2.0959 0.3531  -0.0902 -0.5418 84   MET C N   
6972  C  CA  . MET C  86  ? 3.5251 2.6788 2.0429 0.3638  -0.0466 -0.5259 84   MET C CA  
6973  C  C   . MET C  86  ? 3.6514 2.7315 2.0438 0.4408  -0.0284 -0.5468 84   MET C C   
6974  O  O   . MET C  86  ? 3.8116 2.8315 2.0795 0.4899  -0.0450 -0.5723 84   MET C O   
6975  C  CB  . MET C  86  ? 3.5070 2.6540 2.1201 0.3094  -0.0816 -0.5374 84   MET C CB  
6976  C  CG  . MET C  86  ? 3.6165 2.6552 2.1743 0.3131  -0.1479 -0.5890 84   MET C CG  
6977  S  SD  . MET C  86  ? 3.5663 2.6037 2.2442 0.2611  -0.1711 -0.5886 84   MET C SD  
6978  C  CE  . MET C  86  ? 3.8079 2.7020 2.4055 0.2763  -0.2486 -0.6505 84   MET C CE  
6979  N  N   . VAL C  87  ? 3.7336 2.8191 2.1553 0.4556  0.0067  -0.5355 85   VAL C N   
6980  C  CA  . VAL C  87  ? 4.0327 3.0527 2.3449 0.5319  0.0324  -0.5503 85   VAL C CA  
6981  C  C   . VAL C  87  ? 4.1271 3.0408 2.4073 0.5298  -0.0241 -0.6031 85   VAL C C   
6982  O  O   . VAL C  87  ? 4.3021 3.2211 2.6819 0.4687  -0.0593 -0.6084 85   VAL C O   
6983  C  CB  . VAL C  87  ? 3.9897 3.0855 2.3565 0.5553  0.1108  -0.4988 85   VAL C CB  
6984  C  CG1 . VAL C  87  ? 4.0748 3.1071 2.3228 0.6432  0.1448  -0.5083 85   VAL C CG1 
6985  C  CG2 . VAL C  87  ? 3.8686 3.0706 2.2909 0.5463  0.1597  -0.4445 85   VAL C CG2 
6986  N  N   . GLU C  88  ? 3.9922 2.8062 2.1312 0.6000  -0.0328 -0.6415 86   GLU C N   
6987  C  CA  . GLU C  88  ? 4.0434 2.7396 2.1390 0.6060  -0.0886 -0.6965 86   GLU C CA  
6988  C  C   . GLU C  88  ? 4.0552 2.7641 2.2301 0.6002  -0.0559 -0.6771 86   GLU C C   
6989  O  O   . GLU C  88  ? 3.9305 2.7391 2.1845 0.5958  0.0085  -0.6233 86   GLU C O   
6990  C  CB  . GLU C  88  ? 4.2634 2.8480 2.1749 0.6917  -0.1021 -0.7440 86   GLU C CB  
6991  C  CG  . GLU C  88  ? 4.2807 2.8678 2.1035 0.7105  -0.1218 -0.7538 86   GLU C CG  
6992  C  CD  . GLU C  88  ? 4.5378 3.0332 2.1676 0.8097  -0.1184 -0.7906 86   GLU C CD  
6993  O  OE1 . GLU C  88  ? 4.5843 3.0013 2.1445 0.8636  -0.1064 -0.8152 86   GLU C OE1 
6994  O  OE2 . GLU C  88  ? 4.6801 3.1818 2.2241 0.8378  -0.1264 -0.7938 86   GLU C OE2 
6995  N  N   . THR C  89  ? 4.2308 2.8354 2.3867 0.6005  -0.1038 -0.7213 87   THR C N   
6996  C  CA  . THR C  89  ? 4.1748 2.7720 2.3801 0.6117  -0.0717 -0.7069 87   THR C CA  
6997  C  C   . THR C  89  ? 4.1273 2.7094 2.2323 0.7024  -0.0036 -0.6953 87   THR C C   
6998  O  O   . THR C  89  ? 4.0390 2.6207 2.1780 0.7220  0.0322  -0.6780 87   THR C O   
6999  C  CB  . THR C  89  ? 4.1682 2.6477 2.3775 0.5922  -0.1416 -0.7567 87   THR C CB  
7000  O  OG1 . THR C  89  ? 4.1797 2.5297 2.2392 0.6384  -0.1941 -0.8215 87   THR C OG1 
7001  C  CG2 . THR C  89  ? 3.9771 2.4982 2.3236 0.4992  -0.1940 -0.7481 87   THR C CG2 
7002  N  N   . HIS C  90  ? 4.0985 2.6720 2.0829 0.7608  0.0170  -0.7002 88   HIS C N   
7003  C  CA  . HIS C  90  ? 4.1357 2.7160 2.0296 0.8510  0.0915  -0.6762 88   HIS C CA  
7004  C  C   . HIS C  90  ? 4.0580 2.7935 2.0520 0.8358  0.1655  -0.5981 88   HIS C C   
7005  O  O   . HIS C  90  ? 3.9822 2.8073 2.1187 0.7574  0.1598  -0.5682 88   HIS C O   
7006  C  CB  . HIS C  90  ? 4.2317 2.7217 1.9398 0.9273  0.0747  -0.7196 88   HIS C CB  
7007  C  CG  . HIS C  90  ? 4.4776 2.8162 2.0953 0.9294  -0.0146 -0.8022 88   HIS C CG  
7008  N  ND1 . HIS C  90  ? 4.2621 2.5790 1.9347 0.8521  -0.0973 -0.8344 88   HIS C ND1 
7009  C  CD2 . HIS C  90  ? 4.8890 3.0882 2.3685 0.9998  -0.0366 -0.8591 88   HIS C CD2 
7010  C  CE1 . HIS C  90  ? 4.6675 2.8404 2.2475 0.8704  -0.1697 -0.9066 88   HIS C CE1 
7011  N  NE2 . HIS C  90  ? 4.9606 3.0630 2.4292 0.9561  -0.1359 -0.9218 88   HIS C NE2 
7012  N  N   . ASN C  91  ? 4.2303 2.9980 2.1526 0.9119  0.2346  -0.5635 89   ASN C N   
7013  C  CA  . ASN C  91  ? 4.1531 3.0626 2.1637 0.9027  0.3020  -0.4885 89   ASN C CA  
7014  C  C   . ASN C  91  ? 3.9636 2.9711 2.1446 0.8425  0.3265  -0.4431 89   ASN C C   
7015  O  O   . ASN C  91  ? 3.7587 2.8680 2.0597 0.7775  0.3303  -0.4077 89   ASN C O   
7016  C  CB  . ASN C  91  ? 3.9443 2.8986 1.9674 0.8625  0.2785  -0.4836 89   ASN C CB  
7017  C  CG  . ASN C  91  ? 4.2175 3.1078 2.0731 0.9371  0.2762  -0.5074 89   ASN C CG  
7018  O  OD1 . ASN C  91  ? 4.5524 3.4005 2.2930 1.0283  0.3180  -0.5055 89   ASN C OD1 
7019  N  ND2 . ASN C  91  ? 4.0620 2.9472 1.8999 0.9029  0.2288  -0.5279 89   ASN C ND2 
7020  N  N   . GLU C  92  ? 4.0296 3.0026 2.2164 0.8679  0.3416  -0.4459 90   GLU C N   
7021  C  CA  . GLU C  92  ? 3.8759 2.9388 2.2036 0.8329  0.3742  -0.3993 90   GLU C CA  
7022  C  C   . GLU C  92  ? 3.7608 2.8533 2.2130 0.7363  0.3212  -0.4100 90   GLU C C   
7023  O  O   . GLU C  92  ? 3.7094 2.8928 2.2861 0.6991  0.3437  -0.3691 90   GLU C O   
7024  C  CB  . GLU C  92  ? 3.8124 3.0104 2.2148 0.8424  0.4456  -0.3237 90   GLU C CB  
7025  C  CG  . GLU C  92  ? 3.9626 3.1501 2.2593 0.9431  0.5106  -0.2970 90   GLU C CG  
7026  C  CD  . GLU C  92  ? 3.8982 3.2208 2.2785 0.9466  0.5754  -0.2186 90   GLU C CD  
7027  O  OE1 . GLU C  92  ? 3.8857 3.2970 2.3914 0.8691  0.5618  -0.1952 90   GLU C OE1 
7028  O  OE2 . GLU C  92  ? 3.8376 3.1764 2.1606 1.0281  0.6398  -0.1791 90   GLU C OE2 
7029  N  N   . ILE C  93  ? 3.7968 2.8189 2.2204 0.6968  0.2511  -0.4614 91   ILE C N   
7030  C  CA  . ILE C  93  ? 3.7677 2.8089 2.3037 0.6135  0.2017  -0.4704 91   ILE C CA  
7031  C  C   . ILE C  93  ? 3.8864 2.8612 2.4401 0.6163  0.1836  -0.4895 91   ILE C C   
7032  O  O   . ILE C  93  ? 3.8209 2.8155 2.4747 0.5543  0.1502  -0.4886 91   ILE C O   
7033  C  CB  . ILE C  93  ? 3.8210 2.8177 2.3286 0.5724  0.1356  -0.5109 91   ILE C CB  
7034  C  CG1 . ILE C  93  ? 3.7514 2.7992 2.2194 0.5857  0.1585  -0.4925 91   ILE C CG1 
7035  C  CG2 . ILE C  93  ? 3.7131 2.7597 2.3502 0.4861  0.0963  -0.5047 91   ILE C CG2 
7036  C  CD1 . ILE C  93  ? 3.5958 2.7814 2.1781 0.5543  0.2082  -0.4313 91   ILE C CD1 
7037  N  N   . TYR C  94  ? 4.1090 3.0074 2.5700 0.6905  0.2087  -0.5027 92   TYR C N   
7038  C  CA  . TYR C  94  ? 4.2185 3.0362 2.6843 0.7013  0.1914  -0.5240 92   TYR C CA  
7039  C  C   . TYR C  94  ? 4.3000 3.1860 2.8330 0.7259  0.2544  -0.4728 92   TYR C C   
7040  O  O   . TYR C  94  ? 4.2824 3.1235 2.8506 0.7238  0.2435  -0.4791 92   TYR C O   
7041  C  CB  . TYR C  94  ? 4.2493 2.9099 2.5562 0.7696  0.1654  -0.5849 92   TYR C CB  
7042  C  CG  . TYR C  94  ? 4.1504 2.8002 2.3263 0.8577  0.2174  -0.5795 92   TYR C CG  
7043  C  CD1 . TYR C  94  ? 4.1513 2.8157 2.2583 0.8656  0.2108  -0.5871 92   TYR C CD1 
7044  C  CD2 . TYR C  94  ? 4.1274 2.7522 2.2470 0.9376  0.2750  -0.5634 92   TYR C CD2 
7045  C  CE1 . TYR C  94  ? 4.3206 2.9795 2.3083 0.9509  0.2619  -0.5760 92   TYR C CE1 
7046  C  CE2 . TYR C  94  ? 4.1758 2.7948 2.1756 1.0243  0.3272  -0.5526 92   TYR C CE2 
7047  C  CZ  . TYR C  94  ? 4.2333 2.8703 2.1673 1.0310  0.3207  -0.5581 92   TYR C CZ  
7048  O  OH  . TYR C  94  ? 4.1501 2.7862 1.9652 1.1218  0.3762  -0.5412 92   TYR C OH  
7049  N  N   . ASP C  95  ? 4.3015 3.2971 2.8615 0.7476  0.3185  -0.4190 93   ASP C N   
7050  C  CA  . ASP C  95  ? 4.2436 3.3121 2.8708 0.7728  0.3775  -0.3663 93   ASP C CA  
7051  C  C   . ASP C  95  ? 4.0189 3.1944 2.8036 0.6993  0.3706  -0.3305 93   ASP C C   
7052  O  O   . ASP C  95  ? 3.9301 3.1611 2.7790 0.7138  0.4085  -0.2905 93   ASP C O   
7053  C  CB  . ASP C  95  ? 4.1264 3.2764 2.7329 0.8246  0.4476  -0.3167 93   ASP C CB  
7054  C  CG  . ASP C  95  ? 4.1912 3.2438 2.6336 0.9134  0.4668  -0.3435 93   ASP C CG  
7055  O  OD1 . ASP C  95  ? 4.2638 3.1783 2.6034 0.9386  0.4246  -0.4050 93   ASP C OD1 
7056  O  OD2 . ASP C  95  ? 4.1952 3.3093 2.6119 0.9604  0.5238  -0.3017 93   ASP C OD2 
7057  N  N   . LYS C  96  ? 3.9869 3.1933 2.8313 0.6258  0.3241  -0.3426 94   LYS C N   
7058  C  CA  . LYS C  96  ? 3.9522 3.2722 2.9361 0.5613  0.3215  -0.3065 94   LYS C CA  
7059  C  C   . LYS C  96  ? 4.1111 3.3948 3.1486 0.5061  0.2649  -0.3307 94   LYS C C   
7060  O  O   . LYS C  96  ? 4.0519 3.3981 3.1860 0.4794  0.2697  -0.3016 94   LYS C O   
7061  C  CB  . LYS C  96  ? 3.8324 3.2517 2.8610 0.5230  0.3280  -0.2846 94   LYS C CB  
7062  C  CG  . LYS C  96  ? 3.7835 3.2644 2.7937 0.5689  0.3880  -0.2452 94   LYS C CG  
7063  C  CD  . LYS C  96  ? 3.6941 3.2737 2.7961 0.5773  0.4327  -0.1909 94   LYS C CD  
7064  C  CE  . LYS C  96  ? 3.6096 3.2843 2.7403 0.5969  0.4836  -0.1414 94   LYS C CE  
7065  N  NZ  . LYS C  96  ? 3.6827 3.2945 2.6945 0.6681  0.5155  -0.1464 94   LYS C NZ  
7066  N  N   . PHE C  97  ? 4.2924 3.4814 3.2743 0.4893  0.2110  -0.3793 95   PHE C N   
7067  C  CA  . PHE C  97  ? 4.3108 3.4862 3.3637 0.4289  0.1579  -0.3921 95   PHE C CA  
7068  C  C   . PHE C  97  ? 4.4860 3.5204 3.4871 0.4433  0.1136  -0.4365 95   PHE C C   
7069  O  O   . PHE C  97  ? 4.7132 3.7042 3.7155 0.4754  0.1289  -0.4319 95   PHE C O   
7070  C  CB  . PHE C  97  ? 4.3067 3.5209 3.3792 0.3764  0.1253  -0.4011 95   PHE C CB  
7071  C  CG  . PHE C  97  ? 4.3600 3.6854 3.4579 0.3705  0.1648  -0.3681 95   PHE C CG  
7072  C  CD1 . PHE C  97  ? 4.1468 3.5888 3.3529 0.3335  0.1823  -0.3281 95   PHE C CD1 
7073  C  CD2 . PHE C  97  ? 4.4487 3.7608 3.4631 0.4044  0.1836  -0.3758 95   PHE C CD2 
7074  C  CE1 . PHE C  97  ? 3.9963 3.5340 3.2329 0.3254  0.2131  -0.2999 95   PHE C CE1 
7075  C  CE2 . PHE C  97  ? 4.3260 3.7390 3.3766 0.3972  0.2200  -0.3409 95   PHE C CE2 
7076  C  CZ  . PHE C  97  ? 4.0941 3.6174 3.2590 0.3553  0.2325  -0.3044 95   PHE C CZ  
7077  N  N   . LYS C  98  ? 4.4929 3.4592 3.4576 0.4166  0.0563  -0.4776 96   LYS C N   
7078  C  CA  . LYS C  98  ? 4.6811 3.5011 3.5810 0.4295  0.0023  -0.5299 96   LYS C CA  
7079  C  C   . LYS C  98  ? 4.7017 3.4920 3.7001 0.3848  -0.0389 -0.5266 96   LYS C C   
7080  O  O   . LYS C  98  ? 4.6870 3.4166 3.6952 0.3480  -0.1018 -0.5559 96   LYS C O   
7081  C  CB  . LYS C  98  ? 4.8154 3.5421 3.6016 0.5099  0.0298  -0.5526 96   LYS C CB  
7082  C  CG  . LYS C  98  ? 4.8846 3.4489 3.6067 0.5264  -0.0283 -0.6100 96   LYS C CG  
7083  C  CD  . LYS C  98  ? 4.9391 3.4124 3.5585 0.6101  0.0052  -0.6281 96   LYS C CD  
7084  C  CE  . LYS C  98  ? 5.0681 3.3752 3.6433 0.6208  -0.0565 -0.6849 96   LYS C CE  
7085  N  NZ  . LYS C  98  ? 5.2622 3.4684 3.7321 0.7068  -0.0250 -0.7064 96   LYS C NZ  
7086  N  N   . GLN C  99  ? 4.7158 3.5515 3.7931 0.3877  -0.0050 -0.4871 97   GLN C N   
7087  C  CA  . GLN C  99  ? 4.7447 3.5227 3.8953 0.3661  -0.0378 -0.4853 97   GLN C CA  
7088  C  C   . GLN C  99  ? 4.6429 3.5274 3.9356 0.3056  -0.0418 -0.4373 97   GLN C C   
7089  O  O   . GLN C  99  ? 4.6763 3.5346 4.0461 0.2910  -0.0567 -0.4205 97   GLN C O   
7090  C  CB  . GLN C  99  ? 4.7591 3.4881 3.8916 0.4213  -0.0006 -0.4766 97   GLN C CB  
7091  C  CG  . GLN C  99  ? 4.8768 3.5498 3.8746 0.4962  0.0348  -0.5021 97   GLN C CG  
7092  C  CD  . GLN C  99  ? 4.7883 3.5875 3.8007 0.5243  0.1099  -0.4519 97   GLN C CD  
7093  O  OE1 . GLN C  99  ? 4.8024 3.7300 3.9188 0.4845  0.1296  -0.4047 97   GLN C OE1 
7094  N  NE2 . GLN C  99  ? 4.7465 3.5104 3.6556 0.5950  0.1510  -0.4610 97   GLN C NE2 
7095  N  N   . SER C  100 ? 4.3568 3.3586 3.6861 0.2735  -0.0279 -0.4132 98   SER C N   
7096  C  CA  . SER C  100 ? 4.1553 3.2475 3.6058 0.2197  -0.0379 -0.3737 98   SER C CA  
7097  C  C   . SER C  100 ? 4.2167 3.2498 3.6838 0.1768  -0.1030 -0.3991 98   SER C C   
7098  O  O   . SER C  100 ? 4.1586 3.2200 3.6056 0.1527  -0.1208 -0.4118 98   SER C O   
7099  C  CB  . SER C  100 ? 3.9851 3.2175 3.4665 0.2045  -0.0009 -0.3415 98   SER C CB  
7100  O  OG  . SER C  100 ? 3.9635 3.1986 3.3838 0.1961  -0.0122 -0.3675 98   SER C OG  
7101  N  N   . THR C  101 ? 4.3169 3.2654 3.8269 0.1674  -0.1398 -0.4044 99   THR C N   
7102  C  CA  . THR C  101 ? 4.3031 3.1791 3.8317 0.1293  -0.2087 -0.4305 99   THR C CA  
7103  C  C   . THR C  101 ? 4.1588 3.1358 3.7746 0.0757  -0.2216 -0.3979 99   THR C C   
7104  O  O   . THR C  101 ? 4.1435 3.0817 3.7683 0.0433  -0.2752 -0.4173 99   THR C O   
7105  C  CB  . THR C  101 ? 4.2877 3.0659 3.8738 0.1246  -0.2433 -0.4313 99   THR C CB  
7106  O  OG1 . THR C  101 ? 4.1586 3.0237 3.8722 0.1036  -0.2182 -0.3683 99   THR C OG1 
7107  C  CG2 . THR C  101 ? 4.3456 3.0171 3.8416 0.1832  -0.2281 -0.4645 99   THR C CG2 
7108  N  N   . HIS C  102 ? 4.0212 3.1262 3.6988 0.0681  -0.1752 -0.3494 100  HIS C N   
7109  C  CA  . HIS C  102 ? 3.9465 3.1512 3.7003 0.0254  -0.1806 -0.3168 100  HIS C CA  
7110  C  C   . HIS C  102 ? 3.8296 3.1081 3.5287 0.0255  -0.1573 -0.3254 100  HIS C C   
7111  O  O   . HIS C  102 ? 3.6992 3.0821 3.4528 0.0039  -0.1401 -0.2934 100  HIS C O   
7112  C  CB  . HIS C  102 ? 3.9398 3.2354 3.7991 0.0182  -0.1499 -0.2574 100  HIS C CB  
7113  C  CG  . HIS C  102 ? 4.0660 3.2979 3.9961 0.0164  -0.1689 -0.2388 100  HIS C CG  
7114  N  ND1 . HIS C  102 ? 4.0551 3.2780 4.0814 -0.0214 -0.2081 -0.2142 100  HIS C ND1 
7115  C  CD2 . HIS C  102 ? 4.1274 3.3011 4.0524 0.0483  -0.1533 -0.2376 100  HIS C CD2 
7116  C  CE1 . HIS C  102 ? 4.1122 3.2727 4.1942 -0.0150 -0.2171 -0.1983 100  HIS C CE1 
7117  N  NE2 . HIS C  102 ? 4.1697 3.2966 4.1885 0.0278  -0.1842 -0.2138 100  HIS C NE2 
7118  N  N   . SER C  103 ? 3.9908 3.2154 3.5826 0.0522  -0.1557 -0.3671 101  SER C N   
7119  C  CA  . SER C  103 ? 3.9164 3.2064 3.4610 0.0541  -0.1315 -0.3718 101  SER C CA  
7120  C  C   . SER C  103 ? 4.0160 3.2199 3.4476 0.0771  -0.1509 -0.4199 101  SER C C   
7121  O  O   . SER C  103 ? 4.1587 3.2553 3.5333 0.1025  -0.1733 -0.4520 101  SER C O   
7122  C  CB  . SER C  103 ? 3.8602 3.2352 3.4075 0.0790  -0.0716 -0.3457 101  SER C CB  
7123  O  OG  . SER C  103 ? 3.7680 3.2226 3.4106 0.0631  -0.0557 -0.3026 101  SER C OG  
7124  N  N   . ILE C  104 ? 3.8774 3.1277 3.2743 0.0709  -0.1423 -0.4246 102  ILE C N   
7125  C  CA  . ILE C  104 ? 3.8977 3.0849 3.1850 0.0963  -0.1541 -0.4631 102  ILE C CA  
7126  C  C   . ILE C  104 ? 3.8351 3.0995 3.0916 0.1137  -0.1031 -0.4483 102  ILE C C   
7127  O  O   . ILE C  104 ? 3.6658 3.0233 2.9841 0.0841  -0.0877 -0.4215 102  ILE C O   
7128  C  CB  . ILE C  104 ? 3.8135 2.9637 3.0969 0.0639  -0.2124 -0.4845 102  ILE C CB  
7129  C  CG1 . ILE C  104 ? 3.9284 2.9698 3.2132 0.0583  -0.2701 -0.5117 102  ILE C CG1 
7130  C  CG2 . ILE C  104 ? 3.8418 2.9750 3.0249 0.0861  -0.2112 -0.5096 102  ILE C CG2 
7131  C  CD1 . ILE C  104 ? 3.9336 2.9341 3.2183 0.0267  -0.3351 -0.5333 102  ILE C CD1 
7132  N  N   . TYR C  105 ? 4.0090 3.2336 3.1719 0.1635  -0.0771 -0.4644 103  TYR C N   
7133  C  CA  . TYR C  105 ? 3.9785 3.2735 3.1192 0.1845  -0.0254 -0.4443 103  TYR C CA  
7134  C  C   . TYR C  105 ? 4.0188 3.2758 3.0650 0.2053  -0.0338 -0.4678 103  TYR C C   
7135  O  O   . TYR C  105 ? 4.1934 3.3517 3.1487 0.2357  -0.0614 -0.5045 103  TYR C O   
7136  C  CB  . TYR C  105 ? 4.0436 3.3439 3.1637 0.2318  0.0241  -0.4292 103  TYR C CB  
7137  C  CG  . TYR C  105 ? 4.0157 3.3404 3.2168 0.2201  0.0305  -0.4078 103  TYR C CG  
7138  C  CD1 . TYR C  105 ? 3.8712 3.3070 3.1654 0.1939  0.0567  -0.3687 103  TYR C CD1 
7139  C  CD2 . TYR C  105 ? 4.0916 3.3262 3.2757 0.2366  0.0082  -0.4267 103  TYR C CD2 
7140  C  CE1 . TYR C  105 ? 3.8782 3.3415 3.2426 0.1873  0.0632  -0.3460 103  TYR C CE1 
7141  C  CE2 . TYR C  105 ? 4.0512 3.3100 3.3128 0.2281  0.0167  -0.4019 103  TYR C CE2 
7142  C  CZ  . TYR C  105 ? 3.9936 3.3704 3.3439 0.2048  0.0455  -0.3599 103  TYR C CZ  
7143  O  OH  . TYR C  105 ? 4.0411 3.4470 3.4650 0.2005  0.0547  -0.3322 103  TYR C OH  
7144  N  N   . MET C  106 ? 3.9101 3.2439 2.9762 0.1913  -0.0106 -0.4466 104  MET C N   
7145  C  CA  . MET C  106 ? 3.8811 3.1952 2.8699 0.2089  -0.0137 -0.4594 104  MET C CA  
7146  C  C   . MET C  106 ? 3.7759 3.1609 2.7625 0.2338  0.0465  -0.4265 104  MET C C   
7147  O  O   . MET C  106 ? 3.6364 3.1091 2.7112 0.2083  0.0743  -0.3940 104  MET C O   
7148  C  CB  . MET C  106 ? 3.8301 3.1628 2.8571 0.1601  -0.0539 -0.4637 104  MET C CB  
7149  C  CG  . MET C  106 ? 3.8941 3.1712 2.9480 0.1290  -0.1140 -0.4864 104  MET C CG  
7150  S  SD  . MET C  106 ? 3.9935 3.3206 3.1247 0.0690  -0.1502 -0.4755 104  MET C SD  
7151  C  CE  . MET C  106 ? 3.8741 3.3195 3.1128 0.0419  -0.1030 -0.4320 104  MET C CE  
7152  N  N   . PHE C  107 ? 4.0013 3.3488 2.8885 0.2848  0.0652  -0.4334 105  PHE C N   
7153  C  CA  . PHE C  107 ? 4.1006 3.5106 2.9855 0.3164  0.1260  -0.3960 105  PHE C CA  
7154  C  C   . PHE C  107 ? 4.1865 3.5867 3.0004 0.3384  0.1299  -0.3963 105  PHE C C   
7155  O  O   . PHE C  107 ? 4.2821 3.6050 3.0068 0.3547  0.0909  -0.4325 105  PHE C O   
7156  C  CB  . PHE C  107 ? 4.2379 3.6235 3.0740 0.3768  0.1665  -0.3881 105  PHE C CB  
7157  C  CG  . PHE C  107 ? 4.1110 3.5529 3.0416 0.3597  0.1887  -0.3627 105  PHE C CG  
7158  C  CD1 . PHE C  107 ? 3.9857 3.3950 2.9524 0.3334  0.1539  -0.3824 105  PHE C CD1 
7159  C  CD2 . PHE C  107 ? 4.0891 3.6195 3.0771 0.3708  0.2436  -0.3155 105  PHE C CD2 
7160  C  CE1 . PHE C  107 ? 3.9034 3.3688 2.9535 0.3216  0.1752  -0.3561 105  PHE C CE1 
7161  C  CE2 . PHE C  107 ? 4.0503 3.6369 3.1237 0.3564  0.2605  -0.2918 105  PHE C CE2 
7162  C  CZ  . PHE C  107 ? 3.9732 3.5277 3.0733 0.3335  0.2271  -0.3125 105  PHE C CZ  
7163  N  N   . PHE C  108 ? 4.1370 3.6171 2.9950 0.3389  0.1756  -0.3540 106  PHE C N   
7164  C  CA  . PHE C  108 ? 4.0555 3.5412 2.8622 0.3600  0.1885  -0.3422 106  PHE C CA  
7165  C  C   . PHE C  108 ? 3.9849 3.5286 2.7992 0.4027  0.2574  -0.2923 106  PHE C C   
7166  O  O   . PHE C  108 ? 3.9650 3.5591 2.8462 0.4028  0.2915  -0.2643 106  PHE C O   
7167  C  CB  . PHE C  108 ? 3.8473 3.3773 2.7264 0.3007  0.1650  -0.3363 106  PHE C CB  
7168  C  CG  . PHE C  108 ? 3.8516 3.3356 2.7329 0.2596  0.1002  -0.3760 106  PHE C CG  
7169  C  CD1 . PHE C  108 ? 3.9759 3.3990 2.7746 0.2708  0.0604  -0.4046 106  PHE C CD1 
7170  C  CD2 . PHE C  108 ? 3.7870 3.2938 2.7570 0.2111  0.0790  -0.3807 106  PHE C CD2 
7171  C  CE1 . PHE C  108 ? 4.0269 3.4138 2.8409 0.2310  -0.0005 -0.4352 106  PHE C CE1 
7172  C  CE2 . PHE C  108 ? 3.8761 3.3475 2.8589 0.1748  0.0232  -0.4084 106  PHE C CE2 
7173  C  CZ  . PHE C  108 ? 4.0129 3.4250 2.9228 0.1828  -0.0173 -0.4348 106  PHE C CZ  
7174  N  N   . GLN C  109 ? 3.8054 3.3465 2.5556 0.4398  0.2780  -0.2767 107  GLN C N   
7175  C  CA  . GLN C  109 ? 3.6584 3.2563 2.4165 0.4847  0.3457  -0.2214 107  GLN C CA  
7176  C  C   . GLN C  109 ? 3.6840 3.3575 2.5343 0.4455  0.3617  -0.1818 107  GLN C C   
7177  O  O   . GLN C  109 ? 3.7563 3.4118 2.5847 0.4260  0.3320  -0.1968 107  GLN C O   
7178  C  CB  . GLN C  109 ? 3.6821 3.2212 2.2914 0.5692  0.3657  -0.2258 107  GLN C CB  
7179  C  CG  . GLN C  109 ? 3.7963 3.2554 2.3075 0.6198  0.3579  -0.2624 107  GLN C CG  
7180  C  CD  . GLN C  109 ? 4.0398 3.4375 2.3912 0.7110  0.3777  -0.2698 107  GLN C CD  
7181  O  OE1 . GLN C  109 ? 4.1549 3.5667 2.4614 0.7349  0.3908  -0.2508 107  GLN C OE1 
7182  N  NE2 . GLN C  109 ? 4.1379 3.4653 2.3987 0.7661  0.3805  -0.2972 107  GLN C NE2 
7183  N  N   . THR C  110 ? 3.6520 3.4087 2.6087 0.4343  0.4068  -0.1305 108  THR C N   
7184  C  CA  . THR C  110 ? 3.6059 3.4309 2.6610 0.3966  0.4223  -0.0916 108  THR C CA  
7185  C  C   . THR C  110 ? 3.6766 3.5097 2.6801 0.4478  0.4632  -0.0516 108  THR C C   
7186  O  O   . THR C  110 ? 3.4969 3.3624 2.5548 0.4201  0.4658  -0.0289 108  THR C O   
7187  C  CB  . THR C  110 ? 3.5371 3.4468 2.7300 0.3655  0.4505  -0.0508 108  THR C CB  
7188  O  OG1 . THR C  110 ? 3.5900 3.4921 2.8091 0.3389  0.4226  -0.0821 108  THR C OG1 
7189  C  CG2 . THR C  110 ? 3.3984 3.3624 2.7054 0.3057  0.4430  -0.0312 108  THR C CG2 
7190  N  N   . SER C  111 ? 4.0562 3.8595 2.9536 0.5258  0.4968  -0.0410 109  SER C N   
7191  C  CA  . SER C  111 ? 4.1349 3.9491 2.9734 0.5849  0.5405  0.0018  109  SER C CA  
7192  C  C   . SER C  111 ? 4.0197 3.7861 2.7803 0.5812  0.5016  -0.0288 109  SER C C   
7193  O  O   . SER C  111 ? 4.0592 3.8516 2.8076 0.6090  0.5328  0.0129  109  SER C O   
7194  C  CB  . SER C  111 ? 4.1494 3.9330 2.8705 0.6776  0.5816  0.0124  109  SER C CB  
7195  O  OG  . SER C  111 ? 3.9627 3.7986 2.7609 0.6861  0.6233  0.0495  109  SER C OG  
7196  N  N   . GLU C  112 ? 3.7406 3.4422 2.4553 0.5479  0.4348  -0.0956 110  GLU C N   
7197  C  CA  . GLU C  112 ? 3.7186 3.3807 2.3737 0.5369  0.3912  -0.1243 110  GLU C CA  
7198  C  C   . GLU C  112 ? 3.6759 3.3698 2.4464 0.4533  0.3577  -0.1301 110  GLU C C   
7199  O  O   . GLU C  112 ? 3.7002 3.3857 2.4520 0.4422  0.3361  -0.1337 110  GLU C O   
7200  C  CB  . GLU C  112 ? 3.7686 3.3338 2.2934 0.5588  0.3343  -0.1931 110  GLU C CB  
7201  C  CG  . GLU C  112 ? 3.9175 3.4355 2.3156 0.6443  0.3611  -0.1991 110  GLU C CG  
7202  C  CD  . GLU C  112 ? 4.0428 3.4553 2.3164 0.6625  0.2975  -0.2724 110  GLU C CD  
7203  O  OE1 . GLU C  112 ? 3.8298 3.2126 2.1207 0.6079  0.2331  -0.3128 110  GLU C OE1 
7204  O  OE2 . GLU C  112 ? 4.2960 3.6544 2.4576 0.7323  0.3115  -0.2885 110  GLU C OE2 
7205  N  N   . LEU C  113 ? 3.5293 3.2600 2.4140 0.3988  0.3535  -0.1306 111  LEU C N   
7206  C  CA  . LEU C  113 ? 3.4868 3.2464 2.4750 0.3254  0.3239  -0.1373 111  LEU C CA  
7207  C  C   . LEU C  113 ? 3.4998 3.3204 2.5714 0.3133  0.3617  -0.0840 111  LEU C C   
7208  O  O   . LEU C  113 ? 3.5202 3.3410 2.6125 0.2850  0.3421  -0.0860 111  LEU C O   
7209  C  CB  . LEU C  113 ? 3.4443 3.2267 2.5206 0.2786  0.3096  -0.1526 111  LEU C CB  
7210  C  CG  . LEU C  113 ? 3.5180 3.2400 2.5402 0.2699  0.2597  -0.2074 111  LEU C CG  
7211  C  CD1 . LEU C  113 ? 3.5976 3.3530 2.7116 0.2288  0.2533  -0.2128 111  LEU C CD1 
7212  C  CD2 . LEU C  113 ? 3.4815 3.1659 2.4760 0.2415  0.2074  -0.2402 111  LEU C CD2 
7213  N  N   . ARG C  114 ? 3.4917 3.3651 2.6194 0.3343  0.4160  -0.0329 112  ARG C N   
7214  C  CA  . ARG C  114 ? 3.5115 3.4430 2.7323 0.3232  0.4540  0.0240  112  ARG C CA  
7215  C  C   . ARG C  114 ? 3.6013 3.5234 2.7450 0.3781  0.4829  0.0569  112  ARG C C   
7216  O  O   . ARG C  114 ? 3.7457 3.7169 2.9620 0.3821  0.5249  0.1157  112  ARG C O   
7217  C  CB  . ARG C  114 ? 3.5594 3.5560 2.8810 0.3243  0.4994  0.0724  112  ARG C CB  
7218  C  CG  . ARG C  114 ? 3.4055 3.4260 2.8241 0.2639  0.4708  0.0475  112  ARG C CG  
7219  C  CD  . ARG C  114 ? 3.4029 3.4973 2.9397 0.2582  0.5109  0.1007  112  ARG C CD  
7220  N  NE  . ARG C  114 ? 3.4830 3.5848 2.9716 0.3153  0.5470  0.1211  112  ARG C NE  
7221  C  CZ  . ARG C  114 ? 3.3867 3.5546 2.9654 0.3235  0.5869  0.1731  112  ARG C CZ  
7222  N  NH1 . ARG C  114 ? 3.2953 3.5256 3.0205 0.2745  0.5908  0.2076  112  ARG C NH1 
7223  N  NH2 . ARG C  114 ? 3.3392 3.5097 2.8636 0.3816  0.6213  0.1909  112  ARG C NH2 
7224  N  N   . GLU C  115 ? 3.5377 3.3982 2.5388 0.4210  0.4596  0.0216  113  GLU C N   
7225  C  CA  . GLU C  115 ? 3.6032 3.4508 2.5176 0.4723  0.4761  0.0447  113  GLU C CA  
7226  C  C   . GLU C  115 ? 3.5915 3.4092 2.4871 0.4376  0.4254  0.0123  113  GLU C C   
7227  O  O   . GLU C  115 ? 3.7093 3.5448 2.6062 0.4509  0.4432  0.0477  113  GLU C O   
7228  C  CB  . GLU C  115 ? 3.7138 3.5121 2.4685 0.5537  0.4836  0.0282  113  GLU C CB  
7229  C  CG  . GLU C  115 ? 3.9433 3.7474 2.6093 0.6271  0.5228  0.0714  113  GLU C CG  
7230  C  CD  . GLU C  115 ? 4.0860 3.8349 2.5816 0.7132  0.5274  0.0486  113  GLU C CD  
7231  O  OE1 . GLU C  115 ? 4.1923 3.8915 2.6420 0.7111  0.4959  -0.0043 113  GLU C OE1 
7232  O  OE2 . GLU C  115 ? 4.0353 3.7883 2.4403 0.7859  0.5627  0.0837  113  GLU C OE2 
7233  N  N   . ALA C  116 ? 3.2743 3.0506 2.1586 0.3947  0.3645  -0.0490 114  ALA C N   
7234  C  CA  . ALA C  116 ? 3.2193 2.9765 2.1056 0.3568  0.3171  -0.0744 114  ALA C CA  
7235  C  C   . ALA C  116 ? 3.1952 3.0007 2.2225 0.2964  0.3260  -0.0496 114  ALA C C   
7236  O  O   . ALA C  116 ? 3.2233 3.0342 2.2668 0.2838  0.3190  -0.0369 114  ALA C O   
7237  C  CB  . ALA C  116 ? 3.2063 2.9090 2.0479 0.3310  0.2516  -0.1404 114  ALA C CB  
7238  N  N   . VAL C  117 ? 3.2812 3.1202 2.4092 0.2609  0.3397  -0.0436 115  VAL C N   
7239  C  CA  . VAL C  117 ? 3.3959 3.2759 2.6563 0.2060  0.3460  -0.0245 115  VAL C CA  
7240  C  C   . VAL C  117 ? 3.5107 3.4438 2.8585 0.2119  0.3983  0.0260  115  VAL C C   
7241  O  O   . VAL C  117 ? 3.6118 3.5622 3.0019 0.1970  0.3991  0.0170  115  VAL C O   
7242  C  CB  . VAL C  117 ? 3.3307 3.2013 2.6385 0.1483  0.2988  -0.0722 115  VAL C CB  
7243  C  CG1 . VAL C  117 ? 3.2801 3.1833 2.7075 0.0975  0.3007  -0.0590 115  VAL C CG1 
7244  C  CG2 . VAL C  117 ? 3.2995 3.1211 2.5261 0.1455  0.2473  -0.1167 115  VAL C CG2 
7245  N  N   . PRO C  118 ? 3.5195 3.4831 2.9029 0.2337  0.4429  0.0841  116  PRO C N   
7246  C  CA  . PRO C  118 ? 3.4242 3.4434 2.9032 0.2399  0.4934  0.1406  116  PRO C CA  
7247  C  C   . PRO C  118 ? 3.3868 3.4379 3.0061 0.1737  0.4794  0.1352  116  PRO C C   
7248  O  O   . PRO C  118 ? 3.2283 3.3093 2.8965 0.1670  0.4886  0.1405  116  PRO C O   
7249  C  CB  . PRO C  118 ? 3.4474 3.4878 2.9430 0.2701  0.5366  0.2034  116  PRO C CB  
7250  C  CG  . PRO C  118 ? 3.5639 3.5573 2.9243 0.3061  0.5160  0.1790  116  PRO C CG  
7251  C  CD  . PRO C  118 ? 3.5182 3.4689 2.8518 0.2604  0.4507  0.1059  116  PRO C CD  
7252  N  N   . GLU C  119 ? 3.6755 3.7199 3.3574 0.1274  0.4561  0.1242  117  GLU C N   
7253  C  CA  . GLU C  119 ? 3.7646 3.8339 3.5737 0.0679  0.4397  0.1161  117  GLU C CA  
7254  C  C   . GLU C  119 ? 3.7296 3.7706 3.5139 0.0304  0.3851  0.0478  117  GLU C C   
7255  O  O   . GLU C  119 ? 3.7403 3.7418 3.4542 0.0301  0.3569  0.0151  117  GLU C O   
7256  C  CB  . GLU C  119 ? 3.8655 3.9415 3.7663 0.0417  0.4493  0.1467  117  GLU C CB  
7257  C  CG  . GLU C  119 ? 3.8075 3.9068 3.8449 -0.0151 0.4339  0.1429  117  GLU C CG  
7258  C  CD  . GLU C  119 ? 3.8275 3.9288 3.9626 -0.0360 0.4483  0.1799  117  GLU C CD  
7259  O  OE1 . GLU C  119 ? 3.9120 4.0024 4.0111 -0.0043 0.4752  0.2145  117  GLU C OE1 
7260  O  OE2 . GLU C  119 ? 3.7842 3.8960 4.0319 -0.0831 0.4308  0.1739  117  GLU C OE2 
7261  N  N   . PRO C  120 ? 3.6425 3.7069 3.4855 0.0005  0.3696  0.0289  118  PRO C N   
7262  C  CA  . PRO C  120 ? 3.6899 3.7331 3.5097 -0.0302 0.3215  -0.0305 118  PRO C CA  
7263  C  C   . PRO C  120 ? 3.6189 3.6413 3.4682 -0.0674 0.2918  -0.0558 118  PRO C C   
7264  O  O   . PRO C  120 ? 3.5163 3.5163 3.3261 -0.0821 0.2558  -0.0995 118  PRO C O   
7265  C  CB  . PRO C  120 ? 3.6036 3.6884 3.4974 -0.0514 0.3186  -0.0321 118  PRO C CB  
7266  C  CG  . PRO C  120 ? 3.5322 3.6526 3.4492 -0.0174 0.3658  0.0222  118  PRO C CG  
7267  C  CD  . PRO C  120 ? 3.5187 3.6348 3.4462 -0.0003 0.3965  0.0652  118  PRO C CD  
7268  N  N   . VAL C  121 ? 3.5669 3.5959 3.4883 -0.0812 0.3073  -0.0269 119  VAL C N   
7269  C  CA  . VAL C  121 ? 3.4260 3.4301 3.3732 -0.1118 0.2821  -0.0504 119  VAL C CA  
7270  C  C   . VAL C  121 ? 3.2931 3.2612 3.1515 -0.0898 0.2758  -0.0575 119  VAL C C   
7271  O  O   . VAL C  121 ? 3.2921 3.2372 3.1369 -0.1080 0.2465  -0.0892 119  VAL C O   
7272  C  CB  . VAL C  121 ? 3.5650 3.5810 3.6231 -0.1335 0.2995  -0.0171 119  VAL C CB  
7273  C  CG1 . VAL C  121 ? 3.6591 3.6468 3.7514 -0.1681 0.2684  -0.0513 119  VAL C CG1 
7274  C  CG2 . VAL C  121 ? 3.5198 3.5796 3.6693 -0.1487 0.3098  0.0035  119  VAL C CG2 
7275  N  N   . LEU C  122 ? 3.1479 3.1129 2.9434 -0.0477 0.3022  -0.0269 120  LEU C N   
7276  C  CA  . LEU C  122 ? 3.1651 3.0989 2.8721 -0.0243 0.2916  -0.0333 120  LEU C CA  
7277  C  C   . LEU C  122 ? 3.1196 3.0299 2.7553 -0.0293 0.2492  -0.0829 120  LEU C C   
7278  O  O   . LEU C  122 ? 3.1253 3.0120 2.7163 -0.0279 0.2265  -0.0967 120  LEU C O   
7279  C  CB  . LEU C  122 ? 3.2696 3.2060 2.9114 0.0281  0.3259  0.0059  120  LEU C CB  
7280  C  CG  . LEU C  122 ? 3.4136 3.3798 3.1255 0.0419  0.3756  0.0680  120  LEU C CG  
7281  C  CD1 . LEU C  122 ? 3.5567 3.5283 3.1859 0.1040  0.4110  0.1058  120  LEU C CD1 
7282  C  CD2 . LEU C  122 ? 3.3838 3.3425 3.1585 0.0207  0.3784  0.0858  120  LEU C CD2 
7283  N  N   . LEU C  123 ? 2.9912 2.9100 2.6225 -0.0350 0.2385  -0.1055 121  LEU C N   
7284  C  CA  . LEU C  123 ? 2.9451 2.8423 2.5190 -0.0396 0.2001  -0.1470 121  LEU C CA  
7285  C  C   . LEU C  123 ? 3.0375 2.9318 2.6507 -0.0761 0.1701  -0.1723 121  LEU C C   
7286  O  O   . LEU C  123 ? 3.1008 3.0146 2.7880 -0.1039 0.1711  -0.1768 121  LEU C O   
7287  C  CB  . LEU C  123 ? 2.9012 2.8113 2.4741 -0.0372 0.2001  -0.1598 121  LEU C CB  
7288  C  CG  . LEU C  123 ? 2.8634 2.7449 2.3609 -0.0250 0.1711  -0.1914 121  LEU C CG  
7289  C  CD1 . LEU C  123 ? 2.8007 2.6796 2.3212 -0.0588 0.1332  -0.2232 121  LEU C CD1 
7290  C  CD2 . LEU C  123 ? 2.9262 2.7694 2.3297 0.0092  0.1639  -0.1910 121  LEU C CD2 
7291  N  N   . SER C  124 ? 3.0998 2.9701 2.6629 -0.0737 0.1422  -0.1882 122  SER C N   
7292  C  CA  . SER C  124 ? 3.1157 2.9853 2.7089 -0.1007 0.1167  -0.2070 122  SER C CA  
7293  C  C   . SER C  124 ? 3.1168 2.9822 2.6866 -0.1092 0.0834  -0.2357 122  SER C C   
7294  O  O   . SER C  124 ? 3.1312 3.0137 2.7433 -0.1305 0.0737  -0.2515 122  SER C O   
7295  C  CB  . SER C  124 ? 3.1407 2.9950 2.7152 -0.0933 0.1128  -0.1930 122  SER C CB  
7296  O  OG  . SER C  124 ? 3.1913 3.0255 2.6888 -0.0701 0.0950  -0.1943 122  SER C OG  
7297  N  N   . ARG C  125 ? 3.1273 2.9694 2.6314 -0.0918 0.0642  -0.2423 123  ARG C N   
7298  C  CA  . ARG C  125 ? 2.9725 2.8069 2.4625 -0.1005 0.0312  -0.2651 123  ARG C CA  
7299  C  C   . ARG C  125 ? 3.0799 2.8876 2.5058 -0.0763 0.0258  -0.2736 123  ARG C C   
7300  O  O   . ARG C  125 ? 3.1437 2.9265 2.5085 -0.0500 0.0267  -0.2674 123  ARG C O   
7301  C  CB  . ARG C  125 ? 2.7572 2.5830 2.2428 -0.1097 -0.0003 -0.2672 123  ARG C CB  
7302  C  CG  . ARG C  125 ? 2.6718 2.4940 2.1610 -0.1219 -0.0347 -0.2831 123  ARG C CG  
7303  C  CD  . ARG C  125 ? 2.6772 2.5006 2.1784 -0.1320 -0.0634 -0.2765 123  ARG C CD  
7304  N  NE  . ARG C  125 ? 2.7210 2.5443 2.2388 -0.1445 -0.0956 -0.2842 123  ARG C NE  
7305  C  CZ  . ARG C  125 ? 2.5946 2.4487 2.1672 -0.1600 -0.0962 -0.2803 123  ARG C CZ  
7306  N  NH1 . ARG C  125 ? 2.5784 2.4602 2.1854 -0.1640 -0.0702 -0.2757 123  ARG C NH1 
7307  N  NH2 . ARG C  125 ? 2.5761 2.4317 2.1690 -0.1693 -0.1234 -0.2802 123  ARG C NH2 
7308  N  N   . ALA C  126 ? 3.0058 2.8172 2.4416 -0.0811 0.0207  -0.2876 124  ALA C N   
7309  C  CA  . ALA C  126 ? 2.9286 2.7095 2.3058 -0.0565 0.0166  -0.2985 124  ALA C CA  
7310  C  C   . ALA C  126 ? 3.0314 2.8018 2.4197 -0.0716 -0.0160 -0.3180 124  ALA C C   
7311  O  O   . ALA C  126 ? 3.1329 2.9288 2.5639 -0.0825 -0.0071 -0.3195 124  ALA C O   
7312  C  CB  . ALA C  126 ? 2.8557 2.6558 2.2412 -0.0398 0.0562  -0.2860 124  ALA C CB  
7313  N  N   . GLU C  127 ? 3.0862 2.8210 2.4408 -0.0720 -0.0548 -0.3301 125  GLU C N   
7314  C  CA  . GLU C  127 ? 2.9615 2.6846 2.3376 -0.0884 -0.0889 -0.3426 125  GLU C CA  
7315  C  C   . GLU C  127 ? 2.9439 2.6096 2.2549 -0.0659 -0.1095 -0.3630 125  GLU C C   
7316  O  O   . GLU C  127 ? 2.8946 2.5190 2.1349 -0.0437 -0.1241 -0.3728 125  GLU C O   
7317  C  CB  . GLU C  127 ? 2.8204 2.5488 2.2267 -0.1107 -0.1226 -0.3374 125  GLU C CB  
7318  C  CG  . GLU C  127 ? 2.8108 2.5148 2.1682 -0.0993 -0.1396 -0.3364 125  GLU C CG  
7319  C  CD  . GLU C  127 ? 2.7972 2.5175 2.1972 -0.1218 -0.1695 -0.3248 125  GLU C CD  
7320  O  OE1 . GLU C  127 ? 2.7571 2.4993 2.2180 -0.1434 -0.1817 -0.3190 125  GLU C OE1 
7321  O  OE2 . GLU C  127 ? 2.8641 2.5795 2.2390 -0.1152 -0.1785 -0.3173 125  GLU C OE2 
7322  N  N   . LEU C  128 ? 3.0936 2.7547 2.4250 -0.0686 -0.1112 -0.3700 126  LEU C N   
7323  C  CA  . LEU C  128 ? 3.1952 2.7958 2.4692 -0.0460 -0.1291 -0.3914 126  LEU C CA  
7324  C  C   . LEU C  128 ? 3.3703 2.9320 2.6552 -0.0648 -0.1851 -0.4045 126  LEU C C   
7325  O  O   . LEU C  128 ? 3.5668 3.1559 2.9268 -0.0931 -0.1973 -0.3931 126  LEU C O   
7326  C  CB  . LEU C  128 ? 3.0767 2.6919 2.3740 -0.0385 -0.1017 -0.3884 126  LEU C CB  
7327  C  CG  . LEU C  128 ? 3.0411 2.5927 2.2880 -0.0138 -0.1157 -0.4093 126  LEU C CG  
7328  C  CD1 . LEU C  128 ? 3.3116 2.8119 2.4548 0.0303  -0.1077 -0.4245 126  LEU C CD1 
7329  C  CD2 . LEU C  128 ? 2.9627 2.5434 2.2506 -0.0102 -0.0860 -0.3987 126  LEU C CD2 
7330  N  N   . ARG C  129 ? 3.3017 2.8009 2.5138 -0.0477 -0.2203 -0.4268 127  ARG C N   
7331  C  CA  . ARG C  129 ? 3.1329 2.5917 2.3582 -0.0677 -0.2817 -0.4398 127  ARG C CA  
7332  C  C   . ARG C  129 ? 3.2234 2.6023 2.3969 -0.0487 -0.3108 -0.4712 127  ARG C C   
7333  O  O   . ARG C  129 ? 3.2732 2.6091 2.3552 -0.0079 -0.2957 -0.4913 127  ARG C O   
7334  C  CB  . ARG C  129 ? 3.1133 2.5615 2.3003 -0.0668 -0.3117 -0.4431 127  ARG C CB  
7335  C  CG  . ARG C  129 ? 3.0524 2.5718 2.2901 -0.0836 -0.2845 -0.4121 127  ARG C CG  
7336  C  CD  . ARG C  129 ? 3.0780 2.5917 2.3029 -0.0908 -0.3244 -0.4097 127  ARG C CD  
7337  N  NE  . ARG C  129 ? 3.1575 2.7356 2.4370 -0.1063 -0.2985 -0.3788 127  ARG C NE  
7338  C  CZ  . ARG C  129 ? 3.3122 2.9039 2.6040 -0.1164 -0.3247 -0.3661 127  ARG C CZ  
7339  N  NH1 . ARG C  129 ? 3.4037 2.9529 2.6597 -0.1153 -0.3821 -0.3821 127  ARG C NH1 
7340  N  NH2 . ARG C  129 ? 3.3044 2.9506 2.6445 -0.1266 -0.2959 -0.3382 127  ARG C NH2 
7341  N  N   . LEU C  130 ? 3.1707 2.5285 2.4047 -0.0758 -0.3514 -0.4733 128  LEU C N   
7342  C  CA  . LEU C  130 ? 3.2584 2.5340 2.4560 -0.0614 -0.3820 -0.5033 128  LEU C CA  
7343  C  C   . LEU C  130 ? 3.3046 2.5199 2.5069 -0.0813 -0.4592 -0.5236 128  LEU C C   
7344  O  O   . LEU C  130 ? 3.3179 2.5490 2.5212 -0.0951 -0.4875 -0.5195 128  LEU C O   
7345  C  CB  . LEU C  130 ? 3.2135 2.5108 2.4866 -0.0730 -0.3589 -0.4858 128  LEU C CB  
7346  C  CG  . LEU C  130 ? 3.1317 2.5065 2.4328 -0.0657 -0.2907 -0.4589 128  LEU C CG  
7347  C  CD1 . LEU C  130 ? 3.1530 2.5424 2.5215 -0.0738 -0.2770 -0.4437 128  LEU C CD1 
7348  C  CD2 . LEU C  130 ? 3.1605 2.5227 2.3685 -0.0221 -0.2502 -0.4716 128  LEU C CD2 
7349  N  N   . LEU C  131 ? 3.3394 2.4847 2.5490 -0.0834 -0.4961 -0.5447 129  LEU C N   
7350  C  CA  . LEU C  131 ? 3.3474 2.4297 2.5731 -0.1062 -0.5768 -0.5652 129  LEU C CA  
7351  C  C   . LEU C  131 ? 3.3695 2.4210 2.6839 -0.1307 -0.6011 -0.5585 129  LEU C C   
7352  O  O   . LEU C  131 ? 3.4318 2.4260 2.7080 -0.1056 -0.5895 -0.5796 129  LEU C O   
7353  C  CB  . LEU C  131 ? 3.4783 2.4647 2.5658 -0.0672 -0.6156 -0.6191 129  LEU C CB  
7354  C  CG  . LEU C  131 ? 3.6073 2.5264 2.6900 -0.0871 -0.7082 -0.6481 129  LEU C CG  
7355  C  CD1 . LEU C  131 ? 3.8129 2.6313 2.9040 -0.0908 -0.7595 -0.6812 129  LEU C CD1 
7356  C  CD2 . LEU C  131 ? 3.4971 2.4907 2.7039 -0.1404 -0.7342 -0.6062 129  LEU C CD2 
7357  N  N   . ARG C  132 ? 3.4151 2.5053 2.8504 -0.1772 -0.6335 -0.5255 130  ARG C N   
7358  C  CA  . ARG C  132 ? 3.4269 2.5011 2.9690 -0.2045 -0.6552 -0.5064 130  ARG C CA  
7359  C  C   . ARG C  132 ? 3.5708 2.5403 3.1111 -0.2186 -0.7427 -0.5421 130  ARG C C   
7360  O  O   . ARG C  132 ? 3.8069 2.7513 3.3157 -0.2273 -0.7976 -0.5624 130  ARG C O   
7361  C  CB  . ARG C  132 ? 3.4089 2.5865 3.0898 -0.2435 -0.6401 -0.4441 130  ARG C CB  
7362  C  CG  . ARG C  132 ? 3.4600 2.6275 3.2728 -0.2803 -0.6809 -0.4140 130  ARG C CG  
7363  C  CD  . ARG C  132 ? 3.3859 2.6570 3.3208 -0.3132 -0.6730 -0.3522 130  ARG C CD  
7364  N  NE  . ARG C  132 ? 3.5342 2.8048 3.6076 -0.3488 -0.7123 -0.3135 130  ARG C NE  
7365  C  CZ  . ARG C  132 ? 3.5107 2.8469 3.6888 -0.3569 -0.6739 -0.2585 130  ARG C CZ  
7366  N  NH1 . ARG C  132 ? 3.4994 2.8339 3.8093 -0.3884 -0.7111 -0.2185 130  ARG C NH1 
7367  N  NH2 . ARG C  132 ? 3.4266 2.8314 3.5801 -0.3326 -0.5999 -0.2417 130  ARG C NH2 
7368  N  N   . LEU C  133 ? 3.6240 2.5303 3.1996 -0.2203 -0.7580 -0.5499 131  LEU C N   
7369  C  CA  . LEU C  133 ? 3.9781 2.7780 3.5709 -0.2383 -0.8451 -0.5828 131  LEU C CA  
7370  C  C   . LEU C  133 ? 4.0487 2.8708 3.8140 -0.2866 -0.8709 -0.5340 131  LEU C C   
7371  O  O   . LEU C  133 ? 4.0676 2.8750 3.9106 -0.3258 -0.9418 -0.5266 131  LEU C O   
7372  C  CB  . LEU C  133 ? 4.1029 2.7820 3.5801 -0.1943 -0.8521 -0.6421 131  LEU C CB  
7373  C  CG  . LEU C  133 ? 4.1352 2.7533 3.4301 -0.1415 -0.8529 -0.7018 131  LEU C CG  
7374  C  CD1 . LEU C  133 ? 4.0102 2.7121 3.2408 -0.1055 -0.7607 -0.6823 131  LEU C CD1 
7375  C  CD2 . LEU C  133 ? 4.1918 2.6698 3.3943 -0.1049 -0.8853 -0.7618 131  LEU C CD2 
7376  N  N   . LYS C  134 ? 4.0832 2.9454 3.9148 -0.2835 -0.8149 -0.4960 132  LYS C N   
7377  C  CA  . LYS C  134 ? 4.0462 2.9289 4.0414 -0.3223 -0.8320 -0.4439 132  LYS C CA  
7378  C  C   . LYS C  134 ? 3.9032 2.8913 4.0175 -0.3622 -0.8388 -0.3841 132  LYS C C   
7379  O  O   . LYS C  134 ? 3.8329 2.9180 3.9294 -0.3537 -0.7867 -0.3596 132  LYS C O   
7380  C  CB  . LYS C  134 ? 3.8260 2.7510 3.8553 -0.3030 -0.7585 -0.4096 132  LYS C CB  
7381  C  CG  . LYS C  134 ? 3.8452 2.7247 3.9904 -0.3221 -0.7815 -0.3837 132  LYS C CG  
7382  C  CD  . LYS C  134 ? 3.7064 2.6125 3.8459 -0.2902 -0.7081 -0.3635 132  LYS C CD  
7383  C  CE  . LYS C  134 ? 3.8596 2.7045 4.0994 -0.3018 -0.7294 -0.3430 132  LYS C CE  
7384  N  NZ  . LYS C  134 ? 3.7838 2.6524 4.0092 -0.2662 -0.6585 -0.3249 132  LYS C NZ  
7385  N  N   . LEU C  135 ? 3.7163 2.6842 3.9575 -0.4050 -0.9037 -0.3586 133  LEU C N   
7386  C  CA  . LEU C  135 ? 3.3790 2.4437 3.7430 -0.4418 -0.9156 -0.2974 133  LEU C CA  
7387  C  C   . LEU C  135 ? 3.2356 2.3657 3.7753 -0.4677 -0.8969 -0.2172 133  LEU C C   
7388  O  O   . LEU C  135 ? 3.1134 2.3413 3.7586 -0.4902 -0.8895 -0.1549 133  LEU C O   
7389  C  CB  . LEU C  135 ? 3.3770 2.3836 3.7547 -0.4730 -1.0127 -0.3245 133  LEU C CB  
7390  C  CG  . LEU C  135 ? 3.4933 2.3822 3.9288 -0.5004 -1.1019 -0.3508 133  LEU C CG  
7391  C  CD1 . LEU C  135 ? 3.4464 2.3883 4.0916 -0.5528 -1.1367 -0.2743 133  LEU C CD1 
7392  C  CD2 . LEU C  135 ? 3.5994 2.3909 3.9218 -0.4977 -1.1836 -0.4272 133  LEU C CD2 
7393  N  N   . LYS C  136 ? 3.1721 2.2544 3.7457 -0.4609 -0.8853 -0.2131 134  LYS C N   
7394  C  CA  . LYS C  136 ? 3.0089 2.1442 3.7518 -0.4823 -0.8698 -0.1348 134  LYS C CA  
7395  C  C   . LYS C  136 ? 2.9162 2.1392 3.6463 -0.4480 -0.7731 -0.0974 134  LYS C C   
7396  O  O   . LYS C  136 ? 2.9610 2.1596 3.5609 -0.4105 -0.7320 -0.1431 134  LYS C O   
7397  C  CB  . LYS C  136 ? 2.9442 1.9605 3.7470 -0.5001 -0.9291 -0.1519 134  LYS C CB  
7398  C  CG  . LYS C  136 ? 2.9670 1.8752 3.7527 -0.5286 -1.0331 -0.2079 134  LYS C CG  
7399  C  CD  . LYS C  136 ? 3.0499 1.8111 3.8392 -0.5334 -1.0907 -0.2527 134  LYS C CD  
7400  C  CE  . LYS C  136 ? 3.1640 1.8157 3.9149 -0.5574 -1.1990 -0.3181 134  LYS C CE  
7401  N  NZ  . LYS C  136 ? 3.3011 1.7953 4.0489 -0.5613 -1.2642 -0.3701 134  LYS C NZ  
7402  N  N   . VAL C  137 ? 2.7196 2.0476 3.5866 -0.4589 -0.7381 -0.0118 135  VAL C N   
7403  C  CA  . VAL C  137 ? 2.6870 2.1080 3.5576 -0.4270 -0.6517 0.0320  135  VAL C CA  
7404  C  C   . VAL C  137 ? 2.6687 2.1569 3.4174 -0.3985 -0.5997 0.0080  135  VAL C C   
7405  O  O   . VAL C  137 ? 2.6626 2.1240 3.3269 -0.4024 -0.6267 -0.0391 135  VAL C O   
7406  C  CB  . VAL C  137 ? 2.8329 2.1890 3.6743 -0.4037 -0.6307 0.0131  135  VAL C CB  
7407  C  CG1 . VAL C  137 ? 2.7604 2.2188 3.6572 -0.3788 -0.5544 0.0793  135  VAL C CG1 
7408  C  CG2 . VAL C  137 ? 3.1057 2.3525 4.0329 -0.4322 -0.6989 0.0083  135  VAL C CG2 
7409  N  N   . GLU C  138 ? 2.7929 2.3692 3.5352 -0.3695 -0.5266 0.0420  136  GLU C N   
7410  C  CA  . GLU C  138 ? 2.8468 2.4890 3.4865 -0.3422 -0.4743 0.0235  136  GLU C CA  
7411  C  C   . GLU C  138 ? 3.0017 2.6496 3.5735 -0.3069 -0.4206 0.0081  136  GLU C C   
7412  O  O   . GLU C  138 ? 3.1045 2.7675 3.7451 -0.2992 -0.4005 0.0476  136  GLU C O   
7413  C  CB  . GLU C  138 ? 2.7333 2.4968 3.4465 -0.3424 -0.4417 0.0888  136  GLU C CB  
7414  C  CG  . GLU C  138 ? 2.6752 2.5206 3.3143 -0.3080 -0.3747 0.0885  136  GLU C CG  
7415  C  CD  . GLU C  138 ? 2.6600 2.6065 3.3500 -0.3058 -0.3518 0.1396  136  GLU C CD  
7416  O  OE1 . GLU C  138 ? 2.6014 2.5988 3.4146 -0.3138 -0.3517 0.2095  136  GLU C OE1 
7417  O  OE2 . GLU C  138 ? 2.7225 2.6964 3.3325 -0.2943 -0.3330 0.1127  136  GLU C OE2 
7418  N  N   . GLN C  139 ? 3.0199 2.6582 3.4631 -0.2852 -0.3977 -0.0452 137  GLN C N   
7419  C  CA  . GLN C  139 ? 2.9712 2.6145 3.3479 -0.2525 -0.3506 -0.0625 137  GLN C CA  
7420  C  C   . GLN C  139 ? 2.8702 2.5857 3.1697 -0.2330 -0.3055 -0.0756 137  GLN C C   
7421  O  O   . GLN C  139 ? 2.8138 2.5501 3.0881 -0.2427 -0.3144 -0.0857 137  GLN C O   
7422  C  CB  . GLN C  139 ? 3.1693 2.6964 3.4651 -0.2425 -0.3749 -0.1219 137  GLN C CB  
7423  C  CG  . GLN C  139 ? 3.3348 2.7883 3.7049 -0.2521 -0.4066 -0.1088 137  GLN C CG  
7424  C  CD  . GLN C  139 ? 3.4451 2.7672 3.7281 -0.2422 -0.4427 -0.1747 137  GLN C CD  
7425  O  OE1 . GLN C  139 ? 3.5523 2.8292 3.7358 -0.2378 -0.4636 -0.2273 137  GLN C OE1 
7426  N  NE2 . GLN C  139 ? 3.3349 2.5941 3.6528 -0.2347 -0.4489 -0.1706 137  GLN C NE2 
7427  N  N   . HIS C  140 ? 2.9010 2.6537 3.1675 -0.2055 -0.2587 -0.0743 138  HIS C N   
7428  C  CA  . HIS C  140 ? 2.9615 2.7899 3.1732 -0.1874 -0.2154 -0.0801 138  HIS C CA  
7429  C  C   . HIS C  140 ? 2.9876 2.7740 3.0956 -0.1685 -0.2012 -0.1319 138  HIS C C   
7430  O  O   . HIS C  140 ? 3.1052 2.8492 3.1985 -0.1534 -0.1951 -0.1414 138  HIS C O   
7431  C  CB  . HIS C  140 ? 2.9915 2.9119 3.2568 -0.1694 -0.1741 -0.0306 138  HIS C CB  
7432  C  CG  . HIS C  140 ? 2.9352 2.9375 3.1597 -0.1546 -0.1394 -0.0325 138  HIS C CG  
7433  N  ND1 . HIS C  140 ? 2.9123 2.9586 3.1474 -0.1628 -0.1411 -0.0211 138  HIS C ND1 
7434  C  CD2 . HIS C  140 ? 2.8355 2.8813 3.0119 -0.1319 -0.1050 -0.0448 138  HIS C CD2 
7435  C  CE1 . HIS C  140 ? 2.8051 2.9113 2.9954 -0.1452 -0.1100 -0.0303 138  HIS C CE1 
7436  N  NE2 . HIS C  140 ? 2.7526 2.8610 2.9094 -0.1282 -0.0900 -0.0449 138  HIS C NE2 
7437  N  N   . VAL C  141 ? 2.9040 2.7058 2.9454 -0.1668 -0.1924 -0.1602 139  VAL C N   
7438  C  CA  . VAL C  141 ? 2.9367 2.6964 2.8838 -0.1504 -0.1820 -0.2056 139  VAL C CA  
7439  C  C   . VAL C  141 ? 2.8807 2.7161 2.7995 -0.1374 -0.1406 -0.2059 139  VAL C C   
7440  O  O   . VAL C  141 ? 2.7977 2.6905 2.7335 -0.1461 -0.1340 -0.1935 139  VAL C O   
7441  C  CB  . VAL C  141 ? 3.0135 2.7060 2.9050 -0.1608 -0.2169 -0.2417 139  VAL C CB  
7442  C  CG1 . VAL C  141 ? 3.1799 2.8393 2.9742 -0.1380 -0.1989 -0.2807 139  VAL C CG1 
7443  C  CG2 . VAL C  141 ? 3.1380 2.7484 3.0555 -0.1743 -0.2660 -0.2475 139  VAL C CG2 
7444  N  N   . GLU C  142 ? 2.9913 2.8242 2.8683 -0.1158 -0.1146 -0.2203 140  GLU C N   
7445  C  CA  . GLU C  142 ? 3.0933 2.9877 2.9430 -0.1052 -0.0814 -0.2257 140  GLU C CA  
7446  C  C   . GLU C  142 ? 3.0612 2.9095 2.8356 -0.0927 -0.0741 -0.2596 140  GLU C C   
7447  O  O   . GLU C  142 ? 3.1119 2.8912 2.8509 -0.0787 -0.0814 -0.2754 140  GLU C O   
7448  C  CB  . GLU C  142 ? 3.1309 3.0847 3.0129 -0.0886 -0.0532 -0.2017 140  GLU C CB  
7449  C  CG  . GLU C  142 ? 3.0486 3.0547 3.0028 -0.0923 -0.0540 -0.1614 140  GLU C CG  
7450  C  CD  . GLU C  142 ? 3.0321 3.0949 3.0113 -0.0713 -0.0272 -0.1371 140  GLU C CD  
7451  O  OE1 . GLU C  142 ? 3.1387 3.2063 3.0836 -0.0566 -0.0090 -0.1520 140  GLU C OE1 
7452  O  OE2 . GLU C  142 ? 2.9271 3.0341 2.9634 -0.0674 -0.0235 -0.0990 140  GLU C OE2 
7453  N  N   . LEU C  143 ? 2.8736 2.7588 2.6240 -0.0949 -0.0587 -0.2692 141  LEU C N   
7454  C  CA  . LEU C  143 ? 2.6696 2.5220 2.3564 -0.0825 -0.0478 -0.2930 141  LEU C CA  
7455  C  C   . LEU C  143 ? 2.6491 2.5579 2.3384 -0.0698 -0.0128 -0.2870 141  LEU C C   
7456  O  O   . LEU C  143 ? 2.7513 2.7299 2.4812 -0.0790 -0.0035 -0.2741 141  LEU C O   
7457  C  CB  . LEU C  143 ? 2.5935 2.4366 2.2573 -0.0971 -0.0608 -0.3052 141  LEU C CB  
7458  C  CG  . LEU C  143 ? 2.5948 2.4006 2.1915 -0.0816 -0.0506 -0.3248 141  LEU C CG  
7459  C  CD1 . LEU C  143 ? 2.8573 2.5807 2.3998 -0.0613 -0.0658 -0.3425 141  LEU C CD1 
7460  C  CD2 . LEU C  143 ? 2.5421 2.3486 2.1265 -0.0964 -0.0618 -0.3305 141  LEU C CD2 
7461  N  N   . TYR C  144 ? 2.7143 2.5939 2.3603 -0.0468 0.0052  -0.2957 142  TYR C N   
7462  C  CA  . TYR C  144 ? 2.6976 2.6315 2.3553 -0.0340 0.0376  -0.2847 142  TYR C CA  
7463  C  C   . TYR C  144 ? 2.7365 2.6521 2.3482 -0.0208 0.0552  -0.2933 142  TYR C C   
7464  O  O   . TYR C  144 ? 2.7989 2.6539 2.3577 -0.0147 0.0438  -0.3094 142  TYR C O   
7465  C  CB  . TYR C  144 ? 2.8114 2.7447 2.4789 -0.0107 0.0523  -0.2718 142  TYR C CB  
7466  C  CG  . TYR C  144 ? 2.8775 2.8469 2.6006 -0.0199 0.0429  -0.2536 142  TYR C CG  
7467  C  CD1 . TYR C  144 ? 2.8584 2.9139 2.6284 -0.0240 0.0555  -0.2354 142  TYR C CD1 
7468  C  CD2 . TYR C  144 ? 2.9609 2.8797 2.6919 -0.0232 0.0201  -0.2526 142  TYR C CD2 
7469  C  CE1 . TYR C  144 ? 2.8574 2.9509 2.6725 -0.0260 0.0500  -0.2149 142  TYR C CE1 
7470  C  CE2 . TYR C  144 ? 2.9286 2.8857 2.7169 -0.0286 0.0161  -0.2279 142  TYR C CE2 
7471  C  CZ  . TYR C  144 ? 2.8541 2.9001 2.6801 -0.0274 0.0333  -0.2082 142  TYR C CZ  
7472  O  OH  . TYR C  144 ? 2.8513 2.9401 2.7285 -0.0266 0.0321  -0.1800 142  TYR C OH  
7473  N  N   . GLN C  145 ? 2.9000 2.8723 2.5359 -0.0152 0.0826  -0.2792 143  GLN C N   
7474  C  CA  . GLN C  145 ? 2.9916 2.9613 2.6008 -0.0009 0.1063  -0.2761 143  GLN C CA  
7475  C  C   . GLN C  145 ? 3.0908 3.0792 2.7022 0.0301  0.1387  -0.2572 143  GLN C C   
7476  O  O   . GLN C  145 ? 3.1564 3.1858 2.8092 0.0313  0.1433  -0.2442 143  GLN C O   
7477  C  CB  . GLN C  145 ? 2.9759 3.0010 2.6282 -0.0270 0.1085  -0.2711 143  GLN C CB  
7478  C  CG  . GLN C  145 ? 3.0580 3.0805 2.6935 -0.0161 0.1320  -0.2624 143  GLN C CG  
7479  C  CD  . GLN C  145 ? 3.0891 3.1660 2.7823 -0.0439 0.1331  -0.2557 143  GLN C CD  
7480  O  OE1 . GLN C  145 ? 3.1380 3.2416 2.8660 -0.0705 0.1115  -0.2657 143  GLN C OE1 
7481  N  NE2 . GLN C  145 ? 2.9586 3.0507 2.6632 -0.0357 0.1586  -0.2373 143  GLN C NE2 
7482  N  N   . LYS C  146 ? 3.0217 2.9831 2.5876 0.0591  0.1631  -0.2522 144  LYS C N   
7483  C  CA  . LYS C  146 ? 3.0355 3.0108 2.5971 0.0963  0.1989  -0.2302 144  LYS C CA  
7484  C  C   . LYS C  146 ? 3.1077 3.1739 2.7453 0.0850  0.2218  -0.1997 144  LYS C C   
7485  O  O   . LYS C  146 ? 3.1725 3.2603 2.8264 0.0737  0.2300  -0.1914 144  LYS C O   
7486  C  CB  . LYS C  146 ? 3.0955 3.0057 2.5715 0.1394  0.2183  -0.2343 144  LYS C CB  
7487  C  CG  . LYS C  146 ? 3.1341 3.0544 2.5970 0.1871  0.2607  -0.2086 144  LYS C CG  
7488  C  CD  . LYS C  146 ? 3.1731 3.0299 2.5402 0.2361  0.2818  -0.2127 144  LYS C CD  
7489  C  CE  . LYS C  146 ? 3.1978 3.0661 2.5486 0.2907  0.3293  -0.1832 144  LYS C CE  
7490  N  NZ  . LYS C  146 ? 3.2323 3.0497 2.4872 0.3464  0.3570  -0.1810 144  LYS C NZ  
7491  N  N   . TYR C  147 ? 3.1135 3.2328 2.8020 0.0882  0.2307  -0.1813 145  TYR C N   
7492  C  CA  . TYR C  147 ? 3.0636 3.2724 2.8317 0.0777  0.2470  -0.1514 145  TYR C CA  
7493  C  C   . TYR C  147 ? 3.1622 3.3957 2.9406 0.1164  0.2806  -0.1209 145  TYR C C   
7494  O  O   . TYR C  147 ? 3.2006 3.4096 2.9572 0.1351  0.2792  -0.1251 145  TYR C O   
7495  C  CB  . TYR C  147 ? 2.8652 3.1329 2.6976 0.0375  0.2163  -0.1590 145  TYR C CB  
7496  C  CG  . TYR C  147 ? 2.8024 3.0690 2.6455 0.0007  0.1918  -0.1791 145  TYR C CG  
7497  C  CD1 . TYR C  147 ? 2.7740 3.0892 2.6738 -0.0198 0.1949  -0.1671 145  TYR C CD1 
7498  C  CD2 . TYR C  147 ? 2.8289 3.0450 2.6314 -0.0131 0.1655  -0.2075 145  TYR C CD2 
7499  C  CE1 . TYR C  147 ? 2.7716 3.0791 2.6805 -0.0508 0.1736  -0.1862 145  TYR C CE1 
7500  C  CE2 . TYR C  147 ? 2.8921 3.1071 2.7036 -0.0425 0.1462  -0.2235 145  TYR C CE2 
7501  C  CZ  . TYR C  147 ? 2.8847 3.1424 2.7459 -0.0602 0.1510  -0.2144 145  TYR C CZ  
7502  O  OH  . TYR C  147 ? 2.9899 3.2402 2.8596 -0.0871 0.1327  -0.2311 145  TYR C OH  
7503  N  N   . SER C  148 ? 3.1597 3.4424 2.9767 0.1297  0.3124  -0.0862 146  SER C N   
7504  C  CA  . SER C  148 ? 3.1652 3.4835 3.0019 0.1694  0.3500  -0.0484 146  SER C CA  
7505  C  C   . SER C  148 ? 3.3636 3.5984 3.1052 0.2230  0.3717  -0.0565 146  SER C C   
7506  O  O   . SER C  148 ? 3.4192 3.6684 3.1652 0.2594  0.3985  -0.0326 146  SER C O   
7507  C  CB  . SER C  148 ? 3.0465 3.4398 2.9582 0.1534  0.3375  -0.0346 146  SER C CB  
7508  O  OG  . SER C  148 ? 2.9684 3.4042 2.9080 0.1917  0.3751  0.0071  146  SER C OG  
7509  N  N   . GLN C  149 ? 3.5013 3.6468 3.1562 0.2293  0.3579  -0.0912 147  GLN C N   
7510  C  CA  . GLN C  149 ? 3.5308 3.5802 3.0836 0.2774  0.3670  -0.1106 147  GLN C CA  
7511  C  C   . GLN C  149 ? 3.5384 3.5591 3.0868 0.2853  0.3538  -0.1225 147  GLN C C   
7512  O  O   . GLN C  149 ? 3.5762 3.5182 3.0495 0.3296  0.3637  -0.1355 147  GLN C O   
7513  C  CB  . GLN C  149 ? 3.4924 3.5397 3.0065 0.3377  0.4195  -0.0787 147  GLN C CB  
7514  C  CG  . GLN C  149 ? 3.4547 3.5265 2.9710 0.3374  0.4382  -0.0598 147  GLN C CG  
7515  C  CD  . GLN C  149 ? 3.6276 3.6995 3.1019 0.4045  0.4948  -0.0223 147  GLN C CD  
7516  O  OE1 . GLN C  149 ? 3.7477 3.7742 3.1594 0.4581  0.5165  -0.0231 147  GLN C OE1 
7517  N  NE2 . GLN C  149 ? 3.6461 3.7686 3.1563 0.4049  0.5211  0.0136  147  GLN C NE2 
7518  N  N   . ASN C  150 ? 3.4177 3.4971 3.0424 0.2459  0.3312  -0.1186 148  ASN C N   
7519  C  CA  . ASN C  150 ? 3.3593 3.4225 2.9927 0.2522  0.3209  -0.1218 148  ASN C CA  
7520  C  C   . ASN C  150 ? 3.1587 3.2497 2.8404 0.2016  0.2799  -0.1363 148  ASN C C   
7521  O  O   . ASN C  150 ? 3.1940 3.2333 2.8590 0.1977  0.2573  -0.1538 148  ASN C O   
7522  C  CB  . ASN C  150 ? 3.3532 3.4868 3.0393 0.2798  0.3560  -0.0792 148  ASN C CB  
7523  C  CG  . ASN C  150 ? 3.3241 3.4494 3.0276 0.2874  0.3482  -0.0762 148  ASN C CG  
7524  O  OD1 . ASN C  150 ? 3.4274 3.4665 3.0837 0.2909  0.3277  -0.1043 148  ASN C OD1 
7525  N  ND2 . ASN C  150 ? 3.1958 3.4127 2.9730 0.2897  0.3630  -0.0394 148  ASN C ND2 
7526  N  N   . SER C  151 ? 3.0889 3.2604 2.8322 0.1649  0.2701  -0.1276 149  SER C N   
7527  C  CA  . SER C  151 ? 3.0549 3.2601 2.8391 0.1233  0.2349  -0.1397 149  SER C CA  
7528  C  C   . SER C  151 ? 3.0050 3.1564 2.7520 0.0968  0.2070  -0.1720 149  SER C C   
7529  O  O   . SER C  151 ? 3.0046 3.1269 2.7172 0.0988  0.2137  -0.1806 149  SER C O   
7530  C  CB  . SER C  151 ? 3.0586 3.3698 2.9205 0.0990  0.2325  -0.1205 149  SER C CB  
7531  O  OG  . SER C  151 ? 3.0229 3.3615 2.9099 0.0643  0.1987  -0.1362 149  SER C OG  
7532  N  N   . TRP C  152 ? 2.9268 3.0697 2.6841 0.0743  0.1775  -0.1851 150  TRP C N   
7533  C  CA  . TRP C  152 ? 2.9092 3.0087 2.6412 0.0487  0.1494  -0.2110 150  TRP C CA  
7534  C  C   . TRP C  152 ? 2.7771 2.9416 2.5596 0.0155  0.1290  -0.2108 150  TRP C C   
7535  O  O   . TRP C  152 ? 2.7617 2.9729 2.5823 0.0150  0.1251  -0.1969 150  TRP C O   
7536  C  CB  . TRP C  152 ? 3.0607 3.0762 2.7541 0.0567  0.1314  -0.2258 150  TRP C CB  
7537  C  CG  . TRP C  152 ? 3.2121 3.1573 2.8482 0.0955  0.1489  -0.2305 150  TRP C CG  
7538  C  CD1 . TRP C  152 ? 3.2381 3.1696 2.8748 0.1261  0.1661  -0.2169 150  TRP C CD1 
7539  C  CD2 . TRP C  152 ? 3.3148 3.1928 2.8783 0.1137  0.1525  -0.2498 150  TRP C CD2 
7540  N  NE1 . TRP C  152 ? 3.3584 3.2132 2.9238 0.1634  0.1799  -0.2295 150  TRP C NE1 
7541  C  CE2 . TRP C  152 ? 3.4851 3.3073 3.0016 0.1577  0.1714  -0.2500 150  TRP C CE2 
7542  C  CE3 . TRP C  152 ? 3.2813 3.1409 2.8119 0.1007  0.1424  -0.2659 150  TRP C CE3 
7543  C  CZ2 . TRP C  152 ? 3.6437 3.3919 3.0742 0.1916  0.1794  -0.2682 150  TRP C CZ2 
7544  C  CZ3 . TRP C  152 ? 3.4499 3.2412 2.9001 0.1325  0.1505  -0.2806 150  TRP C CZ3 
7545  C  CH2 . TRP C  152 ? 3.6410 3.3771 3.0383 0.1787  0.1684  -0.2828 150  TRP C CH2 
7546  N  N   . ARG C  153 ? 2.6026 2.7695 2.3816 -0.0078 0.1175  -0.2254 151  ARG C N   
7547  C  CA  . ARG C  153 ? 2.5600 2.7787 2.3755 -0.0349 0.0980  -0.2302 151  ARG C CA  
7548  C  C   . ARG C  153 ? 2.6106 2.7840 2.4032 -0.0506 0.0751  -0.2466 151  ARG C C   
7549  O  O   . ARG C  153 ? 2.5511 2.6636 2.3032 -0.0503 0.0720  -0.2592 151  ARG C O   
7550  C  CB  . ARG C  153 ? 2.6088 2.8736 2.4516 -0.0501 0.1022  -0.2317 151  ARG C CB  
7551  C  CG  . ARG C  153 ? 2.6682 2.9918 2.5511 -0.0386 0.1208  -0.2101 151  ARG C CG  
7552  C  CD  . ARG C  153 ? 2.5232 2.8939 2.4327 -0.0282 0.1174  -0.1961 151  ARG C CD  
7553  N  NE  . ARG C  153 ? 2.3977 2.8226 2.3353 -0.0470 0.0929  -0.2046 151  ARG C NE  
7554  C  CZ  . ARG C  153 ? 2.3666 2.8465 2.3283 -0.0384 0.0867  -0.1922 151  ARG C CZ  
7555  N  NH1 . ARG C  153 ? 2.3808 2.8692 2.3497 -0.0140 0.1043  -0.1684 151  ARG C NH1 
7556  N  NH2 . ARG C  153 ? 2.3260 2.8517 2.3008 -0.0502 0.0638  -0.2030 151  ARG C NH2 
7557  N  N   . TYR C  154 ? 2.8030 3.0112 2.6222 -0.0611 0.0596  -0.2433 152  TYR C N   
7558  C  CA  . TYR C  154 ? 2.7041 2.8816 2.5151 -0.0735 0.0397  -0.2494 152  TYR C CA  
7559  C  C   . TYR C  154 ? 2.5672 2.7249 2.3591 -0.0905 0.0323  -0.2675 152  TYR C C   
7560  O  O   . TYR C  154 ? 2.5248 2.7110 2.3244 -0.0976 0.0391  -0.2742 152  TYR C O   
7561  C  CB  . TYR C  154 ? 2.7309 2.9654 2.5766 -0.0750 0.0317  -0.2360 152  TYR C CB  
7562  C  CG  . TYR C  154 ? 2.7326 2.9455 2.5836 -0.0826 0.0156  -0.2300 152  TYR C CG  
7563  C  CD1 . TYR C  154 ? 2.8046 2.9870 2.6695 -0.0762 0.0105  -0.2124 152  TYR C CD1 
7564  C  CD2 . TYR C  154 ? 2.6182 2.8424 2.4672 -0.0956 0.0055  -0.2387 152  TYR C CD2 
7565  C  CE1 . TYR C  154 ? 2.7882 2.9571 2.6724 -0.0851 -0.0053 -0.2004 152  TYR C CE1 
7566  C  CE2 . TYR C  154 ? 2.5579 2.7702 2.4195 -0.1006 -0.0070 -0.2266 152  TYR C CE2 
7567  C  CZ  . TYR C  154 ? 2.6748 2.8624 2.5579 -0.0965 -0.0128 -0.2056 152  TYR C CZ  
7568  O  OH  . TYR C  154 ? 2.7623 2.9434 2.6719 -0.1035 -0.0263 -0.1873 152  TYR C OH  
7569  N  N   . LEU C  155 ? 2.4391 2.5475 2.2118 -0.0976 0.0166  -0.2730 153  LEU C N   
7570  C  CA  . LEU C  155 ? 2.3880 2.4760 2.1427 -0.1115 0.0091  -0.2865 153  LEU C CA  
7571  C  C   . LEU C  155 ? 2.3601 2.4530 2.1308 -0.1231 -0.0093 -0.2820 153  LEU C C   
7572  O  O   . LEU C  155 ? 2.3075 2.4474 2.0996 -0.1278 -0.0091 -0.2803 153  LEU C O   
7573  C  CB  . LEU C  155 ? 2.4254 2.4464 2.1330 -0.1047 0.0086  -0.2965 153  LEU C CB  
7574  C  CG  . LEU C  155 ? 2.6140 2.6315 2.3013 -0.0878 0.0330  -0.2965 153  LEU C CG  
7575  C  CD1 . LEU C  155 ? 2.7683 2.7193 2.3970 -0.0746 0.0325  -0.3065 153  LEU C CD1 
7576  C  CD2 . LEU C  155 ? 2.5976 2.6676 2.3147 -0.0979 0.0472  -0.2941 153  LEU C CD2 
7577  N  N   . SER C  156 ? 2.4209 2.4657 2.1818 -0.1259 -0.0265 -0.2795 154  SER C N   
7578  C  CA  . SER C  156 ? 2.3990 2.4495 2.1835 -0.1367 -0.0439 -0.2683 154  SER C CA  
7579  C  C   . SER C  156 ? 2.4953 2.5253 2.3062 -0.1356 -0.0592 -0.2503 154  SER C C   
7580  O  O   . SER C  156 ? 2.5407 2.5468 2.3465 -0.1257 -0.0566 -0.2504 154  SER C O   
7581  C  CB  . SER C  156 ? 2.3730 2.3871 2.1321 -0.1472 -0.0560 -0.2796 154  SER C CB  
7582  O  OG  . SER C  156 ? 2.4228 2.3729 2.1456 -0.1445 -0.0692 -0.2906 154  SER C OG  
7583  N  N   . ASN C  157 ? 2.5658 2.6050 2.4107 -0.1452 -0.0748 -0.2319 155  ASN C N   
7584  C  CA  . ASN C  157 ? 2.6340 2.6629 2.5246 -0.1478 -0.0906 -0.2065 155  ASN C CA  
7585  C  C   . ASN C  157 ? 2.6692 2.6785 2.5829 -0.1642 -0.1171 -0.1957 155  ASN C C   
7586  O  O   . ASN C  157 ? 2.6291 2.6588 2.5353 -0.1687 -0.1151 -0.1975 155  ASN C O   
7587  C  CB  . ASN C  157 ? 2.8117 2.9098 2.7486 -0.1358 -0.0728 -0.1754 155  ASN C CB  
7588  C  CG  . ASN C  157 ? 2.9764 3.0672 2.9716 -0.1370 -0.0846 -0.1416 155  ASN C CG  
7589  O  OD1 . ASN C  157 ? 3.1634 3.2735 3.2078 -0.1440 -0.0947 -0.1116 155  ASN C OD1 
7590  N  ND2 . ASN C  157 ? 2.9428 3.0068 2.9390 -0.1290 -0.0819 -0.1424 155  ASN C ND2 
7591  N  N   . ARG C  158 ? 2.7603 2.7287 2.7068 -0.1734 -0.1439 -0.1834 156  ARG C N   
7592  C  CA  . ARG C  158 ? 2.7743 2.7266 2.7552 -0.1918 -0.1751 -0.1692 156  ARG C CA  
7593  C  C   . ARG C  158 ? 2.8260 2.7517 2.8719 -0.2023 -0.2020 -0.1440 156  ARG C C   
7594  O  O   . ARG C  158 ? 2.8244 2.6914 2.8525 -0.2001 -0.2146 -0.1621 156  ARG C O   
7595  C  CB  . ARG C  158 ? 2.7144 2.6081 2.6346 -0.1992 -0.1972 -0.2043 156  ARG C CB  
7596  C  CG  . ARG C  158 ? 2.6984 2.5844 2.6522 -0.2179 -0.2307 -0.1898 156  ARG C CG  
7597  C  CD  . ARG C  158 ? 2.7193 2.5713 2.6052 -0.2183 -0.2402 -0.2208 156  ARG C CD  
7598  N  NE  . ARG C  158 ? 2.7157 2.6030 2.5603 -0.2046 -0.2006 -0.2326 156  ARG C NE  
7599  C  CZ  . ARG C  158 ? 2.8234 2.6909 2.6102 -0.2004 -0.1964 -0.2552 156  ARG C CZ  
7600  N  NH1 . ARG C  158 ? 2.8657 2.6814 2.6196 -0.2050 -0.2286 -0.2696 156  ARG C NH1 
7601  N  NH2 . ARG C  158 ? 2.8114 2.7107 2.5753 -0.1909 -0.1619 -0.2626 156  ARG C NH2 
7602  N  N   . LEU C  159 ? 2.7181 2.6857 2.8424 -0.2120 -0.2099 -0.1003 157  LEU C N   
7603  C  CA  . LEU C  159 ? 2.6669 2.6116 2.8723 -0.2274 -0.2400 -0.0690 157  LEU C CA  
7604  C  C   . LEU C  159 ? 2.6925 2.5737 2.8991 -0.2520 -0.2918 -0.0859 157  LEU C C   
7605  O  O   . LEU C  159 ? 2.6674 2.5531 2.8392 -0.2565 -0.2985 -0.1001 157  LEU C O   
7606  C  CB  . LEU C  159 ? 2.6115 2.6382 2.9104 -0.2240 -0.2225 -0.0052 157  LEU C CB  
7607  C  CG  . LEU C  159 ? 2.6045 2.7005 2.9138 -0.1965 -0.1764 0.0210  157  LEU C CG  
7608  C  CD1 . LEU C  159 ? 2.5807 2.7289 2.8242 -0.1759 -0.1418 0.0024  157  LEU C CD1 
7609  C  CD2 . LEU C  159 ? 2.6472 2.8023 3.0642 -0.1934 -0.1693 0.0917  157  LEU C CD2 
7610  N  N   . LEU C  160 ? 2.7671 2.5868 3.0142 -0.2671 -0.3308 -0.0851 158  LEU C N   
7611  C  CA  . LEU C  160 ? 2.7646 2.5111 3.0052 -0.2896 -0.3895 -0.1096 158  LEU C CA  
7612  C  C   . LEU C  160 ? 2.9016 2.6581 3.2684 -0.3174 -0.4278 -0.0602 158  LEU C C   
7613  O  O   . LEU C  160 ? 2.9184 2.7024 3.3701 -0.3179 -0.4154 -0.0165 158  LEU C O   
7614  C  CB  . LEU C  160 ? 2.7336 2.3789 2.8998 -0.2824 -0.4127 -0.1631 158  LEU C CB  
7615  C  CG  . LEU C  160 ? 2.7469 2.3626 2.7838 -0.2576 -0.3904 -0.2161 158  LEU C CG  
7616  C  CD1 . LEU C  160 ? 2.7507 2.4283 2.7628 -0.2334 -0.3275 -0.2086 158  LEU C CD1 
7617  C  CD2 . LEU C  160 ? 2.8427 2.3508 2.8131 -0.2487 -0.4231 -0.2640 158  LEU C CD2 
7618  N  N   . ALA C  161 ? 3.0364 2.7728 3.4208 -0.3402 -0.4757 -0.0635 159  ALA C N   
7619  C  CA  . ALA C  161 ? 2.9738 2.7301 3.4905 -0.3697 -0.5146 -0.0106 159  ALA C CA  
7620  C  C   . ALA C  161 ? 3.0939 2.7484 3.6249 -0.3967 -0.5913 -0.0416 159  ALA C C   
7621  O  O   . ALA C  161 ? 3.2703 2.8513 3.6971 -0.3931 -0.6217 -0.1038 159  ALA C O   
7622  C  CB  . ALA C  161 ? 2.8845 2.7121 3.4350 -0.3766 -0.5127 0.0223  159  ALA C CB  
7623  N  N   . PRO C  162 ? 2.8985 2.5455 3.5591 -0.4226 -0.6256 0.0018  160  PRO C N   
7624  C  CA  . PRO C  162 ? 3.0010 2.5429 3.6822 -0.4506 -0.7065 -0.0306 160  PRO C CA  
7625  C  C   . PRO C  162 ? 3.0996 2.6259 3.7791 -0.4747 -0.7684 -0.0459 160  PRO C C   
7626  O  O   . PRO C  162 ? 3.1134 2.6727 3.9232 -0.5071 -0.8080 0.0048  160  PRO C O   
7627  C  CB  . PRO C  162 ? 2.9670 2.5256 3.8116 -0.4734 -0.7187 0.0352  160  PRO C CB  
7628  C  CG  . PRO C  162 ? 2.8144 2.5054 3.7400 -0.4636 -0.6583 0.1135  160  PRO C CG  
7629  C  CD  . PRO C  162 ? 2.7595 2.4920 3.5532 -0.4244 -0.5911 0.0834  160  PRO C CD  
7630  N  N   . SER C  163 ? 3.2275 2.7081 3.7639 -0.4575 -0.7767 -0.1113 161  SER C N   
7631  C  CA  . SER C  163 ? 3.2306 2.6890 3.7441 -0.4747 -0.8376 -0.1337 161  SER C CA  
7632  C  C   . SER C  163 ? 3.3788 2.7169 3.8829 -0.4946 -0.9259 -0.1825 161  SER C C   
7633  O  O   . SER C  163 ? 3.3792 2.6274 3.7871 -0.4738 -0.9289 -0.2393 161  SER C O   
7634  C  CB  . SER C  163 ? 3.1678 2.6316 3.5312 -0.4431 -0.8050 -0.1783 161  SER C CB  
7635  O  OG  . SER C  163 ? 3.1765 2.6155 3.5077 -0.4552 -0.8645 -0.2016 161  SER C OG  
7636  N  N   . ASP C  164 ? 3.4564 2.7925 4.0598 -0.5333 -0.9995 -0.1607 162  ASP C N   
7637  C  CA  . ASP C  164 ? 3.5517 2.7717 4.1625 -0.5572 -1.0947 -0.2058 162  ASP C CA  
7638  C  C   . ASP C  164 ? 3.5578 2.6819 3.9864 -0.5308 -1.1302 -0.2966 162  ASP C C   
7639  O  O   . ASP C  164 ? 3.6183 2.6245 4.0062 -0.5343 -1.1962 -0.3525 162  ASP C O   
7640  C  CB  . ASP C  164 ? 3.6214 2.8724 4.3873 -0.6067 -1.1685 -0.1579 162  ASP C CB  
7641  C  CG  . ASP C  164 ? 3.5263 2.8774 4.4804 -0.6293 -1.1325 -0.0592 162  ASP C CG  
7642  O  OD1 . ASP C  164 ? 3.7017 3.0182 4.7390 -0.6409 -1.1358 -0.0403 162  ASP C OD1 
7643  O  OD2 . ASP C  164 ? 3.2397 2.7039 4.2582 -0.6320 -1.0996 0.0019  162  ASP C OD2 
7644  N  N   . SER C  165 ? 3.5704 2.7396 3.8890 -0.5018 -1.0881 -0.3114 163  SER C N   
7645  C  CA  . SER C  165 ? 3.7450 2.8395 3.8903 -0.4705 -1.1124 -0.3871 163  SER C CA  
7646  C  C   . SER C  165 ? 3.5313 2.6209 3.5431 -0.4207 -1.0287 -0.4162 163  SER C C   
7647  O  O   . SER C  165 ? 3.3647 2.5288 3.4173 -0.4129 -0.9510 -0.3746 163  SER C O   
7648  C  CB  . SER C  165 ? 3.8581 3.0093 3.9850 -0.4751 -1.1329 -0.3769 163  SER C CB  
7649  O  OG  . SER C  165 ? 3.7082 2.9743 3.8573 -0.4642 -1.0501 -0.3257 163  SER C OG  
7650  N  N   . PRO C  166 ? 3.7409 2.7448 3.5928 -0.3840 -1.0430 -0.4859 164  PRO C N   
7651  C  CA  . PRO C  166 ? 3.5992 2.6097 3.3299 -0.3356 -0.9613 -0.5065 164  PRO C CA  
7652  C  C   . PRO C  166 ? 3.4676 2.5912 3.1993 -0.3282 -0.8940 -0.4664 164  PRO C C   
7653  O  O   . PRO C  166 ? 3.4241 2.5794 3.1415 -0.3334 -0.9160 -0.4613 164  PRO C O   
7654  C  CB  . PRO C  166 ? 3.8676 2.7729 3.4324 -0.2976 -1.0009 -0.5818 164  PRO C CB  
7655  C  CG  . PRO C  166 ? 4.0540 2.9242 3.6427 -0.3261 -1.0987 -0.5971 164  PRO C CG  
7656  C  CD  . PRO C  166 ? 4.0426 2.9383 3.8154 -0.3815 -1.1348 -0.5488 164  PRO C CD  
7657  N  N   . GLU C  167 ? 3.4919 2.6745 3.2420 -0.3154 -0.8137 -0.4383 165  GLU C N   
7658  C  CA  . GLU C  167 ? 3.4727 2.7604 3.2404 -0.3112 -0.7491 -0.3983 165  GLU C CA  
7659  C  C   . GLU C  167 ? 3.5077 2.7938 3.1512 -0.2678 -0.6866 -0.4259 165  GLU C C   
7660  O  O   . GLU C  167 ? 3.5793 2.8073 3.1550 -0.2420 -0.6717 -0.4583 165  GLU C O   
7661  C  CB  . GLU C  167 ? 3.4117 2.7795 3.3099 -0.3317 -0.7089 -0.3388 165  GLU C CB  
7662  C  CG  . GLU C  167 ? 3.3132 2.7869 3.2613 -0.3373 -0.6668 -0.2913 165  GLU C CG  
7663  C  CD  . GLU C  167 ? 3.3518 2.9006 3.4283 -0.3540 -0.6365 -0.2310 165  GLU C CD  
7664  O  OE1 . GLU C  167 ? 3.3901 2.9110 3.5266 -0.3647 -0.6507 -0.2219 165  GLU C OE1 
7665  O  OE2 . GLU C  167 ? 3.3028 2.9370 3.4180 -0.3530 -0.5974 -0.1918 165  GLU C OE2 
7666  N  N   . TRP C  168 ? 3.4042 2.7547 3.0237 -0.2591 -0.6497 -0.4097 166  TRP C N   
7667  C  CA  . TRP C  168 ? 3.5053 2.8622 3.0208 -0.2213 -0.5922 -0.4283 166  TRP C CA  
7668  C  C   . TRP C  168 ? 3.3768 2.8265 2.9490 -0.2248 -0.5235 -0.3880 166  TRP C C   
7669  O  O   . TRP C  168 ? 3.3007 2.8140 2.9341 -0.2425 -0.5186 -0.3541 166  TRP C O   
7670  C  CB  . TRP C  168 ? 3.5339 2.8744 2.9606 -0.2038 -0.6125 -0.4485 166  TRP C CB  
7671  C  CG  . TRP C  168 ? 3.4725 2.7782 2.7691 -0.1573 -0.5763 -0.4808 166  TRP C CG  
7672  C  CD1 . TRP C  168 ? 3.5527 2.9047 2.8250 -0.1362 -0.5039 -0.4676 166  TRP C CD1 
7673  C  CD2 . TRP C  168 ? 3.3289 2.5487 2.5046 -0.1237 -0.6114 -0.5282 166  TRP C CD2 
7674  N  NE1 . TRP C  168 ? 3.3900 2.6961 2.5432 -0.0924 -0.4878 -0.4973 166  TRP C NE1 
7675  C  CE2 . TRP C  168 ? 3.3212 2.5456 2.4065 -0.0805 -0.5508 -0.5355 166  TRP C CE2 
7676  C  CE3 . TRP C  168 ? 3.4333 2.5718 2.5682 -0.1244 -0.6900 -0.5655 166  TRP C CE3 
7677  C  CZ2 . TRP C  168 ? 3.4029 2.5577 2.3546 -0.0330 -0.5600 -0.5747 166  TRP C CZ2 
7678  C  CZ3 . TRP C  168 ? 3.6694 2.7316 2.6625 -0.0771 -0.7040 -0.6121 166  TRP C CZ3 
7679  C  CH2 . TRP C  168 ? 3.6871 2.7599 2.5877 -0.0294 -0.6362 -0.6145 166  TRP C CH2 
7680  N  N   . LEU C  169 ? 3.3080 2.7645 2.8592 -0.2061 -0.4724 -0.3922 167  LEU C N   
7681  C  CA  . LEU C  169 ? 3.2544 2.7923 2.8528 -0.2076 -0.4124 -0.3607 167  LEU C CA  
7682  C  C   . LEU C  169 ? 3.3058 2.8556 2.8246 -0.1790 -0.3630 -0.3744 167  LEU C C   
7683  O  O   . LEU C  169 ? 3.5241 3.0237 2.9518 -0.1547 -0.3697 -0.4032 167  LEU C O   
7684  C  CB  . LEU C  169 ? 3.3482 2.8996 3.0067 -0.2125 -0.3942 -0.3459 167  LEU C CB  
7685  C  CG  . LEU C  169 ? 3.5118 3.1118 3.2883 -0.2414 -0.4079 -0.3030 167  LEU C CG  
7686  C  CD1 . LEU C  169 ? 3.6228 3.1722 3.4389 -0.2641 -0.4764 -0.3044 167  LEU C CD1 
7687  C  CD2 . LEU C  169 ? 3.5254 3.1560 3.3520 -0.2379 -0.3743 -0.2828 167  LEU C CD2 
7688  N  N   . SER C  170 ? 3.1243 2.7419 2.6800 -0.1803 -0.3137 -0.3518 168  SER C N   
7689  C  CA  . SER C  170 ? 3.1319 2.7691 2.6353 -0.1594 -0.2676 -0.3579 168  SER C CA  
7690  C  C   . SER C  170 ? 2.9133 2.6127 2.4669 -0.1629 -0.2227 -0.3396 168  SER C C   
7691  O  O   . SER C  170 ? 2.8940 2.6386 2.5186 -0.1806 -0.2231 -0.3162 168  SER C O   
7692  C  CB  . SER C  170 ? 3.2628 2.9161 2.7474 -0.1600 -0.2691 -0.3513 168  SER C CB  
7693  O  OG  . SER C  170 ? 3.2703 2.9771 2.8307 -0.1824 -0.2704 -0.3229 168  SER C OG  
7694  N  N   . PHE C  171 ? 2.8386 2.5425 2.3552 -0.1435 -0.1849 -0.3486 169  PHE C N   
7695  C  CA  . PHE C  171 ? 2.7948 2.5561 2.3526 -0.1454 -0.1466 -0.3357 169  PHE C CA  
7696  C  C   . PHE C  171 ? 2.7771 2.5607 2.3107 -0.1359 -0.1124 -0.3363 169  PHE C C   
7697  O  O   . PHE C  171 ? 2.9550 2.7097 2.4326 -0.1152 -0.0997 -0.3465 169  PHE C O   
7698  C  CB  . PHE C  171 ? 2.8269 2.5791 2.3854 -0.1340 -0.1356 -0.3403 169  PHE C CB  
7699  C  CG  . PHE C  171 ? 2.9386 2.6885 2.5491 -0.1469 -0.1596 -0.3294 169  PHE C CG  
7700  C  CD1 . PHE C  171 ? 3.1261 2.9372 2.8028 -0.1575 -0.1462 -0.3061 169  PHE C CD1 
7701  C  CD2 . PHE C  171 ? 3.0234 2.7088 2.6173 -0.1464 -0.1966 -0.3415 169  PHE C CD2 
7702  C  CE1 . PHE C  171 ? 3.1609 2.9751 2.8920 -0.1666 -0.1640 -0.2881 169  PHE C CE1 
7703  C  CE2 . PHE C  171 ? 3.1240 2.8067 2.7788 -0.1602 -0.2187 -0.3264 169  PHE C CE2 
7704  C  CZ  . PHE C  171 ? 3.1475 2.8979 2.8740 -0.1699 -0.1998 -0.2961 169  PHE C CZ  
7705  N  N   . ASP C  172 ? 2.6987 2.5323 2.2759 -0.1487 -0.0970 -0.3237 170  ASP C N   
7706  C  CA  . ASP C  172 ? 2.6859 2.5391 2.2556 -0.1449 -0.0685 -0.3222 170  ASP C CA  
7707  C  C   . ASP C  172 ? 2.6760 2.5515 2.2524 -0.1365 -0.0385 -0.3239 170  ASP C C   
7708  O  O   . ASP C  172 ? 2.6404 2.5578 2.2602 -0.1450 -0.0296 -0.3206 170  ASP C O   
7709  C  CB  . ASP C  172 ? 2.9834 2.8737 2.5966 -0.1598 -0.0665 -0.3120 170  ASP C CB  
7710  C  CG  . ASP C  172 ? 3.1977 3.0926 2.8036 -0.1578 -0.0456 -0.3100 170  ASP C CG  
7711  O  OD1 . ASP C  172 ? 3.2634 3.1541 2.8523 -0.1480 -0.0234 -0.3122 170  ASP C OD1 
7712  O  OD2 . ASP C  172 ? 3.2732 3.1769 2.8955 -0.1647 -0.0496 -0.3026 170  ASP C OD2 
7713  N  N   . VAL C  173 ? 2.7361 2.5874 2.2691 -0.1168 -0.0226 -0.3268 171  VAL C N   
7714  C  CA  . VAL C  173 ? 2.8721 2.7479 2.4166 -0.1068 0.0073  -0.3222 171  VAL C CA  
7715  C  C   . VAL C  173 ? 2.9255 2.8157 2.4735 -0.1028 0.0343  -0.3112 171  VAL C C   
7716  O  O   . VAL C  173 ? 2.9355 2.8290 2.4717 -0.0844 0.0601  -0.3017 171  VAL C O   
7717  C  CB  . VAL C  173 ? 3.0926 2.9333 2.5917 -0.0815 0.0102  -0.3276 171  VAL C CB  
7718  C  CG1 . VAL C  173 ? 3.2450 3.0781 2.7606 -0.0879 -0.0120 -0.3339 171  VAL C CG1 
7719  C  CG2 . VAL C  173 ? 3.0670 2.8511 2.4923 -0.0599 0.0008  -0.3354 171  VAL C CG2 
7720  N  N   . THR C  174 ? 2.8342 2.7339 2.4034 -0.1184 0.0304  -0.3083 172  THR C N   
7721  C  CA  . THR C  174 ? 2.7991 2.7074 2.3791 -0.1160 0.0548  -0.2947 172  THR C CA  
7722  C  C   . THR C  174 ? 2.7388 2.6878 2.3719 -0.1224 0.0778  -0.2864 172  THR C C   
7723  O  O   . THR C  174 ? 2.7890 2.7440 2.4253 -0.1091 0.1045  -0.2684 172  THR C O   
7724  C  CB  . THR C  174 ? 2.8861 2.7953 2.4857 -0.1322 0.0450  -0.2941 172  THR C CB  
7725  O  OG1 . THR C  174 ? 2.9828 2.8588 2.5371 -0.1253 0.0230  -0.2966 172  THR C OG1 
7726  C  CG2 . THR C  174 ? 2.9600 2.8769 2.5830 -0.1319 0.0708  -0.2777 172  THR C CG2 
7727  N  N   . GLY C  175 ? 2.8420 2.8228 2.5194 -0.1408 0.0670  -0.2967 173  GLY C N   
7728  C  CA  . GLY C  175 ? 2.8480 2.8701 2.5793 -0.1494 0.0804  -0.2916 173  GLY C CA  
7729  C  C   . GLY C  175 ? 2.8636 2.8963 2.5881 -0.1305 0.0992  -0.2786 173  GLY C C   
7730  O  O   . GLY C  175 ? 2.8929 2.9588 2.6634 -0.1329 0.1171  -0.2637 173  GLY C O   
7731  N  N   . VAL C  176 ? 2.9329 2.9364 2.6039 -0.1107 0.0948  -0.2829 174  VAL C N   
7732  C  CA  . VAL C  176 ? 3.0543 3.0599 2.7087 -0.0857 0.1152  -0.2710 174  VAL C CA  
7733  C  C   . VAL C  176 ? 3.1227 3.1079 2.7424 -0.0597 0.1426  -0.2519 174  VAL C C   
7734  O  O   . VAL C  176 ? 3.1867 3.1992 2.8294 -0.0449 0.1723  -0.2281 174  VAL C O   
7735  C  CB  . VAL C  176 ? 3.0667 3.0404 2.6769 -0.0725 0.0985  -0.2851 174  VAL C CB  
7736  C  CG1 . VAL C  176 ? 3.1979 3.1642 2.7815 -0.0402 0.1220  -0.2739 174  VAL C CG1 
7737  C  CG2 . VAL C  176 ? 2.9353 2.9394 2.5868 -0.0934 0.0780  -0.2945 174  VAL C CG2 
7738  N  N   . VAL C  177 ? 3.0748 3.0165 2.6404 -0.0512 0.1338  -0.2581 175  VAL C N   
7739  C  CA  . VAL C  177 ? 3.1413 3.0625 2.6603 -0.0192 0.1597  -0.2391 175  VAL C CA  
7740  C  C   . VAL C  177 ? 3.1967 3.1587 2.7799 -0.0276 0.1888  -0.2085 175  VAL C C   
7741  O  O   . VAL C  177 ? 3.2248 3.1984 2.8039 0.0002  0.2240  -0.1785 175  VAL C O   
7742  C  CB  . VAL C  177 ? 3.1223 2.9923 2.5714 -0.0104 0.1373  -0.2536 175  VAL C CB  
7743  C  CG1 . VAL C  177 ? 3.2056 3.0567 2.5966 0.0291  0.1644  -0.2330 175  VAL C CG1 
7744  C  CG2 . VAL C  177 ? 3.0538 2.8814 2.4528 -0.0061 0.1035  -0.2824 175  VAL C CG2 
7745  N  N   . ARG C  178 ? 3.2570 3.2403 2.9032 -0.0642 0.1750  -0.2139 176  ARG C N   
7746  C  CA  . ARG C  178 ? 3.3004 3.3142 3.0164 -0.0770 0.1967  -0.1874 176  ARG C CA  
7747  C  C   . ARG C  178 ? 3.3134 3.3746 3.0917 -0.0753 0.2203  -0.1630 176  ARG C C   
7748  O  O   . ARG C  178 ? 3.3441 3.4262 3.1600 -0.0648 0.2521  -0.1255 176  ARG C O   
7749  C  CB  . ARG C  178 ? 3.2445 3.2642 3.0118 -0.1151 0.1722  -0.2058 176  ARG C CB  
7750  C  CG  . ARG C  178 ? 3.2577 3.3044 3.1112 -0.1349 0.1867  -0.1845 176  ARG C CG  
7751  C  CD  . ARG C  178 ? 3.2875 3.3255 3.1751 -0.1658 0.1614  -0.2080 176  ARG C CD  
7752  N  NE  . ARG C  178 ? 3.3393 3.3400 3.1839 -0.1586 0.1597  -0.2083 176  ARG C NE  
7753  C  CZ  . ARG C  178 ? 3.4074 3.3845 3.1986 -0.1570 0.1365  -0.2318 176  ARG C CZ  
7754  N  NH1 . ARG C  178 ? 3.4374 3.4223 3.2123 -0.1617 0.1149  -0.2558 176  ARG C NH1 
7755  N  NH2 . ARG C  178 ? 3.4210 3.3703 3.1813 -0.1502 0.1354  -0.2267 176  ARG C NH2 
7756  N  N   . GLN C  179 ? 3.3479 3.4313 3.1435 -0.0843 0.2060  -0.1787 177  GLN C N   
7757  C  CA  . GLN C  179 ? 3.3372 3.4720 3.1967 -0.0830 0.2253  -0.1538 177  GLN C CA  
7758  C  C   . GLN C  179 ? 3.3596 3.4912 3.1744 -0.0373 0.2615  -0.1255 177  GLN C C   
7759  O  O   . GLN C  179 ? 3.4339 3.6102 3.3055 -0.0280 0.2905  -0.0883 177  GLN C O   
7760  C  CB  . GLN C  179 ? 3.2237 3.3862 3.1106 -0.1025 0.1988  -0.1775 177  GLN C CB  
7761  C  CG  . GLN C  179 ? 3.1974 3.3659 3.1216 -0.1405 0.1643  -0.2063 177  GLN C CG  
7762  C  CD  . GLN C  179 ? 3.2736 3.4704 3.2102 -0.1512 0.1397  -0.2278 177  GLN C CD  
7763  O  OE1 . GLN C  179 ? 3.3466 3.5607 3.2730 -0.1333 0.1486  -0.2192 177  GLN C OE1 
7764  N  NE2 . GLN C  179 ? 3.2273 3.4288 3.1829 -0.1761 0.1104  -0.2544 177  GLN C NE2 
7765  N  N   . TRP C  180 ? 3.1757 3.2548 2.8906 -0.0066 0.2593  -0.1418 178  TRP C N   
7766  C  CA  . TRP C  180 ? 3.2112 3.2769 2.8666 0.0440  0.2917  -0.1215 178  TRP C CA  
7767  C  C   . TRP C  180 ? 3.2710 3.3385 2.9141 0.0741  0.3301  -0.0823 178  TRP C C   
7768  O  O   . TRP C  180 ? 3.3615 3.4413 2.9848 0.1173  0.3687  -0.0502 178  TRP C O   
7769  C  CB  . TRP C  180 ? 3.1930 3.1930 2.7428 0.0670  0.2699  -0.1573 178  TRP C CB  
7770  C  CG  . TRP C  180 ? 3.1609 3.1628 2.7204 0.0542  0.2468  -0.1812 178  TRP C CG  
7771  C  CD1 . TRP C  180 ? 3.2415 3.2992 2.8837 0.0272  0.2431  -0.1755 178  TRP C CD1 
7772  C  CD2 . TRP C  180 ? 3.1267 3.0725 2.6135 0.0689  0.2231  -0.2125 178  TRP C CD2 
7773  N  NE1 . TRP C  180 ? 3.2646 3.3083 2.8880 0.0271  0.2228  -0.1979 178  TRP C NE1 
7774  C  CE2 . TRP C  180 ? 3.2627 3.2362 2.7961 0.0508  0.2106  -0.2199 178  TRP C CE2 
7775  C  CE3 . TRP C  180 ? 3.1566 3.0305 2.5460 0.0953  0.2081  -0.2350 178  TRP C CE3 
7776  C  CZ2 . TRP C  180 ? 3.2757 3.2073 2.7685 0.0578  0.1878  -0.2444 178  TRP C CZ2 
7777  C  CZ3 . TRP C  180 ? 3.1690 2.9973 2.5195 0.0991  0.1802  -0.2638 178  TRP C CZ3 
7778  C  CH2 . TRP C  180 ? 3.2147 3.0718 2.6202 0.0802  0.1723  -0.2662 178  TRP C CH2 
7779  N  N   . LEU C  181 ? 3.2125 3.2696 2.8664 0.0564  0.3233  -0.0805 179  LEU C N   
7780  C  CA  . LEU C  181 ? 3.3110 3.3744 2.9599 0.0856  0.3619  -0.0372 179  LEU C CA  
7781  C  C   . LEU C  181 ? 3.3997 3.5285 3.1706 0.0699  0.3923  0.0124  179  LEU C C   
7782  O  O   . LEU C  181 ? 3.4792 3.6271 3.2599 0.1020  0.4354  0.0625  179  LEU C O   
7783  C  CB  . LEU C  181 ? 3.2572 3.2847 2.8733 0.0749  0.3439  -0.0503 179  LEU C CB  
7784  C  CG  . LEU C  181 ? 3.2879 3.2554 2.7740 0.1133  0.3326  -0.0723 179  LEU C CG  
7785  C  CD1 . LEU C  181 ? 3.3257 3.2552 2.7477 0.1162  0.2990  -0.1184 179  LEU C CD1 
7786  C  CD2 . LEU C  181 ? 3.2408 3.1851 2.7169 0.0937  0.3104  -0.0831 179  LEU C CD2 
7787  N  N   . SER C  182 ? 3.4281 3.5929 3.2938 0.0227  0.3696  0.0014  180  SER C N   
7788  C  CA  . SER C  182 ? 3.3686 3.5966 3.3599 0.0036  0.3899  0.0457  180  SER C CA  
7789  C  C   . SER C  182 ? 3.4665 3.7394 3.4789 0.0325  0.4198  0.0783  180  SER C C   
7790  O  O   . SER C  182 ? 3.5747 3.9027 3.6808 0.0344  0.4511  0.1330  180  SER C O   
7791  C  CB  . SER C  182 ? 3.1819 3.4276 3.2613 -0.0568 0.3472  0.0163  180  SER C CB  
7792  O  OG  . SER C  182 ? 3.1590 3.4083 3.2178 -0.0678 0.3173  -0.0226 180  SER C OG  
7793  N  N   . ARG C  183 ? 3.4476 3.6987 3.3808 0.0560  0.4120  0.0501  181  ARG C N   
7794  C  CA  . ARG C  183 ? 3.3390 3.6293 3.2866 0.0868  0.4404  0.0789  181  ARG C CA  
7795  C  C   . ARG C  183 ? 3.4611 3.7314 3.3226 0.1566  0.4897  0.1120  181  ARG C C   
7796  O  O   . ARG C  183 ? 3.5588 3.7679 3.3121 0.1842  0.4880  0.0908  181  ARG C O   
7797  C  CB  . ARG C  183 ? 3.1698 3.4451 3.0792 0.0800  0.4091  0.0342  181  ARG C CB  
7798  C  CG  . ARG C  183 ? 3.1430 3.4301 3.1104 0.0203  0.3588  -0.0044 181  ARG C CG  
7799  C  CD  . ARG C  183 ? 3.3302 3.6000 3.2519 0.0190  0.3309  -0.0444 181  ARG C CD  
7800  N  NE  . ARG C  183 ? 3.3300 3.6004 3.2812 -0.0291 0.2843  -0.0838 181  ARG C NE  
7801  C  CZ  . ARG C  183 ? 3.2421 3.5674 3.2814 -0.0635 0.2639  -0.0845 181  ARG C CZ  
7802  N  NH1 . ARG C  183 ? 3.2167 3.6045 3.3340 -0.0604 0.2833  -0.0460 181  ARG C NH1 
7803  N  NH2 . ARG C  183 ? 3.1218 3.4412 3.1702 -0.0985 0.2232  -0.1226 181  ARG C NH2 
7804  N  N   . GLY C  184 ? 3.4273 3.7519 3.3366 0.1878  0.5332  0.1655  182  GLY C N   
7805  C  CA  . GLY C  184 ? 3.5571 3.8668 3.3797 0.2632  0.5843  0.1987  182  GLY C CA  
7806  C  C   . GLY C  184 ? 3.6961 3.9588 3.4084 0.3050  0.5815  0.1641  182  GLY C C   
7807  O  O   . GLY C  184 ? 3.7810 4.0304 3.4176 0.3740  0.6251  0.1899  182  GLY C O   
7808  N  N   . GLY C  185 ? 3.6834 3.9191 3.3847 0.2682  0.5328  0.1084  183  GLY C N   
7809  C  CA  . GLY C  185 ? 3.6751 3.8604 3.2818 0.3029  0.5260  0.0747  183  GLY C CA  
7810  C  C   . GLY C  185 ? 3.6399 3.7335 3.0970 0.3461  0.5198  0.0395  183  GLY C C   
7811  O  O   . GLY C  185 ? 3.5594 3.6038 2.9773 0.3153  0.4757  -0.0062 183  GLY C O   
7812  N  N   . GLU C  186 ? 3.5827 3.6529 2.9539 0.4200  0.5622  0.0605  184  GLU C N   
7813  C  CA  . GLU C  186 ? 3.5341 3.5163 2.7540 0.4696  0.5563  0.0282  184  GLU C CA  
7814  C  C   . GLU C  186 ? 3.5483 3.4454 2.6774 0.4732  0.5119  -0.0376 184  GLU C C   
7815  O  O   . GLU C  186 ? 3.5843 3.4005 2.5820 0.5182  0.5015  -0.0698 184  GLU C O   
7816  C  CB  . GLU C  186 ? 3.6358 3.6232 2.7887 0.5554  0.6202  0.0758  184  GLU C CB  
7817  C  CG  . GLU C  186 ? 3.5444 3.6083 2.7768 0.5603  0.6670  0.1468  184  GLU C CG  
7818  C  CD  . GLU C  186 ? 3.6228 3.6799 2.7607 0.6537  0.7280  0.1906  184  GLU C CD  
7819  O  OE1 . GLU C  186 ? 3.7129 3.6934 2.7046 0.7155  0.7272  0.1553  184  GLU C OE1 
7820  O  OE2 . GLU C  186 ? 3.5132 3.6404 2.7233 0.6676  0.7766  0.2614  184  GLU C OE2 
7821  N  N   . ILE C  187 ? 3.4491 3.3614 2.6454 0.4283  0.4837  -0.0573 185  ILE C N   
7822  C  CA  . ILE C  187 ? 3.4309 3.2666 2.5614 0.4257  0.4409  -0.1138 185  ILE C CA  
7823  C  C   . ILE C  187 ? 3.3243 3.1888 2.5487 0.3502  0.3963  -0.1350 185  ILE C C   
7824  O  O   . ILE C  187 ? 3.2708 3.2113 2.6010 0.3218  0.4077  -0.1074 185  ILE C O   
7825  C  CB  . ILE C  187 ? 3.4345 3.2489 2.5231 0.4806  0.4691  -0.1079 185  ILE C CB  
7826  C  CG1 . ILE C  187 ? 3.4168 3.1555 2.4627 0.4677  0.4214  -0.1630 185  ILE C CG1 
7827  C  CG2 . ILE C  187 ? 3.3238 3.2381 2.5302 0.4739  0.5090  -0.0531 185  ILE C CG2 
7828  C  CD1 . ILE C  187 ? 3.4673 3.1027 2.3973 0.4785  0.3780  -0.2169 185  ILE C CD1 
7829  N  N   . GLU C  188 ? 3.4602 3.2674 2.6466 0.3201  0.3450  -0.1817 186  GLU C N   
7830  C  CA  . GLU C  188 ? 3.5672 3.3944 2.8279 0.2563  0.3028  -0.2028 186  GLU C CA  
7831  C  C   . GLU C  188 ? 3.6673 3.4088 2.8595 0.2542  0.2563  -0.2515 186  GLU C C   
7832  O  O   . GLU C  188 ? 3.8506 3.5170 2.9423 0.3003  0.2547  -0.2717 186  GLU C O   
7833  C  CB  . GLU C  188 ? 3.5698 3.4391 2.8913 0.2089  0.2900  -0.1958 186  GLU C CB  
7834  C  CG  . GLU C  188 ? 3.5889 3.5413 2.9971 0.2019  0.3286  -0.1479 186  GLU C CG  
7835  C  CD  . GLU C  188 ? 3.6046 3.6272 3.1149 0.1732  0.3308  -0.1320 186  GLU C CD  
7836  O  OE1 . GLU C  188 ? 3.7125 3.7240 3.2287 0.1552  0.3024  -0.1575 186  GLU C OE1 
7837  O  OE2 . GLU C  188 ? 3.5055 3.5970 3.0941 0.1688  0.3597  -0.0913 186  GLU C OE2 
7838  N  N   . GLY C  189 ? 3.5729 3.3242 2.8203 0.2025  0.2172  -0.2698 187  GLY C N   
7839  C  CA  . GLY C  189 ? 3.6007 3.2782 2.8046 0.1944  0.1714  -0.3088 187  GLY C CA  
7840  C  C   . GLY C  189 ? 3.5539 3.2651 2.8399 0.1403  0.1398  -0.3141 187  GLY C C   
7841  O  O   . GLY C  189 ? 3.4379 3.2263 2.8052 0.1113  0.1514  -0.2929 187  GLY C O   
7842  N  N   . PHE C  190 ? 3.5158 3.1664 2.7789 0.1292  0.0979  -0.3424 188  PHE C N   
7843  C  CA  . PHE C  190 ? 3.2387 2.9139 2.5728 0.0850  0.0678  -0.3445 188  PHE C CA  
7844  C  C   . PHE C  190 ? 3.2445 2.8735 2.5773 0.0941  0.0514  -0.3545 188  PHE C C   
7845  O  O   . PHE C  190 ? 3.3958 2.9620 2.6653 0.1332  0.0576  -0.3668 188  PHE C O   
7846  C  CB  . PHE C  190 ? 3.1293 2.7850 2.4604 0.0543  0.0292  -0.3601 188  PHE C CB  
7847  C  CG  . PHE C  190 ? 3.0652 2.7658 2.4080 0.0416  0.0434  -0.3486 188  PHE C CG  
7848  C  CD1 . PHE C  190 ? 2.9510 2.7226 2.3709 0.0073  0.0477  -0.3333 188  PHE C CD1 
7849  C  CD2 . PHE C  190 ? 3.2185 2.8870 2.4925 0.0667  0.0517  -0.3533 188  PHE C CD2 
7850  C  CE1 . PHE C  190 ? 2.9033 2.7077 2.3372 -0.0047 0.0592  -0.3242 188  PHE C CE1 
7851  C  CE2 . PHE C  190 ? 3.1721 2.8802 2.4635 0.0553  0.0663  -0.3386 188  PHE C CE2 
7852  C  CZ  . PHE C  190 ? 3.0113 2.7846 2.3856 0.0180  0.0694  -0.3248 188  PHE C CZ  
7853  N  N   . ARG C  191 ? 2.8964 2.5551 2.2997 0.0604  0.0312  -0.3475 189  ARG C N   
7854  C  CA  . ARG C  191 ? 2.9784 2.5991 2.3990 0.0633  0.0143  -0.3503 189  ARG C CA  
7855  C  C   . ARG C  191 ? 2.9468 2.5716 2.4217 0.0235  -0.0245 -0.3497 189  ARG C C   
7856  O  O   . ARG C  191 ? 2.9539 2.6484 2.4814 -0.0041 -0.0225 -0.3343 189  ARG C O   
7857  C  CB  . ARG C  191 ? 3.1236 2.8025 2.5940 0.0745  0.0474  -0.3235 189  ARG C CB  
7858  C  CG  . ARG C  191 ? 3.2750 2.9323 2.7856 0.0712  0.0318  -0.3169 189  ARG C CG  
7859  C  CD  . ARG C  191 ? 3.3203 3.0637 2.8985 0.0716  0.0601  -0.2839 189  ARG C CD  
7860  N  NE  . ARG C  191 ? 3.2439 2.9745 2.8682 0.0685  0.0477  -0.2706 189  ARG C NE  
7861  C  CZ  . ARG C  191 ? 3.1824 2.9836 2.8671 0.0699  0.0662  -0.2398 189  ARG C CZ  
7862  N  NH1 . ARG C  191 ? 3.0871 2.9755 2.7931 0.0719  0.0930  -0.2232 189  ARG C NH1 
7863  N  NH2 . ARG C  191 ? 3.2762 3.0616 3.0035 0.0694  0.0561  -0.2239 189  ARG C NH2 
7864  N  N   . LEU C  192 ? 3.1362 2.6859 2.6011 0.0222  -0.0600 -0.3651 190  LEU C N   
7865  C  CA  . LEU C  192 ? 3.1252 2.6789 2.6532 -0.0140 -0.0969 -0.3571 190  LEU C CA  
7866  C  C   . LEU C  192 ? 3.3691 2.8968 2.9428 -0.0114 -0.1052 -0.3451 190  LEU C C   
7867  O  O   . LEU C  192 ? 3.5666 3.0031 3.1082 0.0005  -0.1317 -0.3668 190  LEU C O   
7868  C  CB  . LEU C  192 ? 3.1226 2.6121 2.6116 -0.0262 -0.1413 -0.3829 190  LEU C CB  
7869  C  CG  . LEU C  192 ? 3.0593 2.5705 2.6214 -0.0660 -0.1764 -0.3676 190  LEU C CG  
7870  C  CD1 . LEU C  192 ? 3.0911 2.5964 2.6209 -0.0791 -0.1983 -0.3813 190  LEU C CD1 
7871  C  CD2 . LEU C  192 ? 3.1337 2.5777 2.7291 -0.0749 -0.2172 -0.3706 190  LEU C CD2 
7872  N  N   . SER C  193 ? 3.3440 2.9492 2.9910 -0.0204 -0.0838 -0.3111 191  SER C N   
7873  C  CA  . SER C  193 ? 3.3787 2.9728 3.0828 -0.0190 -0.0882 -0.2900 191  SER C CA  
7874  C  C   . SER C  193 ? 3.2371 2.8594 3.0219 -0.0531 -0.1154 -0.2652 191  SER C C   
7875  O  O   . SER C  193 ? 3.1195 2.7414 2.9036 -0.0757 -0.1400 -0.2731 191  SER C O   
7876  C  CB  . SER C  193 ? 3.4566 3.1210 3.1850 0.0015  -0.0438 -0.2638 191  SER C CB  
7877  O  OG  . SER C  193 ? 3.4642 3.2301 3.2273 -0.0131 -0.0261 -0.2442 191  SER C OG  
7878  N  N   . ALA C  194 ? 3.2533 2.9046 3.1108 -0.0541 -0.1085 -0.2303 192  ALA C N   
7879  C  CA  . ALA C  194 ? 3.2381 2.9214 3.1812 -0.0806 -0.1285 -0.1966 192  ALA C CA  
7880  C  C   . ALA C  194 ? 3.2475 3.0431 3.2436 -0.0762 -0.0939 -0.1549 192  ALA C C   
7881  O  O   . ALA C  194 ? 3.4270 3.2765 3.3923 -0.0594 -0.0616 -0.1579 192  ALA C O   
7882  C  CB  . ALA C  194 ? 3.2687 2.8768 3.2602 -0.0854 -0.1578 -0.1872 192  ALA C CB  
7883  N  N   . HIS C  195 ? 2.9949 2.8271 3.0730 -0.0901 -0.1024 -0.1139 193  HIS C N   
7884  C  CA  . HIS C  195 ? 2.9308 2.8691 3.0537 -0.0807 -0.0718 -0.0727 193  HIS C CA  
7885  C  C   . HIS C  195 ? 2.9848 2.9428 3.1257 -0.0546 -0.0446 -0.0506 193  HIS C C   
7886  O  O   . HIS C  195 ? 3.0756 2.9679 3.2377 -0.0496 -0.0536 -0.0461 193  HIS C O   
7887  C  CB  . HIS C  195 ? 2.9556 2.9291 3.1616 -0.0968 -0.0849 -0.0285 193  HIS C CB  
7888  C  CG  . HIS C  195 ? 2.9578 3.0408 3.1992 -0.0807 -0.0535 0.0140  193  HIS C CG  
7889  N  ND1 . HIS C  195 ? 2.9025 3.0509 3.0951 -0.0710 -0.0338 -0.0014 193  HIS C ND1 
7890  C  CD2 . HIS C  195 ? 2.9814 3.1188 3.2995 -0.0695 -0.0393 0.0715  193  HIS C CD2 
7891  C  CE1 . HIS C  195 ? 2.9173 3.1529 3.1460 -0.0526 -0.0114 0.0398  193  HIS C CE1 
7892  N  NE2 . HIS C  195 ? 2.9621 3.1966 3.2661 -0.0496 -0.0116 0.0872  193  HIS C NE2 
7893  N  N   . CYS C  196 ? 2.9640 3.0108 3.0959 -0.0369 -0.0133 -0.0379 194  CYS C N   
7894  C  CA  . CYS C  196 ? 2.9713 3.0591 3.1268 -0.0102 0.0141  -0.0090 194  CYS C CA  
7895  C  C   . CYS C  196 ? 2.8704 3.0547 3.0842 -0.0017 0.0286  0.0415  194  CYS C C   
7896  O  O   . CYS C  196 ? 2.6857 2.9413 2.8796 -0.0001 0.0361  0.0387  194  CYS C O   
7897  C  CB  . CYS C  196 ? 3.0530 3.1703 3.1506 0.0076  0.0365  -0.0335 194  CYS C CB  
7898  S  SG  . CYS C  196 ? 3.1130 3.1416 3.1285 0.0054  0.0291  -0.0899 194  CYS C SG  
7899  N  N   . SER C  197 ? 2.9694 3.1539 3.2535 0.0065  0.0330  0.0883  195  SER C N   
7900  C  CA  . SER C  197 ? 2.8314 3.1083 3.1745 0.0211  0.0505  0.1455  195  SER C CA  
7901  C  C   . SER C  197 ? 2.7976 3.1448 3.1374 0.0553  0.0816  0.1686  195  SER C C   
7902  O  O   . SER C  197 ? 2.8146 3.1341 3.1845 0.0690  0.0916  0.1892  195  SER C O   
7903  C  CB  . SER C  197 ? 2.9430 3.1880 3.3780 0.0107  0.0389  0.1929  195  SER C CB  
7904  O  OG  . SER C  197 ? 3.0624 3.2422 3.5259 0.0169  0.0387  0.2009  195  SER C OG  
7905  N  N   . CYS C  198 ? 2.9750 3.4115 3.2786 0.0702  0.0947  0.1648  196  CYS C N   
7906  C  CA  . CYS C  198 ? 3.0403 3.5563 3.3403 0.1034  0.1192  0.1876  196  CYS C CA  
7907  C  C   . CYS C  198 ? 2.8717 3.4937 3.1702 0.1247  0.1297  0.2144  196  CYS C C   
7908  O  O   . CYS C  198 ? 2.7819 3.4141 3.0922 0.1169  0.1231  0.2243  196  CYS C O   
7909  C  CB  . CYS C  198 ? 3.1420 3.6525 3.3805 0.1043  0.1202  0.1410  196  CYS C CB  
7910  S  SG  . CYS C  198 ? 3.2219 3.7770 3.3942 0.0917  0.1077  0.0919  196  CYS C SG  
7911  N  N   . ILE C  209 ? 3.6386 3.2863 3.9275 0.0120  -0.0483 0.0090  207  ILE C N   
7912  C  CA  . ILE C  209 ? 3.6070 3.2175 3.8069 0.0003  -0.0688 -0.0488 207  ILE C CA  
7913  C  C   . ILE C  209 ? 3.6928 3.2312 3.9205 -0.0355 -0.1224 -0.0640 207  ILE C C   
7914  O  O   . ILE C  209 ? 3.7108 3.1489 3.9659 -0.0412 -0.1543 -0.0722 207  ILE C O   
7915  C  CB  . ILE C  209 ? 3.6632 3.1996 3.7654 0.0304  -0.0587 -0.0964 207  ILE C CB  
7916  C  CG1 . ILE C  209 ? 3.7051 3.2141 3.8337 0.0621  -0.0346 -0.0730 207  ILE C CG1 
7917  C  CG2 . ILE C  209 ? 3.5940 3.2057 3.6269 0.0435  -0.0272 -0.1127 207  ILE C CG2 
7918  C  CD1 . ILE C  209 ? 3.8041 3.2104 3.8440 0.0947  -0.0317 -0.1188 207  ILE C CD1 
7919  N  N   . ASN C  210 ? 3.7733 3.3622 3.9970 -0.0593 -0.1342 -0.0676 208  ASN C N   
7920  C  CA  . ASN C  210 ? 3.8413 3.3887 4.1059 -0.0952 -0.1832 -0.0711 208  ASN C CA  
7921  C  C   . ASN C  210 ? 3.8850 3.3613 4.0519 -0.1025 -0.2144 -0.1353 208  ASN C C   
7922  O  O   . ASN C  210 ? 3.9363 3.3633 4.0087 -0.0769 -0.2035 -0.1780 208  ASN C O   
7923  C  CB  . ASN C  210 ? 3.6613 3.3214 3.9974 -0.1121 -0.1715 -0.0212 208  ASN C CB  
7924  C  CG  . ASN C  210 ? 3.4525 3.1949 3.8676 -0.0953 -0.1339 0.0428  208  ASN C CG  
7925  O  OD1 . ASN C  210 ? 3.3268 3.1521 3.7121 -0.0712 -0.0922 0.0534  208  ASN C OD1 
7926  N  ND2 . ASN C  210 ? 3.4804 3.2017 4.0003 -0.1074 -0.1501 0.0877  208  ASN C ND2 
7927  N  N   . GLY C  211 ? 3.8616 3.3368 4.0537 -0.1342 -0.2516 -0.1372 209  GLY C N   
7928  C  CA  . GLY C  211 ? 3.7842 3.2129 3.8927 -0.1433 -0.2816 -0.1888 209  GLY C CA  
7929  C  C   . GLY C  211 ? 3.7932 3.0890 3.8374 -0.1409 -0.3291 -0.2439 209  GLY C C   
7930  O  O   . GLY C  211 ? 3.7507 3.0060 3.7762 -0.1618 -0.3750 -0.2693 209  GLY C O   
7931  N  N   . PHE C  212 ? 3.9106 3.1358 3.9147 -0.1121 -0.3201 -0.2643 210  PHE C N   
7932  C  CA  . PHE C  212 ? 4.1170 3.2070 4.0443 -0.1006 -0.3639 -0.3219 210  PHE C CA  
7933  C  C   . PHE C  212 ? 4.1479 3.1615 4.1315 -0.0951 -0.3781 -0.3125 210  PHE C C   
7934  O  O   . PHE C  212 ? 4.1099 3.1569 4.1145 -0.0709 -0.3311 -0.2844 210  PHE C O   
7935  C  CB  . PHE C  212 ? 4.2289 3.2938 4.0176 -0.0577 -0.3333 -0.3670 210  PHE C CB  
7936  C  CG  . PHE C  212 ? 4.1525 3.2934 3.8897 -0.0603 -0.3128 -0.3724 210  PHE C CG  
7937  C  CD1 . PHE C  212 ? 3.9871 3.2520 3.7663 -0.0650 -0.2644 -0.3319 210  PHE C CD1 
7938  C  CD2 . PHE C  212 ? 4.2117 3.2968 3.8543 -0.0545 -0.3420 -0.4192 210  PHE C CD2 
7939  C  CE1 . PHE C  212 ? 3.9521 3.2786 3.6891 -0.0679 -0.2473 -0.3379 210  PHE C CE1 
7940  C  CE2 . PHE C  212 ? 4.1307 3.2839 3.7318 -0.0558 -0.3206 -0.4202 210  PHE C CE2 
7941  C  CZ  . PHE C  212 ? 4.0348 3.3060 3.6866 -0.0640 -0.2736 -0.3799 210  PHE C CZ  
7942  N  N   . THR C  213 ? 4.2925 3.2035 4.3045 -0.1178 -0.4452 -0.3349 211  THR C N   
7943  C  CA  . THR C  213 ? 4.2948 3.1235 4.3766 -0.1192 -0.4676 -0.3247 211  THR C CA  
7944  C  C   . THR C  213 ? 4.4297 3.1013 4.4085 -0.0909 -0.5051 -0.3951 211  THR C C   
7945  O  O   . THR C  213 ? 4.4400 3.0293 4.4603 -0.0835 -0.5188 -0.3939 211  THR C O   
7946  C  CB  . THR C  213 ? 4.1887 3.0221 4.4165 -0.1715 -0.5190 -0.2847 211  THR C CB  
7947  O  OG1 . THR C  213 ? 4.1678 2.9290 4.3621 -0.1968 -0.5909 -0.3313 211  THR C OG1 
7948  C  CG2 . THR C  213 ? 3.9388 2.9275 4.2590 -0.1917 -0.4789 -0.2142 211  THR C CG2 
7949  N  N   . THR C  214 ? 4.6569 3.2833 4.5012 -0.0714 -0.5209 -0.4550 212  THR C N   
7950  C  CA  . THR C  214 ? 4.8409 3.3200 4.5641 -0.0343 -0.5532 -0.5258 212  THR C CA  
7951  C  C   . THR C  214 ? 4.9195 3.4139 4.5140 0.0264  -0.4864 -0.5449 212  THR C C   
7952  O  O   . THR C  214 ? 4.7604 3.3688 4.3338 0.0321  -0.4350 -0.5217 212  THR C O   
7953  C  CB  . THR C  214 ? 4.8250 3.2324 4.4840 -0.0516 -0.6276 -0.5807 212  THR C CB  
7954  O  OG1 . THR C  214 ? 4.8098 3.2490 4.6040 -0.1135 -0.6793 -0.5474 212  THR C OG1 
7955  C  CG2 . THR C  214 ? 4.8600 3.0932 4.4215 -0.0208 -0.6819 -0.6533 212  THR C CG2 
7956  N  N   . GLY C  215 ? 5.0502 3.4264 4.5618 0.0729  -0.4885 -0.5864 213  GLY C N   
7957  C  CA  . GLY C  215 ? 4.9519 3.3284 4.3418 0.1369  -0.4275 -0.6037 213  GLY C CA  
7958  C  C   . GLY C  215 ? 4.9913 3.2983 4.2175 0.1762  -0.4440 -0.6675 213  GLY C C   
7959  O  O   . GLY C  215 ? 4.9547 3.2686 4.0802 0.2332  -0.3890 -0.6764 213  GLY C O   
7960  N  N   . ARG C  216 ? 4.9890 3.2335 4.1866 0.1504  -0.5173 -0.7088 214  ARG C N   
7961  C  CA  . ARG C  216 ? 5.0093 3.1963 4.0461 0.1909  -0.5329 -0.7665 214  ARG C CA  
7962  C  C   . ARG C  216 ? 4.9550 3.2720 3.9648 0.1900  -0.4853 -0.7402 214  ARG C C   
7963  O  O   . ARG C  216 ? 5.0380 3.3333 3.9128 0.2366  -0.4709 -0.7727 214  ARG C O   
7964  C  CB  . ARG C  216 ? 4.9330 3.0116 3.9479 0.1640  -0.6328 -0.8200 214  ARG C CB  
7965  C  CG  . ARG C  216 ? 4.8908 2.8335 3.9495 0.1546  -0.6935 -0.8478 214  ARG C CG  
7966  C  CD  . ARG C  216 ? 4.8601 2.7011 3.9002 0.1246  -0.7991 -0.9020 214  ARG C CD  
7967  N  NE  . ARG C  216 ? 4.8726 2.5594 3.9309 0.1243  -0.8629 -0.9417 214  ARG C NE  
7968  C  CZ  . ARG C  216 ? 5.0036 2.5705 4.0389 0.1047  -0.9644 -0.9998 214  ARG C CZ  
7969  N  NH1 . ARG C  216 ? 4.9408 2.5308 3.9314 0.0856  -1.0115 -1.0223 214  ARG C NH1 
7970  N  NH2 . ARG C  216 ? 5.2648 2.6872 4.3237 0.1041  -1.0214 -1.0355 214  ARG C NH2 
7971  N  N   . ARG C  217 ? 4.8508 3.2986 3.9856 0.1401  -0.4618 -0.6819 215  ARG C N   
7972  C  CA  . ARG C  217 ? 4.6800 3.2532 3.8126 0.1299  -0.4211 -0.6532 215  ARG C CA  
7973  C  C   . ARG C  217 ? 4.6419 3.1951 3.7199 0.1136  -0.4734 -0.6851 215  ARG C C   
7974  O  O   . ARG C  217 ? 4.5436 3.1957 3.6425 0.0925  -0.4537 -0.6596 215  ARG C O   
7975  C  CB  . ARG C  217 ? 4.6732 3.2884 3.7199 0.1868  -0.3446 -0.6463 215  ARG C CB  
7976  C  CG  . ARG C  217 ? 4.4003 3.1649 3.4991 0.1684  -0.2891 -0.5971 215  ARG C CG  
7977  C  CD  . ARG C  217 ? 4.3723 3.1631 3.3630 0.2178  -0.2395 -0.6039 215  ARG C CD  
7978  N  NE  . ARG C  217 ? 4.4543 3.1945 3.3733 0.2798  -0.2000 -0.6133 215  ARG C NE  
7979  C  CZ  . ARG C  217 ? 4.4866 3.2420 3.3128 0.3333  -0.1508 -0.6138 215  ARG C CZ  
7980  N  NH1 . ARG C  217 ? 4.3437 3.1612 3.1404 0.3300  -0.1362 -0.6058 215  ARG C NH1 
7981  N  NH2 . ARG C  217 ? 4.6484 3.3581 3.4154 0.3921  -0.1139 -0.6182 215  ARG C NH2 
7982  N  N   . GLY C  218 ? 4.5502 2.9747 3.5592 0.1235  -0.5426 -0.7413 216  GLY C N   
7983  C  CA  . GLY C  218 ? 4.4414 2.8362 3.3922 0.1117  -0.6011 -0.7757 216  GLY C CA  
7984  C  C   . GLY C  218 ? 4.3528 2.7454 3.4196 0.0447  -0.6746 -0.7668 216  GLY C C   
7985  O  O   . GLY C  218 ? 4.2232 2.5941 3.2539 0.0302  -0.7306 -0.7929 216  GLY C O   
7986  N  N   . ASP C  219 ? 4.4216 2.8410 3.6321 0.0047  -0.6752 -0.7257 217  ASP C N   
7987  C  CA  . ASP C  219 ? 4.3659 2.7920 3.7066 -0.0590 -0.7402 -0.7056 217  ASP C CA  
7988  C  C   . ASP C  219 ? 4.2045 2.7746 3.6351 -0.0990 -0.7137 -0.6490 217  ASP C C   
7989  O  O   . ASP C  219 ? 4.1481 2.7291 3.6220 -0.1369 -0.7685 -0.6470 217  ASP C O   
7990  C  CB  . ASP C  219 ? 4.2854 2.6739 3.7456 -0.0806 -0.7518 -0.6810 217  ASP C CB  
7991  C  CG  . ASP C  219 ? 4.3471 2.5731 3.7298 -0.0477 -0.7954 -0.7422 217  ASP C CG  
7992  O  OD1 . ASP C  219 ? 4.3818 2.5472 3.6079 0.0114  -0.7764 -0.7913 217  ASP C OD1 
7993  O  OD2 . ASP C  219 ? 4.3372 2.4944 3.8175 -0.0787 -0.8479 -0.7396 217  ASP C OD2 
7994  N  N   . LEU C  220 ? 4.0250 2.7048 3.4831 -0.0898 -0.6330 -0.6038 218  LEU C N   
7995  C  CA  . LEU C  220 ? 3.8799 2.6885 3.4190 -0.1242 -0.6089 -0.5534 218  LEU C CA  
7996  C  C   . LEU C  220 ? 3.7732 2.6172 3.2145 -0.1081 -0.5955 -0.5719 218  LEU C C   
7997  O  O   . LEU C  220 ? 3.5972 2.5118 3.0890 -0.1393 -0.6051 -0.5469 218  LEU C O   
7998  C  CB  . LEU C  220 ? 3.7675 2.6793 3.3816 -0.1233 -0.5355 -0.4984 218  LEU C CB  
7999  C  CG  . LEU C  220 ? 3.6176 2.6551 3.3296 -0.1590 -0.5153 -0.4441 218  LEU C CG  
8000  C  CD1 . LEU C  220 ? 3.5655 2.5935 3.3886 -0.2055 -0.5767 -0.4222 218  LEU C CD1 
8001  C  CD2 . LEU C  220 ? 3.5963 2.7304 3.3728 -0.1539 -0.4489 -0.3946 218  LEU C CD2 
8002  N  N   . ALA C  221 ? 3.9535 2.7514 3.2589 -0.0570 -0.5709 -0.6110 219  ALA C N   
8003  C  CA  . ALA C  221 ? 3.9407 2.7695 3.1514 -0.0358 -0.5532 -0.6246 219  ALA C CA  
8004  C  C   . ALA C  221 ? 4.0597 2.7758 3.1207 0.0126  -0.5818 -0.6857 219  ALA C C   
8005  O  O   . ALA C  221 ? 4.1811 2.8075 3.1956 0.0425  -0.5894 -0.7153 219  ALA C O   
8006  C  CB  . ALA C  221 ? 3.8306 2.7577 3.0329 -0.0153 -0.4679 -0.5922 219  ALA C CB  
8007  N  N   . THR C  222 ? 3.9701 2.6913 2.9506 0.0252  -0.5951 -0.7033 220  THR C N   
8008  C  CA  . THR C  222 ? 4.1223 2.7434 2.9461 0.0793  -0.6191 -0.7599 220  THR C CA  
8009  C  C   . THR C  222 ? 4.2720 2.8936 3.0060 0.1412  -0.5439 -0.7608 220  THR C C   
8010  O  O   . THR C  222 ? 4.1604 2.8801 2.9163 0.1469  -0.4738 -0.7205 220  THR C O   
8011  C  CB  . THR C  222 ? 4.0250 2.6613 2.7859 0.0811  -0.6479 -0.7719 220  THR C CB  
8012  O  OG1 . THR C  222 ? 4.1441 2.6832 2.7413 0.1414  -0.6699 -0.8270 220  THR C OG1 
8013  C  CG2 . THR C  222 ? 3.8464 2.6054 2.6289 0.0800  -0.5770 -0.7248 220  THR C CG2 
8014  N  N   . ILE C  223 ? 4.6372 3.1456 3.2683 0.1898  -0.5608 -0.8076 221  ILE C N   
8015  C  CA  . ILE C  223 ? 4.6877 3.1858 3.2315 0.2552  -0.4918 -0.8083 221  ILE C CA  
8016  C  C   . ILE C  223 ? 4.8550 3.2404 3.2229 0.3222  -0.5199 -0.8679 221  ILE C C   
8017  O  O   . ILE C  223 ? 4.9913 3.2701 3.3188 0.3174  -0.6008 -0.9191 221  ILE C O   
8018  C  CB  . ILE C  223 ? 4.7418 3.2188 3.3543 0.2536  -0.4694 -0.7959 221  ILE C CB  
8019  C  CG1 . ILE C  223 ? 4.5283 3.1151 3.3111 0.1895  -0.4482 -0.7379 221  ILE C CG1 
8020  C  CG2 . ILE C  223 ? 4.7259 3.2060 3.2570 0.3219  -0.3933 -0.7889 221  ILE C CG2 
8021  C  CD1 . ILE C  223 ? 4.3237 3.0418 3.1381 0.1920  -0.3689 -0.6876 221  ILE C CD1 
8022  N  N   . HIS C  224 ? 5.0011 3.4093 3.2657 0.3872  -0.4535 -0.8600 222  HIS C N   
8023  C  CA  . HIS C  224 ? 5.3217 3.6394 3.4039 0.4645  -0.4645 -0.9083 222  HIS C CA  
8024  C  C   . HIS C  224 ? 5.3465 3.6028 3.3702 0.4501  -0.5539 -0.9543 222  HIS C C   
8025  O  O   . HIS C  224 ? 5.5062 3.6393 3.4010 0.4952  -0.6069 -1.0166 222  HIS C O   
8026  C  CB  . HIS C  224 ? 5.4577 3.6595 3.4565 0.5225  -0.4621 -0.9472 222  HIS C CB  
8027  C  CG  . HIS C  224 ? 5.4571 3.5441 3.4887 0.4892  -0.5483 -0.9949 222  HIS C CG  
8028  N  ND1 . HIS C  224 ? 5.2372 3.3493 3.4288 0.4246  -0.5582 -0.9677 222  HIS C ND1 
8029  C  CD2 . HIS C  224 ? 5.5797 3.5231 3.5058 0.5143  -0.6287 -1.0671 222  HIS C CD2 
8030  C  CE1 . HIS C  224 ? 5.2962 3.2878 3.4905 0.4077  -0.6398 -1.0166 222  HIS C CE1 
8031  N  NE2 . HIS C  224 ? 5.5526 3.4371 3.5873 0.4596  -0.6869 -1.0804 222  HIS C NE2 
8032  N  N   . GLY C  225 ? 4.8217 3.1636 2.9376 0.3896  -0.5724 -0.9244 223  GLY C N   
8033  C  CA  . GLY C  225 ? 4.6561 2.9594 2.7330 0.3714  -0.6548 -0.9584 223  GLY C CA  
8034  C  C   . GLY C  225 ? 4.3594 2.7753 2.4553 0.3575  -0.6246 -0.9161 223  GLY C C   
8035  O  O   . GLY C  225 ? 4.1725 2.6994 2.3553 0.3377  -0.5534 -0.8586 223  GLY C O   
8036  N  N   . MET C  226 ? 4.3511 2.7338 2.3633 0.3689  -0.6829 -0.9465 224  MET C N   
8037  C  CA  . MET C  226 ? 4.1531 2.6321 2.1714 0.3618  -0.6592 -0.9089 224  MET C CA  
8038  C  C   . MET C  226 ? 3.9581 2.5333 2.1564 0.2766  -0.6633 -0.8613 224  MET C C   
8039  O  O   . MET C  226 ? 3.8218 2.3765 2.1262 0.2224  -0.7085 -0.8657 224  MET C O   
8040  C  CB  . MET C  226 ? 4.2631 2.6827 2.1552 0.3918  -0.7295 -0.9531 224  MET C CB  
8041  C  CG  . MET C  226 ? 4.2368 2.6017 2.1915 0.3382  -0.8336 -0.9853 224  MET C CG  
8042  S  SD  . MET C  226 ? 4.2567 2.5718 2.0923 0.3849  -0.8912 -1.0207 224  MET C SD  
8043  C  CE  . MET C  226 ? 4.2207 2.6313 1.9880 0.4166  -0.8422 -0.9824 224  MET C CE  
8044  N  N   . ASN C  227 ? 4.1308 2.8111 2.3637 0.2684  -0.6125 -0.8129 225  ASN C N   
8045  C  CA  . ASN C  227 ? 4.0942 2.8751 2.4860 0.1991  -0.5994 -0.7627 225  ASN C CA  
8046  C  C   . ASN C  227 ? 3.9221 2.7495 2.4234 0.1730  -0.5449 -0.7306 225  ASN C C   
8047  O  O   . ASN C  227 ? 3.6418 2.5359 2.2770 0.1154  -0.5438 -0.6963 225  ASN C O   
8048  C  CB  . ASN C  227 ? 4.1169 2.8788 2.5838 0.1416  -0.6887 -0.7753 225  ASN C CB  
8049  C  CG  . ASN C  227 ? 4.1673 2.8936 2.5365 0.1622  -0.7490 -0.8043 225  ASN C CG  
8050  O  OD1 . ASN C  227 ? 4.2089 2.8993 2.4332 0.2269  -0.7343 -0.8273 225  ASN C OD1 
8051  N  ND2 . ASN C  227 ? 4.1388 2.8794 2.5880 0.1101  -0.8169 -0.7999 225  ASN C ND2 
8052  N  N   . ARG C  228 ? 3.9368 2.7318 2.3801 0.2184  -0.4994 -0.7396 226  ARG C N   
8053  C  CA  . ARG C  228 ? 3.6854 2.5259 2.2245 0.1994  -0.4479 -0.7091 226  ARG C CA  
8054  C  C   . ARG C  228 ? 3.5853 2.5483 2.2111 0.1743  -0.3853 -0.6533 226  ARG C C   
8055  O  O   . ARG C  228 ? 3.5033 2.5072 2.0881 0.1915  -0.3615 -0.6380 226  ARG C O   
8056  C  CB  . ARG C  228 ? 3.6785 2.4694 2.1295 0.2612  -0.4047 -0.7245 226  ARG C CB  
8057  C  CG  . ARG C  228 ? 3.6510 2.4668 1.9986 0.3223  -0.3474 -0.7125 226  ARG C CG  
8058  C  CD  . ARG C  228 ? 3.7335 2.4952 2.0002 0.3839  -0.3104 -0.7270 226  ARG C CD  
8059  N  NE  . ARG C  228 ? 3.7765 2.5838 1.9748 0.4419  -0.2368 -0.6981 226  ARG C NE  
8060  C  CZ  . ARG C  228 ? 3.9120 2.6905 2.0424 0.5031  -0.1897 -0.6986 226  ARG C CZ  
8061  N  NH1 . ARG C  228 ? 3.9085 2.6091 2.0289 0.5114  -0.2116 -0.7301 226  ARG C NH1 
8062  N  NH2 . ARG C  228 ? 4.0607 2.8884 2.1394 0.5563  -0.1205 -0.6643 226  ARG C NH2 
8063  N  N   . PRO C  229 ? 3.7091 2.7301 2.4554 0.1350  -0.3588 -0.6223 227  PRO C N   
8064  C  CA  . PRO C  229 ? 3.6553 2.7866 2.4910 0.1057  -0.3101 -0.5750 227  PRO C CA  
8065  C  C   . PRO C  229 ? 3.7120 2.8885 2.4923 0.1413  -0.2538 -0.5553 227  PRO C C   
8066  O  O   . PRO C  229 ? 3.7811 2.9382 2.4885 0.1914  -0.2143 -0.5583 227  PRO C O   
8067  C  CB  . PRO C  229 ? 3.6262 2.7901 2.5451 0.0905  -0.2772 -0.5551 227  PRO C CB  
8068  C  CG  . PRO C  229 ? 3.7332 2.8183 2.6637 0.0787  -0.3326 -0.5830 227  PRO C CG  
8069  C  CD  . PRO C  229 ? 3.8087 2.7923 2.6133 0.1172  -0.3767 -0.6306 227  PRO C CD  
8070  N  N   . PHE C  230 ? 3.6491 2.8862 2.4680 0.1172  -0.2486 -0.5314 228  PHE C N   
8071  C  CA  . PHE C  230 ? 3.6314 2.9133 2.4133 0.1451  -0.1991 -0.5073 228  PHE C CA  
8072  C  C   . PHE C  230 ? 3.3489 2.7229 2.2405 0.1038  -0.1664 -0.4680 228  PHE C C   
8073  O  O   . PHE C  230 ? 3.2729 2.6723 2.2488 0.0571  -0.1923 -0.4624 228  PHE C O   
8074  C  CB  . PHE C  230 ? 3.8311 3.0784 2.5222 0.1690  -0.2310 -0.5224 228  PHE C CB  
8075  C  CG  . PHE C  230 ? 3.7517 3.0224 2.5015 0.1229  -0.2759 -0.5170 228  PHE C CG  
8076  C  CD1 . PHE C  230 ? 3.7060 2.9330 2.4807 0.0920  -0.3447 -0.5423 228  PHE C CD1 
8077  C  CD2 . PHE C  230 ? 3.6639 3.0003 2.4495 0.1114  -0.2489 -0.4835 228  PHE C CD2 
8078  C  CE1 . PHE C  230 ? 3.5525 2.8081 2.3881 0.0517  -0.3837 -0.5309 228  PHE C CE1 
8079  C  CE2 . PHE C  230 ? 3.5611 2.9207 2.4000 0.0735  -0.2866 -0.4755 228  PHE C CE2 
8080  C  CZ  . PHE C  230 ? 3.5099 2.8325 2.3744 0.0443  -0.3532 -0.4976 228  PHE C CZ  
8081  N  N   . LEU C  231 ? 3.1487 2.5714 2.0392 0.1238  -0.1091 -0.4394 229  LEU C N   
8082  C  CA  . LEU C  231 ? 3.0904 2.5932 2.0781 0.0897  -0.0765 -0.4055 229  LEU C CA  
8083  C  C   . LEU C  231 ? 3.0959 2.6179 2.0713 0.0890  -0.0770 -0.3905 229  LEU C C   
8084  O  O   . LEU C  231 ? 3.2474 2.7725 2.1680 0.1262  -0.0452 -0.3756 229  LEU C O   
8085  C  CB  . LEU C  231 ? 3.0938 2.6397 2.1072 0.1067  -0.0167 -0.3808 229  LEU C CB  
8086  C  CG  . LEU C  231 ? 3.1589 2.7818 2.2719 0.0729  0.0144  -0.3501 229  LEU C CG  
8087  C  CD1 . LEU C  231 ? 3.2777 2.9232 2.4719 0.0255  -0.0126 -0.3568 229  LEU C CD1 
8088  C  CD2 . LEU C  231 ? 3.1261 2.7886 2.2650 0.0911  0.0669  -0.3257 229  LEU C CD2 
8089  N  N   . LEU C  232 ? 3.0771 2.6157 2.1071 0.0492  -0.1097 -0.3894 230  LEU C N   
8090  C  CA  . LEU C  232 ? 3.1685 2.7275 2.1956 0.0465  -0.1113 -0.3729 230  LEU C CA  
8091  C  C   . LEU C  232 ? 3.1615 2.7833 2.2566 0.0348  -0.0599 -0.3393 230  LEU C C   
8092  O  O   . LEU C  232 ? 3.1594 2.8183 2.3370 0.0026  -0.0498 -0.3328 230  LEU C O   
8093  C  CB  . LEU C  232 ? 3.1994 2.7559 2.2657 0.0106  -0.1639 -0.3801 230  LEU C CB  
8094  C  CG  . LEU C  232 ? 3.2527 2.8205 2.3050 0.0113  -0.1776 -0.3662 230  LEU C CG  
8095  C  CD1 . LEU C  232 ? 3.4229 2.9424 2.3605 0.0553  -0.1962 -0.3813 230  LEU C CD1 
8096  C  CD2 . LEU C  232 ? 3.1444 2.7232 2.2593 -0.0279 -0.2238 -0.3656 230  LEU C CD2 
8097  N  N   . LEU C  233 ? 3.1797 2.8118 2.2401 0.0626  -0.0290 -0.3175 231  LEU C N   
8098  C  CA  . LEU C  233 ? 3.1436 2.8276 2.2692 0.0540  0.0191  -0.2840 231  LEU C CA  
8099  C  C   . LEU C  233 ? 3.2912 2.9900 2.4297 0.0468  0.0161  -0.2652 231  LEU C C   
8100  O  O   . LEU C  233 ? 3.4756 3.1484 2.5450 0.0696  -0.0056 -0.2681 231  LEU C O   
8101  C  CB  . LEU C  233 ? 3.1417 2.8329 2.2341 0.0949  0.0685  -0.2626 231  LEU C CB  
8102  C  CG  . LEU C  233 ? 3.1955 2.8726 2.2665 0.1127  0.0789  -0.2757 231  LEU C CG  
8103  C  CD1 . LEU C  233 ? 3.3319 3.0191 2.3640 0.1615  0.1305  -0.2468 231  LEU C CD1 
8104  C  CD2 . LEU C  233 ? 3.1528 2.8658 2.3195 0.0717  0.0826  -0.2776 231  LEU C CD2 
8105  N  N   . MET C  234 ? 3.1141 2.8527 2.3390 0.0171  0.0363  -0.2468 232  MET C N   
8106  C  CA  . MET C  234 ? 3.0471 2.8008 2.2958 0.0104  0.0404  -0.2253 232  MET C CA  
8107  C  C   . MET C  234 ? 3.0977 2.8851 2.4138 0.0046  0.0886  -0.1961 232  MET C C   
8108  O  O   . MET C  234 ? 2.9944 2.8037 2.3856 -0.0271 0.0936  -0.2006 232  MET C O   
8109  C  CB  . MET C  234 ? 2.9809 2.7401 2.2734 -0.0243 0.0043  -0.2372 232  MET C CB  
8110  C  CG  . MET C  234 ? 3.0607 2.7897 2.3090 -0.0260 -0.0478 -0.2627 232  MET C CG  
8111  S  SD  . MET C  234 ? 3.1343 2.8824 2.4539 -0.0662 -0.0833 -0.2658 232  MET C SD  
8112  C  CE  . MET C  234 ? 3.1137 2.8219 2.3855 -0.0658 -0.1450 -0.2912 232  MET C CE  
8113  N  N   . ALA C  235 ? 3.3498 3.1414 2.6406 0.0362  0.1225  -0.1652 233  ALA C N   
8114  C  CA  . ALA C  235 ? 3.4292 3.2513 2.7904 0.0326  0.1688  -0.1318 233  ALA C CA  
8115  C  C   . ALA C  235 ? 3.4300 3.2580 2.7995 0.0451  0.1886  -0.0963 233  ALA C C   
8116  O  O   . ALA C  235 ? 3.3442 3.1560 2.6520 0.0640  0.1697  -0.0956 233  ALA C O   
8117  C  CB  . ALA C  235 ? 3.4887 3.3200 2.8303 0.0630  0.2035  -0.1152 233  ALA C CB  
8118  N  N   . THR C  236 ? 3.5468 3.3987 2.9991 0.0338  0.2255  -0.0650 234  THR C N   
8119  C  CA  . THR C  236 ? 3.5415 3.4001 3.0215 0.0434  0.2508  -0.0249 234  THR C CA  
8120  C  C   . THR C  236 ? 3.6346 3.5093 3.0970 0.0858  0.2976  0.0227  234  THR C C   
8121  O  O   . THR C  236 ? 3.6595 3.5549 3.1675 0.0852  0.3251  0.0380  234  THR C O   
8122  C  CB  . THR C  236 ? 3.4503 3.3182 3.0411 0.0028  0.2589  -0.0205 234  THR C CB  
8123  O  OG1 . THR C  236 ? 3.5143 3.3691 3.1125 -0.0276 0.2198  -0.0597 234  THR C OG1 
8124  C  CG2 . THR C  236 ? 3.3258 3.1968 2.9543 0.0136  0.2891  0.0251  234  THR C CG2 
8125  N  N   . PRO C  237 ? 3.7108 3.5815 3.1104 0.1254  0.3086  0.0507  235  PRO C N   
8126  C  CA  . PRO C  237 ? 3.7578 3.6481 3.1338 0.1745  0.3579  0.1025  235  PRO C CA  
8127  C  C   . PRO C  237 ? 3.6797 3.6007 3.1789 0.1588  0.4046  0.1527  235  PRO C C   
8128  O  O   . PRO C  237 ? 3.6953 3.6145 3.2866 0.1159  0.3981  0.1504  235  PRO C O   
8129  C  CB  . PRO C  237 ? 3.7503 3.6313 3.0424 0.2143  0.3532  0.1203  235  PRO C CB  
8130  C  CG  . PRO C  237 ? 3.6880 3.5396 2.9292 0.1926  0.2918  0.0657  235  PRO C CG  
8131  C  CD  . PRO C  237 ? 3.5789 3.4301 2.9168 0.1322  0.2738  0.0364  235  PRO C CD  
8132  N  N   . LEU C  238 ? 3.4177 3.3659 2.9196 0.1965  0.4520  0.2000  236  LEU C N   
8133  C  CA  . LEU C  238 ? 3.3537 3.3347 2.9822 0.1840  0.4977  0.2575  236  LEU C CA  
8134  C  C   . LEU C  238 ? 3.4840 3.4659 3.1445 0.1924  0.5180  0.3019  236  LEU C C   
8135  O  O   . LEU C  238 ? 3.5170 3.5118 3.3016 0.1646  0.5411  0.3376  236  LEU C O   
8136  C  CB  . LEU C  238 ? 3.3512 3.3683 2.9771 0.2284  0.5479  0.3073  236  LEU C CB  
8137  C  CG  . LEU C  238 ? 3.2665 3.2900 2.8731 0.2276  0.5405  0.2779  236  LEU C CG  
8138  C  CD1 . LEU C  238 ? 3.3273 3.3199 2.7741 0.2724  0.5177  0.2373  236  LEU C CD1 
8139  C  CD2 . LEU C  238 ? 3.2368 3.3105 2.9215 0.2486  0.5974  0.3439  236  LEU C CD2 
8140  N  N   . GLU C  239 ? 3.6034 3.5709 3.1562 0.2309  0.5076  0.3008  237  GLU C N   
8141  C  CA  . GLU C  239 ? 3.6576 3.6265 3.2336 0.2413  0.5240  0.3421  237  GLU C CA  
8142  C  C   . GLU C  239 ? 3.7233 3.6691 3.3845 0.1828  0.4951  0.3142  237  GLU C C   
8143  O  O   . GLU C  239 ? 3.7363 3.6839 3.4727 0.1766  0.5184  0.3551  237  GLU C O   
8144  C  CB  . GLU C  239 ? 3.6199 3.5788 3.0535 0.2930  0.5079  0.3375  237  GLU C CB  
8145  C  CG  . GLU C  239 ? 3.5869 3.5582 2.9097 0.3582  0.5295  0.3532  237  GLU C CG  
8146  C  CD  . GLU C  239 ? 3.5606 3.5020 2.7299 0.3882  0.4802  0.3034  237  GLU C CD  
8147  O  OE1 . GLU C  239 ? 3.4477 3.3643 2.6098 0.3520  0.4282  0.2576  237  GLU C OE1 
8148  O  OE2 . GLU C  239 ? 3.6860 3.6279 2.7435 0.4492  0.4922  0.3105  237  GLU C OE2 
8149  N  N   . ARG C  240 ? 3.7028 3.6262 3.3536 0.1430  0.4468  0.2470  238  ARG C N   
8150  C  CA  . ARG C  240 ? 3.5437 3.4443 3.2605 0.0945  0.4188  0.2165  238  ARG C CA  
8151  C  C   . ARG C  240 ? 3.4279 3.3305 3.2750 0.0510  0.4313  0.2195  238  ARG C C   
8152  O  O   . ARG C  240 ? 3.4354 3.3267 3.3690 0.0317  0.4436  0.2408  238  ARG C O   
8153  C  CB  . ARG C  240 ? 3.4653 3.3459 3.1165 0.0752  0.3638  0.1493  238  ARG C CB  
8154  C  CG  . ARG C  240 ? 3.4322 3.3081 2.9556 0.1136  0.3407  0.1377  238  ARG C CG  
8155  C  CD  . ARG C  240 ? 3.4295 3.3034 2.9268 0.1347  0.3405  0.1648  238  ARG C CD  
8156  N  NE  . ARG C  240 ? 3.4703 3.3385 2.8469 0.1677  0.3080  0.1480  238  ARG C NE  
8157  C  CZ  . ARG C  240 ? 3.5861 3.4638 2.8791 0.2216  0.3253  0.1773  238  ARG C CZ  
8158  N  NH1 . ARG C  240 ? 3.5544 3.4537 2.8766 0.2503  0.3811  0.2322  238  ARG C NH1 
8159  N  NH2 . ARG C  240 ? 3.7413 3.6074 2.9227 0.2485  0.2857  0.1531  238  ARG C NH2 
8160  N  N   . ALA C  241 ? 3.2669 3.1820 3.1303 0.0356  0.4256  0.1975  239  ALA C N   
8161  C  CA  . ALA C  241 ? 3.2514 3.1697 3.2354 -0.0089 0.4264  0.1924  239  ALA C CA  
8162  C  C   . ALA C  241 ? 3.3527 3.2879 3.4421 -0.0054 0.4724  0.2604  239  ALA C C   
8163  O  O   . ALA C  241 ? 3.3952 3.3136 3.5899 -0.0417 0.4694  0.2625  239  ALA C O   
8164  C  CB  . ALA C  241 ? 3.2158 3.1534 3.1920 -0.0185 0.4149  0.1649  239  ALA C CB  
8165  N  N   . GLN C  242 ? 3.4386 3.4054 3.5022 0.0402  0.5152  0.3177  240  GLN C N   
8166  C  CA  . GLN C  242 ? 3.4058 3.3963 3.5735 0.0495  0.5651  0.3947  240  GLN C CA  
8167  C  C   . GLN C  242 ? 3.3224 3.2921 3.5060 0.0591  0.5787  0.4262  240  GLN C C   
8168  O  O   . GLN C  242 ? 3.2664 3.2266 3.5724 0.0327  0.5930  0.4569  240  GLN C O   
8169  C  CB  . GLN C  242 ? 3.3871 3.4223 3.5119 0.1051  0.6116  0.4513  240  GLN C CB  
8170  C  CG  . GLN C  242 ? 3.2870 3.3455 3.4004 0.1018  0.6054  0.4289  240  GLN C CG  
8171  C  CD  . GLN C  242 ? 3.3037 3.4037 3.3654 0.1652  0.6554  0.4863  240  GLN C CD  
8172  O  OE1 . GLN C  242 ? 3.3900 3.5051 3.4275 0.2128  0.6966  0.5464  240  GLN C OE1 
8173  N  NE2 . GLN C  242 ? 3.2424 3.3622 3.2837 0.1709  0.6540  0.4701  240  GLN C NE2 
8174  N  N   . ALA C  252 ? 4.0217 3.4693 2.7006 1.4382  0.0555  -0.2864 250  ALA C N   
8175  C  CA  . ALA C  252 ? 3.9865 3.5429 2.7566 1.4171  -0.0187 -0.2924 250  ALA C CA  
8176  C  C   . ALA C  252 ? 3.8028 3.5310 2.7361 1.4377  -0.0123 -0.2913 250  ALA C C   
8177  O  O   . ALA C  252 ? 3.8045 3.5628 2.7570 1.4620  -0.0196 -0.2845 250  ALA C O   
8178  C  CB  . ALA C  252 ? 4.0433 3.5207 2.7184 1.4049  -0.0722 -0.2924 250  ALA C CB  
8179  N  N   . LEU C  253 ? 3.4867 3.3240 2.5299 1.4242  0.0025  -0.2964 251  LEU C N   
8180  C  CA  . LEU C  253 ? 3.2063 3.2165 2.4000 1.4303  0.0038  -0.2944 251  LEU C CA  
8181  C  C   . LEU C  253 ? 3.2364 3.3245 2.4889 1.4014  -0.0640 -0.3065 251  LEU C C   
8182  O  O   . LEU C  253 ? 2.9956 3.0286 2.2065 1.3730  -0.1026 -0.3166 251  LEU C O   
8183  C  CB  . LEU C  253 ? 3.0165 3.1083 2.2943 1.4155  0.0491  -0.2976 251  LEU C CB  
8184  C  CG  . LEU C  253 ? 3.1068 3.1254 2.3364 1.4433  0.1250  -0.2852 251  LEU C CG  
8185  C  CD1 . LEU C  253 ? 3.1042 3.2135 2.4259 1.4213  0.1678  -0.2898 251  LEU C CD1 
8186  C  CD2 . LEU C  253 ? 3.0947 3.1240 2.3333 1.4976  0.1614  -0.2599 251  LEU C CD2 
8187  N  N   . ASP C  254 ? 3.5983 3.8184 2.9507 1.4103  -0.0757 -0.3010 252  ASP C N   
8188  C  CA  . ASP C  254 ? 3.4947 3.7826 2.8947 1.3859  -0.1337 -0.3117 252  ASP C CA  
8189  C  C   . ASP C  254 ? 3.1590 3.5760 2.6662 1.3429  -0.1384 -0.3266 252  ASP C C   
8190  O  O   . ASP C  254 ? 2.9668 3.3723 2.4808 1.3154  -0.1133 -0.3384 252  ASP C O   
8191  C  CB  . ASP C  254 ? 3.5851 3.9161 3.0018 1.4198  -0.1490 -0.2954 252  ASP C CB  
8192  C  CG  . ASP C  254 ? 3.4464 3.8775 2.9380 1.4563  -0.1051 -0.2694 252  ASP C CG  
8193  O  OD1 . ASP C  254 ? 3.5602 4.0583 3.1130 1.4453  -0.0699 -0.2676 252  ASP C OD1 
8194  O  OD2 . ASP C  254 ? 3.1655 3.6123 2.6597 1.4969  -0.1039 -0.2469 252  ASP C OD2 
8195  N  N   . THR C  255 ? 3.0302 3.5608 2.6100 1.3322  -0.1689 -0.3270 253  THR C N   
8196  C  CA  . THR C  255 ? 2.8947 3.5406 2.5592 1.2801  -0.1753 -0.3443 253  THR C CA  
8197  C  C   . THR C  255 ? 3.0145 3.7679 2.7541 1.2701  -0.1342 -0.3364 253  THR C C   
8198  O  O   . THR C  255 ? 3.0465 3.8644 2.8338 1.2154  -0.1259 -0.3561 253  THR C O   
8199  C  CB  . THR C  255 ? 2.8445 3.5773 2.5512 1.2685  -0.2197 -0.3447 253  THR C CB  
8200  O  OG1 . THR C  255 ? 3.0541 3.8689 2.7990 1.3098  -0.2175 -0.3139 253  THR C OG1 
8201  C  CG2 . THR C  255 ? 2.7212 3.3525 2.3616 1.2764  -0.2571 -0.3517 253  THR C CG2 
8202  N  N   . ASN C  256 ? 3.0522 3.8224 2.8024 1.3197  -0.1029 -0.3071 254  ASN C N   
8203  C  CA  . ASN C  256 ? 2.9862 3.8747 2.8239 1.3152  -0.0618 -0.2914 254  ASN C CA  
8204  C  C   . ASN C  256 ? 3.0908 3.9151 2.9044 1.2912  -0.0146 -0.3087 254  ASN C C   
8205  O  O   . ASN C  256 ? 3.0533 3.9749 2.9419 1.2763  0.0227  -0.3004 254  ASN C O   
8206  C  CB  . ASN C  256 ? 2.9377 3.8507 2.7958 1.3852  -0.0318 -0.2484 254  ASN C CB  
8207  C  CG  . ASN C  256 ? 2.9813 3.9641 2.8682 1.4137  -0.0719 -0.2248 254  ASN C CG  
8208  O  OD1 . ASN C  256 ? 2.9095 3.9968 2.8471 1.3729  -0.1189 -0.2333 254  ASN C OD1 
8209  N  ND2 . ASN C  256 ? 3.1151 4.0285 2.9591 1.4821  -0.0487 -0.1955 254  ASN C ND2 
8210  N  N   . TYR C  257 ? 3.2188 3.8875 2.9326 1.2867  -0.0157 -0.3283 255  TYR C N   
8211  C  CA  . TYR C  257 ? 3.2333 3.8218 2.9084 1.2668  0.0278  -0.3421 255  TYR C CA  
8212  C  C   . TYR C  257 ? 3.0543 3.5807 2.6942 1.2223  0.0038  -0.3693 255  TYR C C   
8213  O  O   . TYR C  257 ? 3.0964 3.6037 2.7386 1.1851  0.0362  -0.3858 255  TYR C O   
8214  C  CB  . TYR C  257 ? 3.4723 3.9128 3.0442 1.3155  0.0597  -0.3274 255  TYR C CB  
8215  C  CG  . TYR C  257 ? 3.5267 3.8469 3.0242 1.2968  0.0909  -0.3403 255  TYR C CG  
8216  C  CD1 . TYR C  257 ? 3.5528 3.8968 3.0831 1.2816  0.1506  -0.3429 255  TYR C CD1 
8217  C  CD2 . TYR C  257 ? 3.5435 3.7319 2.9411 1.2937  0.0602  -0.3456 255  TYR C CD2 
8218  C  CE1 . TYR C  257 ? 3.6807 3.9069 3.1359 1.2663  0.1818  -0.3524 255  TYR C CE1 
8219  C  CE2 . TYR C  257 ? 3.6312 3.7132 2.9600 1.2800  0.0863  -0.3497 255  TYR C CE2 
8220  C  CZ  . TYR C  257 ? 3.7500 3.8449 3.1030 1.2674  0.1485  -0.3541 255  TYR C CZ  
8221  O  OH  . TYR C  257 ? 3.9716 3.9530 3.2494 1.2553  0.1773  -0.3561 255  TYR C OH  
8222  N  N   . CYS C  258 ? 2.9491 3.4405 2.5581 1.2281  -0.0475 -0.3716 256  CYS C N   
8223  C  CA  . CYS C  258 ? 3.0548 3.4798 2.6337 1.1974  -0.0667 -0.3886 256  CYS C CA  
8224  C  C   . CYS C  258 ? 3.0830 3.6008 2.7329 1.1401  -0.0688 -0.4124 256  CYS C C   
8225  O  O   . CYS C  258 ? 3.0194 3.4792 2.6521 1.1109  -0.0622 -0.4271 256  CYS C O   
8226  C  CB  . CYS C  258 ? 3.1146 3.4711 2.6394 1.2233  -0.1179 -0.3792 256  CYS C CB  
8227  S  SG  . CYS C  258 ? 3.2834 3.4727 2.6925 1.2463  -0.1173 -0.3642 256  CYS C SG  
8228  N  N   . PHE C  259 ? 3.2103 3.8669 2.9349 1.1221  -0.0754 -0.4134 257  PHE C N   
8229  C  CA  . PHE C  259 ? 3.2666 4.0120 3.0442 1.0557  -0.0778 -0.4379 257  PHE C CA  
8230  C  C   . PHE C  259 ? 3.3306 4.1518 3.1562 1.0080  -0.0323 -0.4491 257  PHE C C   
8231  O  O   . PHE C  259 ? 3.3444 4.1957 3.1859 0.9391  -0.0188 -0.4770 257  PHE C O   
8232  C  CB  . PHE C  259 ? 3.1656 4.0249 2.9886 1.0540  -0.1248 -0.4302 257  PHE C CB  
8233  C  CG  . PHE C  259 ? 3.0935 3.8857 2.8748 1.0756  -0.1672 -0.4303 257  PHE C CG  
8234  C  CD1 . PHE C  259 ? 3.0730 3.7603 2.7957 1.1339  -0.1806 -0.4125 257  PHE C CD1 
8235  C  CD2 . PHE C  259 ? 3.0086 3.8421 2.8050 1.0324  -0.1920 -0.4482 257  PHE C CD2 
8236  C  CE1 . PHE C  259 ? 3.0512 3.6860 2.7420 1.1481  -0.2196 -0.4115 257  PHE C CE1 
8237  C  CE2 . PHE C  259 ? 2.9545 3.7292 2.7190 1.0522  -0.2264 -0.4471 257  PHE C CE2 
8238  C  CZ  . PHE C  259 ? 2.9798 3.6606 2.6972 1.1101  -0.2412 -0.4280 257  PHE C CZ  
8239  N  N   . SER C  260 ? 3.3368 4.1847 3.1823 1.0396  -0.0037 -0.4287 258  SER C N   
8240  C  CA  . SER C  260 ? 3.2366 4.1621 3.1350 0.9968  0.0428  -0.4353 258  SER C CA  
8241  C  C   . SER C  260 ? 3.3597 4.1553 3.1996 0.9889  0.0978  -0.4497 258  SER C C   
8242  O  O   . SER C  260 ? 3.3063 4.1467 3.1798 0.9410  0.1425  -0.4628 258  SER C O   
8243  C  CB  . SER C  260 ? 3.1057 4.1427 3.0726 1.0378  0.0524  -0.3994 258  SER C CB  
8244  O  OG  . SER C  260 ? 3.1079 4.0322 3.0157 1.1138  0.0688  -0.3770 258  SER C OG  
8245  N  N   . SER C  261 ? 3.4549 4.0953 3.2077 1.0311  0.0947  -0.4450 259  SER C N   
8246  C  CA  . SER C  261 ? 3.4716 3.9821 3.1601 1.0304  0.1428  -0.4507 259  SER C CA  
8247  C  C   . SER C  261 ? 3.3863 3.7762 3.0117 1.0298  0.1268  -0.4570 259  SER C C   
8248  O  O   . SER C  261 ? 3.2701 3.6576 2.8901 1.0459  0.0767  -0.4521 259  SER C O   
8249  C  CB  . SER C  261 ? 3.4954 3.9308 3.1322 1.0904  0.1631  -0.4252 259  SER C CB  
8250  O  OG  . SER C  261 ? 3.4550 3.8294 3.0376 1.1429  0.1167  -0.4061 259  SER C OG  
8251  N  N   . THR C  262 ? 3.4393 3.7300 3.0211 1.0129  0.1742  -0.4641 260  THR C N   
8252  C  CA  . THR C  262 ? 3.4821 3.6567 3.0122 1.0178  0.1714  -0.4603 260  THR C CA  
8253  C  C   . THR C  262 ? 3.4220 3.4759 2.8692 1.0734  0.1644  -0.4286 260  THR C C   
8254  O  O   . THR C  262 ? 3.5416 3.5180 2.9433 1.0748  0.2116  -0.4235 260  THR C O   
8255  C  CB  . THR C  262 ? 3.5820 3.7187 3.1134 0.9625  0.2336  -0.4843 260  THR C CB  
8256  O  OG1 . THR C  262 ? 3.5623 3.8108 3.1562 0.8982  0.2385  -0.5163 260  THR C OG1 
8257  C  CG2 . THR C  262 ? 3.5509 3.5713 3.0409 0.9761  0.2376  -0.4717 260  THR C CG2 
8258  N  N   . GLU C  263 ? 3.2621 3.2967 2.6820 1.1138  0.1055  -0.4075 261  GLU C N   
8259  C  CA  . GLU C  263 ? 3.2667 3.1914 2.5959 1.1566  0.0888  -0.3769 261  GLU C CA  
8260  C  C   . GLU C  263 ? 3.2505 3.0865 2.5458 1.1616  0.0804  -0.3557 261  GLU C C   
8261  O  O   . GLU C  263 ? 3.1594 3.0213 2.5015 1.1495  0.0635  -0.3586 261  GLU C O   
8262  C  CB  . GLU C  263 ? 3.2989 3.2399 2.6055 1.1902  0.0318  -0.3638 261  GLU C CB  
8263  C  CG  . GLU C  263 ? 3.3728 3.1998 2.5678 1.2233  0.0171  -0.3368 261  GLU C CG  
8264  C  CD  . GLU C  263 ? 3.2805 3.0680 2.4296 1.2323  0.0710  -0.3383 261  GLU C CD  
8265  O  OE1 . GLU C  263 ? 3.1854 3.0611 2.4026 1.2253  0.1052  -0.3552 261  GLU C OE1 
8266  O  OE2 . GLU C  263 ? 3.3695 3.0407 2.4152 1.2451  0.0797  -0.3196 261  GLU C OE2 
8267  N  N   . LYS C  264 ? 3.5156 3.2465 2.7300 1.1804  0.0960  -0.3306 262  LYS C N   
8268  C  CA  . LYS C  264 ? 3.5360 3.1866 2.7136 1.1963  0.0780  -0.2946 262  LYS C CA  
8269  C  C   . LYS C  264 ? 3.5116 3.1342 2.6322 1.2248  0.0044  -0.2619 262  LYS C C   
8270  O  O   . LYS C  264 ? 3.4234 3.0130 2.5361 1.2373  -0.0279 -0.2258 262  LYS C O   
8271  C  CB  . LYS C  264 ? 3.6770 3.2285 2.7923 1.1980  0.1332  -0.2791 262  LYS C CB  
8272  C  CG  . LYS C  264 ? 3.7261 3.2014 2.8157 1.2168  0.1258  -0.2336 262  LYS C CG  
8273  C  CD  . LYS C  264 ? 3.6993 3.2173 2.8787 1.2076  0.1305  -0.2362 262  LYS C CD  
8274  C  CE  . LYS C  264 ? 3.7308 3.1816 2.8999 1.2360  0.1264  -0.1798 262  LYS C CE  
8275  N  NZ  . LYS C  264 ? 3.5760 3.0591 2.8330 1.2329  0.1381  -0.1780 262  LYS C NZ  
8276  N  N   . ASN C  265 ? 3.4847 3.1210 2.5676 1.2334  -0.0195 -0.2715 263  ASN C N   
8277  C  CA  . ASN C  265 ? 3.4149 3.0152 2.4267 1.2500  -0.0834 -0.2479 263  ASN C CA  
8278  C  C   . ASN C  265 ? 3.3276 3.0111 2.4029 1.2494  -0.1313 -0.2594 263  ASN C C   
8279  O  O   . ASN C  265 ? 3.1808 2.9454 2.3535 1.2368  -0.1214 -0.2798 263  ASN C O   
8280  C  CB  . ASN C  265 ? 3.5873 3.1235 2.4989 1.2592  -0.0666 -0.2520 263  ASN C CB  
8281  C  CG  . ASN C  265 ? 3.7830 3.2095 2.5966 1.2605  -0.0360 -0.2308 263  ASN C CG  
8282  O  OD1 . ASN C  265 ? 3.8380 3.2107 2.6058 1.2615  -0.0673 -0.1948 263  ASN C OD1 
8283  N  ND2 . ASN C  265 ? 3.8816 3.2780 2.6653 1.2613  0.0261  -0.2487 263  ASN C ND2 
8284  N  N   . CYS C  266 ? 3.4367 3.0907 2.4445 1.2587  -0.1809 -0.2475 264  CYS C N   
8285  C  CA  . CYS C  266 ? 3.3953 3.1098 2.4437 1.2592  -0.2281 -0.2547 264  CYS C CA  
8286  C  C   . CYS C  266 ? 3.1741 2.9715 2.2880 1.2611  -0.2018 -0.2888 264  CYS C C   
8287  O  O   . CYS C  266 ? 3.2936 3.0759 2.3620 1.2750  -0.1924 -0.2959 264  CYS C O   
8288  C  CB  . CYS C  266 ? 3.5851 3.2309 2.5254 1.2622  -0.2774 -0.2367 264  CYS C CB  
8289  S  SG  . CYS C  266 ? 3.5997 3.3026 2.5724 1.2621  -0.3275 -0.2478 264  CYS C SG  
8290  N  N   . CYS C  267 ? 2.9925 2.8751 2.2099 1.2463  -0.1864 -0.3067 265  CYS C N   
8291  C  CA  . CYS C  267 ? 2.9410 2.9220 2.2300 1.2405  -0.1691 -0.3336 265  CYS C CA  
8292  C  C   . CYS C  267 ? 2.9189 2.9662 2.2708 1.2310  -0.2080 -0.3408 265  CYS C C   
8293  O  O   . CYS C  267 ? 2.9396 2.9712 2.3114 1.2217  -0.2251 -0.3316 265  CYS C O   
8294  C  CB  . CYS C  267 ? 3.2640 3.2867 2.6069 1.2168  -0.1114 -0.3526 265  CYS C CB  
8295  S  SG  . CYS C  267 ? 3.7642 3.9254 3.1966 1.2000  -0.0887 -0.3783 265  CYS C SG  
8296  N  N   . VAL C  268 ? 3.0541 3.1749 2.4391 1.2359  -0.2180 -0.3533 266  VAL C N   
8297  C  CA  . VAL C  268 ? 3.0251 3.2074 2.4633 1.2251  -0.2514 -0.3617 266  VAL C CA  
8298  C  C   . VAL C  268 ? 2.8582 3.1125 2.3728 1.1873  -0.2233 -0.3846 266  VAL C C   
8299  O  O   . VAL C  268 ? 2.9967 3.3183 2.5459 1.1719  -0.1933 -0.3986 266  VAL C O   
8300  C  CB  . VAL C  268 ? 2.9913 3.2174 2.4266 1.2463  -0.2728 -0.3616 266  VAL C CB  
8301  C  CG1 . VAL C  268 ? 3.0334 3.3081 2.4831 1.2595  -0.2355 -0.3628 266  VAL C CG1 
8302  C  CG2 . VAL C  268 ? 2.8532 3.1563 2.3499 1.2291  -0.2980 -0.3737 266  VAL C CG2 
8303  N  N   . ARG C  269 ? 2.5164 2.7552 2.0557 1.1690  -0.2294 -0.3868 267  ARG C N   
8304  C  CA  . ARG C  269 ? 2.5687 2.8474 2.1597 1.1262  -0.1943 -0.4112 267  ARG C CA  
8305  C  C   . ARG C  269 ? 2.5172 2.8743 2.1471 1.1057  -0.2174 -0.4284 267  ARG C C   
8306  O  O   . ARG C  269 ? 2.3962 2.7545 2.0192 1.1272  -0.2597 -0.4180 267  ARG C O   
8307  C  CB  . ARG C  269 ? 2.6193 2.8237 2.2125 1.1197  -0.1725 -0.4015 267  ARG C CB  
8308  C  CG  . ARG C  269 ? 2.6951 2.8172 2.2436 1.1433  -0.1566 -0.3758 267  ARG C CG  
8309  C  CD  . ARG C  269 ? 2.7945 2.9214 2.3286 1.1294  -0.1111 -0.3907 267  ARG C CD  
8310  N  NE  . ARG C  269 ? 2.9607 3.0033 2.4357 1.1555  -0.1009 -0.3645 267  ARG C NE  
8311  C  CZ  . ARG C  269 ? 3.1594 3.1839 2.6081 1.1512  -0.0602 -0.3708 267  ARG C CZ  
8312  N  NH1 . ARG C  269 ? 3.3397 3.4373 2.8274 1.1209  -0.0278 -0.4005 267  ARG C NH1 
8313  N  NH2 . ARG C  269 ? 3.1295 3.0669 2.5125 1.1741  -0.0527 -0.3452 267  ARG C NH2 
8314  N  N   . GLN C  270 ? 2.6665 3.0865 2.3303 1.0586  -0.1889 -0.4549 268  GLN C N   
8315  C  CA  . GLN C  270 ? 2.6984 3.1969 2.3899 1.0296  -0.2095 -0.4716 268  GLN C CA  
8316  C  C   . GLN C  270 ? 2.5932 3.0415 2.2869 1.0118  -0.2064 -0.4797 268  GLN C C   
8317  O  O   . GLN C  270 ? 2.5552 2.9330 2.2462 0.9967  -0.1651 -0.4838 268  GLN C O   
8318  C  CB  . GLN C  270 ? 2.8109 3.3977 2.5295 0.9740  -0.1829 -0.4954 268  GLN C CB  
8319  C  CG  . GLN C  270 ? 2.8360 3.5165 2.5753 0.9372  -0.2093 -0.5088 268  GLN C CG  
8320  C  CD  . GLN C  270 ? 2.9591 3.7325 2.7212 0.8691  -0.1870 -0.5303 268  GLN C CD  
8321  O  OE1 . GLN C  270 ? 2.9155 3.6838 2.6826 0.8507  -0.1482 -0.5368 268  GLN C OE1 
8322  N  NE2 . GLN C  270 ? 3.0887 3.9486 2.8608 0.8261  -0.2121 -0.5406 268  GLN C NE2 
8323  N  N   . LEU C  271 ? 2.6007 3.0808 2.2998 1.0169  -0.2445 -0.4792 269  LEU C N   
8324  C  CA  . LEU C  271 ? 2.6179 3.0545 2.3227 1.0006  -0.2384 -0.4865 269  LEU C CA  
8325  C  C   . LEU C  271 ? 2.7616 3.2626 2.4684 0.9858  -0.2721 -0.4967 269  LEU C C   
8326  O  O   . LEU C  271 ? 3.0207 3.5411 2.7215 1.0246  -0.3162 -0.4788 269  LEU C O   
8327  C  CB  . LEU C  271 ? 2.4870 2.8474 2.1907 1.0463  -0.2534 -0.4567 269  LEU C CB  
8328  C  CG  . LEU C  271 ? 2.4430 2.7647 2.1674 1.0378  -0.2449 -0.4563 269  LEU C CG  
8329  C  CD1 . LEU C  271 ? 2.5651 2.8448 2.2975 0.9946  -0.1775 -0.4773 269  LEU C CD1 
8330  C  CD2 . LEU C  271 ? 2.5195 2.7911 2.2552 1.0823  -0.2690 -0.4184 269  LEU C CD2 
8331  N  N   . TYR C  272 ? 2.6034 3.1285 2.3082 0.9266  -0.2485 -0.5251 270  TYR C N   
8332  C  CA  . TYR C  272 ? 2.5170 3.0945 2.2137 0.9041  -0.2768 -0.5350 270  TYR C CA  
8333  C  C   . TYR C  272 ? 2.4971 2.9950 2.1880 0.8998  -0.2612 -0.5403 270  TYR C C   
8334  O  O   . TYR C  272 ? 2.6711 3.1021 2.3574 0.8666  -0.2072 -0.5568 270  TYR C O   
8335  C  CB  . TYR C  272 ? 2.6942 3.3474 2.3808 0.8319  -0.2636 -0.5619 270  TYR C CB  
8336  C  CG  . TYR C  272 ? 2.7954 3.4961 2.4612 0.7978  -0.2902 -0.5721 270  TYR C CG  
8337  C  CD1 . TYR C  272 ? 2.7789 3.5699 2.4541 0.8276  -0.3449 -0.5494 270  TYR C CD1 
8338  C  CD2 . TYR C  272 ? 2.9947 3.6407 2.6243 0.7362  -0.2548 -0.6026 270  TYR C CD2 
8339  C  CE1 . TYR C  272 ? 2.9003 3.7334 2.5509 0.7973  -0.3703 -0.5547 270  TYR C CE1 
8340  C  CE2 . TYR C  272 ? 3.1510 3.8323 2.7487 0.7007  -0.2783 -0.6123 270  TYR C CE2 
8341  C  CZ  . TYR C  272 ? 3.1531 3.9321 2.7622 0.7315  -0.3394 -0.5872 270  TYR C CZ  
8342  O  OH  . TYR C  272 ? 3.3918 4.2050 2.9639 0.6972  -0.3641 -0.5927 270  TYR C OH  
8343  N  N   . ILE C  273 ? 2.5446 3.0452 2.2360 0.9336  -0.3014 -0.5250 271  ILE C N   
8344  C  CA  . ILE C  273 ? 2.6730 3.1050 2.3701 0.9376  -0.2892 -0.5236 271  ILE C CA  
8345  C  C   . ILE C  273 ? 2.8742 3.3318 2.5433 0.8959  -0.2946 -0.5451 271  ILE C C   
8346  O  O   . ILE C  273 ? 3.0213 3.5408 2.6770 0.9086  -0.3410 -0.5378 271  ILE C O   
8347  C  CB  . ILE C  273 ? 2.5448 2.9535 2.2581 0.9979  -0.3285 -0.4911 271  ILE C CB  
8348  C  CG1 . ILE C  273 ? 2.3216 2.6975 2.0499 1.0312  -0.3236 -0.4682 271  ILE C CG1 
8349  C  CG2 . ILE C  273 ? 2.7837 3.1406 2.5147 0.9990  -0.3182 -0.4867 271  ILE C CG2 
8350  C  CD1 . ILE C  273 ? 2.2448 2.5932 1.9790 1.0773  -0.3628 -0.4359 271  ILE C CD1 
8351  N  N   . ASP C  274 ? 2.8510 3.2526 2.5045 0.8468  -0.2424 -0.5697 272  ASP C N   
8352  C  CA  . ASP C  274 ? 2.8159 3.2192 2.4281 0.7997  -0.2391 -0.5924 272  ASP C CA  
8353  C  C   . ASP C  274 ? 2.7463 3.0792 2.3738 0.8252  -0.2279 -0.5824 272  ASP C C   
8354  O  O   . ASP C  274 ? 2.7003 2.9665 2.3696 0.8531  -0.1936 -0.5671 272  ASP C O   
8355  C  CB  . ASP C  274 ? 2.9890 3.3599 2.5557 0.7184  -0.1806 -0.6302 272  ASP C CB  
8356  C  CG  . ASP C  274 ? 3.1623 3.5555 2.6651 0.6554  -0.1890 -0.6552 272  ASP C CG  
8357  O  OD1 . ASP C  274 ? 3.1298 3.5106 2.6255 0.6755  -0.2105 -0.6470 272  ASP C OD1 
8358  O  OD2 . ASP C  274 ? 3.3324 3.7548 2.7865 0.5806  -0.1744 -0.6826 272  ASP C OD2 
8359  N  N   . PHE C  275 ? 2.7714 3.1246 2.3688 0.8160  -0.2564 -0.5869 273  PHE C N   
8360  C  CA  . PHE C  275 ? 2.7756 3.0667 2.3875 0.8354  -0.2444 -0.5787 273  PHE C CA  
8361  C  C   . PHE C  275 ? 2.8840 3.0865 2.4722 0.7849  -0.1683 -0.6047 273  PHE C C   
8362  O  O   . PHE C  275 ? 2.8497 2.9817 2.4812 0.8077  -0.1274 -0.5915 273  PHE C O   
8363  C  CB  . PHE C  275 ? 2.6924 3.0262 2.2734 0.8452  -0.2970 -0.5736 273  PHE C CB  
8364  C  CG  . PHE C  275 ? 2.5047 2.9018 2.1026 0.9002  -0.3593 -0.5458 273  PHE C CG  
8365  C  CD1 . PHE C  275 ? 2.3375 2.7076 1.9707 0.9523  -0.3797 -0.5202 273  PHE C CD1 
8366  C  CD2 . PHE C  275 ? 2.5001 2.9823 2.0768 0.8969  -0.3935 -0.5435 273  PHE C CD2 
8367  C  CE1 . PHE C  275 ? 2.1517 2.5594 1.7818 0.9968  -0.4280 -0.4983 273  PHE C CE1 
8368  C  CE2 . PHE C  275 ? 2.3165 2.8419 1.9041 0.9506  -0.4377 -0.5167 273  PHE C CE2 
8369  C  CZ  . PHE C  275 ? 2.1353 2.6136 1.7410 0.9990  -0.4523 -0.4969 273  PHE C CZ  
8370  N  N   . ARG C  276 ? 2.9701 3.1745 2.4882 0.7136  -0.1460 -0.6395 274  ARG C N   
8371  C  CA  . ARG C  276 ? 3.1103 3.2115 2.5822 0.6556  -0.0643 -0.6698 274  ARG C CA  
8372  C  C   . ARG C  276 ? 3.1489 3.1775 2.6445 0.6501  0.0092  -0.6737 274  ARG C C   
8373  O  O   . ARG C  276 ? 3.2111 3.1298 2.7054 0.6391  0.0904  -0.6804 274  ARG C O   
8374  C  CB  . ARG C  276 ? 3.3092 3.4340 2.6793 0.5690  -0.0694 -0.7067 274  ARG C CB  
8375  C  CG  . ARG C  276 ? 3.3806 3.5512 2.7127 0.5678  -0.1248 -0.7022 274  ARG C CG  
8376  C  CD  . ARG C  276 ? 3.6399 3.7003 2.9432 0.5558  -0.0712 -0.7136 274  ARG C CD  
8377  N  NE  . ARG C  276 ? 3.8636 3.8362 3.0669 0.4637  -0.0018 -0.7565 274  ARG C NE  
8378  C  CZ  . ARG C  276 ? 3.9191 3.7700 3.1164 0.4411  0.0952  -0.7745 274  ARG C CZ  
8379  N  NH1 . ARG C  276 ? 3.9105 3.7269 3.2080 0.5088  0.1290  -0.7471 274  ARG C NH1 
8380  N  NH2 . ARG C  276 ? 3.9000 3.6590 2.9854 0.3492  0.1612  -0.8173 274  ARG C NH2 
8381  N  N   . LYS C  277 ? 3.0904 3.1721 2.6083 0.6615  -0.0114 -0.6667 275  LYS C N   
8382  C  CA  . LYS C  277 ? 3.1896 3.2025 2.7153 0.6492  0.0595  -0.6727 275  LYS C CA  
8383  C  C   . LYS C  277 ? 3.1798 3.1693 2.7969 0.7305  0.0670  -0.6279 275  LYS C C   
8384  O  O   . LYS C  277 ? 3.2054 3.0991 2.8441 0.7380  0.1460  -0.6200 275  LYS C O   
8385  C  CB  . LYS C  277 ? 3.2867 3.3680 2.7780 0.6050  0.0396  -0.6925 275  LYS C CB  
8386  C  CG  . LYS C  277 ? 3.4245 3.4298 2.9114 0.5852  0.1158  -0.7027 275  LYS C CG  
8387  C  CD  . LYS C  277 ? 3.6693 3.5451 3.0838 0.5146  0.2147  -0.7397 275  LYS C CD  
8388  C  CE  . LYS C  277 ? 3.8503 3.6389 3.2502 0.4924  0.2987  -0.7507 275  LYS C CE  
8389  N  NZ  . LYS C  277 ? 3.7650 3.5214 3.2576 0.5856  0.3154  -0.7016 275  LYS C NZ  
8390  N  N   . ASP C  278 ? 3.0755 3.1469 2.7419 0.7902  -0.0110 -0.5954 276  ASP C N   
8391  C  CA  . ASP C  278 ? 3.0369 3.0991 2.7773 0.8585  -0.0173 -0.5508 276  ASP C CA  
8392  C  C   . ASP C  278 ? 2.9764 3.0420 2.7747 0.9096  -0.0477 -0.5153 276  ASP C C   
8393  O  O   . ASP C  278 ? 2.8412 2.9065 2.7026 0.9618  -0.0592 -0.4727 276  ASP C O   
8394  C  CB  . ASP C  278 ? 2.8723 3.0101 2.6147 0.8822  -0.0762 -0.5398 276  ASP C CB  
8395  C  CG  . ASP C  278 ? 2.9118 3.0579 2.6084 0.8303  -0.0466 -0.5718 276  ASP C CG  
8396  O  OD1 . ASP C  278 ? 3.0317 3.0996 2.7051 0.7889  0.0313  -0.5926 276  ASP C OD1 
8397  O  OD2 . ASP C  278 ? 2.8764 3.1043 2.5599 0.8291  -0.0964 -0.5751 276  ASP C OD2 
8398  N  N   . LEU C  279 ? 2.9349 3.0068 2.7105 0.8923  -0.0631 -0.5298 277  LEU C N   
8399  C  CA  . LEU C  279 ? 2.7899 2.8661 2.6181 0.9327  -0.0896 -0.4994 277  LEU C CA  
8400  C  C   . LEU C  279 ? 2.7221 2.7364 2.5370 0.9031  -0.0358 -0.5169 277  LEU C C   
8401  O  O   . LEU C  279 ? 2.6482 2.6378 2.5274 0.9327  -0.0181 -0.4883 277  LEU C O   
8402  C  CB  . LEU C  279 ? 2.6891 2.8425 2.4994 0.9539  -0.1794 -0.4932 277  LEU C CB  
8403  C  CG  . LEU C  279 ? 2.4657 2.6659 2.2937 0.9942  -0.2325 -0.4668 277  LEU C CG  
8404  C  CD1 . LEU C  279 ? 2.3648 2.6201 2.1594 1.0111  -0.3053 -0.4648 277  LEU C CD1 
8405  C  CD2 . LEU C  279 ? 2.3541 2.5335 2.2567 1.0355  -0.2272 -0.4217 277  LEU C CD2 
8406  N  N   . GLY C  280 ? 2.6960 2.6875 2.4263 0.8412  -0.0098 -0.5620 278  GLY C N   
8407  C  CA  . GLY C  280 ? 2.8176 2.7400 2.5130 0.8056  0.0420  -0.5832 278  GLY C CA  
8408  C  C   . GLY C  280 ? 2.8994 2.8621 2.5896 0.8198  -0.0160 -0.5773 278  GLY C C   
8409  O  O   . GLY C  280 ? 3.1031 3.0168 2.8224 0.8291  0.0179  -0.5678 278  GLY C O   
8410  N  N   . TRP C  281 ? 2.8497 2.8977 2.5063 0.8245  -0.0974 -0.5798 279  TRP C N   
8411  C  CA  . TRP C  281 ? 2.7892 2.8716 2.4313 0.8411  -0.1528 -0.5726 279  TRP C CA  
8412  C  C   . TRP C  281 ? 2.9276 3.0376 2.4717 0.7905  -0.1750 -0.6033 279  TRP C C   
8413  O  O   . TRP C  281 ? 2.9459 3.1304 2.4628 0.7841  -0.2200 -0.6061 279  TRP C O   
8414  C  CB  . TRP C  281 ? 2.6024 2.7535 2.2869 0.8977  -0.2262 -0.5405 279  TRP C CB  
8415  C  CG  . TRP C  281 ? 2.4868 2.6231 2.2609 0.9425  -0.2204 -0.5041 279  TRP C CG  
8416  C  CD1 . TRP C  281 ? 2.4812 2.5620 2.3181 0.9467  -0.1570 -0.4900 279  TRP C CD1 
8417  C  CD2 . TRP C  281 ? 2.4204 2.6007 2.2300 0.9877  -0.2803 -0.4723 279  TRP C CD2 
8418  N  NE1 . TRP C  281 ? 2.5471 2.6515 2.4664 0.9926  -0.1818 -0.4461 279  TRP C NE1 
8419  C  CE2 . TRP C  281 ? 2.6355 2.7967 2.5311 1.0130  -0.2590 -0.4378 279  TRP C CE2 
8420  C  CE3 . TRP C  281 ? 2.1559 2.3853 1.9286 1.0080  -0.3461 -0.4673 279  TRP C CE3 
8421  C  CZ2 . TRP C  281 ? 2.6325 2.8272 2.5698 1.0487  -0.3097 -0.4010 279  TRP C CZ2 
8422  C  CZ3 . TRP C  281 ? 2.0423 2.2859 1.8471 1.0439  -0.3866 -0.4360 279  TRP C CZ3 
8423  C  CH2 . TRP C  281 ? 2.3355 2.5643 2.2179 1.0594  -0.3726 -0.4043 279  TRP C CH2 
8424  N  N   . LYS C  282 ? 3.3023 3.3565 2.7954 0.7549  -0.1435 -0.6222 280  LYS C N   
8425  C  CA  . LYS C  282 ? 3.3883 3.4680 2.7818 0.7042  -0.1685 -0.6454 280  LYS C CA  
8426  C  C   . LYS C  282 ? 3.4152 3.5245 2.7948 0.7357  -0.2225 -0.6283 280  LYS C C   
8427  O  O   . LYS C  282 ? 3.4503 3.5724 2.7474 0.6996  -0.2415 -0.6404 280  LYS C O   
8428  C  CB  . LYS C  282 ? 3.4939 3.4767 2.8107 0.6307  -0.0922 -0.6822 280  LYS C CB  
8429  C  CG  . LYS C  282 ? 3.4999 3.5166 2.7010 0.5548  -0.1144 -0.7100 280  LYS C CG  
8430  C  CD  . LYS C  282 ? 3.5544 3.4570 2.6651 0.4706  -0.0290 -0.7515 280  LYS C CD  
8431  C  CE  . LYS C  282 ? 3.5307 3.3211 2.6254 0.4731  0.0287  -0.7567 280  LYS C CE  
8432  N  NZ  . LYS C  282 ? 3.6872 3.3476 2.6779 0.3880  0.1224  -0.7991 280  LYS C NZ  
8433  N  N   . TRP C  283 ? 3.2409 3.3587 2.6931 0.7985  -0.2472 -0.5990 281  TRP C N   
8434  C  CA  . TRP C  283 ? 3.1636 3.2952 2.6014 0.8294  -0.2913 -0.5829 281  TRP C CA  
8435  C  C   . TRP C  283 ? 3.0889 3.3060 2.5177 0.8665  -0.3621 -0.5624 281  TRP C C   
8436  O  O   . TRP C  283 ? 3.1591 3.3826 2.5654 0.8944  -0.3962 -0.5476 281  TRP C O   
8437  C  CB  . TRP C  283 ? 3.0788 3.1666 2.5936 0.8671  -0.2751 -0.5629 281  TRP C CB  
8438  C  CG  . TRP C  283 ? 2.9086 3.0282 2.5057 0.9089  -0.2935 -0.5377 281  TRP C CG  
8439  C  CD1 . TRP C  283 ? 2.8930 2.9985 2.5495 0.9094  -0.2548 -0.5331 281  TRP C CD1 
8440  C  CD2 . TRP C  283 ? 2.6675 2.8286 2.2854 0.9540  -0.3522 -0.5123 281  TRP C CD2 
8441  N  NE1 . TRP C  283 ? 2.7960 2.9398 2.5101 0.9517  -0.2921 -0.5042 281  TRP C NE1 
8442  C  CE2 . TRP C  283 ? 2.6428 2.8175 2.3297 0.9760  -0.3514 -0.4934 281  TRP C CE2 
8443  C  CE3 . TRP C  283 ? 2.5917 2.7691 2.1673 0.9764  -0.4002 -0.5031 281  TRP C CE3 
8444  C  CZ2 . TRP C  283 ? 2.4710 2.6746 2.1778 1.0127  -0.4002 -0.4686 281  TRP C CZ2 
8445  C  CZ3 . TRP C  283 ? 2.5805 2.7784 2.1760 1.0140  -0.4414 -0.4804 281  TRP C CZ3 
8446  C  CH2 . TRP C  283 ? 2.4643 2.6749 2.1212 1.0286  -0.4428 -0.4648 281  TRP C CH2 
8447  N  N   . ILE C  284 ? 2.7585 3.0341 2.2020 0.8682  -0.3778 -0.5603 282  ILE C N   
8448  C  CA  . ILE C  284 ? 2.5428 2.8985 1.9811 0.9043  -0.4337 -0.5389 282  ILE C CA  
8449  C  C   . ILE C  284 ? 2.6041 3.0302 1.9909 0.8622  -0.4480 -0.5479 282  ILE C C   
8450  O  O   . ILE C  284 ? 2.6723 3.1171 2.0627 0.8219  -0.4265 -0.5652 282  ILE C O   
8451  C  CB  . ILE C  284 ? 2.3719 2.7461 1.8702 0.9407  -0.4416 -0.5245 282  ILE C CB  
8452  C  CG1 . ILE C  284 ? 2.3547 2.6727 1.9008 0.9757  -0.4378 -0.5095 282  ILE C CG1 
8453  C  CG2 . ILE C  284 ? 2.2181 2.6676 1.7052 0.9754  -0.4871 -0.5036 282  ILE C CG2 
8454  C  CD1 . ILE C  284 ? 2.5362 2.8667 2.1283 1.0082  -0.4500 -0.4921 282  ILE C CD1 
8455  N  N   . HIS C  285 ? 2.6649 3.1335 2.0037 0.8700  -0.4848 -0.5328 283  HIS C N   
8456  C  CA  . HIS C  285 ? 2.8440 3.3959 2.1357 0.8255  -0.5063 -0.5332 283  HIS C CA  
8457  C  C   . HIS C  285 ? 2.6884 3.3439 2.0224 0.8466  -0.5349 -0.5130 283  HIS C C   
8458  O  O   . HIS C  285 ? 2.8122 3.5184 2.1457 0.7954  -0.5279 -0.5274 283  HIS C O   
8459  C  CB  . HIS C  285 ? 3.1001 3.6713 2.3316 0.8332  -0.5378 -0.5137 283  HIS C CB  
8460  C  CG  . HIS C  285 ? 3.2274 3.6993 2.4049 0.8007  -0.5059 -0.5363 283  HIS C CG  
8461  N  ND1 . HIS C  285 ? 3.1635 3.5361 2.3726 0.8240  -0.4710 -0.5465 283  HIS C ND1 
8462  C  CD2 . HIS C  285 ? 3.3359 3.7931 2.4291 0.7441  -0.5020 -0.5487 283  HIS C CD2 
8463  C  CE1 . HIS C  285 ? 3.2793 3.5786 2.4326 0.7871  -0.4415 -0.5647 283  HIS C CE1 
8464  N  NE2 . HIS C  285 ? 3.4349 3.7759 2.5097 0.7376  -0.4585 -0.5683 283  HIS C NE2 
8465  N  N   . GLU C  286 ? 2.5688 3.2492 1.9356 0.9184  -0.5613 -0.4806 284  GLU C N   
8466  C  CA  . GLU C  286 ? 2.5271 3.2983 1.9367 0.9461  -0.5809 -0.4579 284  GLU C CA  
8467  C  C   . GLU C  286 ? 2.4518 3.1767 1.9028 1.0081  -0.5747 -0.4468 284  GLU C C   
8468  O  O   . GLU C  286 ? 2.5916 3.2518 2.0297 1.0507  -0.5784 -0.4362 284  GLU C O   
8469  C  CB  . GLU C  286 ? 2.6281 3.5035 2.0247 0.9706  -0.6212 -0.4175 284  GLU C CB  
8470  C  CG  . GLU C  286 ? 2.7300 3.6789 2.0839 0.9013  -0.6386 -0.4212 284  GLU C CG  
8471  C  CD  . GLU C  286 ? 2.5958 3.6124 1.9690 0.8349  -0.6311 -0.4417 284  GLU C CD  
8472  O  OE1 . GLU C  286 ? 2.4229 3.4679 1.8548 0.8592  -0.6226 -0.4374 284  GLU C OE1 
8473  O  OE2 . GLU C  286 ? 2.6889 3.7216 2.0094 0.7537  -0.6306 -0.4639 284  GLU C OE2 
8474  N  N   . PRO C  287 ? 2.3668 3.1193 1.8594 1.0066  -0.5637 -0.4505 285  PRO C N   
8475  C  CA  . PRO C  287 ? 2.3685 3.1874 1.8711 0.9462  -0.5537 -0.4678 285  PRO C CA  
8476  C  C   . PRO C  287 ? 2.5921 3.3295 2.0856 0.8908  -0.5110 -0.5076 285  PRO C C   
8477  O  O   . PRO C  287 ? 2.7971 3.4401 2.2899 0.9051  -0.4919 -0.5160 285  PRO C O   
8478  C  CB  . PRO C  287 ? 2.3407 3.2074 1.8911 0.9789  -0.5537 -0.4519 285  PRO C CB  
8479  C  CG  . PRO C  287 ? 2.4311 3.2048 1.9897 1.0353  -0.5459 -0.4454 285  PRO C CG  
8480  C  CD  . PRO C  287 ? 2.4907 3.2139 2.0133 1.0605  -0.5610 -0.4364 285  PRO C CD  
8481  N  N   . LYS C  288 ? 2.5933 3.3663 2.0803 0.8267  -0.4922 -0.5297 286  LYS C N   
8482  C  CA  . LYS C  288 ? 2.7533 3.4388 2.2266 0.7740  -0.4381 -0.5665 286  LYS C CA  
8483  C  C   . LYS C  288 ? 2.9594 3.6354 2.4751 0.7770  -0.4093 -0.5724 286  LYS C C   
8484  O  O   . LYS C  288 ? 3.0841 3.7195 2.5835 0.7200  -0.3629 -0.6014 286  LYS C O   
8485  C  CB  . LYS C  288 ? 2.8767 3.5771 2.2842 0.6844  -0.4258 -0.5943 286  LYS C CB  
8486  C  CG  . LYS C  288 ? 2.9667 3.6606 2.3192 0.6753  -0.4486 -0.5901 286  LYS C CG  
8487  C  CD  . LYS C  288 ? 2.9846 3.7101 2.2581 0.5796  -0.4477 -0.6131 286  LYS C CD  
8488  C  CE  . LYS C  288 ? 2.9094 3.6335 2.1221 0.5749  -0.4759 -0.6029 286  LYS C CE  
8489  N  NZ  . LYS C  288 ? 3.0026 3.7621 2.1244 0.4752  -0.4828 -0.6218 286  LYS C NZ  
8490  N  N   . GLY C  289 ? 2.9554 3.6569 2.5156 0.8419  -0.4313 -0.5452 287  GLY C N   
8491  C  CA  . GLY C  289 ? 2.8792 3.5725 2.4744 0.8516  -0.4080 -0.5457 287  GLY C CA  
8492  C  C   . GLY C  289 ? 2.7284 3.4926 2.3527 0.9060  -0.4415 -0.5150 287  GLY C C   
8493  O  O   . GLY C  289 ? 2.7433 3.5993 2.3659 0.9131  -0.4756 -0.4968 287  GLY C O   
8494  N  N   . TYR C  290 ? 2.7713 3.4919 2.4199 0.9462  -0.4294 -0.5050 288  TYR C N   
8495  C  CA  . TYR C  290 ? 2.6496 3.4148 2.3146 0.9988  -0.4505 -0.4773 288  TYR C CA  
8496  C  C   . TYR C  290 ? 2.6325 3.3507 2.3134 1.0121  -0.4230 -0.4776 288  TYR C C   
8497  O  O   . TYR C  290 ? 2.6152 3.2630 2.2979 0.9915  -0.3921 -0.4929 288  TYR C O   
8498  C  CB  . TYR C  290 ? 2.5969 3.3311 2.2442 1.0574  -0.4809 -0.4533 288  TYR C CB  
8499  C  CG  . TYR C  290 ? 2.4747 3.1038 2.1143 1.0841  -0.4759 -0.4512 288  TYR C CG  
8500  C  CD1 . TYR C  290 ? 2.4470 3.0157 2.0905 1.0590  -0.4610 -0.4661 288  TYR C CD1 
8501  C  CD2 . TYR C  290 ? 2.3334 2.9253 1.9605 1.1319  -0.4849 -0.4309 288  TYR C CD2 
8502  C  CE1 . TYR C  290 ? 2.2885 2.7820 1.9388 1.0822  -0.4613 -0.4555 288  TYR C CE1 
8503  C  CE2 . TYR C  290 ? 2.3765 2.8845 1.9933 1.1475  -0.4884 -0.4249 288  TYR C CE2 
8504  C  CZ  . TYR C  290 ? 2.4361 2.9048 2.0720 1.1233  -0.4798 -0.4345 288  TYR C CZ  
8505  O  OH  . TYR C  290 ? 2.7739 3.1790 2.4132 1.1379  -0.4878 -0.4202 288  TYR C OH  
8506  N  N   . HIS C  291 ? 2.4410 3.1944 2.1316 1.0502  -0.4300 -0.4569 289  HIS C N   
8507  C  CA  . HIS C  291 ? 2.4481 3.1595 2.1444 1.0648  -0.4047 -0.4542 289  HIS C CA  
8508  C  C   . HIS C  291 ? 2.5287 3.1545 2.1967 1.1191  -0.4187 -0.4344 289  HIS C C   
8509  O  O   . HIS C  291 ? 2.5496 3.1802 2.2000 1.1615  -0.4303 -0.4142 289  HIS C O   
8510  C  CB  . HIS C  291 ? 2.4722 3.2710 2.1934 1.0660  -0.3958 -0.4448 289  HIS C CB  
8511  C  CG  . HIS C  291 ? 2.7448 3.6268 2.4912 0.9987  -0.3804 -0.4654 289  HIS C CG  
8512  N  ND1 . HIS C  291 ? 2.9489 3.9064 2.6972 0.9588  -0.4018 -0.4718 289  HIS C ND1 
8513  C  CD2 . HIS C  291 ? 2.8406 3.7385 2.6022 0.9574  -0.3454 -0.4817 289  HIS C CD2 
8514  C  CE1 . HIS C  291 ? 2.9715 3.9900 2.7319 0.8905  -0.3834 -0.4920 289  HIS C CE1 
8515  N  NE2 . HIS C  291 ? 2.9756 3.9583 2.7461 0.8883  -0.3470 -0.4995 289  HIS C NE2 
8516  N  N   . ALA C  292 ? 2.5468 3.0924 2.2084 1.1153  -0.4148 -0.4379 290  ALA C N   
8517  C  CA  . ALA C  292 ? 2.3525 2.8227 1.9844 1.1538  -0.4330 -0.4176 290  ALA C CA  
8518  C  C   . ALA C  292 ? 2.3718 2.8033 1.9902 1.1668  -0.4147 -0.4080 290  ALA C C   
8519  O  O   . ALA C  292 ? 2.5464 2.9353 2.1212 1.1988  -0.4286 -0.3909 290  ALA C O   
8520  C  CB  . ALA C  292 ? 2.4190 2.8372 2.0621 1.1450  -0.4405 -0.4161 290  ALA C CB  
8521  N  N   . ASN C  293 ? 2.4210 2.8544 2.0655 1.1392  -0.3794 -0.4196 291  ASN C N   
8522  C  CA  . ASN C  293 ? 2.5904 2.9826 2.2208 1.1480  -0.3557 -0.4110 291  ASN C CA  
8523  C  C   . ASN C  293 ? 2.5152 2.8258 2.1178 1.1718  -0.3739 -0.3857 291  ASN C C   
8524  O  O   . ASN C  293 ? 2.3502 2.6428 1.9545 1.1776  -0.4036 -0.3757 291  ASN C O   
8525  C  CB  . ASN C  293 ? 2.6326 3.0568 2.2429 1.1680  -0.3506 -0.4065 291  ASN C CB  
8526  C  CG  . ASN C  293 ? 2.6088 3.1350 2.2600 1.1412  -0.3350 -0.4228 291  ASN C CG  
8527  O  OD1 . ASN C  293 ? 2.6307 3.1920 2.3113 1.0975  -0.3236 -0.4430 291  ASN C OD1 
8528  N  ND2 . ASN C  293 ? 2.6048 3.1790 2.2564 1.1646  -0.3320 -0.4114 291  ASN C ND2 
8529  N  N   . PHE C  294 ? 2.5243 2.7894 2.1010 1.1820  -0.3574 -0.3730 292  PHE C N   
8530  C  CA  . PHE C  294 ? 2.5474 2.7426 2.0910 1.1997  -0.3792 -0.3428 292  PHE C CA  
8531  C  C   . PHE C  294 ? 2.5646 2.7149 2.0573 1.2113  -0.3606 -0.3330 292  PHE C C   
8532  O  O   . PHE C  294 ? 2.5158 2.6896 2.0158 1.2039  -0.3225 -0.3501 292  PHE C O   
8533  C  CB  . PHE C  294 ? 2.4198 2.5978 2.0139 1.1899  -0.3683 -0.3290 292  PHE C CB  
8534  C  CG  . PHE C  294 ? 2.4547 2.6263 2.0787 1.1722  -0.3105 -0.3406 292  PHE C CG  
8535  C  CD1 . PHE C  294 ? 2.5012 2.7135 2.1608 1.1401  -0.2765 -0.3740 292  PHE C CD1 
8536  C  CD2 . PHE C  294 ? 2.6046 2.7226 2.2111 1.1828  -0.2886 -0.3179 292  PHE C CD2 
8537  C  CE1 . PHE C  294 ? 2.6731 2.8675 2.3473 1.1146  -0.2180 -0.3886 292  PHE C CE1 
8538  C  CE2 . PHE C  294 ? 2.7884 2.8880 2.4152 1.1650  -0.2279 -0.3296 292  PHE C CE2 
8539  C  CZ  . PHE C  294 ? 2.8245 2.9595 2.4838 1.1287  -0.1906 -0.3670 292  PHE C CZ  
8540  N  N   . CYS C  295 ? 2.5304 2.6168 1.9698 1.2247  -0.3878 -0.3036 293  CYS C N   
8541  C  CA  . CYS C  295 ? 2.6241 2.6501 1.9972 1.2340  -0.3731 -0.2903 293  CYS C CA  
8542  C  C   . CYS C  295 ? 2.8797 2.8712 2.2699 1.2322  -0.3620 -0.2629 293  CYS C C   
8543  O  O   . CYS C  295 ? 3.0617 3.0462 2.4688 1.2343  -0.3962 -0.2329 293  CYS C O   
8544  C  CB  . CYS C  295 ? 2.7256 2.6916 2.0011 1.2445  -0.4109 -0.2751 293  CYS C CB  
8545  S  SG  . CYS C  295 ? 3.1743 3.1566 2.4167 1.2563  -0.4164 -0.2976 293  CYS C SG  
8546  N  N   . LEU C  296 ? 3.1013 3.0750 2.4922 1.2293  -0.3117 -0.2696 294  LEU C N   
8547  C  CA  . LEU C  296 ? 3.1571 3.0864 2.5562 1.2329  -0.2899 -0.2406 294  LEU C CA  
8548  C  C   . LEU C  296 ? 3.1485 3.0193 2.4772 1.2376  -0.2592 -0.2376 294  LEU C C   
8549  O  O   . LEU C  296 ? 3.1317 3.0191 2.4591 1.2287  -0.2188 -0.2698 294  LEU C O   
8550  C  CB  . LEU C  296 ? 3.0733 3.0298 2.5557 1.2180  -0.2403 -0.2559 294  LEU C CB  
8551  C  CG  . LEU C  296 ? 3.0648 2.9826 2.5835 1.2289  -0.2184 -0.2175 294  LEU C CG  
8552  C  CD1 . LEU C  296 ? 3.2558 3.1092 2.7348 1.2345  -0.1717 -0.2042 294  LEU C CD1 
8553  C  CD2 . LEU C  296 ? 2.9974 2.9152 2.5187 1.2494  -0.2812 -0.1676 294  LEU C CD2 
8554  N  N   . GLY C  297 ? 3.0862 2.8931 2.3574 1.2496  -0.2788 -0.1962 295  GLY C N   
8555  C  CA  . GLY C  297 ? 3.1473 2.8852 2.3398 1.2534  -0.2487 -0.1903 295  GLY C CA  
8556  C  C   . GLY C  297 ? 3.2895 2.9585 2.3837 1.2605  -0.2954 -0.1463 295  GLY C C   
8557  O  O   . GLY C  297 ? 3.3731 3.0504 2.4424 1.2571  -0.3576 -0.1285 295  GLY C O   
8558  N  N   . PRO C  298 ? 3.4583 3.0562 2.4886 1.2651  -0.2663 -0.1275 296  PRO C N   
8559  C  CA  . PRO C  298 ? 3.5952 3.1205 2.5128 1.2648  -0.3104 -0.0842 296  PRO C CA  
8560  C  C   . PRO C  298 ? 3.5582 3.0211 2.3533 1.2548  -0.3131 -0.1077 296  PRO C C   
8561  O  O   . PRO C  298 ? 3.5557 3.0228 2.3553 1.2569  -0.2644 -0.1504 296  PRO C O   
8562  C  CB  . PRO C  298 ? 3.7312 3.2016 2.6341 1.2757  -0.2653 -0.0559 296  PRO C CB  
8563  C  CG  . PRO C  298 ? 3.6338 3.1178 2.5891 1.2734  -0.1853 -0.1051 296  PRO C CG  
8564  C  CD  . PRO C  298 ? 3.4309 3.0099 2.4894 1.2660  -0.1905 -0.1420 296  PRO C CD  
8565  N  N   . CYS C  299 ? 3.6609 3.0641 2.3436 1.2417  -0.3686 -0.0755 297  CYS C N   
8566  C  CA  . CYS C  299 ? 3.8849 3.2007 2.4245 1.2277  -0.3675 -0.0939 297  CYS C CA  
8567  C  C   . CYS C  299 ? 4.2164 3.4309 2.6130 1.2116  -0.3911 -0.0524 297  CYS C C   
8568  O  O   . CYS C  299 ? 4.3401 3.5386 2.6677 1.1871  -0.4628 -0.0182 297  CYS C O   
8569  C  CB  . CYS C  299 ? 3.8438 3.1781 2.3623 1.2132  -0.4160 -0.1082 297  CYS C CB  
8570  S  SG  . CYS C  299 ? 3.5351 2.9867 2.2073 1.2303  -0.3977 -0.1510 297  CYS C SG  
8571  N  N   . PRO C  300 ? 4.5258 3.6709 2.8707 1.2203  -0.3327 -0.0528 298  PRO C N   
8572  C  CA  . PRO C  300 ? 4.6398 3.6796 2.8342 1.2034  -0.3528 -0.0121 298  PRO C CA  
8573  C  C   . PRO C  300 ? 4.7281 3.6426 2.7450 1.1817  -0.3331 -0.0360 298  PRO C C   
8574  O  O   . PRO C  300 ? 4.7372 3.6470 2.7570 1.1872  -0.2953 -0.0823 298  PRO C O   
8575  C  CB  . PRO C  300 ? 4.6096 3.6367 2.8487 1.2264  -0.2917 0.0004  298  PRO C CB  
8576  C  CG  . PRO C  300 ? 4.5296 3.6216 2.8957 1.2449  -0.2199 -0.0537 298  PRO C CG  
8577  C  CD  . PRO C  300 ? 4.4581 3.6213 2.8792 1.2410  -0.2473 -0.0875 298  PRO C CD  
8578  N  N   . TYR C  301 ? 4.7911 3.5989 2.6479 1.1571  -0.3552 -0.0018 299  TYR C N   
8579  C  CA  . TYR C  301 ? 4.9798 3.6428 2.6415 1.1303  -0.3304 -0.0232 299  TYR C CA  
8580  C  C   . TYR C  301 ? 5.0600 3.6572 2.7059 1.1549  -0.2245 -0.0580 299  TYR C C   
8581  O  O   . TYR C  301 ? 5.2286 3.6872 2.7085 1.1386  -0.1895 -0.0576 299  TYR C O   
8582  C  CB  . TYR C  301 ? 5.1360 3.7027 2.6174 1.0868  -0.3916 0.0263  299  TYR C CB  
8583  C  CG  . TYR C  301 ? 5.0622 3.7158 2.5782 1.0607  -0.5001 0.0733  299  TYR C CG  
8584  C  CD1 . TYR C  301 ? 5.0140 3.6695 2.4802 1.0238  -0.5518 0.0582  299  TYR C CD1 
8585  C  CD2 . TYR C  301 ? 5.0625 3.7968 2.6658 1.0741  -0.5459 0.1360  299  TYR C CD2 
8586  C  CE1 . TYR C  301 ? 5.0288 3.7738 2.5360 0.9960  -0.6502 0.1023  299  TYR C CE1 
8587  C  CE2 . TYR C  301 ? 5.1129 3.9412 2.7653 1.0532  -0.6426 0.1860  299  TYR C CE2 
8588  C  CZ  . TYR C  301 ? 5.0873 3.9251 2.6935 1.0115  -0.6967 0.1679  299  TYR C CZ  
8589  O  OH  . TYR C  301 ? 5.1809 4.1205 2.8427 0.9862  -0.7926 0.2185  299  TYR C OH  
8590  N  N   . PRO C  321 ? 4.3886 2.9952 1.8157 0.9950  -0.5028 -0.1301 319  PRO C N   
8591  C  CA  . PRO C  321 ? 4.4486 3.0862 1.8657 0.9702  -0.5674 -0.0787 319  PRO C CA  
8592  C  C   . PRO C  321 ? 4.5328 3.1228 1.8027 0.8933  -0.6569 -0.0506 319  PRO C C   
8593  O  O   . PRO C  321 ? 4.6649 3.1231 1.7342 0.8446  -0.6652 -0.0388 319  PRO C O   
8594  C  CB  . PRO C  321 ? 4.6053 3.1481 1.9344 0.9819  -0.5109 -0.0726 319  PRO C CB  
8595  N  N   . GLY C  322 ? 4.5934 3.2917 1.9601 0.8775  -0.7235 -0.0396 320  GLY C N   
8596  C  CA  . GLY C  322 ? 4.7031 3.3800 1.9499 0.7981  -0.8140 -0.0113 320  GLY C CA  
8597  C  C   . GLY C  322 ? 4.6398 3.4512 2.0316 0.7932  -0.8700 -0.0062 320  GLY C C   
8598  O  O   . GLY C  322 ? 4.4534 3.3866 2.0483 0.8530  -0.8485 -0.0138 320  GLY C O   
8599  N  N   . ALA C  323 ? 4.7543 3.5374 2.0303 0.7144  -0.9416 0.0063  321  ALA C N   
8600  C  CA  . ALA C  323 ? 4.7666 3.6590 2.1486 0.6938  -0.9983 0.0109  321  ALA C CA  
8601  C  C   . ALA C  323 ? 4.6498 3.7374 2.2517 0.7214  -1.0603 0.0706  321  ALA C C   
8602  O  O   . ALA C  323 ? 4.7347 3.9112 2.3780 0.6560  -1.1337 0.1198  321  ALA C O   
8603  C  CB  . ALA C  323 ? 4.6399 3.5232 2.0924 0.7398  -0.9277 -0.0493 321  ALA C CB  
8604  N  N   . SER C  324 ? 4.4839 3.6554 2.2685 0.8032  -1.0092 0.0674  322  SER C N   
8605  C  CA  . SER C  324 ? 4.3366 3.6737 2.3285 0.8377  -1.0473 0.1223  322  SER C CA  
8606  C  C   . SER C  324 ? 4.4038 3.7467 2.3859 0.8509  -1.0600 0.1798  322  SER C C   
8607  O  O   . SER C  324 ? 4.5401 3.7691 2.4011 0.8584  -1.0121 0.1627  322  SER C O   
8608  C  CB  . SER C  324 ? 3.9869 3.4003 2.1683 0.9114  -0.9815 0.0882  322  SER C CB  
8609  O  OG  . SER C  324 ? 3.9433 3.2935 2.1114 0.9589  -0.8996 0.0577  322  SER C OG  
8610  N  N   . ALA C  325 ? 4.1657 3.6442 2.2866 0.8545  -1.1176 0.2518  323  ALA C N   
8611  C  CA  . ALA C  325 ? 4.0913 3.5891 2.2265 0.8733  -1.1276 0.3174  323  ALA C CA  
8612  C  C   . ALA C  325 ? 4.0272 3.5013 2.2374 0.9546  -1.0376 0.2953  323  ALA C C   
8613  O  O   . ALA C  325 ? 4.0875 3.5143 2.2436 0.9694  -1.0218 0.3274  323  ALA C O   
8614  C  CB  . ALA C  325 ? 3.9624 3.6320 2.2816 0.8573  -1.1839 0.4026  323  ALA C CB  
8615  N  N   . ALA C  326 ? 4.0461 3.5534 2.3806 0.9983  -0.9751 0.2413  324  ALA C N   
8616  C  CA  . ALA C  326 ? 4.0795 3.5773 2.4998 1.0605  -0.8851 0.2140  324  ALA C CA  
8617  C  C   . ALA C  326 ? 3.9752 3.4406 2.4040 1.0743  -0.8215 0.1305  324  ALA C C   
8618  O  O   . ALA C  326 ? 3.8111 3.3537 2.3526 1.0828  -0.8255 0.1103  324  ALA C O   
8619  C  CB  . ALA C  326 ? 3.9825 3.6009 2.6055 1.1077  -0.8783 0.2607  324  ALA C CB  
8620  N  N   . PRO C  327 ? 3.9588 3.3144 2.2726 1.0775  -0.7622 0.0850  325  PRO C N   
8621  C  CA  . PRO C  327 ? 3.8342 3.1708 2.1638 1.0947  -0.7025 0.0154  325  PRO C CA  
8622  C  C   . PRO C  327 ? 3.6813 3.1197 2.2002 1.1406  -0.6576 -0.0025 325  PRO C C   
8623  O  O   . PRO C  327 ? 3.6162 3.0712 2.2020 1.1695  -0.6159 0.0090  325  PRO C O   
8624  C  CB  . PRO C  327 ? 3.9563 3.1662 2.1462 1.0968  -0.6410 -0.0120 325  PRO C CB  
8625  C  CG  . PRO C  327 ? 4.2020 3.3356 2.2444 1.0587  -0.6879 0.0346  325  PRO C CG  
8626  C  CD  . PRO C  327 ? 4.1971 3.4403 2.3579 1.0651  -0.7462 0.0995  325  PRO C CD  
8627  N  N   . CYS C  328 ? 3.5317 3.0294 2.1259 1.1426  -0.6637 -0.0318 326  CYS C N   
8628  C  CA  . CYS C  328 ? 3.2950 2.8890 2.0566 1.1744  -0.6306 -0.0498 326  CYS C CA  
8629  C  C   . CYS C  328 ? 3.2532 2.8393 2.0249 1.1925  -0.5687 -0.1086 326  CYS C C   
8630  O  O   . CYS C  328 ? 3.3531 2.8691 2.0180 1.1848  -0.5557 -0.1347 326  CYS C O   
8631  C  CB  . CYS C  328 ? 3.2957 2.9743 2.1479 1.1637  -0.6830 -0.0348 326  CYS C CB  
8632  S  SG  . CYS C  328 ? 3.6295 3.3680 2.5359 1.1516  -0.7530 0.0463  326  CYS C SG  
8633  N  N   . CYS C  329 ? 3.2412 2.9000 2.1429 1.2157  -0.5272 -0.1254 327  CYS C N   
8634  C  CA  . CYS C  329 ? 3.3243 3.0129 2.2706 1.2307  -0.4751 -0.1735 327  CYS C CA  
8635  C  C   . CYS C  329 ? 3.2392 2.9843 2.2356 1.2273  -0.5027 -0.1911 327  CYS C C   
8636  O  O   . CYS C  329 ? 3.1859 3.0075 2.2945 1.2305  -0.5030 -0.1945 327  CYS C O   
8637  C  CB  . CYS C  329 ? 3.2847 3.0218 2.3332 1.2437  -0.4224 -0.1825 327  CYS C CB  
8638  S  SG  . CYS C  329 ? 3.4195 3.2124 2.5281 1.2518  -0.3618 -0.2342 327  CYS C SG  
8639  N  N   . VAL C  330 ? 3.3441 3.0395 2.2478 1.2195  -0.5198 -0.2029 328  VAL C N   
8640  C  CA  . VAL C  330 ? 3.1831 2.9158 2.1157 1.2154  -0.5455 -0.2173 328  VAL C CA  
8641  C  C   . VAL C  330 ? 2.9174 2.6616 1.8558 1.2377  -0.5003 -0.2523 328  VAL C C   
8642  O  O   . VAL C  330 ? 3.0196 2.7160 1.9005 1.2515  -0.4571 -0.2618 328  VAL C O   
8643  C  CB  . VAL C  330 ? 3.3353 3.0036 2.1601 1.1856  -0.5997 -0.2012 328  VAL C CB  
8644  C  CG1 . VAL C  330 ? 3.4322 3.1238 2.2801 1.1633  -0.6536 -0.1568 328  VAL C CG1 
8645  C  CG2 . VAL C  330 ? 3.5219 3.0711 2.1880 1.1786  -0.5788 -0.2089 328  VAL C CG2 
8646  N  N   . PRO C  331 ? 2.8046 2.6154 1.8159 1.2435  -0.5066 -0.2677 329  PRO C N   
8647  C  CA  . PRO C  331 ? 2.7779 2.6111 1.7990 1.2674  -0.4690 -0.2911 329  PRO C CA  
8648  C  C   . PRO C  331 ? 2.9361 2.6734 1.8333 1.2740  -0.4625 -0.2931 329  PRO C C   
8649  O  O   . PRO C  331 ? 2.9937 2.6682 1.8129 1.2513  -0.5003 -0.2857 329  PRO C O   
8650  C  CB  . PRO C  331 ? 2.9052 2.8255 2.0228 1.2656  -0.4875 -0.3009 329  PRO C CB  
8651  C  CG  . PRO C  331 ? 2.9446 2.8534 2.0638 1.2408  -0.5381 -0.2834 329  PRO C CG  
8652  C  CD  . PRO C  331 ? 2.7738 2.6483 1.8700 1.2305  -0.5439 -0.2605 329  PRO C CD  
8653  N  N   . GLN C  332 ? 2.9704 2.6951 1.8494 1.3033  -0.4096 -0.3016 330  GLN C N   
8654  C  CA  . GLN C  332 ? 3.1653 2.7890 1.9286 1.3182  -0.3828 -0.3031 330  GLN C CA  
8655  C  C   . GLN C  332 ? 3.0263 2.6926 1.8287 1.3457  -0.3708 -0.3086 330  GLN C C   
8656  O  O   . GLN C  332 ? 3.2570 2.8408 1.9696 1.3436  -0.3749 -0.3095 330  GLN C O   
8657  C  CB  . GLN C  332 ? 3.2256 2.7953 1.9394 1.3403  -0.3208 -0.3015 330  GLN C CB  
8658  C  CG  . GLN C  332 ? 3.2676 2.7097 1.8496 1.3581  -0.2768 -0.3014 330  GLN C CG  
8659  C  CD  . GLN C  332 ? 3.4897 2.8669 2.0183 1.3783  -0.2095 -0.2981 330  GLN C CD  
8660  O  OE1 . GLN C  332 ? 3.5031 2.9451 2.1057 1.3811  -0.1953 -0.2966 330  GLN C OE1 
8661  N  NE2 . GLN C  332 ? 3.6562 2.8950 2.0500 1.3907  -0.1611 -0.2976 330  GLN C NE2 
8662  N  N   . ALA C  333 ? 2.8509 2.6415 1.7786 1.3677  -0.3558 -0.3108 331  ALA C N   
8663  C  CA  . ALA C  333 ? 2.7757 2.6239 1.7500 1.3954  -0.3480 -0.3092 331  ALA C CA  
8664  C  C   . ALA C  333 ? 2.7722 2.7366 1.8577 1.3765  -0.3884 -0.3168 331  ALA C C   
8665  O  O   . ALA C  333 ? 2.7972 2.8417 1.9660 1.3605  -0.3909 -0.3225 331  ALA C O   
8666  C  CB  . ALA C  333 ? 2.9736 2.8721 1.9913 1.4395  -0.2901 -0.2977 331  ALA C CB  
8667  N  N   . LEU C  334 ? 2.7021 2.6629 1.7792 1.3751  -0.4142 -0.3184 332  LEU C N   
8668  C  CA  . LEU C  334 ? 2.4460 2.5010 1.6139 1.3575  -0.4465 -0.3261 332  LEU C CA  
8669  C  C   . LEU C  334 ? 2.3961 2.4934 1.5831 1.3773  -0.4360 -0.3199 332  LEU C C   
8670  O  O   . LEU C  334 ? 2.4565 2.4855 1.5723 1.4103  -0.4145 -0.3093 332  LEU C O   
8671  C  CB  . LEU C  334 ? 2.4997 2.5130 1.6473 1.3216  -0.4916 -0.3307 332  LEU C CB  
8672  C  CG  . LEU C  334 ? 2.4754 2.4760 1.6336 1.2934  -0.5081 -0.3278 332  LEU C CG  
8673  C  CD1 . LEU C  334 ? 2.7838 2.6742 1.8277 1.2893  -0.5061 -0.3185 332  LEU C CD1 
8674  C  CD2 . LEU C  334 ? 2.3769 2.4003 1.5813 1.2643  -0.5481 -0.3265 332  LEU C CD2 
8675  N  N   . GLU C  335 ? 2.4657 2.6657 1.7406 1.3483  -0.4456 -0.3251 333  GLU C N   
8676  C  CA  . GLU C  335 ? 2.3595 2.6135 1.6585 1.3541  -0.4360 -0.3143 333  GLU C CA  
8677  C  C   . GLU C  335 ? 2.2963 2.5662 1.6158 1.3205  -0.4655 -0.3265 333  GLU C C   
8678  O  O   . GLU C  335 ? 2.2525 2.5491 1.6158 1.2883  -0.4854 -0.3427 333  GLU C O   
8679  C  CB  . GLU C  335 ? 2.3922 2.7699 1.7749 1.3597  -0.4168 -0.3035 333  GLU C CB  
8680  C  CG  . GLU C  335 ? 2.5623 2.9347 1.9375 1.3970  -0.3781 -0.2867 333  GLU C CG  
8681  C  CD  . GLU C  335 ? 2.6785 3.1925 2.1495 1.4024  -0.3629 -0.2718 333  GLU C CD  
8682  O  OE1 . GLU C  335 ? 2.7394 3.3540 2.2708 1.3794  -0.3858 -0.2731 333  GLU C OE1 
8683  O  OE2 . GLU C  335 ? 2.8775 3.4044 2.3617 1.4302  -0.3283 -0.2580 333  GLU C OE2 
8684  N  N   . PRO C  336 ? 2.2008 2.4464 1.4865 1.3317  -0.4635 -0.3176 334  PRO C N   
8685  C  CA  . PRO C  336 ? 2.1683 2.4210 1.4675 1.3038  -0.4874 -0.3291 334  PRO C CA  
8686  C  C   . PRO C  336 ? 2.1028 2.4684 1.4795 1.2841  -0.4923 -0.3319 334  PRO C C   
8687  O  O   . PRO C  336 ? 2.0872 2.5368 1.5067 1.2945  -0.4800 -0.3199 334  PRO C O   
8688  C  CB  . PRO C  336 ? 2.2365 2.4224 1.4653 1.3323  -0.4771 -0.3158 334  PRO C CB  
8689  C  CG  . PRO C  336 ? 2.2812 2.4781 1.4981 1.3735  -0.4408 -0.2903 334  PRO C CG  
8690  C  CD  . PRO C  336 ? 2.2780 2.4754 1.5051 1.3760  -0.4333 -0.2947 334  PRO C CD  
8691  N  N   . LEU C  337 ? 2.2322 2.5999 1.6233 1.2574  -0.5125 -0.3471 335  LEU C N   
8692  C  CA  . LEU C  337 ? 2.2246 2.6840 1.6707 1.2386  -0.5232 -0.3556 335  LEU C CA  
8693  C  C   . LEU C  337 ? 2.2074 2.6539 1.6313 1.2348  -0.5334 -0.3552 335  LEU C C   
8694  O  O   . LEU C  337 ? 2.0435 2.4206 1.4444 1.2244  -0.5429 -0.3666 335  LEU C O   
8695  C  CB  . LEU C  337 ? 2.1369 2.6117 1.6268 1.2141  -0.5336 -0.3793 335  LEU C CB  
8696  C  CG  . LEU C  337 ? 2.0267 2.5790 1.5565 1.1976  -0.5481 -0.3964 335  LEU C CG  
8697  C  CD1 . LEU C  337 ? 2.4248 3.0872 1.9821 1.1967  -0.5481 -0.3890 335  LEU C CD1 
8698  C  CD2 . LEU C  337 ? 1.9548 2.4812 1.5167 1.1633  -0.5366 -0.4180 335  LEU C CD2 
8699  N  N   . PRO C  338 ? 2.3530 2.8673 1.7841 1.2438  -0.5333 -0.3386 336  PRO C N   
8700  C  CA  . PRO C  338 ? 2.3316 2.8373 1.7390 1.2402  -0.5448 -0.3383 336  PRO C CA  
8701  C  C   . PRO C  338 ? 2.1193 2.6724 1.5550 1.2099  -0.5678 -0.3638 336  PRO C C   
8702  O  O   . PRO C  338 ? 1.9950 2.6352 1.4689 1.1946  -0.5779 -0.3717 336  PRO C O   
8703  C  CB  . PRO C  338 ? 2.2141 2.7854 1.6223 1.2637  -0.5364 -0.3026 336  PRO C CB  
8704  C  CG  . PRO C  338 ? 2.0631 2.7267 1.5254 1.2630  -0.5322 -0.2926 336  PRO C CG  
8705  C  CD  . PRO C  338 ? 2.1111 2.7119 1.5712 1.2620  -0.5217 -0.3120 336  PRO C CD  
8706  N  N   . ILE C  339 ? 2.0301 2.5253 1.4408 1.2034  -0.5767 -0.3777 337  ILE C N   
8707  C  CA  . ILE C  339 ? 2.0138 2.5264 1.4395 1.1685  -0.5851 -0.4032 337  ILE C CA  
8708  C  C   . ILE C  339 ? 2.2159 2.7168 1.5981 1.1643  -0.5919 -0.3993 337  ILE C C   
8709  O  O   . ILE C  339 ? 2.2551 2.7211 1.5973 1.2035  -0.5979 -0.3793 337  ILE C O   
8710  C  CB  . ILE C  339 ? 1.9951 2.4360 1.4461 1.1470  -0.5713 -0.4234 337  ILE C CB  
8711  C  CG1 . ILE C  339 ? 2.0162 2.3757 1.4375 1.1676  -0.5778 -0.4168 337  ILE C CG1 
8712  C  CG2 . ILE C  339 ? 1.9823 2.4310 1.4692 1.1520  -0.5651 -0.4233 337  ILE C CG2 
8713  C  CD1 . ILE C  339 ? 1.9998 2.3086 1.4588 1.1464  -0.5698 -0.4267 337  ILE C CD1 
8714  N  N   . VAL C  340 ? 2.1704 2.6903 1.5510 1.1137  -0.5855 -0.4192 338  VAL C N   
8715  C  CA  . VAL C  340 ? 2.0994 2.6009 1.4310 1.0994  -0.5885 -0.4194 338  VAL C CA  
8716  C  C   . VAL C  340 ? 2.1448 2.5840 1.4805 1.0492  -0.5610 -0.4525 338  VAL C C   
8717  O  O   . VAL C  340 ? 2.1886 2.6466 1.5423 1.0034  -0.5431 -0.4742 338  VAL C O   
8718  C  CB  . VAL C  340 ? 2.1287 2.7275 1.4359 1.0845  -0.6089 -0.4026 338  VAL C CB  
8719  C  CG1 . VAL C  340 ? 2.1838 2.7512 1.4298 1.0618  -0.6101 -0.4052 338  VAL C CG1 
8720  C  CG2 . VAL C  340 ? 2.2044 2.8670 1.5190 1.1454  -0.6291 -0.3595 338  VAL C CG2 
8721  N  N   . TYR C  341 ? 2.2857 2.6455 1.6052 1.0574  -0.5514 -0.4556 339  TYR C N   
8722  C  CA  . TYR C  341 ? 2.4842 2.7822 1.8135 1.0167  -0.5183 -0.4807 339  TYR C CA  
8723  C  C   . TYR C  341 ? 2.7360 2.9776 2.0139 1.0186  -0.5148 -0.4786 339  TYR C C   
8724  O  O   . TYR C  341 ? 2.8505 3.0853 2.0920 1.0570  -0.5362 -0.4575 339  TYR C O   
8725  C  CB  . TYR C  341 ? 2.3473 2.6056 1.7457 1.0230  -0.5013 -0.4846 339  TYR C CB  
8726  C  CG  . TYR C  341 ? 2.2125 2.4300 1.6147 1.0594  -0.5184 -0.4677 339  TYR C CG  
8727  C  CD1 . TYR C  341 ? 2.1400 2.3743 1.5339 1.0978  -0.5453 -0.4496 339  TYR C CD1 
8728  C  CD2 . TYR C  341 ? 2.3100 2.4669 1.7187 1.0500  -0.5035 -0.4708 339  TYR C CD2 
8729  C  CE1 . TYR C  341 ? 2.1212 2.3045 1.5000 1.1200  -0.5575 -0.4379 339  TYR C CE1 
8730  C  CE2 . TYR C  341 ? 2.3381 2.4579 1.7432 1.0714  -0.5200 -0.4574 339  TYR C CE2 
8731  C  CZ  . TYR C  341 ? 2.1902 2.3191 1.5738 1.1035  -0.5474 -0.4425 339  TYR C CZ  
8732  O  OH  . TYR C  341 ? 2.2816 2.3601 1.6437 1.1144  -0.5606 -0.4327 339  TYR C OH  
8733  N  N   . TYR C  342 ? 2.8555 3.0462 2.1271 0.9774  -0.4801 -0.5004 340  TYR C N   
8734  C  CA  . TYR C  342 ? 2.8597 2.9882 2.0816 0.9720  -0.4683 -0.5021 340  TYR C CA  
8735  C  C   . TYR C  342 ? 2.8091 2.8717 2.0847 0.9777  -0.4442 -0.5050 340  TYR C C   
8736  O  O   . TYR C  342 ? 2.5795 2.6430 1.9322 0.9737  -0.4279 -0.5081 340  TYR C O   
8737  C  CB  . TYR C  342 ? 2.8923 3.0019 2.0575 0.9172  -0.4414 -0.5235 340  TYR C CB  
8738  C  CG  . TYR C  342 ? 2.8868 3.0614 1.9776 0.9069  -0.4750 -0.5121 340  TYR C CG  
8739  C  CD1 . TYR C  342 ? 2.8084 3.0734 1.9147 0.8992  -0.4990 -0.5069 340  TYR C CD1 
8740  C  CD2 . TYR C  342 ? 2.9779 3.1292 1.9857 0.9026  -0.4828 -0.5027 340  TYR C CD2 
8741  C  CE1 . TYR C  342 ? 2.8590 3.2037 1.9101 0.8868  -0.5342 -0.4891 340  TYR C CE1 
8742  C  CE2 . TYR C  342 ? 3.0876 3.3130 2.0329 0.8931  -0.5188 -0.4831 340  TYR C CE2 
8743  C  CZ  . TYR C  342 ? 2.9606 3.2895 1.9328 0.8845  -0.5463 -0.4746 340  TYR C CZ  
8744  O  OH  . TYR C  342 ? 2.8357 3.2584 1.7588 0.8727  -0.5868 -0.4478 340  TYR C OH  
8745  N  N   . VAL C  343 ? 3.1703 3.1796 2.4061 0.9861  -0.4420 -0.5002 341  VAL C N   
8746  C  CA  . VAL C  343 ? 3.2518 3.2049 2.5348 0.9841  -0.4206 -0.5006 341  VAL C CA  
8747  C  C   . VAL C  343 ? 3.3795 3.2685 2.6130 0.9564  -0.3850 -0.5138 341  VAL C C   
8748  O  O   . VAL C  343 ? 3.3710 3.2270 2.5312 0.9684  -0.3954 -0.5071 341  VAL C O   
8749  C  CB  . VAL C  343 ? 3.0921 3.0321 2.3683 1.0186  -0.4517 -0.4822 341  VAL C CB  
8750  C  CG1 . VAL C  343 ? 3.2751 3.1706 2.6042 1.0048  -0.4340 -0.4812 341  VAL C CG1 
8751  C  CG2 . VAL C  343 ? 2.6467 2.6392 1.9529 1.0444  -0.4835 -0.4700 341  VAL C CG2 
8752  N  N   . GLY C  344 ? 3.4909 3.3525 2.7590 0.9207  -0.3363 -0.5312 342  GLY C N   
8753  C  CA  . GLY C  344 ? 3.5872 3.3792 2.7967 0.8892  -0.2945 -0.5467 342  GLY C CA  
8754  C  C   . GLY C  344 ? 3.5709 3.3707 2.6636 0.8740  -0.3126 -0.5523 342  GLY C C   
8755  O  O   . GLY C  344 ? 3.5087 3.3244 2.5729 0.8391  -0.3001 -0.5678 342  GLY C O   
8756  N  N   . ARG C  345 ? 3.5428 3.3310 2.5641 0.8975  -0.3412 -0.5370 343  ARG C N   
8757  C  CA  . ARG C  345 ? 3.5490 3.3629 2.4660 0.8928  -0.3691 -0.5284 343  ARG C CA  
8758  C  C   . ARG C  345 ? 3.5502 3.4334 2.4590 0.9455  -0.4243 -0.4964 343  ARG C C   
8759  O  O   . ARG C  345 ? 3.5591 3.4851 2.3973 0.9511  -0.4531 -0.4773 343  ARG C O   
8760  C  CB  . ARG C  345 ? 3.6542 3.3871 2.4783 0.8775  -0.3462 -0.5305 343  ARG C CB  
8761  C  CG  . ARG C  345 ? 3.6898 3.3343 2.5247 0.8331  -0.2796 -0.5593 343  ARG C CG  
8762  C  CD  . ARG C  345 ? 3.7308 3.2911 2.4599 0.8165  -0.2565 -0.5614 343  ARG C CD  
8763  N  NE  . ARG C  345 ? 3.7750 3.2434 2.5292 0.7838  -0.1854 -0.5850 343  ARG C NE  
8764  C  CZ  . ARG C  345 ? 3.7483 3.1699 2.5587 0.8006  -0.1604 -0.5815 343  ARG C CZ  
8765  N  NH1 . ARG C  345 ? 3.6390 3.0844 2.4708 0.8441  -0.2003 -0.5600 343  ARG C NH1 
8766  N  NH2 . ARG C  345 ? 3.7761 3.1246 2.6197 0.7709  -0.0913 -0.5987 343  ARG C NH2 
8767  N  N   . LYS C  346 ? 3.3863 3.2813 2.3632 0.9833  -0.4377 -0.4866 344  LYS C N   
8768  C  CA  . LYS C  346 ? 3.3943 3.3299 2.3578 1.0368  -0.4763 -0.4566 344  LYS C CA  
8769  C  C   . LYS C  346 ? 3.1901 3.2118 2.2142 1.0476  -0.5000 -0.4521 344  LYS C C   
8770  O  O   . LYS C  346 ? 3.1122 3.1324 2.2105 1.0437  -0.4926 -0.4636 344  LYS C O   
8771  C  CB  . LYS C  346 ? 3.3592 3.2271 2.3294 1.0656  -0.4705 -0.4503 344  LYS C CB  
8772  C  CG  . LYS C  346 ? 3.4221 3.1980 2.3449 1.0487  -0.4399 -0.4588 344  LYS C CG  
8773  C  CD  . LYS C  346 ? 3.3224 3.0322 2.2414 1.0690  -0.4357 -0.4530 344  LYS C CD  
8774  C  CE  . LYS C  346 ? 3.3763 2.9962 2.2558 1.0459  -0.4009 -0.4636 344  LYS C CE  
8775  N  NZ  . LYS C  346 ? 3.5272 3.1113 2.2974 1.0619  -0.3963 -0.4490 344  LYS C NZ  
8776  N  N   . PRO C  347 ? 3.1344 3.2369 2.1334 1.0605  -0.5285 -0.4319 345  PRO C N   
8777  C  CA  . PRO C  347 ? 2.9062 3.0912 1.9632 1.0731  -0.5485 -0.4256 345  PRO C CA  
8778  C  C   . PRO C  347 ? 2.8105 2.9900 1.8816 1.1327  -0.5617 -0.4015 345  PRO C C   
8779  O  O   . PRO C  347 ? 2.8175 2.9788 1.8368 1.1747  -0.5679 -0.3734 345  PRO C O   
8780  C  CB  . PRO C  347 ? 2.9163 3.1949 1.9386 1.0599  -0.5736 -0.4083 345  PRO C CB  
8781  C  CG  . PRO C  347 ? 3.0213 3.2717 1.9634 1.0757  -0.5793 -0.3853 345  PRO C CG  
8782  C  CD  . PRO C  347 ? 3.2328 3.3633 2.1523 1.0600  -0.5443 -0.4105 345  PRO C CD  
8783  N  N   . LYS C  348 ? 2.6911 2.8767 1.8246 1.1359  -0.5611 -0.4111 346  LYS C N   
8784  C  CA  . LYS C  348 ? 2.7151 2.8809 1.8517 1.1824  -0.5688 -0.3937 346  LYS C CA  
8785  C  C   . LYS C  348 ? 2.5749 2.8222 1.7548 1.1969  -0.5824 -0.3842 346  LYS C C   
8786  O  O   . LYS C  348 ? 2.5883 2.8655 1.8233 1.1662  -0.5797 -0.4035 346  LYS C O   
8787  C  CB  . LYS C  348 ? 2.6837 2.7743 1.8451 1.1693  -0.5581 -0.4105 346  LYS C CB  
8788  C  CG  . LYS C  348 ? 2.7517 2.7622 1.8762 1.1540  -0.5417 -0.4185 346  LYS C CG  
8789  C  CD  . LYS C  348 ? 2.7165 2.6708 1.8727 1.1381  -0.5375 -0.4281 346  LYS C CD  
8790  C  CE  . LYS C  348 ? 2.8325 2.7122 1.9566 1.1194  -0.5187 -0.4354 346  LYS C CE  
8791  N  NZ  . LYS C  348 ? 3.1291 2.9541 2.1564 1.1518  -0.5147 -0.4204 346  LYS C NZ  
8792  N  N   . VAL C  349 ? 2.3544 2.6340 1.5115 1.2458  -0.5910 -0.3519 347  VAL C N   
8793  C  CA  . VAL C  349 ? 2.2118 2.5589 1.4141 1.2549  -0.5904 -0.3397 347  VAL C CA  
8794  C  C   . VAL C  349 ? 2.2157 2.4872 1.4140 1.2694  -0.5725 -0.3409 347  VAL C C   
8795  O  O   . VAL C  349 ? 2.2720 2.4825 1.4194 1.3009  -0.5554 -0.3216 347  VAL C O   
8796  C  CB  . VAL C  349 ? 2.2412 2.6608 1.4411 1.2725  -0.5841 -0.3001 347  VAL C CB  
8797  C  CG1 . VAL C  349 ? 2.2062 2.6963 1.4633 1.2706  -0.5755 -0.2889 347  VAL C CG1 
8798  C  CG2 . VAL C  349 ? 2.2544 2.7463 1.4416 1.2493  -0.6086 -0.2964 347  VAL C CG2 
8799  N  N   . GLU C  350 ? 2.1681 2.4402 1.4105 1.2476  -0.5766 -0.3616 348  GLU C N   
8800  C  CA  . GLU C  350 ? 2.2180 2.4212 1.4479 1.2527  -0.5683 -0.3634 348  GLU C CA  
8801  C  C   . GLU C  350 ? 2.2786 2.5268 1.5474 1.2475  -0.5602 -0.3599 348  GLU C C   
8802  O  O   . GLU C  350 ? 2.2505 2.5819 1.5696 1.2329  -0.5643 -0.3639 348  GLU C O   
8803  C  CB  . GLU C  350 ? 2.1633 2.3163 1.4080 1.2324  -0.5835 -0.3844 348  GLU C CB  
8804  C  CG  . GLU C  350 ? 2.2281 2.3284 1.4373 1.2276  -0.5836 -0.3897 348  GLU C CG  
8805  C  CD  . GLU C  350 ? 2.4421 2.4876 1.6707 1.1941  -0.5863 -0.4027 348  GLU C CD  
8806  O  OE1 . GLU C  350 ? 2.6827 2.6768 1.8841 1.1808  -0.5795 -0.4074 348  GLU C OE1 
8807  O  OE2 . GLU C  350 ? 2.3435 2.4016 1.6167 1.1808  -0.5954 -0.4045 348  GLU C OE2 
8808  N  N   . GLN C  351 ? 2.2351 2.4225 1.4706 1.2616  -0.5509 -0.3537 349  GLN C N   
8809  C  CA  . GLN C  351 ? 2.1655 2.3793 1.4228 1.2641  -0.5408 -0.3484 349  GLN C CA  
8810  C  C   . GLN C  351 ? 2.2642 2.4161 1.5106 1.2516  -0.5520 -0.3601 349  GLN C C   
8811  O  O   . GLN C  351 ? 2.2703 2.3358 1.4504 1.2658  -0.5570 -0.3583 349  GLN C O   
8812  C  CB  . GLN C  351 ? 2.2208 2.4251 1.4382 1.3045  -0.5150 -0.3213 349  GLN C CB  
8813  C  CG  . GLN C  351 ? 2.2110 2.4452 1.4517 1.3118  -0.5016 -0.3143 349  GLN C CG  
8814  C  CD  . GLN C  351 ? 2.4022 2.6221 1.6072 1.3582  -0.4690 -0.2829 349  GLN C CD  
8815  O  OE1 . GLN C  351 ? 2.5406 2.6981 1.6853 1.3884  -0.4539 -0.2678 349  GLN C OE1 
8816  N  NE2 . GLN C  351 ? 2.4281 2.7030 1.6711 1.3680  -0.4535 -0.2705 349  GLN C NE2 
8817  N  N   . LEU C  352 ? 2.4875 2.6828 1.7926 1.2282  -0.5578 -0.3693 350  LEU C N   
8818  C  CA  . LEU C  352 ? 2.2071 2.3594 1.5114 1.2160  -0.5709 -0.3725 350  LEU C CA  
8819  C  C   . LEU C  352 ? 2.3098 2.4310 1.5687 1.2396  -0.5598 -0.3623 350  LEU C C   
8820  O  O   . LEU C  352 ? 2.5005 2.6662 1.7706 1.2568  -0.5382 -0.3546 350  LEU C O   
8821  C  CB  . LEU C  352 ? 2.0971 2.3022 1.4808 1.1901  -0.5752 -0.3811 350  LEU C CB  
8822  C  CG  . LEU C  352 ? 2.3457 2.5760 1.7761 1.1739  -0.5815 -0.3921 350  LEU C CG  
8823  C  CD1 . LEU C  352 ? 2.5342 2.8041 2.0371 1.1614  -0.5769 -0.3985 350  LEU C CD1 
8824  C  CD2 . LEU C  352 ? 2.5064 2.6804 1.9168 1.1680  -0.5993 -0.3894 350  LEU C CD2 
8825  N  N   . SER C  353 ? 2.4723 2.5184 1.6770 1.2422  -0.5773 -0.3603 351  SER C N   
8826  C  CA  . SER C  353 ? 2.6668 2.6597 1.8047 1.2709  -0.5690 -0.3520 351  SER C CA  
8827  C  C   . SER C  353 ? 2.6871 2.7046 1.8622 1.2558  -0.5761 -0.3512 351  SER C C   
8828  O  O   . SER C  353 ? 2.8774 2.9019 2.0882 1.2256  -0.6015 -0.3510 351  SER C O   
8829  C  CB  . SER C  353 ? 2.9561 2.8342 1.9824 1.2795  -0.5855 -0.3501 351  SER C CB  
8830  O  OG  . SER C  353 ? 3.0475 2.9146 2.0869 1.2328  -0.6220 -0.3533 351  SER C OG  
8831  N  N   . ASN C  354 ? 2.5560 2.5883 1.7267 1.2798  -0.5505 -0.3462 352  ASN C N   
8832  C  CA  . ASN C  354 ? 2.7090 2.7546 1.9016 1.2754  -0.5514 -0.3442 352  ASN C CA  
8833  C  C   . ASN C  354 ? 2.4885 2.6101 1.7809 1.2415  -0.5562 -0.3504 352  ASN C C   
8834  O  O   . ASN C  354 ? 2.5483 2.6578 1.8616 1.2181  -0.5798 -0.3468 352  ASN C O   
8835  C  CB  . ASN C  354 ? 2.9223 2.8750 2.0304 1.2710  -0.5777 -0.3370 352  ASN C CB  
8836  C  CG  . ASN C  354 ? 2.8316 2.6812 1.8192 1.2901  -0.5533 -0.3343 352  ASN C CG  
8837  O  OD1 . ASN C  354 ? 2.7946 2.6168 1.7471 1.3102  -0.5228 -0.3301 352  ASN C OD1 
8838  N  ND2 . ASN C  354 ? 2.7837 2.5660 1.7027 1.2825  -0.5597 -0.3370 352  ASN C ND2 
8839  N  N   . MET C  355 ? 2.1655 2.3652 1.5180 1.2423  -0.5338 -0.3566 353  MET C N   
8840  C  CA  . MET C  355 ? 2.2378 2.4972 1.6698 1.2203  -0.5334 -0.3659 353  MET C CA  
8841  C  C   . MET C  355 ? 2.2273 2.5340 1.6903 1.2330  -0.5127 -0.3691 353  MET C C   
8842  O  O   . MET C  355 ? 2.2701 2.5780 1.7653 1.2284  -0.5098 -0.3711 353  MET C O   
8843  C  CB  . MET C  355 ? 2.1629 2.4752 1.6337 1.2070  -0.5343 -0.3773 353  MET C CB  
8844  C  CG  . MET C  355 ? 2.0640 2.3352 1.5166 1.1943  -0.5515 -0.3769 353  MET C CG  
8845  S  SD  . MET C  355 ? 2.1161 2.3534 1.6034 1.1732  -0.5696 -0.3703 353  MET C SD  
8846  C  CE  . MET C  355 ? 1.9994 2.2985 1.5727 1.1687  -0.5504 -0.3831 353  MET C CE  
8847  N  N   . ILE C  356 ? 2.1029 2.4519 1.5615 1.2523  -0.4957 -0.3664 354  ILE C N   
8848  C  CA  . ILE C  356 ? 2.1111 2.5211 1.6079 1.2656  -0.4755 -0.3693 354  ILE C CA  
8849  C  C   . ILE C  356 ? 2.1967 2.5397 1.6445 1.2865  -0.4612 -0.3591 354  ILE C C   
8850  O  O   . ILE C  356 ? 2.3557 2.6483 1.7430 1.3126  -0.4536 -0.3462 354  ILE C O   
8851  C  CB  . ILE C  356 ? 2.2526 2.7546 1.7789 1.2772  -0.4651 -0.3627 354  ILE C CB  
8852  C  CG1 . ILE C  356 ? 2.2331 2.8085 1.8022 1.2502  -0.4817 -0.3749 354  ILE C CG1 
8853  C  CG2 . ILE C  356 ? 2.2520 2.8117 1.8135 1.2804  -0.4374 -0.3606 354  ILE C CG2 
8854  C  CD1 . ILE C  356 ? 2.3030 2.8472 1.8380 1.2486  -0.4957 -0.3672 354  ILE C CD1 
8855  N  N   . VAL C  357 ? 2.2120 2.5420 1.6763 1.2672  -0.4490 -0.3637 355  VAL C N   
8856  C  CA  . VAL C  357 ? 2.2614 2.5236 1.6728 1.2803  -0.4337 -0.3537 355  VAL C CA  
8857  C  C   . VAL C  357 ? 2.3873 2.6992 1.8191 1.2943  -0.3954 -0.3534 355  VAL C C   
8858  O  O   . VAL C  357 ? 2.4341 2.8186 1.9296 1.2717  -0.3771 -0.3643 355  VAL C O   
8859  C  CB  . VAL C  357 ? 2.2815 2.5064 1.7011 1.2577  -0.4362 -0.3519 355  VAL C CB  
8860  C  CG1 . VAL C  357 ? 2.3682 2.5295 1.7304 1.2684  -0.4168 -0.3414 355  VAL C CG1 
8861  C  CG2 . VAL C  357 ? 2.2795 2.4620 1.6845 1.2484  -0.4753 -0.3420 355  VAL C CG2 
8862  N  N   . ARG C  358 ? 2.4867 2.7567 1.8630 1.3288  -0.3784 -0.3401 356  ARG C N   
8863  C  CA  . ARG C  358 ? 2.5902 2.9090 1.9926 1.3491  -0.3363 -0.3325 356  ARG C CA  
8864  C  C   . ARG C  358 ? 2.6190 2.8654 1.9762 1.3474  -0.3072 -0.3319 356  ARG C C   
8865  O  O   . ARG C  358 ? 2.6353 2.9281 2.0420 1.3272  -0.2856 -0.3397 356  ARG C O   
8866  C  CB  . ARG C  358 ? 2.9168 3.2294 2.2916 1.3948  -0.3208 -0.3131 356  ARG C CB  
8867  C  CG  . ARG C  358 ? 3.0578 3.4432 2.4823 1.4228  -0.2750 -0.2960 356  ARG C CG  
8868  C  CD  . ARG C  358 ? 2.8470 3.3947 2.3875 1.3984  -0.2836 -0.2977 356  ARG C CD  
8869  N  NE  . ARG C  358 ? 2.7811 3.3992 2.3539 1.4048  -0.3143 -0.2888 356  ARG C NE  
8870  C  CZ  . ARG C  358 ? 2.7749 3.5348 2.4333 1.3815  -0.3292 -0.2858 356  ARG C CZ  
8871  N  NH1 . ARG C  358 ? 2.8074 3.6550 2.5295 1.3462  -0.3150 -0.2937 356  ARG C NH1 
8872  N  NH2 . ARG C  358 ? 2.7060 3.5171 2.3789 1.3880  -0.3580 -0.2750 356  ARG C NH2 
8873  N  N   . SER C  359 ? 2.6276 2.7530 1.8808 1.3638  -0.3043 -0.3233 357  SER C N   
8874  C  CA  . SER C  359 ? 2.7637 2.8028 1.9505 1.3624  -0.2773 -0.3201 357  SER C CA  
8875  C  C   . SER C  359 ? 2.8154 2.7760 1.9453 1.3341  -0.3158 -0.3193 357  SER C C   
8876  O  O   . SER C  359 ? 2.7439 2.7059 1.8777 1.3200  -0.3606 -0.3194 357  SER C O   
8877  C  CB  . SER C  359 ? 2.8879 2.8342 1.9805 1.3966  -0.2391 -0.3084 357  SER C CB  
8878  O  OG  . SER C  359 ? 2.9388 2.9654 2.0957 1.4315  -0.2006 -0.2984 357  SER C OG  
8879  N  N   . CYS C  360 ? 2.9602 2.8551 2.0389 1.3268  -0.2969 -0.3142 358  CYS C N   
8880  C  CA  . CYS C  360 ? 3.1185 2.9411 2.1385 1.3034  -0.3326 -0.3026 358  CYS C CA  
8881  C  C   . CYS C  360 ? 3.0776 2.7791 1.9700 1.3058  -0.3109 -0.2928 358  CYS C C   
8882  O  O   . CYS C  360 ? 2.9950 2.6837 1.8786 1.3212  -0.2570 -0.2968 358  CYS C O   
8883  C  CB  . CYS C  360 ? 3.2038 3.0794 2.3059 1.2851  -0.3336 -0.3015 358  CYS C CB  
8884  S  SG  . CYS C  360 ? 3.5076 3.5061 2.7434 1.2729  -0.3486 -0.3167 358  CYS C SG  
8885  N  N   . LYS C  361 ? 3.1004 2.7143 1.8914 1.2861  -0.3526 -0.2791 359  LYS C N   
8886  C  CA  . LYS C  361 ? 3.1918 2.6750 1.8350 1.2761  -0.3417 -0.2690 359  LYS C CA  
8887  C  C   . LYS C  361 ? 3.3137 2.7710 1.9253 1.2460  -0.3908 -0.2435 359  LYS C C   
8888  O  O   . LYS C  361 ? 3.3212 2.8589 2.0303 1.2385  -0.4281 -0.2319 359  LYS C O   
8889  C  CB  . LYS C  361 ? 3.3006 2.6857 1.8191 1.2724  -0.3442 -0.2739 359  LYS C CB  
8890  C  CG  . LYS C  361 ? 3.3011 2.6942 1.8088 1.2448  -0.4118 -0.2685 359  LYS C CG  
8891  C  CD  . LYS C  361 ? 3.3843 2.6584 1.7467 1.2327  -0.4070 -0.2763 359  LYS C CD  
8892  C  CE  . LYS C  361 ? 3.3213 2.6114 1.6804 1.1996  -0.4733 -0.2724 359  LYS C CE  
8893  N  NZ  . LYS C  361 ? 3.4614 2.6254 1.6692 1.1795  -0.4657 -0.2831 359  LYS C NZ  
8894  N  N   . CYS C  362 ? 3.5934 2.9356 2.0658 1.2298  -0.3872 -0.2306 360  CYS C N   
8895  C  CA  . CYS C  362 ? 3.6755 2.9872 2.0979 1.2003  -0.4386 -0.1969 360  CYS C CA  
8896  C  C   . CYS C  362 ? 3.9170 3.1152 2.1680 1.1619  -0.4770 -0.1876 360  CYS C C   
8897  O  O   . CYS C  362 ? 4.2061 3.2838 2.3166 1.1565  -0.4370 -0.1993 360  CYS C O   
8898  C  CB  . CYS C  362 ? 3.7397 3.0187 2.1460 1.2082  -0.4003 -0.1849 360  CYS C CB  
8899  S  SG  . CYS C  362 ? 3.7236 3.1203 2.3113 1.2389  -0.3500 -0.1988 360  CYS C SG  
8900  N  N   . SER C  363 ? 3.9088 3.1415 2.1676 1.1312  -0.5506 -0.1665 361  SER C N   
8901  C  CA  . SER C  363 ? 4.0865 3.2182 2.1785 1.0804  -0.5951 -0.1573 361  SER C CA  
8902  C  C   . SER C  363 ? 4.3102 3.5003 2.4254 1.0428  -0.6828 -0.1108 361  SER C C   
8903  O  O   . SER C  363 ? 4.3314 3.6364 2.5998 1.0646  -0.7013 -0.0861 361  SER C O   
8904  C  CB  . SER C  363 ? 4.0383 3.1389 2.0934 1.0753  -0.5859 -0.1890 361  SER C CB  
8905  O  OG  . SER C  363 ? 3.9474 3.1744 2.1595 1.0905  -0.6127 -0.1913 361  SER C OG  
8906  O  OXT . SER C  363 ? 4.4205 3.5445 2.4013 0.9883  -0.7344 -0.0942 361  SER C OXT 
8907  N  N   . ILE D  9   ? 3.0244 2.4793 2.6573 1.4243  0.1606  0.1451  7    ILE D N   
8908  C  CA  . ILE D  9   ? 3.0646 2.4816 2.7116 1.3868  0.2502  0.0735  7    ILE D CA  
8909  C  C   . ILE D  9   ? 3.0308 2.5321 2.6876 1.3440  0.1969  0.0062  7    ILE D C   
8910  O  O   . ILE D  9   ? 3.0450 2.5447 2.6648 1.2958  0.2248  -0.0672 7    ILE D O   
8911  C  CB  . ILE D  9   ? 3.0434 2.4089 2.7679 1.4137  0.3379  0.1080  7    ILE D CB  
8912  C  CG1 . ILE D  9   ? 3.1621 2.4290 2.8692 1.4566  0.4090  0.1709  7    ILE D CG1 
8913  C  CG2 . ILE D  9   ? 3.1192 2.4440 2.8375 1.3600  0.4210  0.0262  7    ILE D CG2 
8914  C  CD1 . ILE D  9   ? 3.1930 2.4952 2.9333 1.5204  0.3454  0.2788  7    ILE D CD1 
8915  N  N   . ASP D  10  ? 3.0468 2.6252 2.7568 1.3626  0.1203  0.0382  8    ASP D N   
8916  C  CA  . ASP D  10  ? 2.9945 2.6558 2.7145 1.3344  0.0540  -0.0065 8    ASP D CA  
8917  C  C   . ASP D  10  ? 2.9309 2.6068 2.7069 1.3083  0.0976  -0.0511 8    ASP D C   
8918  O  O   . ASP D  10  ? 2.8796 2.6142 2.7101 1.3147  0.0530  -0.0399 8    ASP D O   
8919  C  CB  . ASP D  10  ? 2.9178 2.5928 2.5556 1.3003  0.0251  -0.0637 8    ASP D CB  
8920  C  CG  . ASP D  10  ? 3.1206 2.7843 2.6889 1.3196  -0.0324 -0.0259 8    ASP D CG  
8921  O  OD1 . ASP D  10  ? 3.2710 2.9466 2.8573 1.3518  -0.0804 0.0427  8    ASP D OD1 
8922  O  OD2 . ASP D  10  ? 3.1896 2.8339 2.6844 1.3002  -0.0289 -0.0623 8    ASP D OD2 
8923  N  N   . MET D  11  ? 2.7634 2.3904 2.5143 1.2696  0.1774  -0.1081 9    MET D N   
8924  C  CA  . MET D  11  ? 2.7394 2.3580 2.5267 1.2376  0.2324  -0.1490 9    MET D CA  
8925  C  C   . MET D  11  ? 2.7244 2.4236 2.5006 1.1939  0.1794  -0.2101 9    MET D C   
8926  O  O   . MET D  11  ? 2.6037 2.3638 2.3525 1.1972  0.1017  -0.2142 9    MET D O   
8927  C  CB  . MET D  11  ? 2.8007 2.4055 2.6711 1.2842  0.2508  -0.0849 9    MET D CB  
8928  C  CG  . MET D  11  ? 2.8659 2.4988 2.7850 1.2702  0.2544  -0.1035 9    MET D CG  
8929  S  SD  . MET D  11  ? 2.8016 2.3567 2.6859 1.2050  0.3648  -0.1809 9    MET D SD  
8930  C  CE  . MET D  11  ? 3.0978 2.5351 3.0160 1.2521  0.4748  -0.1187 9    MET D CE  
8931  N  N   . GLU D  12  ? 2.8304 2.5246 2.6178 1.1513  0.2234  -0.2572 10   GLU D N   
8932  C  CA  . GLU D  12  ? 2.7588 2.5319 2.5351 1.1102  0.1742  -0.3096 10   GLU D CA  
8933  C  C   . GLU D  12  ? 2.6212 2.4384 2.4500 1.1284  0.1293  -0.2924 10   GLU D C   
8934  O  O   . GLU D  12  ? 2.4993 2.3762 2.3191 1.0988  0.0901  -0.3304 10   GLU D O   
8935  C  CB  . GLU D  12  ? 2.9556 2.7056 2.6958 1.0386  0.2405  -0.3759 10   GLU D CB  
8936  C  CG  . GLU D  12  ? 2.9180 2.7601 2.6328 0.9891  0.1911  -0.4290 10   GLU D CG  
8937  C  CD  . GLU D  12  ? 3.1630 2.9821 2.8444 0.9114  0.2550  -0.4862 10   GLU D CD  
8938  O  OE1 . GLU D  12  ? 3.3673 3.1449 3.0574 0.8962  0.2905  -0.4939 10   GLU D OE1 
8939  O  OE2 . GLU D  12  ? 3.1578 2.9971 2.8012 0.8617  0.2727  -0.5223 10   GLU D OE2 
8940  N  N   . LEU D  13  ? 2.6242 2.4160 2.5116 1.1758  0.1377  -0.2329 11   LEU D N   
8941  C  CA  . LEU D  13  ? 2.4973 2.3361 2.4428 1.1936  0.0949  -0.2114 11   LEU D CA  
8942  C  C   . LEU D  13  ? 2.3522 2.2737 2.2867 1.2066  -0.0129 -0.2013 11   LEU D C   
8943  O  O   . LEU D  13  ? 2.2859 2.2525 2.2566 1.2113  -0.0552 -0.1940 11   LEU D O   
8944  C  CB  . LEU D  13  ? 2.6802 2.4860 2.7066 1.2442  0.1307  -0.1397 11   LEU D CB  
8945  C  CG  . LEU D  13  ? 2.6058 2.4240 2.6634 1.2996  0.0938  -0.0599 11   LEU D CG  
8946  C  CD1 . LEU D  13  ? 2.4065 2.3160 2.4860 1.3185  -0.0186 -0.0234 11   LEU D CD1 
8947  C  CD2 . LEU D  13  ? 2.7578 2.5217 2.8934 1.3431  0.1720  0.0037  11   LEU D CD2 
8948  N  N   . VAL D  14  ? 2.4713 2.4023 2.3518 1.2120  -0.0511 -0.1994 12   VAL D N   
8949  C  CA  . VAL D  14  ? 2.5857 2.5746 2.4348 1.2189  -0.1421 -0.1961 12   VAL D CA  
8950  C  C   . VAL D  14  ? 2.5522 2.5901 2.3891 1.1878  -0.1668 -0.2476 12   VAL D C   
8951  O  O   . VAL D  14  ? 2.4201 2.5000 2.2570 1.1953  -0.2306 -0.2402 12   VAL D O   
8952  C  CB  . VAL D  14  ? 2.6295 2.6011 2.4079 1.2228  -0.1575 -0.1965 12   VAL D CB  
8953  C  CG1 . VAL D  14  ? 2.4701 2.4799 2.2003 1.2286  -0.2402 -0.1938 12   VAL D CG1 
8954  C  CG2 . VAL D  14  ? 2.7947 2.7124 2.5792 1.2538  -0.1308 -0.1415 12   VAL D CG2 
8955  N  N   . LYS D  15  ? 2.5799 2.6118 2.4019 1.1490  -0.1160 -0.2986 13   LYS D N   
8956  C  CA  . LYS D  15  ? 2.3635 2.4467 2.1742 1.1179  -0.1381 -0.3420 13   LYS D CA  
8957  C  C   . LYS D  15  ? 2.2257 2.3130 2.0836 1.1214  -0.1429 -0.3322 13   LYS D C   
8958  O  O   . LYS D  15  ? 2.1447 2.2777 1.9971 1.1179  -0.1921 -0.3436 13   LYS D O   
8959  C  CB  . LYS D  15  ? 2.4738 2.5543 2.2579 1.0664  -0.0832 -0.3930 13   LYS D CB  
8960  C  CG  . LYS D  15  ? 2.6682 2.7492 2.4143 1.0579  -0.0697 -0.4041 13   LYS D CG  
8961  C  CD  . LYS D  15  ? 2.7359 2.8244 2.4605 0.9962  -0.0169 -0.4533 13   LYS D CD  
8962  C  CE  . LYS D  15  ? 2.7403 2.8375 2.4365 0.9863  -0.0020 -0.4625 13   LYS D CE  
8963  N  NZ  . LYS D  15  ? 2.8057 2.9226 2.4834 0.9163  0.0452  -0.5093 13   LYS D NZ  
8964  N  N   . ARG D  16  ? 2.3328 2.3686 2.2391 1.1321  -0.0873 -0.3071 14   ARG D N   
8965  C  CA  . ARG D  16  ? 2.3384 2.3743 2.2996 1.1391  -0.0814 -0.2923 14   ARG D CA  
8966  C  C   . ARG D  16  ? 2.2945 2.3734 2.2969 1.1782  -0.1527 -0.2410 14   ARG D C   
8967  O  O   . ARG D  16  ? 2.1513 2.2545 2.1889 1.1783  -0.1724 -0.2366 14   ARG D O   
8968  C  CB  . ARG D  16  ? 2.4244 2.3854 2.4285 1.1429  0.0126  -0.2762 14   ARG D CB  
8969  C  CG  . ARG D  16  ? 2.5623 2.4689 2.5163 1.0874  0.0896  -0.3347 14   ARG D CG  
8970  C  CD  . ARG D  16  ? 2.5823 2.5209 2.5101 1.0466  0.0694  -0.3798 14   ARG D CD  
8971  N  NE  . ARG D  16  ? 2.4960 2.4407 2.4841 1.0721  0.0595  -0.3510 14   ARG D NE  
8972  C  CZ  . ARG D  16  ? 2.5027 2.4650 2.4766 1.0456  0.0453  -0.3796 14   ARG D CZ  
8973  N  NH1 . ARG D  16  ? 2.6720 2.6537 2.5731 0.9934  0.0348  -0.4341 14   ARG D NH1 
8974  N  NH2 . ARG D  16  ? 2.4200 2.3855 2.4549 1.0704  0.0415  -0.3501 14   ARG D NH2 
8975  N  N   . LYS D  17  ? 2.2228 2.3091 2.2144 1.2054  -0.1913 -0.2032 15   LYS D N   
8976  C  CA  . LYS D  17  ? 2.1354 2.2647 2.1458 1.2285  -0.2678 -0.1584 15   LYS D CA  
8977  C  C   . LYS D  17  ? 2.0902 2.2557 2.0427 1.2102  -0.3305 -0.1935 15   LYS D C   
8978  O  O   . LYS D  17  ? 2.0674 2.2644 2.0367 1.2137  -0.3818 -0.1746 15   LYS D O   
8979  C  CB  . LYS D  17  ? 2.1809 2.2999 2.1731 1.2535  -0.2928 -0.1110 15   LYS D CB  
8980  C  CG  . LYS D  17  ? 2.2446 2.3438 2.3133 1.2862  -0.2508 -0.0477 15   LYS D CG  
8981  C  CD  . LYS D  17  ? 2.2697 2.3616 2.3049 1.3077  -0.2855 0.0009  15   LYS D CD  
8982  C  CE  . LYS D  17  ? 2.3212 2.4053 2.4392 1.3473  -0.2511 0.0775  15   LYS D CE  
8983  N  NZ  . LYS D  17  ? 2.3794 2.4497 2.4530 1.3660  -0.2810 0.1252  15   LYS D NZ  
8984  N  N   . ARG D  18  ? 2.2268 2.3890 2.1134 1.1911  -0.3239 -0.2410 16   ARG D N   
8985  C  CA  . ARG D  18  ? 2.1648 2.3583 1.9999 1.1793  -0.3699 -0.2724 16   ARG D CA  
8986  C  C   . ARG D  18  ? 2.1518 2.3650 2.0123 1.1605  -0.3606 -0.2985 16   ARG D C   
8987  O  O   . ARG D  18  ? 2.0847 2.3191 1.9311 1.1614  -0.4056 -0.3001 16   ARG D O   
8988  C  CB  . ARG D  18  ? 2.1665 2.3629 1.9425 1.1686  -0.3577 -0.3066 16   ARG D CB  
8989  C  CG  . ARG D  18  ? 2.2627 2.4962 1.9956 1.1606  -0.3889 -0.3370 16   ARG D CG  
8990  C  CD  . ARG D  18  ? 2.3846 2.6083 2.0629 1.1814  -0.4430 -0.3190 16   ARG D CD  
8991  N  NE  . ARG D  18  ? 2.3776 2.6279 2.0190 1.1812  -0.4641 -0.3417 16   ARG D NE  
8992  C  CZ  . ARG D  18  ? 2.4256 2.6560 2.0051 1.1968  -0.4983 -0.3341 16   ARG D CZ  
8993  N  NH1 . ARG D  18  ? 2.6189 2.8028 2.1571 1.2056  -0.5207 -0.3082 16   ARG D NH1 
8994  N  NH2 . ARG D  18  ? 2.2402 2.4916 1.7921 1.2021  -0.5073 -0.3505 16   ARG D NH2 
8995  N  N   . ILE D  19  ? 2.1983 2.3940 2.0855 1.1398  -0.2984 -0.3204 17   ILE D N   
8996  C  CA  . ILE D  19  ? 2.1865 2.3899 2.0830 1.1156  -0.2835 -0.3482 17   ILE D CA  
8997  C  C   . ILE D  19  ? 2.1777 2.3819 2.1309 1.1324  -0.2996 -0.3159 17   ILE D C   
8998  O  O   . ILE D  19  ? 2.0530 2.2762 1.9970 1.1239  -0.3268 -0.3288 17   ILE D O   
8999  C  CB  . ILE D  19  ? 2.3193 2.4856 2.2170 1.0816  -0.2058 -0.3783 17   ILE D CB  
9000  C  CG1 . ILE D  19  ? 2.4504 2.6328 2.2936 1.0542  -0.1958 -0.4130 17   ILE D CG1 
9001  C  CG2 . ILE D  19  ? 2.3379 2.4979 2.2359 1.0534  -0.1861 -0.4040 17   ILE D CG2 
9002  C  CD1 . ILE D  19  ? 2.5494 2.6929 2.3758 1.0056  -0.1216 -0.4485 17   ILE D CD1 
9003  N  N   . GLU D  20  ? 2.2305 2.4181 2.2476 1.1568  -0.2813 -0.2695 18   GLU D N   
9004  C  CA  . GLU D  20  ? 2.0127 2.2178 2.1009 1.1728  -0.2977 -0.2301 18   GLU D CA  
9005  C  C   . GLU D  20  ? 1.9876 2.2338 2.0557 1.1814  -0.3829 -0.2079 18   GLU D C   
9006  O  O   . GLU D  20  ? 1.9735 2.2442 2.0850 1.1822  -0.4080 -0.1869 18   GLU D O   
9007  C  CB  . GLU D  20  ? 2.0482 2.2354 2.2219 1.2003  -0.2511 -0.1769 18   GLU D CB  
9008  C  CG  . GLU D  20  ? 2.1266 2.2535 2.3235 1.1896  -0.1523 -0.1965 18   GLU D CG  
9009  C  CD  . GLU D  20  ? 2.1450 2.2622 2.3561 1.1683  -0.1269 -0.2224 18   GLU D CD  
9010  O  OE1 . GLU D  20  ? 2.2233 2.3828 2.4796 1.1787  -0.1699 -0.1975 18   GLU D OE1 
9011  O  OE2 . GLU D  20  ? 2.1357 2.1994 2.3057 1.1359  -0.0633 -0.2683 18   GLU D OE2 
9012  N  N   . ALA D  21  ? 2.2875 2.5347 2.2856 1.1842  -0.4225 -0.2129 19   ALA D N   
9013  C  CA  . ALA D  21  ? 2.3794 2.6438 2.3279 1.1833  -0.4951 -0.2031 19   ALA D CA  
9014  C  C   . ALA D  21  ? 2.3433 2.6080 2.2287 1.1680  -0.5106 -0.2492 19   ALA D C   
9015  O  O   . ALA D  21  ? 2.3593 2.6267 2.2132 1.1567  -0.5538 -0.2448 19   ALA D O   
9016  C  CB  . ALA D  21  ? 2.4725 2.7216 2.3619 1.1927  -0.5224 -0.1870 19   ALA D CB  
9017  N  N   . ILE D  22  ? 2.2907 2.5513 2.1524 1.1584  -0.4726 -0.2903 20   ILE D N   
9018  C  CA  . ILE D  22  ? 2.2260 2.4975 2.0410 1.1465  -0.4834 -0.3260 20   ILE D CA  
9019  C  C   . ILE D  22  ? 2.0800 2.3534 1.9356 1.1347  -0.4740 -0.3291 20   ILE D C   
9020  O  O   . ILE D  22  ? 2.0934 2.3698 1.9169 1.1314  -0.5032 -0.3381 20   ILE D O   
9021  C  CB  . ILE D  22  ? 2.1915 2.4751 1.9782 1.1334  -0.4498 -0.3619 20   ILE D CB  
9022  C  CG1 . ILE D  22  ? 2.0561 2.3414 1.7975 1.1468  -0.4615 -0.3602 20   ILE D CG1 
9023  C  CG2 . ILE D  22  ? 2.3559 2.6624 2.1085 1.1204  -0.4586 -0.3903 20   ILE D CG2 
9024  C  CD1 . ILE D  22  ? 2.0382 2.3224 1.7178 1.1630  -0.5055 -0.3576 20   ILE D CD1 
9025  N  N   . ARG D  23  ? 1.9641 2.2267 1.8874 1.1293  -0.4259 -0.3207 21   ARG D N   
9026  C  CA  . ARG D  23  ? 1.9679 2.2239 1.9337 1.1184  -0.4045 -0.3224 21   ARG D CA  
9027  C  C   . ARG D  23  ? 1.9339 2.2070 1.9228 1.1264  -0.4536 -0.2929 21   ARG D C   
9028  O  O   . ARG D  23  ? 1.9308 2.2021 1.8960 1.1152  -0.4678 -0.3093 21   ARG D O   
9029  C  CB  . ARG D  23  ? 2.0159 2.2460 2.0551 1.1190  -0.3359 -0.3078 21   ARG D CB  
9030  C  CG  . ARG D  23  ? 2.0581 2.2754 2.1557 1.1136  -0.3040 -0.2996 21   ARG D CG  
9031  C  CD  . ARG D  23  ? 2.1260 2.3089 2.3004 1.1232  -0.2271 -0.2759 21   ARG D CD  
9032  N  NE  . ARG D  23  ? 2.2329 2.3640 2.3579 1.0985  -0.1627 -0.3162 21   ARG D NE  
9033  C  CZ  . ARG D  23  ? 2.3541 2.4373 2.4486 1.0654  -0.1061 -0.3537 21   ARG D CZ  
9034  N  NH1 . ARG D  23  ? 2.3530 2.4313 2.4649 1.0592  -0.1031 -0.3552 21   ARG D NH1 
9035  N  NH2 . ARG D  23  ? 2.4919 2.5278 2.5306 1.0328  -0.0513 -0.3906 21   ARG D NH2 
9036  N  N   . GLY D  24  ? 1.9940 2.2844 2.0222 1.1416  -0.4823 -0.2482 22   GLY D N   
9037  C  CA  . GLY D  24  ? 2.1552 2.4683 2.2004 1.1377  -0.5338 -0.2193 22   GLY D CA  
9038  C  C   . GLY D  24  ? 2.2944 2.5939 2.2369 1.1280  -0.5872 -0.2394 22   GLY D C   
9039  O  O   . GLY D  24  ? 2.4059 2.7090 2.3399 1.1139  -0.6218 -0.2309 22   GLY D O   
9040  N  N   . GLN D  25  ? 2.3614 2.6399 2.2252 1.1304  -0.5856 -0.2650 23   GLN D N   
9041  C  CA  . GLN D  25  ? 2.3398 2.5906 2.1018 1.1203  -0.6181 -0.2809 23   GLN D CA  
9042  C  C   . GLN D  25  ? 2.0924 2.3342 1.8183 1.1209  -0.6131 -0.3133 23   GLN D C   
9043  O  O   . GLN D  25  ? 2.0676 2.2864 1.7468 1.1127  -0.6404 -0.3141 23   GLN D O   
9044  C  CB  . GLN D  25  ? 2.4467 2.6827 2.1503 1.1297  -0.6100 -0.2918 23   GLN D CB  
9045  C  CG  . GLN D  25  ? 2.5203 2.7167 2.1196 1.1284  -0.6337 -0.3020 23   GLN D CG  
9046  C  CD  . GLN D  25  ? 2.5800 2.7691 2.1342 1.1451  -0.6150 -0.3152 23   GLN D CD  
9047  O  OE1 . GLN D  25  ? 2.6284 2.8499 2.2234 1.1541  -0.5856 -0.3270 23   GLN D OE1 
9048  N  NE2 . GLN D  25  ? 2.6247 2.7690 2.0921 1.1522  -0.6311 -0.3138 23   GLN D NE2 
9049  N  N   . ILE D  26  ? 2.0402 2.2968 1.7788 1.1292  -0.5790 -0.3398 24   ILE D N   
9050  C  CA  . ILE D  26  ? 2.0481 2.2996 1.7482 1.1241  -0.5728 -0.3656 24   ILE D CA  
9051  C  C   . ILE D  26  ? 2.2004 2.4388 1.9280 1.1104  -0.5779 -0.3587 24   ILE D C   
9052  O  O   . ILE D  26  ? 2.4759 2.6914 2.1491 1.1090  -0.5948 -0.3671 24   ILE D O   
9053  C  CB  . ILE D  26  ? 2.0555 2.3281 1.7675 1.1143  -0.5325 -0.3907 24   ILE D CB  
9054  C  CG1 . ILE D  26  ? 2.0530 2.3467 1.7447 1.1231  -0.5272 -0.3964 24   ILE D CG1 
9055  C  CG2 . ILE D  26  ? 2.0780 2.3516 1.7434 1.1077  -0.5324 -0.4116 24   ILE D CG2 
9056  C  CD1 . ILE D  26  ? 2.0860 2.4058 1.7835 1.1015  -0.4908 -0.4215 24   ILE D CD1 
9057  N  N   . LEU D  27  ? 2.0926 2.3432 1.9077 1.1019  -0.5582 -0.3401 25   LEU D N   
9058  C  CA  . LEU D  27  ? 2.1725 2.4189 2.0302 1.0883  -0.5570 -0.3299 25   LEU D CA  
9059  C  C   . LEU D  27  ? 2.3044 2.5459 2.1369 1.0808  -0.6082 -0.3096 25   LEU D C   
9060  O  O   . LEU D  27  ? 2.5265 2.7528 2.3497 1.0660  -0.6149 -0.3133 25   LEU D O   
9061  C  CB  . LEU D  27  ? 2.2705 2.5357 2.2397 1.0873  -0.5179 -0.3057 25   LEU D CB  
9062  C  CG  . LEU D  27  ? 2.2202 2.4681 2.2014 1.0835  -0.4550 -0.3306 25   LEU D CG  
9063  C  CD1 . LEU D  27  ? 2.3693 2.6189 2.4589 1.0877  -0.4042 -0.3021 25   LEU D CD1 
9064  C  CD2 . LEU D  27  ? 2.1293 2.3505 2.0506 1.0661  -0.4400 -0.3674 25   LEU D CD2 
9065  N  N   . SER D  28  ? 2.2111 2.4589 2.0242 1.0850  -0.6425 -0.2891 26   SER D N   
9066  C  CA  . SER D  28  ? 2.2593 2.4937 2.0296 1.0660  -0.6917 -0.2720 26   SER D CA  
9067  C  C   . SER D  28  ? 2.1798 2.3544 1.8237 1.0661  -0.7039 -0.3009 26   SER D C   
9068  O  O   . SER D  28  ? 2.2657 2.4087 1.8635 1.0433  -0.7263 -0.3007 26   SER D O   
9069  C  CB  . SER D  28  ? 2.5518 2.8065 2.3324 1.0646  -0.7240 -0.2377 26   SER D CB  
9070  O  OG  . SER D  28  ? 2.6171 2.8452 2.3305 1.0810  -0.7150 -0.2532 26   SER D OG  
9071  N  N   . LYS D  29  ? 2.2541 2.4126 1.8434 1.0913  -0.6853 -0.3233 27   LYS D N   
9072  C  CA  . LYS D  29  ? 2.3062 2.4097 1.7853 1.1013  -0.6878 -0.3426 27   LYS D CA  
9073  C  C   . LYS D  29  ? 2.3195 2.4070 1.7865 1.0992  -0.6711 -0.3595 27   LYS D C   
9074  O  O   . LYS D  29  ? 2.5206 2.5509 1.9036 1.0982  -0.6764 -0.3666 27   LYS D O   
9075  C  CB  . LYS D  29  ? 2.3934 2.5006 1.8374 1.1285  -0.6677 -0.3537 27   LYS D CB  
9076  C  CG  . LYS D  29  ? 2.4436 2.5437 1.8723 1.1257  -0.6762 -0.3396 27   LYS D CG  
9077  C  CD  . LYS D  29  ? 2.3811 2.4875 1.7835 1.1453  -0.6467 -0.3507 27   LYS D CD  
9078  C  CE  . LYS D  29  ? 2.5125 2.5958 1.8800 1.1489  -0.6558 -0.3382 27   LYS D CE  
9079  N  NZ  . LYS D  29  ? 2.6439 2.7345 1.9869 1.1724  -0.6267 -0.3471 27   LYS D NZ  
9080  N  N   . LEU D  30  ? 2.2844 2.4102 1.8252 1.0965  -0.6460 -0.3659 28   LEU D N   
9081  C  CA  . LEU D  30  ? 2.3969 2.5049 1.9269 1.0899  -0.6284 -0.3804 28   LEU D CA  
9082  C  C   . LEU D  30  ? 2.4374 2.5360 2.0093 1.0610  -0.6364 -0.3688 28   LEU D C   
9083  O  O   . LEU D  30  ? 2.3847 2.4618 1.9498 1.0518  -0.6190 -0.3798 28   LEU D O   
9084  C  CB  . LEU D  30  ? 2.4764 2.6188 2.0515 1.0919  -0.5934 -0.3949 28   LEU D CB  
9085  C  CG  . LEU D  30  ? 2.4867 2.6557 2.0302 1.1111  -0.5853 -0.4062 28   LEU D CG  
9086  C  CD1 . LEU D  30  ? 2.5042 2.7024 2.0867 1.0957  -0.5513 -0.4220 28   LEU D CD1 
9087  C  CD2 . LEU D  30  ? 2.5448 2.6917 1.9995 1.1330  -0.5946 -0.4103 28   LEU D CD2 
9088  N  N   . ARG D  31  ? 2.4384 2.5581 2.0550 1.0447  -0.6632 -0.3435 29   ARG D N   
9089  C  CA  . ARG D  31  ? 2.5393 2.6746 2.2173 1.0132  -0.6763 -0.3231 29   ARG D CA  
9090  C  C   . ARG D  31  ? 2.5546 2.7211 2.3343 1.0119  -0.6352 -0.3214 29   ARG D C   
9091  O  O   . ARG D  31  ? 2.5434 2.7001 2.3458 0.9918  -0.6256 -0.3212 29   ARG D O   
9092  C  CB  . ARG D  31  ? 2.4931 2.5677 2.0808 0.9897  -0.6935 -0.3336 29   ARG D CB  
9093  C  CG  . ARG D  31  ? 2.4495 2.5459 2.0802 0.9454  -0.7256 -0.3076 29   ARG D CG  
9094  C  CD  . ARG D  31  ? 2.5707 2.5938 2.1040 0.9165  -0.7307 -0.3251 29   ARG D CD  
9095  N  NE  . ARG D  31  ? 2.5949 2.5391 1.9853 0.9200  -0.7437 -0.3404 29   ARG D NE  
9096  C  CZ  . ARG D  31  ? 2.6497 2.5624 1.9727 0.8807  -0.7799 -0.3313 29   ARG D CZ  
9097  N  NH1 . ARG D  31  ? 2.7000 2.6708 2.0937 0.8324  -0.8164 -0.3034 29   ARG D NH1 
9098  N  NH2 . ARG D  31  ? 2.7461 2.5689 1.9294 0.8874  -0.7776 -0.3475 29   ARG D NH2 
9099  N  N   . LEU D  32  ? 2.5141 2.7087 2.3491 1.0309  -0.6044 -0.3215 30   LEU D N   
9100  C  CA  . LEU D  32  ? 2.2809 2.4860 2.1970 1.0296  -0.5523 -0.3231 30   LEU D CA  
9101  C  C   . LEU D  32  ? 2.4375 2.6930 2.4739 1.0369  -0.5382 -0.2855 30   LEU D C   
9102  O  O   . LEU D  32  ? 2.5605 2.8392 2.6016 1.0495  -0.5597 -0.2690 30   LEU D O   
9103  C  CB  . LEU D  32  ? 2.3649 2.5443 2.2273 1.0393  -0.5157 -0.3586 30   LEU D CB  
9104  C  CG  . LEU D  32  ? 2.6500 2.7871 2.4086 1.0368  -0.5197 -0.3879 30   LEU D CG  
9105  C  CD1 . LEU D  32  ? 2.5039 2.6365 2.2181 1.0399  -0.4913 -0.4149 30   LEU D CD1 
9106  C  CD2 . LEU D  32  ? 2.8889 2.9978 2.6610 1.0177  -0.5042 -0.3886 30   LEU D CD2 
9107  N  N   . ALA D  33  ? 2.5774 2.8465 2.7122 1.0316  -0.4973 -0.2682 31   ALA D N   
9108  C  CA  . ALA D  33  ? 2.5435 2.8560 2.8041 1.0466  -0.4674 -0.2264 31   ALA D CA  
9109  C  C   . ALA D  33  ? 2.3448 2.6201 2.6179 1.0589  -0.3928 -0.2463 31   ALA D C   
9110  O  O   . ALA D  33  ? 2.2896 2.5809 2.6215 1.0779  -0.3687 -0.2220 31   ALA D O   
9111  C  CB  . ALA D  33  ? 2.5540 2.9098 2.9332 1.0369  -0.4590 -0.1850 31   ALA D CB  
9112  N  N   . SER D  34  ? 2.3314 2.5513 2.5406 1.0445  -0.3545 -0.2895 32   SER D N   
9113  C  CA  . SER D  34  ? 2.4784 2.6501 2.6745 1.0415  -0.2823 -0.3153 32   SER D CA  
9114  C  C   . SER D  34  ? 2.4917 2.6208 2.5571 1.0209  -0.2875 -0.3680 32   SER D C   
9115  O  O   . SER D  34  ? 2.4260 2.5505 2.4360 1.0133  -0.3242 -0.3793 32   SER D O   
9116  C  CB  . SER D  34  ? 2.8721 3.0182 3.1602 1.0397  -0.2055 -0.2986 32   SER D CB  
9117  O  OG  . SER D  34  ? 3.1105 3.2393 3.3834 1.0221  -0.2064 -0.3094 32   SER D OG  
9118  N  N   . PRO D  35  ? 2.5718 2.6719 2.5847 1.0097  -0.2521 -0.3975 33   PRO D N   
9119  C  CA  . PRO D  35  ? 2.7238 2.8006 2.6179 0.9867  -0.2617 -0.4403 33   PRO D CA  
9120  C  C   . PRO D  35  ? 2.9481 2.9781 2.8097 0.9657  -0.2344 -0.4565 33   PRO D C   
9121  O  O   . PRO D  35  ? 3.0023 2.9951 2.9238 0.9586  -0.1742 -0.4486 33   PRO D O   
9122  C  CB  . PRO D  35  ? 2.6399 2.6942 2.5064 0.9670  -0.2145 -0.4632 33   PRO D CB  
9123  C  CG  . PRO D  35  ? 2.5369 2.6152 2.4874 0.9925  -0.2077 -0.4323 33   PRO D CG  
9124  C  CD  . PRO D  35  ? 2.5347 2.6289 2.5900 1.0161  -0.2084 -0.3894 33   PRO D CD  
9125  N  N   . PRO D  36  ? 3.0602 3.0877 2.8285 0.9584  -0.2725 -0.4756 34   PRO D N   
9126  C  CA  . PRO D  36  ? 3.0379 3.0154 2.7637 0.9391  -0.2490 -0.4897 34   PRO D CA  
9127  C  C   . PRO D  36  ? 2.8712 2.7906 2.5447 0.9012  -0.1845 -0.5199 34   PRO D C   
9128  O  O   . PRO D  36  ? 2.8741 2.7912 2.5341 0.8851  -0.1595 -0.5335 34   PRO D O   
9129  C  CB  . PRO D  36  ? 3.0449 3.0380 2.6782 0.9482  -0.3093 -0.4962 34   PRO D CB  
9130  C  CG  . PRO D  36  ? 3.0333 3.0763 2.6382 0.9593  -0.3441 -0.4985 34   PRO D CG  
9131  C  CD  . PRO D  36  ? 3.0174 3.0852 2.7151 0.9714  -0.3335 -0.4810 34   PRO D CD  
9132  N  N   . SER D  37  ? 2.8050 2.6684 2.4374 0.8813  -0.1547 -0.5323 35   SER D N   
9133  C  CA  . SER D  37  ? 2.8865 2.6763 2.4519 0.8374  -0.0881 -0.5625 35   SER D CA  
9134  C  C   . SER D  37  ? 2.9314 2.7302 2.3636 0.8092  -0.1241 -0.5879 35   SER D C   
9135  O  O   . SER D  37  ? 2.9141 2.7451 2.2964 0.8251  -0.1826 -0.5812 35   SER D O   
9136  C  CB  . SER D  37  ? 2.9864 2.7056 2.5609 0.8261  -0.0349 -0.5635 35   SER D CB  
9137  O  OG  . SER D  37  ? 2.9755 2.6966 2.4857 0.8303  -0.0811 -0.5645 35   SER D OG  
9138  N  N   . GLN D  38  ? 3.2119 2.9800 2.5850 0.7647  -0.0852 -0.6143 36   GLN D N   
9139  C  CA  . GLN D  38  ? 3.4471 3.2409 2.7011 0.7277  -0.1208 -0.6343 36   GLN D CA  
9140  C  C   . GLN D  38  ? 3.5571 3.2600 2.7007 0.6644  -0.0653 -0.6653 36   GLN D C   
9141  O  O   . GLN D  38  ? 3.5108 3.2267 2.5478 0.6154  -0.0829 -0.6842 36   GLN D O   
9142  C  CB  . GLN D  38  ? 3.5850 3.4351 2.8511 0.7180  -0.1351 -0.6393 36   GLN D CB  
9143  C  CG  . GLN D  38  ? 3.6521 3.5794 2.8336 0.6953  -0.1968 -0.6443 36   GLN D CG  
9144  C  CD  . GLN D  38  ? 3.6482 3.6239 2.8474 0.6775  -0.1986 -0.6522 36   GLN D CD  
9145  O  OE1 . GLN D  38  ? 3.6679 3.6074 2.9323 0.6825  -0.1500 -0.6554 36   GLN D OE1 
9146  N  NE2 . GLN D  38  ? 3.6263 3.6877 2.7722 0.6583  -0.2528 -0.6510 36   GLN D NE2 
9147  N  N   . GLY D  39  ? 3.4692 3.0822 2.6349 0.6617  0.0014  -0.6686 37   GLY D N   
9148  C  CA  . GLY D  39  ? 3.5641 3.0728 2.6183 0.6035  0.0614  -0.6976 37   GLY D CA  
9149  C  C   . GLY D  39  ? 3.5884 3.0933 2.5831 0.6134  0.0232  -0.6895 37   GLY D C   
9150  O  O   . GLY D  39  ? 3.6060 3.0300 2.4883 0.5667  0.0576  -0.7102 37   GLY D O   
9151  N  N   . GLU D  40  ? 3.6069 3.1889 2.6686 0.6724  -0.0435 -0.6593 38   GLU D N   
9152  C  CA  . GLU D  40  ? 3.5252 3.1119 2.5304 0.6907  -0.0880 -0.6467 38   GLU D CA  
9153  C  C   . GLU D  40  ? 3.5038 3.1850 2.4504 0.7041  -0.1734 -0.6328 38   GLU D C   
9154  O  O   . GLU D  40  ? 3.4528 3.1493 2.3548 0.7304  -0.2164 -0.6146 38   GLU D O   
9155  C  CB  . GLU D  40  ? 3.2461 2.8347 2.3593 0.7420  -0.0904 -0.6227 38   GLU D CB  
9156  C  CG  . GLU D  40  ? 3.0495 2.5527 2.2395 0.7315  0.0007  -0.6270 38   GLU D CG  
9157  C  CD  . GLU D  40  ? 2.8807 2.4126 2.2177 0.7757  -0.0010 -0.5962 38   GLU D CD  
9158  O  OE1 . GLU D  40  ? 2.7155 2.3315 2.1418 0.8128  -0.0536 -0.5721 38   GLU D OE1 
9159  O  OE2 . GLU D  40  ? 2.9400 2.4052 2.2979 0.7652  0.0565  -0.5967 38   GLU D OE2 
9160  N  N   . VAL D  41  ? 3.4845 3.2244 2.4256 0.6836  -0.1914 -0.6397 39   VAL D N   
9161  C  CA  . VAL D  41  ? 3.4050 3.2509 2.3114 0.6954  -0.2667 -0.6222 39   VAL D CA  
9162  C  C   . VAL D  41  ? 3.5848 3.4280 2.3741 0.6208  -0.2617 -0.6433 39   VAL D C   
9163  O  O   . VAL D  41  ? 3.6144 3.3940 2.3838 0.5656  -0.2015 -0.6751 39   VAL D O   
9164  C  CB  . VAL D  41  ? 3.3325 3.2575 2.3388 0.7295  -0.2924 -0.6110 39   VAL D CB  
9165  C  CG1 . VAL D  41  ? 3.4786 3.5169 2.4600 0.7442  -0.3629 -0.5897 39   VAL D CG1 
9166  C  CG2 . VAL D  41  ? 3.1947 3.1115 2.3058 0.7888  -0.2936 -0.5924 39   VAL D CG2 
9167  N  N   . PRO D  42  ? 3.7894 3.6975 2.4958 0.6130  -0.3200 -0.6246 40   PRO D N   
9168  C  CA  . PRO D  42  ? 4.0541 3.9668 2.6419 0.5301  -0.3213 -0.6425 40   PRO D CA  
9169  C  C   . PRO D  42  ? 4.0386 4.0592 2.6512 0.5065  -0.3559 -0.6415 40   PRO D C   
9170  O  O   . PRO D  42  ? 3.7187 3.8573 2.3881 0.5573  -0.4186 -0.6064 40   PRO D O   
9171  C  CB  . PRO D  42  ? 4.0238 3.9692 2.5214 0.5396  -0.3737 -0.6114 40   PRO D CB  
9172  C  CG  . PRO D  42  ? 3.7627 3.7578 2.3462 0.6369  -0.4134 -0.5717 40   PRO D CG  
9173  C  CD  . PRO D  42  ? 3.6361 3.6115 2.3473 0.6773  -0.3835 -0.5827 40   PRO D CD  
9174  N  N   . PRO D  43  ? 4.1504 4.1271 2.7189 0.4282  -0.3100 -0.6798 41   PRO D N   
9175  C  CA  . PRO D  43  ? 4.0700 4.1453 2.6561 0.3952  -0.3383 -0.6824 41   PRO D CA  
9176  C  C   . PRO D  43  ? 4.1731 4.3601 2.6689 0.3472  -0.4092 -0.6618 41   PRO D C   
9177  O  O   . PRO D  43  ? 4.1918 4.3324 2.5588 0.2791  -0.4042 -0.6739 41   PRO D O   
9178  C  CB  . PRO D  43  ? 4.0866 4.0477 2.6351 0.3207  -0.2517 -0.7330 41   PRO D CB  
9179  C  CG  . PRO D  43  ? 4.0886 3.9105 2.5405 0.2838  -0.1939 -0.7555 41   PRO D CG  
9180  C  CD  . PRO D  43  ? 4.0639 3.8863 2.5702 0.3691  -0.2184 -0.7230 41   PRO D CD  
9181  N  N   . GLY D  44  ? 4.1261 2.5519 2.7190 -0.0018 -0.1600 -0.1039 42   GLY D N   
9182  C  CA  . GLY D  44  ? 4.2318 2.7016 2.7884 -0.0516 -0.1863 -0.1253 42   GLY D CA  
9183  C  C   . GLY D  44  ? 3.9824 2.5592 2.5884 -0.0479 -0.2350 -0.1044 42   GLY D C   
9184  O  O   . GLY D  44  ? 3.8504 2.4660 2.4710 -0.0709 -0.2594 -0.1057 42   GLY D O   
9185  N  N   . PRO D  45  ? 3.8683 2.4920 2.5038 -0.0180 -0.2466 -0.0841 43   PRO D N   
9186  C  CA  . PRO D  45  ? 3.8448 2.5631 2.5257 -0.0133 -0.2887 -0.0646 43   PRO D CA  
9187  C  C   . PRO D  45  ? 3.9418 2.6905 2.6936 0.0088  -0.3060 -0.0463 43   PRO D C   
9188  O  O   . PRO D  45  ? 4.0427 2.7730 2.8366 0.0451  -0.2929 -0.0322 43   PRO D O   
9189  C  CB  . PRO D  45  ? 3.8039 2.5412 2.4987 0.0160  -0.2837 -0.0461 43   PRO D CB  
9190  C  CG  . PRO D  45  ? 3.7393 2.4038 2.4279 0.0395  -0.2427 -0.0488 43   PRO D CG  
9191  C  CD  . PRO D  45  ? 3.8526 2.4434 2.4820 0.0117  -0.2180 -0.0780 43   PRO D CD  
9192  N  N   . LEU D  46  ? 3.9442 2.7468 2.7088 -0.0133 -0.3357 -0.0482 44   LEU D N   
9193  C  CA  . LEU D  46  ? 3.7858 2.6315 2.6146 0.0055  -0.3555 -0.0330 44   LEU D CA  
9194  C  C   . LEU D  46  ? 3.6558 2.5909 2.5161 0.0002  -0.3931 -0.0252 44   LEU D C   
9195  O  O   . LEU D  46  ? 3.8291 2.7974 2.6656 -0.0346 -0.4094 -0.0371 44   LEU D O   
9196  C  CB  . LEU D  46  ? 3.7609 2.5733 2.5769 -0.0126 -0.3458 -0.0413 44   LEU D CB  
9197  C  CG  . LEU D  46  ? 3.6297 2.3520 2.4247 0.0039  -0.3064 -0.0412 44   LEU D CG  
9198  C  CD1 . LEU D  46  ? 3.5513 2.2182 2.3088 -0.0272 -0.2871 -0.0529 44   LEU D CD1 
9199  C  CD2 . LEU D  46  ? 3.3123 2.0482 2.1667 0.0554  -0.3054 -0.0183 44   LEU D CD2 
9200  N  N   . PRO D  47  ? 3.3366 2.3121 2.2525 0.0335  -0.4053 -0.0063 45   PRO D N   
9201  C  CA  . PRO D  47  ? 3.3615 2.4141 2.3079 0.0344  -0.4361 0.0045  45   PRO D CA  
9202  C  C   . PRO D  47  ? 3.3885 2.4924 2.3638 0.0232  -0.4590 0.0002  45   PRO D C   
9203  O  O   . PRO D  47  ? 3.5469 2.6388 2.5455 0.0307  -0.4541 -0.0028 45   PRO D O   
9204  C  CB  . PRO D  47  ? 3.2224 2.2868 2.2307 0.0742  -0.4344 0.0232  45   PRO D CB  
9205  C  CG  . PRO D  47  ? 3.0042 2.0244 2.0331 0.0927  -0.4138 0.0188  45   PRO D CG  
9206  C  CD  . PRO D  47  ? 2.9739 1.9279 1.9340 0.0719  -0.3898 0.0053  45   PRO D CD  
9207  N  N   . GLU D  48  ? 3.2065 2.3741 2.1793 0.0067  -0.4837 0.0014  46   GLU D N   
9208  C  CA  . GLU D  48  ? 3.0588 2.2871 2.0669 -0.0010 -0.5053 -0.0012 46   GLU D CA  
9209  C  C   . GLU D  48  ? 2.9131 2.1807 1.9969 0.0371  -0.5170 0.0125  46   GLU D C   
9210  O  O   . GLU D  48  ? 2.9087 2.2289 2.0276 0.0366  -0.5330 0.0099  46   GLU D O   
9211  C  CB  . GLU D  48  ? 2.9300 2.2250 1.9165 -0.0293 -0.5284 -0.0049 46   GLU D CB  
9212  C  CG  . GLU D  48  ? 2.9202 2.1903 1.8369 -0.0780 -0.5198 -0.0291 46   GLU D CG  
9213  C  CD  . GLU D  48  ? 2.8892 2.2464 1.7986 -0.1090 -0.5469 -0.0371 46   GLU D CD  
9214  O  OE1 . GLU D  48  ? 2.7666 2.2009 1.7181 -0.0859 -0.5718 -0.0181 46   GLU D OE1 
9215  O  OE2 . GLU D  48  ? 3.0046 2.3542 1.8692 -0.1565 -0.5419 -0.0633 46   GLU D OE2 
9216  N  N   . ALA D  49  ? 2.7785 2.0219 1.8895 0.0680  -0.5069 0.0242  47   ALA D N   
9217  C  CA  . ALA D  49  ? 2.8207 2.0917 2.0061 0.1007  -0.5131 0.0301  47   ALA D CA  
9218  C  C   . ALA D  49  ? 2.7812 2.0358 1.9887 0.1095  -0.5050 0.0178  47   ALA D C   
9219  O  O   . ALA D  49  ? 2.8294 2.1262 2.0881 0.1239  -0.5165 0.0125  47   ALA D O   
9220  C  CB  . ALA D  49  ? 2.6821 1.9327 1.8923 0.1255  -0.5017 0.0454  47   ALA D CB  
9221  N  N   . VAL D  50  ? 2.6984 1.8943 1.8668 0.1040  -0.4844 0.0137  48   VAL D N   
9222  C  CA  . VAL D  50  ? 2.7051 1.8897 1.8868 0.1154  -0.4769 0.0076  48   VAL D CA  
9223  C  C   . VAL D  50  ? 2.7601 1.9528 1.9109 0.0911  -0.4805 0.0024  48   VAL D C   
9224  O  O   . VAL D  50  ? 2.8350 2.0386 2.0010 0.1020  -0.4795 0.0013  48   VAL D O   
9225  C  CB  . VAL D  50  ? 2.6663 1.7864 1.8254 0.1268  -0.4505 0.0099  48   VAL D CB  
9226  C  CG1 . VAL D  50  ? 2.6216 1.7366 1.8136 0.1471  -0.4435 0.0154  48   VAL D CG1 
9227  C  CG2 . VAL D  50  ? 2.7691 1.8298 1.8538 0.0989  -0.4328 0.0073  48   VAL D CG2 
9228  N  N   . LEU D  51  ? 2.7518 1.9439 1.8596 0.0572  -0.4840 -0.0011 49   LEU D N   
9229  C  CA  . LEU D  51  ? 2.7520 1.9598 1.8393 0.0286  -0.4866 -0.0074 49   LEU D CA  
9230  C  C   . LEU D  51  ? 2.8444 2.1358 1.9820 0.0350  -0.5107 -0.0078 49   LEU D C   
9231  O  O   . LEU D  51  ? 3.0732 2.3854 2.2124 0.0249  -0.5104 -0.0103 49   LEU D O   
9232  C  CB  . LEU D  51  ? 2.8000 1.9895 1.8307 -0.0144 -0.4831 -0.0171 49   LEU D CB  
9233  C  CG  . LEU D  51  ? 2.9703 2.0689 1.9415 -0.0291 -0.4532 -0.0237 49   LEU D CG  
9234  C  CD1 . LEU D  51  ? 3.3029 2.3952 2.2206 -0.0787 -0.4518 -0.0421 49   LEU D CD1 
9235  C  CD2 . LEU D  51  ? 2.9696 2.0125 1.9325 -0.0202 -0.4289 -0.0191 49   LEU D CD2 
9236  N  N   . ALA D  52  ? 2.7523 2.0894 1.9312 0.0531  -0.5281 -0.0040 50   ALA D N   
9237  C  CA  . ALA D  52  ? 2.5948 2.0067 1.8279 0.0660  -0.5472 -0.0060 50   ALA D CA  
9238  C  C   . ALA D  52  ? 2.5454 1.9649 1.8207 0.0956  -0.5443 -0.0112 50   ALA D C   
9239  O  O   . ALA D  52  ? 2.5357 2.0081 1.8394 0.0999  -0.5533 -0.0180 50   ALA D O   
9240  C  CB  . ALA D  52  ? 2.5535 2.0038 1.8193 0.0806  -0.5623 0.0024  50   ALA D CB  
9241  N  N   . LEU D  53  ? 2.4056 1.7807 1.6864 0.1160  -0.5320 -0.0101 51   LEU D N   
9242  C  CA  . LEU D  53  ? 2.3942 1.7836 1.7102 0.1418  -0.5303 -0.0180 51   LEU D CA  
9243  C  C   . LEU D  53  ? 2.4303 1.8136 1.7116 0.1337  -0.5222 -0.0159 51   LEU D C   
9244  O  O   . LEU D  53  ? 2.5598 1.9911 1.8638 0.1449  -0.5292 -0.0226 51   LEU D O   
9245  C  CB  . LEU D  53  ? 2.3938 1.7432 1.7237 0.1624  -0.5181 -0.0170 51   LEU D CB  
9246  C  CG  . LEU D  53  ? 2.3585 1.7302 1.7532 0.1832  -0.5233 -0.0246 51   LEU D CG  
9247  C  CD1 . LEU D  53  ? 2.5291 1.8555 1.9284 0.1946  -0.5065 -0.0204 51   LEU D CD1 
9248  C  CD2 . LEU D  53  ? 2.3196 1.7483 1.7668 0.2006  -0.5341 -0.0443 51   LEU D CD2 
9249  N  N   . TYR D  54  ? 2.4529 1.7745 1.6771 0.1151  -0.5046 -0.0062 52   TYR D N   
9250  C  CA  . TYR D  54  ? 2.6176 1.9182 1.8057 0.1082  -0.4903 0.0017  52   TYR D CA  
9251  C  C   . TYR D  54  ? 2.8923 2.2385 2.0756 0.0830  -0.4976 -0.0005 52   TYR D C   
9252  O  O   . TYR D  54  ? 3.1387 2.5005 2.3150 0.0873  -0.4913 0.0057  52   TYR D O   
9253  C  CB  . TYR D  54  ? 2.6300 1.8430 1.7609 0.0924  -0.4650 0.0101  52   TYR D CB  
9254  C  CG  . TYR D  54  ? 2.7206 1.8907 1.8131 0.0910  -0.4420 0.0239  52   TYR D CG  
9255  C  CD1 . TYR D  54  ? 2.6835 1.8485 1.7848 0.1290  -0.4338 0.0366  52   TYR D CD1 
9256  C  CD2 . TYR D  54  ? 2.8380 1.9739 1.8868 0.0517  -0.4269 0.0253  52   TYR D CD2 
9257  C  CE1 . TYR D  54  ? 2.7898 1.9134 1.8542 0.1334  -0.4103 0.0565  52   TYR D CE1 
9258  C  CE2 . TYR D  54  ? 2.9348 2.0211 1.9490 0.0510  -0.4002 0.0421  52   TYR D CE2 
9259  C  CZ  . TYR D  54  ? 2.9367 2.0150 1.9572 0.0946  -0.3915 0.0607  52   TYR D CZ  
9260  O  OH  . TYR D  54  ? 3.0838 2.1112 2.0682 0.0997  -0.3628 0.0844  52   TYR D OH  
9261  N  N   . ASN D  55  ? 2.8853 2.2603 2.0736 0.0585  -0.5104 -0.0075 53   ASN D N   
9262  C  CA  . ASN D  55  ? 2.8894 2.3185 2.0803 0.0332  -0.5174 -0.0109 53   ASN D CA  
9263  C  C   . ASN D  55  ? 2.7252 2.2344 1.9704 0.0578  -0.5336 -0.0177 53   ASN D C   
9264  O  O   . ASN D  55  ? 2.5555 2.1087 1.8028 0.0461  -0.5329 -0.0183 53   ASN D O   
9265  C  CB  . ASN D  55  ? 3.1199 2.5682 2.3027 0.0020  -0.5284 -0.0165 53   ASN D CB  
9266  C  CG  . ASN D  55  ? 3.2900 2.6705 2.4128 -0.0352 -0.5107 -0.0179 53   ASN D CG  
9267  O  OD1 . ASN D  55  ? 3.0003 2.3083 2.0882 -0.0355 -0.4865 -0.0125 53   ASN D OD1 
9268  N  ND2 . ASN D  55  ? 4.0182 3.4235 3.1287 -0.0651 -0.5218 -0.0262 53   ASN D ND2 
9269  N  N   . SER D  56  ? 2.6904 2.2175 1.9801 0.0904  -0.5450 -0.0246 54   SER D N   
9270  C  CA  . SER D  56  ? 2.5416 2.1399 1.8846 0.1131  -0.5580 -0.0377 54   SER D CA  
9271  C  C   . SER D  56  ? 2.7113 2.3224 2.0566 0.1348  -0.5523 -0.0420 54   SER D C   
9272  O  O   . SER D  56  ? 2.8233 2.4981 2.1979 0.1463  -0.5593 -0.0547 54   SER D O   
9273  C  CB  . SER D  56  ? 2.4982 2.1069 1.8922 0.1359  -0.5691 -0.0459 54   SER D CB  
9274  O  OG  . SER D  56  ? 2.7866 2.3421 2.1787 0.1507  -0.5612 -0.0442 54   SER D OG  
9275  N  N   . THR D  57  ? 2.6907 2.2476 2.0039 0.1423  -0.5392 -0.0313 55   THR D N   
9276  C  CA  . THR D  57  ? 2.6713 2.2500 1.9827 0.1665  -0.5356 -0.0312 55   THR D CA  
9277  C  C   . THR D  57  ? 2.7097 2.2948 1.9784 0.1516  -0.5227 -0.0150 55   THR D C   
9278  O  O   . THR D  57  ? 2.9355 2.5739 2.2090 0.1680  -0.5244 -0.0175 55   THR D O   
9279  C  CB  . THR D  57  ? 2.4984 2.0249 1.7964 0.1858  -0.5260 -0.0222 55   THR D CB  
9280  O  OG1 . THR D  57  ? 2.5382 1.9858 1.7851 0.1647  -0.5074 -0.0024 55   THR D OG1 
9281  C  CG2 . THR D  57  ? 2.3623 1.8924 1.7108 0.2017  -0.5361 -0.0397 55   THR D CG2 
9282  N  N   . ARG D  58  ? 2.4219 1.9536 1.6482 0.1189  -0.5077 0.0005  56   ARG D N   
9283  C  CA  . ARG D  58  ? 2.5488 2.0766 1.7371 0.0960  -0.4900 0.0166  56   ARG D CA  
9284  C  C   . ARG D  58  ? 2.5306 2.1294 1.7419 0.0736  -0.4991 0.0055  56   ARG D C   
9285  O  O   . ARG D  58  ? 2.6463 2.2588 1.8353 0.0554  -0.4841 0.0171  56   ARG D O   
9286  C  CB  . ARG D  58  ? 2.6402 2.0764 1.7780 0.0654  -0.4668 0.0315  56   ARG D CB  
9287  C  CG  . ARG D  58  ? 2.6708 2.0352 1.7837 0.0913  -0.4518 0.0461  56   ARG D CG  
9288  C  CD  . ARG D  58  ? 2.8218 2.0924 1.8792 0.0649  -0.4194 0.0635  56   ARG D CD  
9289  N  NE  . ARG D  58  ? 2.8898 2.1278 1.9362 0.0234  -0.4194 0.0472  56   ARG D NE  
9290  C  CZ  . ARG D  58  ? 2.9835 2.2264 2.0157 -0.0235 -0.4130 0.0409  56   ARG D CZ  
9291  N  NH1 . ARG D  58  ? 3.0181 2.2909 2.0470 -0.0350 -0.4027 0.0518  56   ARG D NH1 
9292  N  NH2 . ARG D  58  ? 3.1156 2.3398 2.1371 -0.0596 -0.4167 0.0230  56   ARG D NH2 
9293  N  N   . ASP D  59  ? 2.6436 2.2882 1.9010 0.0763  -0.5208 -0.0142 57   ASP D N   
9294  C  CA  . ASP D  59  ? 2.6777 2.3907 1.9610 0.0563  -0.5294 -0.0234 57   ASP D CA  
9295  C  C   . ASP D  59  ? 2.6598 2.4522 1.9705 0.0761  -0.5322 -0.0326 57   ASP D C   
9296  O  O   . ASP D  59  ? 2.6144 2.4573 1.9291 0.0555  -0.5275 -0.0321 57   ASP D O   
9297  C  CB  . ASP D  59  ? 2.8449 2.5757 2.1672 0.0598  -0.5495 -0.0356 57   ASP D CB  
9298  C  CG  . ASP D  59  ? 3.1704 2.9639 2.5130 0.0348  -0.5582 -0.0397 57   ASP D CG  
9299  O  OD1 . ASP D  59  ? 3.4361 3.2738 2.7758 0.0173  -0.5500 -0.0386 57   ASP D OD1 
9300  O  OD2 . ASP D  59  ? 3.1565 2.9595 2.5186 0.0336  -0.5727 -0.0419 57   ASP D OD2 
9301  N  N   . ARG D  60  ? 2.8405 2.6501 2.1706 0.1138  -0.5388 -0.0437 58   ARG D N   
9302  C  CA  . ARG D  60  ? 2.9210 2.8127 2.2827 0.1347  -0.5444 -0.0623 58   ARG D CA  
9303  C  C   . ARG D  60  ? 3.0767 3.0008 2.4038 0.1248  -0.5272 -0.0479 58   ARG D C   
9304  O  O   . ARG D  60  ? 3.2092 3.1254 2.5034 0.1420  -0.5180 -0.0361 58   ARG D O   
9305  C  CB  . ARG D  60  ? 3.1406 3.0419 2.5255 0.1724  -0.5541 -0.0816 58   ARG D CB  
9306  C  CG  . ARG D  60  ? 3.1981 3.0460 2.5430 0.1843  -0.5465 -0.0640 58   ARG D CG  
9307  C  CD  . ARG D  60  ? 3.0589 2.9481 2.4282 0.2196  -0.5571 -0.0869 58   ARG D CD  
9308  N  NE  . ARG D  60  ? 2.9444 2.7954 2.2798 0.2354  -0.5512 -0.0675 58   ARG D NE  
9309  C  CZ  . ARG D  60  ? 2.7965 2.6734 2.1535 0.2636  -0.5616 -0.0849 58   ARG D CZ  
9310  N  NH1 . ARG D  60  ? 2.7831 2.7165 2.1950 0.2749  -0.5767 -0.1260 58   ARG D NH1 
9311  N  NH2 . ARG D  60  ? 2.6560 2.5034 1.9828 0.2802  -0.5556 -0.0627 58   ARG D NH2 
9312  N  N   . VAL D  61  ? 2.9973 2.9634 2.3326 0.0983  -0.5219 -0.0465 59   VAL D N   
9313  C  CA  . VAL D  61  ? 3.2264 3.2425 2.5419 0.0925  -0.5047 -0.0374 59   VAL D CA  
9314  C  C   . VAL D  61  ? 3.1728 3.2826 2.5325 0.1186  -0.5142 -0.0663 59   VAL D C   
9315  O  O   . VAL D  61  ? 3.2629 3.4223 2.6045 0.1270  -0.5017 -0.0638 59   VAL D O   
9316  C  CB  . VAL D  61  ? 3.2762 3.2902 2.5769 0.0449  -0.4882 -0.0208 59   VAL D CB  
9317  C  CG1 . VAL D  61  ? 3.3110 3.3601 2.5824 0.0362  -0.4626 -0.0032 59   VAL D CG1 
9318  C  CG2 . VAL D  61  ? 3.1852 3.1026 2.4484 0.0162  -0.4794 -0.0025 59   VAL D CG2 
9319  N  N   . ALA D  62  ? 2.8131 2.9454 2.2282 0.1337  -0.5332 -0.0931 60   ALA D N   
9320  C  CA  . ALA D  62  ? 2.6752 2.8868 2.1378 0.1595  -0.5392 -0.1253 60   ALA D CA  
9321  C  C   . ALA D  62  ? 2.5908 2.7890 2.0832 0.1929  -0.5535 -0.1535 60   ALA D C   
9322  O  O   . ALA D  62  ? 2.5558 2.6901 2.0512 0.1941  -0.5622 -0.1486 60   ALA D O   
9323  C  CB  . ALA D  62  ? 2.6357 2.8933 2.1487 0.1497  -0.5442 -0.1333 60   ALA D CB  
9324  N  N   . GLY D  63  ? 2.4125 2.6737 1.9273 0.2178  -0.5538 -0.1857 61   GLY D N   
9325  C  CA  . GLY D  63  ? 2.3700 2.6287 1.9185 0.2453  -0.5649 -0.2210 61   GLY D CA  
9326  C  C   . GLY D  63  ? 2.4987 2.7887 2.0142 0.2625  -0.5646 -0.2339 61   GLY D C   
9327  O  O   . GLY D  63  ? 2.6573 2.9387 2.1136 0.2560  -0.5569 -0.2020 61   GLY D O   
9328  N  N   . GLU D  64  ? 2.4259 2.7535 1.9797 0.2850  -0.5719 -0.2808 62   GLU D N   
9329  C  CA  . GLU D  64  ? 2.3888 2.7618 1.9153 0.3027  -0.5760 -0.3003 62   GLU D CA  
9330  C  C   . GLU D  64  ? 2.3175 2.6777 1.8881 0.3162  -0.5894 -0.3401 62   GLU D C   
9331  O  O   . GLU D  64  ? 2.2958 2.6323 1.9278 0.3166  -0.5907 -0.3669 62   GLU D O   
9332  C  CB  . GLU D  64  ? 2.6017 3.0666 2.1235 0.3132  -0.5679 -0.3287 62   GLU D CB  
9333  C  CG  . GLU D  64  ? 2.8344 3.3232 2.3082 0.2993  -0.5510 -0.2885 62   GLU D CG  
9334  C  CD  . GLU D  64  ? 2.9950 3.5791 2.4654 0.3111  -0.5403 -0.3178 62   GLU D CD  
9335  O  OE1 . GLU D  64  ? 3.0107 3.6372 2.5229 0.3286  -0.5458 -0.3739 62   GLU D OE1 
9336  O  OE2 . GLU D  64  ? 3.0267 3.6417 2.4530 0.3017  -0.5235 -0.2863 62   GLU D OE2 
9337  N  N   . PRO D  72  ? 2.4962 3.6194 2.0286 0.6268  -0.8079 -0.3352 70   PRO D N   
9338  C  CA  . PRO D  72  ? 2.5064 3.5215 2.1098 0.5908  -0.7926 -0.3547 70   PRO D CA  
9339  C  C   . PRO D  72  ? 2.7614 3.7096 2.3665 0.6142  -0.7788 -0.2936 70   PRO D C   
9340  O  O   . PRO D  72  ? 2.7161 3.5540 2.2637 0.6259  -0.7538 -0.2251 70   PRO D O   
9341  C  CB  . PRO D  72  ? 2.3526 3.2431 1.9302 0.5596  -0.7679 -0.3456 70   PRO D CB  
9342  C  CG  . PRO D  72  ? 2.3350 3.3049 1.8658 0.5641  -0.7775 -0.3658 70   PRO D CG  
9343  C  CD  . PRO D  72  ? 2.4581 3.5415 1.9346 0.6131  -0.7947 -0.3299 70   PRO D CD  
9344  N  N   . GLU D  73  ? 2.9310 3.9489 2.6055 0.6189  -0.7935 -0.3225 71   GLU D N   
9345  C  CA  . GLU D  73  ? 2.9052 3.8782 2.5888 0.6454  -0.7807 -0.2699 71   GLU D CA  
9346  C  C   . GLU D  73  ? 2.8065 3.6131 2.5068 0.6147  -0.7484 -0.2521 71   GLU D C   
9347  O  O   . GLU D  73  ? 2.8431 3.5632 2.5108 0.6368  -0.7263 -0.1895 71   GLU D O   
9348  C  CB  . GLU D  73  ? 2.8299 3.9341 2.5932 0.6546  -0.8049 -0.3120 71   GLU D CB  
9349  C  CG  . GLU D  73  ? 2.6479 3.7894 2.5047 0.6017  -0.8150 -0.4053 71   GLU D CG  
9350  C  CD  . GLU D  73  ? 2.4022 3.6323 2.3507 0.6006  -0.8269 -0.4398 71   GLU D CD  
9351  O  OE1 . GLU D  73  ? 2.3857 3.6485 2.3269 0.6437  -0.8279 -0.3895 71   GLU D OE1 
9352  O  OE2 . GLU D  73  ? 2.3128 3.5784 2.3442 0.5563  -0.8327 -0.5172 71   GLU D OE2 
9353  N  N   . ALA D  74  ? 2.7126 3.4734 2.4621 0.5659  -0.7438 -0.3059 72   ALA D N   
9354  C  CA  . ALA D  74  ? 2.7270 3.3426 2.4936 0.5367  -0.7154 -0.2921 72   ALA D CA  
9355  C  C   . ALA D  74  ? 2.8611 3.3601 2.5542 0.5277  -0.6952 -0.2494 72   ALA D C   
9356  O  O   . ALA D  74  ? 2.8969 3.2753 2.5866 0.5097  -0.6715 -0.2257 72   ALA D O   
9357  C  CB  . ALA D  74  ? 2.5804 3.1964 2.4338 0.4917  -0.7166 -0.3628 72   ALA D CB  
9358  N  N   . ASP D  75  ? 2.9238 3.4620 2.5584 0.5389  -0.7033 -0.2397 73   ASP D N   
9359  C  CA  . ASP D  75  ? 2.9970 3.4408 2.5690 0.5258  -0.6848 -0.2059 73   ASP D CA  
9360  C  C   . ASP D  75  ? 2.9325 3.3021 2.4314 0.5526  -0.6637 -0.1284 73   ASP D C   
9361  O  O   . ASP D  75  ? 2.8661 3.1451 2.3159 0.5370  -0.6441 -0.0977 73   ASP D O   
9362  C  CB  . ASP D  75  ? 3.1131 3.6347 2.6588 0.5236  -0.6989 -0.2328 73   ASP D CB  
9363  C  CG  . ASP D  75  ? 3.2051 3.6411 2.7080 0.5006  -0.6807 -0.2136 73   ASP D CG  
9364  O  OD1 . ASP D  75  ? 3.1806 3.5130 2.7017 0.4734  -0.6645 -0.2088 73   ASP D OD1 
9365  O  OD2 . ASP D  75  ? 3.2311 3.7102 2.6827 0.5099  -0.6825 -0.2030 73   ASP D OD2 
9366  N  N   . TYR D  76  ? 2.9646 3.3689 2.4591 0.5915  -0.6651 -0.0974 74   TYR D N   
9367  C  CA  . TYR D  76  ? 2.9706 3.2972 2.3996 0.6207  -0.6403 -0.0236 74   TYR D CA  
9368  C  C   . TYR D  76  ? 2.7226 2.9256 2.1650 0.6076  -0.6143 -0.0044 74   TYR D C   
9369  O  O   . TYR D  76  ? 2.7647 2.8634 2.1504 0.6128  -0.5862 0.0469  74   TYR D O   
9370  C  CB  . TYR D  76  ? 2.9954 3.4227 2.4099 0.6776  -0.6524 0.0067  74   TYR D CB  
9371  C  CG  . TYR D  76  ? 2.9407 3.2886 2.3140 0.7156  -0.6242 0.0783  74   TYR D CG  
9372  C  CD1 . TYR D  76  ? 2.8699 3.1458 2.1616 0.7320  -0.5989 0.1402  74   TYR D CD1 
9373  C  CD2 . TYR D  76  ? 2.8638 3.2084 2.2827 0.7354  -0.6196 0.0832  74   TYR D CD2 
9374  C  CE1 . TYR D  76  ? 2.8192 3.0135 2.0751 0.7674  -0.5685 0.2038  74   TYR D CE1 
9375  C  CE2 . TYR D  76  ? 2.8457 3.1149 2.2288 0.7734  -0.5905 0.1467  74   TYR D CE2 
9376  C  CZ  . TYR D  76  ? 2.7847 2.9752 2.0859 0.7896  -0.5645 0.2062  74   TYR D CZ  
9377  O  OH  . TYR D  76  ? 2.7023 2.8078 1.9695 0.8277  -0.5309 0.2679  74   TYR D OH  
9378  N  N   . TYR D  77  ? 2.4287 2.6392 1.9437 0.5884  -0.6204 -0.0461 75   TYR D N   
9379  C  CA  . TYR D  77  ? 2.4763 2.5780 2.0043 0.5756  -0.5954 -0.0313 75   TYR D CA  
9380  C  C   . TYR D  77  ? 2.3859 2.3801 1.8938 0.5303  -0.5804 -0.0365 75   TYR D C   
9381  O  O   . TYR D  77  ? 2.3657 2.3727 1.8582 0.5094  -0.5895 -0.0530 75   TYR D O   
9382  C  CB  . TYR D  77  ? 2.6664 2.8228 2.2804 0.5723  -0.6048 -0.0709 75   TYR D CB  
9383  C  CG  . TYR D  77  ? 2.6784 2.9381 2.3159 0.6191  -0.6168 -0.0601 75   TYR D CG  
9384  C  CD1 . TYR D  77  ? 2.6625 2.8776 2.2904 0.6516  -0.5950 -0.0159 75   TYR D CD1 
9385  C  CD2 . TYR D  77  ? 2.5882 2.9959 2.2574 0.6322  -0.6498 -0.0953 75   TYR D CD2 
9386  C  CE1 . TYR D  77  ? 2.7241 3.0427 2.3778 0.6992  -0.6064 -0.0031 75   TYR D CE1 
9387  C  CE2 . TYR D  77  ? 2.5974 3.1149 2.2896 0.6766  -0.6641 -0.0852 75   TYR D CE2 
9388  C  CZ  . TYR D  77  ? 2.6903 3.1647 2.3765 0.7117  -0.6427 -0.0368 75   TYR D CZ  
9389  O  OH  . TYR D  77  ? 2.5923 3.1853 2.3055 0.7606  -0.6577 -0.0242 75   TYR D OH  
9390  N  N   . ALA D  78  ? 2.3052 2.1979 1.8124 0.5167  -0.5569 -0.0218 76   ALA D N   
9391  C  CA  . ALA D  78  ? 2.4290 2.2223 1.9122 0.4771  -0.5424 -0.0214 76   ALA D CA  
9392  C  C   . ALA D  78  ? 2.4779 2.2891 2.0242 0.4444  -0.5544 -0.0697 76   ALA D C   
9393  O  O   . ALA D  78  ? 2.4927 2.3597 2.1058 0.4473  -0.5636 -0.1008 76   ALA D O   
9394  C  CB  . ALA D  78  ? 2.5172 2.1986 1.9685 0.4761  -0.5117 0.0117  76   ALA D CB  
9395  N  N   . LYS D  79  ? 2.3760 2.1372 1.9030 0.4130  -0.5516 -0.0742 77   LYS D N   
9396  C  CA  . LYS D  79  ? 2.1866 1.9519 1.7671 0.3849  -0.5589 -0.1123 77   LYS D CA  
9397  C  C   . LYS D  79  ? 2.1794 1.8437 1.7367 0.3598  -0.5405 -0.0945 77   LYS D C   
9398  O  O   . LYS D  79  ? 2.1815 1.7944 1.6795 0.3490  -0.5323 -0.0692 77   LYS D O   
9399  C  CB  . LYS D  79  ? 2.1348 1.9578 1.7209 0.3755  -0.5766 -0.1388 77   LYS D CB  
9400  C  CG  . LYS D  79  ? 2.1770 2.1037 1.7653 0.4006  -0.5950 -0.1530 77   LYS D CG  
9401  C  CD  . LYS D  79  ? 2.2416 2.2423 1.9015 0.4103  -0.6071 -0.1909 77   LYS D CD  
9402  C  CE  . LYS D  79  ? 2.1512 2.2702 1.8114 0.4351  -0.6291 -0.2088 77   LYS D CE  
9403  N  NZ  . LYS D  79  ? 2.0859 2.2882 1.8204 0.4407  -0.6424 -0.2507 77   LYS D NZ  
9404  N  N   . GLU D  80  ? 2.3617 2.0027 1.9661 0.3490  -0.5333 -0.1085 78   GLU D N   
9405  C  CA  . GLU D  80  ? 2.4561 2.0113 2.0387 0.3275  -0.5169 -0.0920 78   GLU D CA  
9406  C  C   . GLU D  80  ? 2.3579 1.9122 1.9448 0.3055  -0.5262 -0.1039 78   GLU D C   
9407  O  O   . GLU D  80  ? 2.3256 1.9184 1.9722 0.3012  -0.5349 -0.1339 78   GLU D O   
9408  C  CB  . GLU D  80  ? 2.4470 1.9820 2.0774 0.3263  -0.5032 -0.0988 78   GLU D CB  
9409  C  CG  . GLU D  80  ? 2.4931 1.9461 2.0964 0.3066  -0.4858 -0.0803 78   GLU D CG  
9410  C  CD  . GLU D  80  ? 2.5123 1.9447 2.1573 0.3072  -0.4676 -0.0820 78   GLU D CD  
9411  O  OE1 . GLU D  80  ? 2.4533 1.9296 2.1429 0.3234  -0.4662 -0.0941 78   GLU D OE1 
9412  O  OE2 . GLU D  80  ? 2.5962 1.9747 2.2297 0.2919  -0.4544 -0.0704 78   GLU D OE2 
9413  N  N   . VAL D  81  ? 2.4196 1.9309 1.9469 0.2916  -0.5226 -0.0815 79   VAL D N   
9414  C  CA  . VAL D  81  ? 2.3961 1.9160 1.9242 0.2736  -0.5321 -0.0885 79   VAL D CA  
9415  C  C   . VAL D  81  ? 2.5642 2.0329 2.0978 0.2578  -0.5236 -0.0804 79   VAL D C   
9416  O  O   . VAL D  81  ? 2.7235 2.1330 2.2108 0.2484  -0.5102 -0.0578 79   VAL D O   
9417  C  CB  . VAL D  81  ? 2.5298 2.0429 1.9955 0.2642  -0.5329 -0.0700 79   VAL D CB  
9418  C  CG1 . VAL D  81  ? 2.5878 2.1185 2.0599 0.2461  -0.5424 -0.0769 79   VAL D CG1 
9419  C  CG2 . VAL D  81  ? 2.6637 2.2301 2.1203 0.2836  -0.5393 -0.0723 79   VAL D CG2 
9420  N  N   . THR D  82  ? 2.4968 1.9881 2.0855 0.2561  -0.5295 -0.0988 80   THR D N   
9421  C  CA  . THR D  82  ? 2.4856 1.9380 2.0815 0.2458  -0.5226 -0.0868 80   THR D CA  
9422  C  C   . THR D  82  ? 2.4476 1.9340 2.0717 0.2435  -0.5343 -0.0973 80   THR D C   
9423  O  O   . THR D  82  ? 2.5023 2.0410 2.1594 0.2509  -0.5444 -0.1231 80   THR D O   
9424  C  CB  . THR D  82  ? 2.4230 1.8547 2.0694 0.2518  -0.5083 -0.0921 80   THR D CB  
9425  O  OG1 . THR D  82  ? 2.3513 1.8332 2.0665 0.2612  -0.5135 -0.1264 80   THR D OG1 
9426  C  CG2 . THR D  82  ? 2.5768 1.9695 2.1904 0.2544  -0.4929 -0.0761 80   THR D CG2 
9427  N  N   . ARG D  83  ? 2.3796 1.8413 1.9888 0.2352  -0.5328 -0.0772 81   ARG D N   
9428  C  CA  . ARG D  83  ? 2.3517 1.8461 1.9892 0.2376  -0.5423 -0.0817 81   ARG D CA  
9429  C  C   . ARG D  83  ? 2.4788 1.9442 2.1493 0.2441  -0.5326 -0.0671 81   ARG D C   
9430  O  O   . ARG D  83  ? 2.5967 2.0162 2.2506 0.2414  -0.5197 -0.0482 81   ARG D O   
9431  C  CB  . ARG D  83  ? 2.3063 1.8186 1.8908 0.2232  -0.5534 -0.0669 81   ARG D CB  
9432  C  CG  . ARG D  83  ? 2.3251 1.8037 1.8650 0.2099  -0.5512 -0.0378 81   ARG D CG  
9433  C  CD  . ARG D  83  ? 2.3909 1.9016 1.8917 0.1918  -0.5636 -0.0299 81   ARG D CD  
9434  N  NE  . ARG D  83  ? 2.4618 1.9584 1.9278 0.1797  -0.5656 -0.0068 81   ARG D NE  
9435  C  CZ  . ARG D  83  ? 2.4804 2.0102 1.9151 0.1603  -0.5771 0.0001  81   ARG D CZ  
9436  N  NH1 . ARG D  83  ? 2.4079 1.9811 1.8435 0.1502  -0.5846 -0.0119 81   ARG D NH1 
9437  N  NH2 . ARG D  83  ? 2.5559 2.0818 1.9584 0.1501  -0.5809 0.0185  81   ARG D NH2 
9438  N  N   . VAL D  84  ? 2.4659 1.9577 2.1833 0.2551  -0.5361 -0.0744 82   VAL D N   
9439  C  CA  . VAL D  84  ? 2.4324 1.8980 2.1838 0.2668  -0.5250 -0.0548 82   VAL D CA  
9440  C  C   . VAL D  84  ? 2.4124 1.9164 2.1718 0.2760  -0.5364 -0.0454 82   VAL D C   
9441  O  O   . VAL D  84  ? 2.3649 1.9128 2.1538 0.2817  -0.5438 -0.0714 82   VAL D O   
9442  C  CB  . VAL D  84  ? 2.4410 1.8875 2.2700 0.2778  -0.5072 -0.0773 82   VAL D CB  
9443  C  CG1 . VAL D  84  ? 2.3934 1.7970 2.2191 0.2705  -0.4911 -0.0723 82   VAL D CG1 
9444  C  CG2 . VAL D  84  ? 2.5324 2.0247 2.4030 0.2799  -0.5143 -0.1239 82   VAL D CG2 
9445  N  N   . LEU D  85  ? 2.3816 1.8763 2.1135 0.2786  -0.5378 -0.0084 83   LEU D N   
9446  C  CA  . LEU D  85  ? 2.3039 1.8425 2.0476 0.2915  -0.5488 0.0060  83   LEU D CA  
9447  C  C   . LEU D  85  ? 2.3100 1.8380 2.1318 0.3207  -0.5337 0.0040  83   LEU D C   
9448  O  O   . LEU D  85  ? 2.3347 1.8153 2.1972 0.3263  -0.5134 -0.0051 83   LEU D O   
9449  C  CB  . LEU D  85  ? 2.2675 1.8095 1.9552 0.2859  -0.5572 0.0460  83   LEU D CB  
9450  C  CG  . LEU D  85  ? 2.2390 1.7861 1.8495 0.2534  -0.5688 0.0444  83   LEU D CG  
9451  C  CD1 . LEU D  85  ? 2.4518 2.0010 2.0083 0.2460  -0.5751 0.0779  83   LEU D CD1 
9452  C  CD2 . LEU D  85  ? 2.2000 1.8034 1.8037 0.2396  -0.5844 0.0233  83   LEU D CD2 
9453  N  N   . MET D  86  ? 2.3817 1.9541 2.2283 0.3393  -0.5412 0.0120  84   MET D N   
9454  C  CA  . MET D  86  ? 2.4264 1.9855 2.3494 0.3701  -0.5235 0.0089  84   MET D CA  
9455  C  C   . MET D  86  ? 2.4802 2.0090 2.4079 0.3939  -0.5121 0.0606  84   MET D C   
9456  O  O   . MET D  86  ? 2.4258 1.9535 2.2945 0.3860  -0.5207 0.0966  84   MET D O   
9457  C  CB  . MET D  86  ? 2.5188 2.1415 2.4749 0.3841  -0.5327 -0.0116 84   MET D CB  
9458  C  CG  . MET D  86  ? 2.4952 2.1803 2.4235 0.3919  -0.5522 0.0216  84   MET D CG  
9459  S  SD  . MET D  86  ? 2.4181 2.1714 2.4090 0.4204  -0.5529 0.0021  84   MET D SD  
9460  C  CE  . MET D  86  ? 2.4445 2.2770 2.3994 0.4256  -0.5778 0.0485  84   MET D CE  
9461  N  N   . VAL D  87  ? 2.6685 2.1708 2.6666 0.4244  -0.4901 0.0639  85   VAL D N   
9462  C  CA  . VAL D  87  ? 2.6793 2.1528 2.6907 0.4559  -0.4749 0.1181  85   VAL D CA  
9463  C  C   . VAL D  87  ? 2.7298 2.2742 2.7402 0.4827  -0.4931 0.1452  85   VAL D C   
9464  O  O   . VAL D  87  ? 2.7426 2.3329 2.7891 0.4913  -0.4993 0.1159  85   VAL D O   
9465  C  CB  . VAL D  87  ? 2.7163 2.1175 2.8089 0.4763  -0.4364 0.1101  85   VAL D CB  
9466  C  CG1 . VAL D  87  ? 2.8771 2.2384 2.9775 0.5103  -0.4158 0.1749  85   VAL D CG1 
9467  C  CG2 . VAL D  87  ? 2.7016 2.0515 2.8040 0.4450  -0.4215 0.0730  85   VAL D CG2 
9468  N  N   . GLU D  88  ? 2.8575 2.4185 2.8269 0.4968  -0.5014 0.2008  86   GLU D N   
9469  C  CA  . GLU D  88  ? 2.9608 2.6032 2.9282 0.5229  -0.5219 0.2307  86   GLU D CA  
9470  C  C   . GLU D  88  ? 3.1029 2.7327 3.1522 0.5746  -0.4986 0.2472  86   GLU D C   
9471  O  O   . GLU D  88  ? 3.2143 2.7626 3.3177 0.5887  -0.4640 0.2400  86   GLU D O   
9472  C  CB  . GLU D  88  ? 3.1205 2.7903 3.0191 0.5239  -0.5381 0.2842  86   GLU D CB  
9473  C  CG  . GLU D  88  ? 3.1268 2.7813 2.9475 0.4756  -0.5499 0.2690  86   GLU D CG  
9474  C  CD  . GLU D  88  ? 3.3020 2.9539 3.0597 0.4793  -0.5531 0.3195  86   GLU D CD  
9475  O  OE1 . GLU D  88  ? 3.2934 2.9653 3.0648 0.5208  -0.5497 0.3705  86   GLU D OE1 
9476  O  OE2 . GLU D  88  ? 3.4020 3.0315 3.0954 0.4433  -0.5571 0.3093  86   GLU D OE2 
9477  N  N   . THR D  89  ? 3.0231 2.7358 3.0841 0.6030  -0.5160 0.2692  87   THR D N   
9478  C  CA  . THR D  89  ? 2.9587 2.6686 3.0942 0.6599  -0.4947 0.2935  87   THR D CA  
9479  C  C   . THR D  89  ? 2.9833 2.6625 3.1151 0.7021  -0.4798 0.3677  87   THR D C   
9480  O  O   . THR D  89  ? 2.9889 2.6664 3.1787 0.7566  -0.4611 0.4006  87   THR D O   
9481  C  CB  . THR D  89  ? 2.9124 2.7346 3.0658 0.6769  -0.5190 0.2891  87   THR D CB  
9482  O  OG1 . THR D  89  ? 2.8586 2.7696 2.9405 0.6527  -0.5583 0.3093  87   THR D OG1 
9483  C  CG2 . THR D  89  ? 2.9177 2.7539 3.1032 0.6540  -0.5177 0.2186  87   THR D CG2 
9484  N  N   . HIS D  90  ? 3.1967 2.8512 3.2613 0.6810  -0.4851 0.3964  88   HIS D N   
9485  C  CA  . HIS D  90  ? 3.4547 3.0891 3.5003 0.7188  -0.4730 0.4713  88   HIS D CA  
9486  C  C   . HIS D  90  ? 3.4988 3.0076 3.5896 0.7363  -0.4225 0.4878  88   HIS D C   
9487  O  O   . HIS D  90  ? 3.6147 3.0951 3.6926 0.7707  -0.4050 0.5551  88   HIS D O   
9488  C  CB  . HIS D  90  ? 3.4855 3.1598 3.4314 0.6870  -0.5015 0.4931  88   HIS D CB  
9489  C  CG  . HIS D  90  ? 3.4482 3.2409 3.3488 0.6613  -0.5483 0.4734  88   HIS D CG  
9490  N  ND1 . HIS D  90  ? 3.2817 3.0952 3.1766 0.6141  -0.5644 0.4080  88   HIS D ND1 
9491  C  CD2 . HIS D  90  ? 3.5011 3.4005 3.3614 0.6745  -0.5811 0.5103  88   HIS D CD2 
9492  C  CE1 . HIS D  90  ? 3.2794 3.1996 3.1352 0.5969  -0.6019 0.4053  88   HIS D CE1 
9493  N  NE2 . HIS D  90  ? 3.4556 3.4336 3.2912 0.6311  -0.6142 0.4637  88   HIS D NE2 
9494  N  N   . ASN D  91  ? 3.3359 2.7729 3.4800 0.7135  -0.3974 0.4292  89   ASN D N   
9495  C  CA  . ASN D  91  ? 3.3788 2.6974 3.5691 0.7212  -0.3478 0.4391  89   ASN D CA  
9496  C  C   . ASN D  91  ? 3.1615 2.4207 3.4513 0.7349  -0.3127 0.3947  89   ASN D C   
9497  O  O   . ASN D  91  ? 3.1128 2.3027 3.4607 0.7764  -0.2713 0.4303  89   ASN D O   
9498  C  CB  . ASN D  91  ? 3.3908 2.6637 3.5387 0.6670  -0.3452 0.4101  89   ASN D CB  
9499  C  CG  . ASN D  91  ? 3.4594 2.7579 3.5151 0.6588  -0.3629 0.4610  89   ASN D CG  
9500  O  OD1 . ASN D  91  ? 3.6727 2.9885 3.7063 0.6987  -0.3609 0.5302  89   ASN D OD1 
9501  N  ND2 . ASN D  91  ? 3.2744 2.5775 3.2742 0.6089  -0.3794 0.4268  89   ASN D ND2 
9502  N  N   . GLU D  92  ? 2.9711 2.2551 3.2806 0.7016  -0.3262 0.3176  90   GLU D N   
9503  C  CA  . GLU D  92  ? 3.0026 2.2329 3.4014 0.7076  -0.2932 0.2643  90   GLU D CA  
9504  C  C   . GLU D  92  ? 3.0080 2.3114 3.4365 0.7205  -0.3108 0.2224  90   GLU D C   
9505  O  O   . GLU D  92  ? 3.0417 2.3038 3.5480 0.7406  -0.2793 0.1894  90   GLU D O   
9506  C  CB  . GLU D  92  ? 3.0595 2.2385 3.4693 0.6539  -0.2820 0.1986  90   GLU D CB  
9507  C  CG  . GLU D  92  ? 3.2943 2.3944 3.6913 0.6387  -0.2560 0.2306  90   GLU D CG  
9508  C  CD  . GLU D  92  ? 3.3724 2.4448 3.7786 0.5853  -0.2516 0.1654  90   GLU D CD  
9509  O  OE1 . GLU D  92  ? 3.2832 2.4051 3.6935 0.5610  -0.2740 0.0997  90   GLU D OE1 
9510  O  OE2 . GLU D  92  ? 3.4673 2.4742 3.8769 0.5689  -0.2253 0.1815  90   GLU D OE2 
9511  N  N   . ILE D  93  ? 3.1613 2.5702 3.5328 0.7086  -0.3567 0.2209  91   ILE D N   
9512  C  CA  . ILE D  93  ? 3.2715 2.7530 3.6699 0.7131  -0.3715 0.1741  91   ILE D CA  
9513  C  C   . ILE D  93  ? 3.2357 2.7558 3.6793 0.7747  -0.3639 0.2142  91   ILE D C   
9514  O  O   . ILE D  93  ? 3.2346 2.8056 3.7165 0.7875  -0.3660 0.1768  91   ILE D O   
9515  C  CB  . ILE D  93  ? 3.1909 2.7654 3.5146 0.6706  -0.4187 0.1533  91   ILE D CB  
9516  C  CG1 . ILE D  93  ? 3.0766 2.6087 3.3513 0.6176  -0.4244 0.1276  91   ILE D CG1 
9517  C  CG2 . ILE D  93  ? 3.0226 2.6621 3.3717 0.6641  -0.4288 0.0945  91   ILE D CG2 
9518  C  CD1 . ILE D  93  ? 2.8620 2.4657 3.0752 0.5747  -0.4611 0.0949  91   ILE D CD1 
9519  N  N   . TYR D  94  ? 3.3331 2.8295 3.7767 0.8170  -0.3517 0.2903  92   TYR D N   
9520  C  CA  . TYR D  94  ? 3.4761 3.0109 3.9654 0.8833  -0.3431 0.3367  92   TYR D CA  
9521  C  C   . TYR D  94  ? 3.5897 3.0108 4.1595 0.9300  -0.2855 0.3557  92   TYR D C   
9522  O  O   . TYR D  94  ? 3.6976 3.1362 4.3199 0.9911  -0.2695 0.3879  92   TYR D O   
9523  C  CB  . TYR D  94  ? 3.5815 3.1954 4.0108 0.9067  -0.3751 0.4168  92   TYR D CB  
9524  C  CG  . TYR D  94  ? 3.7025 3.2415 4.1032 0.9210  -0.3555 0.4836  92   TYR D CG  
9525  C  CD1 . TYR D  94  ? 3.6557 3.1581 3.9905 0.8688  -0.3642 0.4766  92   TYR D CD1 
9526  C  CD2 . TYR D  94  ? 3.7421 3.2514 4.1799 0.9900  -0.3271 0.5580  92   TYR D CD2 
9527  C  CE1 . TYR D  94  ? 3.7141 3.1522 4.0207 0.8816  -0.3438 0.5380  92   TYR D CE1 
9528  C  CE2 . TYR D  94  ? 3.7560 3.1988 4.1635 1.0045  -0.3066 0.6240  92   TYR D CE2 
9529  C  CZ  . TYR D  94  ? 3.7701 3.1791 4.1114 0.9485  -0.3150 0.6123  92   TYR D CZ  
9530  O  OH  . TYR D  94  ? 3.8415 3.1876 4.1509 0.9625  -0.2920 0.6777  92   TYR D OH  
9531  N  N   . ASP D  95  ? 3.6842 2.9899 4.2690 0.9029  -0.2515 0.3362  93   ASP D N   
9532  C  CA  . ASP D  95  ? 3.8982 3.0830 4.5565 0.9417  -0.1917 0.3604  93   ASP D CA  
9533  C  C   . ASP D  95  ? 3.8564 3.0025 4.6057 0.9583  -0.1570 0.2968  93   ASP D C   
9534  O  O   . ASP D  95  ? 3.9784 3.0374 4.7972 1.0055  -0.1062 0.3229  93   ASP D O   
9535  C  CB  . ASP D  95  ? 3.8795 2.9604 4.5269 0.8995  -0.1659 0.3551  93   ASP D CB  
9536  C  CG  . ASP D  95  ? 3.8514 2.8044 4.5622 0.9387  -0.1023 0.4015  93   ASP D CG  
9537  O  OD1 . ASP D  95  ? 3.8664 2.8147 4.6114 1.0061  -0.0828 0.4605  93   ASP D OD1 
9538  O  OD2 . ASP D  95  ? 3.7171 2.5748 4.4453 0.9023  -0.0700 0.3811  93   ASP D OD2 
9539  N  N   . LYS D  96  ? 3.6389 2.8457 4.3882 0.9229  -0.1802 0.2155  94   LYS D N   
9540  C  CA  . LYS D  96  ? 3.7409 2.9133 4.5707 0.9333  -0.1467 0.1452  94   LYS D CA  
9541  C  C   . LYS D  96  ? 3.7153 3.0009 4.5524 0.9573  -0.1715 0.1225  94   LYS D C   
9542  O  O   . LYS D  96  ? 3.8732 3.1400 4.7813 1.0064  -0.1385 0.1150  94   LYS D O   
9543  C  CB  . LYS D  96  ? 3.7304 2.8595 4.5670 0.8666  -0.1402 0.0528  94   LYS D CB  
9544  C  CG  . LYS D  96  ? 3.7861 2.8846 4.6999 0.8694  -0.1068 -0.0319 94   LYS D CG  
9545  C  CD  . LYS D  96  ? 3.6819 2.7517 4.5992 0.8026  -0.1044 -0.1224 94   LYS D CD  
9546  C  CE  . LYS D  96  ? 3.5875 2.6539 4.5679 0.8014  -0.0801 -0.2153 94   LYS D CE  
9547  N  NZ  . LYS D  96  ? 3.6935 2.6586 4.7646 0.8508  -0.0184 -0.2081 94   LYS D NZ  
9548  N  N   . PHE D  97  ? 3.4447 2.8439 4.2134 0.9244  -0.2248 0.1116  95   PHE D N   
9549  C  CA  . PHE D  97  ? 3.3740 2.8837 4.1493 0.9354  -0.2467 0.0793  95   PHE D CA  
9550  C  C   . PHE D  97  ? 3.3186 2.9551 4.0340 0.9421  -0.2965 0.1339  95   PHE D C   
9551  O  O   . PHE D  97  ? 3.3200 3.0436 4.0619 0.9797  -0.3040 0.1432  95   PHE D O   
9552  C  CB  . PHE D  97  ? 3.3200 2.8500 4.0808 0.8774  -0.2578 -0.0153 95   PHE D CB  
9553  C  CG  . PHE D  97  ? 3.3081 2.7891 4.0199 0.8168  -0.2687 -0.0364 95   PHE D CG  
9554  C  CD1 . PHE D  97  ? 3.2226 2.7525 3.8514 0.7853  -0.3104 0.0007  95   PHE D CD1 
9555  C  CD2 . PHE D  97  ? 3.2795 2.6695 4.0312 0.7907  -0.2361 -0.0969 95   PHE D CD2 
9556  C  CE1 . PHE D  97  ? 3.1637 2.6496 3.7507 0.7341  -0.3179 -0.0177 95   PHE D CE1 
9557  C  CE2 . PHE D  97  ? 3.1319 2.4872 3.8443 0.7375  -0.2464 -0.1156 95   PHE D CE2 
9558  C  CZ  . PHE D  97  ? 3.1144 2.5166 3.7446 0.7117  -0.2866 -0.0741 95   PHE D CZ  
9559  N  N   . LYS D  98  ? 3.1942 2.8466 3.8318 0.9040  -0.3293 0.1650  96   LYS D N   
9560  C  CA  . LYS D  98  ? 3.1124 2.8855 3.6854 0.8942  -0.3788 0.2025  96   LYS D CA  
9561  C  C   . LYS D  98  ? 3.0207 2.8856 3.5764 0.8572  -0.4049 0.1407  96   LYS D C   
9562  O  O   . LYS D  98  ? 2.8868 2.7154 3.4438 0.8193  -0.3961 0.0729  96   LYS D O   
9563  C  CB  . LYS D  98  ? 3.0449 2.8805 3.6428 0.9612  -0.3818 0.2770  96   LYS D CB  
9564  C  CG  . LYS D  98  ? 2.9723 2.7281 3.5735 1.0003  -0.3591 0.3518  96   LYS D CG  
9565  C  CD  . LYS D  98  ? 2.8626 2.7110 3.4632 1.0595  -0.3771 0.4332  96   LYS D CD  
9566  C  CE  . LYS D  98  ? 2.8324 2.7058 3.5218 1.1282  -0.3509 0.4386  96   LYS D CE  
9567  N  NZ  . LYS D  98  ? 2.8814 2.6114 3.6418 1.1724  -0.2891 0.4487  96   LYS D NZ  
9568  N  N   . GLN D  99  ? 3.0306 3.0191 3.5697 0.8670  -0.4365 0.1642  97   GLN D N   
9569  C  CA  . GLN D  99  ? 2.9539 3.0371 3.4724 0.8307  -0.4605 0.1152  97   GLN D CA  
9570  C  C   . GLN D  99  ? 3.0286 3.1927 3.6137 0.8791  -0.4505 0.1108  97   GLN D C   
9571  O  O   . GLN D  99  ? 3.0783 3.2806 3.6982 0.9344  -0.4485 0.1672  97   GLN D O   
9572  C  CB  . GLN D  99  ? 2.8906 3.0554 3.3284 0.7870  -0.5063 0.1395  97   GLN D CB  
9573  C  CG  . GLN D  99  ? 2.7497 3.0050 3.1603 0.7431  -0.5285 0.0938  97   GLN D CG  
9574  C  CD  . GLN D  99  ? 2.7494 3.1381 3.1898 0.7692  -0.5437 0.1128  97   GLN D CD  
9575  O  OE1 . GLN D  99  ? 2.8158 3.2586 3.2920 0.7735  -0.5348 0.0735  97   GLN D OE1 
9576  N  NE2 . GLN D  99  ? 2.6970 3.1469 3.1232 0.7870  -0.5667 0.1726  97   GLN D NE2 
9577  N  N   . SER D  100 ? 3.0501 3.2442 3.6524 0.8611  -0.4433 0.0452  98   SER D N   
9578  C  CA  . SER D  100 ? 2.9969 3.2726 3.6616 0.9036  -0.4311 0.0331  98   SER D CA  
9579  C  C   . SER D  100 ? 2.9129 3.2704 3.5520 0.8595  -0.4454 -0.0240 98   SER D C   
9580  O  O   . SER D  100 ? 2.8722 3.2043 3.4532 0.8020  -0.4578 -0.0592 98   SER D O   
9581  C  CB  . SER D  100 ? 2.9523 3.1398 3.6986 0.9548  -0.3807 0.0093  98   SER D CB  
9582  O  OG  . SER D  100 ? 2.9672 3.0797 3.7413 1.0013  -0.3626 0.0704  98   SER D OG  
9583  N  N   . THR D  101 ? 2.8850 3.3447 3.5694 0.8900  -0.4415 -0.0295 99   THR D N   
9584  C  CA  . THR D  101 ? 2.8160 3.3637 3.4819 0.8541  -0.4501 -0.0780 99   THR D CA  
9585  C  C   . THR D  101 ? 2.8211 3.3034 3.4892 0.8351  -0.4236 -0.1536 99   THR D C   
9586  O  O   . THR D  101 ? 2.8741 3.4169 3.5135 0.8002  -0.4296 -0.1953 99   THR D O   
9587  C  CB  . THR D  101 ? 2.9194 3.5904 3.6453 0.8981  -0.4455 -0.0662 99   THR D CB  
9588  O  OG1 . THR D  101 ? 3.0834 3.7073 3.8891 0.9603  -0.4028 -0.0849 99   THR D OG1 
9589  C  CG2 . THR D  101 ? 2.9094 3.6599 3.6371 0.9196  -0.4745 0.0081  99   THR D CG2 
9590  N  N   . HIS D  102 ? 2.8539 3.2176 3.5545 0.8558  -0.3937 -0.1722 100  HIS D N   
9591  C  CA  . HIS D  102 ? 2.9715 3.2775 3.6828 0.8408  -0.3670 -0.2495 100  HIS D CA  
9592  C  C   . HIS D  102 ? 3.0815 3.3226 3.7272 0.7819  -0.3823 -0.2731 100  HIS D C   
9593  O  O   . HIS D  102 ? 3.0794 3.3244 3.7045 0.7515  -0.3780 -0.3359 100  HIS D O   
9594  C  CB  . HIS D  102 ? 2.9770 3.1903 3.7695 0.8937  -0.3213 -0.2644 100  HIS D CB  
9595  C  CG  . HIS D  102 ? 3.0034 3.1708 3.8191 0.8831  -0.2901 -0.3524 100  HIS D CG  
9596  N  ND1 . HIS D  102 ? 3.0046 3.0655 3.8860 0.9134  -0.2461 -0.3822 100  HIS D ND1 
9597  C  CD2 . HIS D  102 ? 2.9821 3.1985 3.7635 0.8454  -0.2954 -0.4180 100  HIS D CD2 
9598  C  CE1 . HIS D  102 ? 2.9898 3.0398 3.8766 0.8917  -0.2277 -0.4681 100  HIS D CE1 
9599  N  NE2 . HIS D  102 ? 2.9749 3.1216 3.7991 0.8525  -0.2582 -0.4894 100  HIS D NE2 
9600  N  N   . SER D  103 ? 3.1400 3.3296 3.7507 0.7667  -0.4004 -0.2235 101  SER D N   
9601  C  CA  . SER D  103 ? 3.0671 3.1933 3.6215 0.7157  -0.4123 -0.2426 101  SER D CA  
9602  C  C   . SER D  103 ? 3.0070 3.1250 3.5065 0.6961  -0.4416 -0.1780 101  SER D C   
9603  O  O   . SER D  103 ? 2.9502 3.0946 3.4616 0.7259  -0.4491 -0.1192 101  SER D O   
9604  C  CB  . SER D  103 ? 3.1702 3.1818 3.7683 0.7227  -0.3789 -0.2812 101  SER D CB  
9605  O  OG  . SER D  103 ? 3.3098 3.2560 3.9633 0.7693  -0.3550 -0.2378 101  SER D OG  
9606  N  N   . ILE D  104 ? 3.0897 3.1755 3.5279 0.6468  -0.4579 -0.1909 102  ILE D N   
9607  C  CA  . ILE D  104 ? 3.0598 3.1238 3.4399 0.6223  -0.4818 -0.1406 102  ILE D CA  
9608  C  C   . ILE D  104 ? 2.9949 2.9590 3.3607 0.5979  -0.4722 -0.1604 102  ILE D C   
9609  O  O   . ILE D  104 ? 3.0553 3.0109 3.4099 0.5709  -0.4695 -0.2144 102  ILE D O   
9610  C  CB  . ILE D  104 ? 2.9331 3.0791 3.2435 0.5814  -0.5146 -0.1323 102  ILE D CB  
9611  C  CG1 . ILE D  104 ? 3.0575 3.3037 3.3826 0.6030  -0.5277 -0.0966 102  ILE D CG1 
9612  C  CG2 . ILE D  104 ? 2.7967 2.8978 3.0394 0.5445  -0.5336 -0.1045 102  ILE D CG2 
9613  C  CD1 . ILE D  104 ? 3.0775 3.4054 3.3424 0.5593  -0.5557 -0.0901 102  ILE D CD1 
9614  N  N   . TYR D  105 ? 2.8450 2.7410 3.2108 0.6077  -0.4670 -0.1157 103  TYR D N   
9615  C  CA  . TYR D  105 ? 2.8497 2.6494 3.2159 0.5891  -0.4520 -0.1308 103  TYR D CA  
9616  C  C   . TYR D  105 ? 3.0050 2.7895 3.2976 0.5546  -0.4749 -0.0967 103  TYR D C   
9617  O  O   . TYR D  105 ? 3.0942 2.9036 3.3531 0.5612  -0.4913 -0.0415 103  TYR D O   
9618  C  CB  . TYR D  105 ? 2.9155 2.6319 3.3487 0.6285  -0.4166 -0.1104 103  TYR D CB  
9619  C  CG  . TYR D  105 ? 2.9932 2.7115 3.5038 0.6668  -0.3879 -0.1437 103  TYR D CG  
9620  C  CD1 . TYR D  105 ? 2.9884 2.6679 3.5415 0.6554  -0.3637 -0.2164 103  TYR D CD1 
9621  C  CD2 . TYR D  105 ? 3.1628 2.9272 3.7051 0.7149  -0.3845 -0.1050 103  TYR D CD2 
9622  C  CE1 . TYR D  105 ? 3.1301 2.8073 3.7529 0.6896  -0.3341 -0.2526 103  TYR D CE1 
9623  C  CE2 . TYR D  105 ? 3.3202 3.0835 3.9353 0.7535  -0.3546 -0.1361 103  TYR D CE2 
9624  C  CZ  . TYR D  105 ? 3.3062 3.0214 3.9601 0.7399  -0.3281 -0.2113 103  TYR D CZ  
9625  O  OH  . TYR D  105 ? 3.3994 3.1097 4.1246 0.7776  -0.2951 -0.2473 103  TYR D OH  
9626  N  N   . MET D  106 ? 3.1475 2.8955 3.4161 0.5187  -0.4755 -0.1319 104  MET D N   
9627  C  CA  . MET D  106 ? 3.0001 2.7220 3.2044 0.4866  -0.4909 -0.1079 104  MET D CA  
9628  C  C   . MET D  106 ? 2.9199 2.5544 3.1517 0.4784  -0.4679 -0.1237 104  MET D C   
9629  O  O   . MET D  106 ? 2.9352 2.5533 3.2101 0.4729  -0.4527 -0.1787 104  MET D O   
9630  C  CB  . MET D  106 ? 2.9089 2.6835 3.0525 0.4496  -0.5154 -0.1328 104  MET D CB  
9631  C  CG  . MET D  106 ? 2.9887 2.8528 3.1123 0.4513  -0.5337 -0.1259 104  MET D CG  
9632  S  SD  . MET D  106 ? 3.0230 2.9388 3.0913 0.4126  -0.5503 -0.1638 104  MET D SD  
9633  C  CE  . MET D  106 ? 3.1108 3.0187 3.2359 0.4232  -0.5302 -0.2318 104  MET D CE  
9634  N  N   . PHE D  107 ? 2.7759 2.3604 2.9818 0.4749  -0.4650 -0.0786 105  PHE D N   
9635  C  CA  . PHE D  107 ? 2.8266 2.3279 3.0647 0.4684  -0.4387 -0.0857 105  PHE D CA  
9636  C  C   . PHE D  107 ? 2.7913 2.2736 2.9677 0.4363  -0.4504 -0.0712 105  PHE D C   
9637  O  O   . PHE D  107 ? 2.8966 2.4044 3.0067 0.4292  -0.4713 -0.0326 105  PHE D O   
9638  C  CB  . PHE D  107 ? 2.9307 2.3719 3.2133 0.5039  -0.4101 -0.0396 105  PHE D CB  
9639  C  CG  . PHE D  107 ? 3.0473 2.4655 3.4144 0.5330  -0.3813 -0.0678 105  PHE D CG  
9640  C  CD1 . PHE D  107 ? 3.1709 2.6470 3.5557 0.5625  -0.3883 -0.0675 105  PHE D CD1 
9641  C  CD2 . PHE D  107 ? 3.0005 2.3392 3.4330 0.5297  -0.3444 -0.0973 105  PHE D CD2 
9642  C  CE1 . PHE D  107 ? 3.2519 2.7023 3.7154 0.5918  -0.3579 -0.0959 105  PHE D CE1 
9643  C  CE2 . PHE D  107 ? 3.1458 2.4549 3.6575 0.5547  -0.3136 -0.1282 105  PHE D CE2 
9644  C  CZ  . PHE D  107 ? 3.2534 2.6161 3.7793 0.5877  -0.3198 -0.1274 105  PHE D CZ  
9645  N  N   . PHE D  108 ? 2.6252 2.0640 2.8277 0.4169  -0.4347 -0.1051 106  PHE D N   
9646  C  CA  . PHE D  108 ? 2.5335 1.9509 2.6906 0.3894  -0.4399 -0.0970 106  PHE D CA  
9647  C  C   . PHE D  108 ? 2.6099 1.9519 2.8188 0.3874  -0.4062 -0.0962 106  PHE D C   
9648  O  O   . PHE D  108 ? 2.7817 2.0877 3.0644 0.4014  -0.3791 -0.1138 106  PHE D O   
9649  C  CB  . PHE D  108 ? 2.5597 2.0225 2.6919 0.3630  -0.4593 -0.1451 106  PHE D CB  
9650  C  CG  . PHE D  108 ? 2.6522 2.1831 2.7284 0.3597  -0.4883 -0.1426 106  PHE D CG  
9651  C  CD1 . PHE D  108 ? 2.6984 2.2790 2.8008 0.3727  -0.4933 -0.1690 106  PHE D CD1 
9652  C  CD2 . PHE D  108 ? 2.7198 2.2630 2.7192 0.3419  -0.5070 -0.1162 106  PHE D CD2 
9653  C  CE1 . PHE D  108 ? 2.7431 2.3881 2.7974 0.3670  -0.5164 -0.1658 106  PHE D CE1 
9654  C  CE2 . PHE D  108 ? 2.8037 2.4046 2.7555 0.3344  -0.5293 -0.1149 106  PHE D CE2 
9655  C  CZ  . PHE D  108 ? 2.8547 2.5085 2.8347 0.3463  -0.5340 -0.1382 106  PHE D CZ  
9656  N  N   . GLN D  109 ? 2.5550 1.8712 2.7274 0.3687  -0.4047 -0.0777 107  GLN D N   
9657  C  CA  . GLN D  109 ? 2.5586 1.8093 2.7779 0.3613  -0.3717 -0.0770 107  GLN D CA  
9658  C  C   . GLN D  109 ? 2.5489 1.8158 2.8021 0.3337  -0.3715 -0.1394 107  GLN D C   
9659  O  O   . GLN D  109 ? 2.6068 1.9293 2.8627 0.3275  -0.3914 -0.1863 107  GLN D O   
9660  C  CB  . GLN D  109 ? 2.7292 1.9468 2.8920 0.3587  -0.3665 -0.0199 107  GLN D CB  
9661  C  CG  . GLN D  109 ? 2.8196 2.0262 2.9489 0.3864  -0.3657 0.0444  107  GLN D CG  
9662  C  CD  . GLN D  109 ? 2.7472 1.9254 2.8158 0.3814  -0.3595 0.0947  107  GLN D CD  
9663  O  OE1 . GLN D  109 ? 2.6357 1.8060 2.6805 0.3570  -0.3585 0.0810  107  GLN D OE1 
9664  N  NE2 . GLN D  109 ? 2.8200 1.9867 2.8636 0.4072  -0.3541 0.1536  107  GLN D NE2 
9665  N  N   . THR D  110 ? 2.4923 1.7167 2.7732 0.3179  -0.3480 -0.1397 108  THR D N   
9666  C  CA  . THR D  110 ? 2.4826 1.7310 2.7949 0.2913  -0.3485 -0.1929 108  THR D CA  
9667  C  C   . THR D  110 ? 2.4634 1.6867 2.7553 0.2767  -0.3371 -0.1679 108  THR D C   
9668  O  O   . THR D  110 ? 2.4512 1.7114 2.7461 0.2585  -0.3467 -0.2009 108  THR D O   
9669  C  CB  . THR D  110 ? 2.5063 1.7356 2.9194 0.2823  -0.3217 -0.2473 108  THR D CB  
9670  O  OG1 . THR D  110 ? 2.5380 1.7710 2.9751 0.3022  -0.3217 -0.2616 108  THR D OG1 
9671  C  CG2 . THR D  110 ? 2.4989 1.7882 2.9391 0.2566  -0.3353 -0.3146 108  THR D CG2 
9672  N  N   . SER D  111 ? 2.6421 1.8090 2.9127 0.2867  -0.3163 -0.1093 109  SER D N   
9673  C  CA  . SER D  111 ? 2.8321 1.9751 3.0756 0.2751  -0.3028 -0.0816 109  SER D CA  
9674  C  C   . SER D  111 ? 2.9266 2.1102 3.0816 0.2713  -0.3339 -0.0713 109  SER D C   
9675  O  O   . SER D  111 ? 3.1323 2.3123 3.2717 0.2593  -0.3265 -0.0677 109  SER D O   
9676  C  CB  . SER D  111 ? 2.8764 1.9542 3.1071 0.2907  -0.2739 -0.0172 109  SER D CB  
9677  O  OG  . SER D  111 ? 3.0464 2.0744 3.3595 0.2971  -0.2392 -0.0203 109  SER D OG  
9678  N  N   . GLU D  112 ? 2.9603 2.1798 3.0598 0.2812  -0.3651 -0.0660 110  GLU D N   
9679  C  CA  . GLU D  112 ? 2.7466 2.0016 2.7670 0.2751  -0.3927 -0.0625 110  GLU D CA  
9680  C  C   . GLU D  112 ? 2.8166 2.1313 2.8479 0.2686  -0.4162 -0.1126 110  GLU D C   
9681  O  O   . GLU D  112 ? 2.8513 2.1908 2.8327 0.2624  -0.4318 -0.1155 110  GLU D O   
9682  C  CB  . GLU D  112 ? 2.8448 2.1032 2.7928 0.2858  -0.4098 -0.0217 110  GLU D CB  
9683  C  CG  . GLU D  112 ? 2.5647 1.7750 2.4817 0.2946  -0.3905 0.0346  110  GLU D CG  
9684  C  CD  . GLU D  112 ? 2.5244 1.7555 2.3710 0.3044  -0.4121 0.0716  110  GLU D CD  
9685  O  OE1 . GLU D  112 ? 2.6073 1.8863 2.4409 0.3044  -0.4386 0.0540  110  GLU D OE1 
9686  O  OE2 . GLU D  112 ? 2.5438 1.7501 2.3485 0.3111  -0.4023 0.1171  110  GLU D OE2 
9687  N  N   . LEU D  113 ? 2.5263 1.8635 2.6204 0.2714  -0.4167 -0.1513 111  LEU D N   
9688  C  CA  . LEU D  113 ? 2.4626 1.8633 2.5685 0.2657  -0.4373 -0.2015 111  LEU D CA  
9689  C  C   . LEU D  113 ? 2.3998 1.8175 2.5455 0.2519  -0.4299 -0.2335 111  LEU D C   
9690  O  O   . LEU D  113 ? 2.4057 1.8702 2.5208 0.2495  -0.4484 -0.2471 111  LEU D O   
9691  C  CB  . LEU D  113 ? 2.5064 1.9276 2.6667 0.2727  -0.4375 -0.2376 111  LEU D CB  
9692  C  CG  . LEU D  113 ? 2.4649 1.9078 2.5850 0.2874  -0.4549 -0.2209 111  LEU D CG  
9693  C  CD1 . LEU D  113 ? 2.5496 2.0525 2.6101 0.2830  -0.4836 -0.2316 111  LEU D CD1 
9694  C  CD2 . LEU D  113 ? 2.4216 1.8228 2.4989 0.2984  -0.4505 -0.1594 111  LEU D CD2 
9695  N  N   . ARG D  114 ? 2.6717 2.0531 2.8874 0.2435  -0.4011 -0.2427 112  ARG D N   
9696  C  CA  . ARG D  114 ? 2.6843 2.0825 2.9452 0.2279  -0.3901 -0.2688 112  ARG D CA  
9697  C  C   . ARG D  114 ? 2.7284 2.0982 2.9395 0.2283  -0.3816 -0.2240 112  ARG D C   
9698  O  O   . ARG D  114 ? 2.7542 2.1371 3.0020 0.2175  -0.3692 -0.2381 112  ARG D O   
9699  C  CB  . ARG D  114 ? 2.7654 2.1300 3.1254 0.2142  -0.3568 -0.2959 112  ARG D CB  
9700  C  CG  . ARG D  114 ? 2.8182 2.2286 3.2616 0.1899  -0.3479 -0.3547 112  ARG D CG  
9701  C  CD  . ARG D  114 ? 2.8635 2.2177 3.4091 0.1692  -0.3024 -0.3723 112  ARG D CD  
9702  N  NE  . ARG D  114 ? 2.9804 2.2397 3.5164 0.1774  -0.2679 -0.3095 112  ARG D NE  
9703  C  CZ  . ARG D  114 ? 2.7521 1.9728 3.2817 0.1725  -0.2425 -0.2685 112  ARG D CZ  
9704  N  NH1 . ARG D  114 ? 2.5611 1.8267 3.0983 0.1591  -0.2450 -0.2817 112  ARG D NH1 
9705  N  NH2 . ARG D  114 ? 2.7537 1.8936 3.2691 0.1840  -0.2129 -0.2113 112  ARG D NH2 
9706  N  N   . GLU D  115 ? 2.6668 2.0047 2.7966 0.2394  -0.3879 -0.1744 113  GLU D N   
9707  C  CA  . GLU D  115 ? 2.7131 2.0271 2.7838 0.2400  -0.3814 -0.1375 113  GLU D CA  
9708  C  C   . GLU D  115 ? 2.6440 1.9951 2.6449 0.2451  -0.4085 -0.1378 113  GLU D C   
9709  O  O   . GLU D  115 ? 2.7046 2.0627 2.6883 0.2452  -0.4046 -0.1346 113  GLU D O   
9710  C  CB  . GLU D  115 ? 2.7454 1.9983 2.7696 0.2462  -0.3669 -0.0840 113  GLU D CB  
9711  C  CG  . GLU D  115 ? 2.7491 1.9660 2.7317 0.2441  -0.3473 -0.0500 113  GLU D CG  
9712  C  CD  . GLU D  115 ? 2.8120 2.0411 2.7091 0.2461  -0.3664 -0.0400 113  GLU D CD  
9713  O  OE1 . GLU D  115 ? 2.6067 1.8520 2.4570 0.2492  -0.3913 -0.0376 113  GLU D OE1 
9714  O  OE2 . GLU D  115 ? 3.0569 2.2776 2.9357 0.2444  -0.3539 -0.0345 113  GLU D OE2 
9715  N  N   . ALA D  116 ? 2.5642 1.9409 2.5306 0.2503  -0.4331 -0.1427 114  ALA D N   
9716  C  CA  . ALA D  116 ? 2.6515 2.0626 2.5586 0.2542  -0.4551 -0.1443 114  ALA D CA  
9717  C  C   . ALA D  116 ? 2.7633 2.2389 2.7125 0.2565  -0.4657 -0.1858 114  ALA D C   
9718  O  O   . ALA D  116 ? 2.9100 2.4063 2.8258 0.2632  -0.4722 -0.1814 114  ALA D O   
9719  C  CB  . ALA D  116 ? 2.5357 1.9591 2.3982 0.2566  -0.4750 -0.1368 114  ALA D CB  
9720  N  N   . VAL D  117 ? 2.5995 2.1094 2.6220 0.2523  -0.4668 -0.2267 115  VAL D N   
9721  C  CA  . VAL D  117 ? 2.4739 2.0567 2.5447 0.2517  -0.4774 -0.2730 115  VAL D CA  
9722  C  C   . VAL D  117 ? 2.5074 2.0862 2.6716 0.2372  -0.4558 -0.3033 115  VAL D C   
9723  O  O   . VAL D  117 ? 2.5822 2.1618 2.8018 0.2291  -0.4505 -0.3352 115  VAL D O   
9724  C  CB  . VAL D  117 ? 2.4646 2.1072 2.5322 0.2562  -0.5011 -0.3056 115  VAL D CB  
9725  C  CG1 . VAL D  117 ? 2.5056 2.2356 2.6109 0.2576  -0.5156 -0.3516 115  VAL D CG1 
9726  C  CG2 . VAL D  117 ? 2.4959 2.1333 2.4749 0.2663  -0.5167 -0.2717 115  VAL D CG2 
9727  N  N   . PRO D  118 ? 2.5809 2.1522 2.7679 0.2328  -0.4392 -0.2952 116  PRO D N   
9728  C  CA  . PRO D  118 ? 2.6434 2.2072 2.9234 0.2143  -0.4135 -0.3219 116  PRO D CA  
9729  C  C   . PRO D  118 ? 2.6625 2.2994 3.0198 0.2016  -0.4238 -0.3898 116  PRO D C   
9730  O  O   . PRO D  118 ? 2.8930 2.5065 3.3143 0.1864  -0.4072 -0.4184 116  PRO D O   
9731  C  CB  . PRO D  118 ? 2.6454 2.2125 2.9260 0.2153  -0.3999 -0.3028 116  PRO D CB  
9732  C  CG  . PRO D  118 ? 2.6370 2.1685 2.8159 0.2337  -0.4074 -0.2516 116  PRO D CG  
9733  C  CD  . PRO D  118 ? 2.5734 2.1368 2.7027 0.2442  -0.4388 -0.2594 116  PRO D CD  
9734  N  N   . GLU D  119 ? 2.5517 2.2780 2.9038 0.2085  -0.4496 -0.4165 117  GLU D N   
9735  C  CA  . GLU D  119 ? 2.6676 2.4779 3.0908 0.1947  -0.4618 -0.4864 117  GLU D CA  
9736  C  C   . GLU D  119 ? 2.6357 2.4846 3.0204 0.2052  -0.4886 -0.5078 117  GLU D C   
9737  O  O   . GLU D  119 ? 2.6704 2.5318 2.9725 0.2270  -0.5091 -0.4746 117  GLU D O   
9738  C  CB  . GLU D  119 ? 2.6827 2.5868 3.1313 0.1973  -0.4753 -0.5070 117  GLU D CB  
9739  C  CG  . GLU D  119 ? 2.7817 2.7799 3.3185 0.1759  -0.4843 -0.5851 117  GLU D CG  
9740  C  CD  . GLU D  119 ? 2.8347 2.9285 3.4120 0.1764  -0.4934 -0.6026 117  GLU D CD  
9741  O  OE1 . GLU D  119 ? 2.8423 2.9229 3.3784 0.1970  -0.4903 -0.5516 117  GLU D OE1 
9742  O  OE2 . GLU D  119 ? 2.8648 3.0508 3.5166 0.1565  -0.5031 -0.6696 117  GLU D OE2 
9743  N  N   . PRO D  120 ? 2.4242 2.2871 2.8660 0.1897  -0.4853 -0.5620 118  PRO D N   
9744  C  CA  . PRO D  120 ? 2.3604 2.2586 2.7655 0.2005  -0.5068 -0.5830 118  PRO D CA  
9745  C  C   . PRO D  120 ? 2.3404 2.3452 2.7016 0.2158  -0.5415 -0.5981 118  PRO D C   
9746  O  O   . PRO D  120 ? 2.3340 2.3614 2.6385 0.2305  -0.5589 -0.5938 118  PRO D O   
9747  C  CB  . PRO D  120 ? 2.4235 2.3244 2.9157 0.1779  -0.4915 -0.6509 118  PRO D CB  
9748  C  CG  . PRO D  120 ? 2.4751 2.2990 3.0337 0.1584  -0.4549 -0.6414 118  PRO D CG  
9749  C  CD  . PRO D  120 ? 2.4415 2.2816 2.9848 0.1609  -0.4569 -0.6068 118  PRO D CD  
9750  N  N   . VAL D  121 ? 2.2446 2.3196 2.6303 0.2147  -0.5510 -0.6127 119  VAL D N   
9751  C  CA  . VAL D  121 ? 2.1907 2.3759 2.5369 0.2339  -0.5840 -0.6249 119  VAL D CA  
9752  C  C   . VAL D  121 ? 2.1787 2.3375 2.4257 0.2640  -0.5932 -0.5531 119  VAL D C   
9753  O  O   . VAL D  121 ? 2.1094 2.3315 2.2999 0.2846  -0.6165 -0.5481 119  VAL D O   
9754  C  CB  . VAL D  121 ? 2.1964 2.4765 2.6078 0.2257  -0.5920 -0.6638 119  VAL D CB  
9755  C  CG1 . VAL D  121 ? 2.2389 2.6520 2.6210 0.2450  -0.6281 -0.6897 119  VAL D CG1 
9756  C  CG2 . VAL D  121 ? 2.2540 2.5325 2.7733 0.1872  -0.5721 -0.7297 119  VAL D CG2 
9757  N  N   . LEU D  122 ? 2.2991 2.3626 2.5214 0.2659  -0.5727 -0.4976 120  LEU D N   
9758  C  CA  . LEU D  122 ? 2.3048 2.3335 2.4371 0.2898  -0.5765 -0.4339 120  LEU D CA  
9759  C  C   . LEU D  122 ? 2.2242 2.2292 2.2877 0.2969  -0.5852 -0.4148 120  LEU D C   
9760  O  O   . LEU D  122 ? 2.1759 2.1826 2.1652 0.3163  -0.5940 -0.3759 120  LEU D O   
9761  C  CB  . LEU D  122 ? 2.4598 2.3904 2.5839 0.2854  -0.5500 -0.3878 120  LEU D CB  
9762  C  CG  . LEU D  122 ? 2.5161 2.4585 2.7079 0.2772  -0.5342 -0.3987 120  LEU D CG  
9763  C  CD1 . LEU D  122 ? 2.4521 2.2918 2.6268 0.2725  -0.5051 -0.3521 120  LEU D CD1 
9764  C  CD2 . LEU D  122 ? 2.5725 2.6027 2.7596 0.2998  -0.5505 -0.3983 120  LEU D CD2 
9765  N  N   . LEU D  123 ? 2.3812 2.3646 2.4718 0.2821  -0.5804 -0.4416 121  LEU D N   
9766  C  CA  . LEU D  123 ? 2.4527 2.4162 2.4878 0.2873  -0.5860 -0.4245 121  LEU D CA  
9767  C  C   . LEU D  123 ? 2.5922 2.6466 2.5879 0.3027  -0.6095 -0.4401 121  LEU D C   
9768  O  O   . LEU D  123 ? 2.6872 2.8268 2.7238 0.3015  -0.6220 -0.4933 121  LEU D O   
9769  C  CB  . LEU D  123 ? 2.4936 2.4252 2.5793 0.2726  -0.5740 -0.4547 121  LEU D CB  
9770  C  CG  . LEU D  123 ? 2.4725 2.3552 2.5149 0.2759  -0.5706 -0.4246 121  LEU D CG  
9771  C  CD1 . LEU D  123 ? 2.4770 2.4267 2.4862 0.2849  -0.5877 -0.4443 121  LEU D CD1 
9772  C  CD2 . LEU D  123 ? 2.4701 2.2894 2.4451 0.2801  -0.5661 -0.3595 121  LEU D CD2 
9773  N  N   . SER D  124 ? 2.5397 2.5777 2.4549 0.3160  -0.6140 -0.3938 122  SER D N   
9774  C  CA  . SER D  124 ? 2.4509 2.5661 2.3178 0.3328  -0.6318 -0.3965 122  SER D CA  
9775  C  C   . SER D  124 ? 2.5477 2.6584 2.3852 0.3287  -0.6319 -0.3977 122  SER D C   
9776  O  O   . SER D  124 ? 2.4410 2.6239 2.2929 0.3305  -0.6419 -0.4413 122  SER D O   
9777  C  CB  . SER D  124 ? 2.3389 2.4434 2.1380 0.3530  -0.6327 -0.3411 122  SER D CB  
9778  O  OG  . SER D  124 ? 2.2953 2.4727 2.0448 0.3724  -0.6469 -0.3362 122  SER D OG  
9779  N  N   . ARG D  125 ? 2.8438 2.8775 2.6410 0.3227  -0.6205 -0.3533 123  ARG D N   
9780  C  CA  . ARG D  125 ? 2.9124 2.9442 2.6878 0.3178  -0.6191 -0.3514 123  ARG D CA  
9781  C  C   . ARG D  125 ? 2.9540 2.9029 2.7433 0.3038  -0.6053 -0.3303 123  ARG D C   
9782  O  O   . ARG D  125 ? 3.0690 2.9527 2.8315 0.2991  -0.5974 -0.2898 123  ARG D O   
9783  C  CB  . ARG D  125 ? 2.9210 2.9678 2.6159 0.3265  -0.6221 -0.3121 123  ARG D CB  
9784  C  CG  . ARG D  125 ? 2.8194 2.8728 2.4942 0.3194  -0.6191 -0.3093 123  ARG D CG  
9785  C  CD  . ARG D  125 ? 2.8548 2.9322 2.4551 0.3260  -0.6188 -0.2746 123  ARG D CD  
9786  N  NE  . ARG D  125 ? 2.9040 3.0003 2.4908 0.3179  -0.6146 -0.2750 123  ARG D NE  
9787  C  CZ  . ARG D  125 ? 2.8690 2.9966 2.3999 0.3205  -0.6109 -0.2519 123  ARG D CZ  
9788  N  NH1 . ARG D  125 ? 2.8510 2.9892 2.3309 0.3339  -0.6105 -0.2233 123  ARG D NH1 
9789  N  NH2 . ARG D  125 ? 2.7731 2.9225 2.3010 0.3114  -0.6054 -0.2550 123  ARG D NH2 
9790  N  N   . ALA D  126 ? 2.8084 2.7629 2.6380 0.2997  -0.6018 -0.3575 124  ALA D N   
9791  C  CA  . ALA D  126 ? 2.8291 2.7174 2.6771 0.2921  -0.5899 -0.3374 124  ALA D CA  
9792  C  C   . ALA D  126 ? 2.6251 2.5382 2.4629 0.2941  -0.5910 -0.3383 124  ALA D C   
9793  O  O   . ALA D  126 ? 2.4906 2.4402 2.3736 0.2996  -0.5891 -0.3802 124  ALA D O   
9794  C  CB  . ALA D  126 ? 2.9947 2.8546 2.9211 0.2891  -0.5782 -0.3671 124  ALA D CB  
9795  N  N   . GLU D  127 ? 2.6011 2.4972 2.3821 0.2884  -0.5922 -0.2954 125  GLU D N   
9796  C  CA  . GLU D  127 ? 2.5874 2.5136 2.3580 0.2882  -0.5927 -0.2915 125  GLU D CA  
9797  C  C   . GLU D  127 ? 2.4921 2.3718 2.2752 0.2837  -0.5872 -0.2632 125  GLU D C   
9798  O  O   . GLU D  127 ? 2.5713 2.3990 2.3235 0.2736  -0.5859 -0.2272 125  GLU D O   
9799  C  CB  . GLU D  127 ? 2.6444 2.5991 2.3448 0.2822  -0.5969 -0.2667 125  GLU D CB  
9800  C  CG  . GLU D  127 ? 2.6534 2.5544 2.2987 0.2719  -0.5950 -0.2248 125  GLU D CG  
9801  C  CD  . GLU D  127 ? 2.6795 2.6024 2.2596 0.2676  -0.5938 -0.2018 125  GLU D CD  
9802  O  OE1 . GLU D  127 ? 2.6072 2.5871 2.1815 0.2691  -0.5943 -0.2123 125  GLU D OE1 
9803  O  OE2 . GLU D  127 ? 2.7548 2.6354 2.2900 0.2636  -0.5891 -0.1723 125  GLU D OE2 
9804  N  N   . LEU D  128 ? 2.3824 2.2843 2.2103 0.2934  -0.5833 -0.2802 126  LEU D N   
9805  C  CA  . LEU D  128 ? 2.4024 2.2772 2.2462 0.2958  -0.5796 -0.2521 126  LEU D CA  
9806  C  C   . LEU D  128 ? 2.3554 2.2677 2.1559 0.2860  -0.5864 -0.2266 126  LEU D C   
9807  O  O   . LEU D  128 ? 2.3749 2.3472 2.1776 0.2898  -0.5869 -0.2455 126  LEU D O   
9808  C  CB  . LEU D  128 ? 2.4844 2.3640 2.4028 0.3159  -0.5689 -0.2803 126  LEU D CB  
9809  C  CG  . LEU D  128 ? 2.6581 2.5224 2.5988 0.3275  -0.5648 -0.2489 126  LEU D CG  
9810  C  CD1 . LEU D  128 ? 2.7967 2.5958 2.7217 0.3219  -0.5632 -0.2088 126  LEU D CD1 
9811  C  CD2 . LEU D  128 ? 2.6590 2.5264 2.6758 0.3522  -0.5495 -0.2790 126  LEU D CD2 
9812  N  N   . ARG D  129 ? 2.4202 2.3010 2.1821 0.2712  -0.5902 -0.1866 127  ARG D N   
9813  C  CA  . ARG D  129 ? 2.4476 2.3619 2.1675 0.2536  -0.5958 -0.1641 127  ARG D CA  
9814  C  C   . ARG D  129 ? 2.6793 2.6081 2.4218 0.2577  -0.5997 -0.1429 127  ARG D C   
9815  O  O   . ARG D  129 ? 2.9204 2.8075 2.6780 0.2658  -0.5990 -0.1260 127  ARG D O   
9816  C  CB  . ARG D  129 ? 2.4661 2.3404 2.1176 0.2284  -0.5967 -0.1392 127  ARG D CB  
9817  C  CG  . ARG D  129 ? 2.3701 2.2326 1.9981 0.2302  -0.5930 -0.1523 127  ARG D CG  
9818  C  CD  . ARG D  129 ? 2.3770 2.2130 1.9360 0.2074  -0.5893 -0.1267 127  ARG D CD  
9819  N  NE  . ARG D  129 ? 2.4048 2.2391 1.9408 0.2158  -0.5855 -0.1336 127  ARG D NE  
9820  C  CZ  . ARG D  129 ? 2.4747 2.2873 1.9530 0.2035  -0.5779 -0.1120 127  ARG D CZ  
9821  N  NH1 . ARG D  129 ? 2.4668 2.2544 1.9061 0.1764  -0.5719 -0.0882 127  ARG D NH1 
9822  N  NH2 . ARG D  129 ? 2.6249 2.4429 2.0858 0.2185  -0.5752 -0.1146 127  ARG D NH2 
9823  N  N   . LEU D  130 ? 2.7013 2.6954 2.4463 0.2534  -0.6030 -0.1418 128  LEU D N   
9824  C  CA  . LEU D  130 ? 2.7020 2.7312 2.4719 0.2599  -0.6090 -0.1217 128  LEU D CA  
9825  C  C   . LEU D  130 ? 2.6789 2.7432 2.4028 0.2267  -0.6174 -0.1002 128  LEU D C   
9826  O  O   . LEU D  130 ? 2.6379 2.6751 2.3062 0.1976  -0.6157 -0.0959 128  LEU D O   
9827  C  CB  . LEU D  130 ? 2.6383 2.7263 2.4714 0.2889  -0.6035 -0.1433 128  LEU D CB  
9828  C  CG  . LEU D  130 ? 2.5568 2.6200 2.4401 0.3169  -0.5910 -0.1780 128  LEU D CG  
9829  C  CD1 . LEU D  130 ? 2.6051 2.7227 2.5508 0.3464  -0.5827 -0.1964 128  LEU D CD1 
9830  C  CD2 . LEU D  130 ? 2.5882 2.5746 2.4889 0.3277  -0.5867 -0.1672 128  LEU D CD2 
9831  N  N   . LEU D  131 ? 2.6801 2.8064 2.4302 0.2309  -0.6251 -0.0873 129  LEU D N   
9832  C  CA  . LEU D  131 ? 2.5912 2.7666 2.3093 0.1960  -0.6333 -0.0727 129  LEU D CA  
9833  C  C   . LEU D  131 ? 2.6389 2.9132 2.4068 0.2087  -0.6353 -0.0771 129  LEU D C   
9834  O  O   . LEU D  131 ? 2.7111 3.0177 2.5273 0.2398  -0.6411 -0.0667 129  LEU D O   
9835  C  CB  . LEU D  131 ? 2.5623 2.7152 2.2514 0.1810  -0.6458 -0.0460 129  LEU D CB  
9836  C  CG  . LEU D  131 ? 2.6712 2.8743 2.3260 0.1372  -0.6546 -0.0374 129  LEU D CG  
9837  C  CD1 . LEU D  131 ? 2.4573 2.6491 2.0731 0.1015  -0.6415 -0.0511 129  LEU D CD1 
9838  C  CD2 . LEU D  131 ? 2.9638 3.1301 2.5748 0.1179  -0.6651 -0.0188 129  LEU D CD2 
9839  N  N   . ARG D  132 ? 2.6361 2.9590 2.3923 0.1863  -0.6282 -0.0891 130  ARG D N   
9840  C  CA  . ARG D  132 ? 2.5380 2.9617 2.3411 0.1954  -0.6266 -0.0953 130  ARG D CA  
9841  C  C   . ARG D  132 ? 2.5304 3.0210 2.3308 0.1661  -0.6400 -0.0756 130  ARG D C   
9842  O  O   . ARG D  132 ? 2.6248 3.0845 2.3749 0.1267  -0.6467 -0.0639 130  ARG D O   
9843  C  CB  . ARG D  132 ? 2.5806 3.0336 2.3721 0.1838  -0.6099 -0.1162 130  ARG D CB  
9844  C  CG  . ARG D  132 ? 2.8170 3.2469 2.6280 0.2186  -0.5982 -0.1442 130  ARG D CG  
9845  C  CD  . ARG D  132 ? 3.0413 3.5235 2.8401 0.2096  -0.5823 -0.1621 130  ARG D CD  
9846  N  NE  . ARG D  132 ? 3.2930 3.7622 3.1038 0.2398  -0.5725 -0.1944 130  ARG D NE  
9847  C  CZ  . ARG D  132 ? 3.3245 3.8367 3.1210 0.2400  -0.5584 -0.2139 130  ARG D CZ  
9848  N  NH1 . ARG D  132 ? 3.3264 3.8918 3.0979 0.2119  -0.5491 -0.2005 130  ARG D NH1 
9849  N  NH2 . ARG D  132 ? 3.2748 3.7798 3.0816 0.2668  -0.5523 -0.2481 130  ARG D NH2 
9850  N  N   . LEU D  133 ? 2.3849 2.9716 2.2432 0.1865  -0.6434 -0.0747 131  LEU D N   
9851  C  CA  . LEU D  133 ? 2.3871 3.0689 2.2556 0.1579  -0.6550 -0.0628 131  LEU D CA  
9852  C  C   . LEU D  133 ? 2.4515 3.2156 2.3454 0.1469  -0.6394 -0.0793 131  LEU D C   
9853  O  O   . LEU D  133 ? 2.5189 3.2687 2.4225 0.1683  -0.6215 -0.0985 131  LEU D O   
9854  C  CB  . LEU D  133 ? 2.3828 3.1237 2.3021 0.1950  -0.6733 -0.0420 131  LEU D CB  
9855  C  CG  . LEU D  133 ? 2.4069 3.0798 2.2925 0.1986  -0.6888 -0.0198 131  LEU D CG  
9856  C  CD1 . LEU D  133 ? 2.6454 3.3854 2.5787 0.2396  -0.7059 0.0074  131  LEU D CD1 
9857  C  CD2 . LEU D  133 ? 2.3501 2.9981 2.1663 0.1368  -0.6971 -0.0184 131  LEU D CD2 
9858  N  N   . LYS D  134 ? 2.4895 3.3450 2.3937 0.1112  -0.6455 -0.0737 132  LYS D N   
9859  C  CA  . LYS D  134 ? 2.6667 3.6065 2.5968 0.0968  -0.6275 -0.0870 132  LYS D CA  
9860  C  C   . LYS D  134 ? 2.7074 3.7066 2.7079 0.1569  -0.6201 -0.0968 132  LYS D C   
9861  O  O   . LYS D  134 ? 2.9693 4.0100 3.0206 0.1971  -0.6343 -0.0851 132  LYS D O   
9862  C  CB  . LYS D  134 ? 2.7730 3.8125 2.7149 0.0475  -0.6360 -0.0806 132  LYS D CB  
9863  C  CG  . LYS D  134 ? 2.6750 3.8090 2.6701 0.0693  -0.6630 -0.0657 132  LYS D CG  
9864  C  CD  . LYS D  134 ? 2.5124 3.7616 2.5238 0.0143  -0.6703 -0.0667 132  LYS D CD  
9865  C  CE  . LYS D  134 ? 2.3582 3.7205 2.4230 0.0380  -0.7004 -0.0506 132  LYS D CE  
9866  N  NZ  . LYS D  134 ? 2.2794 3.7694 2.3670 -0.0190 -0.7087 -0.0570 132  LYS D NZ  
9867  N  N   . LEU D  135 ? 2.3555 3.3546 2.3565 0.1662  -0.5959 -0.1181 133  LEU D N   
9868  C  CA  . LEU D  135 ? 2.3526 3.3961 2.4152 0.2224  -0.5838 -0.1353 133  LEU D CA  
9869  C  C   . LEU D  135 ? 2.4428 3.5912 2.5350 0.2152  -0.5623 -0.1497 133  LEU D C   
9870  O  O   . LEU D  135 ? 2.5289 3.7307 2.6788 0.2617  -0.5504 -0.1655 133  LEU D O   
9871  C  CB  . LEU D  135 ? 2.3791 3.3230 2.4214 0.2534  -0.5735 -0.1565 133  LEU D CB  
9872  C  CG  . LEU D  135 ? 2.4723 3.4303 2.5820 0.3166  -0.5650 -0.1744 133  LEU D CG  
9873  C  CD1 . LEU D  135 ? 2.5019 3.4845 2.6613 0.3457  -0.5826 -0.1475 133  LEU D CD1 
9874  C  CD2 . LEU D  135 ? 2.5443 3.4005 2.6353 0.3387  -0.5577 -0.1982 133  LEU D CD2 
9875  N  N   . LYS D  136 ? 2.5326 3.7090 2.5885 0.1589  -0.5535 -0.1447 134  LYS D N   
9876  C  CA  . LYS D  136 ? 2.6414 3.9181 2.7206 0.1448  -0.5289 -0.1550 134  LYS D CA  
9877  C  C   . LYS D  136 ? 2.8429 4.0994 2.9159 0.1816  -0.5048 -0.1818 134  LYS D C   
9878  O  O   . LYS D  136 ? 2.9610 4.1169 2.9836 0.1893  -0.5046 -0.1899 134  LYS D O   
9879  C  CB  . LYS D  136 ? 2.5593 3.9692 2.7192 0.1576  -0.5359 -0.1492 134  LYS D CB  
9880  C  CG  . LYS D  136 ? 2.5708 4.0231 2.7348 0.1144  -0.5605 -0.1274 134  LYS D CG  
9881  C  CD  . LYS D  136 ? 2.5704 4.1722 2.8221 0.1359  -0.5689 -0.1220 134  LYS D CD  
9882  C  CE  . LYS D  136 ? 2.4263 4.0900 2.6844 0.0912  -0.5965 -0.1046 134  LYS D CE  
9883  N  NZ  . LYS D  136 ? 2.2941 4.1189 2.6424 0.1167  -0.6061 -0.0984 134  LYS D NZ  
9884  N  N   . VAL D  137 ? 2.8949 4.2501 3.0215 0.2077  -0.4856 -0.1983 135  VAL D N   
9885  C  CA  . VAL D  137 ? 3.0119 4.3792 3.1205 0.2219  -0.4561 -0.2245 135  VAL D CA  
9886  C  C   . VAL D  137 ? 3.0344 4.3041 3.1110 0.2568  -0.4565 -0.2490 135  VAL D C   
9887  O  O   . VAL D  137 ? 3.0706 4.2716 3.0760 0.2347  -0.4531 -0.2480 135  VAL D O   
9888  C  CB  . VAL D  137 ? 2.8948 4.3856 3.0783 0.2549  -0.4365 -0.2418 135  VAL D CB  
9889  C  CG1 . VAL D  137 ? 2.8232 4.3501 2.9767 0.2513  -0.4023 -0.2632 135  VAL D CG1 
9890  C  CG2 . VAL D  137 ? 2.8028 4.4000 3.0364 0.2274  -0.4433 -0.2183 135  VAL D CG2 
9891  N  N   . GLU D  138 ? 2.9088 4.1726 3.0395 0.3112  -0.4588 -0.2711 136  GLU D N   
9892  C  CA  . GLU D  138 ? 2.7717 3.9640 2.8824 0.3417  -0.4526 -0.3056 136  GLU D CA  
9893  C  C   . GLU D  138 ? 2.6620 3.7926 2.8199 0.3843  -0.4658 -0.3131 136  GLU D C   
9894  O  O   . GLU D  138 ? 2.7409 3.9145 2.9661 0.4128  -0.4688 -0.3027 136  GLU D O   
9895  C  CB  . GLU D  138 ? 2.7733 4.0350 2.8989 0.3666  -0.4225 -0.3451 136  GLU D CB  
9896  C  CG  . GLU D  138 ? 2.7017 4.0043 2.7648 0.3305  -0.4041 -0.3418 136  GLU D CG  
9897  C  CD  . GLU D  138 ? 2.7482 4.1370 2.8311 0.3569  -0.3728 -0.3789 136  GLU D CD  
9898  O  OE1 . GLU D  138 ? 2.7675 4.1851 2.9178 0.4024  -0.3648 -0.4087 136  GLU D OE1 
9899  O  OE2 . GLU D  138 ? 2.8081 4.2343 2.8379 0.3337  -0.3537 -0.3772 136  GLU D OE2 
9900  N  N   . GLN D  139 ? 2.5376 3.5688 2.6602 0.3881  -0.4728 -0.3278 137  GLN D N   
9901  C  CA  . GLN D  139 ? 2.5706 3.5364 2.7373 0.4298  -0.4750 -0.3467 137  GLN D CA  
9902  C  C   . GLN D  139 ? 2.6594 3.5535 2.7846 0.4289  -0.4717 -0.3829 137  GLN D C   
9903  O  O   . GLN D  139 ? 2.8235 3.7017 2.8794 0.3956  -0.4766 -0.3777 137  GLN D O   
9904  C  CB  . GLN D  139 ? 2.5149 3.4282 2.6956 0.4295  -0.4982 -0.3061 137  GLN D CB  
9905  C  CG  . GLN D  139 ? 2.5720 3.4447 2.8207 0.4807  -0.4936 -0.3142 137  GLN D CG  
9906  C  CD  . GLN D  139 ? 2.6830 3.6407 3.0081 0.5232  -0.4758 -0.3224 137  GLN D CD  
9907  O  OE1 . GLN D  139 ? 2.7177 3.7758 3.0528 0.5122  -0.4747 -0.3086 137  GLN D OE1 
9908  N  NE2 . GLN D  139 ? 2.6897 3.6064 3.0730 0.5721  -0.4593 -0.3451 137  GLN D NE2 
9909  N  N   . HIS D  140 ? 2.4927 3.3453 2.6632 0.4662  -0.4621 -0.4200 138  HIS D N   
9910  C  CA  . HIS D  140 ? 2.4059 3.1984 2.5501 0.4663  -0.4597 -0.4621 138  HIS D CA  
9911  C  C   . HIS D  140 ? 2.4201 3.1151 2.5996 0.4829  -0.4663 -0.4623 138  HIS D C   
9912  O  O   . HIS D  140 ? 2.4422 3.1259 2.6886 0.5163  -0.4573 -0.4584 138  HIS D O   
9913  C  CB  . HIS D  140 ? 2.5351 3.3784 2.6996 0.4902  -0.4344 -0.5232 138  HIS D CB  
9914  C  CG  . HIS D  140 ? 2.5982 3.4064 2.7263 0.4834  -0.4345 -0.5706 138  HIS D CG  
9915  N  ND1 . HIS D  140 ? 2.6227 3.4614 2.7693 0.5042  -0.4137 -0.6368 138  HIS D ND1 
9916  C  CD2 . HIS D  140 ? 2.5942 3.3472 2.6697 0.4586  -0.4532 -0.5634 138  HIS D CD2 
9917  C  CE1 . HIS D  140 ? 2.6121 3.4214 2.7193 0.4907  -0.4222 -0.6694 138  HIS D CE1 
9918  N  NE2 . HIS D  140 ? 2.5250 3.2835 2.5904 0.4646  -0.4461 -0.6239 138  HIS D NE2 
9919  N  N   . VAL D  141 ? 2.5590 3.1852 2.6955 0.4614  -0.4796 -0.4642 139  VAL D N   
9920  C  CA  . VAL D  141 ? 2.6294 3.1606 2.7911 0.4689  -0.4860 -0.4566 139  VAL D CA  
9921  C  C   . VAL D  141 ? 2.7557 3.2434 2.9186 0.4696  -0.4793 -0.5122 139  VAL D C   
9922  O  O   . VAL D  141 ? 2.7459 3.2569 2.8547 0.4489  -0.4858 -0.5321 139  VAL D O   
9923  C  CB  . VAL D  141 ? 2.4665 2.9548 2.5797 0.4391  -0.5094 -0.4012 139  VAL D CB  
9924  C  CG1 . VAL D  141 ? 2.4897 2.8826 2.6268 0.4470  -0.5127 -0.3931 139  VAL D CG1 
9925  C  CG2 . VAL D  141 ? 2.3990 2.9380 2.5141 0.4341  -0.5173 -0.3529 139  VAL D CG2 
9926  N  N   . GLU D  142 ? 2.8722 3.2996 3.0985 0.4937  -0.4653 -0.5366 140  GLU D N   
9927  C  CA  . GLU D  142 ? 2.8242 3.2002 3.0636 0.4897  -0.4590 -0.5893 140  GLU D CA  
9928  C  C   . GLU D  142 ? 2.8018 3.0814 3.0590 0.4851  -0.4645 -0.5602 140  GLU D C   
9929  O  O   . GLU D  142 ? 2.7511 2.9941 3.0447 0.5041  -0.4597 -0.5194 140  GLU D O   
9930  C  CB  . GLU D  142 ? 2.8625 3.2447 3.1676 0.5182  -0.4295 -0.6544 140  GLU D CB  
9931  C  CG  . GLU D  142 ? 2.9339 3.4141 3.2242 0.5259  -0.4193 -0.6888 140  GLU D CG  
9932  C  CD  . GLU D  142 ? 3.0218 3.5020 3.3780 0.5551  -0.3869 -0.7574 140  GLU D CD  
9933  O  OE1 . GLU D  142 ? 3.0640 3.4622 3.4769 0.5657  -0.3718 -0.7810 140  GLU D OE1 
9934  O  OE2 . GLU D  142 ? 3.0496 3.6089 3.4017 0.5669  -0.3732 -0.7883 140  GLU D OE2 
9935  N  N   . LEU D  143 ? 2.8750 3.1193 3.1078 0.4620  -0.4737 -0.5804 141  LEU D N   
9936  C  CA  . LEU D  143 ? 2.9616 3.1192 3.2054 0.4532  -0.4779 -0.5541 141  LEU D CA  
9937  C  C   . LEU D  143 ? 3.0612 3.1655 3.3654 0.4569  -0.4578 -0.6122 141  LEU D C   
9938  O  O   . LEU D  143 ? 3.2936 3.4356 3.6038 0.4516  -0.4522 -0.6779 141  LEU D O   
9939  C  CB  . LEU D  143 ? 2.9403 3.0969 3.1117 0.4222  -0.5029 -0.5253 141  LEU D CB  
9940  C  CG  . LEU D  143 ? 2.8372 2.9120 3.0082 0.4112  -0.5083 -0.4896 141  LEU D CG  
9941  C  CD1 . LEU D  143 ? 2.7466 2.7877 2.9296 0.4248  -0.5070 -0.4295 141  LEU D CD1 
9942  C  CD2 . LEU D  143 ? 2.8616 2.9427 2.9618 0.3839  -0.5295 -0.4701 141  LEU D CD2 
9943  N  N   . TYR D  144 ? 2.9536 2.9723 3.3026 0.4647  -0.4454 -0.5888 142  TYR D N   
9944  C  CA  . TYR D  144 ? 2.9420 2.8969 3.3581 0.4656  -0.4204 -0.6394 142  TYR D CA  
9945  C  C   . TYR D  144 ? 2.7920 2.6734 3.2079 0.4462  -0.4240 -0.6119 142  TYR D C   
9946  O  O   . TYR D  144 ? 2.6903 2.5596 3.0601 0.4395  -0.4422 -0.5485 142  TYR D O   
9947  C  CB  . TYR D  144 ? 2.9953 2.9084 3.4867 0.5023  -0.3871 -0.6431 142  TYR D CB  
9948  C  CG  . TYR D  144 ? 2.9655 2.9487 3.4696 0.5229  -0.3765 -0.6842 142  TYR D CG  
9949  C  CD1 . TYR D  144 ? 3.0022 2.9963 3.5419 0.5201  -0.3565 -0.7703 142  TYR D CD1 
9950  C  CD2 . TYR D  144 ? 2.8927 2.9370 3.3736 0.5431  -0.3858 -0.6404 142  TYR D CD2 
9951  C  CE1 . TYR D  144 ? 3.0233 3.0831 3.5718 0.5397  -0.3442 -0.8103 142  TYR D CE1 
9952  C  CE2 . TYR D  144 ? 2.9718 3.0847 3.4663 0.5623  -0.3734 -0.6776 142  TYR D CE2 
9953  C  CZ  . TYR D  144 ? 3.0117 3.1302 3.5381 0.5620  -0.3518 -0.7618 142  TYR D CZ  
9954  O  OH  . TYR D  144 ? 3.0606 3.2487 3.5979 0.5822  -0.3369 -0.8009 142  TYR D OH  
9955  N  N   . GLN D  145 ? 2.8994 2.7327 3.3701 0.4354  -0.4041 -0.6640 143  GLN D N   
9956  C  CA  . GLN D  145 ? 2.9092 2.6740 3.3939 0.4155  -0.4007 -0.6487 143  GLN D CA  
9957  C  C   . GLN D  145 ? 2.9545 2.6254 3.5257 0.4289  -0.3602 -0.6591 143  GLN D C   
9958  O  O   . GLN D  145 ? 3.0483 2.7118 3.6745 0.4439  -0.3344 -0.7092 143  GLN D O   
9959  C  CB  . GLN D  145 ? 3.0048 2.8095 3.4754 0.3821  -0.4153 -0.7048 143  GLN D CB  
9960  C  CG  . GLN D  145 ? 3.0194 2.7705 3.5003 0.3590  -0.4148 -0.6887 143  GLN D CG  
9961  C  CD  . GLN D  145 ? 3.0025 2.8032 3.4879 0.3296  -0.4262 -0.7541 143  GLN D CD  
9962  O  OE1 . GLN D  145 ? 3.0171 2.9014 3.4776 0.3267  -0.4415 -0.8015 143  GLN D OE1 
9963  N  NE2 . GLN D  145 ? 2.9378 2.6943 3.4554 0.3084  -0.4184 -0.7564 143  GLN D NE2 
9964  N  N   . LYS D  146 ? 2.8657 2.4610 3.4486 0.4242  -0.3510 -0.6115 144  LYS D N   
9965  C  CA  . LYS D  146 ? 2.8614 2.3570 3.5238 0.4373  -0.3084 -0.6098 144  LYS D CA  
9966  C  C   . LYS D  146 ? 2.9226 2.3858 3.6443 0.4044  -0.2871 -0.6847 144  LYS D C   
9967  O  O   . LYS D  146 ? 2.9331 2.3987 3.6388 0.3730  -0.2999 -0.6865 144  LYS D O   
9968  C  CB  . LYS D  146 ? 2.8414 2.2736 3.4872 0.4475  -0.3052 -0.5223 144  LYS D CB  
9969  C  CG  . LYS D  146 ? 2.8516 2.1772 3.5744 0.4673  -0.2578 -0.5053 144  LYS D CG  
9970  C  CD  . LYS D  146 ? 3.0200 2.2919 3.7164 0.4778  -0.2560 -0.4156 144  LYS D CD  
9971  C  CE  . LYS D  146 ? 3.2420 2.5153 3.9003 0.4379  -0.2729 -0.4112 144  LYS D CE  
9972  N  NZ  . LYS D  146 ? 3.3077 2.5351 4.0318 0.4054  -0.2454 -0.4723 144  LYS D NZ  
9973  N  N   . TYR D  147 ? 3.0414 2.4753 3.8352 0.4112  -0.2530 -0.7479 145  TYR D N   
9974  C  CA  . TYR D  147 ? 3.0452 2.4485 3.9068 0.3774  -0.2278 -0.8306 145  TYR D CA  
9975  C  C   . TYR D  147 ? 3.1606 2.4410 4.1122 0.3912  -0.1712 -0.8288 145  TYR D C   
9976  O  O   . TYR D  147 ? 3.2665 2.5119 4.2429 0.4319  -0.1476 -0.8098 145  TYR D O   
9977  C  CB  . TYR D  147 ? 3.0303 2.5167 3.8949 0.3655  -0.2364 -0.9267 145  TYR D CB  
9978  C  CG  . TYR D  147 ? 3.1004 2.6958 3.8972 0.3368  -0.2834 -0.9498 145  TYR D CG  
9979  C  CD1 . TYR D  147 ? 3.0850 2.6982 3.9044 0.2954  -0.2885 -1.0023 145  TYR D CD1 
9980  C  CD2 . TYR D  147 ? 3.2056 2.8878 3.9181 0.3521  -0.3210 -0.9165 145  TYR D CD2 
9981  C  CE1 . TYR D  147 ? 3.1262 2.8426 3.8840 0.2758  -0.3312 -1.0172 145  TYR D CE1 
9982  C  CE2 . TYR D  147 ? 3.1969 2.9720 3.8464 0.3306  -0.3601 -0.9307 145  TYR D CE2 
9983  C  CZ  . TYR D  147 ? 3.1416 2.9345 3.8127 0.2955  -0.3659 -0.9789 145  TYR D CZ  
9984  O  OH  . TYR D  147 ? 2.9932 2.8830 3.6007 0.2811  -0.4049 -0.9864 145  TYR D OH  
9985  N  N   . SER D  148 ? 3.0841 2.2990 4.0870 0.3588  -0.1469 -0.8458 146  SER D N   
9986  C  CA  . SER D  148 ? 3.0226 2.1083 4.1121 0.3670  -0.0877 -0.8377 146  SER D CA  
9987  C  C   . SER D  148 ? 3.0828 2.1032 4.1560 0.4161  -0.0746 -0.7285 146  SER D C   
9988  O  O   . SER D  148 ? 2.8819 1.8008 4.0204 0.4419  -0.0244 -0.7113 146  SER D O   
9989  C  CB  . SER D  148 ? 2.8400 1.8947 4.0054 0.3701  -0.0481 -0.9257 146  SER D CB  
9990  O  OG  . SER D  148 ? 2.8062 1.9224 3.9911 0.3212  -0.0581 -1.0321 146  SER D OG  
9991  N  N   . GLN D  149 ? 3.3322 2.4135 4.3182 0.4306  -0.1189 -0.6559 147  GLN D N   
9992  C  CA  . GLN D  149 ? 3.3791 2.4204 4.3349 0.4716  -0.1168 -0.5491 147  GLN D CA  
9993  C  C   . GLN D  149 ? 3.3829 2.4157 4.3579 0.5269  -0.1010 -0.5247 147  GLN D C   
9994  O  O   . GLN D  149 ? 3.3643 2.3609 4.3293 0.5677  -0.0925 -0.4387 147  GLN D O   
9995  C  CB  . GLN D  149 ? 3.4001 2.3320 4.3968 0.4638  -0.0774 -0.5054 147  GLN D CB  
9996  C  CG  . GLN D  149 ? 3.1772 2.1348 4.1293 0.4224  -0.1030 -0.4926 147  GLN D CG  
9997  C  CD  . GLN D  149 ? 3.1942 2.0537 4.1715 0.4199  -0.0666 -0.4327 147  GLN D CD  
9998  O  OE1 . GLN D  149 ? 3.3893 2.1735 4.3874 0.4594  -0.0339 -0.3692 147  GLN D OE1 
9999  N  NE2 . GLN D  149 ? 3.1070 1.9710 4.0828 0.3757  -0.0708 -0.4499 147  GLN D NE2 
10000 N  N   . ASN D  150 ? 3.1264 2.2031 4.1251 0.5302  -0.0991 -0.5988 148  ASN D N   
10001 C  CA  . ASN D  150 ? 2.8874 1.9557 3.9211 0.5811  -0.0763 -0.5949 148  ASN D CA  
10002 C  C   . ASN D  150 ? 2.8359 2.0089 3.8479 0.5754  -0.1008 -0.6685 148  ASN D C   
10003 O  O   . ASN D  150 ? 2.8557 2.0836 3.8476 0.6143  -0.1123 -0.6418 148  ASN D O   
10004 C  CB  . ASN D  150 ? 2.8420 1.7798 3.9763 0.5945  -0.0087 -0.6161 148  ASN D CB  
10005 C  CG  . ASN D  150 ? 2.6871 1.5149 3.8398 0.6134  0.0219  -0.5199 148  ASN D CG  
10006 O  OD1 . ASN D  150 ? 2.6630 1.5080 3.7661 0.6493  0.0023  -0.4223 148  ASN D OD1 
10007 N  ND2 . ASN D  150 ? 2.7991 1.5212 4.0212 0.5832  0.0695  -0.5531 148  ASN D ND2 
10008 N  N   . SER D  151 ? 2.9607 2.1724 3.9737 0.5282  -0.1102 -0.7587 149  SER D N   
10009 C  CA  . SER D  151 ? 2.9874 2.3009 3.9755 0.5245  -0.1308 -0.8277 149  SER D CA  
10010 C  C   . SER D  151 ? 2.9678 2.3940 3.8569 0.5080  -0.1902 -0.7985 149  SER D C   
10011 O  O   . SER D  151 ? 3.0103 2.4364 3.8587 0.4826  -0.2144 -0.7603 149  SER D O   
10012 C  CB  . SER D  151 ? 2.9876 2.2996 4.0224 0.4845  -0.1123 -0.9431 149  SER D CB  
10013 O  OG  . SER D  151 ? 2.9724 2.1663 4.1023 0.4912  -0.0529 -0.9733 149  SER D OG  
10014 N  N   . TRP D  152 ? 3.0980 2.6175 3.9495 0.5233  -0.2101 -0.8154 150  TRP D N   
10015 C  CA  . TRP D  152 ? 2.9991 2.6210 3.7588 0.5104  -0.2605 -0.7854 150  TRP D CA  
10016 C  C   . TRP D  152 ? 3.0029 2.7175 3.7357 0.4875  -0.2763 -0.8683 150  TRP D C   
10017 O  O   . TRP D  152 ? 3.2418 2.9733 4.0114 0.5015  -0.2531 -0.9306 150  TRP D O   
10018 C  CB  . TRP D  152 ? 3.0028 2.6621 3.7325 0.5497  -0.2723 -0.7126 150  TRP D CB  
10019 C  CG  . TRP D  152 ? 3.0067 2.5858 3.7634 0.5794  -0.2562 -0.6313 150  TRP D CG  
10020 C  CD1 . TRP D  152 ? 3.0788 2.5915 3.9057 0.6224  -0.2161 -0.6161 150  TRP D CD1 
10021 C  CD2 . TRP D  152 ? 2.9541 2.5143 3.6644 0.5714  -0.2787 -0.5525 150  TRP D CD2 
10022 N  NE1 . TRP D  152 ? 3.0174 2.4759 3.8421 0.6427  -0.2140 -0.5289 150  TRP D NE1 
10023 C  CE2 . TRP D  152 ? 2.9783 2.4666 3.7306 0.6104  -0.2526 -0.4912 150  TRP D CE2 
10024 C  CE3 . TRP D  152 ? 2.8816 2.4780 3.5181 0.5370  -0.3165 -0.5277 150  TRP D CE3 
10025 C  CZ2 . TRP D  152 ? 2.9667 2.4256 3.6848 0.6137  -0.2652 -0.4089 150  TRP D CZ2 
10026 C  CZ3 . TRP D  152 ? 2.8223 2.3830 3.4283 0.5391  -0.3267 -0.4501 150  TRP D CZ3 
10027 C  CH2 . TRP D  152 ? 2.8355 2.3317 3.4801 0.5761  -0.3023 -0.3927 150  TRP D CH2 
10028 N  N   . ARG D  153 ? 2.8051 2.5803 3.4729 0.4547  -0.3137 -0.8687 151  ARG D N   
10029 C  CA  . ARG D  153 ? 2.8003 2.6713 3.4330 0.4338  -0.3322 -0.9394 151  ARG D CA  
10030 C  C   . ARG D  153 ? 2.8212 2.7837 3.3626 0.4354  -0.3704 -0.8933 151  ARG D C   
10031 O  O   . ARG D  153 ? 2.8165 2.7685 3.3124 0.4305  -0.3925 -0.8211 151  ARG D O   
10032 C  CB  . ARG D  153 ? 2.7441 2.6140 3.3874 0.3933  -0.3396 -0.9913 151  ARG D CB  
10033 C  CG  . ARG D  153 ? 2.8740 2.8507 3.4827 0.3740  -0.3592 -1.0672 151  ARG D CG  
10034 C  CD  . ARG D  153 ? 3.0346 3.0282 3.6482 0.3355  -0.3743 -1.1065 151  ARG D CD  
10035 N  NE  . ARG D  153 ? 3.1831 3.2949 3.7516 0.3212  -0.3992 -1.1688 151  ARG D NE  
10036 C  CZ  . ARG D  153 ? 3.1974 3.3912 3.6821 0.3194  -0.4371 -1.1329 151  ARG D CZ  
10037 N  NH1 . ARG D  153 ? 3.1893 3.3554 3.6284 0.3272  -0.4535 -1.0407 151  ARG D NH1 
10038 N  NH2 . ARG D  153 ? 3.1187 3.4219 3.5640 0.3105  -0.4569 -1.1891 151  ARG D NH2 
10039 N  N   . TYR D  154 ? 2.7587 2.8088 3.2734 0.4406  -0.3750 -0.9382 152  TYR D N   
10040 C  CA  . TYR D  154 ? 2.7548 2.8940 3.1865 0.4416  -0.4044 -0.9008 152  TYR D CA  
10041 C  C   . TYR D  154 ? 2.6812 2.8469 3.0486 0.4130  -0.4380 -0.8769 152  TYR D C   
10042 O  O   . TYR D  154 ? 2.6242 2.7776 3.0073 0.3907  -0.4419 -0.9157 152  TYR D O   
10043 C  CB  . TYR D  154 ? 3.0253 3.2540 3.4436 0.4490  -0.3982 -0.9656 152  TYR D CB  
10044 C  CG  . TYR D  154 ? 3.0299 3.3514 3.3668 0.4508  -0.4211 -0.9291 152  TYR D CG  
10045 C  CD1 . TYR D  154 ? 3.0352 3.3752 3.3665 0.4740  -0.4153 -0.8802 152  TYR D CD1 
10046 C  CD2 . TYR D  154 ? 2.9415 3.3352 3.2097 0.4299  -0.4467 -0.9429 152  TYR D CD2 
10047 C  CE1 . TYR D  154 ? 2.9157 3.3380 3.1772 0.4710  -0.4318 -0.8482 152  TYR D CE1 
10048 C  CE2 . TYR D  154 ? 2.8239 3.2943 3.0183 0.4313  -0.4622 -0.9061 152  TYR D CE2 
10049 C  CZ  . TYR D  154 ? 2.8112 3.2929 3.0036 0.4493  -0.4534 -0.8603 152  TYR D CZ  
10050 O  OH  . TYR D  154 ? 2.6840 3.2395 2.8073 0.4463  -0.4647 -0.8247 152  TYR D OH  
10051 N  N   . LEU D  155 ? 2.8235 3.0254 3.1217 0.4137  -0.4605 -0.8117 153  LEU D N   
10052 C  CA  . LEU D  155 ? 2.7582 2.9867 2.9889 0.3920  -0.4896 -0.7832 153  LEU D CA  
10053 C  C   . LEU D  155 ? 2.7242 3.0456 2.8799 0.3928  -0.5053 -0.7721 153  LEU D C   
10054 O  O   . LEU D  155 ? 2.6873 3.0803 2.8192 0.3880  -0.5114 -0.8229 153  LEU D O   
10055 C  CB  . LEU D  155 ? 2.7154 2.8739 2.9322 0.3872  -0.4981 -0.7059 153  LEU D CB  
10056 C  CG  . LEU D  155 ? 2.7451 2.8119 3.0257 0.3832  -0.4829 -0.7086 153  LEU D CG  
10057 C  CD1 . LEU D  155 ? 2.7358 2.7453 2.9890 0.3784  -0.4926 -0.6317 153  LEU D CD1 
10058 C  CD2 . LEU D  155 ? 2.6855 2.7611 2.9899 0.3625  -0.4842 -0.7714 153  LEU D CD2 
10059 N  N   . SER D  156 ? 2.7091 3.0334 2.8266 0.3975  -0.5111 -0.7061 154  SER D N   
10060 C  CA  . SER D  156 ? 2.6822 3.0852 2.7301 0.3956  -0.5210 -0.6864 154  SER D CA  
10061 C  C   . SER D  156 ? 2.7058 3.1284 2.7646 0.4104  -0.5087 -0.6584 154  SER D C   
10062 O  O   . SER D  156 ? 2.7725 3.1502 2.8896 0.4256  -0.4953 -0.6500 154  SER D O   
10063 C  CB  . SER D  156 ? 2.5497 2.9432 2.5283 0.3776  -0.5423 -0.6296 154  SER D CB  
10064 O  OG  . SER D  156 ? 2.5084 2.8351 2.4906 0.3731  -0.5445 -0.5693 154  SER D OG  
10065 N  N   . ASN D  157 ? 2.5874 3.0825 2.5909 0.4071  -0.5119 -0.6421 155  ASN D N   
10066 C  CA  . ASN D  157 ? 2.5654 3.0987 2.5748 0.4168  -0.5013 -0.6150 155  ASN D CA  
10067 C  C   . ASN D  157 ? 2.4769 3.0443 2.4119 0.3967  -0.5124 -0.5608 155  ASN D C   
10068 O  O   . ASN D  157 ? 2.4903 3.0688 2.3662 0.3828  -0.5234 -0.5556 155  ASN D O   
10069 C  CB  . ASN D  157 ? 2.7262 3.3289 2.7618 0.4367  -0.4807 -0.6722 155  ASN D CB  
10070 C  CG  . ASN D  157 ? 2.8489 3.5260 2.8242 0.4292  -0.4840 -0.7052 155  ASN D CG  
10071 O  OD1 . ASN D  157 ? 2.8431 3.5800 2.7634 0.4223  -0.4841 -0.6762 155  ASN D OD1 
10072 N  ND2 . ASN D  157 ? 2.8714 3.5483 2.8565 0.4295  -0.4860 -0.7656 155  ASN D ND2 
10073 N  N   . ARG D  158 ? 2.6806 3.2666 2.6212 0.3954  -0.5079 -0.5202 156  ARG D N   
10074 C  CA  . ARG D  158 ? 2.6813 3.2928 2.5581 0.3711  -0.5138 -0.4697 156  ARG D CA  
10075 C  C   . ARG D  158 ? 2.8326 3.5021 2.7312 0.3729  -0.5023 -0.4496 156  ARG D C   
10076 O  O   . ARG D  158 ? 2.9286 3.5853 2.8847 0.3867  -0.5007 -0.4411 156  ARG D O   
10077 C  CB  . ARG D  158 ? 2.5548 3.0897 2.4041 0.3499  -0.5307 -0.4213 156  ARG D CB  
10078 C  CG  . ARG D  158 ? 2.5245 3.0685 2.3027 0.3215  -0.5339 -0.3748 156  ARG D CG  
10079 C  CD  . ARG D  158 ? 2.4900 2.9528 2.2337 0.3046  -0.5481 -0.3428 156  ARG D CD  
10080 N  NE  . ARG D  158 ? 2.5703 3.0055 2.3123 0.3162  -0.5550 -0.3732 156  ARG D NE  
10081 C  CZ  . ARG D  158 ? 2.5685 2.9379 2.2904 0.3080  -0.5657 -0.3553 156  ARG D CZ  
10082 N  NH1 . ARG D  158 ? 2.4308 2.7485 2.1275 0.2884  -0.5697 -0.3085 156  ARG D NH1 
10083 N  NH2 . ARG D  158 ? 2.6466 3.0067 2.3751 0.3184  -0.5717 -0.3871 156  ARG D NH2 
10084 N  N   . LEU D  159 ? 2.8763 3.6134 2.7304 0.3604  -0.4930 -0.4401 157  LEU D N   
10085 C  CA  . LEU D  159 ? 2.8639 3.6645 2.7355 0.3548  -0.4814 -0.4172 157  LEU D CA  
10086 C  C   . LEU D  159 ? 2.9608 3.7302 2.8055 0.3214  -0.4931 -0.3590 157  LEU D C   
10087 O  O   . LEU D  159 ? 2.8268 3.5375 2.6188 0.3003  -0.5039 -0.3355 157  LEU D O   
10088 C  CB  . LEU D  159 ? 2.8151 3.7022 2.6512 0.3528  -0.4620 -0.4314 157  LEU D CB  
10089 C  CG  . LEU D  159 ? 2.8394 3.8138 2.7106 0.3556  -0.4428 -0.4266 157  LEU D CG  
10090 C  CD1 . LEU D  159 ? 2.8620 3.8589 2.8152 0.3947  -0.4333 -0.4675 157  LEU D CD1 
10091 C  CD2 . LEU D  159 ? 2.9317 3.9825 2.7513 0.3470  -0.4220 -0.4310 157  LEU D CD2 
10092 N  N   . LEU D  160 ? 3.1753 3.9864 3.0594 0.3174  -0.4905 -0.3382 158  LEU D N   
10093 C  CA  . LEU D  160 ? 2.9674 3.7560 2.8372 0.2849  -0.5029 -0.2909 158  LEU D CA  
10094 C  C   . LEU D  160 ? 2.9627 3.8244 2.8125 0.2535  -0.4893 -0.2688 158  LEU D C   
10095 O  O   . LEU D  160 ? 3.0826 4.0298 2.9620 0.2658  -0.4718 -0.2856 158  LEU D O   
10096 C  CB  . LEU D  160 ? 2.7998 3.5796 2.7334 0.3031  -0.5153 -0.2814 158  LEU D CB  
10097 C  CG  . LEU D  160 ? 2.7027 3.3865 2.6429 0.3181  -0.5301 -0.2826 158  LEU D CG  
10098 C  CD1 . LEU D  160 ? 2.7043 3.3631 2.6683 0.3515  -0.5213 -0.3293 158  LEU D CD1 
10099 C  CD2 . LEU D  160 ? 2.8135 3.4917 2.8027 0.3315  -0.5419 -0.2584 158  LEU D CD2 
10100 N  N   . ALA D  161 ? 2.8907 3.7161 2.6925 0.2114  -0.4944 -0.2323 159  ALA D N   
10101 C  CA  . ALA D  161 ? 2.9644 3.8389 2.7405 0.1711  -0.4787 -0.2081 159  ALA D CA  
10102 C  C   . ALA D  161 ? 2.9343 3.8331 2.7422 0.1426  -0.4897 -0.1847 159  ALA D C   
10103 O  O   . ALA D  161 ? 2.8936 3.7403 2.7106 0.1436  -0.5116 -0.1753 159  ALA D O   
10104 C  CB  . ALA D  161 ? 3.0475 3.8567 2.7418 0.1417  -0.4710 -0.1856 159  ALA D CB  
10105 N  N   . PRO D  162 ? 3.0559 4.0404 2.8811 0.1154  -0.4745 -0.1757 160  PRO D N   
10106 C  CA  . PRO D  162 ? 3.0660 4.0941 2.9274 0.0863  -0.4870 -0.1585 160  PRO D CA  
10107 C  C   . PRO D  162 ? 2.8807 3.8331 2.6906 0.0368  -0.4960 -0.1342 160  PRO D C   
10108 O  O   . PRO D  162 ? 2.8036 3.7711 2.5888 -0.0138 -0.4800 -0.1199 160  PRO D O   
10109 C  CB  . PRO D  162 ? 3.1888 4.3316 3.0798 0.0666  -0.4630 -0.1592 160  PRO D CB  
10110 C  CG  . PRO D  162 ? 3.2139 4.3402 3.0517 0.0651  -0.4351 -0.1630 160  PRO D CG  
10111 C  CD  . PRO D  162 ? 3.1492 4.2068 2.9675 0.1124  -0.4448 -0.1833 160  PRO D CD  
10112 N  N   . SER D  163 ? 2.8114 3.6807 2.6068 0.0499  -0.5186 -0.1308 161  SER D N   
10113 C  CA  . SER D  163 ? 2.7603 3.5574 2.5100 0.0070  -0.5279 -0.1119 161  SER D CA  
10114 C  C   . SER D  163 ? 2.6981 3.5606 2.4902 -0.0132 -0.5471 -0.1058 161  SER D C   
10115 O  O   . SER D  163 ? 2.6226 3.5169 2.4626 0.0246  -0.5675 -0.1086 161  SER D O   
10116 C  CB  . SER D  163 ? 2.6980 3.3838 2.4132 0.0302  -0.5418 -0.1110 161  SER D CB  
10117 O  OG  . SER D  163 ? 2.6944 3.3148 2.3700 -0.0077 -0.5508 -0.0953 161  SER D OG  
10118 N  N   . ASP D  164 ? 2.8876 3.7722 2.6627 -0.0727 -0.5393 -0.0973 162  ASP D N   
10119 C  CA  . ASP D  164 ? 2.9016 3.8570 2.7114 -0.1000 -0.5595 -0.0947 162  ASP D CA  
10120 C  C   . ASP D  164 ? 2.8872 3.7636 2.6625 -0.1071 -0.5836 -0.0878 162  ASP D C   
10121 O  O   . ASP D  164 ? 2.9986 3.9338 2.8013 -0.1150 -0.6076 -0.0854 162  ASP D O   
10122 C  CB  . ASP D  164 ? 2.9994 4.0075 2.8054 -0.1685 -0.5400 -0.0943 162  ASP D CB  
10123 C  CG  . ASP D  164 ? 3.0008 4.0870 2.8361 -0.1650 -0.5110 -0.0983 162  ASP D CG  
10124 O  OD1 . ASP D  164 ? 2.9218 4.1228 2.8259 -0.1365 -0.5167 -0.1056 162  ASP D OD1 
10125 O  OD2 . ASP D  164 ? 3.0291 4.0622 2.8171 -0.1883 -0.4803 -0.0921 162  ASP D OD2 
10126 N  N   . SER D  165 ? 2.8104 3.5625 2.5263 -0.1021 -0.5775 -0.0840 163  SER D N   
10127 C  CA  . SER D  165 ? 2.8563 3.5195 2.5296 -0.1107 -0.5933 -0.0779 163  SER D CA  
10128 C  C   . SER D  165 ? 2.9347 3.5341 2.6095 -0.0514 -0.6041 -0.0761 163  SER D C   
10129 O  O   . SER D  165 ? 2.8990 3.5000 2.5932 -0.0115 -0.5947 -0.0833 163  SER D O   
10130 C  CB  . SER D  165 ? 2.8212 3.3860 2.4238 -0.1592 -0.5715 -0.0743 163  SER D CB  
10131 O  OG  . SER D  165 ? 2.7928 3.2971 2.3676 -0.1365 -0.5498 -0.0707 163  SER D OG  
10132 N  N   . PRO D  166 ? 2.8836 3.4294 2.5393 -0.0458 -0.6225 -0.0689 164  PRO D N   
10133 C  CA  . PRO D  166 ? 2.8452 3.3207 2.5016 0.0046  -0.6283 -0.0668 164  PRO D CA  
10134 C  C   . PRO D  166 ? 2.8596 3.2451 2.4733 0.0085  -0.6089 -0.0716 164  PRO D C   
10135 O  O   . PRO D  166 ? 2.8849 3.2119 2.4439 -0.0290 -0.5960 -0.0672 164  PRO D O   
10136 C  CB  . PRO D  166 ? 2.7859 3.2213 2.4172 -0.0042 -0.6469 -0.0551 164  PRO D CB  
10137 C  CG  . PRO D  166 ? 2.7718 3.2255 2.3682 -0.0672 -0.6462 -0.0569 164  PRO D CG  
10138 C  CD  . PRO D  166 ? 2.7432 3.3005 2.3796 -0.0850 -0.6387 -0.0643 164  PRO D CD  
10139 N  N   . GLU D  167 ? 2.9216 3.3001 2.5625 0.0549  -0.6058 -0.0816 165  GLU D N   
10140 C  CA  . GLU D  167 ? 3.0248 3.3424 2.6335 0.0657  -0.5908 -0.0888 165  GLU D CA  
10141 C  C   . GLU D  167 ? 3.0699 3.3159 2.6813 0.1001  -0.5984 -0.0927 165  GLU D C   
10142 O  O   . GLU D  167 ? 3.1269 3.3829 2.7809 0.1281  -0.6104 -0.0937 165  GLU D O   
10143 C  CB  . GLU D  167 ? 3.0871 3.4713 2.7235 0.0849  -0.5779 -0.1049 165  GLU D CB  
10144 C  CG  . GLU D  167 ? 3.2770 3.6249 2.8679 0.0839  -0.5605 -0.1076 165  GLU D CG  
10145 C  CD  . GLU D  167 ? 3.3803 3.8066 2.9923 0.0990  -0.5468 -0.1232 165  GLU D CD  
10146 O  OE1 . GLU D  167 ? 3.3408 3.8472 3.0049 0.1071  -0.5489 -0.1321 165  GLU D OE1 
10147 O  OE2 . GLU D  167 ? 3.4519 3.8644 3.0276 0.1047  -0.5334 -0.1255 165  GLU D OE2 
10148 N  N   . TRP D  168 ? 2.8941 3.0688 2.4617 0.0987  -0.5894 -0.0925 166  TRP D N   
10149 C  CA  . TRP D  168 ? 2.7679 2.8759 2.3370 0.1257  -0.5940 -0.0974 166  TRP D CA  
10150 C  C   . TRP D  168 ? 2.7028 2.8173 2.2797 0.1524  -0.5864 -0.1183 166  TRP D C   
10151 O  O   . TRP D  168 ? 2.7461 2.8571 2.2824 0.1419  -0.5752 -0.1149 166  TRP D O   
10152 C  CB  . TRP D  168 ? 3.0072 3.0305 2.5203 0.1025  -0.5915 -0.0802 166  TRP D CB  
10153 C  CG  . TRP D  168 ? 3.0614 3.0243 2.5826 0.1235  -0.5980 -0.0796 166  TRP D CG  
10154 C  CD1 . TRP D  168 ? 3.2787 3.2052 2.8078 0.1491  -0.5949 -0.0910 166  TRP D CD1 
10155 C  CD2 . TRP D  168 ? 2.9691 2.9068 2.4917 0.1196  -0.6076 -0.0665 166  TRP D CD2 
10156 N  NE1 . TRP D  168 ? 3.2983 3.1741 2.8370 0.1594  -0.5992 -0.0854 166  TRP D NE1 
10157 C  CE2 . TRP D  168 ? 3.1087 2.9887 2.6405 0.1432  -0.6065 -0.0686 166  TRP D CE2 
10158 C  CE3 . TRP D  168 ? 2.7834 2.7490 2.2999 0.0978  -0.6173 -0.0536 166  TRP D CE3 
10159 C  CZ2 . TRP D  168 ? 2.8881 2.7316 2.4199 0.1472  -0.6117 -0.0546 166  TRP D CZ2 
10160 C  CZ3 . TRP D  168 ? 2.7490 2.6837 2.2622 0.1036  -0.6257 -0.0407 166  TRP D CZ3 
10161 C  CH2 . TRP D  168 ? 2.7356 2.6066 2.2548 0.1287  -0.6214 -0.0395 166  TRP D CH2 
10162 N  N   . LEU D  169 ? 2.6726 2.7971 2.3006 0.1867  -0.5913 -0.1398 167  LEU D N   
10163 C  CA  . LEU D  169 ? 2.9120 3.0552 2.5557 0.2116  -0.5863 -0.1693 167  LEU D CA  
10164 C  C   . LEU D  169 ? 2.9980 3.0795 2.6463 0.2270  -0.5895 -0.1796 167  LEU D C   
10165 O  O   . LEU D  169 ? 3.0575 3.0783 2.6956 0.2201  -0.5934 -0.1613 167  LEU D O   
10166 C  CB  . LEU D  169 ? 2.7974 3.0063 2.5027 0.2365  -0.5845 -0.1958 167  LEU D CB  
10167 C  CG  . LEU D  169 ? 2.9147 3.2028 2.6134 0.2309  -0.5749 -0.2034 167  LEU D CG  
10168 C  CD1 . LEU D  169 ? 2.7492 3.0473 2.4105 0.2348  -0.5676 -0.2190 167  LEU D CD1 
10169 C  CD2 . LEU D  169 ? 3.1391 3.4446 2.8072 0.1958  -0.5735 -0.1713 167  LEU D CD2 
10170 N  N   . SER D  170 ? 2.8564 2.9607 2.5210 0.2470  -0.5872 -0.2116 168  SER D N   
10171 C  CA  . SER D  170 ? 2.6476 2.7100 2.3255 0.2600  -0.5899 -0.2284 168  SER D CA  
10172 C  C   . SER D  170 ? 2.5447 2.6569 2.2608 0.2815  -0.5883 -0.2760 168  SER D C   
10173 O  O   . SER D  170 ? 2.5161 2.6894 2.2139 0.2840  -0.5853 -0.2893 168  SER D O   
10174 C  CB  . SER D  170 ? 2.6292 2.6533 2.2485 0.2490  -0.5900 -0.2073 168  SER D CB  
10175 O  OG  . SER D  170 ? 2.7613 2.8322 2.3426 0.2498  -0.5863 -0.2094 168  SER D OG  
10176 N  N   . PHE D  171 ? 2.6382 2.7241 2.4068 0.2949  -0.5880 -0.3030 169  PHE D N   
10177 C  CA  . PHE D  171 ? 2.6541 2.7800 2.4663 0.3114  -0.5849 -0.3572 169  PHE D CA  
10178 C  C   . PHE D  171 ? 2.6161 2.7147 2.4399 0.3121  -0.5888 -0.3777 169  PHE D C   
10179 O  O   . PHE D  171 ? 2.6921 2.7290 2.5439 0.3100  -0.5862 -0.3678 169  PHE D O   
10180 C  CB  . PHE D  171 ? 2.7134 2.8374 2.5950 0.3264  -0.5751 -0.3792 169  PHE D CB  
10181 C  CG  . PHE D  171 ? 2.7622 2.9434 2.6462 0.3326  -0.5701 -0.3776 169  PHE D CG  
10182 C  CD1 . PHE D  171 ? 2.7689 3.0177 2.6627 0.3433  -0.5639 -0.4210 169  PHE D CD1 
10183 C  CD2 . PHE D  171 ? 2.8694 3.0445 2.7465 0.3272  -0.5714 -0.3349 169  PHE D CD2 
10184 C  CE1 . PHE D  171 ? 2.8816 3.1874 2.7806 0.3498  -0.5564 -0.4197 169  PHE D CE1 
10185 C  CE2 . PHE D  171 ? 2.9482 3.1858 2.8342 0.3323  -0.5664 -0.3339 169  PHE D CE2 
10186 C  CZ  . PHE D  171 ? 3.0054 3.3068 2.9035 0.3443  -0.5576 -0.3754 169  PHE D CZ  
10187 N  N   . ASP D  172 ? 2.5653 2.7171 2.3695 0.3160  -0.5946 -0.4059 170  ASP D N   
10188 C  CA  . ASP D  172 ? 2.6480 2.7958 2.4661 0.3170  -0.6007 -0.4297 170  ASP D CA  
10189 C  C   . ASP D  172 ? 2.7012 2.8394 2.5998 0.3206  -0.5931 -0.4824 170  ASP D C   
10190 O  O   . ASP D  172 ? 2.8298 3.0239 2.7556 0.3268  -0.5914 -0.5364 170  ASP D O   
10191 C  CB  . ASP D  172 ? 2.6151 2.8387 2.3898 0.3236  -0.6107 -0.4455 170  ASP D CB  
10192 C  CG  . ASP D  172 ? 2.5063 2.7329 2.2822 0.3254  -0.6205 -0.4540 170  ASP D CG  
10193 O  OD1 . ASP D  172 ? 2.4817 2.7338 2.3121 0.3260  -0.6230 -0.5075 170  ASP D OD1 
10194 O  OD2 . ASP D  172 ? 2.4561 2.6609 2.1814 0.3258  -0.6242 -0.4085 170  ASP D OD2 
10195 N  N   . VAL D  173 ? 2.6573 2.7222 2.5938 0.3158  -0.5857 -0.4681 171  VAL D N   
10196 C  CA  . VAL D  173 ? 2.7093 2.7488 2.7256 0.3167  -0.5727 -0.5126 171  VAL D CA  
10197 C  C   . VAL D  173 ? 2.6619 2.6832 2.6986 0.3066  -0.5751 -0.5249 171  VAL D C   
10198 O  O   . VAL D  173 ? 2.6683 2.6321 2.7609 0.3014  -0.5608 -0.5312 171  VAL D O   
10199 C  CB  . VAL D  173 ? 2.7692 2.7407 2.8213 0.3224  -0.5569 -0.4847 171  VAL D CB  
10200 C  CG1 . VAL D  173 ? 2.7011 2.7071 2.7537 0.3357  -0.5528 -0.4866 171  VAL D CG1 
10201 C  CG2 . VAL D  173 ? 2.8474 2.7630 2.8578 0.3160  -0.5607 -0.4193 171  VAL D CG2 
10202 N  N   . THR D  174 ? 2.6314 2.7047 2.6244 0.3055  -0.5914 -0.5258 172  THR D N   
10203 C  CA  . THR D  174 ? 2.6595 2.7299 2.6706 0.2984  -0.5957 -0.5344 172  THR D CA  
10204 C  C   . THR D  174 ? 2.7300 2.8156 2.8243 0.2892  -0.5874 -0.6028 172  THR D C   
10205 O  O   . THR D  174 ? 2.7776 2.8168 2.9204 0.2783  -0.5765 -0.6058 172  THR D O   
10206 C  CB  . THR D  174 ? 2.6576 2.7961 2.6089 0.3059  -0.6149 -0.5249 172  THR D CB  
10207 O  OG1 . THR D  174 ? 2.4616 2.5687 2.3399 0.3105  -0.6166 -0.4603 172  THR D OG1 
10208 C  CG2 . THR D  174 ? 2.7225 2.8717 2.6991 0.3021  -0.6202 -0.5353 172  THR D CG2 
10209 N  N   . GLY D  175 ? 2.6557 2.8058 2.7684 0.2913  -0.5897 -0.6608 173  GLY D N   
10210 C  CA  . GLY D  175 ? 2.6311 2.7954 2.8246 0.2783  -0.5794 -0.7347 173  GLY D CA  
10211 C  C   . GLY D  175 ? 2.6284 2.6962 2.8906 0.2722  -0.5504 -0.7347 173  GLY D C   
10212 O  O   . GLY D  175 ? 2.7148 2.7634 3.0498 0.2557  -0.5359 -0.7799 173  GLY D O   
10213 N  N   . VAL D  176 ? 2.5689 2.5774 2.8104 0.2852  -0.5407 -0.6825 174  VAL D N   
10214 C  CA  . VAL D  176 ? 2.5805 2.4978 2.8805 0.2864  -0.5129 -0.6702 174  VAL D CA  
10215 C  C   . VAL D  176 ? 2.6024 2.4531 2.9092 0.2770  -0.5060 -0.6254 174  VAL D C   
10216 O  O   . VAL D  176 ? 2.6713 2.4678 3.0464 0.2664  -0.4827 -0.6429 174  VAL D O   
10217 C  CB  . VAL D  176 ? 2.6083 2.5024 2.8834 0.3071  -0.5078 -0.6290 174  VAL D CB  
10218 C  CG1 . VAL D  176 ? 2.6497 2.4509 2.9772 0.3148  -0.4805 -0.6017 174  VAL D CG1 
10219 C  CG2 . VAL D  176 ? 2.7651 2.7226 3.0446 0.3173  -0.5080 -0.6782 174  VAL D CG2 
10220 N  N   . VAL D  177 ? 2.4379 2.2893 2.6742 0.2799  -0.5230 -0.5678 175  VAL D N   
10221 C  CA  . VAL D  177 ? 2.3354 2.1238 2.5677 0.2734  -0.5152 -0.5211 175  VAL D CA  
10222 C  C   . VAL D  177 ? 2.3185 2.1231 2.5973 0.2560  -0.5120 -0.5581 175  VAL D C   
10223 O  O   . VAL D  177 ? 2.3262 2.0712 2.6452 0.2465  -0.4920 -0.5443 175  VAL D O   
10224 C  CB  . VAL D  177 ? 2.3106 2.1001 2.4544 0.2793  -0.5328 -0.4600 175  VAL D CB  
10225 C  CG1 . VAL D  177 ? 2.3317 2.0558 2.4678 0.2734  -0.5224 -0.4148 175  VAL D CG1 
10226 C  CG2 . VAL D  177 ? 2.3223 2.1078 2.4275 0.2916  -0.5363 -0.4292 175  VAL D CG2 
10227 N  N   . ARG D  178 ? 2.3818 2.2740 2.6552 0.2520  -0.5315 -0.6033 176  ARG D N   
10228 C  CA  . ARG D  178 ? 2.3704 2.2971 2.6946 0.2349  -0.5314 -0.6445 176  ARG D CA  
10229 C  C   . ARG D  178 ? 2.4477 2.3364 2.8694 0.2162  -0.5033 -0.6962 176  ARG D C   
10230 O  O   . ARG D  178 ? 2.4377 2.2980 2.9123 0.1988  -0.4872 -0.7018 176  ARG D O   
10231 C  CB  . ARG D  178 ? 2.3754 2.4171 2.6758 0.2375  -0.5596 -0.6867 176  ARG D CB  
10232 C  CG  . ARG D  178 ? 2.4252 2.5281 2.7864 0.2191  -0.5635 -0.7418 176  ARG D CG  
10233 C  CD  . ARG D  178 ? 2.4835 2.7101 2.8058 0.2287  -0.5958 -0.7695 176  ARG D CD  
10234 N  NE  . ARG D  178 ? 2.3837 2.6232 2.6290 0.2497  -0.6127 -0.7040 176  ARG D NE  
10235 C  CZ  . ARG D  178 ? 2.3324 2.5761 2.4943 0.2706  -0.6240 -0.6608 176  ARG D CZ  
10236 N  NH1 . ARG D  178 ? 2.3382 2.5831 2.4833 0.2739  -0.6223 -0.6755 176  ARG D NH1 
10237 N  NH2 . ARG D  178 ? 2.2987 2.5441 2.3968 0.2878  -0.6341 -0.6035 176  ARG D NH2 
10238 N  N   . GLN D  179 ? 2.6682 2.5514 3.1170 0.2195  -0.4930 -0.7332 177  GLN D N   
10239 C  CA  . GLN D  179 ? 2.7229 2.5566 3.2659 0.2027  -0.4604 -0.7826 177  GLN D CA  
10240 C  C   . GLN D  179 ? 2.6365 2.3549 3.2041 0.2061  -0.4289 -0.7257 177  GLN D C   
10241 O  O   . GLN D  179 ? 2.6308 2.2960 3.2768 0.1875  -0.3979 -0.7498 177  GLN D O   
10242 C  CB  . GLN D  179 ? 2.8014 2.6521 3.3635 0.2104  -0.4538 -0.8339 177  GLN D CB  
10243 C  CG  . GLN D  179 ? 2.8948 2.8635 3.4374 0.2058  -0.4806 -0.8995 177  GLN D CG  
10244 C  CD  . GLN D  179 ? 2.8314 2.8140 3.3882 0.2153  -0.4707 -0.9489 177  GLN D CD  
10245 O  OE1 . GLN D  179 ? 2.7746 2.6759 3.3657 0.2261  -0.4418 -0.9370 177  GLN D OE1 
10246 N  NE2 . GLN D  179 ? 2.7509 2.8399 3.2801 0.2144  -0.4934 -1.0031 177  GLN D NE2 
10247 N  N   . TRP D  180 ? 2.6989 2.3802 3.2002 0.2285  -0.4354 -0.6507 178  TRP D N   
10248 C  CA  . TRP D  180 ? 2.8079 2.3905 3.3206 0.2355  -0.4088 -0.5909 178  TRP D CA  
10249 C  C   . TRP D  180 ? 2.7018 2.2594 3.2163 0.2204  -0.4024 -0.5616 178  TRP D C   
10250 O  O   . TRP D  180 ? 2.7503 2.2278 3.3003 0.2179  -0.3715 -0.5311 178  TRP D O   
10251 C  CB  . TRP D  180 ? 2.9072 2.4736 3.3468 0.2622  -0.4211 -0.5252 178  TRP D CB  
10252 C  CG  . TRP D  180 ? 2.9549 2.5220 3.4103 0.2813  -0.4149 -0.5412 178  TRP D CG  
10253 C  CD1 . TRP D  180 ? 3.0346 2.6073 3.5576 0.2782  -0.3977 -0.6075 178  TRP D CD1 
10254 C  CD2 . TRP D  180 ? 2.8725 2.4402 3.2776 0.3062  -0.4248 -0.4930 178  TRP D CD2 
10255 N  NE1 . TRP D  180 ? 3.0348 2.6078 3.5525 0.3035  -0.3945 -0.6009 178  TRP D NE1 
10256 C  CE2 . TRP D  180 ? 2.9758 2.5505 3.4234 0.3209  -0.4121 -0.5301 178  TRP D CE2 
10257 C  CE3 . TRP D  180 ? 2.7129 2.2788 3.0435 0.3158  -0.4422 -0.4256 178  TRP D CE3 
10258 C  CZ2 . TRP D  180 ? 2.9685 2.5546 3.3898 0.3472  -0.4170 -0.4982 178  TRP D CZ2 
10259 C  CZ3 . TRP D  180 ? 2.7058 2.2851 3.0105 0.3375  -0.4486 -0.3972 178  TRP D CZ3 
10260 C  CH2 . TRP D  180 ? 2.8749 2.4670 3.2262 0.3542  -0.4365 -0.4315 178  TRP D CH2 
10261 N  N   . LEU D  181 ? 2.5924 2.2177 3.0707 0.2128  -0.4284 -0.5686 179  LEU D N   
10262 C  CA  . LEU D  181 ? 2.6404 2.2500 3.1228 0.2008  -0.4214 -0.5435 179  LEU D CA  
10263 C  C   . LEU D  181 ? 2.6954 2.3194 3.2722 0.1724  -0.4023 -0.6023 179  LEU D C   
10264 O  O   . LEU D  181 ? 2.6526 2.2424 3.2571 0.1599  -0.3826 -0.5818 179  LEU D O   
10265 C  CB  . LEU D  181 ? 2.5500 2.2237 2.9574 0.2089  -0.4541 -0.5227 179  LEU D CB  
10266 C  CG  . LEU D  181 ? 2.5304 2.1632 2.8500 0.2259  -0.4610 -0.4475 179  LEU D CG  
10267 C  CD1 . LEU D  181 ? 2.5276 2.1326 2.8104 0.2415  -0.4641 -0.4226 179  LEU D CD1 
10268 C  CD2 . LEU D  181 ? 2.5486 2.2440 2.8049 0.2332  -0.4887 -0.4380 179  LEU D CD2 
10269 N  N   . SER D  182 ? 2.8703 2.5450 3.4985 0.1599  -0.4055 -0.6774 180  SER D N   
10270 C  CA  . SER D  182 ? 3.0380 2.7328 3.7622 0.1268  -0.3871 -0.7435 180  SER D CA  
10271 C  C   . SER D  182 ? 3.1553 2.7449 3.9563 0.1141  -0.3389 -0.7463 180  SER D C   
10272 O  O   . SER D  182 ? 3.2488 2.8172 4.1245 0.0855  -0.3117 -0.7683 180  SER D O   
10273 C  CB  . SER D  182 ? 3.1260 2.9219 3.8732 0.1157  -0.4093 -0.8294 180  SER D CB  
10274 O  OG  . SER D  182 ? 3.2431 3.0551 4.0914 0.0787  -0.3885 -0.9030 180  SER D OG  
10275 N  N   . ARG D  183 ? 3.1714 2.6953 3.9578 0.1359  -0.3255 -0.7219 181  ARG D N   
10276 C  CA  . ARG D  183 ? 3.2016 2.6155 4.0529 0.1330  -0.2769 -0.7094 181  ARG D CA  
10277 C  C   . ARG D  183 ? 3.3996 2.7355 4.2092 0.1511  -0.2619 -0.6147 181  ARG D C   
10278 O  O   . ARG D  183 ? 3.2767 2.6323 3.9974 0.1737  -0.2902 -0.5590 181  ARG D O   
10279 C  CB  . ARG D  183 ? 2.9362 2.3201 3.7993 0.1528  -0.2667 -0.7294 181  ARG D CB  
10280 C  CG  . ARG D  183 ? 2.9217 2.3821 3.8192 0.1368  -0.2794 -0.8262 181  ARG D CG  
10281 C  CD  . ARG D  183 ? 3.0708 2.4919 3.9825 0.1595  -0.2628 -0.8422 181  ARG D CD  
10282 N  NE  . ARG D  183 ? 3.1275 2.6375 4.0440 0.1512  -0.2829 -0.9272 181  ARG D NE  
10283 C  CZ  . ARG D  183 ? 3.0576 2.6447 3.8982 0.1736  -0.3202 -0.9221 181  ARG D CZ  
10284 N  NH1 . ARG D  183 ? 2.9375 2.5210 3.6967 0.2023  -0.3411 -0.8393 181  ARG D NH1 
10285 N  NH2 . ARG D  183 ? 3.0912 2.7605 3.9367 0.1654  -0.3349 -1.0013 181  ARG D NH2 
10286 N  N   . GLY D  184 ? 3.7082 2.9558 4.5822 0.1393  -0.2152 -0.5983 182  GLY D N   
10287 C  CA  . GLY D  184 ? 3.7922 2.9612 4.6303 0.1577  -0.1949 -0.5089 182  GLY D CA  
10288 C  C   . GLY D  184 ? 3.7874 2.8877 4.6059 0.1940  -0.1806 -0.4606 182  GLY D C   
10289 O  O   . GLY D  184 ? 3.9439 2.9630 4.7610 0.2087  -0.1497 -0.3951 182  GLY D O   
10290 N  N   . GLY D  185 ? 3.4448 2.5856 4.2445 0.2114  -0.2042 -0.4892 183  GLY D N   
10291 C  CA  . GLY D  185 ? 3.2272 2.3214 4.0119 0.2492  -0.1948 -0.4489 183  GLY D CA  
10292 C  C   . GLY D  185 ? 3.1907 2.2713 3.8895 0.2774  -0.2096 -0.3568 183  GLY D C   
10293 O  O   . GLY D  185 ? 3.2580 2.4046 3.8768 0.2822  -0.2514 -0.3411 183  GLY D O   
10294 N  N   . GLU D  186 ? 3.1169 2.1119 3.8306 0.2961  -0.1738 -0.2954 184  GLU D N   
10295 C  CA  . GLU D  186 ? 3.1168 2.0975 3.7519 0.3185  -0.1832 -0.2084 184  GLU D CA  
10296 C  C   . GLU D  186 ? 2.9410 1.9623 3.5114 0.3532  -0.2155 -0.1745 184  GLU D C   
10297 O  O   . GLU D  186 ? 2.9278 1.9596 3.4226 0.3672  -0.2331 -0.1123 184  GLU D O   
10298 C  CB  . GLU D  186 ? 3.1862 2.0668 3.8612 0.3291  -0.1316 -0.1539 184  GLU D CB  
10299 C  CG  . GLU D  186 ? 3.2832 2.1426 3.8821 0.3514  -0.1330 -0.0623 184  GLU D CG  
10300 C  CD  . GLU D  186 ? 3.1256 1.9747 3.6932 0.3989  -0.1370 -0.0036 184  GLU D CD  
10301 O  OE1 . GLU D  186 ? 3.0289 1.8526 3.6551 0.4190  -0.1193 -0.0219 184  GLU D OE1 
10302 O  OE2 . GLU D  186 ? 3.1464 2.0159 3.6325 0.4166  -0.1571 0.0593  184  GLU D OE2 
10303 N  N   . ILE D  187 ? 2.8773 1.9305 3.4736 0.3643  -0.2248 -0.2181 185  ILE D N   
10304 C  CA  . ILE D  187 ? 2.8063 1.9049 3.3505 0.3963  -0.2528 -0.1879 185  ILE D CA  
10305 C  C   . ILE D  187 ? 2.7496 1.9176 3.3045 0.3907  -0.2753 -0.2575 185  ILE D C   
10306 O  O   . ILE D  187 ? 2.8264 1.9793 3.4534 0.3823  -0.2537 -0.3197 185  ILE D O   
10307 C  CB  . ILE D  187 ? 2.9423 1.9825 3.5144 0.4390  -0.2239 -0.1332 185  ILE D CB  
10308 C  CG1 . ILE D  187 ? 2.8495 1.9537 3.3759 0.4712  -0.2551 -0.1076 185  ILE D CG1 
10309 C  CG2 . ILE D  187 ? 2.9740 1.9458 3.6490 0.4424  -0.1771 -0.1757 185  ILE D CG2 
10310 C  CD1 . ILE D  187 ? 2.7175 1.8809 3.1455 0.4660  -0.2963 -0.0640 185  ILE D CD1 
10311 N  N   . GLU D  188 ? 2.5925 1.8373 3.0744 0.3931  -0.3168 -0.2490 186  GLU D N   
10312 C  CA  . GLU D  188 ? 2.6060 1.9241 3.0848 0.3912  -0.3391 -0.3043 186  GLU D CA  
10313 C  C   . GLU D  188 ? 2.6173 1.9843 3.0426 0.4174  -0.3635 -0.2633 186  GLU D C   
10314 O  O   . GLU D  188 ? 2.6078 1.9555 3.0019 0.4361  -0.3647 -0.1965 186  GLU D O   
10315 C  CB  . GLU D  188 ? 2.7604 2.1368 3.2063 0.3577  -0.3654 -0.3483 186  GLU D CB  
10316 C  CG  . GLU D  188 ? 2.9582 2.3091 3.4639 0.3292  -0.3453 -0.3991 186  GLU D CG  
10317 C  CD  . GLU D  188 ? 2.7733 2.1282 3.3564 0.3246  -0.3262 -0.4758 186  GLU D CD  
10318 O  OE1 . GLU D  188 ? 2.6639 2.0475 3.2483 0.3449  -0.3305 -0.4925 186  GLU D OE1 
10319 O  OE2 . GLU D  188 ? 2.6810 2.0128 3.3256 0.2991  -0.3055 -0.5223 186  GLU D OE2 
10320 N  N   . GLY D  189 ? 2.6515 2.0892 3.0664 0.4175  -0.3828 -0.3045 187  GLY D N   
10321 C  CA  . GLY D  189 ? 2.6628 2.1578 3.0343 0.4377  -0.4048 -0.2730 187  GLY D CA  
10322 C  C   . GLY D  189 ? 2.6912 2.2565 3.0700 0.4380  -0.4150 -0.3294 187  GLY D C   
10323 O  O   . GLY D  189 ? 2.7115 2.2806 3.1295 0.4253  -0.4047 -0.3947 187  GLY D O   
10324 N  N   . PHE D  190 ? 2.6437 2.2706 2.9842 0.4514  -0.4348 -0.3046 188  PHE D N   
10325 C  CA  . PHE D  190 ? 2.6793 2.3817 3.0177 0.4537  -0.4441 -0.3486 188  PHE D CA  
10326 C  C   . PHE D  190 ? 2.9720 2.6982 3.3423 0.4911  -0.4349 -0.3292 188  PHE D C   
10327 O  O   . PHE D  190 ? 3.1527 2.8429 3.5409 0.5163  -0.4253 -0.2772 188  PHE D O   
10328 C  CB  . PHE D  190 ? 2.6564 2.4253 2.9143 0.4288  -0.4768 -0.3413 188  PHE D CB  
10329 C  CG  . PHE D  190 ? 2.8290 2.5880 3.0576 0.3982  -0.4859 -0.3641 188  PHE D CG  
10330 C  CD1 . PHE D  190 ? 2.9866 2.7851 3.2245 0.3867  -0.4874 -0.4268 188  PHE D CD1 
10331 C  CD2 . PHE D  190 ? 2.8176 2.5350 3.0087 0.3831  -0.4930 -0.3232 188  PHE D CD2 
10332 C  CE1 . PHE D  190 ? 2.9364 2.7376 3.1501 0.3628  -0.4977 -0.4452 188  PHE D CE1 
10333 C  CE2 . PHE D  190 ? 2.8048 2.5183 2.9734 0.3592  -0.5002 -0.3425 188  PHE D CE2 
10334 C  CZ  . PHE D  190 ? 2.8028 2.5606 2.9844 0.3502  -0.5035 -0.4020 188  PHE D CZ  
10335 N  N   . ARG D  191 ? 3.0849 2.8781 3.4619 0.4970  -0.4371 -0.3703 189  ARG D N   
10336 C  CA  . ARG D  191 ? 3.0659 2.8989 3.4746 0.5330  -0.4288 -0.3585 189  ARG D CA  
10337 C  C   . ARG D  191 ? 2.9723 2.9056 3.3388 0.5228  -0.4490 -0.3759 189  ARG D C   
10338 O  O   . ARG D  191 ? 2.9746 2.9386 3.3199 0.5004  -0.4540 -0.4264 189  ARG D O   
10339 C  CB  . ARG D  191 ? 3.1170 2.9083 3.6103 0.5610  -0.3913 -0.4039 189  ARG D CB  
10340 C  CG  . ARG D  191 ? 3.0536 2.8958 3.5824 0.6010  -0.3804 -0.4010 189  ARG D CG  
10341 C  CD  . ARG D  191 ? 3.1628 2.9794 3.7628 0.6195  -0.3444 -0.4696 189  ARG D CD  
10342 N  NE  . ARG D  191 ? 3.3092 3.1879 3.9385 0.6570  -0.3343 -0.4732 189  ARG D NE  
10343 C  CZ  . ARG D  191 ? 3.4786 3.3531 4.1653 0.6780  -0.3026 -0.5341 189  ARG D CZ  
10344 N  NH1 . ARG D  191 ? 3.5187 3.3301 4.2393 0.6612  -0.2791 -0.6001 189  ARG D NH1 
10345 N  NH2 . ARG D  191 ? 3.5259 3.4628 4.2380 0.7144  -0.2932 -0.5325 189  ARG D NH2 
10346 N  N   . LEU D  192 ? 2.9394 2.9289 3.2946 0.5393  -0.4598 -0.3330 190  LEU D N   
10347 C  CA  . LEU D  192 ? 2.9517 3.0385 3.2703 0.5284  -0.4756 -0.3418 190  LEU D CA  
10348 C  C   . LEU D  192 ? 3.0839 3.2248 3.4563 0.5680  -0.4608 -0.3426 190  LEU D C   
10349 O  O   . LEU D  192 ? 3.2303 3.3966 3.6136 0.5888  -0.4672 -0.2909 190  LEU D O   
10350 C  CB  . LEU D  192 ? 2.8118 2.9281 3.0598 0.5003  -0.5049 -0.2909 190  LEU D CB  
10351 C  CG  . LEU D  192 ? 2.7433 2.9451 2.9414 0.4756  -0.5197 -0.2993 190  LEU D CG  
10352 C  CD1 . LEU D  192 ? 2.7216 2.9068 2.8439 0.4352  -0.5410 -0.2739 190  LEU D CD1 
10353 C  CD2 . LEU D  192 ? 2.8762 3.1584 3.0930 0.4927  -0.5229 -0.2725 190  LEU D CD2 
10354 N  N   . SER D  193 ? 3.0411 3.2058 3.4473 0.5797  -0.4410 -0.4023 191  SER D N   
10355 C  CA  . SER D  193 ? 3.0565 3.2847 3.5095 0.6154  -0.4249 -0.4124 191  SER D CA  
10356 C  C   . SER D  193 ? 3.0120 3.3419 3.4198 0.5937  -0.4370 -0.4325 191  SER D C   
10357 O  O   . SER D  193 ? 3.0494 3.3970 3.3879 0.5540  -0.4599 -0.4219 191  SER D O   
10358 C  CB  . SER D  193 ? 3.1749 3.3514 3.7011 0.6462  -0.3876 -0.4672 191  SER D CB  
10359 O  OG  . SER D  193 ? 3.2936 3.4607 3.8024 0.6185  -0.3830 -0.5364 191  SER D OG  
10360 N  N   . ALA D  194 ? 2.9022 3.2967 3.3487 0.6207  -0.4184 -0.4599 192  ALA D N   
10361 C  CA  . ALA D  194 ? 2.8135 3.3086 3.2212 0.6028  -0.4245 -0.4761 192  ALA D CA  
10362 C  C   . ALA D  194 ? 2.7523 3.2670 3.1732 0.6095  -0.4007 -0.5531 192  ALA D C   
10363 O  O   . ALA D  194 ? 2.7529 3.2007 3.2075 0.6196  -0.3829 -0.5993 192  ALA D O   
10364 C  CB  . ALA D  194 ? 2.8530 3.4344 3.2874 0.6244  -0.4256 -0.4363 192  ALA D CB  
10365 N  N   . HIS D  195 ? 2.7362 3.3473 3.1300 0.6018  -0.3990 -0.5682 193  HIS D N   
10366 C  CA  . HIS D  195 ? 2.7443 3.3931 3.1390 0.6071  -0.3776 -0.6403 193  HIS D CA  
10367 C  C   . HIS D  195 ? 2.7412 3.3873 3.2203 0.6556  -0.3426 -0.6766 193  HIS D C   
10368 O  O   . HIS D  195 ? 2.7163 3.3755 3.2473 0.6883  -0.3352 -0.6376 193  HIS D O   
10369 C  CB  . HIS D  195 ? 2.7710 3.5258 3.1101 0.5867  -0.3825 -0.6373 193  HIS D CB  
10370 C  CG  . HIS D  195 ? 2.7507 3.5554 3.0778 0.5909  -0.3619 -0.7087 193  HIS D CG  
10371 N  ND1 . HIS D  195 ? 2.7159 3.4843 3.0175 0.5773  -0.3629 -0.7633 193  HIS D ND1 
10372 C  CD2 . HIS D  195 ? 2.7868 3.6820 3.1229 0.6072  -0.3396 -0.7361 193  HIS D CD2 
10373 C  CE1 . HIS D  195 ? 2.7976 3.6328 3.0889 0.5847  -0.3436 -0.8226 193  HIS D CE1 
10374 N  NE2 . HIS D  195 ? 2.8277 3.7375 3.1384 0.6034  -0.3276 -0.8068 193  HIS D NE2 
10375 N  N   . CYS D  196 ? 2.7008 3.3318 3.1944 0.6613  -0.3201 -0.7534 194  CYS D N   
10376 C  CA  . CYS D  196 ? 2.7367 3.3571 3.3087 0.7060  -0.2808 -0.8000 194  CYS D CA  
10377 C  C   . CYS D  196 ? 2.7621 3.4754 3.3140 0.7073  -0.2628 -0.8619 194  CYS D C   
10378 O  O   . CYS D  196 ? 2.7894 3.5077 3.3014 0.6833  -0.2634 -0.9223 194  CYS D O   
10379 C  CB  . CYS D  196 ? 2.8056 3.3119 3.4232 0.7115  -0.2628 -0.8448 194  CYS D CB  
10380 S  SG  . CYS D  196 ? 2.9088 3.3046 3.5199 0.6909  -0.2877 -0.7845 194  CYS D SG  
10381 N  N   . SER D  197 ? 2.8324 3.6271 3.4112 0.7358  -0.2472 -0.8465 195  SER D N   
10382 C  CA  . SER D  197 ? 2.8163 3.7030 3.3836 0.7437  -0.2234 -0.9033 195  SER D CA  
10383 C  C   . SER D  197 ? 2.8022 3.6515 3.4506 0.7893  -0.1790 -0.9677 195  SER D C   
10384 O  O   . SER D  197 ? 2.7676 3.6189 3.4877 0.8344  -0.1581 -0.9420 195  SER D O   
10385 C  CB  . SER D  197 ? 2.7847 3.7841 3.3410 0.7474  -0.2271 -0.8529 195  SER D CB  
10386 O  OG  . SER D  197 ? 2.7937 3.8870 3.3321 0.7526  -0.2027 -0.9038 195  SER D OG  
10387 N  N   . CYS D  198 ? 2.7999 3.6199 3.4379 0.7783  -0.1635 -1.0529 196  CYS D N   
10388 C  CA  . CYS D  198 ? 2.8078 3.5682 3.5226 0.8144  -0.1191 -1.1229 196  CYS D CA  
10389 C  C   . CYS D  198 ? 2.8956 3.7243 3.5848 0.8110  -0.0947 -1.2179 196  CYS D C   
10390 O  O   . CYS D  198 ? 2.8497 3.7570 3.4556 0.7763  -0.1160 -1.2320 196  CYS D O   
10391 C  CB  . CYS D  198 ? 2.7609 3.3866 3.5074 0.8027  -0.1187 -1.1422 196  CYS D CB  
10392 S  SG  . CYS D  198 ? 2.7528 3.3617 3.4386 0.7469  -0.1348 -1.2258 196  CYS D SG  
10393 N  N   . ASP D  199 ? 3.1000 3.8972 3.8608 0.8498  -0.0473 -1.2818 197  ASP D N   
10394 C  CA  . ASP D  199 ? 3.1821 4.0228 3.9286 0.8480  -0.0177 -1.3888 197  ASP D CA  
10395 C  C   . ASP D  199 ? 3.3011 4.0588 4.1450 0.8915  0.0372  -1.4518 197  ASP D C   
10396 O  O   . ASP D  199 ? 3.2839 3.9180 4.1868 0.8987  0.0463  -1.4441 197  ASP D O   
10397 C  CB  . ASP D  199 ? 3.2167 4.2020 3.9143 0.8541  -0.0131 -1.3885 197  ASP D CB  
10398 C  CG  . ASP D  199 ? 3.3196 4.3648 3.9713 0.8399  0.0058  -1.4946 197  ASP D CG  
10399 O  OD1 . ASP D  199 ? 3.3190 4.4071 3.8842 0.7960  -0.0266 -1.5078 197  ASP D OD1 
10400 O  OD2 . ASP D  199 ? 3.3244 4.3755 4.0255 0.8744  0.0534  -1.5650 197  ASP D OD2 
10401 N  N   . THR D  204 ? 2.2587 3.0351 2.9855 0.8289  -0.3387 -0.4208 202  THR D N   
10402 C  CA  . THR D  204 ? 2.2046 2.9274 2.9095 0.8181  -0.3667 -0.3590 202  THR D CA  
10403 C  C   . THR D  204 ? 2.2372 2.9606 2.8508 0.7505  -0.4008 -0.3493 202  THR D C   
10404 O  O   . THR D  204 ? 2.1851 2.9258 2.7532 0.7151  -0.3998 -0.3928 202  THR D O   
10405 C  CB  . THR D  204 ? 2.1375 2.9366 2.8836 0.8540  -0.3790 -0.2922 202  THR D CB  
10406 O  OG1 . THR D  204 ? 2.1044 3.0406 2.8586 0.8496  -0.3814 -0.2966 202  THR D OG1 
10407 C  CG2 . THR D  204 ? 2.1698 2.9194 3.0014 0.9266  -0.3479 -0.2799 202  THR D CG2 
10408 N  N   . LEU D  205 ? 2.5327 3.2400 3.1181 0.7351  -0.4295 -0.2909 203  LEU D N   
10409 C  CA  . LEU D  205 ? 2.5436 3.2410 3.0451 0.6742  -0.4595 -0.2768 203  LEU D CA  
10410 C  C   . LEU D  205 ? 2.5767 3.3640 3.0604 0.6570  -0.4874 -0.2236 203  LEU D C   
10411 O  O   . LEU D  205 ? 2.5940 3.4049 3.1169 0.6905  -0.4945 -0.1790 203  LEU D O   
10412 C  CB  . LEU D  205 ? 2.4753 3.0505 2.9512 0.6632  -0.4659 -0.2657 203  LEU D CB  
10413 C  CG  . LEU D  205 ? 2.3437 2.8995 2.7372 0.6074  -0.4959 -0.2422 203  LEU D CG  
10414 C  CD1 . LEU D  205 ? 2.3549 2.9316 2.6949 0.5657  -0.4969 -0.2837 203  LEU D CD1 
10415 C  CD2 . LEU D  205 ? 2.3396 2.7815 2.7192 0.6049  -0.4990 -0.2257 203  LEU D CD2 
10416 N  N   . GLN D  206 ? 2.5659 3.4046 2.9907 0.6045  -0.5023 -0.2281 204  GLN D N   
10417 C  CA  . GLN D  206 ? 2.5120 3.4383 2.9184 0.5768  -0.5270 -0.1870 204  GLN D CA  
10418 C  C   . GLN D  206 ? 2.4241 3.3058 2.7472 0.5169  -0.5504 -0.1712 204  GLN D C   
10419 O  O   . GLN D  206 ? 2.3434 3.2941 2.6408 0.4799  -0.5675 -0.1493 204  GLN D O   
10420 C  CB  . GLN D  206 ? 2.5293 3.5793 2.9549 0.5683  -0.5173 -0.2030 204  GLN D CB  
10421 C  CG  . GLN D  206 ? 2.6591 3.7609 3.1649 0.6262  -0.4890 -0.2263 204  GLN D CG  
10422 C  CD  . GLN D  206 ? 2.6735 3.8914 3.1885 0.6118  -0.4750 -0.2485 204  GLN D CD  
10423 O  OE1 . GLN D  206 ? 2.5715 3.8143 3.0279 0.5571  -0.4816 -0.2524 204  GLN D OE1 
10424 N  NE2 . GLN D  206 ? 2.7924 4.0799 3.3824 0.6624  -0.4521 -0.2614 204  GLN D NE2 
10425 N  N   . VAL D  207 ? 2.4292 3.1998 2.7127 0.5055  -0.5497 -0.1837 205  VAL D N   
10426 C  CA  . VAL D  207 ? 2.3761 3.0995 2.5809 0.4522  -0.5674 -0.1718 205  VAL D CA  
10427 C  C   . VAL D  207 ? 2.3010 3.0040 2.4922 0.4471  -0.5901 -0.1253 205  VAL D C   
10428 O  O   . VAL D  207 ? 2.2899 2.9501 2.5155 0.4860  -0.5890 -0.1070 205  VAL D O   
10429 C  CB  . VAL D  207 ? 2.3519 2.9761 2.5234 0.4444  -0.5581 -0.2034 205  VAL D CB  
10430 C  CG1 . VAL D  207 ? 2.2313 2.8010 2.3270 0.3974  -0.5748 -0.1855 205  VAL D CG1 
10431 C  CG2 . VAL D  207 ? 2.4942 3.1534 2.6640 0.4426  -0.5397 -0.2489 205  VAL D CG2 
10432 N  N   . ASP D  208 ? 2.2541 2.9857 2.3932 0.3986  -0.6085 -0.1064 206  ASP D N   
10433 C  CA  . ASP D  208 ? 2.2106 2.9259 2.3224 0.3850  -0.6313 -0.0679 206  ASP D CA  
10434 C  C   . ASP D  208 ? 2.1903 2.7999 2.2313 0.3499  -0.6344 -0.0706 206  ASP D C   
10435 O  O   . ASP D  208 ? 2.1679 2.7754 2.1546 0.3015  -0.6373 -0.0771 206  ASP D O   
10436 C  CB  . ASP D  208 ? 2.1727 2.9954 2.2781 0.3519  -0.6486 -0.0506 206  ASP D CB  
10437 C  CG  . ASP D  208 ? 2.4675 3.4090 2.6444 0.3822  -0.6429 -0.0528 206  ASP D CG  
10438 O  OD1 . ASP D  208 ? 2.6473 3.5875 2.8646 0.4157  -0.6205 -0.0783 206  ASP D OD1 
10439 O  OD2 . ASP D  208 ? 2.5370 3.5783 2.7310 0.3720  -0.6605 -0.0314 206  ASP D OD2 
10440 N  N   . ILE D  209 ? 2.3654 2.8858 2.4100 0.3755  -0.6308 -0.0643 207  ILE D N   
10441 C  CA  . ILE D  209 ? 2.4325 2.8556 2.4176 0.3486  -0.6337 -0.0623 207  ILE D CA  
10442 C  C   . ILE D  209 ? 2.5961 3.0019 2.5622 0.3494  -0.6500 -0.0225 207  ILE D C   
10443 O  O   . ILE D  209 ? 2.7241 3.1652 2.7333 0.3869  -0.6543 0.0029  207  ILE D O   
10444 C  CB  . ILE D  209 ? 2.3913 2.7272 2.3918 0.3705  -0.6158 -0.0881 207  ILE D CB  
10445 C  CG1 . ILE D  209 ? 2.5230 2.8323 2.5858 0.4216  -0.6061 -0.0759 207  ILE D CG1 
10446 C  CG2 . ILE D  209 ? 2.4603 2.8223 2.4711 0.3685  -0.6017 -0.1302 207  ILE D CG2 
10447 C  CD1 . ILE D  209 ? 2.5321 2.7371 2.5994 0.4312  -0.5920 -0.0887 207  ILE D CD1 
10448 N  N   . ASN D  210 ? 2.5988 2.9546 2.4978 0.3092  -0.6582 -0.0158 208  ASN D N   
10449 C  CA  . ASN D  210 ? 2.6396 2.9707 2.5088 0.3068  -0.6718 0.0177  208  ASN D CA  
10450 C  C   . ASN D  210 ? 2.8648 3.1403 2.7723 0.3560  -0.6620 0.0360  208  ASN D C   
10451 O  O   . ASN D  210 ? 2.8666 3.0579 2.7790 0.3645  -0.6452 0.0201  208  ASN D O   
10452 C  CB  . ASN D  210 ? 2.4128 2.6737 2.2066 0.2614  -0.6733 0.0134  208  ASN D CB  
10453 C  CG  . ASN D  210 ? 2.4040 2.6774 2.1524 0.2401  -0.6911 0.0403  208  ASN D CG  
10454 O  OD1 . ASN D  210 ? 2.4911 2.8534 2.2549 0.2429  -0.7078 0.0569  208  ASN D OD1 
10455 N  ND2 . ASN D  210 ? 2.3925 2.5830 2.0854 0.2197  -0.6878 0.0433  208  ASN D ND2 
10456 N  N   . GLY D  211 ? 2.9867 3.3121 2.9234 0.3885  -0.6713 0.0707  209  GLY D N   
10457 C  CA  . GLY D  211 ? 2.8298 3.1000 2.8027 0.4373  -0.6582 0.0963  209  GLY D CA  
10458 C  C   . GLY D  211 ? 2.7989 3.0767 2.7389 0.4445  -0.6734 0.1439  209  GLY D C   
10459 O  O   . GLY D  211 ? 2.8062 3.1015 2.6820 0.4029  -0.6918 0.1480  209  GLY D O   
10460 N  N   . PHE D  212 ? 2.9765 3.2417 2.9588 0.4981  -0.6639 0.1803  210  PHE D N   
10461 C  CA  . PHE D  212 ? 3.1786 3.4553 3.1289 0.5132  -0.6766 0.2318  210  PHE D CA  
10462 C  C   . PHE D  212 ? 3.1742 3.5807 3.1449 0.5374  -0.7004 0.2632  210  PHE D C   
10463 O  O   . PHE D  212 ? 3.1478 3.5992 3.0743 0.5341  -0.7217 0.2981  210  PHE D O   
10464 C  CB  . PHE D  212 ? 3.2441 3.4281 3.2241 0.5604  -0.6496 0.2638  210  PHE D CB  
10465 C  CG  . PHE D  212 ? 3.3814 3.4440 3.3557 0.5411  -0.6240 0.2333  210  PHE D CG  
10466 C  CD1 . PHE D  212 ? 3.4537 3.4819 3.4783 0.5425  -0.6043 0.1871  210  PHE D CD1 
10467 C  CD2 . PHE D  212 ? 3.3192 3.3098 3.2401 0.5232  -0.6192 0.2499  210  PHE D CD2 
10468 C  CE1 . PHE D  212 ? 3.4594 3.3909 3.4826 0.5244  -0.5837 0.1570  210  PHE D CE1 
10469 C  CE2 . PHE D  212 ? 3.2460 3.1364 3.1687 0.5063  -0.5961 0.2219  210  PHE D CE2 
10470 C  CZ  . PHE D  212 ? 3.3602 3.2241 3.3356 0.5066  -0.5797 0.1753  210  PHE D CZ  
10471 N  N   . THR D  213 ? 3.1905 3.6631 3.2281 0.5639  -0.6966 0.2510  211  THR D N   
10472 C  CA  . THR D  213 ? 3.1296 3.7360 3.2035 0.5949  -0.7166 0.2800  211  THR D CA  
10473 C  C   . THR D  213 ? 3.2065 3.8156 3.2975 0.6575  -0.7154 0.3443  211  THR D C   
10474 O  O   . THR D  213 ? 3.2393 3.9606 3.3662 0.6964  -0.7309 0.3776  211  THR D O   
10475 C  CB  . THR D  213 ? 2.9361 3.6488 2.9593 0.5391  -0.7515 0.2698  211  THR D CB  
10476 O  OG1 . THR D  213 ? 2.8853 3.5711 2.8331 0.5144  -0.7669 0.2917  211  THR D OG1 
10477 C  CG2 . THR D  213 ? 2.7628 3.4614 2.7671 0.4788  -0.7471 0.2125  211  THR D CG2 
10478 N  N   . THR D  214 ? 3.1903 3.6820 3.2550 0.6678  -0.6966 0.3649  212  THR D N   
10479 C  CA  . THR D  214 ? 3.2306 3.6946 3.3110 0.7297  -0.6847 0.4290  212  THR D CA  
10480 C  C   . THR D  214 ? 3.2231 3.7867 3.2528 0.7360  -0.7188 0.4798  212  THR D C   
10481 O  O   . THR D  214 ? 3.4349 3.9519 3.4316 0.7601  -0.7124 0.5281  212  THR D O   
10482 C  CB  . THR D  214 ? 3.2243 3.6984 3.4000 0.8001  -0.6607 0.4461  212  THR D CB  
10483 O  OG1 . THR D  214 ? 3.3129 3.7202 3.5333 0.7872  -0.6339 0.3871  212  THR D OG1 
10484 C  CG2 . THR D  214 ? 3.1244 3.5213 3.3207 0.8632  -0.6335 0.5085  212  THR D CG2 
10485 N  N   . GLY D  215 ? 2.9584 3.6635 2.9812 0.7138  -0.7543 0.4692  213  GLY D N   
10486 C  CA  . GLY D  215 ? 2.8623 3.6860 2.8526 0.7303  -0.7881 0.5180  213  GLY D CA  
10487 C  C   . GLY D  215 ? 2.8237 3.7017 2.7241 0.6625  -0.8222 0.5004  213  GLY D C   
10488 O  O   . GLY D  215 ? 2.8506 3.8416 2.7230 0.6743  -0.8532 0.5364  213  GLY D O   
10489 N  N   . ARG D  216 ? 2.6154 3.4179 2.4692 0.5934  -0.8167 0.4461  214  ARG D N   
10490 C  CA  . ARG D  216 ? 2.5165 3.3582 2.2855 0.5268  -0.8438 0.4244  214  ARG D CA  
10491 C  C   . ARG D  216 ? 2.4761 3.2563 2.1747 0.5362  -0.8412 0.4620  214  ARG D C   
10492 O  O   . ARG D  216 ? 2.4562 3.0982 2.1440 0.5441  -0.8099 0.4655  214  ARG D O   
10493 C  CB  . ARG D  216 ? 2.3542 3.1282 2.0981 0.4557  -0.8341 0.3588  214  ARG D CB  
10494 C  CG  . ARG D  216 ? 2.3141 3.1354 2.1242 0.4478  -0.8301 0.3230  214  ARG D CG  
10495 C  CD  . ARG D  216 ? 2.5224 3.5173 2.3622 0.4446  -0.8616 0.3264  214  ARG D CD  
10496 N  NE  . ARG D  216 ? 2.5580 3.5932 2.4620 0.4376  -0.8523 0.2924  214  ARG D NE  
10497 C  CZ  . ARG D  216 ? 2.5466 3.7306 2.4994 0.4409  -0.8716 0.2913  214  ARG D CZ  
10498 N  NH1 . ARG D  216 ? 2.4412 3.7549 2.3880 0.4515  -0.9045 0.3218  214  ARG D NH1 
10499 N  NH2 . ARG D  216 ? 2.5185 3.7287 2.5263 0.4342  -0.8577 0.2597  214  ARG D NH2 
10500 N  N   . ARG D  217 ? 2.2503 3.1400 1.9014 0.5343  -0.8738 0.4887  215  ARG D N   
10501 C  CA  . ARG D  217 ? 2.3117 3.1621 1.8902 0.5464  -0.8729 0.5283  215  ARG D CA  
10502 C  C   . ARG D  217 ? 2.3274 3.2221 1.8134 0.4756  -0.8991 0.4940  215  ARG D C   
10503 O  O   . ARG D  217 ? 2.3294 3.2359 1.8054 0.4101  -0.9071 0.4339  215  ARG D O   
10504 C  CB  . ARG D  217 ? 2.3752 3.3131 1.9742 0.6242  -0.8844 0.6044  215  ARG D CB  
10505 C  CG  . ARG D  217 ? 2.3781 3.2603 2.0672 0.6996  -0.8527 0.6433  215  ARG D CG  
10506 C  CD  . ARG D  217 ? 2.4591 3.3941 2.1517 0.7792  -0.8556 0.7288  215  ARG D CD  
10507 N  NE  . ARG D  217 ? 2.4902 3.5809 2.1919 0.7710  -0.8873 0.7306  215  ARG D NE  
10508 C  CZ  . ARG D  217 ? 2.4907 3.6627 2.2772 0.8110  -0.8892 0.7424  215  ARG D CZ  
10509 N  NH1 . ARG D  217 ? 2.4626 3.5723 2.3301 0.8623  -0.8606 0.7523  215  ARG D NH1 
10510 N  NH2 . ARG D  217 ? 2.5241 3.8398 2.3156 0.8010  -0.9178 0.7420  215  ARG D NH2 
10511 N  N   . GLY D  218 ? 2.3941 3.3093 1.8106 0.4886  -0.9094 0.5318  216  GLY D N   
10512 C  CA  . GLY D  218 ? 2.4247 3.3912 1.7496 0.4260  -0.9343 0.5001  216  GLY D CA  
10513 C  C   . GLY D  218 ? 2.4236 3.2472 1.6797 0.3764  -0.9083 0.4643  216  GLY D C   
10514 O  O   . GLY D  218 ? 2.4208 3.1114 1.6831 0.4035  -0.8725 0.4845  216  GLY D O   
10515 N  N   . ASP D  219 ? 2.4312 3.2835 1.6238 0.3030  -0.9246 0.4099  217  ASP D N   
10516 C  CA  . ASP D  219 ? 2.4340 3.1543 1.5619 0.2549  -0.8989 0.3721  217  ASP D CA  
10517 C  C   . ASP D  219 ? 2.3625 2.9804 1.5352 0.2245  -0.8737 0.3265  217  ASP D C   
10518 O  O   . ASP D  219 ? 2.3499 2.8310 1.5064 0.2189  -0.8412 0.3169  217  ASP D O   
10519 C  CB  . ASP D  219 ? 2.4842 3.2674 1.5237 0.1898  -0.9219 0.3309  217  ASP D CB  
10520 C  CG  . ASP D  219 ? 2.4915 3.1388 1.4671 0.1400  -0.8929 0.2882  217  ASP D CG  
10521 O  OD1 . ASP D  219 ? 2.4886 3.0151 1.4597 0.1709  -0.8604 0.3130  217  ASP D OD1 
10522 O  OD2 . ASP D  219 ? 2.5050 3.1659 1.4376 0.0709  -0.9003 0.2303  217  ASP D OD2 
10523 N  N   . LEU D  220 ? 2.3476 3.0371 1.5770 0.2064  -0.8880 0.2998  218  LEU D N   
10524 C  CA  . LEU D  220 ? 2.2565 2.8677 1.5242 0.1767  -0.8667 0.2574  218  LEU D CA  
10525 C  C   . LEU D  220 ? 2.3797 2.9134 1.7213 0.2324  -0.8406 0.2816  218  LEU D C   
10526 O  O   . LEU D  220 ? 2.4439 2.9011 1.8114 0.2136  -0.8200 0.2492  218  LEU D O   
10527 C  CB  . LEU D  220 ? 2.2333 2.9583 1.5339 0.1362  -0.8895 0.2222  218  LEU D CB  
10528 C  CG  . LEU D  220 ? 2.3827 3.0474 1.6977 0.0847  -0.8714 0.1706  218  LEU D CG  
10529 C  CD1 . LEU D  220 ? 2.2149 2.7610 1.4536 0.0356  -0.8508 0.1381  218  LEU D CD1 
10530 C  CD2 . LEU D  220 ? 2.4441 3.2375 1.7865 0.0416  -0.8941 0.1407  218  LEU D CD2 
10531 N  N   . ALA D  221 ? 2.2324 2.7832 1.6072 0.3000  -0.8392 0.3370  219  ALA D N   
10532 C  CA  . ALA D  221 ? 2.2012 2.6806 1.6518 0.3515  -0.8122 0.3558  219  ALA D CA  
10533 C  C   . ALA D  221 ? 2.1985 2.5241 1.6346 0.3392  -0.7773 0.3373  219  ALA D C   
10534 O  O   . ALA D  221 ? 2.1666 2.4314 1.6593 0.3492  -0.7567 0.3193  219  ALA D O   
10535 C  CB  . ALA D  221 ? 2.2569 2.7690 1.7377 0.4254  -0.8119 0.4226  219  ALA D CB  
10536 N  N   . THR D  222 ? 2.3037 2.5714 1.6652 0.3184  -0.7701 0.3402  220  THR D N   
10537 C  CA  . THR D  222 ? 2.3657 2.4965 1.7158 0.3091  -0.7368 0.3254  220  THR D CA  
10538 C  C   . THR D  222 ? 2.1898 2.2781 1.5495 0.2643  -0.7297 0.2694  220  THR D C   
10539 O  O   . THR D  222 ? 2.1708 2.1717 1.5652 0.2725  -0.7048 0.2564  220  THR D O   
10540 C  CB  . THR D  222 ? 2.5008 2.5918 1.7641 0.2906  -0.7312 0.3346  220  THR D CB  
10541 O  OG1 . THR D  222 ? 2.5849 2.7764 1.7886 0.2591  -0.7627 0.3263  220  THR D OG1 
10542 C  CG2 . THR D  222 ? 2.3837 2.4368 1.6512 0.3444  -0.7126 0.3925  220  THR D CG2 
10543 N  N   . ILE D  223 ? 2.3501 2.5016 1.6797 0.2161  -0.7503 0.2362  221  ILE D N   
10544 C  CA  . ILE D  223 ? 2.5559 2.6672 1.8914 0.1754  -0.7409 0.1892  221  ILE D CA  
10545 C  C   . ILE D  223 ? 2.6832 2.8339 2.0987 0.1954  -0.7419 0.1816  221  ILE D C   
10546 O  O   . ILE D  223 ? 2.5392 2.6473 1.9694 0.1753  -0.7289 0.1497  221  ILE D O   
10547 C  CB  . ILE D  223 ? 2.6977 2.8487 1.9717 0.1122  -0.7557 0.1555  221  ILE D CB  
10548 C  CG1 . ILE D  223 ? 2.4733 2.6107 1.6674 0.0972  -0.7588 0.1640  221  ILE D CG1 
10549 C  CG2 . ILE D  223 ? 2.9024 2.9773 2.1644 0.0713  -0.7365 0.1143  221  ILE D CG2 
10550 C  CD1 . ILE D  223 ? 2.5186 2.6585 1.6469 0.0299  -0.7630 0.1212  221  ILE D CD1 
10551 N  N   . HIS D  224 ? 2.8201 3.0488 2.2876 0.2393  -0.7542 0.2121  222  HIS D N   
10552 C  CA  . HIS D  224 ? 2.7854 3.0522 2.3311 0.2632  -0.7519 0.2041  222  HIS D CA  
10553 C  C   . HIS D  224 ? 2.5490 2.7204 2.1428 0.2977  -0.7230 0.2028  222  HIS D C   
10554 O  O   . HIS D  224 ? 2.4368 2.6308 2.0965 0.3222  -0.7170 0.1939  222  HIS D O   
10555 C  CB  . HIS D  224 ? 2.9362 3.3202 2.5253 0.3032  -0.7726 0.2380  222  HIS D CB  
10556 C  CG  . HIS D  224 ? 2.9875 3.4625 2.6323 0.2989  -0.7820 0.2174  222  HIS D CG  
10557 N  ND1 . HIS D  224 ? 2.9228 3.3595 2.5987 0.2853  -0.7649 0.1814  222  HIS D ND1 
10558 C  CD2 . HIS D  224 ? 2.8964 3.5062 2.5714 0.3068  -0.8063 0.2283  222  HIS D CD2 
10559 C  CE1 . HIS D  224 ? 2.9131 3.4519 2.6346 0.2846  -0.7756 0.1712  222  HIS D CE1 
10560 N  NE2 . HIS D  224 ? 3.0532 3.6992 2.7785 0.2972  -0.8006 0.1986  222  HIS D NE2 
10561 N  N   . GLY D  225 ? 2.4083 2.4783 1.9722 0.2978  -0.7041 0.2073  223  GLY D N   
10562 C  CA  . GLY D  225 ? 2.4302 2.4132 2.0393 0.3208  -0.6769 0.1979  223  GLY D CA  
10563 C  C   . GLY D  225 ? 2.4233 2.3478 2.0060 0.2805  -0.6671 0.1560  223  GLY D C   
10564 O  O   . GLY D  225 ? 2.4354 2.3009 2.0538 0.2911  -0.6480 0.1377  223  GLY D O   
10565 N  N   . MET D  226 ? 2.4551 2.3979 1.9764 0.2342  -0.6792 0.1401  224  MET D N   
10566 C  CA  . MET D  226 ? 2.4203 2.3119 1.9151 0.1985  -0.6689 0.1052  224  MET D CA  
10567 C  C   . MET D  226 ? 2.3904 2.3219 1.9308 0.1977  -0.6695 0.0801  224  MET D C   
10568 O  O   . MET D  226 ? 2.3779 2.3819 1.9672 0.2195  -0.6787 0.0862  224  MET D O   
10569 C  CB  . MET D  226 ? 2.4275 2.3225 1.8469 0.1488  -0.6771 0.0945  224  MET D CB  
10570 C  CG  . MET D  226 ? 2.5904 2.4018 1.9524 0.1372  -0.6632 0.0981  224  MET D CG  
10571 S  SD  . MET D  226 ? 2.6551 2.4566 1.9333 0.0750  -0.6656 0.0732  224  MET D SD  
10572 C  CE  . MET D  226 ? 2.7555 2.4446 1.9838 0.0758  -0.6407 0.0758  224  MET D CE  
10573 N  N   . ASN D  227 ? 2.3918 2.2772 1.9151 0.1752  -0.6578 0.0533  225  ASN D N   
10574 C  CA  . ASN D  227 ? 2.5253 2.4406 2.0805 0.1727  -0.6546 0.0288  225  ASN D CA  
10575 C  C   . ASN D  227 ? 2.5333 2.4635 2.1626 0.2167  -0.6486 0.0250  225  ASN D C   
10576 O  O   . ASN D  227 ? 2.6111 2.5851 2.2728 0.2205  -0.6474 0.0054  225  ASN D O   
10577 C  CB  . ASN D  227 ? 2.5820 2.5809 2.1278 0.1433  -0.6682 0.0234  225  ASN D CB  
10578 C  CG  . ASN D  227 ? 2.5625 2.5393 2.0378 0.0923  -0.6687 0.0174  225  ASN D CG  
10579 O  OD1 . ASN D  227 ? 2.7627 2.6571 2.1955 0.0801  -0.6558 0.0131  225  ASN D OD1 
10580 N  ND2 . ASN D  227 ? 2.3802 2.4318 1.8462 0.0618  -0.6819 0.0150  225  ASN D ND2 
10581 N  N   . ARG D  228 ? 2.3737 2.2662 2.0305 0.2492  -0.6416 0.0423  226  ARG D N   
10582 C  CA  . ARG D  228 ? 2.1879 2.0820 1.9173 0.2888  -0.6309 0.0351  226  ARG D CA  
10583 C  C   . ARG D  228 ? 2.1946 2.0444 1.9386 0.2858  -0.6165 -0.0002 226  ARG D C   
10584 O  O   . ARG D  228 ? 2.3538 2.1553 2.0549 0.2630  -0.6126 -0.0079 226  ARG D O   
10585 C  CB  . ARG D  228 ? 2.3595 2.2161 2.1146 0.3226  -0.6222 0.0662  226  ARG D CB  
10586 C  CG  . ARG D  228 ? 2.5190 2.2882 2.2460 0.3153  -0.6082 0.0724  226  ARG D CG  
10587 C  CD  . ARG D  228 ? 2.5024 2.2374 2.2586 0.3501  -0.5953 0.1077  226  ARG D CD  
10588 N  NE  . ARG D  228 ? 2.6688 2.3254 2.3996 0.3424  -0.5793 0.1164  226  ARG D NE  
10589 C  CZ  . ARG D  228 ? 2.7047 2.3468 2.3774 0.3328  -0.5825 0.1465  226  ARG D CZ  
10590 N  NH1 . ARG D  228 ? 2.7557 2.4598 2.3889 0.3278  -0.6039 0.1687  226  ARG D NH1 
10591 N  NH2 . ARG D  228 ? 2.5721 2.1440 2.2270 0.3273  -0.5640 0.1523  226  ARG D NH2 
10592 N  N   . PRO D  229 ? 2.1047 1.9769 1.9080 0.3091  -0.6088 -0.0239 227  PRO D N   
10593 C  CA  . PRO D  229 ? 2.1216 1.9640 1.9423 0.3084  -0.5970 -0.0615 227  PRO D CA  
10594 C  C   . PRO D  229 ? 2.1433 1.9081 1.9526 0.3036  -0.5863 -0.0621 227  PRO D C   
10595 O  O   . PRO D  229 ? 2.1814 1.9027 2.0134 0.3198  -0.5764 -0.0430 227  PRO D O   
10596 C  CB  . PRO D  229 ? 2.2424 2.1057 2.1388 0.3425  -0.5861 -0.0807 227  PRO D CB  
10597 C  CG  . PRO D  229 ? 2.2903 2.2264 2.1962 0.3523  -0.5967 -0.0617 227  PRO D CG  
10598 C  CD  . PRO D  229 ? 2.1191 2.0562 1.9743 0.3365  -0.6111 -0.0204 227  PRO D CD  
10599 N  N   . PHE D  230 ? 2.3346 2.0842 2.1093 0.2828  -0.5866 -0.0809 228  PHE D N   
10600 C  CA  . PHE D  230 ? 2.3584 2.0461 2.1255 0.2782  -0.5766 -0.0846 228  PHE D CA  
10601 C  C   . PHE D  230 ? 2.3300 2.0295 2.1138 0.2777  -0.5737 -0.1243 228  PHE D C   
10602 O  O   . PHE D  230 ? 2.3192 2.0686 2.0927 0.2736  -0.5808 -0.1419 228  PHE D O   
10603 C  CB  . PHE D  230 ? 2.3268 1.9817 2.0224 0.2542  -0.5802 -0.0601 228  PHE D CB  
10604 C  CG  . PHE D  230 ? 2.2867 1.9591 1.9330 0.2324  -0.5861 -0.0700 228  PHE D CG  
10605 C  CD1 . PHE D  230 ? 2.2301 1.9502 1.8504 0.2175  -0.5961 -0.0647 228  PHE D CD1 
10606 C  CD2 . PHE D  230 ? 2.3878 2.0309 2.0164 0.2279  -0.5797 -0.0822 228  PHE D CD2 
10607 C  CE1 . PHE D  230 ? 2.2143 1.9426 1.7900 0.1970  -0.5963 -0.0700 228  PHE D CE1 
10608 C  CE2 . PHE D  230 ? 2.4612 2.1151 2.0435 0.2127  -0.5817 -0.0847 228  PHE D CE2 
10609 C  CZ  . PHE D  230 ? 2.3021 1.9938 1.8568 0.1964  -0.5884 -0.0779 228  PHE D CZ  
10610 N  N   . LEU D  231 ? 2.2956 1.9546 2.1047 0.2814  -0.5629 -0.1376 229  LEU D N   
10611 C  CA  . LEU D  231 ? 2.4558 2.1334 2.2853 0.2819  -0.5619 -0.1771 229  LEU D CA  
10612 C  C   . LEU D  231 ? 2.5104 2.1680 2.2875 0.2682  -0.5642 -0.1675 229  LEU D C   
10613 O  O   . LEU D  231 ? 2.5658 2.1750 2.3411 0.2655  -0.5551 -0.1540 229  LEU D O   
10614 C  CB  . LEU D  231 ? 2.6327 2.2886 2.5368 0.2936  -0.5471 -0.2045 229  LEU D CB  
10615 C  CG  . LEU D  231 ? 2.6963 2.3832 2.6330 0.2928  -0.5471 -0.2542 229  LEU D CG  
10616 C  CD1 . LEU D  231 ? 2.6502 2.4064 2.5820 0.2973  -0.5579 -0.2835 229  LEU D CD1 
10617 C  CD2 . LEU D  231 ? 2.6744 2.3314 2.6899 0.2981  -0.5286 -0.2817 229  LEU D CD2 
10618 N  N   . LEU D  232 ? 2.3618 2.0552 2.0957 0.2615  -0.5734 -0.1711 230  LEU D N   
10619 C  CA  . LEU D  232 ? 2.2959 1.9705 1.9802 0.2539  -0.5730 -0.1597 230  LEU D CA  
10620 C  C   . LEU D  232 ? 2.2952 1.9882 2.0137 0.2647  -0.5721 -0.1899 230  LEU D C   
10621 O  O   . LEU D  232 ? 2.2787 2.0272 2.0267 0.2729  -0.5782 -0.2239 230  LEU D O   
10622 C  CB  . LEU D  232 ? 2.2387 1.9414 1.8662 0.2445  -0.5790 -0.1483 230  LEU D CB  
10623 C  CG  . LEU D  232 ? 2.2364 1.9059 1.8033 0.2369  -0.5740 -0.1262 230  LEU D CG  
10624 C  CD1 . LEU D  232 ? 2.3560 1.9583 1.8935 0.2237  -0.5659 -0.0989 230  LEU D CD1 
10625 C  CD2 . LEU D  232 ? 2.2275 1.9241 1.7464 0.2274  -0.5752 -0.1157 230  LEU D CD2 
10626 N  N   . LEU D  233 ? 2.3160 1.9693 2.0311 0.2642  -0.5644 -0.1798 231  LEU D N   
10627 C  CA  . LEU D  233 ? 2.3290 2.0056 2.0831 0.2729  -0.5637 -0.2075 231  LEU D CA  
10628 C  C   . LEU D  233 ? 2.2865 1.9642 1.9917 0.2779  -0.5650 -0.1906 231  LEU D C   
10629 O  O   . LEU D  233 ? 2.2683 1.8943 1.9216 0.2721  -0.5572 -0.1558 231  LEU D O   
10630 C  CB  . LEU D  233 ? 2.4226 2.0578 2.2300 0.2708  -0.5495 -0.2117 231  LEU D CB  
10631 C  CG  . LEU D  233 ? 2.3917 2.0089 2.2491 0.2700  -0.5419 -0.2194 231  LEU D CG  
10632 C  CD1 . LEU D  233 ? 2.3773 1.9425 2.2771 0.2673  -0.5223 -0.2125 231  LEU D CD1 
10633 C  CD2 . LEU D  233 ? 2.4022 2.0750 2.3112 0.2754  -0.5477 -0.2663 231  LEU D CD2 
10634 N  N   . MET D  234 ? 2.4521 2.1906 2.1743 0.2902  -0.5738 -0.2162 232  MET D N   
10635 C  CA  . MET D  234 ? 2.5195 2.2693 2.2037 0.3032  -0.5748 -0.1991 232  MET D CA  
10636 C  C   . MET D  234 ? 2.4583 2.2599 2.2009 0.3139  -0.5795 -0.2320 232  MET D C   
10637 O  O   . MET D  234 ? 2.3869 2.2655 2.1581 0.3202  -0.5933 -0.2688 232  MET D O   
10638 C  CB  . MET D  234 ? 2.5891 2.3793 2.2197 0.3111  -0.5835 -0.1886 232  MET D CB  
10639 C  CG  . MET D  234 ? 2.7361 2.4877 2.3174 0.2955  -0.5786 -0.1620 232  MET D CG  
10640 S  SD  . MET D  234 ? 3.0977 2.9020 2.6248 0.3021  -0.5839 -0.1516 232  MET D SD  
10641 C  CE  . MET D  234 ? 2.9988 2.7550 2.4878 0.2748  -0.5755 -0.1264 232  MET D CE  
10642 N  N   . ALA D  235 ? 2.4021 2.1681 2.1630 0.3147  -0.5676 -0.2213 233  ALA D N   
10643 C  CA  . ALA D  235 ? 2.3391 2.1548 2.1665 0.3197  -0.5696 -0.2538 233  ALA D CA  
10644 C  C   . ALA D  235 ? 2.3980 2.2175 2.2034 0.3385  -0.5653 -0.2284 233  ALA D C   
10645 O  O   . ALA D  235 ? 2.5585 2.3263 2.2981 0.3465  -0.5565 -0.1860 233  ALA D O   
10646 C  CB  . ALA D  235 ? 2.4779 2.2531 2.3707 0.3017  -0.5541 -0.2704 233  ALA D CB  
10647 N  N   . THR D  236 ? 2.3260 2.2104 2.1920 0.3456  -0.5701 -0.2575 234  THR D N   
10648 C  CA  . THR D  236 ? 2.3304 2.2344 2.1913 0.3680  -0.5661 -0.2372 234  THR D CA  
10649 C  C   . THR D  236 ? 2.3657 2.2180 2.2676 0.3575  -0.5431 -0.2317 234  THR D C   
10650 O  O   . THR D  236 ? 2.4387 2.3021 2.4126 0.3370  -0.5384 -0.2664 234  THR D O   
10651 C  CB  . THR D  236 ? 2.3426 2.3693 2.2453 0.3843  -0.5881 -0.2718 234  THR D CB  
10652 O  OG1 . THR D  236 ? 2.3356 2.4127 2.1917 0.3967  -0.6075 -0.2729 234  THR D OG1 
10653 C  CG2 . THR D  236 ? 2.4380 2.4933 2.3410 0.4129  -0.5841 -0.2474 234  THR D CG2 
10654 N  N   . PRO D  237 ? 2.5028 2.2949 2.3613 0.3700  -0.5250 -0.1897 235  PRO D N   
10655 C  CA  . PRO D  237 ? 2.5536 2.2945 2.4440 0.3603  -0.4996 -0.1822 235  PRO D CA  
10656 C  C   . PRO D  237 ? 2.5815 2.3988 2.5632 0.3605  -0.4995 -0.2161 235  PRO D C   
10657 O  O   . PRO D  237 ? 2.5815 2.4951 2.5897 0.3783  -0.5185 -0.2353 235  PRO D O   
10658 C  CB  . PRO D  237 ? 2.6391 2.3203 2.4608 0.3807  -0.4825 -0.1362 235  PRO D CB  
10659 C  CG  . PRO D  237 ? 2.6274 2.2879 2.3724 0.3866  -0.4936 -0.1156 235  PRO D CG  
10660 C  CD  . PRO D  237 ? 2.5256 2.2822 2.2995 0.3911  -0.5222 -0.1469 235  PRO D CD  
10661 N  N   . LEU D  238 ? 2.7123 2.4892 2.7422 0.3397  -0.4767 -0.2223 236  LEU D N   
10662 C  CA  . LEU D  238 ? 2.7202 2.5621 2.8445 0.3325  -0.4704 -0.2553 236  LEU D CA  
10663 C  C   . LEU D  238 ? 2.8069 2.6834 2.9336 0.3602  -0.4625 -0.2356 236  LEU D C   
10664 O  O   . LEU D  238 ? 2.7233 2.6943 2.9238 0.3638  -0.4688 -0.2649 236  LEU D O   
10665 C  CB  . LEU D  238 ? 2.7406 2.5193 2.9119 0.3030  -0.4418 -0.2598 236  LEU D CB  
10666 C  CG  . LEU D  238 ? 2.7341 2.4708 2.9178 0.2780  -0.4418 -0.2761 236  LEU D CG  
10667 C  CD1 . LEU D  238 ? 2.7205 2.3649 2.8152 0.2806  -0.4374 -0.2329 236  LEU D CD1 
10668 C  CD2 . LEU D  238 ? 2.8472 2.5643 3.1163 0.2512  -0.4145 -0.2961 236  LEU D CD2 
10669 N  N   . GLU D  239 ? 2.9046 2.7090 2.9540 0.3799  -0.4478 -0.1883 237  GLU D N   
10670 C  CA  . GLU D  239 ? 2.8465 2.6721 2.8953 0.4110  -0.4349 -0.1659 237  GLU D CA  
10671 C  C   . GLU D  239 ? 2.7822 2.7169 2.8414 0.4434  -0.4628 -0.1737 237  GLU D C   
10672 O  O   . GLU D  239 ? 2.9112 2.9122 3.0110 0.4685  -0.4592 -0.1716 237  GLU D O   
10673 C  CB  . GLU D  239 ? 2.8006 2.5182 2.7572 0.4248  -0.4121 -0.1180 237  GLU D CB  
10674 C  CG  . GLU D  239 ? 2.8055 2.4238 2.7437 0.3977  -0.3836 -0.1061 237  GLU D CG  
10675 C  CD  . GLU D  239 ? 2.9168 2.4890 2.8256 0.3691  -0.3950 -0.1117 237  GLU D CD  
10676 O  OE1 . GLU D  239 ? 3.0204 2.6258 2.9119 0.3709  -0.4222 -0.1220 237  GLU D OE1 
10677 O  OE2 . GLU D  239 ? 2.9413 2.4492 2.8450 0.3471  -0.3758 -0.1042 237  GLU D OE2 
10678 N  N   . ARG D  240 ? 2.6113 2.5726 2.6346 0.4454  -0.4901 -0.1812 238  ARG D N   
10679 C  CA  . ARG D  240 ? 2.6063 2.6757 2.6298 0.4784  -0.5175 -0.1849 238  ARG D CA  
10680 C  C   . ARG D  240 ? 2.6289 2.8275 2.7489 0.4655  -0.5394 -0.2418 238  ARG D C   
10681 O  O   . ARG D  240 ? 2.6721 2.9650 2.8440 0.4871  -0.5446 -0.2491 238  ARG D O   
10682 C  CB  . ARG D  240 ? 2.6151 2.6658 2.5610 0.4839  -0.5352 -0.1709 238  ARG D CB  
10683 C  CG  . ARG D  240 ? 2.6673 2.5845 2.5251 0.4816  -0.5127 -0.1257 238  ARG D CG  
10684 C  CD  . ARG D  240 ? 2.6719 2.5819 2.4557 0.4916  -0.5270 -0.1066 238  ARG D CD  
10685 N  NE  . ARG D  240 ? 2.6827 2.4707 2.3940 0.4746  -0.5079 -0.0771 238  ARG D NE  
10686 C  CZ  . ARG D  240 ? 2.7028 2.4070 2.3573 0.4894  -0.4825 -0.0361 238  ARG D CZ  
10687 N  NH1 . ARG D  240 ? 2.7550 2.4783 2.4167 0.5264  -0.4710 -0.0150 238  ARG D NH1 
10688 N  NH2 . ARG D  240 ? 2.6431 2.2465 2.2354 0.4671  -0.4678 -0.0181 238  ARG D NH2 
10689 N  N   . ALA D  241 ? 2.4352 2.6403 2.5839 0.4294  -0.5505 -0.2847 239  ALA D N   
10690 C  CA  . ALA D  241 ? 2.4653 2.7830 2.7062 0.4086  -0.5686 -0.3485 239  ALA D CA  
10691 C  C   . ALA D  241 ? 2.5216 2.9849 2.7743 0.4418  -0.5998 -0.3607 239  ALA D C   
10692 O  O   . ALA D  241 ? 2.4704 2.9464 2.6479 0.4768  -0.6144 -0.3265 239  ALA D O   
10693 C  CB  . ALA D  241 ? 2.5157 2.8257 2.8458 0.3821  -0.5432 -0.3695 239  ALA D CB  
10694 N  N   . GLN D  242 ? 2.5387 3.1152 2.8864 0.4311  -0.6089 -0.4079 240  GLN D N   
10695 C  CA  . GLN D  242 ? 2.4739 3.2107 2.8442 0.4622  -0.6411 -0.4241 240  GLN D CA  
10696 C  C   . GLN D  242 ? 2.5594 3.3572 2.8764 0.4726  -0.6744 -0.4397 240  GLN D C   
10697 O  O   . GLN D  242 ? 2.6079 3.3617 2.9147 0.4405  -0.6760 -0.4701 240  GLN D O   
10698 C  CB  . GLN D  242 ? 2.3766 3.1204 2.7119 0.5162  -0.6334 -0.3612 240  GLN D CB  
10699 C  CG  . GLN D  242 ? 2.3383 3.2544 2.6963 0.5573  -0.6662 -0.3679 240  GLN D CG  
10700 C  CD  . GLN D  242 ? 2.3127 3.2521 2.5757 0.5982  -0.6892 -0.3327 240  GLN D CD  
10701 O  OE1 . GLN D  242 ? 2.3496 3.1640 2.5258 0.6024  -0.6745 -0.2908 240  GLN D OE1 
10702 N  NE2 . GLN D  242 ? 2.2369 3.3417 2.5160 0.6274  -0.7249 -0.3498 240  GLN D NE2 
10703 N  N   . CYS D  258 ? 3.1023 3.6147 2.8343 0.2254  -0.5469 -0.2338 256  CYS D N   
10704 C  CA  . CYS D  258 ? 3.1462 3.8089 2.8850 0.2052  -0.5702 -0.2127 256  CYS D CA  
10705 C  C   . CYS D  258 ? 3.1780 3.9095 2.8784 0.1270  -0.5869 -0.2356 256  CYS D C   
10706 O  O   . CYS D  258 ? 3.1160 3.9994 2.8298 0.1019  -0.6070 -0.2232 256  CYS D O   
10707 C  CB  . CYS D  258 ? 3.3114 3.9562 2.9803 0.1936  -0.5787 -0.1978 256  CYS D CB  
10708 S  SG  . CYS D  258 ? 3.6508 4.1309 3.3062 0.2505  -0.5528 -0.1942 256  CYS D SG  
10709 N  N   . PHE D  259 ? 3.4583 4.0805 3.1076 0.0888  -0.5774 -0.2689 257  PHE D N   
10710 C  CA  . PHE D  259 ? 3.5617 4.2336 3.1789 0.0172  -0.5875 -0.2934 257  PHE D CA  
10711 C  C   . PHE D  259 ? 3.5662 4.2940 3.2827 0.0469  -0.5810 -0.2976 257  PHE D C   
10712 O  O   . PHE D  259 ? 3.6224 4.4535 3.3484 0.0006  -0.5926 -0.3085 257  PHE D O   
10713 C  CB  . PHE D  259 ? 3.6572 4.1700 3.1446 -0.0456 -0.5789 -0.3271 257  PHE D CB  
10714 C  CG  . PHE D  259 ? 3.7940 4.1600 3.2871 -0.0036 -0.5564 -0.3408 257  PHE D CG  
10715 C  CD1 . PHE D  259 ? 3.9110 4.1623 3.3860 0.0453  -0.5416 -0.3340 257  PHE D CD1 
10716 C  CD2 . PHE D  259 ? 3.8039 4.1537 3.3169 -0.0157 -0.5501 -0.3614 257  PHE D CD2 
10717 C  CE1 . PHE D  259 ? 3.9432 4.0787 3.4237 0.0833  -0.5215 -0.3469 257  PHE D CE1 
10718 C  CE2 . PHE D  259 ? 3.8053 4.0335 3.3221 0.0225  -0.5306 -0.3732 257  PHE D CE2 
10719 C  CZ  . PHE D  259 ? 3.8729 3.9991 3.3743 0.0725  -0.5166 -0.3658 257  PHE D CZ  
10720 N  N   . SER D  260 ? 3.5451 4.2085 3.3318 0.1184  -0.5613 -0.2912 258  SER D N   
10721 C  CA  . SER D  260 ? 3.4602 4.1755 3.3446 0.1516  -0.5518 -0.2933 258  SER D CA  
10722 C  C   . SER D  260 ? 3.3412 4.2070 3.3252 0.2046  -0.5554 -0.2611 258  SER D C   
10723 O  O   . SER D  260 ? 3.3864 4.3156 3.4501 0.2297  -0.5477 -0.2612 258  SER D O   
10724 C  CB  . SER D  260 ? 3.3884 3.9750 3.3002 0.2005  -0.5264 -0.3018 258  SER D CB  
10725 O  OG  . SER D  260 ? 3.3560 3.9043 3.2888 0.2586  -0.5153 -0.2792 258  SER D OG  
10726 N  N   . SER D  261 ? 3.1574 4.0805 3.1340 0.2242  -0.5656 -0.2328 259  SER D N   
10727 C  CA  . SER D  261 ? 3.0655 4.1236 3.1256 0.2856  -0.5672 -0.1968 259  SER D CA  
10728 C  C   . SER D  261 ? 3.1514 4.3556 3.1794 0.2498  -0.5956 -0.1806 259  SER D C   
10729 O  O   . SER D  261 ? 3.3764 4.5437 3.3160 0.1985  -0.6085 -0.1870 259  SER D O   
10730 C  CB  . SER D  261 ? 3.0048 3.9876 3.0963 0.3652  -0.5463 -0.1706 259  SER D CB  
10731 O  OG  . SER D  261 ? 3.0970 3.9975 3.1113 0.3480  -0.5514 -0.1684 259  SER D OG  
10732 N  N   . THR D  262 ? 2.9736 4.3498 3.0716 0.2764  -0.6041 -0.1601 260  THR D N   
10733 C  CA  . THR D  262 ? 2.9907 4.5348 3.0760 0.2625  -0.6299 -0.1360 260  THR D CA  
10734 C  C   . THR D  262 ? 2.9671 4.5246 3.0766 0.3439  -0.6255 -0.0917 260  THR D C   
10735 O  O   . THR D  262 ? 2.9817 4.6371 3.0563 0.3294  -0.6467 -0.0714 260  THR D O   
10736 C  CB  . THR D  262 ? 2.8155 4.5584 2.9645 0.2598  -0.6416 -0.1316 260  THR D CB  
10737 O  OG1 . THR D  262 ? 2.7858 4.5522 3.0338 0.3568  -0.6199 -0.1074 260  THR D OG1 
10738 C  CG2 . THR D  262 ? 2.6787 4.4084 2.7965 0.1722  -0.6454 -0.1767 260  THR D CG2 
10739 N  N   . GLU D  263 ? 2.7937 4.2513 2.9547 0.4247  -0.5968 -0.0772 261  GLU D N   
10740 C  CA  . GLU D  263 ? 2.7307 4.1709 2.9041 0.5018  -0.5866 -0.0368 261  GLU D CA  
10741 C  C   . GLU D  263 ? 2.7268 4.0039 2.8286 0.4824  -0.5807 -0.0462 261  GLU D C   
10742 O  O   . GLU D  263 ? 2.6566 3.8100 2.7143 0.4312  -0.5757 -0.0827 261  GLU D O   
10743 C  CB  . GLU D  263 ? 2.5700 3.9727 2.8222 0.5940  -0.5530 -0.0180 261  GLU D CB  
10744 C  CG  . GLU D  263 ? 2.5510 4.1065 2.8764 0.6260  -0.5532 -0.0066 261  GLU D CG  
10745 C  CD  . GLU D  263 ? 2.5645 4.3194 2.8991 0.6505  -0.5779 0.0315  261  GLU D CD  
10746 O  OE1 . GLU D  263 ? 2.6140 4.3694 2.9197 0.6857  -0.5821 0.0639  261  GLU D OE1 
10747 O  OE2 . GLU D  263 ? 2.4244 4.3434 2.7947 0.6344  -0.5932 0.0290  261  GLU D OE2 
10748 N  N   . LYS D  264 ? 2.9266 4.2069 3.0139 0.5273  -0.5806 -0.0115 262  LYS D N   
10749 C  CA  . LYS D  264 ? 2.9107 4.0372 2.9384 0.5211  -0.5705 -0.0172 262  LYS D CA  
10750 C  C   . LYS D  264 ? 3.0731 4.0557 3.1395 0.5727  -0.5331 -0.0244 262  LYS D C   
10751 O  O   . LYS D  264 ? 3.0859 4.0484 3.1874 0.6466  -0.5111 0.0053  262  LYS D O   
10752 C  CB  . LYS D  264 ? 2.7813 3.9568 2.7771 0.5481  -0.5819 0.0211  262  LYS D CB  
10753 C  CG  . LYS D  264 ? 2.7063 3.9311 2.7560 0.6472  -0.5667 0.0694  262  LYS D CG  
10754 C  CD  . LYS D  264 ? 2.6956 4.1058 2.8062 0.6802  -0.5784 0.0929  262  LYS D CD  
10755 C  CE  . LYS D  264 ? 2.6938 4.0636 2.8778 0.7427  -0.5457 0.0937  262  LYS D CE  
10756 N  NZ  . LYS D  264 ? 2.6691 4.1982 2.9081 0.7402  -0.5580 0.0922  262  LYS D NZ  
10757 N  N   . ASN D  265 ? 3.2413 4.1255 3.2968 0.5325  -0.5241 -0.0641 263  ASN D N   
10758 C  CA  . ASN D  265 ? 3.1443 3.9075 3.2360 0.5694  -0.4899 -0.0769 263  ASN D CA  
10759 C  C   . ASN D  265 ? 3.1882 3.8240 3.2338 0.5814  -0.4750 -0.0759 263  ASN D C   
10760 O  O   . ASN D  265 ? 3.2762 3.9204 3.2703 0.5727  -0.4892 -0.0598 263  ASN D O   
10761 C  CB  . ASN D  265 ? 2.9767 3.6975 3.0721 0.5230  -0.4881 -0.1179 263  ASN D CB  
10762 C  CG  . ASN D  265 ? 2.8218 3.4821 2.9808 0.5643  -0.4551 -0.1270 263  ASN D CG  
10763 O  OD1 . ASN D  265 ? 2.7851 3.3918 2.9676 0.6187  -0.4283 -0.1101 263  ASN D OD1 
10764 N  ND2 . ASN D  265 ? 2.7721 3.4379 2.9534 0.5343  -0.4551 -0.1550 263  ASN D ND2 
10765 N  N   . CYS D  266 ? 3.1286 3.6508 3.1911 0.5988  -0.4455 -0.0943 264  CYS D N   
10766 C  CA  . CYS D  266 ? 3.1558 3.5615 3.1744 0.6035  -0.4301 -0.0999 264  CYS D CA  
10767 C  C   . CYS D  266 ? 3.1969 3.5645 3.1373 0.5416  -0.4519 -0.1239 264  CYS D C   
10768 O  O   . CYS D  266 ? 3.1591 3.4458 3.0770 0.5172  -0.4443 -0.1553 264  CYS D O   
10769 C  CB  . CYS D  266 ? 3.0322 3.3462 3.0875 0.6274  -0.3943 -0.1186 264  CYS D CB  
10770 S  SG  . CYS D  266 ? 2.9954 3.1742 3.0035 0.6256  -0.3721 -0.1368 264  CYS D SG  
10771 N  N   . CYS D  267 ? 3.2074 3.6362 3.1001 0.5159  -0.4781 -0.1084 265  CYS D N   
10772 C  CA  . CYS D  267 ? 3.2806 3.6647 3.0829 0.4558  -0.4951 -0.1283 265  CYS D CA  
10773 C  C   . CYS D  267 ? 3.2838 3.6185 3.0356 0.4680  -0.4922 -0.1119 265  CYS D C   
10774 O  O   . CYS D  267 ? 3.4036 3.7899 3.1801 0.5080  -0.4917 -0.0781 265  CYS D O   
10775 C  CB  . CYS D  267 ? 3.3969 3.8885 3.1696 0.3996  -0.5260 -0.1299 265  CYS D CB  
10776 S  SG  . CYS D  267 ? 3.4365 3.9563 3.2334 0.3593  -0.5305 -0.1616 265  CYS D SG  
10777 N  N   . VAL D  268 ? 3.0949 3.3255 2.7725 0.4374  -0.4883 -0.1350 266  VAL D N   
10778 C  CA  . VAL D  268 ? 3.0918 3.2640 2.7197 0.4482  -0.4822 -0.1237 266  VAL D CA  
10779 C  C   . VAL D  268 ? 3.1463 3.3930 2.7195 0.4130  -0.5091 -0.1053 266  VAL D C   
10780 O  O   . VAL D  268 ? 3.1574 3.4278 2.6737 0.3521  -0.5280 -0.1213 266  VAL D O   
10781 C  CB  . VAL D  268 ? 3.1669 3.2088 2.7323 0.4322  -0.4671 -0.1543 266  VAL D CB  
10782 C  CG1 . VAL D  268 ? 3.2400 3.2548 2.7441 0.3756  -0.4787 -0.1835 266  VAL D CG1 
10783 C  CG2 . VAL D  268 ? 3.2750 3.2650 2.7746 0.4313  -0.4644 -0.1450 266  VAL D CG2 
10784 N  N   . ARG D  269 ? 3.3019 3.5863 2.8870 0.4486  -0.5094 -0.0718 267  ARG D N   
10785 C  CA  . ARG D  269 ? 3.4419 3.8211 2.9867 0.4234  -0.5355 -0.0484 267  ARG D CA  
10786 C  C   . ARG D  269 ? 3.4620 3.7612 2.9153 0.3955  -0.5350 -0.0532 267  ARG D C   
10787 O  O   . ARG D  269 ? 3.4078 3.5979 2.8498 0.4220  -0.5119 -0.0594 267  ARG D O   
10788 C  CB  . ARG D  269 ? 3.4774 3.9567 3.0865 0.4852  -0.5372 -0.0039 267  ARG D CB  
10789 C  CG  . ARG D  269 ? 3.3852 3.9513 3.0814 0.5172  -0.5362 0.0038  267  ARG D CG  
10790 C  CD  . ARG D  269 ? 3.3525 4.0176 3.0385 0.4561  -0.5629 -0.0137 267  ARG D CD  
10791 N  NE  . ARG D  269 ? 3.2267 3.9437 2.9913 0.4781  -0.5572 -0.0187 267  ARG D NE  
10792 C  CZ  . ARG D  269 ? 3.0946 3.8889 2.8623 0.4289  -0.5746 -0.0379 267  ARG D CZ  
10793 N  NH1 . ARG D  269 ? 3.1138 3.9382 2.8050 0.3514  -0.5972 -0.0548 267  ARG D NH1 
10794 N  NH2 . ARG D  269 ? 2.9757 3.8127 2.8171 0.4531  -0.5669 -0.0419 267  ARG D NH2 
10795 N  N   . GLN D  270 ? 3.5054 3.8654 2.8909 0.3384  -0.5595 -0.0515 268  GLN D N   
10796 C  CA  . GLN D  270 ? 3.5282 3.8154 2.8150 0.3013  -0.5596 -0.0586 268  GLN D CA  
10797 C  C   . GLN D  270 ? 3.5591 3.8677 2.8547 0.3457  -0.5579 -0.0221 268  GLN D C   
10798 O  O   . GLN D  270 ? 3.6055 4.0337 2.9522 0.3793  -0.5709 0.0137  268  GLN D O   
10799 C  CB  . GLN D  270 ? 3.6006 3.9479 2.8051 0.2165  -0.5839 -0.0711 268  GLN D CB  
10800 C  CG  . GLN D  270 ? 3.7807 4.0502 2.8702 0.1686  -0.5825 -0.0812 268  GLN D CG  
10801 C  CD  . GLN D  270 ? 3.8922 4.2319 2.8961 0.0777  -0.6046 -0.0930 268  GLN D CD  
10802 O  OE1 . GLN D  270 ? 3.8662 4.3180 2.8981 0.0481  -0.6218 -0.0954 268  GLN D OE1 
10803 N  NE2 . GLN D  270 ? 3.9725 4.2484 2.8680 0.0290  -0.6024 -0.1022 268  GLN D NE2 
10804 N  N   . LEU D  271 ? 3.5305 3.7221 2.7721 0.3485  -0.5405 -0.0305 269  LEU D N   
10805 C  CA  . LEU D  271 ? 3.5572 3.7502 2.7959 0.3864  -0.5358 0.0013  269  LEU D CA  
10806 C  C   . LEU D  271 ? 3.7385 3.8160 2.8839 0.3555  -0.5243 -0.0178 269  LEU D C   
10807 O  O   . LEU D  271 ? 3.7809 3.7412 2.9192 0.3694  -0.4991 -0.0425 269  LEU D O   
10808 C  CB  . LEU D  271 ? 3.4728 3.6377 2.7948 0.4634  -0.5111 0.0183  269  LEU D CB  
10809 C  CG  . LEU D  271 ? 3.4866 3.6302 2.7999 0.5053  -0.4996 0.0498  269  LEU D CG  
10810 C  CD1 . LEU D  271 ? 3.6324 3.9043 2.9347 0.5072  -0.5270 0.0902  269  LEU D CD1 
10811 C  CD2 . LEU D  271 ? 3.4391 3.5378 2.8232 0.5721  -0.4690 0.0605  269  LEU D CD2 
10812 N  N   . TYR D  272 ? 3.9068 4.0236 2.9808 0.3151  -0.5419 -0.0062 270  TYR D N   
10813 C  CA  . TYR D  272 ? 4.0264 4.0386 3.0037 0.2831  -0.5309 -0.0224 270  TYR D CA  
10814 C  C   . TYR D  272 ? 4.1048 4.1055 3.0912 0.3289  -0.5215 0.0076  270  TYR D C   
10815 O  O   . TYR D  272 ? 4.1292 4.2344 3.1325 0.3432  -0.5394 0.0448  270  TYR D O   
10816 C  CB  . TYR D  272 ? 4.0262 4.0773 2.9058 0.2005  -0.5524 -0.0324 270  TYR D CB  
10817 C  CG  . TYR D  272 ? 4.0787 4.0280 2.8507 0.1661  -0.5407 -0.0456 270  TYR D CG  
10818 C  CD1 . TYR D  272 ? 4.0870 3.8855 2.7927 0.1499  -0.5156 -0.0831 270  TYR D CD1 
10819 C  CD2 . TYR D  272 ? 4.0676 4.0732 2.8011 0.1527  -0.5538 -0.0195 270  TYR D CD2 
10820 C  CE1 . TYR D  272 ? 4.1211 3.8234 2.7251 0.1222  -0.5018 -0.0953 270  TYR D CE1 
10821 C  CE2 . TYR D  272 ? 4.0934 4.0044 2.7265 0.1195  -0.5416 -0.0327 270  TYR D CE2 
10822 C  CZ  . TYR D  272 ? 4.1395 3.8970 2.7080 0.1045  -0.5147 -0.0712 270  TYR D CZ  
10823 O  OH  . TYR D  272 ? 4.2631 3.9235 2.7284 0.0750  -0.4996 -0.0843 270  TYR D OH  
10824 N  N   . ILE D  273 ? 3.9780 3.8558 2.9489 0.3520  -0.4927 -0.0082 271  ILE D N   
10825 C  CA  . ILE D  273 ? 3.8275 3.6766 2.8056 0.3944  -0.4775 0.0154  271  ILE D CA  
10826 C  C   . ILE D  273 ? 3.8689 3.6398 2.7461 0.3570  -0.4709 0.0018  271  ILE D C   
10827 O  O   . ILE D  273 ? 3.8161 3.4837 2.6473 0.3398  -0.4525 -0.0335 271  ILE D O   
10828 C  CB  . ILE D  273 ? 3.6900 3.4720 2.7368 0.4513  -0.4460 0.0084  271  ILE D CB  
10829 C  CG1 . ILE D  273 ? 3.7006 3.5580 2.8426 0.4907  -0.4497 0.0259  271  ILE D CG1 
10830 C  CG2 . ILE D  273 ? 3.6963 3.4292 2.7299 0.4824  -0.4256 0.0257  271  ILE D CG2 
10831 C  CD1 . ILE D  273 ? 3.7171 3.5153 2.9231 0.5417  -0.4165 0.0210  271  ILE D CD1 
10832 N  N   . ASP D  274 ? 3.9957 3.8158 2.8364 0.3485  -0.4843 0.0309  272  ASP D N   
10833 C  CA  . ASP D  274 ? 4.0818 3.8336 2.8280 0.3157  -0.4771 0.0226  272  ASP D CA  
10834 C  C   . ASP D  274 ? 4.0188 3.7181 2.7837 0.3658  -0.4535 0.0391  272  ASP D C   
10835 O  O   . ASP D  274 ? 3.9491 3.6983 2.7783 0.4155  -0.4530 0.0721  272  ASP D O   
10836 C  CB  . ASP D  274 ? 4.0446 3.8894 2.7284 0.2642  -0.5076 0.0422  272  ASP D CB  
10837 C  CG  . ASP D  274 ? 3.9485 3.7131 2.5164 0.2106  -0.5000 0.0227  272  ASP D CG  
10838 O  OD1 . ASP D  274 ? 3.8938 3.5529 2.4401 0.2326  -0.4729 0.0120  272  ASP D OD1 
10839 O  OD2 . ASP D  274 ? 3.9484 3.7577 2.4431 0.1431  -0.5195 0.0167  272  ASP D OD2 
10840 N  N   . PHE D  275 ? 3.9830 3.5770 2.6852 0.3528  -0.4312 0.0156  273  PHE D N   
10841 C  CA  . PHE D  275 ? 3.9494 3.4897 2.6635 0.3932  -0.4056 0.0258  273  PHE D CA  
10842 C  C   . PHE D  275 ? 3.9786 3.5632 2.6541 0.3893  -0.4183 0.0630  273  PHE D C   
10843 O  O   . PHE D  275 ? 3.9768 3.5694 2.6892 0.4343  -0.4080 0.0921  273  PHE D O   
10844 C  CB  . PHE D  275 ? 4.0633 3.4874 2.7273 0.3843  -0.3761 -0.0129 273  PHE D CB  
10845 C  CG  . PHE D  275 ? 4.0369 3.4184 2.7420 0.4005  -0.3600 -0.0460 273  PHE D CG  
10846 C  CD1 . PHE D  275 ? 3.9435 3.3091 2.7244 0.4480  -0.3359 -0.0499 273  PHE D CD1 
10847 C  CD2 . PHE D  275 ? 4.0382 3.3940 2.6997 0.3659  -0.3673 -0.0734 273  PHE D CD2 
10848 C  CE1 . PHE D  275 ? 3.8895 3.2275 2.7085 0.4626  -0.3223 -0.0795 273  PHE D CE1 
10849 C  CE2 . PHE D  275 ? 3.9483 3.2658 2.6439 0.3848  -0.3528 -0.1013 273  PHE D CE2 
10850 C  CZ  . PHE D  275 ? 3.8953 3.2105 2.6730 0.4342  -0.3317 -0.1038 273  PHE D CZ  
10851 N  N   . ARG D  276 ? 4.0825 3.6926 2.6771 0.3342  -0.4389 0.0627  274  ARG D N   
10852 C  CA  . ARG D  276 ? 4.1822 3.8450 2.7355 0.3271  -0.4536 0.0986  274  ARG D CA  
10853 C  C   . ARG D  276 ? 4.2478 4.0490 2.8547 0.3522  -0.4826 0.1434  274  ARG D C   
10854 O  O   . ARG D  276 ? 4.3940 4.2407 2.9935 0.3769  -0.4894 0.1834  274  ARG D O   
10855 C  CB  . ARG D  276 ? 4.1881 3.8371 2.6322 0.2539  -0.4646 0.0813  274  ARG D CB  
10856 C  CG  . ARG D  276 ? 4.1814 3.6905 2.5578 0.2362  -0.4329 0.0427  274  ARG D CG  
10857 C  CD  . ARG D  276 ? 4.1977 3.6619 2.5516 0.2591  -0.4148 0.0584  274  ARG D CD  
10858 N  NE  . ARG D  276 ? 4.2998 3.8147 2.5809 0.2194  -0.4349 0.0819  274  ARG D NE  
10859 C  CZ  . ARG D  276 ? 4.1895 3.7995 2.4944 0.2418  -0.4550 0.1288  274  ARG D CZ  
10860 N  NH1 . ARG D  276 ? 4.1266 3.7793 2.5216 0.3053  -0.4548 0.1572  274  ARG D NH1 
10861 N  NH2 . ARG D  276 ? 4.1759 3.8362 2.4089 0.2022  -0.4737 0.1481  274  ARG D NH2 
10862 N  N   . LYS D  277 ? 4.2401 4.1103 2.8988 0.3503  -0.4987 0.1386  275  LYS D N   
10863 C  CA  . LYS D  277 ? 4.2195 4.2364 2.9270 0.3734  -0.5273 0.1794  275  LYS D CA  
10864 C  C   . LYS D  277 ? 4.1906 4.2120 2.9931 0.4527  -0.5123 0.2024  275  LYS D C   
10865 O  O   . LYS D  277 ? 4.1874 4.2822 3.0147 0.5009  -0.5202 0.2490  275  LYS D O   
10866 C  CB  . LYS D  277 ? 4.1028 4.2065 2.8054 0.3187  -0.5541 0.1612  275  LYS D CB  
10867 C  CG  . LYS D  277 ? 4.0077 4.2840 2.7638 0.3400  -0.5850 0.2001  275  LYS D CG  
10868 C  CD  . LYS D  277 ? 4.0434 4.4239 2.7539 0.3331  -0.6084 0.2406  275  LYS D CD  
10869 C  CE  . LYS D  277 ? 3.9375 4.5104 2.6979 0.3539  -0.6408 0.2785  275  LYS D CE  
10870 N  NZ  . LYS D  277 ? 3.8357 4.4209 2.6930 0.4459  -0.6285 0.3062  275  LYS D NZ  
10871 N  N   . ASP D  278 ? 4.0378 3.9789 2.8878 0.4685  -0.4886 0.1712  276  ASP D N   
10872 C  CA  . ASP D  278 ? 3.9093 3.8497 2.8452 0.5342  -0.4716 0.1866  276  ASP D CA  
10873 C  C   . ASP D  278 ? 3.9005 3.7207 2.8431 0.5716  -0.4312 0.1819  276  ASP D C   
10874 O  O   . ASP D  278 ? 3.9048 3.7088 2.9067 0.6229  -0.4107 0.1942  276  ASP D O   
10875 C  CB  . ASP D  278 ? 3.7637 3.7166 2.7551 0.5245  -0.4737 0.1564  276  ASP D CB  
10876 C  CG  . ASP D  278 ? 3.6916 3.7700 2.6788 0.4842  -0.5114 0.1596  276  ASP D CG  
10877 O  OD1 . ASP D  278 ? 3.7150 3.9071 2.6939 0.4904  -0.5359 0.1977  276  ASP D OD1 
10878 O  OD2 . ASP D  278 ? 3.6811 3.7484 2.6705 0.4457  -0.5157 0.1241  276  ASP D OD2 
10879 N  N   . LEU D  279 ? 3.8550 3.5911 2.7346 0.5449  -0.4167 0.1633  277  LEU D N   
10880 C  CA  . LEU D  279 ? 3.9043 3.5354 2.7878 0.5730  -0.3770 0.1548  277  LEU D CA  
10881 C  C   . LEU D  279 ? 3.9625 3.5578 2.7748 0.5663  -0.3708 0.1727  277  LEU D C   
10882 O  O   . LEU D  279 ? 3.9868 3.5275 2.7996 0.6006  -0.3433 0.1888  277  LEU D O   
10883 C  CB  . LEU D  279 ? 3.9336 3.4843 2.8228 0.5518  -0.3554 0.1025  277  LEU D CB  
10884 C  CG  . LEU D  279 ? 3.9726 3.5321 2.9386 0.5688  -0.3488 0.0826  277  LEU D CG  
10885 C  CD1 . LEU D  279 ? 3.9707 3.4572 2.9305 0.5500  -0.3289 0.0335  277  LEU D CD1 
10886 C  CD2 . LEU D  279 ? 3.9756 3.5283 3.0015 0.6215  -0.3253 0.1048  277  LEU D CD2 
10887 N  N   . GLY D  280 ? 3.9676 3.5885 2.7122 0.5182  -0.3941 0.1689  278  GLY D N   
10888 C  CA  . GLY D  280 ? 4.0221 3.6085 2.6932 0.5045  -0.3892 0.1820  278  GLY D CA  
10889 C  C   . GLY D  280 ? 4.0461 3.5156 2.6882 0.4941  -0.3537 0.1460  278  GLY D C   
10890 O  O   . GLY D  280 ? 4.0766 3.4979 2.6881 0.5077  -0.3338 0.1600  278  GLY D O   
10891 N  N   . TRP D  281 ? 4.0779 3.5033 2.7264 0.4725  -0.3441 0.1006  279  TRP D N   
10892 C  CA  . TRP D  281 ? 4.0839 3.4134 2.7122 0.4688  -0.3096 0.0639  279  TRP D CA  
10893 C  C   . TRP D  281 ? 3.9950 3.2890 2.5409 0.4197  -0.3156 0.0356  279  TRP D C   
10894 O  O   . TRP D  281 ? 3.9850 3.2802 2.5236 0.3970  -0.3261 0.0111  279  TRP D O   
10895 C  CB  . TRP D  281 ? 4.1271 3.4328 2.8277 0.4938  -0.2884 0.0354  279  TRP D CB  
10896 C  CG  . TRP D  281 ? 4.1339 3.4469 2.9015 0.5382  -0.2706 0.0568  279  TRP D CG  
10897 C  CD1 . TRP D  281 ? 4.0964 3.4249 2.8601 0.5628  -0.2703 0.0995  279  TRP D CD1 
10898 C  CD2 . TRP D  281 ? 4.0796 3.3773 2.9182 0.5628  -0.2474 0.0364  279  TRP D CD2 
10899 N  NE1 . TRP D  281 ? 4.0222 3.3339 2.8440 0.6006  -0.2453 0.1063  279  TRP D NE1 
10900 C  CE2 . TRP D  281 ? 4.0423 3.3387 2.9126 0.5977  -0.2313 0.0667  279  TRP D CE2 
10901 C  CE3 . TRP D  281 ? 3.9665 3.2501 2.8394 0.5593  -0.2373 -0.0038 279  TRP D CE3 
10902 C  CZ2 . TRP D  281 ? 3.9855 3.2647 2.9187 0.6220  -0.2042 0.0551  279  TRP D CZ2 
10903 C  CZ3 . TRP D  281 ? 3.8863 3.1665 2.8287 0.5849  -0.2139 -0.0140 279  TRP D CZ3 
10904 C  CH2 . TRP D  281 ? 3.8953 3.1722 2.8664 0.6124  -0.1970 0.0139  279  TRP D CH2 
10905 N  N   . LYS D  282 ? 3.9560 3.2101 2.4328 0.4026  -0.3060 0.0386  280  LYS D N   
10906 C  CA  . LYS D  282 ? 4.0123 3.2187 2.3982 0.3566  -0.3056 0.0124  280  LYS D CA  
10907 C  C   . LYS D  282 ? 4.1247 3.2406 2.4925 0.3658  -0.2680 -0.0269 280  LYS D C   
10908 O  O   . LYS D  282 ? 4.2911 3.3512 2.5761 0.3357  -0.2593 -0.0485 280  LYS D O   
10909 C  CB  . LYS D  282 ? 4.1215 3.3481 2.4348 0.3274  -0.3202 0.0399  280  LYS D CB  
10910 C  CG  . LYS D  282 ? 4.1690 3.3821 2.3853 0.2660  -0.3342 0.0227  280  LYS D CG  
10911 C  CD  . LYS D  282 ? 4.1816 3.4399 2.3354 0.2358  -0.3536 0.0547  280  LYS D CD  
10912 C  CE  . LYS D  282 ? 4.1904 3.3989 2.3270 0.2574  -0.3293 0.0652  280  LYS D CE  
10913 N  NZ  . LYS D  282 ? 4.2606 3.5123 2.3317 0.2287  -0.3483 0.0976  280  LYS D NZ  
10914 N  N   . TRP D  283 ? 4.0616 3.1661 2.5021 0.4062  -0.2440 -0.0373 281  TRP D N   
10915 C  CA  . TRP D  283 ? 4.1536 3.1961 2.5875 0.4195  -0.2082 -0.0742 281  TRP D CA  
10916 C  C   . TRP D  283 ? 4.2203 3.2440 2.6675 0.4264  -0.2037 -0.1087 281  TRP D C   
10917 O  O   . TRP D  283 ? 4.2032 3.1856 2.6440 0.4431  -0.1750 -0.1398 281  TRP D O   
10918 C  CB  . TRP D  283 ? 4.1392 3.1856 2.6376 0.4531  -0.1811 -0.0699 281  TRP D CB  
10919 C  CG  . TRP D  283 ? 4.1662 3.2555 2.7556 0.4803  -0.1852 -0.0632 281  TRP D CG  
10920 C  CD1 . TRP D  283 ? 4.1476 3.2865 2.7761 0.4905  -0.2071 -0.0272 281  TRP D CD1 
10921 C  CD2 . TRP D  283 ? 4.1626 3.2530 2.8135 0.5024  -0.1659 -0.0932 281  TRP D CD2 
10922 N  NE1 . TRP D  283 ? 4.1337 3.2960 2.8424 0.5157  -0.2010 -0.0342 281  TRP D NE1 
10923 C  CE2 . TRP D  283 ? 4.1204 3.2551 2.8446 0.5208  -0.1766 -0.0748 281  TRP D CE2 
10924 C  CE3 . TRP D  283 ? 4.1238 3.1886 2.7736 0.5110  -0.1403 -0.1329 281  TRP D CE3 
10925 C  CZ2 . TRP D  283 ? 4.0516 3.2013 2.8463 0.5411  -0.1626 -0.0963 281  TRP D CZ2 
10926 C  CZ3 . TRP D  283 ? 4.0573 3.1469 2.7792 0.5341  -0.1282 -0.1525 281  TRP D CZ3 
10927 C  CH2 . TRP D  283 ? 4.0169 3.1464 2.8097 0.5457  -0.1395 -0.1350 281  TRP D CH2 
10928 N  N   . ILE D  284 ? 4.2916 3.3484 2.7550 0.4156  -0.2306 -0.1034 282  ILE D N   
10929 C  CA  . ILE D  284 ? 4.1841 3.2178 2.6513 0.4204  -0.2280 -0.1331 282  ILE D CA  
10930 C  C   . ILE D  284 ? 4.2748 3.2735 2.6443 0.3746  -0.2443 -0.1405 282  ILE D C   
10931 O  O   . ILE D  284 ? 4.3390 3.3868 2.6986 0.3426  -0.2747 -0.1194 282  ILE D O   
10932 C  CB  . ILE D  284 ? 4.0263 3.1196 2.5881 0.4410  -0.2416 -0.1251 282  ILE D CB  
10933 C  CG1 . ILE D  284 ? 4.0557 3.1709 2.7028 0.4806  -0.2192 -0.1225 282  ILE D CG1 
10934 C  CG2 . ILE D  284 ? 3.9259 2.9919 2.4787 0.4410  -0.2417 -0.1537 282  ILE D CG2 
10935 C  CD1 . ILE D  284 ? 4.0627 3.2311 2.8007 0.5010  -0.2286 -0.1152 282  ILE D CD1 
10936 N  N   . HIS D  285 ? 4.3736 3.2886 2.6661 0.3709  -0.2219 -0.1712 283  HIS D N   
10937 C  CA  . HIS D  285 ? 4.4118 3.2701 2.5911 0.3226  -0.2291 -0.1820 283  HIS D CA  
10938 C  C   . HIS D  285 ? 4.3233 3.1758 2.4996 0.3104  -0.2418 -0.1940 283  HIS D C   
10939 O  O   . HIS D  285 ? 4.2851 3.1620 2.4223 0.2609  -0.2670 -0.1848 283  HIS D O   
10940 C  CB  . HIS D  285 ? 4.4489 3.2058 2.5353 0.3278  -0.1950 -0.2095 283  HIS D CB  
10941 C  CG  . HIS D  285 ? 4.4577 3.2140 2.5283 0.3283  -0.1825 -0.2000 283  HIS D CG  
10942 N  ND1 . HIS D  285 ? 4.6825 3.3914 2.6465 0.2846  -0.1805 -0.1997 283  HIS D ND1 
10943 C  CD2 . HIS D  285 ? 4.4141 3.2082 2.5560 0.3628  -0.1693 -0.1917 283  HIS D CD2 
10944 C  CE1 . HIS D  285 ? 4.7393 3.4588 2.7132 0.2954  -0.1683 -0.1904 283  HIS D CE1 
10945 N  NE2 . HIS D  285 ? 4.6035 3.3723 2.6825 0.3417  -0.1606 -0.1856 283  HIS D NE2 
10946 N  N   . GLU D  286 ? 4.1740 2.9990 2.3875 0.3526  -0.2240 -0.2151 284  GLU D N   
10947 C  CA  . GLU D  286 ? 4.1114 2.9203 2.3181 0.3450  -0.2325 -0.2280 284  GLU D CA  
10948 C  C   . GLU D  286 ? 4.0269 2.8957 2.3558 0.3929  -0.2334 -0.2274 284  GLU D C   
10949 O  O   . GLU D  286 ? 4.0685 2.9418 2.4497 0.4400  -0.2112 -0.2356 284  GLU D O   
10950 C  CB  . GLU D  286 ? 4.1655 2.8498 2.2559 0.3451  -0.2051 -0.2591 284  GLU D CB  
10951 C  CG  . GLU D  286 ? 4.2361 2.8440 2.1885 0.2901  -0.2000 -0.2641 284  GLU D CG  
10952 C  CD  . GLU D  286 ? 4.1568 2.7916 2.0642 0.2182  -0.2298 -0.2549 284  GLU D CD  
10953 O  OE1 . GLU D  286 ? 4.1146 2.7916 2.0696 0.2132  -0.2475 -0.2533 284  GLU D OE1 
10954 O  OE2 . GLU D  286 ? 4.2066 2.8272 2.0301 0.1639  -0.2350 -0.2501 284  GLU D OE2 
10955 N  N   . PRO D  287 ? 3.9937 2.9142 2.3670 0.3773  -0.2581 -0.2193 285  PRO D N   
10956 C  CA  . PRO D  287 ? 4.0998 3.0350 2.4164 0.3166  -0.2849 -0.2109 285  PRO D CA  
10957 C  C   . PRO D  287 ? 4.1537 3.1857 2.5075 0.2939  -0.3115 -0.1769 285  PRO D C   
10958 O  O   . PRO D  287 ? 4.0997 3.1705 2.5166 0.3271  -0.3067 -0.1593 285  PRO D O   
10959 C  CB  . PRO D  287 ? 4.0113 2.9747 2.3789 0.3210  -0.2968 -0.2174 285  PRO D CB  
10960 C  CG  . PRO D  287 ? 3.9136 2.9320 2.4060 0.3800  -0.2895 -0.2115 285  PRO D CG  
10961 C  CD  . PRO D  287 ? 3.9404 2.9111 2.4204 0.4164  -0.2592 -0.2214 285  PRO D CD  
10962 N  N   . LYS D  288 ? 4.2136 3.2857 2.5231 0.2375  -0.3379 -0.1677 286  LYS D N   
10963 C  CA  . LYS D  288 ? 4.0866 3.2641 2.4225 0.2162  -0.3659 -0.1333 286  LYS D CA  
10964 C  C   . LYS D  288 ? 3.9539 3.2441 2.3707 0.2139  -0.3951 -0.1152 286  LYS D C   
10965 O  O   . LYS D  288 ? 3.8120 3.1974 2.2257 0.1814  -0.4229 -0.0912 286  LYS D O   
10966 C  CB  . LYS D  288 ? 4.0507 3.2065 2.2647 0.1485  -0.3734 -0.1352 286  LYS D CB  
10967 C  CG  . LYS D  288 ? 3.9915 3.0357 2.1194 0.1497  -0.3434 -0.1522 286  LYS D CG  
10968 C  CD  . LYS D  288 ? 4.0510 3.0584 2.0445 0.0745  -0.3470 -0.1602 286  LYS D CD  
10969 C  CE  . LYS D  288 ? 4.1132 3.0003 2.0163 0.0785  -0.3133 -0.1793 286  LYS D CE  
10970 N  NZ  . LYS D  288 ? 4.2825 3.1181 2.0425 0.0009  -0.3117 -0.1908 286  LYS D NZ  
10971 N  N   . GLY D  289 ? 4.0565 3.3444 2.5456 0.2490  -0.3887 -0.1265 287  GLY D N   
10972 C  CA  . GLY D  289 ? 4.0355 3.4257 2.6054 0.2516  -0.4127 -0.1117 287  GLY D CA  
10973 C  C   . GLY D  289 ? 4.0655 3.4207 2.6605 0.2603  -0.4052 -0.1377 287  GLY D C   
10974 O  O   . GLY D  289 ? 4.1548 3.4123 2.6672 0.2379  -0.3904 -0.1677 287  GLY D O   
10975 N  N   . TYR D  290 ? 3.9862 3.4152 2.6891 0.2947  -0.4134 -0.1257 288  TYR D N   
10976 C  CA  . TYR D  290 ? 3.9932 3.4027 2.7270 0.3019  -0.4091 -0.1479 288  TYR D CA  
10977 C  C   . TYR D  290 ? 3.8372 3.3634 2.6717 0.3150  -0.4300 -0.1272 288  TYR D C   
10978 O  O   . TYR D  290 ? 3.8065 3.4191 2.6902 0.3311  -0.4431 -0.0949 288  TYR D O   
10979 C  CB  . TYR D  290 ? 4.0473 3.3791 2.8105 0.3531  -0.3782 -0.1675 288  TYR D CB  
10980 C  CG  . TYR D  290 ? 4.0735 3.4582 2.9507 0.4074  -0.3700 -0.1508 288  TYR D CG  
10981 C  CD1 . TYR D  290 ? 4.0772 3.4851 2.9730 0.4261  -0.3658 -0.1267 288  TYR D CD1 
10982 C  CD2 . TYR D  290 ? 4.1613 3.5649 3.1191 0.4370  -0.3635 -0.1601 288  TYR D CD2 
10983 C  CE1 . TYR D  290 ? 4.0859 3.5255 3.0712 0.4714  -0.3527 -0.1129 288  TYR D CE1 
10984 C  CE2 . TYR D  290 ? 4.1154 3.5569 3.1663 0.4802  -0.3512 -0.1476 288  TYR D CE2 
10985 C  CZ  . TYR D  290 ? 4.0647 3.5196 3.1259 0.4965  -0.3445 -0.1244 288  TYR D CZ  
10986 O  OH  . TYR D  290 ? 4.0260 3.5032 3.1661 0.5353  -0.3271 -0.1134 288  TYR D OH  
10987 N  N   . HIS D  291 ? 3.8764 3.4011 2.7375 0.3119  -0.4311 -0.1452 289  HIS D N   
10988 C  CA  . HIS D  291 ? 3.8975 3.5300 2.8444 0.3175  -0.4505 -0.1306 289  HIS D CA  
10989 C  C   . HIS D  291 ? 3.8439 3.4785 2.8957 0.3793  -0.4330 -0.1292 289  HIS D C   
10990 O  O   . HIS D  291 ? 3.7619 3.3569 2.8329 0.3882  -0.4221 -0.1528 289  HIS D O   
10991 C  CB  . HIS D  291 ? 3.9303 3.5645 2.8327 0.2650  -0.4632 -0.1522 289  HIS D CB  
10992 C  CG  . HIS D  291 ? 4.0326 3.6866 2.8354 0.1937  -0.4811 -0.1529 289  HIS D CG  
10993 N  ND1 . HIS D  291 ? 4.1095 3.8986 2.9336 0.1621  -0.5101 -0.1323 289  HIS D ND1 
10994 C  CD2 . HIS D  291 ? 4.0465 3.6054 2.7235 0.1459  -0.4722 -0.1725 289  HIS D CD2 
10995 C  CE1 . HIS D  291 ? 4.1399 3.9234 2.8568 0.0919  -0.5195 -0.1406 289  HIS D CE1 
10996 N  NE2 . HIS D  291 ? 4.1241 3.7605 2.7471 0.0796  -0.4955 -0.1654 289  HIS D NE2 
10997 N  N   . ALA D  292 ? 3.8438 3.5232 2.9577 0.4203  -0.4287 -0.1012 290  ALA D N   
10998 C  CA  . ALA D  292 ? 3.7717 3.4553 2.9794 0.4727  -0.4091 -0.0985 290  ALA D CA  
10999 C  C   . ALA D  292 ? 3.7577 3.5425 3.0403 0.4840  -0.4253 -0.0785 290  ALA D C   
11000 O  O   . ALA D  292 ? 3.8344 3.6875 3.1455 0.5049  -0.4337 -0.0444 290  ALA D O   
11001 C  CB  . ALA D  292 ? 3.8565 3.5130 3.0760 0.5086  -0.3884 -0.0817 290  ALA D CB  
11002 N  N   . ASN D  293 ? 3.5961 3.3903 2.9087 0.4743  -0.4284 -0.0988 291  ASN D N   
11003 C  CA  . ASN D  293 ? 3.5389 3.4315 2.9189 0.4810  -0.4438 -0.0840 291  ASN D CA  
11004 C  C   . ASN D  293 ? 3.4077 3.3097 2.8768 0.5382  -0.4216 -0.0704 291  ASN D C   
11005 O  O   . ASN D  293 ? 3.3462 3.1870 2.8207 0.5671  -0.3960 -0.0698 291  ASN D O   
11006 C  CB  . ASN D  293 ? 3.5821 3.4752 2.9533 0.4445  -0.4538 -0.1123 291  ASN D CB  
11007 C  CG  . ASN D  293 ? 3.6814 3.5657 2.9540 0.3809  -0.4734 -0.1243 291  ASN D CG  
11008 O  OD1 . ASN D  293 ? 3.7203 3.6306 2.9433 0.3608  -0.4857 -0.1076 291  ASN D OD1 
11009 N  ND2 . ASN D  293 ? 3.7703 3.6138 3.0070 0.3461  -0.4745 -0.1538 291  ASN D ND2 
11010 N  N   . PHE D  294 ? 3.3361 3.3136 2.8710 0.5522  -0.4287 -0.0606 292  PHE D N   
11011 C  CA  . PHE D  294 ? 3.3262 3.3066 2.9378 0.6035  -0.4044 -0.0485 292  PHE D CA  
11012 C  C   . PHE D  294 ? 3.2878 3.3291 2.9602 0.6033  -0.4112 -0.0559 292  PHE D C   
11013 O  O   . PHE D  294 ? 3.1788 3.2765 2.8357 0.5654  -0.4375 -0.0637 292  PHE D O   
11014 C  CB  . PHE D  294 ? 3.3998 3.4174 3.0199 0.6439  -0.4013 -0.0056 292  PHE D CB  
11015 C  CG  . PHE D  294 ? 3.4397 3.5780 3.0628 0.6409  -0.4330 0.0239  292  PHE D CG  
11016 C  CD1 . PHE D  294 ? 3.5445 3.7230 3.1028 0.6027  -0.4608 0.0315  292  PHE D CD1 
11017 C  CD2 . PHE D  294 ? 3.3725 3.5904 3.0609 0.6758  -0.4336 0.0434  292  PHE D CD2 
11018 C  CE1 . PHE D  294 ? 3.5618 3.8701 3.1231 0.5961  -0.4905 0.0575  292  PHE D CE1 
11019 C  CE2 . PHE D  294 ? 3.3949 3.7425 3.0888 0.6762  -0.4630 0.0709  292  PHE D CE2 
11020 C  CZ  . PHE D  294 ? 3.4900 3.8892 3.1217 0.6348  -0.4924 0.0778  292  PHE D CZ  
11021 N  N   . CYS D  295 ? 3.3312 3.3580 3.0682 0.6421  -0.3848 -0.0549 293  CYS D N   
11022 C  CA  . CYS D  295 ? 3.1439 3.2203 2.9437 0.6470  -0.3851 -0.0626 293  CYS D CA  
11023 C  C   . CYS D  295 ? 3.0750 3.2207 2.9220 0.6944  -0.3805 -0.0252 293  CYS D C   
11024 O  O   . CYS D  295 ? 3.0532 3.1544 2.9115 0.7374  -0.3518 -0.0070 293  CYS D O   
11025 C  CB  . CYS D  295 ? 3.0718 3.0783 2.9056 0.6524  -0.3558 -0.0935 293  CYS D CB  
11026 S  SG  . CYS D  295 ? 3.1204 3.0469 2.8996 0.6130  -0.3562 -0.1349 293  CYS D SG  
11027 N  N   . LEU D  296 ? 2.9536 3.2064 2.8231 0.6873  -0.4062 -0.0139 294  LEU D N   
11028 C  CA  . LEU D  296 ? 2.9998 3.3351 2.9131 0.7384  -0.4039 0.0237  294  LEU D CA  
11029 C  C   . LEU D  296 ? 2.9329 3.3417 2.9041 0.7339  -0.4102 0.0125  294  LEU D C   
11030 O  O   . LEU D  296 ? 2.9408 3.4086 2.9014 0.6834  -0.4387 -0.0062 294  LEU D O   
11031 C  CB  . LEU D  296 ? 3.0714 3.5005 2.9495 0.7412  -0.4332 0.0589  294  LEU D CB  
11032 C  CG  . LEU D  296 ? 3.0992 3.5924 3.0024 0.8122  -0.4251 0.1083  294  LEU D CG  
11033 C  CD1 . LEU D  296 ? 2.9831 3.6026 2.9449 0.8332  -0.4363 0.1203  294  LEU D CD1 
11034 C  CD2 . LEU D  296 ? 3.1542 3.5278 3.0654 0.8650  -0.3788 0.1172  294  LEU D CD2 
11035 N  N   . GLY D  297 ? 2.8441 3.2438 2.8696 0.7841  -0.3811 0.0230  295  GLY D N   
11036 C  CA  . GLY D  297 ? 2.7204 3.1861 2.8037 0.7858  -0.3824 0.0135  295  GLY D CA  
11037 C  C   . GLY D  297 ? 2.6809 3.0682 2.8076 0.8200  -0.3390 0.0037  295  GLY D C   
11038 O  O   . GLY D  297 ? 2.7999 3.0748 2.9104 0.8177  -0.3112 -0.0128 295  GLY D O   
11039 N  N   . PRO D  298 ? 2.4592 2.9088 2.6393 0.8502  -0.3307 0.0127  296  PRO D N   
11040 C  CA  . PRO D  298 ? 2.4175 2.7926 2.6348 0.8777  -0.2868 0.0012  296  PRO D CA  
11041 C  C   . PRO D  298 ? 2.4311 2.7870 2.6755 0.8274  -0.2877 -0.0447 296  PRO D C   
11042 O  O   . PRO D  298 ? 2.4035 2.8204 2.6464 0.7801  -0.3221 -0.0632 296  PRO D O   
11043 C  CB  . PRO D  298 ? 2.4953 2.9548 2.7514 0.9377  -0.2788 0.0353  296  PRO D CB  
11044 C  CG  . PRO D  298 ? 2.5525 3.1599 2.8168 0.9111  -0.3276 0.0412  296  PRO D CG  
11045 C  CD  . PRO D  298 ? 2.5474 3.1458 2.7534 0.8637  -0.3585 0.0361  296  PRO D CD  
11046 N  N   . CYS D  299 ? 2.6961 2.9622 2.9588 0.8363  -0.2468 -0.0632 297  CYS D N   
11047 C  CA  . CYS D  299 ? 2.7392 2.9830 3.0302 0.7962  -0.2410 -0.1050 297  CYS D CA  
11048 C  C   . CYS D  299 ? 2.6820 2.8930 3.0144 0.8280  -0.1971 -0.1071 297  CYS D C   
11049 O  O   . CYS D  299 ? 2.7878 2.9039 3.1117 0.8308  -0.1575 -0.1202 297  CYS D O   
11050 C  CB  . CYS D  299 ? 2.8884 3.0468 3.1457 0.7586  -0.2357 -0.1355 297  CYS D CB  
11051 S  SG  . CYS D  299 ? 2.9068 3.0617 3.0975 0.7235  -0.2746 -0.1369 297  CYS D SG  
11052 N  N   . PRO D  300 ? 2.4882 2.7773 2.8623 0.8503  -0.2002 -0.0955 298  PRO D N   
11053 C  CA  . PRO D  300 ? 2.4818 2.7324 2.8898 0.8804  -0.1550 -0.0989 298  PRO D CA  
11054 C  C   . PRO D  300 ? 2.2559 2.5233 2.7048 0.8383  -0.1560 -0.1379 298  PRO D C   
11055 O  O   . PRO D  300 ? 2.2253 2.5301 2.6728 0.7881  -0.1918 -0.1611 298  PRO D O   
11056 C  CB  . PRO D  300 ? 2.6234 2.9542 3.0482 0.9423  -0.1558 -0.0567 298  PRO D CB  
11057 C  CG  . PRO D  300 ? 2.5956 3.0498 3.0161 0.9215  -0.2132 -0.0446 298  PRO D CG  
11058 C  CD  . PRO D  300 ? 2.4910 2.9096 2.8780 0.8554  -0.2402 -0.0744 298  PRO D CD  
11059 N  N   . TYR D  301 ? 2.2789 2.5114 2.7569 0.8578  -0.1145 -0.1453 299  TYR D N   
11060 C  CA  . TYR D  301 ? 2.2378 2.4875 2.7549 0.8190  -0.1131 -0.1815 299  TYR D CA  
11061 C  C   . TYR D  301 ? 2.2772 2.5236 2.8281 0.8572  -0.0730 -0.1752 299  TYR D C   
11062 O  O   . TYR D  301 ? 2.2819 2.4790 2.8160 0.9119  -0.0360 -0.1477 299  TYR D O   
11063 C  CB  . TYR D  301 ? 2.2578 2.4282 2.7607 0.7713  -0.0992 -0.2200 299  TYR D CB  
11064 C  CG  . TYR D  301 ? 2.4365 2.5044 2.9292 0.7819  -0.0405 -0.2294 299  TYR D CG  
11065 C  CD1 . TYR D  301 ? 2.4631 2.4682 2.9250 0.8297  -0.0053 -0.1997 299  TYR D CD1 
11066 C  CD2 . TYR D  301 ? 2.5149 2.5474 3.0214 0.7405  -0.0186 -0.2688 299  TYR D CD2 
11067 C  CE1 . TYR D  301 ? 2.5464 2.4467 2.9861 0.8307  0.0527  -0.2113 299  TYR D CE1 
11068 C  CE2 . TYR D  301 ? 2.4777 2.4209 2.9686 0.7393  0.0370  -0.2814 299  TYR D CE2 
11069 C  CZ  . TYR D  301 ? 2.4980 2.3704 2.9526 0.7817  0.0739  -0.2537 299  TYR D CZ  
11070 O  OH  . TYR D  301 ? 2.5207 2.2935 2.9476 0.7728  0.1337  -0.2687 299  TYR D OH  
11071 N  N   . ILE D  302 ? 2.4793 2.7715 3.0718 0.8281  -0.0787 -0.2013 300  ILE D N   
11072 C  CA  . ILE D  302 ? 2.6248 2.9230 3.2529 0.8566  -0.0432 -0.2014 300  ILE D CA  
11073 C  C   . ILE D  302 ? 2.7294 3.0859 3.3623 0.9290  -0.0399 -0.1558 300  ILE D C   
11074 O  O   . ILE D  302 ? 2.6357 2.9254 3.2541 0.9843  0.0085  -0.1356 300  ILE D O   
11075 C  CB  . ILE D  302 ? 2.5522 2.7254 3.1654 0.8539  0.0173  -0.2209 300  ILE D CB  
11076 C  CG1 . ILE D  302 ? 2.3795 2.5124 2.9841 0.7866  0.0101  -0.2619 300  ILE D CG1 
11077 C  CG2 . ILE D  302 ? 2.7315 2.9076 3.3799 0.8671  0.0524  -0.2313 300  ILE D CG2 
11078 C  CD1 . ILE D  302 ? 2.2772 2.4830 2.9189 0.7381  -0.0234 -0.2916 300  ILE D CD1 
11079 N  N   . TRP D  303 ? 2.9150 3.3963 3.5616 0.9292  -0.0895 -0.1390 301  TRP D N   
11080 C  CA  . TRP D  303 ? 2.8446 3.4182 3.5027 0.9964  -0.0939 -0.0960 301  TRP D CA  
11081 C  C   . TRP D  303 ? 2.7473 3.4339 3.4605 0.9968  -0.1022 -0.1039 301  TRP D C   
11082 O  O   . TRP D  303 ? 2.7428 3.4580 3.4795 0.9333  -0.1222 -0.1406 301  TRP D O   
11083 C  CB  . TRP D  303 ? 2.8186 3.4736 3.4525 0.9946  -0.1426 -0.0708 301  TRP D CB  
11084 C  CG  . TRP D  303 ? 3.0875 3.7768 3.7065 1.0781  -0.1317 -0.0187 301  TRP D CG  
11085 C  CD1 . TRP D  303 ? 3.1214 3.9639 3.7627 1.1181  -0.1575 0.0134  301  TRP D CD1 
11086 C  CD2 . TRP D  303 ? 3.1598 3.7300 3.7335 1.1339  -0.0899 0.0081  301  TRP D CD2 
11087 N  NE1 . TRP D  303 ? 3.1023 3.9308 3.7162 1.2018  -0.1358 0.0613  301  TRP D NE1 
11088 C  CE2 . TRP D  303 ? 3.1170 3.7704 3.6855 1.2124  -0.0932 0.0591  301  TRP D CE2 
11089 C  CE3 . TRP D  303 ? 3.1206 3.5256 3.6537 1.1232  -0.0491 -0.0063 301  TRP D CE3 
11090 C  CZ2 . TRP D  303 ? 3.0930 3.6557 3.6120 1.2835  -0.0562 0.0976  301  TRP D CZ2 
11091 C  CZ3 . TRP D  303 ? 3.2101 3.5248 3.6935 1.1861  -0.0114 0.0288  301  TRP D CZ3 
11092 C  CH2 . TRP D  303 ? 3.2019 3.5884 3.6760 1.2671  -0.0147 0.0811  301  TRP D CH2 
11093 N  N   . SER D  304 ? 2.6792 3.4298 3.4098 1.0720  -0.0850 -0.0684 302  SER D N   
11094 C  CA  . SER D  304 ? 2.6387 3.4948 3.4226 1.0833  -0.0839 -0.0739 302  SER D CA  
11095 C  C   . SER D  304 ? 2.5760 3.5787 3.3866 1.0184  -0.1436 -0.0920 302  SER D C   
11096 O  O   . SER D  304 ? 2.5632 3.6210 3.3497 0.9909  -0.1867 -0.0836 302  SER D O   
11097 C  CB  . SER D  304 ? 2.6761 3.5963 3.4683 1.1849  -0.0607 -0.0258 302  SER D CB  
11098 O  OG  . SER D  304 ? 2.6558 3.6678 3.4291 1.2154  -0.0959 0.0128  302  SER D OG  
11099 N  N   . LEU D  305 ? 2.5221 3.5802 3.3761 0.9901  -0.1427 -0.1188 303  LEU D N   
11100 C  CA  . LEU D  305 ? 2.3867 3.5737 3.2618 0.9219  -0.1916 -0.1415 303  LEU D CA  
11101 C  C   . LEU D  305 ? 2.1808 3.2956 3.0193 0.8349  -0.2200 -0.1762 303  LEU D C   
11102 O  O   . LEU D  305 ? 2.2068 3.3195 3.0045 0.8163  -0.2490 -0.1663 303  LEU D O   
11103 C  CB  . LEU D  305 ? 2.4927 3.8528 3.3733 0.9457  -0.2295 -0.1081 303  LEU D CB  
11104 C  CG  . LEU D  305 ? 2.3853 3.8460 3.3006 1.0423  -0.2065 -0.0677 303  LEU D CG  
11105 C  CD1 . LEU D  305 ? 2.1064 3.7336 3.0168 1.0672  -0.2458 -0.0308 303  LEU D CD1 
11106 C  CD2 . LEU D  305 ? 2.2583 3.7959 3.2282 1.0400  -0.1928 -0.0872 303  LEU D CD2 
11107 N  N   . VAL D  312 ? 2.2934 3.2952 3.0683 0.6353  -0.2767 -0.2702 310  VAL D N   
11108 C  CA  . VAL D  312 ? 2.1711 3.1253 2.9582 0.5902  -0.2669 -0.3085 310  VAL D CA  
11109 C  C   . VAL D  312 ? 2.1137 2.9408 2.8561 0.5570  -0.2660 -0.3297 310  VAL D C   
11110 O  O   . VAL D  312 ? 2.0394 2.8392 2.7653 0.5036  -0.2776 -0.3603 310  VAL D O   
11111 C  CB  . VAL D  312 ? 2.0473 3.1027 2.8371 0.5322  -0.2993 -0.3279 310  VAL D CB  
11112 C  CG1 . VAL D  312 ? 2.0022 3.1973 2.8452 0.5677  -0.2958 -0.3098 310  VAL D CG1 
11113 C  CG2 . VAL D  312 ? 1.9869 3.0607 2.7136 0.4816  -0.3421 -0.3290 310  VAL D CG2 
11114 N  N   . LEU D  313 ? 2.3224 3.0757 3.0429 0.5919  -0.2512 -0.3120 311  LEU D N   
11115 C  CA  . LEU D  313 ? 2.4590 3.1033 3.1370 0.5705  -0.2487 -0.3272 311  LEU D CA  
11116 C  C   . LEU D  313 ? 2.4736 3.1179 3.0977 0.5143  -0.2897 -0.3424 311  LEU D C   
11117 O  O   . LEU D  313 ? 2.3991 2.9630 2.9889 0.4901  -0.2896 -0.3621 311  LEU D O   
11118 C  CB  . LEU D  313 ? 2.4700 3.0388 3.1691 0.5625  -0.2131 -0.3546 311  LEU D CB  
11119 C  CG  . LEU D  313 ? 2.2012 2.7663 2.9045 0.5105  -0.2206 -0.3906 311  LEU D CG  
11120 C  CD1 . LEU D  313 ? 2.0824 2.5592 2.7530 0.4889  -0.2142 -0.4118 311  LEU D CD1 
11121 C  CD2 . LEU D  313 ? 2.0509 2.6400 2.8092 0.5189  -0.1901 -0.4016 311  LEU D CD2 
11122 N  N   . ALA D  314 ? 2.4043 3.1379 3.0138 0.4939  -0.3228 -0.3329 312  ALA D N   
11123 C  CA  . ALA D  314 ? 2.4150 3.1397 2.9607 0.4340  -0.3571 -0.3495 312  ALA D CA  
11124 C  C   . ALA D  314 ? 2.5404 3.1964 3.0242 0.4358  -0.3677 -0.3395 312  ALA D C   
11125 O  O   . ALA D  314 ? 2.3832 2.9492 2.8214 0.4140  -0.3684 -0.3580 312  ALA D O   
11126 C  CB  . ALA D  314 ? 2.2686 3.1153 2.8128 0.4032  -0.3853 -0.3452 312  ALA D CB  
11127 N  N   . LEU D  315 ? 2.7439 3.4446 3.2235 0.4646  -0.3754 -0.3092 313  LEU D N   
11128 C  CA  . LEU D  315 ? 2.6010 3.2447 3.0211 0.4658  -0.3859 -0.2979 313  LEU D CA  
11129 C  C   . LEU D  315 ? 2.5619 3.1073 2.9922 0.5055  -0.3544 -0.2961 313  LEU D C   
11130 O  O   . LEU D  315 ? 2.6020 3.1456 3.0537 0.5540  -0.3363 -0.2711 313  LEU D O   
11131 C  CB  . LEU D  315 ? 2.5265 3.2583 2.9414 0.4842  -0.4033 -0.2653 313  LEU D CB  
11132 C  CG  . LEU D  315 ? 2.5611 3.4038 2.9541 0.4356  -0.4367 -0.2673 313  LEU D CG  
11133 C  CD1 . LEU D  315 ? 2.6018 3.5466 2.9959 0.4610  -0.4519 -0.2322 313  LEU D CD1 
11134 C  CD2 . LEU D  315 ? 2.5173 3.2952 2.8246 0.3662  -0.4572 -0.2938 313  LEU D CD2 
11135 N  N   . TYR D  316 ? 2.4607 2.9248 2.8703 0.4836  -0.3466 -0.3233 314  TYR D N   
11136 C  CA  . TYR D  316 ? 2.4617 2.8433 2.8778 0.5098  -0.3169 -0.3282 314  TYR D CA  
11137 C  C   . TYR D  316 ? 2.4202 2.7279 2.7696 0.4959  -0.3267 -0.3359 314  TYR D C   
11138 O  O   . TYR D  316 ? 2.4140 2.6639 2.7635 0.5168  -0.3038 -0.3383 314  TYR D O   
11139 C  CB  . TYR D  316 ? 2.5478 2.9103 3.0057 0.5031  -0.2930 -0.3540 314  TYR D CB  
11140 C  CG  . TYR D  316 ? 2.5406 2.8633 3.0369 0.5381  -0.2509 -0.3519 314  TYR D CG  
11141 C  CD1 . TYR D  316 ? 2.4881 2.7411 2.9640 0.5389  -0.2330 -0.3645 314  TYR D CD1 
11142 C  CD2 . TYR D  316 ? 2.4178 2.7718 2.9646 0.5692  -0.2260 -0.3384 314  TYR D CD2 
11143 C  CE1 . TYR D  316 ? 2.2842 2.4991 2.7862 0.5606  -0.1913 -0.3660 314  TYR D CE1 
11144 C  CE2 . TYR D  316 ? 2.2963 2.5968 2.8634 0.5960  -0.1819 -0.3382 314  TYR D CE2 
11145 C  CZ  . TYR D  316 ? 2.1692 2.3999 2.7124 0.5870  -0.1647 -0.3533 314  TYR D CZ  
11146 O  OH  . TYR D  316 ? 2.1283 2.3045 2.6829 0.6036  -0.1180 -0.3564 314  TYR D OH  
11147 N  N   . ASN D  317 ? 2.3398 2.6467 2.6274 0.4600  -0.3571 -0.3406 315  ASN D N   
11148 C  CA  . ASN D  317 ? 2.4076 2.6366 2.6227 0.4490  -0.3641 -0.3489 315  ASN D CA  
11149 C  C   . ASN D  317 ? 2.5684 2.7835 2.7514 0.4677  -0.3682 -0.3257 315  ASN D C   
11150 O  O   . ASN D  317 ? 2.5544 2.7009 2.6913 0.4730  -0.3639 -0.3304 315  ASN D O   
11151 C  CB  . ASN D  317 ? 2.5139 2.7275 2.6605 0.4008  -0.3892 -0.3652 315  ASN D CB  
11152 C  CG  . ASN D  317 ? 2.6783 2.9773 2.8301 0.3703  -0.4105 -0.3582 315  ASN D CG  
11153 O  OD1 . ASN D  317 ? 2.7999 3.1728 2.9926 0.3898  -0.4127 -0.3354 315  ASN D OD1 
11154 N  ND2 . ASN D  317 ? 2.7156 3.0081 2.8223 0.3229  -0.4251 -0.3776 315  ASN D ND2 
11155 N  N   . GLN D  318 ? 2.7318 3.0150 2.9367 0.4802  -0.3763 -0.3000 316  GLN D N   
11156 C  CA  . GLN D  318 ? 2.6462 2.9228 2.8239 0.5010  -0.3795 -0.2751 316  GLN D CA  
11157 C  C   . GLN D  318 ? 2.5781 2.8688 2.8114 0.5529  -0.3538 -0.2516 316  GLN D C   
11158 O  O   . GLN D  318 ? 2.5303 2.7792 2.7415 0.5755  -0.3442 -0.2373 316  GLN D O   
11159 C  CB  . GLN D  318 ? 2.6563 3.0023 2.7963 0.4732  -0.4115 -0.2604 316  GLN D CB  
11160 C  CG  . GLN D  318 ? 2.7603 3.0699 2.8172 0.4169  -0.4336 -0.2813 316  GLN D CG  
11161 C  CD  . GLN D  318 ? 2.9241 3.2957 2.9315 0.3840  -0.4611 -0.2672 316  GLN D CD  
11162 O  OE1 . GLN D  318 ? 3.0608 3.4122 2.9938 0.3296  -0.4778 -0.2837 316  GLN D OE1 
11163 N  NE2 . GLN D  318 ? 2.9164 3.3628 2.9583 0.4157  -0.4640 -0.2364 316  GLN D NE2 
11164 N  N   . HIS D  319 ? 2.7151 3.0560 3.0128 0.5723  -0.3397 -0.2475 317  HIS D N   
11165 C  CA  . HIS D  319 ? 2.7674 3.1100 3.1056 0.6250  -0.3106 -0.2230 317  HIS D CA  
11166 C  C   . HIS D  319 ? 2.6866 2.9354 3.0284 0.6398  -0.2735 -0.2360 317  HIS D C   
11167 O  O   . HIS D  319 ? 2.6879 2.8958 3.0169 0.6705  -0.2539 -0.2175 317  HIS D O   
11168 C  CB  . HIS D  319 ? 2.8068 3.2221 3.2059 0.6431  -0.3019 -0.2169 317  HIS D CB  
11169 C  CG  . HIS D  319 ? 2.8756 3.4052 3.2771 0.6336  -0.3352 -0.2007 317  HIS D CG  
11170 N  ND1 . HIS D  319 ? 2.9702 3.5306 3.3180 0.5990  -0.3708 -0.1971 317  HIS D ND1 
11171 C  CD2 . HIS D  319 ? 2.8305 3.4578 3.2792 0.6520  -0.3367 -0.1883 317  HIS D CD2 
11172 C  CE1 . HIS D  319 ? 2.8971 3.5757 3.2593 0.5915  -0.3936 -0.1843 317  HIS D CE1 
11173 N  NE2 . HIS D  319 ? 2.8205 3.5467 3.2467 0.6260  -0.3744 -0.1781 317  HIS D NE2 
11174 N  N   . ASN D  320 ? 2.6543 2.8727 3.0105 0.6158  -0.2626 -0.2681 318  ASN D N   
11175 C  CA  . ASN D  320 ? 2.6426 2.7902 3.0038 0.6218  -0.2270 -0.2847 318  ASN D CA  
11176 C  C   . ASN D  320 ? 2.5343 2.6637 2.8885 0.5871  -0.2321 -0.3198 318  ASN D C   
11177 O  O   . ASN D  320 ? 2.4591 2.5958 2.8521 0.5781  -0.2149 -0.3392 318  ASN D O   
11178 C  CB  . ASN D  320 ? 2.6393 2.7788 3.0476 0.6493  -0.1864 -0.2797 318  ASN D CB  
11179 C  CG  . ASN D  320 ? 2.5198 2.5865 2.9244 0.6497  -0.1446 -0.2960 318  ASN D CG  
11180 O  OD1 . ASN D  320 ? 2.4921 2.5215 2.8612 0.6404  -0.1454 -0.3030 318  ASN D OD1 
11181 N  ND2 . ASN D  320 ? 2.5047 2.5528 2.9425 0.6580  -0.1056 -0.3033 318  ASN D ND2 
11182 N  N   . PRO D  321 ? 2.6556 2.7599 2.9567 0.5696  -0.2539 -0.3280 319  PRO D N   
11183 C  CA  . PRO D  321 ? 2.6396 2.7238 2.9266 0.5466  -0.2566 -0.3579 319  PRO D CA  
11184 C  C   . PRO D  321 ? 2.6374 2.6875 2.9335 0.5543  -0.2250 -0.3747 319  PRO D C   
11185 O  O   . PRO D  321 ? 2.7457 2.7957 3.0432 0.5406  -0.2222 -0.3992 319  PRO D O   
11186 C  CB  . PRO D  321 ? 2.6951 2.7571 2.9096 0.5318  -0.2883 -0.3560 319  PRO D CB  
11187 C  CG  . PRO D  321 ? 2.8250 2.8765 3.0170 0.5501  -0.2898 -0.3307 319  PRO D CG  
11188 C  CD  . PRO D  321 ? 2.8010 2.8951 3.0471 0.5711  -0.2773 -0.3093 319  PRO D CD  
11189 N  N   . GLY D  322 ? 2.4099 2.4353 2.7084 0.5740  -0.2007 -0.3625 320  GLY D N   
11190 C  CA  . GLY D  322 ? 2.3637 2.3657 2.6726 0.5741  -0.1654 -0.3801 320  GLY D CA  
11191 C  C   . GLY D  322 ? 2.4554 2.4613 2.8145 0.5713  -0.1281 -0.3897 320  GLY D C   
11192 O  O   . GLY D  322 ? 2.4120 2.4085 2.7792 0.5592  -0.0980 -0.4115 320  GLY D O   
11193 N  N   . ALA D  323 ? 2.3795 2.4024 2.7688 0.5810  -0.1275 -0.3750 321  ALA D N   
11194 C  CA  . ALA D  323 ? 2.2094 2.2253 2.6393 0.5817  -0.0884 -0.3823 321  ALA D CA  
11195 C  C   . ALA D  323 ? 2.2503 2.2083 2.6658 0.5912  -0.0427 -0.3793 321  ALA D C   
11196 O  O   . ALA D  323 ? 2.3029 2.2394 2.7338 0.5758  -0.0020 -0.3991 321  ALA D O   
11197 C  CB  . ALA D  323 ? 2.1568 2.1985 2.6147 0.5511  -0.0822 -0.4159 321  ALA D CB  
11198 N  N   . SER D  324 ? 2.2350 2.1642 2.6148 0.6126  -0.0474 -0.3553 322  SER D N   
11199 C  CA  . SER D  324 ? 2.3976 2.2632 2.7521 0.6194  -0.0040 -0.3515 322  SER D CA  
11200 C  C   . SER D  324 ? 2.4384 2.2659 2.7978 0.6507  0.0274  -0.3272 322  SER D C   
11201 O  O   . SER D  324 ? 2.3220 2.1852 2.7038 0.6753  0.0082  -0.3066 322  SER D O   
11202 C  CB  . SER D  324 ? 2.5721 2.4184 2.8814 0.6296  -0.0203 -0.3357 322  SER D CB  
11203 O  OG  . SER D  324 ? 2.7407 2.5262 3.0208 0.6260  0.0231  -0.3393 322  SER D OG  
11204 N  N   . ALA D  325 ? 2.5763 2.3297 2.9087 0.6500  0.0792  -0.3300 323  ALA D N   
11205 C  CA  . ALA D  325 ? 2.4676 2.1630 2.7896 0.6847  0.1185  -0.3065 323  ALA D CA  
11206 C  C   . ALA D  325 ? 2.4612 2.1562 2.7618 0.7366  0.0973  -0.2601 323  ALA D C   
11207 O  O   . ALA D  325 ? 2.3753 2.0603 2.6798 0.7797  0.1108  -0.2327 323  ALA D O   
11208 C  CB  . ALA D  325 ? 2.5048 2.1050 2.7852 0.6655  0.1827  -0.3221 323  ALA D CB  
11209 N  N   . ALA D  326 ? 2.6214 2.3320 2.8967 0.7353  0.0645  -0.2500 324  ALA D N   
11210 C  CA  . ALA D  326 ? 2.5985 2.3203 2.8507 0.7788  0.0403  -0.2070 324  ALA D CA  
11211 C  C   . ALA D  326 ? 2.5094 2.2923 2.7577 0.7596  -0.0151 -0.2094 324  ALA D C   
11212 O  O   . ALA D  326 ? 2.5249 2.2784 2.7383 0.7428  -0.0161 -0.2170 324  ALA D O   
11213 C  CB  . ALA D  326 ? 2.7243 2.3525 2.9191 0.8029  0.0808  -0.1856 324  ALA D CB  
11214 N  N   . PRO D  327 ? 2.4405 2.3053 2.7181 0.7588  -0.0593 -0.2047 325  PRO D N   
11215 C  CA  . PRO D  327 ? 2.5449 2.4542 2.8050 0.7370  -0.1082 -0.2078 325  PRO D CA  
11216 C  C   . PRO D  327 ? 2.6781 2.5869 2.8972 0.7627  -0.1250 -0.1721 325  PRO D C   
11217 O  O   . PRO D  327 ? 2.8900 2.8211 3.1119 0.8018  -0.1243 -0.1379 325  PRO D O   
11218 C  CB  . PRO D  327 ? 2.5065 2.4964 2.8033 0.7259  -0.1423 -0.2124 325  PRO D CB  
11219 C  CG  . PRO D  327 ? 2.3714 2.3563 2.7124 0.7322  -0.1094 -0.2238 325  PRO D CG  
11220 C  CD  . PRO D  327 ? 2.4090 2.3259 2.7336 0.7687  -0.0629 -0.2036 325  PRO D CD  
11221 N  N   . CYS D  328 ? 2.5519 2.4391 2.7311 0.7430  -0.1394 -0.1796 326  CYS D N   
11222 C  CA  . CYS D  328 ? 2.6083 2.4938 2.7431 0.7594  -0.1571 -0.1498 326  CYS D CA  
11223 C  C   . CYS D  328 ? 2.6545 2.5858 2.7657 0.7308  -0.2048 -0.1557 326  CYS D C   
11224 O  O   . CYS D  328 ? 2.7454 2.6732 2.8548 0.6986  -0.2150 -0.1869 326  CYS D O   
11225 C  CB  . CYS D  328 ? 2.6390 2.4449 2.7333 0.7607  -0.1262 -0.1518 326  CYS D CB  
11226 S  SG  . CYS D  328 ? 2.8474 2.5725 2.9411 0.7872  -0.0625 -0.1443 326  CYS D SG  
11227 N  N   . CYS D  329 ? 2.7621 2.7326 2.8471 0.7433  -0.2316 -0.1250 327  CYS D N   
11228 C  CA  . CYS D  329 ? 2.9162 2.9234 2.9639 0.7118  -0.2738 -0.1283 327  CYS D CA  
11229 C  C   . CYS D  329 ? 2.9756 2.9176 2.9683 0.6996  -0.2698 -0.1364 327  CYS D C   
11230 O  O   . CYS D  329 ? 3.1158 3.0495 3.0704 0.7115  -0.2747 -0.1122 327  CYS D O   
11231 C  CB  . CYS D  329 ? 2.9598 3.0492 3.0027 0.7258  -0.3019 -0.0933 327  CYS D CB  
11232 S  SG  . CYS D  329 ? 3.1081 3.2578 3.0982 0.6778  -0.3528 -0.0954 327  CYS D SG  
11233 N  N   . VAL D  330 ? 2.8341 2.7340 2.8224 0.6777  -0.2600 -0.1708 328  VAL D N   
11234 C  CA  . VAL D  330 ? 2.8828 2.7243 2.8255 0.6701  -0.2499 -0.1831 328  VAL D CA  
11235 C  C   . VAL D  330 ? 2.8793 2.7153 2.7745 0.6406  -0.2777 -0.2018 328  VAL D C   
11236 O  O   . VAL D  330 ? 2.8557 2.7176 2.7599 0.6220  -0.2952 -0.2159 328  VAL D O   
11237 C  CB  . VAL D  330 ? 2.9867 2.7878 2.9554 0.6734  -0.2105 -0.2072 328  VAL D CB  
11238 C  CG1 . VAL D  330 ? 2.9999 2.7823 2.9950 0.6991  -0.1763 -0.1891 328  VAL D CG1 
11239 C  CG2 . VAL D  330 ? 2.9485 2.7711 2.9529 0.6568  -0.2121 -0.2370 328  VAL D CG2 
11240 N  N   . PRO D  331 ? 2.7535 2.5487 2.5908 0.6354  -0.2797 -0.2028 329  PRO D N   
11241 C  CA  . PRO D  331 ? 2.8090 2.5808 2.5883 0.6111  -0.2996 -0.2213 329  PRO D CA  
11242 C  C   . PRO D  331 ? 2.7502 2.4993 2.5404 0.6106  -0.2850 -0.2538 329  PRO D C   
11243 O  O   . PRO D  331 ? 2.7168 2.4562 2.5375 0.6254  -0.2565 -0.2651 329  PRO D O   
11244 C  CB  . PRO D  331 ? 2.8791 2.6101 2.5969 0.6125  -0.2981 -0.2120 329  PRO D CB  
11245 C  CG  . PRO D  331 ? 2.8224 2.5419 2.5734 0.6373  -0.2673 -0.2030 329  PRO D CG  
11246 C  CD  . PRO D  331 ? 2.7973 2.5590 2.6113 0.6518  -0.2620 -0.1866 329  PRO D CD  
11247 N  N   . GLN D  332 ? 2.9761 2.7185 2.7354 0.5918  -0.3037 -0.2688 330  GLN D N   
11248 C  CA  . GLN D  332 ? 3.0173 2.7397 2.7756 0.5957  -0.2934 -0.2969 330  GLN D CA  
11249 C  C   . GLN D  332 ? 3.1553 2.8195 2.8344 0.5995  -0.2923 -0.3085 330  GLN D C   
11250 O  O   . GLN D  332 ? 3.2986 2.9535 2.9823 0.6192  -0.2724 -0.3255 330  GLN D O   
11251 C  CB  . GLN D  332 ? 2.9189 2.6606 2.6870 0.5772  -0.3102 -0.3066 330  GLN D CB  
11252 C  CG  . GLN D  332 ? 2.8939 2.6207 2.6630 0.5852  -0.2999 -0.3328 330  GLN D CG  
11253 C  CD  . GLN D  332 ? 3.0335 2.7784 2.8151 0.5659  -0.3144 -0.3415 330  GLN D CD  
11254 O  OE1 . GLN D  332 ? 3.1365 2.9050 2.9187 0.5427  -0.3336 -0.3299 330  GLN D OE1 
11255 N  NE2 . GLN D  332 ? 3.0285 2.7702 2.8198 0.5750  -0.3053 -0.3620 330  GLN D NE2 
11256 N  N   . ALA D  333 ? 3.0447 2.6731 2.6478 0.5809  -0.3115 -0.3001 331  ALA D N   
11257 C  CA  . ALA D  333 ? 3.1081 2.6676 2.6219 0.5847  -0.3085 -0.3102 331  ALA D CA  
11258 C  C   . ALA D  333 ? 3.2831 2.8235 2.7555 0.5799  -0.3102 -0.2932 331  ALA D C   
11259 O  O   . ALA D  333 ? 3.3971 2.9612 2.8642 0.5570  -0.3284 -0.2740 331  ALA D O   
11260 C  CB  . ALA D  333 ? 3.0981 2.6096 2.5348 0.5604  -0.3249 -0.3198 331  ALA D CB  
11261 N  N   . LEU D  334 ? 3.3077 2.8138 2.7513 0.6018  -0.2914 -0.3002 332  LEU D N   
11262 C  CA  . LEU D  334 ? 3.2896 2.7719 2.6895 0.5984  -0.2899 -0.2864 332  LEU D CA  
11263 C  C   . LEU D  334 ? 3.3390 2.7467 2.6438 0.6058  -0.2818 -0.3002 332  LEU D C   
11264 O  O   . LEU D  334 ? 3.3119 2.6952 2.5991 0.6273  -0.2705 -0.3194 332  LEU D O   
11265 C  CB  . LEU D  334 ? 3.1959 2.7122 2.6581 0.6183  -0.2689 -0.2787 332  LEU D CB  
11266 C  CG  . LEU D  334 ? 3.0832 2.6546 2.6216 0.6162  -0.2710 -0.2589 332  LEU D CG  
11267 C  CD1 . LEU D  334 ? 2.9707 2.5812 2.5846 0.6242  -0.2617 -0.2718 332  LEU D CD1 
11268 C  CD2 . LEU D  334 ? 3.1964 2.7675 2.7486 0.6282  -0.2517 -0.2446 332  LEU D CD2 
11269 N  N   . GLU D  335 ? 3.5002 2.8717 2.7393 0.5905  -0.2866 -0.2891 333  GLU D N   
11270 C  CA  . GLU D  335 ? 3.6477 2.9374 2.7833 0.5948  -0.2774 -0.3006 333  GLU D CA  
11271 C  C   . GLU D  335 ? 3.5538 2.8347 2.6742 0.6059  -0.2631 -0.2940 333  GLU D C   
11272 O  O   . GLU D  335 ? 3.5432 2.8574 2.6892 0.5903  -0.2712 -0.2739 333  GLU D O   
11273 C  CB  . GLU D  335 ? 3.7529 2.9870 2.7925 0.5522  -0.2963 -0.2983 333  GLU D CB  
11274 C  CG  . GLU D  335 ? 3.8683 3.0985 2.9048 0.5357  -0.3082 -0.3076 333  GLU D CG  
11275 C  CD  . GLU D  335 ? 3.9988 3.1673 2.9264 0.4851  -0.3221 -0.3095 333  GLU D CD  
11276 O  OE1 . GLU D  335 ? 4.0328 3.1530 2.8795 0.4653  -0.3203 -0.3058 333  GLU D OE1 
11277 O  OE2 . GLU D  335 ? 4.0704 3.2382 2.9890 0.4605  -0.3333 -0.3161 333  GLU D OE2 
11278 N  N   . PRO D  336 ? 3.4819 2.7206 2.5582 0.6352  -0.2411 -0.3096 334  PRO D N   
11279 C  CA  . PRO D  336 ? 3.5113 2.7434 2.5717 0.6448  -0.2252 -0.3060 334  PRO D CA  
11280 C  C   . PRO D  336 ? 3.6812 2.8532 2.6471 0.6133  -0.2358 -0.2952 334  PRO D C   
11281 O  O   . PRO D  336 ? 3.7583 2.8845 2.6566 0.5842  -0.2513 -0.2950 334  PRO D O   
11282 C  CB  . PRO D  336 ? 3.5703 2.7839 2.6082 0.6879  -0.1992 -0.3281 334  PRO D CB  
11283 C  CG  . PRO D  336 ? 3.6107 2.7724 2.5931 0.6950  -0.2046 -0.3390 334  PRO D CG  
11284 C  CD  . PRO D  336 ? 3.5835 2.7814 2.6193 0.6650  -0.2285 -0.3303 334  PRO D CD  
11285 N  N   . LEU D  337 ? 3.7557 2.9283 2.7127 0.6149  -0.2254 -0.2876 335  LEU D N   
11286 C  CA  . LEU D  337 ? 3.7714 2.8973 2.6441 0.5830  -0.2343 -0.2761 335  LEU D CA  
11287 C  C   . LEU D  337 ? 3.7237 2.8062 2.5436 0.6030  -0.2092 -0.2857 335  LEU D C   
11288 O  O   . LEU D  337 ? 3.6929 2.8184 2.5694 0.6225  -0.1934 -0.2844 335  LEU D O   
11289 C  CB  . LEU D  337 ? 3.7672 2.9522 2.6864 0.5572  -0.2539 -0.2481 335  LEU D CB  
11290 C  CG  . LEU D  337 ? 3.8753 3.0291 2.7130 0.5235  -0.2637 -0.2342 335  LEU D CG  
11291 C  CD1 . LEU D  337 ? 3.9538 3.0529 2.6953 0.4846  -0.2779 -0.2420 335  LEU D CD1 
11292 C  CD2 . LEU D  337 ? 3.8961 3.1192 2.7850 0.5106  -0.2809 -0.2029 335  LEU D CD2 
11293 N  N   . PRO D  338 ? 3.6498 2.6452 2.3578 0.5973  -0.2017 -0.2966 336  PRO D N   
11294 C  CA  . PRO D  338 ? 3.7510 2.7050 2.4029 0.6144  -0.1777 -0.3042 336  PRO D CA  
11295 C  C   . PRO D  338 ? 3.9201 2.8721 2.5418 0.5766  -0.1874 -0.2856 336  PRO D C   
11296 O  O   . PRO D  338 ? 4.0501 2.9967 2.6390 0.5324  -0.2114 -0.2714 336  PRO D O   
11297 C  CB  . PRO D  338 ? 3.8255 2.6744 2.3591 0.6242  -0.1642 -0.3221 336  PRO D CB  
11298 C  CG  . PRO D  338 ? 3.7456 2.5663 2.2438 0.5821  -0.1881 -0.3173 336  PRO D CG  
11299 C  CD  . PRO D  338 ? 3.6091 2.5320 2.2322 0.5788  -0.2092 -0.3057 336  PRO D CD  
11300 N  N   . ILE D  339 ? 3.8902 2.8538 2.5215 0.5928  -0.1683 -0.2860 337  ILE D N   
11301 C  CA  . ILE D  339 ? 3.8920 2.8572 2.4983 0.5625  -0.1747 -0.2673 337  ILE D CA  
11302 C  C   . ILE D  339 ? 4.1125 3.0196 2.6414 0.5736  -0.1483 -0.2809 337  ILE D C   
11303 O  O   . ILE D  339 ? 4.0747 2.9656 2.5959 0.6138  -0.1225 -0.3026 337  ILE D O   
11304 C  CB  . ILE D  339 ? 3.7122 2.7581 2.4189 0.5659  -0.1783 -0.2477 337  ILE D CB  
11305 C  CG1 . ILE D  339 ? 3.6883 2.7647 2.4523 0.6038  -0.1479 -0.2648 337  ILE D CG1 
11306 C  CG2 . ILE D  339 ? 3.6627 2.7641 2.4413 0.5575  -0.2029 -0.2326 337  ILE D CG2 
11307 C  CD1 . ILE D  339 ? 3.6514 2.7861 2.4957 0.6031  -0.1431 -0.2487 337  ILE D CD1 
11308 N  N   . VAL D  340 ? 4.3476 3.2306 2.8186 0.5390  -0.1548 -0.2671 338  VAL D N   
11309 C  CA  . VAL D  340 ? 4.2332 3.0607 2.6262 0.5425  -0.1307 -0.2777 338  VAL D CA  
11310 C  C   . VAL D  340 ? 4.1793 3.0425 2.5904 0.5199  -0.1360 -0.2559 338  VAL D C   
11311 O  O   . VAL D  340 ? 4.0887 2.9639 2.4821 0.4805  -0.1619 -0.2328 338  VAL D O   
11312 C  CB  . VAL D  340 ? 4.2143 2.9399 2.4734 0.5162  -0.1287 -0.2878 338  VAL D CB  
11313 C  CG1 . VAL D  340 ? 4.2508 2.9207 2.4290 0.5157  -0.1042 -0.2961 338  VAL D CG1 
11314 C  CG2 . VAL D  340 ? 4.1988 2.8701 2.4238 0.5455  -0.1169 -0.3092 338  VAL D CG2 
11315 N  N   . TYR D  341 ? 4.2008 3.0851 2.6429 0.5442  -0.1108 -0.2628 339  TYR D N   
11316 C  CA  . TYR D  341 ? 4.3599 3.2678 2.8127 0.5259  -0.1105 -0.2430 339  TYR D CA  
11317 C  C   . TYR D  341 ? 4.6112 3.4916 3.0218 0.5395  -0.0773 -0.2616 339  TYR D C   
11318 O  O   . TYR D  341 ? 4.6085 3.4795 3.0138 0.5737  -0.0529 -0.2887 339  TYR D O   
11319 C  CB  . TYR D  341 ? 4.2326 3.2134 2.7923 0.5363  -0.1137 -0.2269 339  TYR D CB  
11320 C  CG  . TYR D  341 ? 4.1926 3.2089 2.8169 0.5707  -0.0840 -0.2505 339  TYR D CG  
11321 C  CD1 . TYR D  341 ? 4.1266 3.1637 2.7921 0.5974  -0.0816 -0.2696 339  TYR D CD1 
11322 C  CD2 . TYR D  341 ? 4.1802 3.2144 2.8208 0.5730  -0.0575 -0.2543 339  TYR D CD2 
11323 C  CE1 . TYR D  341 ? 4.0249 3.1103 2.7493 0.6258  -0.0553 -0.2916 339  TYR D CE1 
11324 C  CE2 . TYR D  341 ? 4.0792 3.1594 2.7765 0.5968  -0.0294 -0.2785 339  TYR D CE2 
11325 C  CZ  . TYR D  341 ? 4.0180 3.1291 2.7588 0.6233  -0.0291 -0.2969 339  TYR D CZ  
11326 O  OH  . TYR D  341 ? 4.0123 3.1842 2.8094 0.6441  -0.0019 -0.3213 339  TYR D OH  
11327 N  N   . TYR D  342 ? 4.7220 3.5954 3.1023 0.5148  -0.0761 -0.2459 340  TYR D N   
11328 C  CA  . TYR D  342 ? 4.6615 3.5117 2.9988 0.5210  -0.0453 -0.2617 340  TYR D CA  
11329 C  C   . TYR D  342 ? 4.5377 3.4411 2.9431 0.5260  -0.0285 -0.2562 340  TYR D C   
11330 O  O   . TYR D  342 ? 4.4349 3.3711 2.8929 0.5152  -0.0435 -0.2309 340  TYR D O   
11331 C  CB  . TYR D  342 ? 4.6331 3.4242 2.8677 0.4839  -0.0515 -0.2515 340  TYR D CB  
11332 C  CG  . TYR D  342 ? 4.5742 3.2869 2.7085 0.4779  -0.0487 -0.2692 340  TYR D CG  
11333 C  CD1 . TYR D  342 ? 4.4550 3.1183 2.5302 0.5037  -0.0147 -0.2975 340  TYR D CD1 
11334 C  CD2 . TYR D  342 ? 4.5860 3.2715 2.6766 0.4450  -0.0769 -0.2580 340  TYR D CD2 
11335 C  CE1 . TYR D  342 ? 4.4655 3.0386 2.4348 0.5007  -0.0066 -0.3130 340  TYR D CE1 
11336 C  CE2 . TYR D  342 ? 4.5281 3.1262 2.5119 0.4329  -0.0693 -0.2758 340  TYR D CE2 
11337 C  CZ  . TYR D  342 ? 4.4981 3.0320 2.4181 0.4625  -0.0328 -0.3026 340  TYR D CZ  
11338 O  OH  . TYR D  342 ? 4.5833 3.0126 2.3838 0.4533  -0.0199 -0.3198 340  TYR D OH  
11339 N  N   . VAL D  343 ? 4.5580 3.4678 2.9560 0.5426  0.0056  -0.2808 341  VAL D N   
11340 C  CA  . VAL D  343 ? 4.5220 3.4708 2.9615 0.5368  0.0281  -0.2803 341  VAL D CA  
11341 C  C   . VAL D  343 ? 4.5934 3.5138 2.9637 0.5283  0.0536  -0.2937 341  VAL D C   
11342 O  O   . VAL D  343 ? 4.5973 3.4746 2.8981 0.5370  0.0589  -0.3085 341  VAL D O   
11343 C  CB  . VAL D  343 ? 4.3935 3.4118 2.9194 0.5628  0.0490  -0.3027 341  VAL D CB  
11344 C  CG1 . VAL D  343 ? 4.4272 3.4769 2.9787 0.5467  0.0781  -0.3066 341  VAL D CG1 
11345 C  CG2 . VAL D  343 ? 4.2457 3.2900 2.8401 0.5685  0.0255  -0.2889 341  VAL D CG2 
11346 N  N   . ARG D  345 ? 4.4268 3.2873 2.6431 0.5616  0.1147  -0.3528 343  ARG D N   
11347 C  CA  . ARG D  345 ? 4.4716 3.2687 2.5978 0.5822  0.1269  -0.3702 343  ARG D CA  
11348 C  C   . ARG D  345 ? 4.3863 3.1888 2.5285 0.6303  0.1280  -0.3860 343  ARG D C   
11349 O  O   . ARG D  345 ? 4.3959 3.1333 2.4580 0.6555  0.1399  -0.3994 343  ARG D O   
11350 C  CB  . ARG D  345 ? 4.6140 3.4225 2.7038 0.5935  0.1653  -0.3935 343  ARG D CB  
11351 C  CG  . ARG D  345 ? 4.6095 3.5255 2.7844 0.6171  0.1922  -0.4148 343  ARG D CG  
11352 C  CD  . ARG D  345 ? 4.7537 3.6874 2.8886 0.6197  0.2292  -0.4366 343  ARG D CD  
11353 N  NE  . ARG D  345 ? 4.7162 3.7369 2.9185 0.5983  0.2477  -0.4443 343  ARG D NE  
11354 C  CZ  . ARG D  345 ? 4.5982 3.7228 2.8571 0.6251  0.2759  -0.4729 343  ARG D CZ  
11355 N  NH1 . ARG D  345 ? 4.5227 3.6828 2.7830 0.6838  0.2876  -0.4937 343  ARG D NH1 
11356 N  NH2 . ARG D  345 ? 4.5777 3.7715 2.8859 0.5925  0.2943  -0.4805 343  ARG D NH2 
11357 N  N   . LYS D  346 ? 4.2916 3.1653 2.5311 0.6433  0.1176  -0.3839 344  LYS D N   
11358 C  CA  . LYS D  346 ? 4.4780 3.3692 2.7425 0.6901  0.1182  -0.3977 344  LYS D CA  
11359 C  C   . LYS D  346 ? 4.5245 3.3881 2.8077 0.6721  0.0814  -0.3768 344  LYS D C   
11360 O  O   . LYS D  346 ? 4.3693 3.2862 2.7343 0.6523  0.0639  -0.3617 344  LYS D O   
11361 C  CB  . LYS D  346 ? 4.3382 3.3459 2.6997 0.7200  0.1381  -0.4165 344  LYS D CB  
11362 C  CG  . LYS D  346 ? 4.2564 3.3171 2.6129 0.7285  0.1746  -0.4379 344  LYS D CG  
11363 C  CD  . LYS D  346 ? 4.0332 3.2233 2.4846 0.7508  0.1941  -0.4590 344  LYS D CD  
11364 C  CE  . LYS D  346 ? 3.9654 3.2222 2.4174 0.7452  0.2299  -0.4803 344  LYS D CE  
11365 N  NZ  . LYS D  346 ? 3.9797 3.2151 2.3546 0.7884  0.2542  -0.4979 344  LYS D NZ  
11366 N  N   . PRO D  347 ? 4.7317 3.5107 2.9369 0.6761  0.0711  -0.3758 345  PRO D N   
11367 C  CA  . PRO D  347 ? 4.6533 3.4174 2.8787 0.6582  0.0377  -0.3594 345  PRO D CA  
11368 C  C   . PRO D  347 ? 4.5035 3.3247 2.8041 0.7016  0.0392  -0.3708 345  PRO D C   
11369 O  O   . PRO D  347 ? 4.6876 3.5004 2.9619 0.7516  0.0618  -0.3912 345  PRO D O   
11370 C  CB  . PRO D  347 ? 4.6354 3.2828 2.7344 0.6434  0.0346  -0.3606 345  PRO D CB  
11371 C  CG  . PRO D  347 ? 4.6637 3.2669 2.6893 0.6843  0.0732  -0.3843 345  PRO D CG  
11372 C  CD  . PRO D  347 ? 4.6926 3.3765 2.7764 0.6906  0.0918  -0.3895 345  PRO D CD  
11373 N  N   . LYS D  348 ? 3.9141 2.7946 2.3056 0.6853  0.0162  -0.3565 346  LYS D N   
11374 C  CA  . LYS D  348 ? 3.7697 2.7165 2.2434 0.7193  0.0167  -0.3664 346  LYS D CA  
11375 C  C   . LYS D  348 ? 3.7643 2.6836 2.2440 0.7045  -0.0143 -0.3529 346  LYS D C   
11376 O  O   . LYS D  348 ? 3.8053 2.7269 2.3055 0.6633  -0.0403 -0.3304 346  LYS D O   
11377 C  CB  . LYS D  348 ? 3.7131 2.7601 2.2928 0.7131  0.0241  -0.3664 346  LYS D CB  
11378 C  CG  . LYS D  348 ? 3.7229 2.8116 2.3014 0.7254  0.0580  -0.3845 346  LYS D CG  
11379 C  CD  . LYS D  348 ? 3.6799 2.8647 2.3553 0.7146  0.0704  -0.3897 346  LYS D CD  
11380 C  CE  . LYS D  348 ? 3.7364 2.9706 2.4064 0.7206  0.1060  -0.4111 346  LYS D CE  
11381 N  NZ  . LYS D  348 ? 3.7369 2.9985 2.3795 0.7746  0.1269  -0.4366 346  LYS D NZ  
11382 N  N   . VAL D  349 ? 3.8718 2.7687 2.3312 0.7404  -0.0105 -0.3661 347  VAL D N   
11383 C  CA  . VAL D  349 ? 3.9494 2.8221 2.4127 0.7287  -0.0362 -0.3577 347  VAL D CA  
11384 C  C   . VAL D  349 ? 3.7981 2.7666 2.3768 0.7512  -0.0394 -0.3617 347  VAL D C   
11385 O  O   . VAL D  349 ? 3.6629 2.6706 2.2635 0.7989  -0.0191 -0.3801 347  VAL D O   
11386 C  CB  . VAL D  349 ? 4.0741 2.8439 2.4265 0.7506  -0.0274 -0.3691 347  VAL D CB  
11387 C  CG1 . VAL D  349 ? 4.1114 2.8527 2.4605 0.7288  -0.0534 -0.3613 347  VAL D CG1 
11388 C  CG2 . VAL D  349 ? 4.1477 2.8188 2.3783 0.7267  -0.0172 -0.3690 347  VAL D CG2 
11389 N  N   . GLU D  350 ? 3.8051 2.8156 2.4555 0.7183  -0.0636 -0.3444 348  GLU D N   
11390 C  CA  . GLU D  350 ? 3.7231 2.8190 2.4812 0.7309  -0.0660 -0.3473 348  GLU D CA  
11391 C  C   . GLU D  350 ? 3.6866 2.7722 2.4640 0.7125  -0.0954 -0.3350 348  GLU D C   
11392 O  O   . GLU D  350 ? 3.8311 2.8613 2.5524 0.6799  -0.1164 -0.3206 348  GLU D O   
11393 C  CB  . GLU D  350 ? 3.7049 2.8674 2.5393 0.7115  -0.0592 -0.3393 348  GLU D CB  
11394 C  CG  . GLU D  350 ? 3.8214 3.0018 2.6394 0.7210  -0.0290 -0.3525 348  GLU D CG  
11395 C  CD  . GLU D  350 ? 3.8938 3.1382 2.7856 0.7020  -0.0156 -0.3497 348  GLU D CD  
11396 O  OE1 . GLU D  350 ? 4.0578 3.3290 2.9442 0.7046  0.0115  -0.3634 348  GLU D OE1 
11397 O  OE2 . GLU D  350 ? 3.7938 3.0581 2.7434 0.6838  -0.0295 -0.3346 348  GLU D OE2 
11398 N  N   . GLN D  351 ? 3.3840 2.5306 2.2409 0.7304  -0.0962 -0.3421 349  GLN D N   
11399 C  CA  . GLN D  351 ? 3.3040 2.4503 2.1872 0.7162  -0.1216 -0.3335 349  GLN D CA  
11400 C  C   . GLN D  351 ? 3.2125 2.4427 2.2085 0.7092  -0.1245 -0.3277 349  GLN D C   
11401 O  O   . GLN D  351 ? 3.1185 2.4099 2.1728 0.7315  -0.1041 -0.3434 349  GLN D O   
11402 C  CB  . GLN D  351 ? 3.2613 2.3772 2.1083 0.7486  -0.1182 -0.3497 349  GLN D CB  
11403 C  CG  . GLN D  351 ? 3.2627 2.3689 2.1234 0.7297  -0.1434 -0.3428 349  GLN D CG  
11404 C  CD  . GLN D  351 ? 3.3534 2.4213 2.1709 0.7639  -0.1371 -0.3580 349  GLN D CD  
11405 O  OE1 . GLN D  351 ? 3.4715 2.5449 2.2725 0.8112  -0.1137 -0.3729 349  GLN D OE1 
11406 N  NE2 . GLN D  351 ? 3.3396 2.3712 2.1347 0.7417  -0.1571 -0.3536 349  GLN D NE2 
11407 N  N   . LEU D  352 ? 3.3171 2.5524 2.3392 0.6780  -0.1479 -0.3058 350  LEU D N   
11408 C  CA  . LEU D  352 ? 3.2935 2.5927 2.4117 0.6723  -0.1487 -0.2975 350  LEU D CA  
11409 C  C   . LEU D  352 ? 3.2488 2.5751 2.4132 0.6807  -0.1592 -0.3057 350  LEU D C   
11410 O  O   . LEU D  352 ? 3.1900 2.4798 2.3107 0.6762  -0.1773 -0.3062 350  LEU D O   
11411 C  CB  . LEU D  352 ? 3.3112 2.6087 2.4350 0.6441  -0.1675 -0.2671 350  LEU D CB  
11412 C  CG  . LEU D  352 ? 3.4881 2.7613 2.5691 0.6331  -0.1592 -0.2541 350  LEU D CG  
11413 C  CD1 . LEU D  352 ? 3.6383 2.9198 2.7254 0.6123  -0.1805 -0.2203 350  LEU D CD1 
11414 C  CD2 . LEU D  352 ? 3.4797 2.7786 2.5970 0.6454  -0.1256 -0.2667 350  LEU D CD2 
11415 N  N   . SER D  353 ? 3.3653 2.7526 2.6133 0.6885  -0.1455 -0.3131 351  SER D N   
11416 C  CA  . SER D  353 ? 3.3148 2.7365 2.6146 0.6961  -0.1521 -0.3225 351  SER D CA  
11417 C  C   . SER D  353 ? 3.2934 2.7338 2.6448 0.6748  -0.1694 -0.3020 351  SER D C   
11418 O  O   . SER D  353 ? 3.2974 2.7539 2.6840 0.6660  -0.1599 -0.2883 351  SER D O   
11419 C  CB  . SER D  353 ? 3.2796 2.7647 2.6372 0.7148  -0.1249 -0.3459 351  SER D CB  
11420 O  OG  . SER D  353 ? 3.2117 2.7269 2.6141 0.7000  -0.1044 -0.3427 351  SER D OG  
11421 N  N   . ASN D  354 ? 3.3709 2.8060 2.7206 0.6684  -0.1925 -0.2995 352  ASN D N   
11422 C  CA  . ASN D  354 ? 3.4444 2.9086 2.8455 0.6527  -0.2096 -0.2820 352  ASN D CA  
11423 C  C   . ASN D  354 ? 3.4758 2.9318 2.8577 0.6359  -0.2230 -0.2525 352  ASN D C   
11424 O  O   . ASN D  354 ? 3.5607 3.0310 2.9752 0.6398  -0.2084 -0.2394 352  ASN D O   
11425 C  CB  . ASN D  354 ? 3.4249 2.9405 2.9139 0.6608  -0.1895 -0.2893 352  ASN D CB  
11426 C  CG  . ASN D  354 ? 3.3816 2.9233 2.8966 0.6751  -0.1804 -0.3166 352  ASN D CG  
11427 O  OD1 . ASN D  354 ? 3.3539 2.9080 2.8898 0.6722  -0.1952 -0.3197 352  ASN D OD1 
11428 N  ND2 . ASN D  354 ? 3.3697 2.9274 2.8830 0.6908  -0.1558 -0.3364 352  ASN D ND2 
11429 N  N   . MET D  355 ? 3.4055 2.8387 2.7290 0.6158  -0.2491 -0.2417 353  MET D N   
11430 C  CA  . MET D  355 ? 3.4080 2.8489 2.7100 0.5990  -0.2654 -0.2126 353  MET D CA  
11431 C  C   . MET D  355 ? 3.3810 2.8511 2.6772 0.5747  -0.2968 -0.1999 353  MET D C   
11432 O  O   . MET D  355 ? 3.3513 2.8721 2.6852 0.5734  -0.3091 -0.1743 353  MET D O   
11433 C  CB  . MET D  355 ? 3.5504 2.9402 2.7672 0.5897  -0.2628 -0.2121 353  MET D CB  
11434 C  CG  . MET D  355 ? 3.5593 2.9315 2.7800 0.6100  -0.2321 -0.2212 353  MET D CG  
11435 S  SD  . MET D  355 ? 3.5799 2.9867 2.8668 0.6207  -0.2160 -0.1980 353  MET D SD  
11436 C  CE  . MET D  355 ? 3.4624 2.8740 2.7046 0.6029  -0.2437 -0.1597 353  MET D CE  
11437 N  N   . ILE D  356 ? 3.3947 2.8334 2.6383 0.5561  -0.3081 -0.2173 354  ILE D N   
11438 C  CA  . ILE D  356 ? 3.4430 2.9066 2.6660 0.5225  -0.3362 -0.2106 354  ILE D CA  
11439 C  C   . ILE D  356 ? 3.4868 2.9964 2.7862 0.5305  -0.3396 -0.2165 354  ILE D C   
11440 O  O   . ILE D  356 ? 3.5457 3.0288 2.8549 0.5441  -0.3272 -0.2395 354  ILE D O   
11441 C  CB  . ILE D  356 ? 3.5672 2.9586 2.6815 0.4921  -0.3418 -0.2283 354  ILE D CB  
11442 C  CG1 . ILE D  356 ? 3.7961 3.1460 2.8292 0.4763  -0.3405 -0.2207 354  ILE D CG1 
11443 C  CG2 . ILE D  356 ? 3.5704 2.9879 2.6641 0.4508  -0.3667 -0.2282 354  ILE D CG2 
11444 C  CD1 . ILE D  356 ? 3.9028 3.1867 2.9040 0.5065  -0.3124 -0.2360 354  ILE D CD1 
11445 N  N   . VAL D  357 ? 3.4802 3.0628 2.8311 0.5241  -0.3563 -0.1952 355  VAL D N   
11446 C  CA  . VAL D  357 ? 3.3241 2.9562 2.7487 0.5303  -0.3597 -0.1988 355  VAL D CA  
11447 C  C   . VAL D  357 ? 3.3296 2.9689 2.7113 0.4901  -0.3830 -0.2086 355  VAL D C   
11448 O  O   . VAL D  357 ? 3.4478 3.1204 2.7897 0.4574  -0.4050 -0.1950 355  VAL D O   
11449 C  CB  . VAL D  357 ? 3.3676 3.0729 2.8670 0.5506  -0.3614 -0.1700 355  VAL D CB  
11450 C  CG1 . VAL D  357 ? 3.3515 3.1104 2.9195 0.5532  -0.3664 -0.1735 355  VAL D CG1 
11451 C  CG2 . VAL D  357 ? 3.4026 3.0836 2.9348 0.5859  -0.3320 -0.1640 355  VAL D CG2 
11452 N  N   . ARG D  358 ? 3.3210 2.9324 2.7067 0.4896  -0.3774 -0.2328 356  ARG D N   
11453 C  CA  . ARG D  358 ? 3.3704 2.9728 2.7051 0.4485  -0.3949 -0.2456 356  ARG D CA  
11454 C  C   . ARG D  358 ? 3.2585 2.9471 2.6718 0.4426  -0.4077 -0.2396 356  ARG D C   
11455 O  O   . ARG D  358 ? 3.2469 3.0014 2.6573 0.4123  -0.4295 -0.2259 356  ARG D O   
11456 C  CB  . ARG D  358 ? 3.4726 2.9848 2.7507 0.4537  -0.3803 -0.2735 356  ARG D CB  
11457 C  CG  . ARG D  358 ? 3.5420 3.0189 2.7465 0.4094  -0.3928 -0.2883 356  ARG D CG  
11458 C  CD  . ARG D  358 ? 3.6399 3.0837 2.7390 0.3605  -0.4046 -0.2847 356  ARG D CD  
11459 N  NE  . ARG D  358 ? 3.5973 2.9419 2.6091 0.3729  -0.3869 -0.2919 356  ARG D NE  
11460 C  CZ  . ARG D  358 ? 3.6495 2.9373 2.5505 0.3321  -0.3897 -0.2936 356  ARG D CZ  
11461 N  NH1 . ARG D  358 ? 3.6410 2.9698 2.5056 0.2718  -0.4106 -0.2893 356  ARG D NH1 
11462 N  NH2 . ARG D  358 ? 3.7317 2.9264 2.5559 0.3495  -0.3702 -0.3006 356  ARG D NH2 
11463 N  N   . SER D  359 ? 3.1609 2.8570 2.6442 0.4705  -0.3937 -0.2504 357  SER D N   
11464 C  CA  . SER D  359 ? 3.0927 2.8621 2.6512 0.4682  -0.4014 -0.2480 357  SER D CA  
11465 C  C   . SER D  359 ? 3.0469 2.8659 2.7015 0.5095  -0.3859 -0.2316 357  SER D C   
11466 O  O   . SER D  359 ? 3.1008 2.8908 2.7632 0.5373  -0.3670 -0.2261 357  SER D O   
11467 C  CB  . SER D  359 ? 3.1810 2.9159 2.7365 0.4622  -0.3961 -0.2748 357  SER D CB  
11468 O  OG  . SER D  359 ? 3.1899 2.9955 2.8156 0.4565  -0.4034 -0.2739 357  SER D OG  
11469 N  N   . CYS D  360 ? 3.0121 2.9019 2.7342 0.5119  -0.3914 -0.2245 358  CYS D N   
11470 C  CA  . CYS D  360 ? 2.9632 2.8894 2.7689 0.5505  -0.3723 -0.2099 358  CYS D CA  
11471 C  C   . CYS D  360 ? 2.9985 2.9527 2.8668 0.5519  -0.3657 -0.2252 358  CYS D C   
11472 O  O   . CYS D  360 ? 3.0494 3.0400 2.9133 0.5239  -0.3852 -0.2323 358  CYS D O   
11473 C  CB  . CYS D  360 ? 3.0292 3.0248 2.8529 0.5632  -0.3837 -0.1749 358  CYS D CB  
11474 S  SG  . CYS D  360 ? 3.0500 3.0261 2.7984 0.5574  -0.3949 -0.1538 358  CYS D SG  
11475 N  N   . LYS D  361 ? 3.0759 3.0131 2.9980 0.5799  -0.3365 -0.2317 359  LYS D N   
11476 C  CA  . LYS D  361 ? 3.0215 2.9807 3.0037 0.5815  -0.3253 -0.2477 359  LYS D CA  
11477 C  C   . LYS D  361 ? 2.8697 2.8517 2.9167 0.6137  -0.2999 -0.2316 359  LYS D C   
11478 O  O   . LYS D  361 ? 2.8749 2.8447 2.9157 0.6372  -0.2882 -0.2091 359  LYS D O   
11479 C  CB  . LYS D  361 ? 3.0821 2.9929 3.0577 0.5782  -0.3096 -0.2785 359  LYS D CB  
11480 C  CG  . LYS D  361 ? 3.1339 3.0055 3.1116 0.6000  -0.2803 -0.2817 359  LYS D CG  
11481 C  CD  . LYS D  361 ? 3.0611 2.9106 3.0392 0.5988  -0.2653 -0.3120 359  LYS D CD  
11482 C  CE  . LYS D  361 ? 2.9064 2.7318 2.8850 0.6144  -0.2357 -0.3175 359  LYS D CE  
11483 N  NZ  . LYS D  361 ? 2.8724 2.6980 2.8535 0.6153  -0.2217 -0.3465 359  LYS D NZ  
11484 N  N   . CYS D  362 ? 2.6614 2.6688 2.7640 0.6146  -0.2887 -0.2433 360  CYS D N   
11485 C  CA  . CYS D  362 ? 2.6924 2.7022 2.8494 0.6433  -0.2560 -0.2344 360  CYS D CA  
11486 C  C   . CYS D  362 ? 2.7035 2.6785 2.8856 0.6358  -0.2268 -0.2652 360  CYS D C   
11487 O  O   . CYS D  362 ? 2.6986 2.6936 2.9018 0.6166  -0.2332 -0.2872 360  CYS D O   
11488 C  CB  . CYS D  362 ? 2.7917 2.8695 2.9932 0.6527  -0.2641 -0.2199 360  CYS D CB  
11489 S  SG  . CYS D  362 ? 3.1309 3.2878 3.3109 0.6576  -0.3018 -0.1847 360  CYS D SG  
11490 N  N   . SER D  363 ? 2.8017 2.7297 2.9791 0.6477  -0.1940 -0.2675 361  SER D N   
11491 C  CA  . SER D  363 ? 2.8116 2.7195 3.0108 0.6357  -0.1639 -0.2979 361  SER D CA  
11492 C  C   . SER D  363 ? 2.7055 2.5708 2.9126 0.6485  -0.1178 -0.2941 361  SER D C   
11493 O  O   . SER D  363 ? 2.5822 2.4233 2.7733 0.6724  -0.1085 -0.2656 361  SER D O   
11494 C  CB  . SER D  363 ? 2.8623 2.7574 3.0252 0.6203  -0.1741 -0.3198 361  SER D CB  
11495 O  OG  . SER D  363 ? 2.8686 2.7310 2.9857 0.6294  -0.1740 -0.3071 361  SER D OG  
11496 O  OXT . SER D  363 ? 2.6772 2.5299 2.9011 0.6332  -0.0868 -0.3198 361  SER D OXT 
11497 N  N   . PHE E  1   ? 2.1471 3.1484 1.9995 0.8579  -0.5306 -0.0033 1    PHE E N   
11498 C  CA  . PHE E  1   ? 2.2761 3.3233 2.1040 0.8915  -0.5649 0.0470  1    PHE E CA  
11499 C  C   . PHE E  1   ? 2.3146 3.4593 2.1745 0.9578  -0.5878 0.0643  1    PHE E C   
11500 O  O   . PHE E  1   ? 2.3976 3.5483 2.2369 1.0084  -0.6177 0.1164  1    PHE E O   
11501 C  CB  . PHE E  1   ? 2.4251 3.5761 2.2401 0.8391  -0.5696 0.0343  1    PHE E CB  
11502 C  CG  . PHE E  1   ? 2.4370 3.7497 2.2943 0.8077  -0.5615 -0.0168 1    PHE E CG  
11503 C  CD1 . PHE E  1   ? 2.4177 3.7237 2.2911 0.7490  -0.5279 -0.0756 1    PHE E CD1 
11504 C  CD2 . PHE E  1   ? 2.3995 3.8719 2.2766 0.8343  -0.5874 -0.0053 1    PHE E CD2 
11505 C  CE1 . PHE E  1   ? 2.3208 3.7697 2.2271 0.7126  -0.5188 -0.1240 1    PHE E CE1 
11506 C  CE2 . PHE E  1   ? 2.2366 3.8656 2.1503 0.7988  -0.5790 -0.0546 1    PHE E CE2 
11507 C  CZ  . PHE E  1   ? 2.1353 3.7492 2.0622 0.7352  -0.5440 -0.1150 1    PHE E CZ  
11508 N  N   . ASN E  2   ? 2.1998 3.4212 2.1090 0.9581  -0.5733 0.0206  2    ASN E N   
11509 C  CA  . ASN E  2   ? 2.3335 3.6831 2.2819 1.0153  -0.5921 0.0254  2    ASN E CA  
11510 C  C   . ASN E  2   ? 2.3300 3.5970 2.2925 1.0840  -0.5923 0.0403  2    ASN E C   
11511 O  O   . ASN E  2   ? 2.3946 3.7678 2.3969 1.1327  -0.6022 0.0343  2    ASN E O   
11512 C  CB  . ASN E  2   ? 2.4400 3.9481 2.4341 0.9700  -0.5766 -0.0344 2    ASN E CB  
11513 C  CG  . ASN E  2   ? 2.3912 3.8280 2.3990 0.9183  -0.5384 -0.0858 2    ASN E CG  
11514 O  OD1 . ASN E  2   ? 2.1031 3.3966 2.0795 0.8866  -0.5209 -0.0854 2    ASN E OD1 
11515 N  ND2 . ASN E  2   ? 2.6066 4.1482 2.6599 0.9090  -0.5253 -0.1293 2    ASN E ND2 
11516 N  N   . LEU E  3   ? 2.3275 3.4145 2.2582 1.0895  -0.5814 0.0580  3    LEU E N   
11517 C  CA  . LEU E  3   ? 2.4042 3.4031 2.3423 1.1548  -0.5814 0.0724  3    LEU E CA  
11518 C  C   . LEU E  3   ? 2.4711 3.4592 2.3869 1.2332  -0.6159 0.1327  3    LEU E C   
11519 O  O   . LEU E  3   ? 2.5734 3.5048 2.4405 1.2295  -0.6330 0.1772  3    LEU E O   
11520 C  CB  . LEU E  3   ? 2.3076 3.1209 2.2153 1.1309  -0.5582 0.0712  3    LEU E CB  
11521 C  CG  . LEU E  3   ? 2.2363 3.0441 2.1718 1.0755  -0.5228 0.0140  3    LEU E CG  
11522 C  CD1 . LEU E  3   ? 2.2824 2.9143 2.1831 1.0518  -0.5025 0.0185  3    LEU E CD1 
11523 C  CD2 . LEU E  3   ? 2.2147 3.1044 2.2038 1.1106  -0.5158 -0.0175 3    LEU E CD2 
11524 N  N   . ASP E  4   ? 2.5241 3.5653 2.4735 1.3052  -0.6257 0.1347  4    ASP E N   
11525 C  CA  . ASP E  4   ? 2.6463 3.6826 2.5772 1.3889  -0.6582 0.1914  4    ASP E CA  
11526 C  C   . ASP E  4   ? 2.5690 3.3834 2.4510 1.4080  -0.6501 0.2265  4    ASP E C   
11527 O  O   . ASP E  4   ? 2.5751 3.3068 2.4711 1.4303  -0.6311 0.2068  4    ASP E O   
11528 C  CB  . ASP E  4   ? 2.8671 4.0248 2.8521 1.4350  -0.6567 0.1735  4    ASP E CB  
11529 C  CG  . ASP E  4   ? 3.0892 4.2096 3.0549 1.4885  -0.6711 0.2259  4    ASP E CG  
11530 O  OD1 . ASP E  4   ? 3.1025 4.2896 3.0504 1.4836  -0.6919 0.2601  4    ASP E OD1 
11531 O  OD2 . ASP E  4   ? 3.2175 4.2423 3.1855 1.5349  -0.6614 0.2318  4    ASP E OD2 
11532 N  N   . VAL E  5   ? 2.5852 3.3088 2.4091 1.3948  -0.6638 0.2771  5    VAL E N   
11533 C  CA  . VAL E  5   ? 2.7113 3.2309 2.4830 1.4059  -0.6580 0.3146  5    VAL E CA  
11534 C  C   . VAL E  5   ? 2.7697 3.2577 2.5273 1.4551  -0.6722 0.3630  5    VAL E C   
11535 O  O   . VAL E  5   ? 2.8586 3.1804 2.5740 1.4685  -0.6684 0.3957  5    VAL E O   
11536 C  CB  . VAL E  5   ? 2.8017 3.2251 2.5122 1.3540  -0.6616 0.3383  5    VAL E CB  
11537 C  CG1 . VAL E  5   ? 2.8618 3.0807 2.5304 1.3476  -0.6436 0.3478  5    VAL E CG1 
11538 C  CG2 . VAL E  5   ? 2.6248 3.1422 2.3559 1.2887  -0.6505 0.2931  5    VAL E CG2 
11539 N  N   . ASP E  6   ? 2.8588 3.5043 2.6496 1.4811  -0.6886 0.3681  6    ASP E N   
11540 C  CA  . ASP E  6   ? 3.0447 3.6691 2.8242 1.5332  -0.7039 0.4148  6    ASP E CA  
11541 C  C   . ASP E  6   ? 3.0355 3.6065 2.8425 1.5897  -0.6893 0.3992  6    ASP E C   
11542 O  O   . ASP E  6   ? 3.1652 3.5982 2.9399 1.6232  -0.6907 0.4357  6    ASP E O   
11543 C  CB  . ASP E  6   ? 3.2482 4.0671 3.0545 1.5421  -0.7255 0.4238  6    ASP E CB  
11544 C  CG  . ASP E  6   ? 3.2913 4.1625 3.0657 1.4866  -0.7410 0.4429  6    ASP E CG  
11545 O  OD1 . ASP E  6   ? 3.4702 4.2095 3.1928 1.4505  -0.7392 0.4634  6    ASP E OD1 
11546 O  OD2 . ASP E  6   ? 3.0833 4.1320 2.8834 1.4769  -0.7540 0.4360  6    ASP E OD2 
11547 N  N   . SER E  7   ? 3.0584 3.7352 2.9231 1.5986  -0.6744 0.3437  7    SER E N   
11548 C  CA  . SER E  7   ? 3.0886 3.7405 2.9843 1.6518  -0.6600 0.3228  7    SER E CA  
11549 C  C   . SER E  7   ? 2.9684 3.6206 2.8968 1.6292  -0.6336 0.2624  7    SER E C   
11550 O  O   . SER E  7   ? 3.0022 3.8036 2.9865 1.6372  -0.6271 0.2179  7    SER E O   
11551 C  CB  . SER E  7   ? 3.1091 3.9310 3.0490 1.7018  -0.6729 0.3214  7    SER E CB  
11552 O  OG  . SER E  7   ? 2.9831 4.0063 2.9650 1.6712  -0.6767 0.2864  7    SER E OG  
11553 N  N   . PRO E  8   ? 2.8669 3.3570 2.7607 1.5981  -0.6177 0.2594  8    PRO E N   
11554 C  CA  . PRO E  8   ? 2.7891 3.2653 2.7111 1.5790  -0.5918 0.2049  8    PRO E CA  
11555 C  C   . PRO E  8   ? 2.8952 3.2980 2.8316 1.6239  -0.5742 0.1895  8    PRO E C   
11556 O  O   . PRO E  8   ? 3.1747 3.4688 3.0817 1.6606  -0.5779 0.2246  8    PRO E O   
11557 C  CB  . PRO E  8   ? 2.7602 3.0928 2.6317 1.5250  -0.5840 0.2143  8    PRO E CB  
11558 C  CG  . PRO E  8   ? 2.8700 3.0744 2.6822 1.5348  -0.5975 0.2743  8    PRO E CG  
11559 C  CD  . PRO E  8   ? 2.9199 3.2436 2.7453 1.5715  -0.6228 0.3049  8    PRO E CD  
11560 N  N   . ALA E  9   ? 2.8296 3.2948 2.8117 1.6191  -0.5544 0.1348  9    ALA E N   
11561 C  CA  . ALA E  9   ? 3.0331 3.4457 3.0334 1.6568  -0.5353 0.1114  9    ALA E CA  
11562 C  C   . ALA E  9   ? 3.0797 3.2932 3.0374 1.6311  -0.5151 0.1121  9    ALA E C   
11563 O  O   . ALA E  9   ? 2.7834 2.9627 2.7325 1.5793  -0.5034 0.0924  9    ALA E O   
11564 C  CB  . ALA E  9   ? 2.9963 3.5664 3.0619 1.6578  -0.5222 0.0522  9    ALA E CB  
11565 N  N   . GLU E  10  ? 3.3533 3.4370 3.2835 1.6666  -0.5107 0.1342  10   GLU E N   
11566 C  CA  . GLU E  10  ? 3.3603 3.2540 3.2463 1.6424  -0.4914 0.1366  10   GLU E CA  
11567 C  C   . GLU E  10  ? 3.3994 3.2757 3.3156 1.6658  -0.4667 0.0928  10   GLU E C   
11568 O  O   . GLU E  10  ? 3.3817 3.2595 3.3108 1.7224  -0.4677 0.0958  10   GLU E O   
11569 C  CB  . GLU E  10  ? 3.4477 3.1968 3.2744 1.6574  -0.5032 0.1930  10   GLU E CB  
11570 C  CG  . GLU E  10  ? 3.4049 2.9598 3.1831 1.6319  -0.4828 0.1950  10   GLU E CG  
11571 C  CD  . GLU E  10  ? 3.3718 2.7858 3.0863 1.6369  -0.4953 0.2520  10   GLU E CD  
11572 O  OE1 . GLU E  10  ? 3.3675 2.8311 3.0710 1.6496  -0.5208 0.2931  10   GLU E OE1 
11573 O  OE2 . GLU E  10  ? 3.4239 2.6798 3.0980 1.6257  -0.4794 0.2553  10   GLU E OE2 
11574 N  N   . TYR E  11  ? 3.3808 3.2435 3.3079 1.6232  -0.4448 0.0523  11   TYR E N   
11575 C  CA  . TYR E  11  ? 3.3718 3.2103 3.3228 1.6345  -0.4191 0.0092  11   TYR E CA  
11576 C  C   . TYR E  11  ? 3.4634 3.1113 3.3630 1.6035  -0.4004 0.0147  11   TYR E C   
11577 O  O   . TYR E  11  ? 3.5873 3.1581 3.4469 1.5523  -0.4003 0.0314  11   TYR E O   
11578 C  CB  . TYR E  11  ? 3.0991 3.0700 3.1023 1.6086  -0.4062 -0.0435 11   TYR E CB  
11579 C  CG  . TYR E  11  ? 3.1352 3.3075 3.1928 1.6363  -0.4214 -0.0573 11   TYR E CG  
11580 C  CD1 . TYR E  11  ? 2.9641 3.2315 3.0253 1.6156  -0.4417 -0.0410 11   TYR E CD1 
11581 C  CD2 . TYR E  11  ? 3.3921 3.6659 3.4966 1.6819  -0.4155 -0.0876 11   TYR E CD2 
11582 C  CE1 . TYR E  11  ? 3.0617 3.5219 3.1719 1.6361  -0.4548 -0.0556 11   TYR E CE1 
11583 C  CE2 . TYR E  11  ? 3.4354 3.9032 3.5884 1.7037  -0.4288 -0.1013 11   TYR E CE2 
11584 C  CZ  . TYR E  11  ? 3.3100 3.8711 3.4656 1.6790  -0.4481 -0.0855 11   TYR E CZ  
11585 O  OH  . TYR E  11  ? 3.3121 4.0741 3.5153 1.6953  -0.4603 -0.1014 11   TYR E OH  
11586 N  N   . SER E  12  ? 3.3704 2.9482 3.2711 1.6337  -0.3840 -0.0014 12   SER E N   
11587 C  CA  . SER E  12  ? 3.1775 2.5779 3.0292 1.6067  -0.3652 0.0014  12   SER E CA  
11588 C  C   . SER E  12  ? 3.1721 2.5677 3.0515 1.6113  -0.3374 -0.0497 12   SER E C   
11589 O  O   . SER E  12  ? 3.1747 2.6759 3.1040 1.6550  -0.3346 -0.0781 12   SER E O   
11590 C  CB  . SER E  12  ? 3.3264 2.5976 3.1305 1.6393  -0.3752 0.0462  12   SER E CB  
11591 O  OG  . SER E  12  ? 3.5869 2.9003 3.4211 1.7093  -0.3783 0.0408  12   SER E OG  
11592 N  N   . GLY E  13  ? 3.1272 2.4031 2.9722 1.5645  -0.3167 -0.0611 13   GLY E N   
11593 C  CA  . GLY E  13  ? 3.1765 2.4283 3.0381 1.5616  -0.2888 -0.1070 13   GLY E CA  
11594 C  C   . GLY E  13  ? 3.3354 2.4068 3.1422 1.5538  -0.2750 -0.0964 13   GLY E C   
11595 O  O   . GLY E  13  ? 3.3880 2.3563 3.1454 1.5560  -0.2881 -0.0524 13   GLY E O   
11596 N  N   . PRO E  14  ? 3.3043 2.3356 3.1171 1.5426  -0.2480 -0.1374 14   PRO E N   
11597 C  CA  . PRO E  14  ? 3.3789 2.2392 3.1387 1.5320  -0.2325 -0.1331 14   PRO E CA  
11598 C  C   . PRO E  14  ? 3.3349 2.0815 3.0298 1.4729  -0.2363 -0.0997 14   PRO E C   
11599 O  O   . PRO E  14  ? 3.2253 2.0134 2.9190 1.4234  -0.2372 -0.1010 14   PRO E O   
11600 C  CB  . PRO E  14  ? 3.3029 2.1749 3.0867 1.5161  -0.2023 -0.1890 14   PRO E CB  
11601 C  CG  . PRO E  14  ? 3.2204 2.2695 3.0759 1.5477  -0.2046 -0.2198 14   PRO E CG  
11602 C  CD  . PRO E  14  ? 3.1735 2.3186 3.0415 1.5404  -0.2302 -0.1907 14   PRO E CD  
11603 N  N   . GLU E  15  ? 3.4427 2.0453 3.0819 1.4792  -0.2386 -0.0697 15   GLU E N   
11604 C  CA  . GLU E  15  ? 3.4624 1.9505 3.0331 1.4243  -0.2424 -0.0364 15   GLU E CA  
11605 C  C   . GLU E  15  ? 3.4270 1.8508 2.9722 1.3632  -0.2163 -0.0680 15   GLU E C   
11606 O  O   . GLU E  15  ? 3.4517 1.8556 3.0115 1.3688  -0.1929 -0.1092 15   GLU E O   
11607 C  CB  . GLU E  15  ? 3.6242 1.9757 3.1406 1.4483  -0.2513 0.0034  15   GLU E CB  
11608 C  CG  . GLU E  15  ? 3.7737 1.9869 3.2567 1.4479  -0.2271 -0.0185 15   GLU E CG  
11609 C  CD  . GLU E  15  ? 4.0342 2.0957 3.4511 1.4583  -0.2357 0.0245  15   GLU E CD  
11610 O  OE1 . GLU E  15  ? 4.0147 2.0905 3.4194 1.4768  -0.2616 0.0721  15   GLU E OE1 
11611 O  OE2 . GLU E  15  ? 4.2666 2.1956 3.6435 1.4481  -0.2160 0.0098  15   GLU E OE2 
11612 N  N   . GLY E  16  ? 3.4733 1.8676 2.9786 1.3049  -0.2208 -0.0483 16   GLY E N   
11613 C  CA  . GLY E  16  ? 3.5793 1.9234 3.0565 1.2437  -0.1991 -0.0733 16   GLY E CA  
11614 C  C   . GLY E  16  ? 3.4916 1.9559 3.0240 1.2289  -0.1861 -0.1157 16   GLY E C   
11615 O  O   . GLY E  16  ? 3.5142 1.9473 3.0267 1.1799  -0.1674 -0.1383 16   GLY E O   
11616 N  N   . SER E  17  ? 3.3716 1.9737 2.9694 1.2679  -0.1955 -0.1267 17   SER E N   
11617 C  CA  . SER E  17  ? 3.2570 1.9777 2.9100 1.2591  -0.1825 -0.1690 17   SER E CA  
11618 C  C   . SER E  17  ? 3.1188 1.9233 2.7835 1.2245  -0.1931 -0.1598 17   SER E C   
11619 O  O   . SER E  17  ? 2.9436 1.8483 2.6527 1.2156  -0.1835 -0.1926 17   SER E O   
11620 C  CB  . SER E  17  ? 3.3514 2.1805 3.0687 1.3203  -0.1847 -0.1914 17   SER E CB  
11621 O  OG  . SER E  17  ? 3.3637 2.2643 3.0993 1.3553  -0.2120 -0.1598 17   SER E OG  
11622 N  N   . TYR E  18  ? 3.2164 1.9824 2.8416 1.2052  -0.2122 -0.1172 18   TYR E N   
11623 C  CA  . TYR E  18  ? 3.1054 1.9513 2.7415 1.1784  -0.2246 -0.1064 18   TYR E CA  
11624 C  C   . TYR E  18  ? 2.9834 1.9795 2.6862 1.2170  -0.2364 -0.1190 18   TYR E C   
11625 O  O   . TYR E  18  ? 2.8352 1.9232 2.5683 1.1980  -0.2357 -0.1352 18   TYR E O   
11626 C  CB  . TYR E  18  ? 3.0851 1.9262 2.7119 1.1240  -0.2056 -0.1299 18   TYR E CB  
11627 C  CG  . TYR E  18  ? 3.1413 1.8519 2.6965 1.0777  -0.1986 -0.1122 18   TYR E CG  
11628 C  CD1 . TYR E  18  ? 3.2434 1.8417 2.7455 1.0832  -0.2070 -0.0803 18   TYR E CD1 
11629 C  CD2 . TYR E  18  ? 3.0982 1.7987 2.6358 1.0283  -0.1835 -0.1274 18   TYR E CD2 
11630 C  CE1 . TYR E  18  ? 3.3236 1.8044 2.7558 1.0375  -0.2003 -0.0659 18   TYR E CE1 
11631 C  CE2 . TYR E  18  ? 3.2247 1.8129 2.6939 0.9856  -0.1773 -0.1128 18   TYR E CE2 
11632 C  CZ  . TYR E  18  ? 3.4103 1.8894 2.8261 0.9886  -0.1857 -0.0830 18   TYR E CZ  
11633 O  OH  . TYR E  18  ? 3.6178 1.9853 2.9602 0.9420  -0.1792 -0.0698 18   TYR E OH  
11634 N  N   . PHE E  19  ? 3.1480 2.1683 2.8715 1.2721  -0.2469 -0.1118 19   PHE E N   
11635 C  CA  . PHE E  19  ? 2.9755 2.1415 2.7573 1.3125  -0.2611 -0.1200 19   PHE E CA  
11636 C  C   . PHE E  19  ? 2.8009 2.0279 2.5803 1.2952  -0.2827 -0.0942 19   PHE E C   
11637 O  O   . PHE E  19  ? 2.7904 1.9611 2.5292 1.2937  -0.3008 -0.0516 19   PHE E O   
11638 C  CB  . PHE E  19  ? 2.8896 2.0534 2.6804 1.3749  -0.2722 -0.1057 19   PHE E CB  
11639 C  CG  . PHE E  19  ? 2.8513 2.1712 2.6991 1.4188  -0.2880 -0.1129 19   PHE E CG  
11640 C  CD1 . PHE E  19  ? 2.8166 2.2421 2.7210 1.4428  -0.2756 -0.1574 19   PHE E CD1 
11641 C  CD2 . PHE E  19  ? 2.8505 2.2192 2.6946 1.4339  -0.3152 -0.0763 19   PHE E CD2 
11642 C  CE1 . PHE E  19  ? 2.7965 2.3751 2.7522 1.4805  -0.2899 -0.1658 19   PHE E CE1 
11643 C  CE2 . PHE E  19  ? 2.8161 2.3373 2.7116 1.4718  -0.3297 -0.0844 19   PHE E CE2 
11644 C  CZ  . PHE E  19  ? 2.8417 2.4691 2.7929 1.4948  -0.3171 -0.1295 19   PHE E CZ  
11645 N  N   . GLY E  20  ? 2.7613 2.1032 2.5827 1.2813  -0.2804 -0.1211 20   GLY E N   
11646 C  CA  . GLY E  20  ? 2.7752 2.1796 2.5973 1.2626  -0.2981 -0.1042 20   GLY E CA  
11647 C  C   . GLY E  20  ? 2.6555 2.0262 2.4562 1.2042  -0.2864 -0.1111 20   GLY E C   
11648 O  O   . GLY E  20  ? 2.5989 2.0130 2.3951 1.1655  -0.2952 -0.0937 20   GLY E O   
11649 N  N   . PHE E  21  ? 2.7487 2.0557 2.5382 1.1769  -0.2615 -0.1342 21   PHE E N   
11650 C  CA  . PHE E  21  ? 2.7726 2.0651 2.5468 1.1020  -0.2439 -0.1384 21   PHE E CA  
11651 C  C   . PHE E  21  ? 2.8075 2.2315 2.6310 1.0676  -0.2364 -0.1613 21   PHE E C   
11652 O  O   . PHE E  21  ? 2.6928 2.1233 2.5041 1.0122  -0.2307 -0.1540 21   PHE E O   
11653 C  CB  . PHE E  21  ? 2.7518 1.9619 2.5070 1.0853  -0.2192 -0.1603 21   PHE E CB  
11654 C  CG  . PHE E  21  ? 2.9025 2.0830 2.6321 1.0143  -0.2029 -0.1581 21   PHE E CG  
11655 C  CD1 . PHE E  21  ? 3.0704 2.1476 2.7398 0.9869  -0.2066 -0.1279 21   PHE E CD1 
11656 C  CD2 . PHE E  21  ? 3.0630 2.3222 2.8267 0.9748  -0.1843 -0.1845 21   PHE E CD2 
11657 C  CE1 . PHE E  21  ? 3.0735 2.1354 2.7210 0.9250  -0.1922 -0.1257 21   PHE E CE1 
11658 C  CE2 . PHE E  21  ? 3.0253 2.2596 2.7649 0.9154  -0.1702 -0.1796 21   PHE E CE2 
11659 C  CZ  . PHE E  21  ? 3.0827 2.2230 2.7659 0.8924  -0.1744 -0.1509 21   PHE E CZ  
11660 N  N   . ALA E  22  ? 2.8890 2.4167 2.7659 1.0987  -0.2348 -0.1903 22   ALA E N   
11661 C  CA  . ALA E  22  ? 2.8398 2.4960 2.7616 1.0671  -0.2288 -0.2124 22   ALA E CA  
11662 C  C   . ALA E  22  ? 2.8139 2.5842 2.7798 1.1184  -0.2454 -0.2213 22   ALA E C   
11663 O  O   . ALA E  22  ? 2.7918 2.5656 2.7736 1.1772  -0.2485 -0.2322 22   ALA E O   
11664 C  CB  . ALA E  22  ? 2.8053 2.4862 2.7489 1.0313  -0.1999 -0.2489 22   ALA E CB  
11665 N  N   . VAL E  23  ? 2.6477 2.5137 2.6324 1.0973  -0.2558 -0.2177 23   VAL E N   
11666 C  CA  . VAL E  23  ? 2.5577 2.5496 2.5837 1.1396  -0.2728 -0.2251 23   VAL E CA  
11667 C  C   . VAL E  23  ? 2.3773 2.4995 2.4427 1.0915  -0.2617 -0.2556 23   VAL E C   
11668 O  O   . VAL E  23  ? 2.2466 2.3501 2.2985 1.0271  -0.2473 -0.2593 23   VAL E O   
11669 C  CB  . VAL E  23  ? 2.4643 2.4462 2.4664 1.1692  -0.3029 -0.1840 23   VAL E CB  
11670 C  CG1 . VAL E  23  ? 2.5407 2.3851 2.4984 1.2159  -0.3132 -0.1526 23   VAL E CG1 
11671 C  CG2 . VAL E  23  ? 2.3758 2.3493 2.3530 1.1072  -0.3045 -0.1674 23   VAL E CG2 
11672 N  N   . ASP E  24  ? 2.5411 2.7958 2.6538 1.1233  -0.2676 -0.2781 24   ASP E N   
11673 C  CA  . ASP E  24  ? 2.4986 2.8894 2.6481 1.0780  -0.2584 -0.3085 24   ASP E CA  
11674 C  C   . ASP E  24  ? 2.3874 2.9259 2.5825 1.1302  -0.2746 -0.3221 24   ASP E C   
11675 O  O   . ASP E  24  ? 2.1468 2.6751 2.3454 1.2048  -0.2916 -0.3076 24   ASP E O   
11676 C  CB  . ASP E  24  ? 2.5997 2.9915 2.7617 1.0298  -0.2274 -0.3429 24   ASP E CB  
11677 C  CG  . ASP E  24  ? 2.5447 3.0205 2.7201 0.9590  -0.2143 -0.3642 24   ASP E CG  
11678 O  OD1 . ASP E  24  ? 2.4445 2.8508 2.5877 0.9064  -0.2066 -0.3516 24   ASP E OD1 
11679 O  OD2 . ASP E  24  ? 2.6200 3.2316 2.8363 0.9559  -0.2113 -0.3942 24   ASP E OD2 
11680 N  N   . PHE E  25  ? 2.3293 3.0056 2.5576 1.0902  -0.2684 -0.3504 25   PHE E N   
11681 C  CA  . PHE E  25  ? 2.2867 3.1311 2.5624 1.1275  -0.2807 -0.3696 25   PHE E CA  
11682 C  C   . PHE E  25  ? 2.3400 3.2718 2.6571 1.1237  -0.2594 -0.4145 25   PHE E C   
11683 O  O   . PHE E  25  ? 2.3569 3.2227 2.6653 1.0852  -0.2346 -0.4309 25   PHE E O   
11684 C  CB  . PHE E  25  ? 2.3216 3.2774 2.6049 1.0802  -0.2884 -0.3737 25   PHE E CB  
11685 C  CG  . PHE E  25  ? 2.3619 3.2682 2.6115 1.0905  -0.3125 -0.3322 25   PHE E CG  
11686 C  CD1 . PHE E  25  ? 2.4946 3.2817 2.6997 1.0387  -0.3059 -0.3133 25   PHE E CD1 
11687 C  CD2 . PHE E  25  ? 2.3584 3.3460 2.6207 1.1522  -0.3418 -0.3118 25   PHE E CD2 
11688 C  CE1 . PHE E  25  ? 2.6599 3.4096 2.8335 1.0455  -0.3275 -0.2768 25   PHE E CE1 
11689 C  CE2 . PHE E  25  ? 2.4701 3.4178 2.6994 1.1587  -0.3641 -0.2723 25   PHE E CE2 
11690 C  CZ  . PHE E  25  ? 2.7229 3.5522 2.9078 1.1034  -0.3566 -0.2558 25   PHE E CZ  
11691 N  N   . PHE E  26  ? 2.4230 3.5138 2.7856 1.1654  -0.2699 -0.4341 26   PHE E N   
11692 C  CA  . PHE E  26  ? 2.4430 3.6494 2.8498 1.1626  -0.2517 -0.4795 26   PHE E CA  
11693 C  C   . PHE E  26  ? 2.5783 3.9921 3.0277 1.1561  -0.2606 -0.5027 26   PHE E C   
11694 O  O   . PHE E  26  ? 2.6145 4.1103 3.0825 1.2233  -0.2862 -0.4891 26   PHE E O   
11695 C  CB  . PHE E  26  ? 2.4567 3.6310 2.8776 1.2473  -0.2533 -0.4838 26   PHE E CB  
11696 C  CG  . PHE E  26  ? 2.4143 3.6896 2.8759 1.2408  -0.2311 -0.5317 26   PHE E CG  
11697 C  CD1 . PHE E  26  ? 2.4049 3.7121 2.8689 1.1513  -0.2047 -0.5598 26   PHE E CD1 
11698 C  CD2 . PHE E  26  ? 2.5352 3.8741 3.0306 1.3250  -0.2363 -0.5485 26   PHE E CD2 
11699 C  CE1 . PHE E  26  ? 2.5623 3.9676 3.0614 1.1410  -0.1840 -0.6032 26   PHE E CE1 
11700 C  CE2 . PHE E  26  ? 2.6427 4.0846 3.1764 1.3184  -0.2152 -0.5950 26   PHE E CE2 
11701 C  CZ  . PHE E  26  ? 2.6381 4.1159 3.1735 1.2238  -0.1892 -0.6221 26   PHE E CZ  
11702 N  N   . VAL E  27  ? 2.7028 4.2022 3.1652 1.0750  -0.2393 -0.5369 27   VAL E N   
11703 C  CA  . VAL E  27  ? 2.8217 4.5267 3.3227 1.0538  -0.2433 -0.5655 27   VAL E CA  
11704 C  C   . VAL E  27  ? 2.7735 4.5822 3.3072 1.0175  -0.2171 -0.6135 27   VAL E C   
11705 O  O   . VAL E  27  ? 2.8259 4.6208 3.3448 0.9274  -0.1928 -0.6326 27   VAL E O   
11706 C  CB  . VAL E  27  ? 2.7045 4.4206 3.1810 0.9779  -0.2450 -0.5587 27   VAL E CB  
11707 C  CG1 . VAL E  27  ? 2.4931 4.0542 2.9254 0.8980  -0.2207 -0.5551 27   VAL E CG1 
11708 C  CG2 . VAL E  27  ? 2.7835 4.7105 3.2950 0.9350  -0.2423 -0.5960 27   VAL E CG2 
11709 N  N   . PRO E  28  ? 2.5451 4.4557 3.1211 1.0861  -0.2205 -0.6337 28   PRO E N   
11710 C  CA  . PRO E  28  ? 2.5595 4.5739 3.1667 1.0526  -0.1951 -0.6805 28   PRO E CA  
11711 C  C   . PRO E  28  ? 2.6184 4.8445 3.2576 0.9971  -0.1902 -0.7164 28   PRO E C   
11712 O  O   . PRO E  28  ? 2.5979 4.8745 3.2275 0.9579  -0.2005 -0.7087 28   PRO E O   
11713 C  CB  . PRO E  28  ? 2.6048 4.6461 3.2440 1.1572  -0.2027 -0.6877 28   PRO E CB  
11714 C  CG  . PRO E  28  ? 2.5846 4.6403 3.2273 1.2414  -0.2368 -0.6543 28   PRO E CG  
11715 C  CD  . PRO E  28  ? 2.4794 4.3935 3.0715 1.2010  -0.2462 -0.6129 28   PRO E CD  
11716 N  N   . SER E  29  ? 2.5687 4.9235 3.2450 0.9911  -0.1733 -0.7584 29   SER E N   
11717 C  CA  . SER E  29  ? 2.4759 5.0289 3.1784 0.9205  -0.1616 -0.7987 29   SER E CA  
11718 C  C   . SER E  29  ? 2.5346 5.2636 3.2663 0.9532  -0.1876 -0.7992 29   SER E C   
11719 O  O   . SER E  29  ? 2.4132 5.1812 3.1689 1.0568  -0.2133 -0.7822 29   SER E O   
11720 C  CB  . SER E  29  ? 2.3079 4.9790 3.0488 0.9253  -0.1421 -0.8423 29   SER E CB  
11721 O  OG  . SER E  29  ? 2.2924 4.8109 3.0064 0.8949  -0.1182 -0.8420 29   SER E OG  
11722 N  N   . ALA E  30  ? 2.9163 5.7516 3.6435 0.8624  -0.1799 -0.8190 30   ALA E N   
11723 C  CA  . ALA E  30  ? 2.9532 5.9874 3.7069 0.8642  -0.1990 -0.8290 30   ALA E CA  
11724 C  C   . ALA E  30  ? 3.0221 5.9930 3.7632 0.9368  -0.2327 -0.7821 30   ALA E C   
11725 O  O   . ALA E  30  ? 2.8736 5.6356 3.5726 0.9457  -0.2365 -0.7440 30   ALA E O   
11726 C  CB  . ALA E  30  ? 2.7062 5.9725 3.5202 0.9076  -0.2002 -0.8673 30   ALA E CB  
11727 N  N   . SER E  31  ? 2.9772 6.1358 3.7535 0.9863  -0.2576 -0.7836 31   SER E N   
11728 C  CA  . SER E  31  ? 2.7616 5.8874 3.5276 1.0564  -0.2916 -0.7380 31   SER E CA  
11729 C  C   . SER E  31  ? 2.7746 5.8813 3.5654 1.1926  -0.3126 -0.7146 31   SER E C   
11730 O  O   . SER E  31  ? 2.7408 6.0082 3.5658 1.2641  -0.3328 -0.7151 31   SER E O   
11731 C  CB  . SER E  31  ? 2.6162 5.9543 3.4012 1.0290  -0.3070 -0.7502 31   SER E CB  
11732 O  OG  . SER E  31  ? 2.5474 6.1276 3.3881 1.0510  -0.3066 -0.7893 31   SER E OG  
11733 N  N   . SER E  32  ? 2.6892 5.5780 3.4513 1.2234  -0.3058 -0.6917 32   SER E N   
11734 C  CA  . SER E  32  ? 2.4262 5.2550 3.2012 1.3454  -0.3207 -0.6709 32   SER E CA  
11735 C  C   . SER E  32  ? 2.2355 4.9005 2.9697 1.4002  -0.3470 -0.6113 32   SER E C   
11736 O  O   . SER E  32  ? 2.1935 4.8459 2.9015 1.3553  -0.3585 -0.5888 32   SER E O   
11737 C  CB  . SER E  32  ? 2.3472 5.0578 3.1182 1.3397  -0.2928 -0.6918 32   SER E CB  
11738 O  OG  . SER E  32  ? 2.2006 5.0656 3.0060 1.2827  -0.2681 -0.7455 32   SER E OG  
11739 N  N   . ARG E  33  ? 2.0887 4.5883 2.7925 1.4719  -0.3510 -0.5808 33   ARG E N   
11740 C  CA  . ARG E  33  ? 2.1735 4.4875 2.8279 1.5127  -0.3707 -0.5230 33   ARG E CA  
11741 C  C   . ARG E  33  ? 2.3151 4.4530 2.9423 1.4685  -0.3581 -0.5166 33   ARG E C   
11742 O  O   . ARG E  33  ? 2.4316 4.5413 3.0581 1.3963  -0.3283 -0.5493 33   ARG E O   
11743 C  CB  . ARG E  33  ? 2.2470 4.4505 2.8764 1.5968  -0.3768 -0.4945 33   ARG E CB  
11744 C  CG  . ARG E  33  ? 2.4325 4.7852 3.0767 1.6471  -0.3929 -0.4883 33   ARG E CG  
11745 C  CD  . ARG E  33  ? 2.5762 4.8376 3.2058 1.7290  -0.3934 -0.4726 33   ARG E CD  
11746 N  NE  . ARG E  33  ? 2.5961 4.8357 3.2439 1.7254  -0.3677 -0.5144 33   ARG E NE  
11747 C  CZ  . ARG E  33  ? 2.6388 4.6827 3.2599 1.7380  -0.3547 -0.5068 33   ARG E CZ  
11748 N  NH1 . ARG E  33  ? 2.6084 4.4583 3.1818 1.7542  -0.3650 -0.4585 33   ARG E NH1 
11749 N  NH2 . ARG E  33  ? 2.6850 4.7312 3.3251 1.7309  -0.3309 -0.5480 33   ARG E NH2 
11750 N  N   . MET E  34  ? 2.1439 4.1283 2.7245 1.4866  -0.3756 -0.4667 34   MET E N   
11751 C  CA  . MET E  34  ? 2.0413 3.8209 2.5690 1.4233  -0.3611 -0.4487 34   MET E CA  
11752 C  C   . MET E  34  ? 2.1074 3.6931 2.6006 1.4947  -0.3680 -0.4138 34   MET E C   
11753 O  O   . MET E  34  ? 2.1897 3.7537 2.6714 1.5634  -0.3851 -0.3842 34   MET E O   
11754 C  CB  . MET E  34  ? 2.1338 3.9019 2.6304 1.3638  -0.3728 -0.4232 34   MET E CB  
11755 C  CG  . MET E  34  ? 2.3498 4.2875 2.8701 1.2803  -0.3632 -0.4588 34   MET E CG  
11756 S  SD  . MET E  34  ? 2.5314 4.3586 3.0151 1.1510  -0.3307 -0.4768 34   MET E SD  
11757 C  CE  . MET E  34  ? 2.2152 4.2574 2.7246 1.0722  -0.3267 -0.5143 34   MET E CE  
11758 N  N   . PHE E  35  ? 2.2544 3.6657 2.7100 1.4470  -0.3474 -0.4111 35   PHE E N   
11759 C  CA  . PHE E  35  ? 2.3006 3.5260 2.7214 1.5018  -0.3480 -0.3862 35   PHE E CA  
11760 C  C   . PHE E  35  ? 2.4326 3.4745 2.7945 1.4427  -0.3424 -0.3560 35   PHE E C   
11761 O  O   . PHE E  35  ? 2.2832 3.3334 2.6349 1.3571  -0.3314 -0.3627 35   PHE E O   
11762 C  CB  . PHE E  35  ? 2.3212 3.5298 2.7625 1.5162  -0.3227 -0.4248 35   PHE E CB  
11763 C  CG  . PHE E  35  ? 2.5295 3.8938 3.0143 1.5530  -0.3218 -0.4513 35   PHE E CG  
11764 C  CD1 . PHE E  35  ? 2.6580 3.9780 3.1276 1.6179  -0.3321 -0.4272 35   PHE E CD1 
11765 C  CD2 . PHE E  35  ? 2.4880 4.0454 3.0280 1.5208  -0.3098 -0.5011 35   PHE E CD2 
11766 C  CE1 . PHE E  35  ? 2.5617 4.0269 3.0699 1.6555  -0.3316 -0.4521 35   PHE E CE1 
11767 C  CE2 . PHE E  35  ? 2.4296 4.1370 3.0067 1.5518  -0.3090 -0.5261 35   PHE E CE2 
11768 C  CZ  . PHE E  35  ? 2.4307 4.0920 2.9917 1.6220  -0.3205 -0.5015 35   PHE E CZ  
11769 N  N   . LEU E  36  ? 2.6482 3.5231 2.9693 1.4907  -0.3496 -0.3233 36   LEU E N   
11770 C  CA  . LEU E  36  ? 2.5702 3.2629 2.8340 1.4423  -0.3422 -0.2970 36   LEU E CA  
11771 C  C   . LEU E  36  ? 2.5431 3.1235 2.7960 1.4332  -0.3154 -0.3190 36   LEU E C   
11772 O  O   . LEU E  36  ? 2.6439 3.1935 2.9017 1.4845  -0.3108 -0.3261 36   LEU E O   
11773 C  CB  . LEU E  36  ? 2.6849 3.2625 2.9009 1.4867  -0.3675 -0.2418 36   LEU E CB  
11774 C  CG  . LEU E  36  ? 2.7414 3.4019 2.9549 1.4976  -0.3971 -0.2094 36   LEU E CG  
11775 C  CD1 . LEU E  36  ? 3.1155 3.8954 3.3592 1.5520  -0.4099 -0.2063 36   LEU E CD1 
11776 C  CD2 . LEU E  36  ? 2.7773 3.2771 2.9253 1.4920  -0.4102 -0.1555 36   LEU E CD2 
11777 N  N   . LEU E  37  ? 2.2542 2.7683 2.4856 1.3516  -0.2942 -0.3267 37   LEU E N   
11778 C  CA  . LEU E  37  ? 2.2631 2.6650 2.4769 1.3329  -0.2691 -0.3429 37   LEU E CA  
11779 C  C   . LEU E  37  ? 2.3162 2.5357 2.4669 1.3211  -0.2730 -0.3034 37   LEU E C   
11780 O  O   . LEU E  37  ? 2.2802 2.4681 2.4039 1.2679  -0.2769 -0.2809 37   LEU E O   
11781 C  CB  . LEU E  37  ? 2.2148 2.6719 2.4464 1.2509  -0.2421 -0.3769 37   LEU E CB  
11782 C  CG  . LEU E  37  ? 2.1850 2.8210 2.4753 1.2498  -0.2335 -0.4203 37   LEU E CG  
11783 C  CD1 . LEU E  37  ? 2.2044 2.8669 2.5002 1.1629  -0.2056 -0.4480 37   LEU E CD1 
11784 C  CD2 . LEU E  37  ? 2.2956 2.9614 2.6143 1.3256  -0.2313 -0.4436 37   LEU E CD2 
11785 N  N   . VAL E  38  ? 2.6699 2.7719 2.7954 1.3704  -0.2717 -0.2963 38   VAL E N   
11786 C  CA  . VAL E  38  ? 2.7763 2.7045 2.8379 1.3552  -0.2739 -0.2592 38   VAL E CA  
11787 C  C   . VAL E  38  ? 2.7576 2.5838 2.7999 1.3308  -0.2463 -0.2798 38   VAL E C   
11788 O  O   . VAL E  38  ? 2.6762 2.5233 2.7421 1.3547  -0.2323 -0.3072 38   VAL E O   
11789 C  CB  . VAL E  38  ? 3.0283 2.8938 3.0610 1.3966  -0.2933 -0.2163 38   VAL E CB  
11790 C  CG1 . VAL E  38  ? 2.9934 2.6921 2.9588 1.3672  -0.2948 -0.1779 38   VAL E CG1 
11791 C  CG2 . VAL E  38  ? 3.0384 3.0250 3.0943 1.4241  -0.3205 -0.1982 38   VAL E CG2 
11792 N  N   . GLY E  39  ? 2.7213 2.4454 2.7210 1.2796  -0.2379 -0.2671 39   GLY E N   
11793 C  CA  . GLY E  39  ? 2.7696 2.3937 2.7444 1.2544  -0.2134 -0.2836 39   GLY E CA  
11794 C  C   . GLY E  39  ? 2.7399 2.2128 2.6595 1.2577  -0.2144 -0.2522 39   GLY E C   
11795 O  O   . GLY E  39  ? 2.7126 2.1217 2.5933 1.2531  -0.2319 -0.2111 39   GLY E O   
11796 N  N   . ALA E  40  ? 2.6537 2.0725 2.5698 1.2646  -0.1947 -0.2741 40   ALA E N   
11797 C  CA  . ALA E  40  ? 2.7306 1.9992 2.5931 1.2609  -0.1894 -0.2540 40   ALA E CA  
11798 C  C   . ALA E  40  ? 2.8028 2.0166 2.6512 1.2230  -0.1610 -0.2853 40   ALA E C   
11799 O  O   . ALA E  40  ? 2.7608 1.9758 2.6268 1.2420  -0.1439 -0.3170 40   ALA E O   
11800 C  CB  . ALA E  40  ? 2.8019 2.0531 2.6719 1.3192  -0.1954 -0.2482 40   ALA E CB  
11801 N  N   . PRO E  41  ? 2.9885 2.1584 2.8046 1.1699  -0.1553 -0.2782 41   PRO E N   
11802 C  CA  . PRO E  41  ? 3.0040 2.1461 2.8109 1.1324  -0.1285 -0.3105 41   PRO E CA  
11803 C  C   . PRO E  41  ? 3.0342 2.0512 2.7981 1.1267  -0.1135 -0.3146 41   PRO E C   
11804 O  O   . PRO E  41  ? 3.0418 2.0525 2.8076 1.1087  -0.0898 -0.3500 41   PRO E O   
11805 C  CB  . PRO E  41  ? 2.8600 1.9926 2.6412 1.0797  -0.1302 -0.2935 41   PRO E CB  
11806 C  CG  . PRO E  41  ? 2.8807 1.9725 2.6324 1.0882  -0.1561 -0.2478 41   PRO E CG  
11807 C  CD  . PRO E  41  ? 2.9389 2.0971 2.7286 1.1434  -0.1729 -0.2426 41   PRO E CD  
11808 N  N   . LYS E  42  ? 3.1423 2.0601 2.8657 1.1406  -0.1255 -0.2815 42   LYS E N   
11809 C  CA  . LYS E  42  ? 3.1145 1.9056 2.7933 1.1342  -0.1106 -0.2870 42   LYS E CA  
11810 C  C   . LYS E  42  ? 3.1933 1.9766 2.8946 1.1907  -0.1087 -0.2989 42   LYS E C   
11811 O  O   . LYS E  42  ? 3.3920 2.0578 3.0531 1.1951  -0.1013 -0.2954 42   LYS E O   
11812 C  CB  . LYS E  42  ? 3.0207 1.6896 2.6298 1.1061  -0.1217 -0.2445 42   LYS E CB  
11813 C  CG  . LYS E  42  ? 2.9965 1.6312 2.5654 1.0443  -0.1131 -0.2429 42   LYS E CG  
11814 C  CD  . LYS E  42  ? 3.0772 1.5773 2.5691 1.0148  -0.1188 -0.2088 42   LYS E CD  
11815 C  CE  . LYS E  42  ? 3.0986 1.5591 2.5456 0.9544  -0.1053 -0.2152 42   LYS E CE  
11816 N  NZ  . LYS E  42  ? 3.4557 1.7872 2.8218 0.9205  -0.1097 -0.1844 42   LYS E NZ  
11817 N  N   . ALA E  43  ? 3.0155 1.9212 2.7782 1.2341  -0.1149 -0.3141 43   ALA E N   
11818 C  CA  . ALA E  43  ? 3.0975 2.0086 2.8839 1.2945  -0.1158 -0.3226 43   ALA E CA  
11819 C  C   . ALA E  43  ? 3.1509 2.0525 2.9513 1.2985  -0.0871 -0.3719 43   ALA E C   
11820 O  O   . ALA E  43  ? 3.1755 2.1573 3.0053 1.2755  -0.0713 -0.4082 43   ALA E O   
11821 C  CB  . ALA E  43  ? 3.0944 2.1522 2.9399 1.3388  -0.1337 -0.3218 43   ALA E CB  
11822 N  N   . ASN E  44  ? 3.1004 1.9025 2.8781 1.3273  -0.0799 -0.3738 44   ASN E N   
11823 C  CA  . ASN E  44  ? 3.1470 1.9477 2.9431 1.3423  -0.0535 -0.4225 44   ASN E CA  
11824 C  C   . ASN E  44  ? 3.1101 2.0622 2.9769 1.3927  -0.0554 -0.4490 44   ASN E C   
11825 O  O   . ASN E  44  ? 3.1208 2.1310 3.0117 1.4389  -0.0776 -0.4253 44   ASN E O   
11826 C  CB  . ASN E  44  ? 3.3036 1.9577 3.0583 1.3658  -0.0465 -0.4169 44   ASN E CB  
11827 C  CG  . ASN E  44  ? 3.4748 1.9868 3.1617 1.3069  -0.0318 -0.4155 44   ASN E CG  
11828 O  OD1 . ASN E  44  ? 3.2918 1.8171 2.9735 1.2595  -0.0122 -0.4464 44   ASN E OD1 
11829 N  ND2 . ASN E  44  ? 4.5526 2.9298 4.1845 1.3087  -0.0413 -0.3799 44   ASN E ND2 
11830 N  N   . THR E  45  ? 3.1718 2.1967 3.0705 1.3812  -0.0324 -0.4985 45   THR E N   
11831 C  CA  . THR E  45  ? 3.1795 2.3540 3.1434 1.4235  -0.0308 -0.5302 45   THR E CA  
11832 C  C   . THR E  45  ? 3.1983 2.3497 3.1722 1.4511  -0.0056 -0.5741 45   THR E C   
11833 O  O   . THR E  45  ? 3.2851 2.3024 3.2157 1.4369  0.0112  -0.5811 45   THR E O   
11834 C  CB  . THR E  45  ? 3.1053 2.4168 3.1057 1.3858  -0.0266 -0.5530 45   THR E CB  
11835 O  OG1 . THR E  45  ? 2.9774 2.2581 2.9614 1.3373  0.0008  -0.5872 45   THR E OG1 
11836 C  CG2 . THR E  45  ? 3.0836 2.4081 3.0713 1.3562  -0.0488 -0.5128 45   THR E CG2 
11837 N  N   . THR E  46  ? 3.0977 2.3869 3.1288 1.4890  -0.0023 -0.6062 46   THR E N   
11838 C  CA  . THR E  46  ? 3.3358 2.6308 3.3851 1.5206  0.0212  -0.6517 46   THR E CA  
11839 C  C   . THR E  46  ? 3.2514 2.5971 3.3109 1.4724  0.0498  -0.7011 46   THR E C   
11840 O  O   . THR E  46  ? 3.3775 2.7442 3.4543 1.4923  0.0719  -0.7447 46   THR E O   
11841 C  CB  . THR E  46  ? 3.4116 2.8389 3.5168 1.5887  0.0095  -0.6618 46   THR E CB  
11842 O  OG1 . THR E  46  ? 3.2614 2.8603 3.4124 1.5706  0.0012  -0.6727 46   THR E OG1 
11843 C  CG2 . THR E  46  ? 3.2740 2.6498 3.3666 1.6409  -0.0181 -0.6133 46   THR E CG2 
11844 N  N   . GLN E  47  ? 3.0587 2.4262 3.1070 1.4111  0.0498  -0.6951 47   GLN E N   
11845 C  CA  . GLN E  47  ? 2.9928 2.4140 3.0484 1.3624  0.0753  -0.7384 47   GLN E CA  
11846 C  C   . GLN E  47  ? 3.0834 2.3802 3.0976 1.3452  0.1031  -0.7651 47   GLN E C   
11847 O  O   . GLN E  47  ? 3.1488 2.2952 3.1089 1.3302  0.1014  -0.7394 47   GLN E O   
11848 C  CB  . GLN E  47  ? 2.8810 2.3219 2.9224 1.3023  0.0683  -0.7193 47   GLN E CB  
11849 C  CG  . GLN E  47  ? 2.7959 2.3779 2.8824 1.3099  0.0474  -0.7059 47   GLN E CG  
11850 C  CD  . GLN E  47  ? 2.8201 2.3828 2.8827 1.2609  0.0356  -0.6743 47   GLN E CD  
11851 O  OE1 . GLN E  47  ? 2.8430 2.2796 2.8523 1.2279  0.0379  -0.6537 47   GLN E OE1 
11852 N  NE2 . GLN E  47  ? 2.7747 2.4646 2.8756 1.2548  0.0238  -0.6723 47   GLN E NE2 
11853 N  N   . PRO E  48  ? 3.2522 2.6093 3.2883 1.3441  0.1292  -0.8178 48   PRO E N   
11854 C  CA  . PRO E  48  ? 3.5209 2.7641 3.5185 1.3303  0.1580  -0.8491 48   PRO E CA  
11855 C  C   . PRO E  48  ? 3.3767 2.5246 3.3180 1.2603  0.1670  -0.8420 48   PRO E C   
11856 O  O   . PRO E  48  ? 3.0760 2.2989 3.0218 1.2116  0.1711  -0.8511 48   PRO E O   
11857 C  CB  . PRO E  48  ? 3.5281 2.8969 3.5677 1.3352  0.1818  -0.9071 48   PRO E CB  
11858 C  CG  . PRO E  48  ? 3.2859 2.8161 3.3882 1.3746  0.1624  -0.9028 48   PRO E CG  
11859 C  CD  . PRO E  48  ? 3.1403 2.6794 3.2378 1.3553  0.1341  -0.8532 48   PRO E CD  
11860 N  N   . GLY E  49  ? 3.5721 2.5547 3.4584 1.2553  0.1693  -0.8250 49   GLY E N   
11861 C  CA  . GLY E  49  ? 3.3622 2.2451 3.1884 1.1902  0.1791  -0.8219 49   GLY E CA  
11862 C  C   . GLY E  49  ? 3.1519 2.0284 2.9573 1.1563  0.1545  -0.7733 49   GLY E C   
11863 O  O   . GLY E  49  ? 3.1676 1.9686 2.9205 1.1015  0.1604  -0.7681 49   GLY E O   
11864 N  N   . ILE E  50  ? 3.1897 2.1461 3.0326 1.1862  0.1278  -0.7396 50   ILE E N   
11865 C  CA  . ILE E  50  ? 3.2923 2.2568 3.1213 1.1571  0.1047  -0.6953 50   ILE E CA  
11866 C  C   . ILE E  50  ? 3.4169 2.2666 3.2112 1.1775  0.0822  -0.6446 50   ILE E C   
11867 O  O   . ILE E  50  ? 3.4248 2.2939 3.2463 1.2325  0.0659  -0.6267 50   ILE E O   
11868 C  CB  . ILE E  50  ? 3.1479 2.2753 3.0373 1.1710  0.0908  -0.6929 50   ILE E CB  
11869 C  CG1 . ILE E  50  ? 3.1820 2.4247 3.1040 1.1483  0.1141  -0.7442 50   ILE E CG1 
11870 C  CG2 . ILE E  50  ? 2.9534 2.0819 2.8264 1.1407  0.0690  -0.6492 50   ILE E CG2 
11871 C  CD1 . ILE E  50  ? 2.9949 2.3943 2.9690 1.1461  0.1035  -0.7450 50   ILE E CD1 
11872 N  N   . VAL E  51  ? 3.5776 2.3127 3.3095 1.1324  0.0807  -0.6214 51   VAL E N   
11873 C  CA  . VAL E  51  ? 3.6655 2.2893 3.3564 1.1414  0.0597  -0.5717 51   VAL E CA  
11874 C  C   . VAL E  51  ? 3.3760 2.0507 3.0698 1.1262  0.0335  -0.5275 51   VAL E C   
11875 O  O   . VAL E  51  ? 3.1269 1.8257 2.8054 1.0776  0.0365  -0.5272 51   VAL E O   
11876 C  CB  . VAL E  51  ? 3.8913 2.3582 3.5073 1.0991  0.0733  -0.5727 51   VAL E CB  
11877 C  CG1 . VAL E  51  ? 3.9175 2.3954 3.5058 1.0343  0.0917  -0.5978 51   VAL E CG1 
11878 C  CG2 . VAL E  51  ? 3.9199 2.2848 3.4867 1.0930  0.0497  -0.5164 51   VAL E CG2 
11879 N  N   . GLU E  52  ? 3.3216 2.0158 3.0348 1.1695  0.0083  -0.4916 52   GLU E N   
11880 C  CA  . GLU E  52  ? 3.1664 1.9056 2.8822 1.1603  -0.0177 -0.4489 52   GLU E CA  
11881 C  C   . GLU E  52  ? 3.0289 1.9039 2.7872 1.1394  -0.0157 -0.4666 52   GLU E C   
11882 O  O   . GLU E  52  ? 2.9343 1.8125 2.6722 1.0977  -0.0214 -0.4486 52   GLU E O   
11883 C  CB  . GLU E  52  ? 3.2265 1.8463 2.8720 1.1154  -0.0253 -0.4120 52   GLU E CB  
11884 C  CG  . GLU E  52  ? 3.5148 2.0050 3.1157 1.1353  -0.0339 -0.3832 52   GLU E CG  
11885 C  CD  . GLU E  52  ? 3.6717 2.0635 3.2045 1.0901  -0.0450 -0.3426 52   GLU E CD  
11886 O  OE1 . GLU E  52  ? 3.8876 2.1817 3.3816 1.1039  -0.0569 -0.3102 52   GLU E OE1 
11887 O  OE2 . GLU E  52  ? 3.5481 1.9608 3.0641 1.0412  -0.0418 -0.3425 52   GLU E OE2 
11888 N  N   . GLY E  53  ? 3.1626 2.1511 2.9792 1.1693  -0.0072 -0.5024 53   GLY E N   
11889 C  CA  . GLY E  53  ? 3.1494 2.2719 3.0082 1.1520  -0.0058 -0.5199 53   GLY E CA  
11890 C  C   . GLY E  53  ? 3.0623 2.2503 2.9403 1.1602  -0.0324 -0.4849 53   GLY E C   
11891 O  O   . GLY E  53  ? 3.0048 2.2616 2.8956 1.1298  -0.0334 -0.4868 53   GLY E O   
11892 N  N   . GLY E  54  ? 3.0281 2.1960 2.9068 1.2014  -0.0537 -0.4538 54   GLY E N   
11893 C  CA  . GLY E  54  ? 2.7696 2.0071 2.6676 1.2133  -0.0793 -0.4234 54   GLY E CA  
11894 C  C   . GLY E  54  ? 2.7227 2.1140 2.6874 1.2521  -0.0838 -0.4478 54   GLY E C   
11895 O  O   . GLY E  54  ? 2.8888 2.3551 2.8883 1.2549  -0.0653 -0.4910 54   GLY E O   
11896 N  N   . GLN E  55  ? 2.5874 2.0339 2.5689 1.2804  -0.1089 -0.4205 55   GLN E N   
11897 C  CA  . GLN E  55  ? 2.6389 2.2410 2.6818 1.3169  -0.1156 -0.4422 55   GLN E CA  
11898 C  C   . GLN E  55  ? 2.7924 2.4639 2.8469 1.3193  -0.1410 -0.4141 55   GLN E C   
11899 O  O   . GLN E  55  ? 2.7807 2.3719 2.7949 1.3038  -0.1558 -0.3737 55   GLN E O   
11900 C  CB  . GLN E  55  ? 2.6117 2.2218 2.6725 1.3787  -0.1176 -0.4491 55   GLN E CB  
11901 C  CG  . GLN E  55  ? 2.7098 2.2129 2.7323 1.4105  -0.1368 -0.4029 55   GLN E CG  
11902 C  CD  . GLN E  55  ? 2.8187 2.3107 2.8540 1.4723  -0.1350 -0.4117 55   GLN E CD  
11903 O  OE1 . GLN E  55  ? 2.8222 2.3827 2.8936 1.4905  -0.1183 -0.4540 55   GLN E OE1 
11904 N  NE2 . GLN E  55  ? 2.9912 2.3979 2.9961 1.5054  -0.1520 -0.3717 55   GLN E NE2 
11905 N  N   . VAL E  56  ? 2.9080 2.7368 3.0182 1.3370  -0.1450 -0.4383 56   VAL E N   
11906 C  CA  . VAL E  56  ? 2.7651 2.6870 2.8956 1.3454  -0.1684 -0.4200 56   VAL E CA  
11907 C  C   . VAL E  56  ? 2.7298 2.7469 2.8963 1.4064  -0.1830 -0.4211 56   VAL E C   
11908 O  O   . VAL E  56  ? 2.6543 2.7662 2.8622 1.4280  -0.1712 -0.4589 56   VAL E O   
11909 C  CB  . VAL E  56  ? 2.6164 2.6535 2.7802 1.3001  -0.1592 -0.4475 56   VAL E CB  
11910 C  CG1 . VAL E  56  ? 2.6511 2.7955 2.8373 1.2956  -0.1803 -0.4298 56   VAL E CG1 
11911 C  CG2 . VAL E  56  ? 2.5364 2.4754 2.6581 1.2224  -0.1438 -0.4340 56   VAL E CG2 
11912 N  N   . LEU E  57  ? 2.8698 2.8681 3.0198 1.4335  -0.2084 -0.3798 57   LEU E N   
11913 C  CA  . LEU E  57  ? 2.9710 3.0426 3.1461 1.4953  -0.2241 -0.3730 57   LEU E CA  
11914 C  C   . LEU E  57  ? 2.8276 3.0699 3.0452 1.5033  -0.2424 -0.3761 57   LEU E C   
11915 O  O   . LEU E  57  ? 2.6975 2.9521 2.9057 1.4714  -0.2535 -0.3594 57   LEU E O   
11916 C  CB  . LEU E  57  ? 3.0728 3.0120 3.2001 1.5251  -0.2398 -0.3240 57   LEU E CB  
11917 C  CG  . LEU E  57  ? 3.1899 2.9693 3.2782 1.5307  -0.2232 -0.3218 57   LEU E CG  
11918 C  CD1 . LEU E  57  ? 3.1568 2.7971 3.1924 1.4716  -0.2138 -0.3062 57   LEU E CD1 
11919 C  CD2 . LEU E  57  ? 3.2795 2.9944 3.3474 1.5872  -0.2385 -0.2877 57   LEU E CD2 
11920 N  N   . LYS E  58  ? 2.8142 3.1919 3.0783 1.5456  -0.2451 -0.3991 58   LYS E N   
11921 C  CA  . LYS E  58  ? 2.8159 3.3725 3.1226 1.5583  -0.2628 -0.4040 58   LYS E CA  
11922 C  C   . LYS E  58  ? 3.1183 3.6663 3.4114 1.6147  -0.2881 -0.3630 58   LYS E C   
11923 O  O   . LYS E  58  ? 3.3731 3.9196 3.6734 1.6664  -0.2872 -0.3657 58   LYS E O   
11924 C  CB  . LYS E  58  ? 2.7956 3.5233 3.1621 1.5632  -0.2485 -0.4576 58   LYS E CB  
11925 C  CG  . LYS E  58  ? 2.7135 3.6472 3.1279 1.5647  -0.2629 -0.4708 58   LYS E CG  
11926 C  CD  . LYS E  58  ? 2.6069 3.7074 3.0758 1.5790  -0.2500 -0.5200 58   LYS E CD  
11927 C  CE  . LYS E  58  ? 2.6598 3.7319 3.1255 1.6472  -0.2531 -0.5141 58   LYS E CE  
11928 N  NZ  . LYS E  58  ? 2.5987 3.8437 3.1161 1.6650  -0.2430 -0.5608 58   LYS E NZ  
11929 N  N   . CYS E  59  ? 3.0623 3.6043 3.3349 1.6055  -0.3102 -0.3251 59   CYS E N   
11930 C  CA  . CYS E  59  ? 3.0669 3.6044 3.3237 1.6539  -0.3353 -0.2820 59   CYS E CA  
11931 C  C   . CYS E  59  ? 2.8708 3.6147 3.1731 1.6657  -0.3528 -0.2906 59   CYS E C   
11932 O  O   . CYS E  59  ? 2.6237 3.4662 2.9487 1.6213  -0.3528 -0.3097 59   CYS E O   
11933 C  CB  . CYS E  59  ? 2.9435 3.3316 3.1409 1.6340  -0.3487 -0.2304 59   CYS E CB  
11934 S  SG  . CYS E  59  ? 3.0716 3.2178 3.2082 1.6100  -0.3289 -0.2170 59   CYS E SG  
11935 N  N   . ASP E  60  ? 3.0105 3.8218 3.3255 1.7244  -0.3673 -0.2771 60   ASP E N   
11936 C  CA  . ASP E  60  ? 2.8552 3.8765 3.2141 1.7371  -0.3827 -0.2878 60   ASP E CA  
11937 C  C   . ASP E  60  ? 2.5870 3.6068 2.9196 1.7452  -0.4108 -0.2372 60   ASP E C   
11938 O  O   . ASP E  60  ? 2.6823 3.5705 2.9726 1.7783  -0.4218 -0.1920 60   ASP E O   
11939 C  CB  . ASP E  60  ? 2.7934 3.9172 3.1863 1.7964  -0.3810 -0.3083 60   ASP E CB  
11940 C  CG  . ASP E  60  ? 2.6716 4.0183 3.1057 1.8090  -0.3975 -0.3172 60   ASP E CG  
11941 O  OD1 . ASP E  60  ? 2.7020 4.1760 3.1638 1.7562  -0.3959 -0.3427 60   ASP E OD1 
11942 O  OD2 . ASP E  60  ? 2.6902 4.0871 3.1286 1.8697  -0.4111 -0.2999 60   ASP E OD2 
11943 N  N   . TRP E  61  ? 2.5993 3.7686 2.9569 1.7114  -0.4216 -0.2463 61   TRP E N   
11944 C  CA  . TRP E  61  ? 2.6098 3.8165 2.9495 1.7135  -0.4484 -0.2046 61   TRP E CA  
11945 C  C   . TRP E  61  ? 2.7856 4.1463 3.1509 1.7643  -0.4654 -0.1968 61   TRP E C   
11946 O  O   . TRP E  61  ? 2.7695 4.0936 3.1060 1.7966  -0.4863 -0.1486 61   TRP E O   
11947 C  CB  . TRP E  61  ? 2.4940 3.7857 2.8467 1.6479  -0.4508 -0.2206 61   TRP E CB  
11948 C  CG  . TRP E  61  ? 2.5160 3.9272 2.8702 1.6448  -0.4765 -0.1958 61   TRP E CG  
11949 C  CD1 . TRP E  61  ? 2.5257 4.1484 2.9237 1.6171  -0.4817 -0.2254 61   TRP E CD1 
11950 C  CD2 . TRP E  61  ? 2.8037 4.1379 3.1133 1.6665  -0.4996 -0.1374 61   TRP E CD2 
11951 N  NE1 . TRP E  61  ? 2.7506 4.4329 3.1333 1.6198  -0.5065 -0.1898 61   TRP E NE1 
11952 C  CE2 . TRP E  61  ? 2.8988 4.4072 3.2278 1.6516  -0.5182 -0.1346 61   TRP E CE2 
11953 C  CE3 . TRP E  61  ? 2.9478 4.0863 3.2020 1.6922  -0.5054 -0.0882 61   TRP E CE3 
11954 C  CZ2 . TRP E  61  ? 2.9936 4.4870 3.2890 1.6643  -0.5427 -0.0832 61   TRP E CZ2 
11955 C  CZ3 . TRP E  61  ? 3.0343 4.1569 3.2557 1.7041  -0.5299 -0.0366 61   TRP E CZ3 
11956 C  CH2 . TRP E  61  ? 3.0243 4.3236 3.2665 1.6915  -0.5485 -0.0339 61   TRP E CH2 
11957 N  N   . SER E  62  ? 2.6464 4.1810 3.0639 1.7702  -0.4562 -0.2431 62   SER E N   
11958 C  CA  . SER E  62  ? 2.5669 4.2848 3.0143 1.8091  -0.4703 -0.2447 62   SER E CA  
11959 C  C   . SER E  62  ? 2.6939 4.3342 3.1086 1.8774  -0.4899 -0.1906 62   SER E C   
11960 O  O   . SER E  62  ? 2.7159 4.4588 3.1309 1.8916  -0.5112 -0.1648 62   SER E O   
11961 C  CB  . SER E  62  ? 2.5619 4.4040 3.0560 1.8252  -0.4526 -0.2974 62   SER E CB  
11962 O  OG  . SER E  62  ? 2.6528 4.3661 3.1333 1.8790  -0.4424 -0.2941 62   SER E OG  
11963 N  N   . SER E  63  ? 2.7808 4.2396 3.1663 1.9163  -0.4822 -0.1733 63   SER E N   
11964 C  CA  . SER E  63  ? 2.9118 4.2624 3.2610 1.9776  -0.4985 -0.1201 63   SER E CA  
11965 C  C   . SER E  63  ? 2.9834 4.1196 3.3010 1.9961  -0.4820 -0.1149 63   SER E C   
11966 O  O   . SER E  63  ? 2.9368 4.0311 3.2648 1.9659  -0.4587 -0.1542 63   SER E O   
11967 C  CB  . SER E  63  ? 2.9872 4.4886 3.3650 2.0441  -0.5104 -0.1198 63   SER E CB  
11968 O  OG  . SER E  63  ? 3.1118 4.5201 3.4541 2.0998  -0.5294 -0.0631 63   SER E OG  
11969 N  N   . THR E  64  ? 3.1069 4.1078 3.3842 2.0425  -0.4940 -0.0655 64   THR E N   
11970 C  CA  . THR E  64  ? 3.2102 4.0242 3.4592 2.0753  -0.4801 -0.0591 64   THR E CA  
11971 C  C   . THR E  64  ? 3.1791 3.8027 3.3862 2.0186  -0.4651 -0.0544 64   THR E C   
11972 O  O   . THR E  64  ? 3.2773 3.7202 3.4450 2.0367  -0.4584 -0.0335 64   THR E O   
11973 C  CB  . THR E  64  ? 3.2264 4.1132 3.5175 2.1107  -0.4613 -0.1104 64   THR E CB  
11974 O  OG1 . THR E  64  ? 3.2208 4.3242 3.5567 2.1463  -0.4734 -0.1248 64   THR E OG1 
11975 C  CG2 . THR E  64  ? 3.3712 4.0992 3.6371 2.1687  -0.4538 -0.0969 64   THR E CG2 
11976 N  N   . ARG E  65  ? 3.0485 3.7123 3.2629 1.9495  -0.4589 -0.0749 65   ARG E N   
11977 C  CA  . ARG E  65  ? 3.0096 3.5103 3.1824 1.8907  -0.4473 -0.0674 65   ARG E CA  
11978 C  C   . ARG E  65  ? 3.0389 3.4116 3.2032 1.8874  -0.4195 -0.0964 65   ARG E C   
11979 O  O   . ARG E  65  ? 3.0583 3.2594 3.1765 1.8552  -0.4103 -0.0805 65   ARG E O   
11980 C  CB  . ARG E  65  ? 3.0805 3.4428 3.1947 1.8885  -0.4650 -0.0057 65   ARG E CB  
11981 C  CG  . ARG E  65  ? 3.0820 3.5578 3.1991 1.9024  -0.4941 0.0301  65   ARG E CG  
11982 C  CD  . ARG E  65  ? 2.9567 3.5073 3.0768 1.8384  -0.5004 0.0257  65   ARG E CD  
11983 N  NE  . ARG E  65  ? 2.9611 3.6247 3.0829 1.8488  -0.5277 0.0588  65   ARG E NE  
11984 C  CZ  . ARG E  65  ? 3.0104 3.5899 3.0852 1.8424  -0.5461 0.1125  65   ARG E CZ  
11985 N  NH1 . ARG E  65  ? 3.0605 3.4412 3.0816 1.8243  -0.5400 0.1390  65   ARG E NH1 
11986 N  NH2 . ARG E  65  ? 3.0111 3.7114 3.0914 1.8508  -0.5702 0.1388  65   ARG E NH2 
11987 N  N   . ARG E  66  ? 3.1936 3.6525 3.4008 1.9172  -0.4052 -0.1404 66   ARG E N   
11988 C  CA  . ARG E  66  ? 3.1738 3.5217 3.3750 1.9198  -0.3790 -0.1693 66   ARG E CA  
11989 C  C   . ARG E  66  ? 3.0360 3.4060 3.2542 1.8556  -0.3568 -0.2140 66   ARG E C   
11990 O  O   . ARG E  66  ? 2.9259 3.4599 3.1874 1.8333  -0.3567 -0.2448 66   ARG E O   
11991 C  CB  . ARG E  66  ? 3.1594 3.5851 3.3964 1.9879  -0.3744 -0.1942 66   ARG E CB  
11992 C  CG  . ARG E  66  ? 3.3100 3.6625 3.5225 2.0576  -0.3899 -0.1521 66   ARG E CG  
11993 C  CD  . ARG E  66  ? 3.4021 3.8383 3.6521 2.1260  -0.3839 -0.1815 66   ARG E CD  
11994 N  NE  . ARG E  66  ? 3.6709 4.0280 3.8972 2.1978  -0.3976 -0.1418 66   ARG E NE  
11995 C  CZ  . ARG E  66  ? 3.7436 4.1642 3.9964 2.2709  -0.3977 -0.1560 66   ARG E CZ  
11996 N  NH1 . ARG E  66  ? 3.5797 4.1499 3.8833 2.2788  -0.3848 -0.2099 66   ARG E NH1 
11997 N  NH2 . ARG E  66  ? 3.8861 4.2223 4.1137 2.3362  -0.4107 -0.1163 66   ARG E NH2 
11998 N  N   . CYS E  67  ? 3.2194 3.4259 3.4029 1.8251  -0.3372 -0.2180 67   CYS E N   
11999 C  CA  . CYS E  67  ? 3.0416 3.2444 3.2337 1.7645  -0.3147 -0.2564 67   CYS E CA  
12000 C  C   . CYS E  67  ? 3.0654 3.2729 3.2821 1.7798  -0.2892 -0.3035 67   CYS E C   
12001 O  O   . CYS E  67  ? 3.2675 3.3891 3.4702 1.8243  -0.2836 -0.2995 67   CYS E O   
12002 C  CB  . CYS E  67  ? 3.2413 3.2702 3.3762 1.7120  -0.3096 -0.2303 67   CYS E CB  
12003 S  SG  . CYS E  67  ? 3.3833 3.4049 3.4863 1.6841  -0.3376 -0.1781 67   CYS E SG  
12004 N  N   . GLN E  68  ? 2.9840 3.2919 3.2366 1.7415  -0.2730 -0.3491 68   GLN E N   
12005 C  CA  . GLN E  68  ? 3.0799 3.4159 3.3598 1.7481  -0.2480 -0.3981 68   GLN E CA  
12006 C  C   . GLN E  68  ? 3.0501 3.3340 3.3204 1.6799  -0.2249 -0.4235 68   GLN E C   
12007 O  O   . GLN E  68  ? 3.0031 3.3498 3.2830 1.6323  -0.2274 -0.4275 68   GLN E O   
12008 C  CB  . GLN E  68  ? 2.9537 3.5054 3.2959 1.7747  -0.2508 -0.4341 68   GLN E CB  
12009 C  CG  . GLN E  68  ? 3.1463 3.7396 3.5031 1.8537  -0.2606 -0.4292 68   GLN E CG  
12010 C  CD  . GLN E  68  ? 3.2453 3.7155 3.5862 1.8849  -0.2412 -0.4434 68   GLN E CD  
12011 O  OE1 . GLN E  68  ? 3.1378 3.5576 3.4763 1.8482  -0.2164 -0.4754 68   GLN E OE1 
12012 N  NE2 . GLN E  68  ? 3.3207 3.7429 3.6502 1.9532  -0.2518 -0.4202 68   GLN E NE2 
12013 N  N   . PRO E  69  ? 2.9970 3.1660 3.2471 1.6728  -0.2020 -0.4409 69   PRO E N   
12014 C  CA  . PRO E  69  ? 2.9001 3.0269 3.1407 1.6085  -0.1791 -0.4660 69   PRO E CA  
12015 C  C   . PRO E  69  ? 2.8686 3.1673 3.1634 1.5849  -0.1667 -0.5150 69   PRO E C   
12016 O  O   . PRO E  69  ? 2.9962 3.4213 3.3344 1.6205  -0.1643 -0.5447 69   PRO E O   
12017 C  CB  . PRO E  69  ? 2.8978 2.8857 3.1100 1.6177  -0.1579 -0.4776 69   PRO E CB  
12018 C  CG  . PRO E  69  ? 2.9537 2.8579 3.1423 1.6760  -0.1731 -0.4424 69   PRO E CG  
12019 C  CD  . PRO E  69  ? 3.0885 3.1479 3.3179 1.7220  -0.1961 -0.4352 69   PRO E CD  
12020 N  N   . ILE E  70  ? 2.7316 3.0378 3.0229 1.5237  -0.1587 -0.5230 70   ILE E N   
12021 C  CA  . ILE E  70  ? 2.6987 3.1494 3.0354 1.4899  -0.1423 -0.5701 70   ILE E CA  
12022 C  C   . ILE E  70  ? 2.7523 3.1387 3.0786 1.4616  -0.1124 -0.6025 70   ILE E C   
12023 O  O   . ILE E  70  ? 2.5944 2.8462 2.8774 1.4239  -0.1034 -0.5887 70   ILE E O   
12024 C  CB  . ILE E  70  ? 2.4440 2.9436 2.7843 1.4402  -0.1484 -0.5634 70   ILE E CB  
12025 C  CG1 . ILE E  70  ? 2.4359 2.9993 2.7841 1.4663  -0.1782 -0.5316 70   ILE E CG1 
12026 C  CG2 . ILE E  70  ? 2.3822 3.0359 2.7705 1.4041  -0.1295 -0.6134 70   ILE E CG2 
12027 C  CD1 . ILE E  70  ? 2.4839 3.0944 2.8359 1.4209  -0.1847 -0.5258 70   ILE E CD1 
12028 N  N   . GLU E  71  ? 2.9674 3.4572 3.3327 1.4777  -0.0971 -0.6462 71   GLU E N   
12029 C  CA  . GLU E  71  ? 2.7939 3.2435 3.1539 1.4529  -0.0678 -0.6817 71   GLU E CA  
12030 C  C   . GLU E  71  ? 2.8598 3.3714 3.2310 1.3854  -0.0512 -0.7062 71   GLU E C   
12031 O  O   . GLU E  71  ? 3.0108 3.6838 3.4283 1.3701  -0.0421 -0.7429 71   GLU E O   
12032 C  CB  . GLU E  71  ? 2.5951 3.1412 2.9929 1.4941  -0.0575 -0.7204 71   GLU E CB  
12033 C  CG  . GLU E  71  ? 2.6194 3.1159 3.0082 1.4728  -0.0274 -0.7567 71   GLU E CG  
12034 C  CD  . GLU E  71  ? 3.0407 3.6408 3.4681 1.5134  -0.0169 -0.7975 71   GLU E CD  
12035 O  OE1 . GLU E  71  ? 3.2733 3.9928 3.7358 1.5569  -0.0332 -0.7984 71   GLU E OE1 
12036 O  OE2 . GLU E  71  ? 3.3673 3.9355 3.7894 1.5008  0.0079  -0.8300 71   GLU E OE2 
12037 N  N   . PHE E  72  ? 2.5617 2.9459 2.8885 1.3427  -0.0464 -0.6857 72   PHE E N   
12038 C  CA  . PHE E  72  ? 2.3897 2.8092 2.7190 1.2799  -0.0277 -0.7077 72   PHE E CA  
12039 C  C   . PHE E  72  ? 2.6311 3.0268 2.9543 1.2570  0.0015  -0.7436 72   PHE E C   
12040 O  O   . PHE E  72  ? 2.5506 3.0434 2.8952 1.2033  0.0207  -0.7703 72   PHE E O   
12041 C  CB  . PHE E  72  ? 2.3981 2.6953 2.6771 1.2265  -0.0359 -0.6593 72   PHE E CB  
12042 C  CG  . PHE E  72  ? 2.6533 3.0022 2.9403 1.2160  -0.0587 -0.6273 72   PHE E CG  
12043 C  CD1 . PHE E  72  ? 2.6634 3.1171 2.9701 1.1489  -0.0528 -0.6305 72   PHE E CD1 
12044 C  CD2 . PHE E  72  ? 2.8007 3.0897 3.0717 1.2705  -0.0852 -0.5939 72   PHE E CD2 
12045 C  CE1 . PHE E  72  ? 2.4892 2.9893 2.8010 1.1359  -0.0720 -0.6051 72   PHE E CE1 
12046 C  CE2 . PHE E  72  ? 2.7269 3.0697 3.0045 1.2581  -0.1057 -0.5662 72   PHE E CE2 
12047 C  CZ  . PHE E  72  ? 2.4836 2.9332 2.7823 1.1905  -0.0985 -0.5739 72   PHE E CZ  
12048 N  N   . ASP E  73  ? 3.0673 3.3305 3.3552 1.2772  0.0062  -0.7352 73   ASP E N   
12049 C  CA  . ASP E  73  ? 3.0863 3.3191 3.3641 1.2557  0.0342  -0.7699 73   ASP E CA  
12050 C  C   . ASP E  73  ? 2.9783 3.1028 3.2338 1.3012  0.0357  -0.7660 73   ASP E C   
12051 O  O   . ASP E  73  ? 3.2371 3.2212 3.4496 1.3132  0.0234  -0.7275 73   ASP E O   
12052 C  CB  . ASP E  73  ? 2.9306 3.0751 3.1663 1.1954  0.0467  -0.7628 73   ASP E CB  
12053 C  CG  . ASP E  73  ? 2.8066 2.9063 3.0239 1.1729  0.0746  -0.7955 73   ASP E CG  
12054 O  OD1 . ASP E  73  ? 2.6526 2.8555 2.9057 1.1793  0.0911  -0.8378 73   ASP E OD1 
12055 O  OD2 . ASP E  73  ? 2.8492 2.8161 3.0152 1.1469  0.0802  -0.7800 73   ASP E OD2 
12056 N  N   . ALA E  74  ? 2.7602 2.9498 3.0436 1.3249  0.0516  -0.8064 74   ALA E N   
12057 C  CA  . ALA E  74  ? 2.9348 3.0247 3.1994 1.3697  0.0573  -0.8097 74   ALA E CA  
12058 C  C   . ALA E  74  ? 3.2036 3.2094 3.4375 1.3371  0.0865  -0.8384 74   ALA E C   
12059 O  O   . ALA E  74  ? 3.4140 3.3103 3.6225 1.3659  0.0947  -0.8414 74   ALA E O   
12060 C  CB  . ALA E  74  ? 3.0152 3.2266 3.3291 1.4276  0.0547  -0.8355 74   ALA E CB  
12061 N  N   . THR E  75  ? 3.3182 3.3737 3.5526 1.2776  0.1032  -0.8606 75   THR E N   
12062 C  CA  . THR E  75  ? 3.4229 3.4269 3.6319 1.2426  0.1321  -0.8933 75   THR E CA  
12063 C  C   . THR E  75  ? 3.3237 3.1540 3.4676 1.2117  0.1335  -0.8655 75   THR E C   
12064 O  O   . THR E  75  ? 3.1718 2.9379 3.2917 1.2041  0.1132  -0.8213 75   THR E O   
12065 C  CB  . THR E  75  ? 3.3375 3.4768 3.5731 1.1892  0.1495  -0.9278 75   THR E CB  
12066 O  OG1 . THR E  75  ? 3.3101 3.4373 3.5279 1.1421  0.1417  -0.9010 75   THR E OG1 
12067 C  CG2 . THR E  75  ? 3.2973 3.6199 3.5965 1.2117  0.1464  -0.9527 75   THR E CG2 
12068 N  N   . GLY E  76  ? 3.2213 2.9806 3.3352 1.1921  0.1584  -0.8940 76   GLY E N   
12069 C  CA  . GLY E  76  ? 3.1771 2.7870 3.2276 1.1540  0.1647  -0.8781 76   GLY E CA  
12070 C  C   . GLY E  76  ? 3.1092 2.7581 3.1460 1.0873  0.1750  -0.8868 76   GLY E C   
12071 O  O   . GLY E  76  ? 2.9474 2.7133 3.0173 1.0691  0.1687  -0.8850 76   GLY E O   
12072 N  N   . ASN E  77  ? 3.1457 2.6960 3.1310 1.0492  0.1920  -0.8977 77   ASN E N   
12073 C  CA  . ASN E  77  ? 3.0774 2.6581 3.0433 0.9807  0.2030  -0.9021 77   ASN E CA  
12074 C  C   . ASN E  77  ? 3.0769 2.7881 3.0762 0.9527  0.2289  -0.9505 77   ASN E C   
12075 O  O   . ASN E  77  ? 3.2348 2.9285 3.2279 0.9664  0.2501  -0.9968 77   ASN E O   
12076 C  CB  . ASN E  77  ? 3.2459 2.6816 3.1422 0.9412  0.2107  -0.8888 77   ASN E CB  
12077 C  CG  . ASN E  77  ? 3.3844 2.7005 3.2435 0.9541  0.1856  -0.8360 77   ASN E CG  
12078 O  OD1 . ASN E  77  ? 3.4276 2.7500 3.3106 1.0056  0.1631  -0.8137 77   ASN E OD1 
12079 N  ND2 . ASN E  77  ? 3.4637 2.6790 3.2638 0.9028  0.1896  -0.8140 77   ASN E ND2 
12080 N  N   . ARG E  78  ? 2.9038 2.7425 2.9352 0.9068  0.2282  -0.9354 78   ARG E N   
12081 C  CA  . ARG E  78  ? 2.9502 2.9130 3.0059 0.8661  0.2527  -0.9734 78   ARG E CA  
12082 C  C   . ARG E  78  ? 2.9194 2.8299 2.9274 0.8037  0.2738  -0.9796 78   ARG E C   
12083 O  O   . ARG E  78  ? 2.8765 2.6923 2.8385 0.7680  0.2671  -0.9396 78   ARG E O   
12084 C  CB  . ARG E  78  ? 2.8611 2.9542 2.9513 0.8234  0.2468  -0.9481 78   ARG E CB  
12085 C  CG  . ARG E  78  ? 2.9476 3.1459 3.0949 0.8750  0.2346  -0.9617 78   ARG E CG  
12086 C  CD  . ARG E  78  ? 2.9454 3.2475 3.1157 0.8255  0.2272  -0.9304 78   ARG E CD  
12087 N  NE  . ARG E  78  ? 2.9496 3.1666 3.0889 0.8004  0.2079  -0.8702 78   ARG E NE  
12088 C  CZ  . ARG E  78  ? 2.7994 3.0718 2.9500 0.7641  0.1979  -0.8365 78   ARG E CZ  
12089 N  NH1 . ARG E  78  ? 2.7417 3.1528 2.9315 0.7438  0.2054  -0.8550 78   ARG E NH1 
12090 N  NH2 . ARG E  78  ? 2.7328 2.9215 2.8532 0.7460  0.1815  -0.7857 78   ARG E NH2 
12091 N  N   . ASP E  79  ? 2.9333 2.9149 2.9531 0.7904  0.2998  -1.0321 79   ASP E N   
12092 C  CA  . ASP E  79  ? 2.9668 2.9277 2.9464 0.7278  0.3225  -1.0451 79   ASP E CA  
12093 C  C   . ASP E  79  ? 3.0240 3.1114 3.0166 0.6552  0.3309  -1.0277 79   ASP E C   
12094 O  O   . ASP E  79  ? 3.1345 3.3529 3.1735 0.6569  0.3350  -1.0455 79   ASP E O   
12095 C  CB  . ASP E  79  ? 2.8915 2.8505 2.8708 0.7542  0.3479  -1.1160 79   ASP E CB  
12096 C  CG  . ASP E  79  ? 2.9685 2.7590 2.9047 0.7987  0.3471  -1.1291 79   ASP E CG  
12097 O  OD1 . ASP E  79  ? 3.0051 2.6818 2.8891 0.7663  0.3403  -1.0920 79   ASP E OD1 
12098 O  OD2 . ASP E  79  ? 3.1191 2.8883 3.0695 0.8557  0.3531  -1.1615 79   ASP E OD2 
12099 N  N   . TYR E  80  ? 2.8695 2.9188 2.8193 0.5918  0.3329  -0.9910 80   TYR E N   
12100 C  CA  . TYR E  80  ? 2.7468 2.9053 2.6987 0.5220  0.3459  -0.9797 80   TYR E CA  
12101 C  C   . TYR E  80  ? 2.9317 3.1547 2.8829 0.5002  0.3756  -1.0380 80   TYR E C   
12102 O  O   . TYR E  80  ? 3.0192 3.3735 2.9986 0.4721  0.3884  -1.0548 80   TYR E O   
12103 C  CB  . TYR E  80  ? 2.6183 2.7207 2.5247 0.4680  0.3384  -0.9219 80   TYR E CB  
12104 C  CG  . TYR E  80  ? 2.6031 2.8011 2.5005 0.3967  0.3527  -0.9065 80   TYR E CG  
12105 C  CD1 . TYR E  80  ? 2.5747 2.8515 2.4924 0.3709  0.3452  -0.8689 80   TYR E CD1 
12106 C  CD2 . TYR E  80  ? 2.7718 2.9788 2.6367 0.3539  0.3740  -0.9287 80   TYR E CD2 
12107 C  CE1 . TYR E  80  ? 2.5682 2.9245 2.4730 0.3081  0.3578  -0.8503 80   TYR E CE1 
12108 C  CE2 . TYR E  80  ? 2.7665 3.0651 2.6215 0.2908  0.3860  -0.9111 80   TYR E CE2 
12109 C  CZ  . TYR E  80  ? 2.5852 2.9552 2.4596 0.2699  0.3774  -0.8701 80   TYR E CZ  
12110 O  OH  . TYR E  80  ? 2.5745 3.0281 2.4344 0.2093  0.3890  -0.8485 80   TYR E OH  
12111 N  N   . ALA E  81  ? 2.9437 3.0752 2.8603 0.5102  0.3876  -1.0707 81   ALA E N   
12112 C  CA  . ALA E  81  ? 2.8047 2.9846 2.7186 0.4964  0.4169  -1.1343 81   ALA E CA  
12113 C  C   . ALA E  81  ? 2.8628 2.9141 2.7530 0.5481  0.4231  -1.1771 81   ALA E C   
12114 O  O   . ALA E  81  ? 2.8254 2.7564 2.7011 0.5917  0.4039  -1.1529 81   ALA E O   
12115 C  CB  . ALA E  81  ? 2.7639 2.9848 2.6412 0.4131  0.4329  -1.1217 81   ALA E CB  
12116 N  N   . LYS E  82  ? 2.9320 3.0072 2.8159 0.5430  0.4509  -1.2417 82   LYS E N   
12117 C  CA  . LYS E  82  ? 2.9385 2.8845 2.7940 0.5888  0.4614  -1.2886 82   LYS E CA  
12118 C  C   . LYS E  82  ? 2.9472 2.7412 2.7358 0.5582  0.4556  -1.2551 82   LYS E C   
12119 O  O   . LYS E  82  ? 2.9287 2.7417 2.6828 0.4836  0.4634  -1.2352 82   LYS E O   
12120 C  CB  . LYS E  82  ? 2.7776 2.7807 2.6314 0.5715  0.4925  -1.3523 82   LYS E CB  
12121 C  CG  . LYS E  82  ? 2.9050 2.7631 2.7207 0.6100  0.5016  -1.3798 82   LYS E CG  
12122 C  CD  . LYS E  82  ? 2.9649 2.8764 2.7717 0.5815  0.5308  -1.4329 82   LYS E CD  
12123 C  CE  . LYS E  82  ? 3.1217 2.8720 2.8800 0.6173  0.5423  -1.4608 82   LYS E CE  
12124 N  NZ  . LYS E  82  ? 3.1877 2.9801 2.9304 0.5855  0.5710  -1.5145 82   LYS E NZ  
12125 N  N   . ASP E  83  ? 3.1327 2.7811 2.9023 0.6160  0.4412  -1.2469 83   ASP E N   
12126 C  CA  . ASP E  83  ? 3.1899 2.6853 2.8950 0.5925  0.4331  -1.2130 83   ASP E CA  
12127 C  C   . ASP E  83  ? 3.2362 2.7588 2.9334 0.5425  0.4117  -1.1378 83   ASP E C   
12128 O  O   . ASP E  83  ? 3.3016 2.7493 2.9451 0.4943  0.4107  -1.1107 83   ASP E O   
12129 C  CB  . ASP E  83  ? 3.2696 2.7056 2.9174 0.5421  0.4621  -1.2571 83   ASP E CB  
12130 C  CG  . ASP E  83  ? 3.4638 2.8533 3.1099 0.5898  0.4839  -1.3263 83   ASP E CG  
12131 O  OD1 . ASP E  83  ? 3.5627 2.8033 3.1801 0.6421  0.4768  -1.3195 83   ASP E OD1 
12132 O  OD2 . ASP E  83  ? 3.5287 3.0264 3.1935 0.5679  0.5049  -1.3639 83   ASP E OD2 
12133 N  N   . ASP E  84  ? 3.1300 2.7612 2.8789 0.5528  0.3953  -1.1053 84   ASP E N   
12134 C  CA  . ASP E  84  ? 3.1964 2.8610 2.9420 0.5101  0.3763  -1.0365 84   ASP E CA  
12135 C  C   . ASP E  84  ? 3.3720 3.0481 3.1595 0.5628  0.3489  -1.0011 84   ASP E C   
12136 O  O   . ASP E  84  ? 3.4657 3.2627 3.3023 0.5662  0.3459  -0.9980 84   ASP E O   
12137 C  CB  . ASP E  84  ? 3.0145 2.8219 2.7729 0.4446  0.3901  -1.0323 84   ASP E CB  
12138 C  CG  . ASP E  84  ? 2.9881 2.8027 2.7215 0.3906  0.3771  -0.9663 84   ASP E CG  
12139 O  OD1 . ASP E  84  ? 3.1589 2.8658 2.8506 0.3850  0.3657  -0.9362 84   ASP E OD1 
12140 O  OD2 . ASP E  84  ? 2.8563 2.7850 2.6099 0.3538  0.3788  -0.9446 84   ASP E OD2 
12141 N  N   . PRO E  85  ? 3.3561 2.9092 3.1236 0.6035  0.3290  -0.9756 85   PRO E N   
12142 C  CA  . PRO E  85  ? 3.1807 2.7456 2.9866 0.6552  0.3025  -0.9437 85   PRO E CA  
12143 C  C   . PRO E  85  ? 2.9814 2.6232 2.8022 0.6137  0.2881  -0.8888 85   PRO E C   
12144 O  O   . PRO E  85  ? 2.9718 2.5877 2.7559 0.5607  0.2864  -0.8522 85   PRO E O   
12145 C  CB  . PRO E  85  ? 3.0701 2.4751 2.8359 0.6927  0.2864  -0.9237 85   PRO E CB  
12146 C  CG  . PRO E  85  ? 3.1905 2.5013 2.9069 0.6796  0.3091  -0.9654 85   PRO E CG  
12147 C  CD  . PRO E  85  ? 3.2617 2.6595 2.9684 0.6036  0.3311  -0.9782 85   PRO E CD  
12148 N  N   . LEU E  86  ? 3.0861 2.8230 2.9600 0.6395  0.2779  -0.8839 86   LEU E N   
12149 C  CA  . LEU E  86  ? 3.0816 2.8904 2.9704 0.6019  0.2664  -0.8366 86   LEU E CA  
12150 C  C   . LEU E  86  ? 3.0793 2.8125 2.9555 0.6187  0.2389  -0.7836 86   LEU E C   
12151 O  O   . LEU E  86  ? 2.9764 2.7180 2.8383 0.5766  0.2315  -0.7385 86   LEU E O   
12152 C  CB  . LEU E  86  ? 3.0393 2.9840 2.9859 0.6134  0.2689  -0.8557 86   LEU E CB  
12153 C  CG  . LEU E  86  ? 2.9544 2.9643 2.9157 0.5784  0.2572  -0.8092 86   LEU E CG  
12154 C  CD1 . LEU E  86  ? 3.0237 3.0833 2.9635 0.5059  0.2730  -0.7934 86   LEU E CD1 
12155 C  CD2 . LEU E  86  ? 2.9503 3.0684 2.9670 0.6048  0.2530  -0.8263 86   LEU E CD2 
12156 N  N   . GLU E  87  ? 3.0961 2.7579 2.9768 0.6809  0.2238  -0.7874 87   GLU E N   
12157 C  CA  . GLU E  87  ? 2.9178 2.5222 2.7915 0.7002  0.1969  -0.7395 87   GLU E CA  
12158 C  C   . GLU E  87  ? 2.9325 2.3992 2.7707 0.7431  0.1876  -0.7394 87   GLU E C   
12159 O  O   . GLU E  87  ? 3.1527 2.5707 2.9789 0.7688  0.2012  -0.7802 87   GLU E O   
12160 C  CB  . GLU E  87  ? 2.8730 2.5661 2.8007 0.7349  0.1822  -0.7353 87   GLU E CB  
12161 C  CG  . GLU E  87  ? 3.0609 2.7982 3.0277 0.7962  0.1870  -0.7844 87   GLU E CG  
12162 C  CD  . GLU E  87  ? 3.1498 3.0140 3.1734 0.8138  0.1785  -0.7877 87   GLU E CD  
12163 O  OE1 . GLU E  87  ? 3.1580 3.0638 3.1872 0.7764  0.1694  -0.7517 87   GLU E OE1 
12164 O  OE2 . GLU E  87  ? 3.2074 3.1317 3.2688 0.8644  0.1820  -0.8281 87   GLU E OE2 
12165 N  N   . PHE E  88  ? 2.8167 2.2175 2.6354 0.7503  0.1647  -0.6930 88   PHE E N   
12166 C  CA  . PHE E  88  ? 2.9107 2.1747 2.6896 0.7863  0.1530  -0.6828 88   PHE E CA  
12167 C  C   . PHE E  88  ? 2.9366 2.1985 2.7365 0.8318  0.1244  -0.6493 88   PHE E C   
12168 O  O   . PHE E  88  ? 2.7547 2.0107 2.5428 0.8057  0.1090  -0.6046 88   PHE E O   
12169 C  CB  . PHE E  88  ? 3.1608 2.3334 2.8768 0.7327  0.1562  -0.6572 88   PHE E CB  
12170 C  CG  . PHE E  88  ? 3.2857 2.4796 2.9809 0.6785  0.1834  -0.6855 88   PHE E CG  
12171 C  CD1 . PHE E  88  ? 3.2896 2.4080 2.9535 0.6845  0.2015  -0.7265 88   PHE E CD1 
12172 C  CD2 . PHE E  88  ? 3.1846 2.4724 2.8890 0.6215  0.1912  -0.6710 88   PHE E CD2 
12173 C  CE1 . PHE E  88  ? 3.2284 2.3737 2.8721 0.6314  0.2271  -0.7546 88   PHE E CE1 
12174 C  CE2 . PHE E  88  ? 3.0656 2.3818 2.7501 0.5715  0.2153  -0.6949 88   PHE E CE2 
12175 C  CZ  . PHE E  88  ? 3.1610 2.4106 2.8161 0.5748  0.2333  -0.7379 88   PHE E CZ  
12176 N  N   . LYS E  89  ? 3.1657 2.4370 2.9964 0.9012  0.1177  -0.6720 89   LYS E N   
12177 C  CA  . LYS E  89  ? 3.2227 2.5079 3.0776 0.9500  0.0908  -0.6447 89   LYS E CA  
12178 C  C   . LYS E  89  ? 3.2283 2.3719 3.0378 0.9876  0.0741  -0.6196 89   LYS E C   
12179 O  O   . LYS E  89  ? 3.3426 2.4862 3.1630 1.0244  0.0497  -0.5898 89   LYS E O   
12180 C  CB  . LYS E  89  ? 3.2272 2.6171 3.1427 1.0081  0.0909  -0.6805 89   LYS E CB  
12181 C  CG  . LYS E  89  ? 3.1209 2.6662 3.0854 0.9713  0.1020  -0.6975 89   LYS E CG  
12182 C  CD  . LYS E  89  ? 3.1108 2.7622 3.1317 1.0273  0.1051  -0.7397 89   LYS E CD  
12183 C  CE  . LYS E  89  ? 2.9895 2.7936 3.0534 0.9831  0.1185  -0.7584 89   LYS E CE  
12184 N  NZ  . LYS E  89  ? 3.0310 2.9503 3.1493 1.0339  0.1235  -0.8039 89   LYS E NZ  
12185 N  N   . SER E  90  ? 3.0304 2.0548 2.7871 0.9773  0.0872  -0.6315 90   SER E N   
12186 C  CA  . SER E  90  ? 2.9551 1.8410 2.6626 0.9926  0.0738  -0.5993 90   SER E CA  
12187 C  C   . SER E  90  ? 3.0440 1.9002 2.7186 0.9542  0.0560  -0.5496 90   SER E C   
12188 O  O   . SER E  90  ? 3.0174 1.9114 2.6825 0.8873  0.0655  -0.5407 90   SER E O   
12189 C  CB  . SER E  90  ? 3.0581 1.8286 2.7141 0.9724  0.0958  -0.6241 90   SER E CB  
12190 O  OG  . SER E  90  ? 3.0806 1.8736 2.7701 1.0077  0.1121  -0.6639 90   SER E OG  
12191 N  N   . HIS E  91  ? 3.2006 2.0093 2.8659 0.9854  0.0312  -0.5101 91   HIS E N   
12192 C  CA  . HIS E  91  ? 3.2689 2.0498 2.9032 0.9539  0.0127  -0.4618 91   HIS E CA  
12193 C  C   . HIS E  91  ? 3.0883 2.0021 2.7655 0.9150  0.0103  -0.4500 91   HIS E C   
12194 O  O   . HIS E  91  ? 2.8961 1.8072 2.5492 0.8620  0.0076  -0.4205 91   HIS E O   
12195 C  CB  . HIS E  91  ? 3.4483 2.1180 3.0114 0.8972  0.0227  -0.4495 91   HIS E CB  
12196 C  CG  . HIS E  91  ? 3.5818 2.1139 3.0970 0.9202  0.0303  -0.4637 91   HIS E CG  
12197 N  ND1 . HIS E  91  ? 3.5452 2.0114 3.0511 0.9518  0.0129  -0.4319 91   HIS E ND1 
12198 C  CD2 . HIS E  91  ? 3.6254 2.0930 3.1086 0.8997  0.0556  -0.5007 91   HIS E CD2 
12199 C  CE1 . HIS E  91  ? 3.4974 1.8582 2.9675 0.9513  0.0272  -0.4479 91   HIS E CE1 
12200 N  NE2 . HIS E  91  ? 3.5588 1.9184 3.0152 0.9188  0.0536  -0.4911 91   HIS E NE2 
12201 N  N   . GLN E  92  ? 3.0399 2.0701 2.7789 0.9416  0.0117  -0.4730 92   GLN E N   
12202 C  CA  . GLN E  92  ? 2.9395 2.0893 2.7166 0.9040  0.0119  -0.4652 92   GLN E CA  
12203 C  C   . GLN E  92  ? 2.8644 2.0462 2.6556 0.9173  -0.0138 -0.4285 92   GLN E C   
12204 O  O   . GLN E  92  ? 2.7750 2.0389 2.5893 0.8828  -0.0144 -0.4179 92   GLN E O   
12205 C  CB  . GLN E  92  ? 2.9135 2.1795 2.7472 0.9174  0.0263  -0.5073 92   GLN E CB  
12206 C  CG  . GLN E  92  ? 2.9475 2.2713 2.8265 0.9868  0.0122  -0.5202 92   GLN E CG  
12207 C  CD  . GLN E  92  ? 3.0775 2.5203 3.0095 0.9970  0.0287  -0.5661 92   GLN E CD  
12208 O  OE1 . GLN E  92  ? 3.1171 2.6147 3.0565 0.9452  0.0482  -0.5815 92   GLN E OE1 
12209 N  NE2 . GLN E  92  ? 3.1446 2.6336 3.1130 1.0643  0.0207  -0.5869 92   GLN E NE2 
12210 N  N   . TRP E  93  ? 2.8944 2.0134 2.6708 0.9665  -0.0342 -0.4095 93   TRP E N   
12211 C  CA  . TRP E  93  ? 2.9368 2.0827 2.7213 0.9788  -0.0597 -0.3735 93   TRP E CA  
12212 C  C   . TRP E  93  ? 2.8852 2.1722 2.7334 0.9930  -0.0641 -0.3875 93   TRP E C   
12213 O  O   . TRP E  93  ? 2.8498 2.1937 2.7100 0.9661  -0.0735 -0.3671 93   TRP E O   
12214 C  CB  . TRP E  93  ? 2.8679 1.9808 2.6151 0.9201  -0.0635 -0.3376 93   TRP E CB  
12215 C  CG  . TRP E  93  ? 2.8516 1.8329 2.5347 0.9161  -0.0709 -0.3110 93   TRP E CG  
12216 C  CD1 . TRP E  93  ? 2.7765 1.6586 2.4154 0.9048  -0.0561 -0.3231 93   TRP E CD1 
12217 C  CD2 . TRP E  93  ? 2.9837 1.9202 2.6365 0.9179  -0.0937 -0.2686 93   TRP E CD2 
12218 N  NE1 . TRP E  93  ? 2.8359 1.6109 2.4169 0.8977  -0.0684 -0.2898 93   TRP E NE1 
12219 C  CE2 . TRP E  93  ? 3.0071 1.8155 2.5961 0.9062  -0.0919 -0.2551 93   TRP E CE2 
12220 C  CE3 . TRP E  93  ? 2.6721 1.6666 2.3433 0.9251  -0.1148 -0.2420 93   TRP E CE3 
12221 C  CZ2 . TRP E  93  ? 3.1978 1.9371 2.7414 0.9012  -0.1110 -0.2140 93   TRP E CZ2 
12222 C  CZ3 . TRP E  93  ? 2.6958 1.6248 2.3241 0.9227  -0.1339 -0.2026 93   TRP E CZ3 
12223 C  CH2 . TRP E  93  ? 2.8743 1.6778 2.4395 0.9108  -0.1322 -0.1879 93   TRP E CH2 
12224 N  N   . PHE E  94  ? 2.8698 2.2153 2.7573 1.0340  -0.0563 -0.4249 94   PHE E N   
12225 C  CA  . PHE E  94  ? 2.6726 2.1581 2.6197 1.0500  -0.0608 -0.4410 94   PHE E CA  
12226 C  C   . PHE E  94  ? 2.7681 2.2707 2.7242 1.0953  -0.0894 -0.4142 94   PHE E C   
12227 O  O   . PHE E  94  ? 2.7092 2.1460 2.6495 1.1537  -0.1027 -0.4054 94   PHE E O   
12228 C  CB  . PHE E  94  ? 2.6478 2.1959 2.6332 1.0867  -0.0458 -0.4887 94   PHE E CB  
12229 C  CG  . PHE E  94  ? 2.5487 2.2497 2.5953 1.1056  -0.0505 -0.5081 94   PHE E CG  
12230 C  CD1 . PHE E  94  ? 2.5291 2.3302 2.6011 1.0479  -0.0397 -0.5162 94   PHE E CD1 
12231 C  CD2 . PHE E  94  ? 2.6417 2.3873 2.7178 1.1807  -0.0653 -0.5182 94   PHE E CD2 
12232 C  CE1 . PHE E  94  ? 2.5056 2.4487 2.6298 1.0577  -0.0426 -0.5358 94   PHE E CE1 
12233 C  CE2 . PHE E  94  ? 2.6609 2.5601 2.7932 1.1947  -0.0693 -0.5379 94   PHE E CE2 
12234 C  CZ  . PHE E  94  ? 2.5674 2.5656 2.7229 1.1297  -0.0574 -0.5477 94   PHE E CZ  
12235 N  N   . GLY E  95  ? 2.7921 2.3815 2.7711 1.0680  -0.0984 -0.4011 95   GLY E N   
12236 C  CA  . GLY E  95  ? 2.7254 2.3362 2.7082 1.0981  -0.1254 -0.3727 95   GLY E CA  
12237 C  C   . GLY E  95  ? 2.4754 2.0120 2.4136 1.0618  -0.1372 -0.3304 95   GLY E C   
12238 O  O   . GLY E  95  ? 2.4506 1.9814 2.3807 1.0894  -0.1607 -0.3025 95   GLY E O   
12239 N  N   . ALA E  96  ? 2.4818 1.9666 2.3903 1.0025  -0.1217 -0.3245 96   ALA E N   
12240 C  CA  . ALA E  96  ? 2.7002 2.1296 2.5691 0.9662  -0.1316 -0.2870 96   ALA E CA  
12241 C  C   . ALA E  96  ? 2.7811 2.3029 2.6751 0.9404  -0.1393 -0.2795 96   ALA E C   
12242 O  O   . ALA E  96  ? 3.0453 2.5437 2.9159 0.9294  -0.1547 -0.2490 96   ALA E O   
12243 C  CB  . ALA E  96  ? 2.7434 2.1030 2.5751 0.9135  -0.1125 -0.2844 96   ALA E CB  
12244 N  N   . SER E  97  ? 2.4606 2.0864 2.3991 0.9273  -0.1278 -0.3082 97   SER E N   
12245 C  CA  . SER E  97  ? 2.3038 2.0197 2.2664 0.9025  -0.1332 -0.3070 97   SER E CA  
12246 C  C   . SER E  97  ? 2.2730 2.1093 2.2891 0.9259  -0.1316 -0.3395 97   SER E C   
12247 O  O   . SER E  97  ? 2.2581 2.1301 2.2954 0.9181  -0.1125 -0.3693 97   SER E O   
12248 C  CB  . SER E  97  ? 2.2120 1.9232 2.1621 0.8373  -0.1150 -0.3060 97   SER E CB  
12249 O  OG  . SER E  97  ? 2.2305 1.9754 2.1999 0.8187  -0.0921 -0.3351 97   SER E OG  
12250 N  N   . VAL E  98  ? 2.1698 2.0783 2.2075 0.9515  -0.1512 -0.3345 98   VAL E N   
12251 C  CA  . VAL E  98  ? 2.1728 2.2126 2.2620 0.9746  -0.1522 -0.3645 98   VAL E CA  
12252 C  C   . VAL E  98  ? 2.1898 2.3207 2.2952 0.9338  -0.1554 -0.3665 98   VAL E C   
12253 O  O   . VAL E  98  ? 2.4147 2.5287 2.5014 0.9298  -0.1722 -0.3405 98   VAL E O   
12254 C  CB  . VAL E  98  ? 2.1694 2.2278 2.2729 1.0533  -0.1735 -0.3603 98   VAL E CB  
12255 C  CG1 . VAL E  98  ? 2.1643 2.3713 2.3241 1.0787  -0.1720 -0.3957 98   VAL E CG1 
12256 C  CG2 . VAL E  98  ? 2.3138 2.2548 2.3898 1.0926  -0.1706 -0.3551 98   VAL E CG2 
12257 N  N   . ARG E  99  ? 2.1675 2.3947 2.3049 0.9008  -0.1386 -0.3986 99   ARG E N   
12258 C  CA  . ARG E  99  ? 2.1960 2.5103 2.3470 0.8550  -0.1374 -0.4069 99   ARG E CA  
12259 C  C   . ARG E  99  ? 2.2084 2.6686 2.4087 0.8609  -0.1320 -0.4443 99   ARG E C   
12260 O  O   . ARG E  99  ? 2.2116 2.6952 2.4296 0.8631  -0.1155 -0.4690 99   ARG E O   
12261 C  CB  . ARG E  99  ? 2.3821 2.6422 2.5063 0.7837  -0.1165 -0.4040 99   ARG E CB  
12262 C  CG  . ARG E  99  ? 2.4810 2.6310 2.5600 0.7698  -0.1240 -0.3685 99   ARG E CG  
12263 C  CD  . ARG E  99  ? 2.4377 2.6194 2.5146 0.7823  -0.1471 -0.3526 99   ARG E CD  
12264 N  NE  . ARG E  99  ? 2.5223 2.6542 2.5861 0.8394  -0.1699 -0.3267 99   ARG E NE  
12265 C  CZ  . ARG E  99  ? 2.4483 2.4744 2.4703 0.8400  -0.1774 -0.2948 99   ARG E CZ  
12266 N  NH1 . ARG E  99  ? 2.4859 2.4519 2.4791 0.7914  -0.1644 -0.2860 99   ARG E NH1 
12267 N  NH2 . ARG E  99  ? 2.3355 2.3164 2.3427 0.8896  -0.1978 -0.2710 99   ARG E NH2 
12268 N  N   . SER E  100 ? 2.2741 2.8399 2.4961 0.8613  -0.1456 -0.4498 100  SER E N   
12269 C  CA  . SER E  100 ? 2.3434 3.0667 2.6135 0.8709  -0.1442 -0.4844 100  SER E CA  
12270 C  C   . SER E  100 ? 2.5368 3.3507 2.8137 0.8043  -0.1374 -0.5002 100  SER E C   
12271 O  O   . SER E  100 ? 2.5844 3.3701 2.8385 0.7807  -0.1467 -0.4814 100  SER E O   
12272 C  CB  . SER E  100 ? 2.1301 2.9181 2.4253 0.9518  -0.1707 -0.4783 100  SER E CB  
12273 O  OG  . SER E  100 ? 2.1188 3.0642 2.4632 0.9704  -0.1684 -0.5139 100  SER E OG  
12274 N  N   . LYS E  101 ? 2.6877 3.6100 2.9936 0.7714  -0.1198 -0.5365 101  LYS E N   
12275 C  CA  . LYS E  101 ? 2.6413 3.6592 2.9535 0.7033  -0.1103 -0.5577 101  LYS E CA  
12276 C  C   . LYS E  101 ? 2.5267 3.7248 2.8889 0.7157  -0.1098 -0.5950 101  LYS E C   
12277 O  O   . LYS E  101 ? 2.3807 3.6192 2.7605 0.7052  -0.0916 -0.6200 101  LYS E O   
12278 C  CB  . LYS E  101 ? 2.6456 3.5897 2.9274 0.6247  -0.0820 -0.5623 101  LYS E CB  
12279 C  CG  . LYS E  101 ? 2.6778 3.7015 2.9580 0.5478  -0.0686 -0.5853 101  LYS E CG  
12280 C  CD  . LYS E  101 ? 2.6942 3.6338 2.9411 0.4766  -0.0398 -0.5868 101  LYS E CD  
12281 C  CE  . LYS E  101 ? 2.7749 3.7722 3.0110 0.3963  -0.0249 -0.6084 101  LYS E CE  
12282 N  NZ  . LYS E  101 ? 2.8736 4.0479 3.1505 0.3818  -0.0216 -0.6470 101  LYS E NZ  
12283 N  N   . GLN E  102 ? 2.5198 3.8348 2.9046 0.7360  -0.1295 -0.5992 102  GLN E N   
12284 C  CA  . GLN E  102 ? 2.5597 4.0677 2.9944 0.7526  -0.1325 -0.6337 102  GLN E CA  
12285 C  C   . GLN E  102 ? 2.6497 4.1748 3.1142 0.8361  -0.1380 -0.6389 102  GLN E C   
12286 O  O   . GLN E  102 ? 2.7339 4.1872 3.1925 0.9110  -0.1589 -0.6105 102  GLN E O   
12287 C  CB  . GLN E  102 ? 2.5969 4.1878 3.0356 0.6625  -0.1053 -0.6699 102  GLN E CB  
12288 C  CG  . GLN E  102 ? 2.6536 4.2113 3.0573 0.5767  -0.0956 -0.6683 102  GLN E CG  
12289 C  CD  . GLN E  102 ? 2.6885 4.2694 3.0825 0.4884  -0.0639 -0.6971 102  GLN E CD  
12290 O  OE1 . GLN E  102 ? 2.5923 4.2359 3.0101 0.4906  -0.0507 -0.7196 102  GLN E OE1 
12291 N  NE2 . GLN E  102 ? 2.7649 4.2962 3.1220 0.4100  -0.0510 -0.6971 102  GLN E NE2 
12292 N  N   . ASP E  103 ? 2.5808 4.1927 3.0738 0.8257  -0.1194 -0.6745 103  ASP E N   
12293 C  CA  . ASP E  103 ? 2.4494 4.0833 2.9715 0.9020  -0.1207 -0.6868 103  ASP E CA  
12294 C  C   . ASP E  103 ? 2.3538 3.8305 2.8475 0.8964  -0.1029 -0.6788 103  ASP E C   
12295 O  O   . ASP E  103 ? 2.2994 3.7955 2.8144 0.9387  -0.0949 -0.6989 103  ASP E O   
12296 C  CB  . ASP E  103 ? 2.3416 4.1767 2.9133 0.8952  -0.1102 -0.7339 103  ASP E CB  
12297 C  CG  . ASP E  103 ? 2.3315 4.1842 2.8937 0.7992  -0.0784 -0.7602 103  ASP E CG  
12298 O  OD1 . ASP E  103 ? 2.4453 4.1984 2.9659 0.7249  -0.0678 -0.7438 103  ASP E OD1 
12299 O  OD2 . ASP E  103 ? 2.2208 4.1874 2.8155 0.7987  -0.0638 -0.7966 103  ASP E OD2 
12300 N  N   . LYS E  104 ? 2.3622 3.6912 2.8086 0.8450  -0.0957 -0.6517 104  LYS E N   
12301 C  CA  . LYS E  104 ? 2.3911 3.5723 2.8061 0.8331  -0.0794 -0.6405 104  LYS E CA  
12302 C  C   . LYS E  104 ? 2.3421 3.3715 2.7254 0.8853  -0.0975 -0.6005 104  LYS E C   
12303 O  O   . LYS E  104 ? 2.3181 3.3080 2.6811 0.8824  -0.1143 -0.5728 104  LYS E O   
12304 C  CB  . LYS E  104 ? 2.4412 3.5680 2.8232 0.7372  -0.0572 -0.6375 104  LYS E CB  
12305 C  CG  . LYS E  104 ? 2.5313 3.7994 2.9353 0.6728  -0.0390 -0.6735 104  LYS E CG  
12306 C  CD  . LYS E  104 ? 2.5981 3.7942 2.9615 0.5807  -0.0190 -0.6647 104  LYS E CD  
12307 C  CE  . LYS E  104 ? 2.6823 4.0098 3.0606 0.5103  0.0003  -0.6994 104  LYS E CE  
12308 N  NZ  . LYS E  104 ? 2.7708 4.1722 3.1752 0.5144  0.0168  -0.7283 104  LYS E NZ  
12309 N  N   . ILE E  105 ? 2.3831 3.3291 2.7596 0.9290  -0.0931 -0.5991 105  ILE E N   
12310 C  CA  . ILE E  105 ? 2.3831 3.1744 2.7232 0.9706  -0.1065 -0.5631 105  ILE E CA  
12311 C  C   . ILE E  105 ? 2.4684 3.1379 2.7759 0.9366  -0.0851 -0.5596 105  ILE E C   
12312 O  O   . ILE E  105 ? 2.3856 3.0785 2.7085 0.9426  -0.0679 -0.5873 105  ILE E O   
12313 C  CB  . ILE E  105 ? 2.4085 3.2071 2.7667 1.0675  -0.1248 -0.5628 105  ILE E CB  
12314 C  CG1 . ILE E  105 ? 2.5329 3.4657 2.9243 1.1041  -0.1476 -0.5637 105  ILE E CG1 
12315 C  CG2 . ILE E  105 ? 2.3624 2.9889 2.6748 1.1006  -0.1362 -0.5249 105  ILE E CG2 
12316 C  CD1 . ILE E  105 ? 2.7356 3.6783 3.1436 1.2058  -0.1673 -0.5593 105  ILE E CD1 
12317 N  N   . LEU E  106 ? 2.5372 3.0858 2.8003 0.9010  -0.0859 -0.5266 106  LEU E N   
12318 C  CA  . LEU E  106 ? 2.4818 2.9170 2.7102 0.8666  -0.0675 -0.5181 106  LEU E CA  
12319 C  C   . LEU E  106 ? 2.6173 2.9138 2.8087 0.9057  -0.0803 -0.4870 106  LEU E C   
12320 O  O   . LEU E  106 ? 2.5593 2.8047 2.7276 0.9094  -0.0980 -0.4558 106  LEU E O   
12321 C  CB  . LEU E  106 ? 2.3278 2.7414 2.5325 0.7879  -0.0547 -0.5066 106  LEU E CB  
12322 C  CG  . LEU E  106 ? 2.3200 2.6236 2.4869 0.7513  -0.0370 -0.4929 106  LEU E CG  
12323 C  CD1 . LEU E  106 ? 2.2981 2.6410 2.4813 0.7419  -0.0149 -0.5231 106  LEU E CD1 
12324 C  CD2 . LEU E  106 ? 2.3485 2.6192 2.4880 0.6862  -0.0289 -0.4747 106  LEU E CD2 
12325 N  N   . ALA E  107 ? 2.6039 2.8418 2.7874 0.9315  -0.0704 -0.4973 107  ALA E N   
12326 C  CA  . ALA E  107 ? 2.4735 2.5723 2.6159 0.9592  -0.0780 -0.4716 107  ALA E CA  
12327 C  C   . ALA E  107 ? 2.4397 2.4625 2.5542 0.9193  -0.0551 -0.4756 107  ALA E C   
12328 O  O   . ALA E  107 ? 2.4412 2.5218 2.5753 0.8959  -0.0345 -0.5052 107  ALA E O   
12329 C  CB  . ALA E  107 ? 2.4403 2.5285 2.5943 1.0404  -0.0905 -0.4799 107  ALA E CB  
12330 N  N   . CYS E  108 ? 2.5041 2.4036 2.5714 0.9099  -0.0590 -0.4454 108  CYS E N   
12331 C  CA  . CYS E  108 ? 2.6861 2.5183 2.7226 0.8659  -0.0390 -0.4438 108  CYS E CA  
12332 C  C   . CYS E  108 ? 2.6636 2.3721 2.6589 0.8904  -0.0422 -0.4307 108  CYS E C   
12333 O  O   . CYS E  108 ? 2.4927 2.1460 2.4722 0.9307  -0.0620 -0.4108 108  CYS E O   
12334 C  CB  . CYS E  108 ? 2.7233 2.5423 2.7383 0.8052  -0.0353 -0.4188 108  CYS E CB  
12335 S  SG  . CYS E  108 ? 2.8737 2.8175 2.9254 0.7621  -0.0256 -0.4355 108  CYS E SG  
12336 N  N   . ALA E  109 ? 2.7471 2.4129 2.7217 0.8611  -0.0218 -0.4414 109  ALA E N   
12337 C  CA  . ALA E  109 ? 2.7260 2.2759 2.6568 0.8699  -0.0189 -0.4349 109  ALA E CA  
12338 C  C   . ALA E  109 ? 2.8260 2.3265 2.7177 0.8093  -0.0086 -0.4130 109  ALA E C   
12339 O  O   . ALA E  109 ? 2.9100 2.4288 2.7997 0.7742  0.0127  -0.4295 109  ALA E O   
12340 C  CB  . ALA E  109 ? 2.6843 2.2371 2.6270 0.8957  -0.0022 -0.4754 109  ALA E CB  
12341 N  N   . PRO E  110 ? 2.8808 2.3275 2.7414 0.7960  -0.0232 -0.3756 110  PRO E N   
12342 C  CA  . PRO E  110 ? 2.7331 2.1473 2.5593 0.7416  -0.0143 -0.3539 110  PRO E CA  
12343 C  C   . PRO E  110 ? 2.8620 2.2055 2.6499 0.7235  0.0003  -0.3599 110  PRO E C   
12344 O  O   . PRO E  110 ? 2.8520 2.2034 2.6237 0.6780  0.0146  -0.3545 110  PRO E O   
12345 C  CB  . PRO E  110 ? 2.6439 2.0189 2.4470 0.7428  -0.0355 -0.3164 110  PRO E CB  
12346 C  CG  . PRO E  110 ? 2.6977 2.1231 2.5360 0.7846  -0.0530 -0.3200 110  PRO E CG  
12347 C  CD  . PRO E  110 ? 2.9649 2.4008 2.8258 0.8281  -0.0486 -0.3518 110  PRO E CD  
12348 N  N   . LEU E  111 ? 3.0398 2.3141 2.8101 0.7571  -0.0023 -0.3710 111  LEU E N   
12349 C  CA  . LEU E  111 ? 3.0522 2.2536 2.7814 0.7362  0.0128  -0.3802 111  LEU E CA  
12350 C  C   . LEU E  111 ? 3.1646 2.3966 2.9149 0.7447  0.0337  -0.4250 111  LEU E C   
12351 O  O   . LEU E  111 ? 3.3324 2.4963 3.0511 0.7418  0.0456  -0.4420 111  LEU E O   
12352 C  CB  . LEU E  111 ? 3.1064 2.1937 2.7909 0.7594  -0.0004 -0.3639 111  LEU E CB  
12353 C  CG  . LEU E  111 ? 2.9828 2.0263 2.6260 0.7263  -0.0123 -0.3221 111  LEU E CG  
12354 C  CD1 . LEU E  111 ? 3.3258 2.2570 2.9224 0.7472  -0.0258 -0.3046 111  LEU E CD1 
12355 C  CD2 . LEU E  111 ? 2.6706 1.7217 2.2878 0.6667  0.0053  -0.3193 111  LEU E CD2 
12356 N  N   . TYR E  112 ? 3.0617 2.3961 2.8627 0.7529  0.0391  -0.4461 112  TYR E N   
12357 C  CA  . TYR E  112 ? 2.8086 2.1934 2.6318 0.7512  0.0610  -0.4887 112  TYR E CA  
12358 C  C   . TYR E  112 ? 2.7697 2.1630 2.5690 0.6903  0.0812  -0.4884 112  TYR E C   
12359 O  O   . TYR E  112 ? 2.7786 2.2127 2.5778 0.6513  0.0814  -0.4638 112  TYR E O   
12360 C  CB  . TYR E  112 ? 2.5945 2.0980 2.4759 0.7668  0.0610  -0.5074 112  TYR E CB  
12361 C  CG  . TYR E  112 ? 2.6819 2.2657 2.5883 0.7468  0.0851  -0.5457 112  TYR E CG  
12362 C  CD1 . TYR E  112 ? 2.8879 2.4850 2.8126 0.7848  0.0954  -0.5892 112  TYR E CD1 
12363 C  CD2 . TYR E  112 ? 2.6965 2.3445 2.6072 0.6914  0.0977  -0.5379 112  TYR E CD2 
12364 C  CE1 . TYR E  112 ? 2.8974 2.5773 2.8453 0.7643  0.1179  -0.6260 112  TYR E CE1 
12365 C  CE2 . TYR E  112 ? 2.7352 2.4608 2.6662 0.6697  0.1193  -0.5704 112  TYR E CE2 
12366 C  CZ  . TYR E  112 ? 2.8180 2.5635 2.7685 0.7046  0.1294  -0.6153 112  TYR E CZ  
12367 O  OH  . TYR E  112 ? 2.8157 2.6461 2.7863 0.6809  0.1514  -0.6491 112  TYR E OH  
12368 N  N   . HIS E  113 ? 2.7794 2.1356 2.5575 0.6835  0.0986  -0.5165 113  HIS E N   
12369 C  CA  . HIS E  113 ? 2.7796 2.1539 2.5352 0.6272  0.1188  -0.5205 113  HIS E CA  
12370 C  C   . HIS E  113 ? 2.8764 2.3427 2.6677 0.6218  0.1390  -0.5610 113  HIS E C   
12371 O  O   . HIS E  113 ? 2.9855 2.4711 2.8061 0.6647  0.1416  -0.5962 113  HIS E O   
12372 C  CB  . HIS E  113 ? 2.8124 2.0875 2.5134 0.6114  0.1267  -0.5255 113  HIS E CB  
12373 C  CG  . HIS E  113 ? 3.0049 2.1929 2.6645 0.6075  0.1089  -0.4858 113  HIS E CG  
12374 N  ND1 . HIS E  113 ? 3.2111 2.3367 2.8691 0.6543  0.0884  -0.4727 113  HIS E ND1 
12375 C  CD2 . HIS E  113 ? 3.0764 2.2369 2.6944 0.5620  0.1083  -0.4559 113  HIS E CD2 
12376 C  CE1 . HIS E  113 ? 3.3088 2.3697 2.9247 0.6348  0.0764  -0.4367 113  HIS E CE1 
12377 N  NE2 . HIS E  113 ? 3.2573 2.3402 2.8492 0.5792  0.0883  -0.4270 113  HIS E NE2 
12378 N  N   . TRP E  114 ? 2.8561 2.3825 2.6438 0.5700  0.1535  -0.5552 114  TRP E N   
12379 C  CA  . TRP E  114 ? 2.8397 2.4600 2.6572 0.5562  0.1734  -0.5902 114  TRP E CA  
12380 C  C   . TRP E  114 ? 2.7597 2.3942 2.5460 0.5011  0.1932  -0.5916 114  TRP E C   
12381 O  O   . TRP E  114 ? 2.7159 2.3383 2.4738 0.4648  0.1901  -0.5537 114  TRP E O   
12382 C  CB  . TRP E  114 ? 2.8854 2.6010 2.7443 0.5512  0.1691  -0.5795 114  TRP E CB  
12383 C  CG  . TRP E  114 ? 2.9276 2.7381 2.7990 0.5079  0.1895  -0.5924 114  TRP E CG  
12384 C  CD1 . TRP E  114 ? 2.9464 2.8366 2.8491 0.5125  0.2053  -0.6360 114  TRP E CD1 
12385 C  CD2 . TRP E  114 ? 2.8551 2.6946 2.7073 0.4550  0.1960  -0.5595 114  TRP E CD2 
12386 N  NE1 . TRP E  114 ? 2.8538 2.8196 2.7558 0.4613  0.2213  -0.6315 114  TRP E NE1 
12387 C  CE2 . TRP E  114 ? 2.8664 2.7995 2.7369 0.4271  0.2156  -0.5833 114  TRP E CE2 
12388 C  CE3 . TRP E  114 ? 2.7846 2.5821 2.6049 0.4307  0.1873  -0.5121 114  TRP E CE3 
12389 C  CZ2 . TRP E  114 ? 2.8400 2.8188 2.6953 0.3763  0.2260  -0.5578 114  TRP E CZ2 
12390 C  CZ3 . TRP E  114 ? 2.7335 2.5776 2.5411 0.3850  0.1978  -0.4885 114  TRP E CZ3 
12391 C  CH2 . TRP E  114 ? 2.7675 2.6981 2.5912 0.3582  0.2166  -0.5097 114  TRP E CH2 
12392 N  N   . ARG E  115 ? 2.9582 2.6234 2.7498 0.4973  0.2135  -0.6368 115  ARG E N   
12393 C  CA  . ARG E  115 ? 2.9265 2.6118 2.6881 0.4459  0.2338  -0.6452 115  ARG E CA  
12394 C  C   . ARG E  115 ? 2.9132 2.7094 2.6946 0.4066  0.2434  -0.6333 115  ARG E C   
12395 O  O   . ARG E  115 ? 2.9911 2.8601 2.8141 0.4201  0.2442  -0.6466 115  ARG E O   
12396 C  CB  . ARG E  115 ? 2.9449 2.6173 2.7027 0.4572  0.2532  -0.7025 115  ARG E CB  
12397 C  CG  . ARG E  115 ? 2.9848 2.7073 2.7202 0.4020  0.2772  -0.7203 115  ARG E CG  
12398 C  CD  . ARG E  115 ? 2.9496 2.6955 2.6986 0.4172  0.2983  -0.7850 115  ARG E CD  
12399 N  NE  . ARG E  115 ? 2.8960 2.6994 2.6242 0.3623  0.3223  -0.8058 115  ARG E NE  
12400 C  CZ  . ARG E  115 ? 2.9038 2.8265 2.6531 0.3279  0.3335  -0.8055 115  ARG E CZ  
12401 N  NH1 . ARG E  115 ? 3.0160 3.0073 2.8059 0.3402  0.3241  -0.7871 115  ARG E NH1 
12402 N  NH2 . ARG E  115 ? 2.8794 2.8536 2.6062 0.2781  0.3545  -0.8232 115  ARG E NH2 
12403 N  N   . THR E  116 ? 2.7970 2.6075 2.5462 0.3574  0.2501  -0.6064 116  THR E N   
12404 C  CA  . THR E  116 ? 2.7829 2.6845 2.5432 0.3212  0.2568  -0.5844 116  THR E CA  
12405 C  C   . THR E  116 ? 2.9192 2.9108 2.7037 0.3083  0.2780  -0.6289 116  THR E C   
12406 O  O   . THR E  116 ? 3.0904 3.0734 2.8710 0.3151  0.2913  -0.6743 116  THR E O   
12407 C  CB  . THR E  116 ? 2.8191 2.7191 2.5370 0.2765  0.2599  -0.5464 116  THR E CB  
12408 O  OG1 . THR E  116 ? 2.8272 2.6470 2.5223 0.2898  0.2409  -0.5098 116  THR E OG1 
12409 C  CG2 . THR E  116 ? 2.8238 2.8037 2.5475 0.2438  0.2647  -0.5148 116  THR E CG2 
12410 N  N   . GLU E  117 ? 2.9145 2.9914 2.7206 0.2869  0.2825  -0.6166 117  GLU E N   
12411 C  CA  . GLU E  117 ? 2.8810 3.0563 2.7105 0.2698  0.3024  -0.6561 117  GLU E CA  
12412 C  C   . GLU E  117 ? 2.7887 3.0175 2.5889 0.2148  0.3197  -0.6468 117  GLU E C   
12413 O  O   . GLU E  117 ? 2.7785 3.0963 2.5915 0.1913  0.3380  -0.6765 117  GLU E O   
12414 C  CB  . GLU E  117 ? 2.8583 3.1028 2.7258 0.2723  0.2988  -0.6506 117  GLU E CB  
12415 C  CG  . GLU E  117 ? 2.9017 3.2448 2.8048 0.2732  0.3156  -0.7033 117  GLU E CG  
12416 C  CD  . GLU E  117 ? 2.8288 3.2411 2.7683 0.2744  0.3112  -0.7002 117  GLU E CD  
12417 O  OE1 . GLU E  117 ? 2.6994 3.0797 2.6337 0.2702  0.2966  -0.6562 117  GLU E OE1 
12418 O  OE2 . GLU E  117 ? 2.9543 3.4547 2.9270 0.2794  0.3230  -0.7446 117  GLU E OE2 
12419 N  N   . MET E  118 ? 2.8908 3.0739 2.6518 0.1944  0.3138  -0.6059 118  MET E N   
12420 C  CA  . MET E  118 ? 3.0000 3.2293 2.7277 0.1454  0.3272  -0.5908 118  MET E CA  
12421 C  C   . MET E  118 ? 3.0023 3.1907 2.6990 0.1377  0.3355  -0.6183 118  MET E C   
12422 O  O   . MET E  118 ? 3.0983 3.3473 2.7805 0.1019  0.3545  -0.6415 118  MET E O   
12423 C  CB  . MET E  118 ? 3.1305 3.3465 2.8343 0.1289  0.3150  -0.5240 118  MET E CB  
12424 C  CG  . MET E  118 ? 3.2400 3.5005 2.9633 0.1219  0.3121  -0.4946 118  MET E CG  
12425 S  SD  . MET E  118 ? 3.5938 3.7957 3.2949 0.1272  0.2928  -0.4225 118  MET E SD  
12426 C  CE  . MET E  118 ? 3.3606 3.6044 3.0873 0.1192  0.2938  -0.4076 118  MET E CE  
12427 N  N   . LYS E  119 ? 3.0084 3.0951 2.6925 0.1680  0.3223  -0.6180 119  LYS E N   
12428 C  CA  . LYS E  119 ? 2.9918 3.0208 2.6405 0.1592  0.3295  -0.6437 119  LYS E CA  
12429 C  C   . LYS E  119 ? 2.8959 2.8160 2.5496 0.2095  0.3167  -0.6616 119  LYS E C   
12430 O  O   . LYS E  119 ? 3.0114 2.9136 2.6977 0.2504  0.3021  -0.6536 119  LYS E O   
12431 C  CB  . LYS E  119 ? 3.0221 3.0449 2.6260 0.1219  0.3260  -0.6007 119  LYS E CB  
12432 C  CG  . LYS E  119 ? 3.0864 3.2173 2.6780 0.0721  0.3403  -0.5857 119  LYS E CG  
12433 C  CD  . LYS E  119 ? 3.0835 3.2195 2.6307 0.0383  0.3375  -0.5471 119  LYS E CD  
12434 C  CE  . LYS E  119 ? 3.1311 3.3828 2.6666 -0.0081 0.3524  -0.5347 119  LYS E CE  
12435 N  NZ  . LYS E  119 ? 3.1995 3.4760 2.6931 -0.0399 0.3500  -0.4967 119  LYS E NZ  
12436 N  N   . GLN E  120 ? 2.6977 2.5444 2.3154 0.2042  0.3227  -0.6854 120  GLN E N   
12437 C  CA  . GLN E  120 ? 2.7222 2.4556 2.3361 0.2503  0.3135  -0.7058 120  GLN E CA  
12438 C  C   . GLN E  120 ? 2.7441 2.3962 2.3322 0.2574  0.2912  -0.6570 120  GLN E C   
12439 O  O   . GLN E  120 ? 2.7785 2.3758 2.3198 0.2303  0.2929  -0.6502 120  GLN E O   
12440 C  CB  . GLN E  120 ? 2.7536 2.4378 2.3368 0.2397  0.3335  -0.7597 120  GLN E CB  
12441 C  CG  . GLN E  120 ? 2.9453 2.6926 2.5582 0.2487  0.3547  -0.8186 120  GLN E CG  
12442 C  CD  . GLN E  120 ? 3.1323 2.8327 2.7078 0.2293  0.3777  -0.8727 120  GLN E CD  
12443 O  OE1 . GLN E  120 ? 3.1993 2.7965 2.7280 0.2196  0.3759  -0.8699 120  GLN E OE1 
12444 N  NE2 . GLN E  120 ? 3.2057 2.9807 2.7996 0.2212  0.4004  -0.9244 120  GLN E NE2 
12445 N  N   . GLU E  121 ? 2.9127 2.5618 2.5304 0.2910  0.2708  -0.6242 121  GLU E N   
12446 C  CA  . GLU E  121 ? 3.0341 2.6080 2.6331 0.3051  0.2486  -0.5818 121  GLU E CA  
12447 C  C   . GLU E  121 ? 2.9492 2.4485 2.5679 0.3641  0.2334  -0.5926 121  GLU E C   
12448 O  O   . GLU E  121 ? 2.8867 2.3890 2.5319 0.3968  0.2405  -0.6342 121  GLU E O   
12449 C  CB  . GLU E  121 ? 3.0390 2.6688 2.6486 0.2917  0.2368  -0.5297 121  GLU E CB  
12450 C  CG  . GLU E  121 ? 2.9982 2.6963 2.5833 0.2391  0.2484  -0.5088 121  GLU E CG  
12451 C  CD  . GLU E  121 ? 3.0427 2.6937 2.5757 0.2103  0.2478  -0.4954 121  GLU E CD  
12452 O  OE1 . GLU E  121 ? 3.1946 2.9024 2.7029 0.1661  0.2609  -0.4916 121  GLU E OE1 
12453 O  OE2 . GLU E  121 ? 2.9820 2.5445 2.4973 0.2298  0.2342  -0.4881 121  GLU E OE2 
12454 N  N   . ARG E  122 ? 3.0429 2.4792 2.6477 0.3794  0.2121  -0.5543 122  ARG E N   
12455 C  CA  . ARG E  122 ? 3.0731 2.4420 2.6930 0.4344  0.1937  -0.5532 122  ARG E CA  
12456 C  C   . ARG E  122 ? 3.0217 2.3946 2.6469 0.4381  0.1718  -0.5018 122  ARG E C   
12457 O  O   . ARG E  122 ? 2.9707 2.2773 2.5620 0.4337  0.1589  -0.4734 122  ARG E O   
12458 C  CB  . ARG E  122 ? 3.1855 2.4357 2.7632 0.4472  0.1933  -0.5688 122  ARG E CB  
12459 C  CG  . ARG E  122 ? 3.2166 2.3989 2.8100 0.5106  0.1760  -0.5716 122  ARG E CG  
12460 C  CD  . ARG E  122 ? 3.2338 2.2934 2.7836 0.5256  0.1808  -0.5953 122  ARG E CD  
12461 N  NE  . ARG E  122 ? 3.2157 2.2206 2.7851 0.5945  0.1669  -0.6033 122  ARG E NE  
12462 C  CZ  . ARG E  122 ? 3.0818 2.0203 2.6387 0.6223  0.1434  -0.5682 122  ARG E CZ  
12463 N  NH1 . ARG E  122 ? 3.0410 1.9593 2.5665 0.5859  0.1320  -0.5251 122  ARG E NH1 
12464 N  NH2 . ARG E  122 ? 3.0702 1.9688 2.6462 0.6880  0.1311  -0.5758 122  ARG E NH2 
12465 N  N   . GLU E  123 ? 2.9697 2.4223 2.6363 0.4440  0.1685  -0.4917 123  GLU E N   
12466 C  CA  . GLU E  123 ? 2.8462 2.3128 2.5163 0.4394  0.1526  -0.4465 123  GLU E CA  
12467 C  C   . GLU E  123 ? 2.7557 2.2162 2.4605 0.4851  0.1344  -0.4427 123  GLU E C   
12468 O  O   . GLU E  123 ? 2.7935 2.3089 2.5391 0.5053  0.1384  -0.4678 123  GLU E O   
12469 C  CB  . GLU E  123 ? 2.9108 2.4663 2.5931 0.4044  0.1635  -0.4325 123  GLU E CB  
12470 C  CG  . GLU E  123 ? 3.0900 2.6666 2.7385 0.3587  0.1802  -0.4315 123  GLU E CG  
12471 C  CD  . GLU E  123 ? 3.0908 2.7499 2.7467 0.3275  0.1890  -0.4100 123  GLU E CD  
12472 O  OE1 . GLU E  123 ? 3.2914 2.9771 2.9184 0.2910  0.1997  -0.3995 123  GLU E OE1 
12473 O  OE2 . GLU E  123 ? 2.8832 2.5801 2.5711 0.3385  0.1853  -0.4026 123  GLU E OE2 
12474 N  N   . PRO E  124 ? 2.6647 2.0720 2.3550 0.4993  0.1157  -0.4140 124  PRO E N   
12475 C  CA  . PRO E  124 ? 2.6053 2.0071 2.3251 0.5430  0.0967  -0.4092 124  PRO E CA  
12476 C  C   . PRO E  124 ? 2.5654 2.0409 2.3188 0.5374  0.0926  -0.3944 124  PRO E C   
12477 O  O   . PRO E  124 ? 2.6860 2.1528 2.4320 0.5318  0.0800  -0.3618 124  PRO E O   
12478 C  CB  . PRO E  124 ? 2.5856 1.9028 2.2683 0.5503  0.0790  -0.3795 124  PRO E CB  
12479 C  CG  . PRO E  124 ? 2.6276 1.9393 2.2720 0.5033  0.0865  -0.3571 124  PRO E CG  
12480 C  CD  . PRO E  124 ? 2.6963 2.0463 2.3386 0.4751  0.1101  -0.3843 124  PRO E CD  
12481 N  N   . VAL E  125 ? 2.6269 2.1776 2.4163 0.5364  0.1048  -0.4209 125  VAL E N   
12482 C  CA  . VAL E  125 ? 2.6525 2.2709 2.4696 0.5242  0.1039  -0.4101 125  VAL E CA  
12483 C  C   . VAL E  125 ? 2.5867 2.2197 2.4356 0.5617  0.0866  -0.4135 125  VAL E C   
12484 O  O   . VAL E  125 ? 2.5979 2.2728 2.4632 0.5500  0.0830  -0.4010 125  VAL E O   
12485 C  CB  . VAL E  125 ? 2.7186 2.4190 2.5578 0.4997  0.1247  -0.4349 125  VAL E CB  
12486 C  CG1 . VAL E  125 ? 2.6651 2.3649 2.4721 0.4574  0.1405  -0.4238 125  VAL E CG1 
12487 C  CG2 . VAL E  125 ? 2.7110 2.4390 2.5781 0.5306  0.1308  -0.4807 125  VAL E CG2 
12488 N  N   . GLY E  126 ? 2.6450 2.2461 2.5015 0.6061  0.0766  -0.4306 126  GLY E N   
12489 C  CA  . GLY E  126 ? 2.5722 2.1984 2.4598 0.6453  0.0595  -0.4338 126  GLY E CA  
12490 C  C   . GLY E  126 ? 2.5667 2.2954 2.5020 0.6520  0.0674  -0.4655 126  GLY E C   
12491 O  O   . GLY E  126 ? 2.6260 2.4134 2.5700 0.6137  0.0844  -0.4737 126  GLY E O   
12492 N  N   . THR E  127 ? 2.4407 2.1963 2.4060 0.7005  0.0549  -0.4824 127  THR E N   
12493 C  CA  . THR E  127 ? 2.4403 2.3060 2.4532 0.7104  0.0608  -0.5145 127  THR E CA  
12494 C  C   . THR E  127 ? 2.5459 2.4449 2.5858 0.7533  0.0391  -0.5121 127  THR E C   
12495 O  O   . THR E  127 ? 2.5963 2.4262 2.6197 0.7895  0.0207  -0.4934 127  THR E O   
12496 C  CB  . THR E  127 ? 2.6175 2.5083 2.6458 0.7329  0.0760  -0.5563 127  THR E CB  
12497 O  OG1 . THR E  127 ? 2.6540 2.6680 2.7285 0.7332  0.0841  -0.5877 127  THR E OG1 
12498 C  CG2 . THR E  127 ? 2.7661 2.5899 2.7890 0.7970  0.0635  -0.5645 127  THR E CG2 
12499 N  N   . CYS E  128 ? 2.6719 2.6816 2.7512 0.7458  0.0415  -0.5303 128  CYS E N   
12500 C  CA  . CYS E  128 ? 2.6770 2.7449 2.7867 0.7833  0.0224  -0.5327 128  CYS E CA  
12501 C  C   . CYS E  128 ? 2.5516 2.7381 2.7098 0.8102  0.0291  -0.5757 128  CYS E C   
12502 O  O   . CYS E  128 ? 2.5506 2.7958 2.7216 0.7804  0.0501  -0.6016 128  CYS E O   
12503 C  CB  . CYS E  128 ? 2.5296 2.6275 2.6381 0.7424  0.0162  -0.5107 128  CYS E CB  
12504 S  SG  . CYS E  128 ? 2.5622 2.5351 2.6167 0.7131  0.0091  -0.4626 128  CYS E SG  
12505 N  N   . PHE E  129 ? 2.3422 2.5685 2.5267 0.8686  0.0107  -0.5826 129  PHE E N   
12506 C  CA  . PHE E  129 ? 2.4103 2.7699 2.6455 0.8991  0.0132  -0.6216 129  PHE E CA  
12507 C  C   . PHE E  129 ? 2.4210 2.8789 2.6829 0.8942  -0.0016 -0.6164 129  PHE E C   
12508 O  O   . PHE E  129 ? 2.3079 2.7265 2.5589 0.9179  -0.0235 -0.5882 129  PHE E O   
12509 C  CB  . PHE E  129 ? 2.5734 2.9091 2.8194 0.9807  0.0058  -0.6394 129  PHE E CB  
12510 C  CG  . PHE E  129 ? 2.6767 2.9455 2.9041 0.9826  0.0255  -0.6594 129  PHE E CG  
12511 C  CD1 . PHE E  129 ? 2.6770 3.0385 2.9342 0.9774  0.0465  -0.7037 129  PHE E CD1 
12512 C  CD2 . PHE E  129 ? 2.6469 2.7662 2.8253 0.9846  0.0240  -0.6357 129  PHE E CD2 
12513 C  CE1 . PHE E  129 ? 2.6291 2.9341 2.8684 0.9766  0.0656  -0.7251 129  PHE E CE1 
12514 C  CE2 . PHE E  129 ? 2.6071 2.6684 2.7660 0.9813  0.0433  -0.6570 129  PHE E CE2 
12515 C  CZ  . PHE E  129 ? 2.5778 2.7315 2.7675 0.9779  0.0642  -0.7023 129  PHE E CZ  
12516 N  N   . LEU E  130 ? 2.6478 3.2366 2.9424 0.8597  0.0111  -0.6442 130  LEU E N   
12517 C  CA  . LEU E  130 ? 2.5837 3.2833 2.9042 0.8433  0.0014  -0.6468 130  LEU E CA  
12518 C  C   . LEU E  130 ? 2.6428 3.4913 3.0163 0.8911  -0.0015 -0.6859 130  LEU E C   
12519 O  O   . LEU E  130 ? 2.5337 3.4463 2.9286 0.8914  0.0164  -0.7207 130  LEU E O   
12520 C  CB  . LEU E  130 ? 2.5320 3.2641 2.8416 0.7545  0.0195  -0.6463 130  LEU E CB  
12521 C  CG  . LEU E  130 ? 2.5444 3.3955 2.8770 0.7241  0.0145  -0.6554 130  LEU E CG  
12522 C  CD1 . LEU E  130 ? 2.4612 3.2741 2.7832 0.7470  -0.0106 -0.6265 130  LEU E CD1 
12523 C  CD2 . LEU E  130 ? 2.6443 3.5078 2.9583 0.6342  0.0358  -0.6557 130  LEU E CD2 
12524 N  N   . GLN E  131 ? 2.6880 3.5997 3.0830 0.9316  -0.0240 -0.6805 131  GLN E N   
12525 C  CA  . GLN E  131 ? 2.6683 3.7319 3.1151 0.9861  -0.0307 -0.7139 131  GLN E CA  
12526 C  C   . GLN E  131 ? 2.5940 3.8014 3.0660 0.9471  -0.0360 -0.7221 131  GLN E C   
12527 O  O   . GLN E  131 ? 2.8051 4.0024 3.2684 0.9515  -0.0559 -0.6962 131  GLN E O   
12528 C  CB  . GLN E  131 ? 2.5814 3.6007 3.0327 1.0844  -0.0544 -0.7011 131  GLN E CB  
12529 C  CG  . GLN E  131 ? 2.3337 3.5086 2.8389 1.1528  -0.0615 -0.7352 131  GLN E CG  
12530 C  CD  . GLN E  131 ? 2.3571 3.4639 2.8611 1.2562  -0.0797 -0.7248 131  GLN E CD  
12531 O  OE1 . GLN E  131 ? 2.2842 3.2216 2.7447 1.2719  -0.0840 -0.6958 131  GLN E OE1 
12532 N  NE2 . GLN E  131 ? 2.5113 3.7504 3.0607 1.3277  -0.0906 -0.7476 131  GLN E NE2 
12533 N  N   . ASP E  132 ? 2.5001 3.8429 3.0005 0.9042  -0.0174 -0.7589 132  ASP E N   
12534 C  CA  . ASP E  132 ? 2.4671 3.9657 2.9935 0.8655  -0.0202 -0.7745 132  ASP E CA  
12535 C  C   . ASP E  132 ? 2.4354 4.1113 3.0187 0.9287  -0.0273 -0.8115 132  ASP E C   
12536 O  O   . ASP E  132 ? 2.5005 4.3283 3.1142 0.8940  -0.0123 -0.8489 132  ASP E O   
12537 C  CB  . ASP E  132 ? 2.5807 4.1092 3.0926 0.7617  0.0060  -0.7872 132  ASP E CB  
12538 C  CG  . ASP E  132 ? 2.6170 4.2746 3.1415 0.7062  0.0043  -0.7983 132  ASP E CG  
12539 O  OD1 . ASP E  132 ? 2.7181 4.3136 3.2152 0.6767  -0.0056 -0.7709 132  ASP E OD1 
12540 O  OD2 . ASP E  132 ? 2.5001 4.3250 3.0608 0.6895  0.0141  -0.8368 132  ASP E OD2 
12541 N  N   . GLY E  133 ? 2.3988 4.0525 2.9941 1.0242  -0.0504 -0.7995 133  GLY E N   
12542 C  CA  . GLY E  133 ? 2.5574 4.3691 3.2054 1.1003  -0.0601 -0.8300 133  GLY E CA  
12543 C  C   . GLY E  133 ? 2.5833 4.3523 3.2418 1.1714  -0.0520 -0.8501 133  GLY E C   
12544 O  O   . GLY E  133 ? 2.6412 4.2856 3.2825 1.2454  -0.0660 -0.8276 133  GLY E O   
12545 N  N   . THR E  134 ? 2.4308 4.3018 3.1150 1.1464  -0.0282 -0.8938 134  THR E N   
12546 C  CA  . THR E  134 ? 2.4121 4.2603 3.1087 1.2061  -0.0160 -0.9222 134  THR E CA  
12547 C  C   . THR E  134 ? 2.2499 3.9504 2.9047 1.1507  0.0071  -0.9172 134  THR E C   
12548 O  O   . THR E  134 ? 2.2432 3.8043 2.8753 1.1990  0.0079  -0.9098 134  THR E O   
12549 C  CB  . THR E  134 ? 2.5780 4.6441 3.3311 1.2176  -0.0032 -0.9777 134  THR E CB  
12550 O  OG1 . THR E  134 ? 2.5322 4.6638 3.2810 1.1099  0.0222  -0.9966 134  THR E OG1 
12551 C  CG2 . THR E  134 ? 2.5866 4.8131 3.3745 1.2512  -0.0266 -0.9782 134  THR E CG2 
12552 N  N   . LYS E  135 ? 2.2040 3.9313 2.8452 1.0484  0.0260  -0.9199 135  LYS E N   
12553 C  CA  . LYS E  135 ? 2.2919 3.9027 2.8958 0.9924  0.0487  -0.9157 135  LYS E CA  
12554 C  C   . LYS E  135 ? 2.3473 3.7500 2.8979 0.9908  0.0383  -0.8660 135  LYS E C   
12555 O  O   . LYS E  135 ? 2.3069 3.6683 2.8394 0.9715  0.0220  -0.8311 135  LYS E O   
12556 C  CB  . LYS E  135 ? 2.3363 4.0258 2.9349 0.8846  0.0694  -0.9245 135  LYS E CB  
12557 C  CG  . LYS E  135 ? 2.4050 4.3142 3.0541 0.8746  0.0800  -0.9735 135  LYS E CG  
12558 C  CD  . LYS E  135 ? 2.3772 4.3373 3.0512 0.9163  0.0969  -1.0165 135  LYS E CD  
12559 C  CE  . LYS E  135 ? 2.2659 4.4600 2.9944 0.9164  0.1053  -1.0671 135  LYS E CE  
12560 N  NZ  . LYS E  135 ? 2.1982 4.4933 2.9211 0.8070  0.1189  -1.0705 135  LYS E NZ  
12561 N  N   . THR E  136 ? 2.5026 3.7805 3.0281 1.0116  0.0479  -0.8652 136  THR E N   
12562 C  CA  . THR E  136 ? 2.5384 3.6235 3.0106 1.0032  0.0418  -0.8220 136  THR E CA  
12563 C  C   . THR E  136 ? 2.7047 3.7253 3.1450 0.9303  0.0668  -0.8212 136  THR E C   
12564 O  O   . THR E  136 ? 2.9407 3.9872 3.3902 0.9353  0.0859  -0.8546 136  THR E O   
12565 C  CB  . THR E  136 ? 2.4205 3.4022 2.8839 1.0944  0.0293  -0.8181 136  THR E CB  
12566 O  OG1 . THR E  136 ? 2.3066 3.3485 2.7972 1.1641  0.0041  -0.8127 136  THR E OG1 
12567 C  CG2 . THR E  136 ? 2.2662 3.0559 2.6719 1.0778  0.0244  -0.7749 136  THR E CG2 
12568 N  N   . VAL E  137 ? 2.4181 3.3570 2.8201 0.8653  0.0668  -0.7832 137  VAL E N   
12569 C  CA  . VAL E  137 ? 2.3391 3.2191 2.7079 0.7953  0.0886  -0.7754 137  VAL E CA  
12570 C  C   . VAL E  137 ? 2.3815 3.0865 2.7001 0.7955  0.0815  -0.7343 137  VAL E C   
12571 O  O   . VAL E  137 ? 2.4117 3.0470 2.7176 0.8284  0.0599  -0.7059 137  VAL E O   
12572 C  CB  . VAL E  137 ? 2.3478 3.2956 2.7128 0.7095  0.0995  -0.7686 137  VAL E CB  
12573 C  CG1 . VAL E  137 ? 2.4123 3.5419 2.8248 0.7026  0.1062  -0.8094 137  VAL E CG1 
12574 C  CG2 . VAL E  137 ? 2.3624 3.2476 2.7041 0.6891  0.0825  -0.7281 137  VAL E CG2 
12575 N  N   . GLU E  138 ? 2.3889 3.0314 2.6781 0.7558  0.1001  -0.7312 138  GLU E N   
12576 C  CA  . GLU E  138 ? 2.3456 2.8375 2.5851 0.7430  0.0973  -0.6942 138  GLU E CA  
12577 C  C   . GLU E  138 ? 2.3678 2.8347 2.5789 0.6692  0.1027  -0.6609 138  GLU E C   
12578 O  O   . GLU E  138 ? 2.3955 2.9445 2.6164 0.6172  0.1174  -0.6711 138  GLU E O   
12579 C  CB  . GLU E  138 ? 2.4419 2.8828 2.6646 0.7480  0.1145  -0.7124 138  GLU E CB  
12580 C  CG  . GLU E  138 ? 2.4092 2.6986 2.5827 0.7494  0.1098  -0.6807 138  GLU E CG  
12581 C  CD  . GLU E  138 ? 2.4672 2.7173 2.6235 0.7484  0.1288  -0.7041 138  GLU E CD  
12582 O  OE1 . GLU E  138 ? 2.3982 2.7394 2.5773 0.7330  0.1479  -0.7402 138  GLU E OE1 
12583 O  OE2 . GLU E  138 ? 2.5107 2.6426 2.6289 0.7588  0.1255  -0.6875 138  GLU E OE2 
12584 N  N   . TYR E  139 ? 2.5546 2.9053 2.7279 0.6653  0.0911  -0.6207 139  TYR E N   
12585 C  CA  . TYR E  139 ? 2.7024 3.0144 2.8453 0.6050  0.0946  -0.5865 139  TYR E CA  
12586 C  C   . TYR E  139 ? 2.7320 2.9160 2.8287 0.6001  0.0932  -0.5541 139  TYR E C   
12587 O  O   . TYR E  139 ? 2.6638 2.7718 2.7446 0.6320  0.0752  -0.5327 139  TYR E O   
12588 C  CB  . TYR E  139 ? 2.7402 3.0741 2.8913 0.6028  0.0781  -0.5711 139  TYR E CB  
12589 C  CG  . TYR E  139 ? 2.6914 2.9759 2.8090 0.5462  0.0823  -0.5380 139  TYR E CG  
12590 C  CD1 . TYR E  139 ? 2.8423 3.1598 2.9510 0.4861  0.1031  -0.5395 139  TYR E CD1 
12591 C  CD2 . TYR E  139 ? 2.6560 2.8589 2.7488 0.5541  0.0660  -0.5049 139  TYR E CD2 
12592 C  CE1 . TYR E  139 ? 2.9379 3.2006 3.0127 0.4397  0.1075  -0.5083 139  TYR E CE1 
12593 C  CE2 . TYR E  139 ? 2.7091 2.8651 2.7711 0.5078  0.0707  -0.4770 139  TYR E CE2 
12594 C  CZ  . TYR E  139 ? 2.8137 2.9957 2.8663 0.4529  0.0915  -0.4785 139  TYR E CZ  
12595 O  OH  . TYR E  139 ? 2.7831 2.9089 2.8021 0.4121  0.0966  -0.4497 139  TYR E OH  
12596 N  N   . ALA E  140 ? 2.8377 3.0053 2.9119 0.5581  0.1121  -0.5500 140  ALA E N   
12597 C  CA  . ALA E  140 ? 2.9544 3.0189 2.9845 0.5460  0.1135  -0.5209 140  ALA E CA  
12598 C  C   . ALA E  140 ? 2.9434 3.0054 2.9483 0.4858  0.1269  -0.4957 140  ALA E C   
12599 O  O   . ALA E  140 ? 2.8183 2.9005 2.8135 0.4560  0.1453  -0.5023 140  ALA E O   
12600 C  CB  . ALA E  140 ? 2.9343 2.9755 2.9580 0.5652  0.1233  -0.5438 140  ALA E CB  
12601 N  N   . PRO E  141 ? 2.9098 2.9454 2.9016 0.4679  0.1186  -0.4662 141  PRO E N   
12602 C  CA  . PRO E  141 ? 2.9349 2.9599 2.8999 0.4153  0.1316  -0.4404 141  PRO E CA  
12603 C  C   . PRO E  141 ? 2.8867 2.8390 2.8114 0.4040  0.1359  -0.4115 141  PRO E C   
12604 O  O   . PRO E  141 ? 2.9745 2.9230 2.8760 0.3648  0.1486  -0.3905 141  PRO E O   
12605 C  CB  . PRO E  141 ? 2.7359 2.7439 2.6981 0.4090  0.1200  -0.4217 141  PRO E CB  
12606 C  CG  . PRO E  141 ? 2.6133 2.5864 2.5836 0.4584  0.0981  -0.4213 141  PRO E CG  
12607 C  CD  . PRO E  141 ? 2.7108 2.7247 2.7096 0.4958  0.0974  -0.4555 141  PRO E CD  
12608 N  N   . CYS E  142 ? 2.6394 2.5346 2.5524 0.4363  0.1256  -0.4084 142  CYS E N   
12609 C  CA  . CYS E  142 ? 2.5498 2.3866 2.4247 0.4249  0.1294  -0.3847 142  CYS E CA  
12610 C  C   . CYS E  142 ? 2.5985 2.4564 2.4720 0.4205  0.1439  -0.4091 142  CYS E C   
12611 O  O   . CYS E  142 ? 2.6798 2.5079 2.5218 0.4024  0.1508  -0.3932 142  CYS E O   
12612 C  CB  . CYS E  142 ? 2.4891 2.2493 2.3455 0.4545  0.1103  -0.3659 142  CYS E CB  
12613 S  SG  . CYS E  142 ? 2.4723 2.2003 2.3158 0.4473  0.0976  -0.3297 142  CYS E SG  
12614 N  N   . ARG E  143 ? 2.5708 2.4834 2.4775 0.4380  0.1488  -0.4492 143  ARG E N   
12615 C  CA  . ARG E  143 ? 2.6994 2.6457 2.6091 0.4317  0.1657  -0.4801 143  ARG E CA  
12616 C  C   . ARG E  143 ? 2.8640 2.8803 2.7736 0.3832  0.1846  -0.4781 143  ARG E C   
12617 O  O   . ARG E  143 ? 2.9905 3.0874 2.9302 0.3753  0.1936  -0.5050 143  ARG E O   
12618 C  CB  . ARG E  143 ? 2.7158 2.6981 2.6624 0.4737  0.1637  -0.5244 143  ARG E CB  
12619 C  CG  . ARG E  143 ? 2.7968 2.7944 2.7437 0.4785  0.1796  -0.5614 143  ARG E CG  
12620 C  CD  . ARG E  143 ? 2.7848 2.8114 2.7684 0.5307  0.1759  -0.6040 143  ARG E CD  
12621 N  NE  . ARG E  143 ? 2.7017 2.8361 2.7276 0.5280  0.1792  -0.6238 143  ARG E NE  
12622 C  CZ  . ARG E  143 ? 2.6640 2.8440 2.7281 0.5747  0.1712  -0.6525 143  ARG E CZ  
12623 N  NH1 . ARG E  143 ? 2.5885 2.7058 2.6524 0.6315  0.1591  -0.6623 143  ARG E NH1 
12624 N  NH2 . ARG E  143 ? 2.7018 2.9917 2.8024 0.5643  0.1755  -0.6707 143  ARG E NH2 
12625 N  N   . SER E  144 ? 2.8379 2.8266 2.7116 0.3499  0.1905  -0.4438 144  SER E N   
12626 C  CA  . SER E  144 ? 2.9218 2.9630 2.7866 0.3034  0.2067  -0.4305 144  SER E CA  
12627 C  C   . SER E  144 ? 3.1632 3.2124 3.0007 0.2787  0.2208  -0.4267 144  SER E C   
12628 O  O   . SER E  144 ? 3.2685 3.2910 3.0979 0.2948  0.2207  -0.4434 144  SER E O   
12629 C  CB  . SER E  144 ? 2.8020 2.8070 2.6473 0.2866  0.2003  -0.3864 144  SER E CB  
12630 O  OG  . SER E  144 ? 2.8406 2.8892 2.6757 0.2431  0.2156  -0.3723 144  SER E OG  
12631 N  N   . GLN E  145 ? 3.3914 3.4761 3.2112 0.2373  0.2334  -0.4031 145  GLN E N   
12632 C  CA  . GLN E  145 ? 3.3573 3.4569 3.1470 0.2099  0.2457  -0.3901 145  GLN E CA  
12633 C  C   . GLN E  145 ? 3.2295 3.2651 2.9816 0.2104  0.2366  -0.3428 145  GLN E C   
12634 O  O   . GLN E  145 ? 3.2754 3.3214 3.0001 0.1923  0.2439  -0.3297 145  GLN E O   
12635 C  CB  . GLN E  145 ? 3.2654 3.4399 3.0517 0.1657  0.2634  -0.3839 145  GLN E CB  
12636 C  CG  . GLN E  145 ? 3.1223 3.3775 2.9458 0.1583  0.2739  -0.4291 145  GLN E CG  
12637 C  CD  . GLN E  145 ? 3.0060 3.2878 2.8527 0.1826  0.2783  -0.4824 145  GLN E CD  
12638 O  OE1 . GLN E  145 ? 2.9691 3.2727 2.8520 0.2105  0.2745  -0.5192 145  GLN E OE1 
12639 N  NE2 . GLN E  145 ? 2.9386 3.2214 2.7634 0.1721  0.2871  -0.4878 145  GLN E NE2 
12640 N  N   . ASP E  146 ? 2.8439 2.8216 2.5945 0.2305  0.2212  -0.3188 146  ASP E N   
12641 C  CA  . ASP E  146 ? 2.7268 2.6441 2.4457 0.2389  0.2106  -0.2783 146  ASP E CA  
12642 C  C   . ASP E  146 ? 2.6824 2.5588 2.3982 0.2646  0.2006  -0.2952 146  ASP E C   
12643 O  O   . ASP E  146 ? 2.6823 2.5107 2.4084 0.2944  0.1854  -0.2995 146  ASP E O   
12644 C  CB  . ASP E  146 ? 2.7768 2.6509 2.4959 0.2497  0.1997  -0.2521 146  ASP E CB  
12645 C  CG  . ASP E  146 ? 2.9294 2.7509 2.6152 0.2579  0.1909  -0.2093 146  ASP E CG  
12646 O  OD1 . ASP E  146 ? 2.8341 2.6684 2.4936 0.2462  0.1963  -0.1909 146  ASP E OD1 
12647 O  OD2 . ASP E  146 ? 3.0510 2.8254 2.7375 0.2762  0.1788  -0.1955 146  ASP E OD2 
12648 N  N   . ILE E  147 ? 2.6838 2.5806 2.3827 0.2496  0.2103  -0.3061 147  ILE E N   
12649 C  CA  . ILE E  147 ? 2.7798 2.6377 2.4720 0.2662  0.2055  -0.3297 147  ILE E CA  
12650 C  C   . ILE E  147 ? 2.7823 2.5955 2.4381 0.2653  0.1961  -0.2962 147  ILE E C   
12651 O  O   . ILE E  147 ? 2.7189 2.5351 2.3580 0.2575  0.1931  -0.2555 147  ILE E O   
12652 C  CB  . ILE E  147 ? 2.8786 2.7812 2.5706 0.2474  0.2231  -0.3680 147  ILE E CB  
12653 C  CG1 . ILE E  147 ? 2.8081 2.7560 2.4683 0.2088  0.2353  -0.3449 147  ILE E CG1 
12654 C  CG2 . ILE E  147 ? 2.8158 2.7755 2.5452 0.2483  0.2330  -0.4024 147  ILE E CG2 
12655 C  CD1 . ILE E  147 ? 2.7227 2.7240 2.3800 0.1841  0.2542  -0.3825 147  ILE E CD1 
12656 N  N   . ASP E  148 ? 2.8329 2.6033 2.4746 0.2739  0.1920  -0.3139 148  ASP E N   
12657 C  CA  . ASP E  148 ? 2.7544 2.4882 2.3594 0.2683  0.1844  -0.2896 148  ASP E CA  
12658 C  C   . ASP E  148 ? 2.8012 2.4886 2.4046 0.2920  0.1654  -0.2573 148  ASP E C   
12659 O  O   . ASP E  148 ? 2.8867 2.5715 2.5158 0.3097  0.1590  -0.2517 148  ASP E O   
12660 C  CB  . ASP E  148 ? 2.7525 2.5425 2.3294 0.2335  0.1957  -0.2661 148  ASP E CB  
12661 C  CG  . ASP E  148 ? 2.7781 2.5534 2.3174 0.2159  0.1961  -0.2657 148  ASP E CG  
12662 O  OD1 . ASP E  148 ? 2.7721 2.4833 2.3005 0.2315  0.1835  -0.2662 148  ASP E OD1 
12663 O  OD2 . ASP E  148 ? 2.8728 2.7040 2.3913 0.1836  0.2093  -0.2648 148  ASP E OD2 
12664 N  N   . ALA E  149 ? 2.8904 2.5449 2.4625 0.2896  0.1569  -0.2384 149  ALA E N   
12665 C  CA  . ALA E  149 ? 2.9035 2.5174 2.4718 0.3112  0.1391  -0.2102 149  ALA E CA  
12666 C  C   . ALA E  149 ? 2.8645 2.5072 2.4389 0.3130  0.1389  -0.1774 149  ALA E C   
12667 O  O   . ALA E  149 ? 2.7595 2.3742 2.3469 0.3346  0.1275  -0.1657 149  ALA E O   
12668 C  CB  . ALA E  149 ? 2.9410 2.5302 2.4710 0.3011  0.1325  -0.1954 149  ALA E CB  
12669 N  N   . ASP E  150 ? 2.9160 2.6121 2.4783 0.2904  0.1520  -0.1619 150  ASP E N   
12670 C  CA  . ASP E  150 ? 2.8631 2.5767 2.4260 0.2931  0.1537  -0.1289 150  ASP E CA  
12671 C  C   . ASP E  150 ? 2.8063 2.5108 2.4011 0.3020  0.1547  -0.1417 150  ASP E C   
12672 O  O   . ASP E  150 ? 2.7706 2.4599 2.3662 0.3105  0.1519  -0.1185 150  ASP E O   
12673 C  CB  . ASP E  150 ? 2.9186 2.6939 2.4626 0.2677  0.1682  -0.1109 150  ASP E CB  
12674 C  CG  . ASP E  150 ? 3.1143 2.9160 2.6280 0.2518  0.1695  -0.1058 150  ASP E CG  
12675 O  OD1 . ASP E  150 ? 3.3317 3.1335 2.8236 0.2602  0.1618  -0.0748 150  ASP E OD1 
12676 O  OD2 . ASP E  150 ? 2.9833 2.8097 2.4942 0.2297  0.1791  -0.1347 150  ASP E OD2 
12677 N  N   . GLY E  151 ? 2.8203 2.5362 2.4401 0.2996  0.1596  -0.1798 151  GLY E N   
12678 C  CA  . GLY E  151 ? 2.9362 2.6576 2.5878 0.3056  0.1607  -0.1959 151  GLY E CA  
12679 C  C   . GLY E  151 ? 2.8918 2.5756 2.5666 0.3341  0.1463  -0.2184 151  GLY E C   
12680 O  O   . GLY E  151 ? 2.8101 2.4488 2.4749 0.3526  0.1316  -0.2035 151  GLY E O   
12681 N  N   . GLN E  152 ? 2.7325 2.4410 2.4382 0.3391  0.1502  -0.2543 152  GLN E N   
12682 C  CA  . GLN E  152 ? 2.5965 2.2824 2.3283 0.3695  0.1368  -0.2760 152  GLN E CA  
12683 C  C   . GLN E  152 ? 2.5747 2.2434 2.3094 0.3867  0.1351  -0.3065 152  GLN E C   
12684 O  O   . GLN E  152 ? 2.5289 2.1918 2.2892 0.4149  0.1271  -0.3305 152  GLN E O   
12685 C  CB  . GLN E  152 ? 2.5928 2.3247 2.3589 0.3673  0.1413  -0.2944 152  GLN E CB  
12686 C  CG  . GLN E  152 ? 2.6427 2.3754 2.4021 0.3498  0.1431  -0.2665 152  GLN E CG  
12687 C  CD  . GLN E  152 ? 2.6887 2.4734 2.4764 0.3356  0.1513  -0.2863 152  GLN E CD  
12688 O  OE1 . GLN E  152 ? 2.8028 2.6363 2.6176 0.3389  0.1566  -0.3211 152  GLN E OE1 
12689 N  NE2 . GLN E  152 ? 2.6646 2.4393 2.4440 0.3188  0.1533  -0.2656 152  GLN E NE2 
12690 N  N   . GLY E  153 ? 2.7689 2.4296 2.4759 0.3704  0.1432  -0.3062 153  GLY E N   
12691 C  CA  . GLY E  153 ? 2.9309 2.5646 2.6339 0.3823  0.1448  -0.3374 153  GLY E CA  
12692 C  C   . GLY E  153 ? 2.8662 2.4289 2.5624 0.4141  0.1260  -0.3344 153  GLY E C   
12693 O  O   . GLY E  153 ? 2.9681 2.5043 2.6747 0.4397  0.1235  -0.3632 153  GLY E O   
12694 N  N   . PHE E  154 ? 2.6802 2.2117 2.3578 0.4146  0.1127  -0.2994 154  PHE E N   
12695 C  CA  . PHE E  154 ? 2.6632 2.1307 2.3297 0.4402  0.0939  -0.2910 154  PHE E CA  
12696 C  C   . PHE E  154 ? 2.6744 2.1469 2.3639 0.4611  0.0789  -0.2761 154  PHE E C   
12697 O  O   . PHE E  154 ? 2.5676 1.9992 2.2434 0.4741  0.0627  -0.2564 154  PHE E O   
12698 C  CB  . PHE E  154 ? 2.6629 2.0931 2.2842 0.4206  0.0909  -0.2664 154  PHE E CB  
12699 C  CG  . PHE E  154 ? 2.7384 2.1485 2.3324 0.4016  0.1030  -0.2863 154  PHE E CG  
12700 C  CD1 . PHE E  154 ? 2.8079 2.2694 2.4001 0.3731  0.1226  -0.2994 154  PHE E CD1 
12701 C  CD2 . PHE E  154 ? 2.7582 2.0959 2.3246 0.4096  0.0955  -0.2921 154  PHE E CD2 
12702 C  CE1 . PHE E  154 ? 2.9172 2.3626 2.4827 0.3521  0.1351  -0.3215 154  PHE E CE1 
12703 C  CE2 . PHE E  154 ? 2.8437 2.1551 2.3803 0.3880  0.1086  -0.3135 154  PHE E CE2 
12704 C  CZ  . PHE E  154 ? 2.9041 2.2715 2.4410 0.3588  0.1287  -0.3299 154  PHE E CZ  
12705 N  N   . CYS E  155 ? 2.7119 2.2381 2.4352 0.4610  0.0852  -0.2878 155  CYS E N   
12706 C  CA  . CYS E  155 ? 2.7327 2.2728 2.4780 0.4734  0.0744  -0.2786 155  CYS E CA  
12707 C  C   . CYS E  155 ? 2.7619 2.2734 2.5199 0.5106  0.0554  -0.2863 155  CYS E C   
12708 O  O   . CYS E  155 ? 2.7005 2.1983 2.4577 0.5199  0.0410  -0.2679 155  CYS E O   
12709 C  CB  . CYS E  155 ? 2.6623 2.2683 2.4394 0.4615  0.0869  -0.2969 155  CYS E CB  
12710 S  SG  . CYS E  155 ? 2.6529 2.2888 2.4652 0.4785  0.0752  -0.3039 155  CYS E SG  
12711 N  N   . GLN E  156 ? 3.0076 2.5114 2.7770 0.5339  0.0554  -0.3135 156  GLN E N   
12712 C  CA  . GLN E  156 ? 2.9867 2.4684 2.7703 0.5757  0.0376  -0.3210 156  GLN E CA  
12713 C  C   . GLN E  156 ? 2.8126 2.3508 2.6324 0.5865  0.0295  -0.3236 156  GLN E C   
12714 O  O   . GLN E  156 ? 2.6785 2.2020 2.4981 0.6030  0.0117  -0.3076 156  GLN E O   
12715 C  CB  . GLN E  156 ? 2.8867 2.2927 2.6335 0.5842  0.0216  -0.2948 156  GLN E CB  
12716 C  CG  . GLN E  156 ? 2.8106 2.1608 2.5173 0.5677  0.0303  -0.2942 156  GLN E CG  
12717 C  CD  . GLN E  156 ? 2.6990 1.9734 2.3670 0.5748  0.0145  -0.2711 156  GLN E CD  
12718 O  OE1 . GLN E  156 ? 2.6147 1.8719 2.2504 0.5473  0.0139  -0.2464 156  GLN E OE1 
12719 N  NE2 . GLN E  156 ? 2.7842 2.0155 2.4540 0.6124  0.0017  -0.2782 156  GLN E NE2 
12720 N  N   . GLY E  157 ? 2.7677 2.3755 2.6164 0.5723  0.0436  -0.3445 157  GLY E N   
12721 C  CA  . GLY E  157 ? 2.7333 2.4026 2.6147 0.5745  0.0389  -0.3514 157  GLY E CA  
12722 C  C   . GLY E  157 ? 2.9467 2.6308 2.8536 0.6211  0.0217  -0.3659 157  GLY E C   
12723 O  O   . GLY E  157 ? 3.1210 2.7956 3.0355 0.6532  0.0210  -0.3855 157  GLY E O   
12724 N  N   . GLY E  158 ? 2.8895 2.5973 2.8085 0.6262  0.0080  -0.3563 158  GLY E N   
12725 C  CA  . GLY E  158 ? 2.8631 2.5929 2.8048 0.6707  -0.0110 -0.3641 158  GLY E CA  
12726 C  C   . GLY E  158 ? 2.7711 2.4269 2.6849 0.6953  -0.0313 -0.3368 158  GLY E C   
12727 O  O   . GLY E  158 ? 2.7844 2.4477 2.7115 0.7379  -0.0485 -0.3390 158  GLY E O   
12728 N  N   . PHE E  159 ? 2.5921 2.1814 2.4665 0.6701  -0.0300 -0.3101 159  PHE E N   
12729 C  CA  . PHE E  159 ? 2.7348 2.2588 2.5789 0.6857  -0.0487 -0.2825 159  PHE E CA  
12730 C  C   . PHE E  159 ? 2.6965 2.2574 2.5551 0.6966  -0.0665 -0.2731 159  PHE E C   
12731 O  O   . PHE E  159 ? 2.8987 2.4342 2.7488 0.7272  -0.0863 -0.2594 159  PHE E O   
12732 C  CB  . PHE E  159 ? 2.8020 2.2701 2.6046 0.6509  -0.0418 -0.2584 159  PHE E CB  
12733 C  CG  . PHE E  159 ? 3.0300 2.4288 2.7954 0.6609  -0.0580 -0.2318 159  PHE E CG  
12734 C  CD1 . PHE E  159 ? 3.1605 2.4972 2.9033 0.6795  -0.0609 -0.2322 159  PHE E CD1 
12735 C  CD2 . PHE E  159 ? 2.8664 2.2596 2.6158 0.6488  -0.0687 -0.2073 159  PHE E CD2 
12736 C  CE1 . PHE E  159 ? 3.0831 2.3528 2.7861 0.6828  -0.0750 -0.2064 159  PHE E CE1 
12737 C  CE2 . PHE E  159 ? 2.8198 2.1556 2.5329 0.6539  -0.0832 -0.1826 159  PHE E CE2 
12738 C  CZ  . PHE E  159 ? 2.9180 2.1917 2.6069 0.6691  -0.0865 -0.1809 159  PHE E CZ  
12739 N  N   . SER E  160 ? 2.2420 1.8613 2.1194 0.6695  -0.0592 -0.2801 160  SER E N   
12740 C  CA  . SER E  160 ? 2.2156 1.8861 2.1113 0.6745  -0.0727 -0.2798 160  SER E CA  
12741 C  C   . SER E  160 ? 2.2160 1.9716 2.1466 0.6541  -0.0596 -0.3070 160  SER E C   
12742 O  O   . SER E  160 ? 2.2425 2.0014 2.1708 0.6209  -0.0393 -0.3146 160  SER E O   
12743 C  CB  . SER E  160 ? 2.4640 2.0990 2.3304 0.6514  -0.0781 -0.2543 160  SER E CB  
12744 O  OG  . SER E  160 ? 2.5653 2.1888 2.4189 0.6115  -0.0586 -0.2525 160  SER E OG  
12745 N  N   . ILE E  161 ? 2.0916 1.9202 2.0528 0.6720  -0.0713 -0.3207 161  ILE E N   
12746 C  CA  . ILE E  161 ? 2.1457 2.0674 2.1406 0.6512  -0.0601 -0.3493 161  ILE E CA  
12747 C  C   . ILE E  161 ? 2.4267 2.4086 2.4347 0.6463  -0.0729 -0.3518 161  ILE E C   
12748 O  O   . ILE E  161 ? 2.6277 2.5919 2.6260 0.6702  -0.0931 -0.3339 161  ILE E O   
12749 C  CB  . ILE E  161 ? 2.1505 2.1325 2.1801 0.6826  -0.0573 -0.3768 161  ILE E CB  
12750 C  CG1 . ILE E  161 ? 2.3481 2.3183 2.3835 0.7444  -0.0798 -0.3698 161  ILE E CG1 
12751 C  CG2 . ILE E  161 ? 2.1630 2.1093 2.1831 0.6681  -0.0369 -0.3841 161  ILE E CG2 
12752 C  CD1 . ILE E  161 ? 2.5436 2.5738 2.6141 0.7855  -0.0783 -0.3981 161  ILE E CD1 
12753 N  N   . ASP E  162 ? 2.4723 2.5293 2.5006 0.6112  -0.0603 -0.3753 162  ASP E N   
12754 C  CA  . ASP E  162 ? 2.4710 2.6018 2.5138 0.5967  -0.0681 -0.3860 162  ASP E CA  
12755 C  C   . ASP E  162 ? 2.4327 2.6498 2.4992 0.5569  -0.0496 -0.4177 162  ASP E C   
12756 O  O   . ASP E  162 ? 2.3623 2.5645 2.4253 0.5331  -0.0296 -0.4251 162  ASP E O   
12757 C  CB  . ASP E  162 ? 2.5003 2.5723 2.5094 0.5680  -0.0698 -0.3664 162  ASP E CB  
12758 C  CG  . ASP E  162 ? 2.4367 2.5687 2.4558 0.5750  -0.0882 -0.3691 162  ASP E CG  
12759 O  OD1 . ASP E  162 ? 2.4148 2.6495 2.4688 0.5892  -0.0956 -0.3900 162  ASP E OD1 
12760 O  OD2 . ASP E  162 ? 2.4524 2.5359 2.4446 0.5664  -0.0951 -0.3512 162  ASP E OD2 
12761 N  N   . PHE E  163 ? 2.6116 2.9253 2.7008 0.5478  -0.0564 -0.4363 163  PHE E N   
12762 C  CA  . PHE E  163 ? 2.6446 3.0486 2.7523 0.5011  -0.0392 -0.4675 163  PHE E CA  
12763 C  C   . PHE E  163 ? 2.6246 3.0197 2.7091 0.4443  -0.0313 -0.4702 163  PHE E C   
12764 O  O   . PHE E  163 ? 2.5670 2.9444 2.6395 0.4520  -0.0459 -0.4582 163  PHE E O   
12765 C  CB  . PHE E  163 ? 2.6825 3.2261 2.8372 0.5313  -0.0508 -0.4939 163  PHE E CB  
12766 C  CG  . PHE E  163 ? 2.5418 3.1138 2.7231 0.5752  -0.0496 -0.5046 163  PHE E CG  
12767 C  CD1 . PHE E  163 ? 2.4330 3.0418 2.6247 0.5438  -0.0270 -0.5271 163  PHE E CD1 
12768 C  CD2 . PHE E  163 ? 2.4525 3.0141 2.6464 0.6474  -0.0705 -0.4931 163  PHE E CD2 
12769 C  CE1 . PHE E  163 ? 2.3478 2.9878 2.5644 0.5843  -0.0248 -0.5411 163  PHE E CE1 
12770 C  CE2 . PHE E  163 ? 2.3168 2.8987 2.5331 0.6898  -0.0678 -0.5065 163  PHE E CE2 
12771 C  CZ  . PHE E  163 ? 2.3035 2.9278 2.5326 0.6585  -0.0447 -0.5323 163  PHE E CZ  
12772 N  N   . THR E  164 ? 2.5377 2.9436 2.6135 0.3855  -0.0071 -0.4868 164  THR E N   
12773 C  CA  . THR E  164 ? 2.5149 2.9215 2.5692 0.3260  0.0041  -0.4974 164  THR E CA  
12774 C  C   . THR E  164 ? 2.5490 3.1013 2.6357 0.3037  0.0029  -0.5328 164  THR E C   
12775 O  O   . THR E  164 ? 2.5355 3.1907 2.6628 0.3365  -0.0058 -0.5482 164  THR E O   
12776 C  CB  . THR E  164 ? 2.5294 2.8567 2.5486 0.2710  0.0320  -0.4933 164  THR E CB  
12777 O  OG1 . THR E  164 ? 2.5391 2.9402 2.5778 0.2455  0.0474  -0.5155 164  THR E OG1 
12778 C  CG2 . THR E  164 ? 2.5103 2.7145 2.5022 0.2969  0.0331  -0.4593 164  THR E CG2 
12779 N  N   . LYS E  165 ? 2.5645 3.1278 2.6319 0.2470  0.0126  -0.5474 165  LYS E N   
12780 C  CA  . LYS E  165 ? 2.7002 3.4075 2.7938 0.2152  0.0132  -0.5831 165  LYS E CA  
12781 C  C   . LYS E  165 ? 2.9411 3.7019 3.0385 0.1605  0.0381  -0.6079 165  LYS E C   
12782 O  O   . LYS E  165 ? 3.0722 3.9720 3.1965 0.1353  0.0395  -0.6401 165  LYS E O   
12783 C  CB  . LYS E  165 ? 2.6507 3.3523 2.7193 0.1723  0.0139  -0.5924 165  LYS E CB  
12784 C  CG  . LYS E  165 ? 2.6120 3.4744 2.7077 0.1424  0.0103  -0.6288 165  LYS E CG  
12785 C  CD  . LYS E  165 ? 2.6083 3.4688 2.6832 0.1176  0.0041  -0.6349 165  LYS E CD  
12786 C  CE  . LYS E  165 ? 2.5883 3.6138 2.6855 0.0752  0.0044  -0.6744 165  LYS E CE  
12787 N  NZ  . LYS E  165 ? 2.6147 3.6435 2.6886 0.0411  0.0016  -0.6857 165  LYS E NZ  
12788 N  N   . ALA E  166 ? 2.9562 3.6203 3.0282 0.1425  0.0569  -0.5933 166  ALA E N   
12789 C  CA  . ALA E  166 ? 2.8606 3.5654 2.9299 0.0866  0.0815  -0.6126 166  ALA E CA  
12790 C  C   . ALA E  166 ? 2.6925 3.4245 2.7889 0.1254  0.0819  -0.6097 166  ALA E C   
12791 O  O   . ALA E  166 ? 2.6244 3.3321 2.7049 0.0875  0.1032  -0.6098 166  ALA E O   
12792 C  CB  . ALA E  166 ? 2.8476 3.4234 2.8595 0.0235  0.1065  -0.5994 166  ALA E CB  
12793 N  N   . ASP E  167 ? 2.6330 3.4123 2.7674 0.2004  0.0590  -0.6070 167  ASP E N   
12794 C  CA  . ASP E  167 ? 2.5907 3.4066 2.7546 0.2438  0.0582  -0.6107 167  ASP E CA  
12795 C  C   . ASP E  167 ? 2.5918 3.2776 2.7234 0.2410  0.0715  -0.5840 167  ASP E C   
12796 O  O   . ASP E  167 ? 2.5421 3.2510 2.6789 0.2259  0.0872  -0.5929 167  ASP E O   
12797 C  CB  . ASP E  167 ? 2.6122 3.5800 2.8087 0.2134  0.0705  -0.6492 167  ASP E CB  
12798 C  CG  . ASP E  167 ? 2.5979 3.7159 2.8318 0.2238  0.0555  -0.6766 167  ASP E CG  
12799 O  OD1 . ASP E  167 ? 2.6994 3.7991 2.9225 0.2243  0.0424  -0.6684 167  ASP E OD1 
12800 O  OD2 . ASP E  167 ? 2.4511 3.7130 2.7259 0.2327  0.0567  -0.7069 167  ASP E OD2 
12801 N  N   . ARG E  168 ? 2.6938 3.2500 2.7916 0.2550  0.0651  -0.5514 168  ARG E N   
12802 C  CA  . ARG E  168 ? 2.6773 3.1159 2.7473 0.2667  0.0720  -0.5225 168  ARG E CA  
12803 C  C   . ARG E  168 ? 2.5200 2.9108 2.5978 0.3384  0.0494  -0.5027 168  ARG E C   
12804 O  O   . ARG E  168 ? 2.4620 2.8515 2.5431 0.3650  0.0303  -0.4964 168  ARG E O   
12805 C  CB  . ARG E  168 ? 2.7504 3.0738 2.7686 0.2197  0.0862  -0.4993 168  ARG E CB  
12806 C  CG  . ARG E  168 ? 2.7578 3.1012 2.7566 0.1440  0.1115  -0.5138 168  ARG E CG  
12807 C  CD  . ARG E  168 ? 2.7515 2.9616 2.6946 0.1070  0.1279  -0.4856 168  ARG E CD  
12808 N  NE  . ARG E  168 ? 2.7354 2.8769 2.6618 0.1212  0.1355  -0.4594 168  ARG E NE  
12809 C  CZ  . ARG E  168 ? 2.8305 2.9457 2.7309 0.0764  0.1577  -0.4517 168  ARG E CZ  
12810 N  NH1 . ARG E  168 ? 2.8565 3.0003 2.7421 0.0125  0.1752  -0.4682 168  ARG E NH1 
12811 N  NH2 . ARG E  168 ? 2.9265 2.9885 2.8128 0.0924  0.1627  -0.4271 168  ARG E NH2 
12812 N  N   . VAL E  169 ? 2.5326 2.8852 2.6105 0.3664  0.0522  -0.4934 169  VAL E N   
12813 C  CA  . VAL E  169 ? 2.4604 2.7510 2.5367 0.4268  0.0342  -0.4735 169  VAL E CA  
12814 C  C   . VAL E  169 ? 2.6535 2.8161 2.6843 0.4157  0.0376  -0.4385 169  VAL E C   
12815 O  O   . VAL E  169 ? 2.6398 2.7592 2.6456 0.3770  0.0568  -0.4294 169  VAL E O   
12816 C  CB  . VAL E  169 ? 2.4845 2.8066 2.5848 0.4634  0.0361  -0.4874 169  VAL E CB  
12817 C  CG1 . VAL E  169 ? 2.5316 2.7633 2.6168 0.5129  0.0230  -0.4642 169  VAL E CG1 
12818 C  CG2 . VAL E  169 ? 2.5893 3.0405 2.7371 0.4906  0.0280  -0.5204 169  VAL E CG2 
12819 N  N   . LEU E  170 ? 2.7088 2.8151 2.7277 0.4504  0.0187  -0.4175 170  LEU E N   
12820 C  CA  . LEU E  170 ? 2.4954 2.4911 2.4739 0.4483  0.0193  -0.3849 170  LEU E CA  
12821 C  C   . LEU E  170 ? 2.4810 2.4314 2.4564 0.4948  0.0080  -0.3711 170  LEU E C   
12822 O  O   . LEU E  170 ? 2.4784 2.4392 2.4666 0.5367  -0.0120 -0.3701 170  LEU E O   
12823 C  CB  . LEU E  170 ? 2.3757 2.3407 2.3363 0.4421  0.0087  -0.3722 170  LEU E CB  
12824 C  CG  . LEU E  170 ? 2.3175 2.1804 2.2395 0.4485  0.0059  -0.3397 170  LEU E CG  
12825 C  CD1 . LEU E  170 ? 2.3468 2.1561 2.2414 0.4154  0.0280  -0.3276 170  LEU E CD1 
12826 C  CD2 . LEU E  170 ? 2.3384 2.1849 2.2463 0.4430  -0.0042 -0.3330 170  LEU E CD2 
12827 N  N   . LEU E  171 ? 2.5950 2.4934 2.5500 0.4853  0.0211  -0.3593 171  LEU E N   
12828 C  CA  . LEU E  171 ? 2.6008 2.4532 2.5474 0.5191  0.0150  -0.3494 171  LEU E CA  
12829 C  C   . LEU E  171 ? 2.6739 2.4376 2.5787 0.5092  0.0166  -0.3172 171  LEU E C   
12830 O  O   . LEU E  171 ? 2.8929 2.6344 2.7772 0.4746  0.0312  -0.3058 171  LEU E O   
12831 C  CB  . LEU E  171 ? 2.5915 2.4779 2.5533 0.5172  0.0301  -0.3699 171  LEU E CB  
12832 C  CG  . LEU E  171 ? 2.6816 2.5189 2.6313 0.5442  0.0290  -0.3656 171  LEU E CG  
12833 C  CD1 . LEU E  171 ? 2.8595 2.7579 2.8415 0.5652  0.0346  -0.3990 171  LEU E CD1 
12834 C  CD2 . LEU E  171 ? 2.5702 2.3545 2.4856 0.5134  0.0441  -0.3458 171  LEU E CD2 
12835 N  N   . GLY E  172 ? 2.4688 2.1835 2.3592 0.5401  0.0016  -0.3020 172  GLY E N   
12836 C  CA  . GLY E  172 ? 2.4030 2.0450 2.2547 0.5334  0.0015  -0.2730 172  GLY E CA  
12837 C  C   . GLY E  172 ? 2.3460 1.9573 2.1847 0.5412  0.0074  -0.2717 172  GLY E C   
12838 O  O   . GLY E  172 ? 2.3391 1.9531 2.1902 0.5699  0.0004  -0.2855 172  GLY E O   
12839 N  N   . GLY E  173 ? 2.2770 1.8593 2.0890 0.5161  0.0207  -0.2555 173  GLY E N   
12840 C  CA  . GLY E  173 ? 2.2732 1.8302 2.0677 0.5150  0.0281  -0.2537 173  GLY E CA  
12841 C  C   . GLY E  173 ? 2.2991 1.8068 2.0539 0.5039  0.0273  -0.2237 173  GLY E C   
12842 O  O   . GLY E  173 ? 2.5686 2.0777 2.3076 0.4800  0.0398  -0.2090 173  GLY E O   
12843 N  N   . PRO E  174 ? 2.2336 1.6993 1.9700 0.5217  0.0125  -0.2129 174  PRO E N   
12844 C  CA  . PRO E  174 ? 2.2175 1.6473 1.9168 0.5110  0.0094  -0.1844 174  PRO E CA  
12845 C  C   . PRO E  174 ? 2.2688 1.6936 1.9436 0.4895  0.0238  -0.1772 174  PRO E C   
12846 O  O   . PRO E  174 ? 2.2703 1.6846 1.9176 0.4776  0.0247  -0.1535 174  PRO E O   
12847 C  CB  . PRO E  174 ? 2.1962 1.5868 1.8823 0.5327  -0.0098 -0.1783 174  PRO E CB  
12848 C  CG  . PRO E  174 ? 2.1810 1.5905 1.9005 0.5591  -0.0194 -0.1987 174  PRO E CG  
12849 C  CD  . PRO E  174 ? 2.2124 1.6637 1.9595 0.5533  -0.0031 -0.2242 174  PRO E CD  
12850 N  N   . GLY E  175 ? 2.3041 1.7431 1.9880 0.4844  0.0354  -0.1978 175  GLY E N   
12851 C  CA  . GLY E  175 ? 2.3710 1.8085 2.0288 0.4623  0.0481  -0.1929 175  GLY E CA  
12852 C  C   . GLY E  175 ? 2.6480 2.1285 2.3086 0.4383  0.0663  -0.1894 175  GLY E C   
12853 O  O   . GLY E  175 ? 2.8702 2.3601 2.5080 0.4185  0.0767  -0.1820 175  GLY E O   
12854 N  N   . SER E  176 ? 2.6925 2.2012 2.3782 0.4373  0.0707  -0.1943 176  SER E N   
12855 C  CA  . SER E  176 ? 2.6013 2.1465 2.2872 0.4131  0.0883  -0.1894 176  SER E CA  
12856 C  C   . SER E  176 ? 2.8344 2.3719 2.4872 0.4007  0.0923  -0.1550 176  SER E C   
12857 O  O   . SER E  176 ? 3.1134 2.6229 2.7510 0.4119  0.0817  -0.1348 176  SER E O   
12858 C  CB  . SER E  176 ? 2.4801 2.0465 2.1914 0.4105  0.0911  -0.1972 176  SER E CB  
12859 O  OG  . SER E  176 ? 2.4765 2.0736 2.2207 0.4185  0.0914  -0.2309 176  SER E OG  
12860 N  N   . PHE E  177 ? 2.8586 2.4275 2.5003 0.3791  0.1078  -0.1485 177  PHE E N   
12861 C  CA  . PHE E  177 ? 2.8970 2.4722 2.5092 0.3695  0.1137  -0.1141 177  PHE E CA  
12862 C  C   . PHE E  177 ? 2.9552 2.5134 2.5408 0.3774  0.1035  -0.0976 177  PHE E C   
12863 O  O   . PHE E  177 ? 3.0239 2.5668 2.5942 0.3886  0.0972  -0.0725 177  PHE E O   
12864 C  CB  . PHE E  177 ? 2.9205 2.4797 2.5320 0.3733  0.1153  -0.0941 177  PHE E CB  
12865 C  CG  . PHE E  177 ? 3.0008 2.5730 2.6362 0.3613  0.1240  -0.1116 177  PHE E CG  
12866 C  CD1 . PHE E  177 ? 3.1562 2.7716 2.8017 0.3403  0.1374  -0.1272 177  PHE E CD1 
12867 C  CD2 . PHE E  177 ? 2.9407 2.4876 2.5868 0.3674  0.1196  -0.1140 177  PHE E CD2 
12868 C  CE1 . PHE E  177 ? 3.1644 2.8004 2.8307 0.3255  0.1458  -0.1439 177  PHE E CE1 
12869 C  CE2 . PHE E  177 ? 3.0027 2.5678 2.6683 0.3506  0.1284  -0.1312 177  PHE E CE2 
12870 C  CZ  . PHE E  177 ? 3.1012 2.7124 2.7771 0.3295  0.1413  -0.1456 177  PHE E CZ  
12871 N  N   . TYR E  178 ? 2.8559 2.4187 2.4336 0.3691  0.1034  -0.1133 178  TYR E N   
12872 C  CA  . TYR E  178 ? 2.8153 2.3632 2.3650 0.3691  0.0945  -0.1025 178  TYR E CA  
12873 C  C   . TYR E  178 ? 2.6303 2.1362 2.1817 0.3916  0.0769  -0.0962 178  TYR E C   
12874 O  O   . TYR E  178 ? 2.4861 1.9896 2.0162 0.3957  0.0698  -0.0733 178  TYR E O   
12875 C  CB  . TYR E  178 ? 2.8743 2.4607 2.3953 0.3565  0.1010  -0.0727 178  TYR E CB  
12876 C  CG  . TYR E  178 ? 3.0010 2.6174 2.4995 0.3304  0.1088  -0.0805 178  TYR E CG  
12877 C  CD1 . TYR E  178 ? 3.2045 2.7977 2.6820 0.3232  0.1011  -0.0882 178  TYR E CD1 
12878 C  CD2 . TYR E  178 ? 2.9114 2.5794 2.4064 0.3092  0.1245  -0.0807 178  TYR E CD2 
12879 C  CE1 . TYR E  178 ? 3.2747 2.8922 2.7275 0.2936  0.1099  -0.0985 178  TYR E CE1 
12880 C  CE2 . TYR E  178 ? 2.9437 2.6439 2.4167 0.2815  0.1327  -0.0910 178  TYR E CE2 
12881 C  CZ  . TYR E  178 ? 3.1082 2.7815 2.5598 0.2728  0.1259  -0.1013 178  TYR E CZ  
12882 O  OH  . TYR E  178 ? 3.1506 2.8532 2.5761 0.2396  0.1357  -0.1145 178  TYR E OH  
12883 N  N   . TRP E  179 ? 2.6842 2.1650 2.2621 0.4067  0.0697  -0.1176 179  TRP E N   
12884 C  CA  . TRP E  179 ? 2.5576 2.0033 2.1401 0.4277  0.0522  -0.1154 179  TRP E CA  
12885 C  C   . TRP E  179 ? 2.4930 1.9399 2.0760 0.4369  0.0487  -0.0948 179  TRP E C   
12886 O  O   . TRP E  179 ? 2.3976 1.8242 1.9732 0.4495  0.0351  -0.0856 179  TRP E O   
12887 C  CB  . TRP E  179 ? 2.6121 2.0297 2.1660 0.4262  0.0414  -0.1095 179  TRP E CB  
12888 C  CG  . TRP E  179 ? 2.6603 2.0541 2.2119 0.4226  0.0425  -0.1332 179  TRP E CG  
12889 C  CD1 . TRP E  179 ? 2.5189 1.8772 2.0854 0.4431  0.0324  -0.1511 179  TRP E CD1 
12890 C  CD2 . TRP E  179 ? 2.6987 2.0998 2.2291 0.3986  0.0549  -0.1423 179  TRP E CD2 
12891 N  NE1 . TRP E  179 ? 2.5816 1.9161 2.1369 0.4364  0.0385  -0.1712 179  TRP E NE1 
12892 C  CE2 . TRP E  179 ? 2.6645 2.0240 2.1969 0.4062  0.0529  -0.1681 179  TRP E CE2 
12893 C  CE3 . TRP E  179 ? 2.7874 2.2288 2.2962 0.3719  0.0678  -0.1317 179  TRP E CE3 
12894 C  CZ2 . TRP E  179 ? 2.7609 2.1105 2.2729 0.3854  0.0649  -0.1865 179  TRP E CZ2 
12895 C  CZ3 . TRP E  179 ? 2.8382 2.2805 2.3284 0.3485  0.0788  -0.1494 179  TRP E CZ3 
12896 C  CH2 . TRP E  179 ? 2.8357 2.2289 2.3268 0.3539  0.0780  -0.1781 179  TRP E CH2 
12897 N  N   . GLN E  180 ? 2.7779 2.2450 2.3669 0.4300  0.0615  -0.0876 180  GLN E N   
12898 C  CA  . GLN E  180 ? 2.8664 2.3209 2.4593 0.4399  0.0599  -0.0764 180  GLN E CA  
12899 C  C   . GLN E  180 ? 2.7895 2.2326 2.4111 0.4490  0.0520  -0.0984 180  GLN E C   
12900 O  O   . GLN E  180 ? 2.8557 2.2823 2.4781 0.4589  0.0449  -0.0939 180  GLN E O   
12901 C  CB  . GLN E  180 ? 2.8216 2.2894 2.4094 0.4288  0.0766  -0.0629 180  GLN E CB  
12902 C  CG  . GLN E  180 ? 2.6617 2.1467 2.2197 0.4263  0.0831  -0.0343 180  GLN E CG  
12903 C  CD  . GLN E  180 ? 2.7984 2.2885 2.3482 0.4199  0.0984  -0.0161 180  GLN E CD  
12904 O  OE1 . GLN E  180 ? 2.8520 2.3203 2.4129 0.4171  0.1036  -0.0220 180  GLN E OE1 
12905 N  NE2 . GLN E  180 ? 2.9377 2.4578 2.4652 0.4156  0.1058  0.0068  180  GLN E NE2 
12906 N  N   . GLY E  181 ? 2.6265 2.0839 2.2717 0.4465  0.0534  -0.1234 181  GLY E N   
12907 C  CA  . GLY E  181 ? 2.6115 2.0755 2.2872 0.4551  0.0472  -0.1458 181  GLY E CA  
12908 C  C   . GLY E  181 ? 2.7632 2.2496 2.4547 0.4386  0.0611  -0.1542 181  GLY E C   
12909 O  O   . GLY E  181 ? 2.9272 2.4100 2.6021 0.4234  0.0740  -0.1372 181  GLY E O   
12910 N  N   . GLN E  182 ? 2.7088 2.2204 2.4312 0.4415  0.0583  -0.1800 182  GLN E N   
12911 C  CA  . GLN E  182 ? 2.6356 2.1758 2.3733 0.4200  0.0717  -0.1922 182  GLN E CA  
12912 C  C   . GLN E  182 ? 2.6484 2.2188 2.4178 0.4280  0.0626  -0.2179 182  GLN E C   
12913 O  O   . GLN E  182 ? 2.6779 2.2609 2.4648 0.4521  0.0493  -0.2318 182  GLN E O   
12914 C  CB  . GLN E  182 ? 2.6327 2.2067 2.3760 0.4027  0.0874  -0.2017 182  GLN E CB  
12915 C  CG  . GLN E  182 ? 2.7534 2.3556 2.5038 0.3729  0.1037  -0.2086 182  GLN E CG  
12916 C  CD  . GLN E  182 ? 2.9005 2.5432 2.6551 0.3543  0.1190  -0.2176 182  GLN E CD  
12917 O  OE1 . GLN E  182 ? 2.8891 2.5478 2.6513 0.3663  0.1170  -0.2300 182  GLN E OE1 
12918 N  NE2 . GLN E  182 ? 2.9889 2.6456 2.7355 0.3228  0.1352  -0.2115 182  GLN E NE2 
12919 N  N   . LEU E  183 ? 2.6838 2.2653 2.4576 0.4070  0.0701  -0.2235 183  LEU E N   
12920 C  CA  . LEU E  183 ? 2.6601 2.2884 2.4646 0.4055  0.0651  -0.2506 183  LEU E CA  
12921 C  C   . LEU E  183 ? 2.6452 2.3242 2.4655 0.3761  0.0823  -0.2699 183  LEU E C   
12922 O  O   . LEU E  183 ? 2.6728 2.3334 2.4721 0.3453  0.0990  -0.2579 183  LEU E O   
12923 C  CB  . LEU E  183 ? 2.6137 2.2206 2.4086 0.3980  0.0606  -0.2467 183  LEU E CB  
12924 C  CG  . LEU E  183 ? 2.5429 2.1076 2.3213 0.4237  0.0440  -0.2288 183  LEU E CG  
12925 C  CD1 . LEU E  183 ? 2.7592 2.3151 2.5322 0.4132  0.0415  -0.2330 183  LEU E CD1 
12926 C  CD2 . LEU E  183 ? 2.3908 1.9748 2.1875 0.4570  0.0248  -0.2354 183  LEU E CD2 
12927 N  N   . ILE E  184 ? 2.7160 2.4602 2.5719 0.3864  0.0783  -0.2989 184  ILE E N   
12928 C  CA  . ILE E  184 ? 2.7614 2.5708 2.6367 0.3590  0.0937  -0.3220 184  ILE E CA  
12929 C  C   . ILE E  184 ? 2.6924 2.5680 2.5984 0.3563  0.0875  -0.3495 184  ILE E C   
12930 O  O   . ILE E  184 ? 2.5460 2.4439 2.4739 0.3922  0.0693  -0.3598 184  ILE E O   
12931 C  CB  . ILE E  184 ? 2.8631 2.7064 2.7544 0.3735  0.0980  -0.3362 184  ILE E CB  
12932 C  CG1 . ILE E  184 ? 2.8698 2.6586 2.7285 0.3686  0.1059  -0.3101 184  ILE E CG1 
12933 C  CG2 . ILE E  184 ? 3.0152 2.9403 2.9300 0.3460  0.1133  -0.3640 184  ILE E CG2 
12934 C  CD1 . ILE E  184 ? 2.7323 2.5541 2.6014 0.3737  0.1141  -0.3263 184  ILE E CD1 
12935 N  N   . SER E  185 ? 2.7615 2.6697 2.6663 0.3120  0.1026  -0.3601 185  SER E N   
12936 C  CA  . SER E  185 ? 2.8041 2.7886 2.7358 0.2984  0.1000  -0.3887 185  SER E CA  
12937 C  C   . SER E  185 ? 2.9513 3.0152 2.8991 0.2621  0.1178  -0.4128 185  SER E C   
12938 O  O   . SER E  185 ? 2.9844 3.0213 2.9050 0.2187  0.1370  -0.4015 185  SER E O   
12939 C  CB  . SER E  185 ? 2.6963 2.6399 2.6038 0.2703  0.1013  -0.3805 185  SER E CB  
12940 O  OG  . SER E  185 ? 2.6421 2.6670 2.5754 0.2565  0.0973  -0.4097 185  SER E OG  
12941 N  N   . ASP E  186 ? 2.9351 3.0994 2.9257 0.2804  0.1116  -0.4451 186  ASP E N   
12942 C  CA  . ASP E  186 ? 2.8718 3.1321 2.8829 0.2474  0.1274  -0.4733 186  ASP E CA  
12943 C  C   . ASP E  186 ? 2.8666 3.2333 2.9113 0.2412  0.1212  -0.5055 186  ASP E C   
12944 O  O   . ASP E  186 ? 2.8983 3.2890 2.9658 0.2844  0.1009  -0.5119 186  ASP E O   
12945 C  CB  . ASP E  186 ? 2.8078 3.1077 2.8416 0.2776  0.1299  -0.4869 186  ASP E CB  
12946 C  CG  . ASP E  186 ? 2.8681 3.0971 2.8685 0.2613  0.1437  -0.4620 186  ASP E CG  
12947 O  OD1 . ASP E  186 ? 2.8821 3.1185 2.8628 0.2089  0.1630  -0.4574 186  ASP E OD1 
12948 O  OD2 . ASP E  186 ? 2.9162 3.0844 2.9077 0.2987  0.1354  -0.4462 186  ASP E OD2 
12949 N  N   . GLN E  187 ? 2.8142 3.2497 2.8602 0.1850  0.1391  -0.5248 187  GLN E N   
12950 C  CA  . GLN E  187 ? 2.7460 3.3052 2.8249 0.1705  0.1363  -0.5597 187  GLN E CA  
12951 C  C   . GLN E  187 ? 2.6349 3.3073 2.7660 0.2209  0.1272  -0.5896 187  GLN E C   
12952 O  O   . GLN E  187 ? 2.6067 3.2949 2.7460 0.2304  0.1365  -0.5959 187  GLN E O   
12953 C  CB  . GLN E  187 ? 2.7423 3.3400 2.8020 0.0895  0.1603  -0.5715 187  GLN E CB  
12954 C  CG  . GLN E  187 ? 2.7260 3.2100 2.7321 0.0407  0.1702  -0.5455 187  GLN E CG  
12955 C  CD  . GLN E  187 ? 2.7803 3.2785 2.7574 -0.0410 0.1963  -0.5516 187  GLN E CD  
12956 O  OE1 . GLN E  187 ? 2.8301 3.4216 2.8254 -0.0635 0.2078  -0.5720 187  GLN E OE1 
12957 N  NE2 . GLN E  187 ? 2.8487 3.2516 2.7776 -0.0866 0.2066  -0.5343 187  GLN E NE2 
12958 N  N   . VAL E  188 ? 2.5132 3.2628 2.6784 0.2571  0.1085  -0.6074 188  VAL E N   
12959 C  CA  . VAL E  188 ? 2.4562 3.3092 2.6710 0.3165  0.0977  -0.6343 188  VAL E CA  
12960 C  C   . VAL E  188 ? 2.5626 3.5414 2.8020 0.2840  0.1163  -0.6695 188  VAL E C   
12961 O  O   . VAL E  188 ? 2.5920 3.6342 2.8643 0.3285  0.1153  -0.6907 188  VAL E O   
12962 C  CB  . VAL E  188 ? 2.3564 3.2769 2.6002 0.3581  0.0739  -0.6437 188  VAL E CB  
12963 C  CG1 . VAL E  188 ? 2.3602 3.1573 2.5769 0.3870  0.0559  -0.6080 188  VAL E CG1 
12964 C  CG2 . VAL E  188 ? 2.3829 3.4157 2.6362 0.3014  0.0803  -0.6680 188  VAL E CG2 
12965 N  N   . ALA E  189 ? 2.5322 3.5482 2.7539 0.2051  0.1345  -0.6774 189  ALA E N   
12966 C  CA  . ALA E  189 ? 2.4897 3.6280 2.7303 0.1656  0.1536  -0.7096 189  ALA E CA  
12967 C  C   . ALA E  189 ? 2.4705 3.5568 2.6959 0.1617  0.1691  -0.7005 189  ALA E C   
12968 O  O   . ALA E  189 ? 2.4378 3.6276 2.6919 0.1655  0.1788  -0.7300 189  ALA E O   
12969 C  CB  . ALA E  189 ? 2.5134 3.6895 2.7294 0.0743  0.1706  -0.7173 189  ALA E CB  
12970 N  N   . GLU E  190 ? 2.5749 3.5100 2.7557 0.1542  0.1717  -0.6612 190  GLU E N   
12971 C  CA  . GLU E  190 ? 2.6821 3.5626 2.8444 0.1505  0.1851  -0.6481 190  GLU E CA  
12972 C  C   . GLU E  190 ? 2.5538 3.4124 2.7389 0.2286  0.1726  -0.6516 190  GLU E C   
12973 O  O   . GLU E  190 ? 2.5686 3.4451 2.7578 0.2321  0.1844  -0.6616 190  GLU E O   
12974 C  CB  . GLU E  190 ? 2.8478 3.5825 2.9521 0.1126  0.1926  -0.6034 190  GLU E CB  
12975 C  CG  . GLU E  190 ? 2.9662 3.6583 3.0428 0.0861  0.2106  -0.5865 190  GLU E CG  
12976 C  CD  . GLU E  190 ? 3.0119 3.5626 3.0322 0.0584  0.2154  -0.5399 190  GLU E CD  
12977 O  OE1 . GLU E  190 ? 3.1514 3.6685 3.1403 0.0220  0.2321  -0.5205 190  GLU E OE1 
12978 O  OE2 . GLU E  190 ? 2.9315 3.4086 2.9386 0.0743  0.2023  -0.5224 190  GLU E OE2 
12979 N  N   . ILE E  191 ? 2.5695 3.3873 2.7661 0.2886  0.1497  -0.6437 191  ILE E N   
12980 C  CA  . ILE E  191 ? 2.5679 3.3439 2.7774 0.3601  0.1380  -0.6439 191  ILE E CA  
12981 C  C   . ILE E  191 ? 2.5517 3.4513 2.8079 0.3955  0.1413  -0.6878 191  ILE E C   
12982 O  O   . ILE E  191 ? 2.6916 3.5769 2.9503 0.4185  0.1490  -0.6978 191  ILE E O   
12983 C  CB  . ILE E  191 ? 2.6884 3.3991 2.8972 0.4124  0.1123  -0.6246 191  ILE E CB  
12984 C  CG1 . ILE E  191 ? 2.6508 3.2363 2.8123 0.3816  0.1103  -0.5827 191  ILE E CG1 
12985 C  CG2 . ILE E  191 ? 2.6602 3.3305 2.8807 0.4857  0.1005  -0.6274 191  ILE E CG2 
12986 C  CD1 . ILE E  191 ? 2.5609 3.0878 2.7190 0.4260  0.0859  -0.5634 191  ILE E CD1 
12987 N  N   . VAL E  192 ? 2.4342 3.4622 2.7280 0.4004  0.1362  -0.7167 192  VAL E N   
12988 C  CA  . VAL E  192 ? 2.5398 3.6971 2.8818 0.4419  0.1380  -0.7604 192  VAL E CA  
12989 C  C   . VAL E  192 ? 2.5659 3.8108 2.9115 0.3853  0.1643  -0.7855 192  VAL E C   
12990 O  O   . VAL E  192 ? 2.4471 3.7471 2.8160 0.4149  0.1728  -0.8148 192  VAL E O   
12991 C  CB  . VAL E  192 ? 2.5223 3.7980 2.9044 0.4717  0.1215  -0.7811 192  VAL E CB  
12992 C  CG1 . VAL E  192 ? 2.4657 3.7929 2.8358 0.3948  0.1275  -0.7781 192  VAL E CG1 
12993 C  CG2 . VAL E  192 ? 2.5217 3.9480 2.9558 0.5153  0.1246  -0.8285 192  VAL E CG2 
12994 N  N   . SER E  193 ? 2.5532 3.8072 2.8724 0.3022  0.1785  -0.7743 193  SER E N   
12995 C  CA  . SER E  193 ? 2.5522 3.8979 2.8717 0.2411  0.2033  -0.7963 193  SER E CA  
12996 C  C   . SER E  193 ? 2.5283 3.7976 2.8217 0.2331  0.2177  -0.7836 193  SER E C   
12997 O  O   . SER E  193 ? 2.4361 3.7941 2.7477 0.2265  0.2330  -0.8139 193  SER E O   
12998 C  CB  . SER E  193 ? 2.5373 3.8936 2.8267 0.1518  0.2147  -0.7834 193  SER E CB  
12999 O  OG  . SER E  193 ? 2.4982 3.6970 2.7320 0.1173  0.2185  -0.7366 193  SER E OG  
13000 N  N   . LYS E  194 ? 2.6929 3.8068 2.9446 0.2348  0.2130  -0.7408 194  LYS E N   
13001 C  CA  . LYS E  194 ? 2.6351 3.6771 2.8576 0.2228  0.2260  -0.7248 194  LYS E CA  
13002 C  C   . LYS E  194 ? 2.4675 3.4731 2.7063 0.2966  0.2177  -0.7372 194  LYS E C   
13003 O  O   . LYS E  194 ? 2.4767 3.4201 2.6911 0.2912  0.2272  -0.7257 194  LYS E O   
13004 C  CB  . LYS E  194 ? 2.7514 3.6513 2.9188 0.1863  0.2262  -0.6720 194  LYS E CB  
13005 C  CG  . LYS E  194 ? 2.6836 3.5933 2.8215 0.1059  0.2399  -0.6561 194  LYS E CG  
13006 C  CD  . LYS E  194 ? 2.7162 3.7233 2.8546 0.0518  0.2633  -0.6759 194  LYS E CD  
13007 C  CE  . LYS E  194 ? 2.7085 3.7115 2.8099 -0.0320 0.2778  -0.6570 194  LYS E CE  
13008 N  NZ  . LYS E  194 ? 2.6819 3.7265 2.7972 -0.0437 0.2694  -0.6704 194  LYS E NZ  
13009 N  N   . TYR E  195 ? 2.4009 3.4431 2.6773 0.3639  0.2009  -0.7601 195  TYR E N   
13010 C  CA  . TYR E  195 ? 2.3708 3.3686 2.6589 0.4361  0.1934  -0.7732 195  TYR E CA  
13011 C  C   . TYR E  195 ? 2.5810 3.6677 2.8908 0.4394  0.2126  -0.8157 195  TYR E C   
13012 O  O   . TYR E  195 ? 2.7289 3.9575 3.0714 0.4231  0.2223  -0.8507 195  TYR E O   
13013 C  CB  . TYR E  195 ? 2.3363 3.3545 2.6574 0.5085  0.1704  -0.7846 195  TYR E CB  
13014 C  CG  . TYR E  195 ? 2.3805 3.3621 2.7153 0.5869  0.1640  -0.8039 195  TYR E CG  
13015 C  CD1 . TYR E  195 ? 2.5084 3.3438 2.8070 0.6065  0.1596  -0.7778 195  TYR E CD1 
13016 C  CD2 . TYR E  195 ? 2.3593 3.4524 2.7411 0.6411  0.1635  -0.8494 195  TYR E CD2 
13017 C  CE1 . TYR E  195 ? 2.5431 3.3336 2.8479 0.6736  0.1556  -0.7965 195  TYR E CE1 
13018 C  CE2 . TYR E  195 ? 2.3585 3.4054 2.7485 0.7154  0.1591  -0.8677 195  TYR E CE2 
13019 C  CZ  . TYR E  195 ? 2.3681 3.2580 2.7174 0.7291  0.1556  -0.8411 195  TYR E CZ  
13020 O  OH  . TYR E  195 ? 2.3198 3.1513 2.6706 0.7980  0.1529  -0.8598 195  TYR E OH  
13021 N  N   . ASP E  196 ? 2.5636 3.5719 2.8539 0.4578  0.2189  -0.8145 196  ASP E N   
13022 C  CA  . ASP E  196 ? 2.4436 3.5221 2.7505 0.4648  0.2377  -0.8567 196  ASP E CA  
13023 C  C   . ASP E  196 ? 2.4149 3.3937 2.7116 0.5244  0.2336  -0.8636 196  ASP E C   
13024 O  O   . ASP E  196 ? 2.4398 3.2988 2.6943 0.5084  0.2334  -0.8306 196  ASP E O   
13025 C  CB  . ASP E  196 ? 2.4044 3.5072 2.6838 0.3848  0.2605  -0.8473 196  ASP E CB  
13026 C  CG  . ASP E  196 ? 2.3927 3.6352 2.6911 0.3299  0.2722  -0.8638 196  ASP E CG  
13027 O  OD1 . ASP E  196 ? 2.3539 3.7110 2.6973 0.3599  0.2683  -0.9011 196  ASP E OD1 
13028 O  OD2 . ASP E  196 ? 2.4351 3.6741 2.7015 0.2562  0.2853  -0.8385 196  ASP E OD2 
13029 N  N   . PRO E  197 ? 2.4431 3.4669 2.7753 0.5933  0.2311  -0.9063 197  PRO E N   
13030 C  CA  . PRO E  197 ? 2.4357 3.3491 2.7527 0.6511  0.2275  -0.9134 197  PRO E CA  
13031 C  C   . PRO E  197 ? 2.5074 3.3829 2.7949 0.6175  0.2492  -0.9230 197  PRO E C   
13032 O  O   . PRO E  197 ? 2.6019 3.3696 2.8657 0.6503  0.2482  -0.9242 197  PRO E O   
13033 C  CB  . PRO E  197 ? 2.5021 3.4955 2.8667 0.7293  0.2237  -0.9622 197  PRO E CB  
13034 C  CG  . PRO E  197 ? 2.5582 3.7292 2.9619 0.6968  0.2359  -0.9934 197  PRO E CG  
13035 C  CD  . PRO E  197 ? 2.5143 3.6928 2.9000 0.6226  0.2321  -0.9510 197  PRO E CD  
13036 N  N   . ASN E  198 ? 2.5404 3.5022 2.8261 0.5509  0.2689  -0.9299 198  ASN E N   
13037 C  CA  . ASN E  198 ? 2.6652 3.6076 2.9222 0.5119  0.2898  -0.9369 198  ASN E CA  
13038 C  C   . ASN E  198 ? 2.8161 3.6845 3.0252 0.4458  0.2906  -0.8814 198  ASN E C   
13039 O  O   . ASN E  198 ? 2.8422 3.6961 3.0234 0.4086  0.3065  -0.8797 198  ASN E O   
13040 C  CB  . ASN E  198 ? 2.6895 3.7863 2.9748 0.4832  0.3126  -0.9831 198  ASN E CB  
13041 C  CG  . ASN E  198 ? 2.6646 3.8676 2.9634 0.4280  0.3142  -0.9695 198  ASN E CG  
13042 O  OD1 . ASN E  198 ? 2.5561 3.7530 2.8648 0.4372  0.2967  -0.9472 198  ASN E OD1 
13043 N  ND2 . ASN E  198 ? 2.7696 4.0710 3.0662 0.3672  0.3358  -0.9835 198  ASN E ND2 
13044 N  N   . VAL E  199 ? 2.8072 3.6325 3.0059 0.4323  0.2741  -0.8370 199  VAL E N   
13045 C  CA  . VAL E  199 ? 2.7349 3.4837 2.8884 0.3789  0.2730  -0.7822 199  VAL E CA  
13046 C  C   . VAL E  199 ? 2.7084 3.3218 2.8389 0.4155  0.2521  -0.7482 199  VAL E C   
13047 O  O   . VAL E  199 ? 2.6390 3.2356 2.7868 0.4524  0.2335  -0.7423 199  VAL E O   
13048 C  CB  . VAL E  199 ? 2.7140 3.5206 2.8685 0.3260  0.2739  -0.7589 199  VAL E CB  
13049 C  CG1 . VAL E  199 ? 2.7992 3.5188 2.9042 0.2774  0.2739  -0.7019 199  VAL E CG1 
13050 C  CG2 . VAL E  199 ? 2.6576 3.6062 2.8346 0.2874  0.2945  -0.7941 199  VAL E CG2 
13051 N  N   . TYR E  200 ? 2.7527 3.2772 2.8431 0.4027  0.2552  -0.7257 200  TYR E N   
13052 C  CA  . TYR E  200 ? 2.7760 3.1758 2.8410 0.4339  0.2372  -0.6961 200  TYR E CA  
13053 C  C   . TYR E  200 ? 2.7456 3.0884 2.7807 0.4004  0.2275  -0.6403 200  TYR E C   
13054 O  O   . TYR E  200 ? 2.7445 3.0004 2.7654 0.4266  0.2095  -0.6145 200  TYR E O   
13055 C  CB  . TYR E  200 ? 2.7859 3.1199 2.8215 0.4392  0.2457  -0.7051 200  TYR E CB  
13056 C  CG  . TYR E  200 ? 2.8579 3.2437 2.9160 0.4649  0.2606  -0.7632 200  TYR E CG  
13057 C  CD1 . TYR E  200 ? 2.8563 3.2839 2.9557 0.5205  0.2547  -0.8006 200  TYR E CD1 
13058 C  CD2 . TYR E  200 ? 3.1137 3.5119 3.1514 0.4348  0.2811  -0.7819 200  TYR E CD2 
13059 C  CE1 . TYR E  200 ? 3.0705 3.5448 3.1906 0.5492  0.2694  -0.8562 200  TYR E CE1 
13060 C  CE2 . TYR E  200 ? 3.2793 3.7239 3.3364 0.4582  0.2966  -0.8392 200  TYR E CE2 
13061 C  CZ  . TYR E  200 ? 3.2251 3.7048 3.3234 0.5172  0.2910  -0.8768 200  TYR E CZ  
13062 O  OH  . TYR E  200 ? 3.1276 3.6523 3.2451 0.5457  0.3073  -0.9359 200  TYR E OH  
13063 N  N   . SER E  201 ? 2.5789 2.9670 2.6026 0.3444  0.2392  -0.6211 201  SER E N   
13064 C  CA  . SER E  201 ? 2.6078 2.9414 2.6012 0.3134  0.2324  -0.5695 201  SER E CA  
13065 C  C   . SER E  201 ? 2.6474 3.0549 2.6553 0.2768  0.2383  -0.5682 201  SER E C   
13066 O  O   . SER E  201 ? 2.6613 3.1203 2.6580 0.2281  0.2554  -0.5643 201  SER E O   
13067 C  CB  . SER E  201 ? 2.6547 2.9474 2.6053 0.2789  0.2422  -0.5386 201  SER E CB  
13068 O  OG  . SER E  201 ? 2.6611 2.8838 2.5944 0.3072  0.2365  -0.5394 201  SER E OG  
13069 N  N   . ILE E  202 ? 2.7312 3.1460 2.7615 0.2972  0.2245  -0.5718 202  ILE E N   
13070 C  CA  . ILE E  202 ? 2.7063 3.1911 2.7493 0.2603  0.2296  -0.5745 202  ILE E CA  
13071 C  C   . ILE E  202 ? 2.6849 3.0931 2.6910 0.2286  0.2254  -0.5261 202  ILE E C   
13072 O  O   . ILE E  202 ? 2.6085 2.9356 2.6037 0.2565  0.2087  -0.5037 202  ILE E O   
13073 C  CB  . ILE E  202 ? 2.7653 3.3146 2.8534 0.2974  0.2179  -0.6082 202  ILE E CB  
13074 C  CG1 . ILE E  202 ? 2.8227 3.4393 2.9463 0.3394  0.2219  -0.6564 202  ILE E CG1 
13075 C  CG2 . ILE E  202 ? 2.7658 3.3982 2.8650 0.2509  0.2253  -0.6147 202  ILE E CG2 
13076 C  CD1 . ILE E  202 ? 2.7853 3.4729 2.9548 0.3853  0.2094  -0.6890 202  ILE E CD1 
13077 N  N   . LYS E  203 ? 2.7277 3.1594 2.7123 0.1707  0.2411  -0.5101 203  LYS E N   
13078 C  CA  . LYS E  203 ? 2.8539 3.2123 2.8004 0.1386  0.2406  -0.4662 203  LYS E CA  
13079 C  C   . LYS E  203 ? 2.8572 3.2568 2.8177 0.1151  0.2398  -0.4781 203  LYS E C   
13080 O  O   . LYS E  203 ? 2.7239 3.2217 2.7034 0.0836  0.2520  -0.5060 203  LYS E O   
13081 C  CB  . LYS E  203 ? 2.9160 3.2627 2.8230 0.0893  0.2584  -0.4364 203  LYS E CB  
13082 C  CG  . LYS E  203 ? 2.8840 3.1293 2.7449 0.0714  0.2566  -0.3851 203  LYS E CG  
13083 C  CD  . LYS E  203 ? 2.8145 2.9722 2.6688 0.1204  0.2379  -0.3668 203  LYS E CD  
13084 C  CE  . LYS E  203 ? 2.8532 2.9158 2.6653 0.1088  0.2358  -0.3203 203  LYS E CE  
13085 N  NZ  . LYS E  203 ? 2.8033 2.7928 2.6110 0.1550  0.2174  -0.3056 203  LYS E NZ  
13086 N  N   . TYR E  204 ? 3.0269 3.3574 2.9769 0.1275  0.2263  -0.4587 204  TYR E N   
13087 C  CA  . TYR E  204 ? 3.2018 3.5626 3.1604 0.1035  0.2248  -0.4693 204  TYR E CA  
13088 C  C   . TYR E  204 ? 3.3436 3.6265 3.2530 0.0542  0.2346  -0.4317 204  TYR E C   
13089 O  O   . TYR E  204 ? 3.3970 3.5775 3.2730 0.0670  0.2301  -0.3944 204  TYR E O   
13090 C  CB  . TYR E  204 ? 3.1151 3.4631 3.0990 0.1540  0.2024  -0.4799 204  TYR E CB  
13091 C  CG  . TYR E  204 ? 2.9610 3.3603 2.9863 0.2121  0.1913  -0.5104 204  TYR E CG  
13092 C  CD1 . TYR E  204 ? 2.8229 3.3425 2.8921 0.2200  0.1929  -0.5536 204  TYR E CD1 
13093 C  CD2 . TYR E  204 ? 2.9039 3.2304 2.9216 0.2588  0.1801  -0.4966 204  TYR E CD2 
13094 C  CE1 . TYR E  204 ? 2.7227 3.2811 2.8272 0.2787  0.1834  -0.5814 204  TYR E CE1 
13095 C  CE2 . TYR E  204 ? 2.7612 3.1196 2.8104 0.3115  0.1714  -0.5241 204  TYR E CE2 
13096 C  CZ  . TYR E  204 ? 2.6409 3.1115 2.7334 0.3240  0.1730  -0.5661 204  TYR E CZ  
13097 O  OH  . TYR E  204 ? 2.5851 3.0804 2.7069 0.3820  0.1650  -0.5935 204  TYR E OH  
13098 N  N   . ASN E  205 ? 3.3607 3.6929 3.2637 -0.0023 0.2488  -0.4422 205  ASN E N   
13099 C  CA  . ASN E  205 ? 3.2979 3.5509 3.1484 -0.0543 0.2618  -0.4078 205  ASN E CA  
13100 C  C   . ASN E  205 ? 3.2950 3.4667 3.1298 -0.0459 0.2512  -0.3954 205  ASN E C   
13101 O  O   . ASN E  205 ? 3.4173 3.4794 3.2067 -0.0544 0.2546  -0.3574 205  ASN E O   
13102 C  CB  . ASN E  205 ? 3.2622 3.5910 3.1058 -0.1237 0.2819  -0.4241 205  ASN E CB  
13103 C  CG  . ASN E  205 ? 3.2301 3.6844 3.1224 -0.1268 0.2782  -0.4742 205  ASN E CG  
13104 O  OD1 . ASN E  205 ? 3.2546 3.8154 3.1883 -0.1077 0.2777  -0.5067 205  ASN E OD1 
13105 N  ND2 . ASN E  205 ? 3.1592 3.6060 3.0463 -0.1502 0.2760  -0.4822 205  ASN E ND2 
13106 N  N   . ASN E  206 ? 3.1021 3.3293 2.9731 -0.0281 0.2386  -0.4271 206  ASN E N   
13107 C  CA  . ASN E  206 ? 2.9999 3.1635 2.8589 -0.0212 0.2283  -0.4202 206  ASN E CA  
13108 C  C   . ASN E  206 ? 2.9827 3.0856 2.8500 0.0455  0.2069  -0.4053 206  ASN E C   
13109 O  O   . ASN E  206 ? 2.9069 2.9943 2.7821 0.0647  0.1931  -0.4110 206  ASN E O   
13110 C  CB  . ASN E  206 ? 2.9504 3.2122 2.8413 -0.0397 0.2251  -0.4602 206  ASN E CB  
13111 C  CG  . ASN E  206 ? 2.9629 3.2867 2.8410 -0.1143 0.2471  -0.4761 206  ASN E CG  
13112 O  OD1 . ASN E  206 ? 3.0361 3.2863 2.8649 -0.1624 0.2647  -0.4500 206  ASN E OD1 
13113 N  ND2 . ASN E  206 ? 2.9262 3.3881 2.8471 -0.1240 0.2463  -0.5181 206  ASN E ND2 
13114 N  N   . GLN E  207 ? 3.0695 3.1426 2.9332 0.0771  0.2046  -0.3870 207  GLN E N   
13115 C  CA  . GLN E  207 ? 2.9506 2.9662 2.8171 0.1344  0.1859  -0.3718 207  GLN E CA  
13116 C  C   . GLN E  207 ? 2.8562 2.7582 2.6786 0.1318  0.1852  -0.3347 207  GLN E C   
13117 O  O   . GLN E  207 ? 2.9496 2.7972 2.7329 0.1020  0.2002  -0.3076 207  GLN E O   
13118 C  CB  . GLN E  207 ? 2.8754 2.8993 2.7478 0.1602  0.1865  -0.3669 207  GLN E CB  
13119 C  CG  . GLN E  207 ? 2.6860 2.6627 2.5628 0.2163  0.1679  -0.3567 207  GLN E CG  
13120 C  CD  . GLN E  207 ? 2.6539 2.6470 2.5361 0.2344  0.1711  -0.3596 207  GLN E CD  
13121 O  OE1 . GLN E  207 ? 2.6746 2.7365 2.5711 0.2152  0.1840  -0.3800 207  GLN E OE1 
13122 N  NE2 . GLN E  207 ? 2.6024 2.5356 2.4714 0.2685  0.1601  -0.3412 207  GLN E NE2 
13123 N  N   . LEU E  208 ? 2.6667 2.5348 2.4945 0.1654  0.1678  -0.3331 208  LEU E N   
13124 C  CA  . LEU E  208 ? 2.6942 2.4610 2.4847 0.1737  0.1648  -0.3016 208  LEU E CA  
13125 C  C   . LEU E  208 ? 2.8103 2.5449 2.6025 0.2240  0.1496  -0.2844 208  LEU E C   
13126 O  O   . LEU E  208 ? 2.8411 2.6109 2.6635 0.2589  0.1329  -0.3010 208  LEU E O   
13127 C  CB  . LEU E  208 ? 2.6626 2.4189 2.4540 0.1672  0.1579  -0.3144 208  LEU E CB  
13128 C  CG  . LEU E  208 ? 2.7569 2.5347 2.5383 0.1096  0.1745  -0.3317 208  LEU E CG  
13129 C  CD1 . LEU E  208 ? 2.7536 2.5226 2.5347 0.1039  0.1671  -0.3466 208  LEU E CD1 
13130 C  CD2 . LEU E  208 ? 2.8408 2.5410 2.5730 0.0727  0.1956  -0.3031 208  LEU E CD2 
13131 N  N   . ALA E  209 ? 2.9401 2.6086 2.6974 0.2274  0.1552  -0.2503 209  ALA E N   
13132 C  CA  . ALA E  209 ? 2.8679 2.5139 2.6233 0.2673  0.1429  -0.2346 209  ALA E CA  
13133 C  C   . ALA E  209 ? 2.8470 2.4127 2.5616 0.2750  0.1443  -0.1972 209  ALA E C   
13134 O  O   . ALA E  209 ? 2.8535 2.3826 2.5378 0.2503  0.1595  -0.1771 209  ALA E O   
13135 C  CB  . ALA E  209 ? 2.7899 2.4797 2.5553 0.2673  0.1493  -0.2391 209  ALA E CB  
13136 N  N   . THR E  210 ? 2.8725 2.4122 2.5851 0.3103  0.1284  -0.1875 210  THR E N   
13137 C  CA  . THR E  210 ? 2.9665 2.4448 2.6440 0.3247  0.1279  -0.1537 210  THR E CA  
13138 C  C   . THR E  210 ? 2.8486 2.3353 2.5115 0.3258  0.1348  -0.1331 210  THR E C   
13139 O  O   . THR E  210 ? 2.7246 2.2387 2.3997 0.3414  0.1268  -0.1392 210  THR E O   
13140 C  CB  . THR E  210 ? 2.9776 2.4375 2.6581 0.3575  0.1087  -0.1526 210  THR E CB  
13141 O  OG1 . THR E  210 ? 2.9560 2.4543 2.6609 0.3755  0.0963  -0.1675 210  THR E OG1 
13142 C  CG2 . THR E  210 ? 3.0551 2.5059 2.7439 0.3540  0.1031  -0.1693 210  THR E CG2 
13143 N  N   . ARG E  211 ? 2.9505 2.4125 2.5846 0.3079  0.1502  -0.1085 211  ARG E N   
13144 C  CA  . ARG E  211 ? 2.9544 2.4339 2.5726 0.3046  0.1581  -0.0871 211  ARG E CA  
13145 C  C   . ARG E  211 ? 3.0673 2.5274 2.6667 0.3348  0.1486  -0.0623 211  ARG E C   
13146 O  O   . ARG E  211 ? 3.1262 2.5506 2.7191 0.3569  0.1382  -0.0568 211  ARG E O   
13147 C  CB  . ARG E  211 ? 3.0272 2.4859 2.6177 0.2766  0.1767  -0.0652 211  ARG E CB  
13148 C  CG  . ARG E  211 ? 3.1555 2.6495 2.7649 0.2397  0.1870  -0.0925 211  ARG E CG  
13149 C  CD  . ARG E  211 ? 3.3941 2.8592 2.9713 0.2052  0.2059  -0.0711 211  ARG E CD  
13150 N  NE  . ARG E  211 ? 3.4956 3.0090 3.0920 0.1654  0.2156  -0.1001 211  ARG E NE  
13151 C  CZ  . ARG E  211 ? 3.4281 2.9330 3.0328 0.1453  0.2174  -0.1231 211  ARG E CZ  
13152 N  NH1 . ARG E  211 ? 3.3714 2.8167 2.9667 0.1612  0.2104  -0.1217 211  ARG E NH1 
13153 N  NH2 . ARG E  211 ? 3.4080 2.9719 3.0305 0.1074  0.2266  -0.1497 211  ARG E NH2 
13154 N  N   . THR E  212 ? 2.9915 2.4838 2.5815 0.3329  0.1527  -0.0489 212  THR E N   
13155 C  CA  . THR E  212 ? 2.9241 2.4168 2.4971 0.3554  0.1445  -0.0286 212  THR E CA  
13156 C  C   . THR E  212 ? 3.0129 2.4634 2.5529 0.3725  0.1466  0.0080  212  THR E C   
13157 O  O   . THR E  212 ? 3.0968 2.5219 2.6174 0.3632  0.1591  0.0277  212  THR E O   
13158 C  CB  . THR E  212 ? 2.9010 2.4464 2.4701 0.3425  0.1509  -0.0257 212  THR E CB  
13159 O  OG1 . THR E  212 ? 2.8715 2.4241 2.4188 0.3589  0.1451  -0.0029 212  THR E OG1 
13160 C  CG2 . THR E  212 ? 3.0364 2.5988 2.5922 0.3177  0.1682  -0.0096 212  THR E CG2 
13161 N  N   . ALA E  213 ? 2.9624 2.4041 2.4942 0.3984  0.1345  0.0169  213  ALA E N   
13162 C  CA  . ALA E  213 ? 2.9661 2.3755 2.4692 0.4225  0.1348  0.0480  213  ALA E CA  
13163 C  C   . ALA E  213 ? 2.9296 2.3825 2.4151 0.4352  0.1316  0.0712  213  ALA E C   
13164 O  O   . ALA E  213 ? 2.9564 2.4591 2.4466 0.4188  0.1332  0.0661  213  ALA E O   
13165 C  CB  . ALA E  213 ? 2.9099 2.2793 2.4181 0.4413  0.1240  0.0362  213  ALA E CB  
13166 N  N   . GLN E  214 ? 2.8495 2.2872 2.3132 0.4637  0.1284  0.0955  214  GLN E N   
13167 C  CA  . GLN E  214 ? 2.7804 2.2684 2.2255 0.4775  0.1254  0.1192  214  GLN E CA  
13168 C  C   . GLN E  214 ? 2.7327 2.2602 2.1889 0.4696  0.1129  0.0993  214  GLN E C   
13169 O  O   . GLN E  214 ? 2.7559 2.2609 2.2309 0.4660  0.1035  0.0727  214  GLN E O   
13170 C  CB  . GLN E  214 ? 2.8076 2.2739 2.2296 0.5146  0.1243  0.1458  214  GLN E CB  
13171 C  CG  . GLN E  214 ? 2.8805 2.2967 2.2819 0.5269  0.1378  0.1710  214  GLN E CG  
13172 C  CD  . GLN E  214 ? 2.7926 2.1295 2.2001 0.5241  0.1412  0.1525  214  GLN E CD  
13173 O  OE1 . GLN E  214 ? 2.7613 2.0915 2.1944 0.5038  0.1355  0.1192  214  GLN E OE1 
13174 N  NE2 . GLN E  214 ? 2.8383 2.1146 2.2200 0.5449  0.1509  0.1738  214  GLN E NE2 
13175 N  N   . ALA E  215 ? 2.4078 1.9954 1.8488 0.4661  0.1130  0.1141  215  ALA E N   
13176 C  CA  . ALA E  215 ? 2.5607 2.1841 2.0041 0.4508  0.1040  0.0967  215  ALA E CA  
13177 C  C   . ALA E  215 ? 2.6841 2.2921 2.1251 0.4671  0.0897  0.0917  215  ALA E C   
13178 O  O   . ALA E  215 ? 2.7194 2.3346 2.1630 0.4521  0.0812  0.0732  215  ALA E O   
13179 C  CB  . ALA E  215 ? 2.6464 2.3432 2.0690 0.4394  0.1090  0.1146  215  ALA E CB  
13180 N  N   . ILE E  216 ? 2.8542 2.4403 2.2874 0.4968  0.0875  0.1075  216  ILE E N   
13181 C  CA  . ILE E  216 ? 2.7210 2.3004 2.1516 0.5107  0.0743  0.1017  216  ILE E CA  
13182 C  C   . ILE E  216 ? 2.5231 2.0551 1.9758 0.5017  0.0655  0.0723  216  ILE E C   
13183 O  O   . ILE E  216 ? 2.3474 1.8802 1.7985 0.5020  0.0528  0.0634  216  ILE E O   
13184 C  CB  . ILE E  216 ? 2.4933 2.0599 1.9109 0.5472  0.0757  0.1217  216  ILE E CB  
13185 C  CG1 . ILE E  216 ? 2.3703 1.9529 1.7817 0.5594  0.0626  0.1173  216  ILE E CG1 
13186 C  CG2 . ILE E  216 ? 2.5592 2.0548 1.9870 0.5565  0.0825  0.1152  216  ILE E CG2 
13187 C  CD1 . ILE E  216 ? 2.3025 1.8713 1.7031 0.5979  0.0641  0.1302  216  ILE E CD1 
13188 N  N   . PHE E  217 ? 2.6389 2.1358 2.1112 0.4927  0.0717  0.0578  217  PHE E N   
13189 C  CA  . PHE E  217 ? 2.6838 2.1458 2.1794 0.4873  0.0636  0.0305  217  PHE E CA  
13190 C  C   . PHE E  217 ? 2.8796 2.3534 2.3877 0.4668  0.0593  0.0099  217  PHE E C   
13191 O  O   . PHE E  217 ? 2.8929 2.3437 2.4215 0.4657  0.0519  -0.0120 217  PHE E O   
13192 C  CB  . PHE E  217 ? 2.5305 1.9556 2.0406 0.4864  0.0728  0.0227  217  PHE E CB  
13193 C  CG  . PHE E  217 ? 2.5646 1.9581 2.0600 0.5069  0.0778  0.0378  217  PHE E CG  
13194 C  CD1 . PHE E  217 ? 2.7764 2.1473 2.2727 0.5218  0.0684  0.0293  217  PHE E CD1 
13195 C  CD2 . PHE E  217 ? 2.6703 2.0537 2.1488 0.5119  0.0923  0.0603  217  PHE E CD2 
13196 C  CE1 . PHE E  217 ? 2.8597 2.1964 2.3408 0.5416  0.0747  0.0392  217  PHE E CE1 
13197 C  CE2 . PHE E  217 ? 2.9365 2.2788 2.3977 0.5342  0.0981  0.0736  217  PHE E CE2 
13198 C  CZ  . PHE E  217 ? 2.9862 2.3037 2.4489 0.5493  0.0900  0.0610  217  PHE E CZ  
13199 N  N   . ASP E  218 ? 2.9451 2.4548 2.4403 0.4517  0.0642  0.0155  218  ASP E N   
13200 C  CA  . ASP E  218 ? 2.8048 2.3169 2.3058 0.4335  0.0610  -0.0059 218  ASP E CA  
13201 C  C   . ASP E  218 ? 2.6136 2.1039 2.1090 0.4385  0.0446  -0.0126 218  ASP E C   
13202 O  O   . ASP E  218 ? 2.4136 1.9074 1.8944 0.4498  0.0368  0.0024  218  ASP E O   
13203 C  CB  . ASP E  218 ? 2.8035 2.3599 2.2848 0.4126  0.0699  0.0007  218  ASP E CB  
13204 C  CG  . ASP E  218 ? 2.7050 2.2881 2.1911 0.4037  0.0859  0.0067  218  ASP E CG  
13205 O  OD1 . ASP E  218 ? 2.7244 2.2860 2.2285 0.4105  0.0907  0.0039  218  ASP E OD1 
13206 O  OD2 . ASP E  218 ? 2.6522 2.2811 2.1217 0.3864  0.0940  0.0142  218  ASP E OD2 
13207 N  N   . ASP E  219 ? 2.7477 2.2156 2.2537 0.4313  0.0395  -0.0350 219  ASP E N   
13208 C  CA  . ASP E  219 ? 2.7646 2.2042 2.2617 0.4347  0.0237  -0.0397 219  ASP E CA  
13209 C  C   . ASP E  219 ? 2.6625 2.0846 2.1714 0.4559  0.0120  -0.0362 219  ASP E C   
13210 O  O   . ASP E  219 ? 2.6642 2.0860 2.1556 0.4602  0.0014  -0.0241 219  ASP E O   
13211 C  CB  . ASP E  219 ? 2.9670 2.4253 2.4275 0.4181  0.0215  -0.0254 219  ASP E CB  
13212 C  CG  . ASP E  219 ? 3.3517 2.7749 2.7960 0.4145  0.0065  -0.0292 219  ASP E CG  
13213 O  OD1 . ASP E  219 ? 3.3906 2.7735 2.8458 0.4174  0.0023  -0.0473 219  ASP E OD1 
13214 O  OD2 . ASP E  219 ? 3.6051 3.0426 3.0243 0.4095  -0.0009 -0.0131 219  ASP E OD2 
13215 N  N   . SER E  220 ? 2.6521 2.0653 2.1900 0.4659  0.0148  -0.0485 220  SER E N   
13216 C  CA  . SER E  220 ? 2.6427 2.0430 2.1929 0.4817  0.0058  -0.0499 220  SER E CA  
13217 C  C   . SER E  220 ? 2.7364 2.1208 2.3109 0.4900  -0.0051 -0.0703 220  SER E C   
13218 O  O   . SER E  220 ? 2.8282 2.2054 2.4064 0.5011  -0.0176 -0.0706 220  SER E O   
13219 C  CB  . SER E  220 ? 2.5048 1.9088 2.0639 0.4845  0.0185  -0.0464 220  SER E CB  
13220 O  OG  . SER E  220 ? 2.4451 1.8611 1.9803 0.4875  0.0253  -0.0236 220  SER E OG  
13221 N  N   . TYR E  221 ? 2.6511 2.0361 2.2426 0.4864  -0.0004 -0.0879 221  TYR E N   
13222 C  CA  . TYR E  221 ? 2.4776 1.8550 2.0936 0.4998  -0.0106 -0.1077 221  TYR E CA  
13223 C  C   . TYR E  221 ? 2.4232 1.8166 2.0662 0.5066  -0.0118 -0.1181 221  TYR E C   
13224 O  O   . TYR E  221 ? 2.3533 1.7465 2.0078 0.5205  -0.0263 -0.1240 221  TYR E O   
13225 C  CB  . TYR E  221 ? 2.4423 1.7925 2.0413 0.5101  -0.0290 -0.1009 221  TYR E CB  
13226 C  CG  . TYR E  221 ? 2.5440 1.8699 2.1148 0.4995  -0.0279 -0.0967 221  TYR E CG  
13227 C  CD1 . TYR E  221 ? 2.9781 2.3153 2.5410 0.4814  -0.0113 -0.1001 221  TYR E CD1 
13228 C  CD2 . TYR E  221 ? 2.5206 1.8113 2.0692 0.5044  -0.0430 -0.0893 221  TYR E CD2 
13229 C  CE1 . TYR E  221 ? 3.0378 2.3536 2.5719 0.4665  -0.0088 -0.0998 221  TYR E CE1 
13230 C  CE2 . TYR E  221 ? 2.5796 1.8400 2.0966 0.4891  -0.0405 -0.0871 221  TYR E CE2 
13231 C  CZ  . TYR E  221 ? 2.7533 2.0272 2.2634 0.4693  -0.0229 -0.0942 221  TYR E CZ  
13232 O  OH  . TYR E  221 ? 2.7111 1.9563 2.1873 0.4490  -0.0187 -0.0954 221  TYR E OH  
13233 N  N   . LEU E  222 ? 2.5107 1.9183 2.1603 0.4942  0.0039  -0.1193 222  LEU E N   
13234 C  CA  . LEU E  222 ? 2.6464 2.0690 2.3199 0.4922  0.0065  -0.1340 222  LEU E CA  
13235 C  C   . LEU E  222 ? 2.4694 1.9186 2.1751 0.4975  0.0042  -0.1596 222  LEU E C   
13236 O  O   . LEU E  222 ? 2.4480 1.9084 2.1605 0.4929  0.0130  -0.1688 222  LEU E O   
13237 C  CB  . LEU E  222 ? 2.8435 2.2658 2.5105 0.4743  0.0257  -0.1281 222  LEU E CB  
13238 C  CG  . LEU E  222 ? 2.7159 2.1543 2.4050 0.4616  0.0333  -0.1472 222  LEU E CG  
13239 C  CD1 . LEU E  222 ? 2.6843 2.1173 2.3768 0.4674  0.0230  -0.1531 222  LEU E CD1 
13240 C  CD2 . LEU E  222 ? 2.7044 2.1327 2.3804 0.4409  0.0536  -0.1381 222  LEU E CD2 
13241 N  N   . GLY E  223 ? 2.5276 1.9938 2.2534 0.5078  -0.0073 -0.1724 223  GLY E N   
13242 C  CA  . GLY E  223 ? 2.5772 2.0782 2.3350 0.5199  -0.0123 -0.1961 223  GLY E CA  
13243 C  C   . GLY E  223 ? 2.5633 2.0523 2.3217 0.5485  -0.0317 -0.1946 223  GLY E C   
13244 O  O   . GLY E  223 ? 2.4849 1.9988 2.2680 0.5665  -0.0362 -0.2129 223  GLY E O   
13245 N  N   . TYR E  224 ? 2.5839 2.0353 2.3137 0.5540  -0.0431 -0.1726 224  TYR E N   
13246 C  CA  . TYR E  224 ? 2.4030 1.8318 2.1249 0.5781  -0.0617 -0.1662 224  TYR E CA  
13247 C  C   . TYR E  224 ? 2.3957 1.8596 2.1442 0.5998  -0.0774 -0.1768 224  TYR E C   
13248 O  O   . TYR E  224 ? 2.3843 1.8441 2.1408 0.6269  -0.0893 -0.1808 224  TYR E O   
13249 C  CB  . TYR E  224 ? 2.4612 1.8525 2.1450 0.5723  -0.0699 -0.1399 224  TYR E CB  
13250 C  CG  . TYR E  224 ? 2.6628 2.0148 2.3254 0.5882  -0.0855 -0.1284 224  TYR E CG  
13251 C  CD1 . TYR E  224 ? 2.8781 2.1909 2.5174 0.5820  -0.0790 -0.1253 224  TYR E CD1 
13252 C  CD2 . TYR E  224 ? 2.6162 1.9679 2.2778 0.6068  -0.1061 -0.1200 224  TYR E CD2 
13253 C  CE1 . TYR E  224 ? 2.8169 2.0813 2.4300 0.5926  -0.0916 -0.1146 224  TYR E CE1 
13254 C  CE2 . TYR E  224 ? 2.5844 1.8909 2.2206 0.6203  -0.1201 -0.1059 224  TYR E CE2 
13255 C  CZ  . TYR E  224 ? 2.6888 1.9467 2.2994 0.6125  -0.1123 -0.1034 224  TYR E CZ  
13256 O  OH  . TYR E  224 ? 2.7513 1.9525 2.3304 0.6222  -0.1248 -0.0893 224  TYR E OH  
13257 N  N   . SER E  225 ? 2.4608 1.9593 2.2211 0.5887  -0.0773 -0.1816 225  SER E N   
13258 C  CA  . SER E  225 ? 2.5099 2.0586 2.2974 0.6032  -0.0903 -0.1946 225  SER E CA  
13259 C  C   . SER E  225 ? 2.5796 2.1730 2.3866 0.5775  -0.0764 -0.2137 225  SER E C   
13260 O  O   . SER E  225 ? 2.6587 2.2296 2.4496 0.5514  -0.0608 -0.2095 225  SER E O   
13261 C  CB  . SER E  225 ? 2.5177 2.0574 2.2880 0.6141  -0.1108 -0.1764 225  SER E CB  
13262 O  OG  . SER E  225 ? 2.5389 2.0639 2.2875 0.5907  -0.1050 -0.1667 225  SER E OG  
13263 N  N   . VAL E  226 ? 2.4048 2.0624 2.2445 0.5847  -0.0817 -0.2346 226  VAL E N   
13264 C  CA  . VAL E  226 ? 2.4045 2.1089 2.2614 0.5548  -0.0677 -0.2563 226  VAL E CA  
13265 C  C   . VAL E  226 ? 2.2403 2.0114 2.1181 0.5591  -0.0814 -0.2701 226  VAL E C   
13266 O  O   . VAL E  226 ? 2.1604 1.9583 2.0500 0.5923  -0.1017 -0.2662 226  VAL E O   
13267 C  CB  . VAL E  226 ? 2.4219 2.1591 2.3017 0.5456  -0.0513 -0.2769 226  VAL E CB  
13268 C  CG1 . VAL E  226 ? 2.2889 1.9696 2.1461 0.5312  -0.0343 -0.2647 226  VAL E CG1 
13269 C  CG2 . VAL E  226 ? 2.4335 2.2140 2.3421 0.5831  -0.0635 -0.2888 226  VAL E CG2 
13270 N  N   . ALA E  227 ? 2.2106 2.0085 2.0908 0.5235  -0.0691 -0.2864 227  ALA E N   
13271 C  CA  . ALA E  227 ? 2.2778 2.1489 2.1765 0.5144  -0.0770 -0.3054 227  ALA E CA  
13272 C  C   . ALA E  227 ? 2.3708 2.2584 2.2693 0.4658  -0.0541 -0.3279 227  ALA E C   
13273 O  O   . ALA E  227 ? 2.3767 2.2035 2.2532 0.4429  -0.0350 -0.3216 227  ALA E O   
13274 C  CB  . ALA E  227 ? 2.3897 2.2463 2.2691 0.5208  -0.0929 -0.2913 227  ALA E CB  
13275 N  N   . VAL E  228 ? 2.3170 2.2879 2.2375 0.4488  -0.0559 -0.3534 228  VAL E N   
13276 C  CA  . VAL E  228 ? 2.4442 2.4359 2.3628 0.3967  -0.0336 -0.3780 228  VAL E CA  
13277 C  C   . VAL E  228 ? 2.5992 2.6208 2.5097 0.3679  -0.0351 -0.3942 228  VAL E C   
13278 O  O   . VAL E  228 ? 2.6359 2.7055 2.5573 0.3901  -0.0560 -0.3933 228  VAL E O   
13279 C  CB  . VAL E  228 ? 2.4704 2.5503 2.4245 0.3906  -0.0278 -0.4019 228  VAL E CB  
13280 C  CG1 . VAL E  228 ? 2.4850 2.5320 2.4440 0.4138  -0.0227 -0.3900 228  VAL E CG1 
13281 C  CG2 . VAL E  228 ? 2.4860 2.6737 2.4760 0.4195  -0.0496 -0.4153 228  VAL E CG2 
13282 N  N   . GLY E  229 ? 2.6694 2.6600 2.5578 0.3166  -0.0120 -0.4090 229  GLY E N   
13283 C  CA  . GLY E  229 ? 2.7019 2.7090 2.5762 0.2797  -0.0076 -0.4297 229  GLY E CA  
13284 C  C   . GLY E  229 ? 2.7521 2.6808 2.5893 0.2281  0.0213  -0.4384 229  GLY E C   
13285 O  O   . GLY E  229 ? 2.7802 2.6238 2.5963 0.2307  0.0345  -0.4185 229  GLY E O   
13286 N  N   . ASP E  230 ? 2.7935 2.7496 2.6201 0.1804  0.0319  -0.4677 230  ASP E N   
13287 C  CA  . ASP E  230 ? 2.9775 2.8503 2.7627 0.1279  0.0607  -0.4785 230  ASP E CA  
13288 C  C   . ASP E  230 ? 3.1251 2.9004 2.8725 0.1363  0.0635  -0.4680 230  ASP E C   
13289 O  O   . ASP E  230 ? 3.2429 3.0519 2.9945 0.1496  0.0481  -0.4745 230  ASP E O   
13290 C  CB  . ASP E  230 ? 3.1104 3.0559 2.8976 0.0666  0.0730  -0.5188 230  ASP E CB  
13291 C  CG  . ASP E  230 ? 3.2028 3.0564 2.9441 0.0072  0.1054  -0.5296 230  ASP E CG  
13292 O  OD1 . ASP E  230 ? 3.1841 2.9327 2.8995 0.0167  0.1179  -0.5036 230  ASP E OD1 
13293 O  OD2 . ASP E  230 ? 3.2700 3.1554 2.9985 -0.0499 0.1184  -0.5636 230  ASP E OD2 
13294 N  N   . PHE E  231 ? 3.0853 2.7449 2.7952 0.1298  0.0832  -0.4516 231  PHE E N   
13295 C  CA  . PHE E  231 ? 3.0081 2.5763 2.6834 0.1469  0.0860  -0.4398 231  PHE E CA  
13296 C  C   . PHE E  231 ? 3.0327 2.4924 2.6590 0.1077  0.1162  -0.4476 231  PHE E C   
13297 O  O   . PHE E  231 ? 3.0200 2.4230 2.6163 0.1024  0.1234  -0.4580 231  PHE E O   
13298 C  CB  . PHE E  231 ? 2.9488 2.4766 2.6263 0.2030  0.0735  -0.4006 231  PHE E CB  
13299 C  CG  . PHE E  231 ? 2.8565 2.4639 2.5697 0.2446  0.0438  -0.3906 231  PHE E CG  
13300 C  CD1 . PHE E  231 ? 2.7960 2.4226 2.5074 0.2623  0.0277  -0.3926 231  PHE E CD1 
13301 C  CD2 . PHE E  231 ? 2.8276 2.4885 2.5735 0.2657  0.0324  -0.3798 231  PHE E CD2 
13302 C  CE1 . PHE E  231 ? 2.7382 2.4301 2.4767 0.2995  0.0003  -0.3797 231  PHE E CE1 
13303 C  CE2 . PHE E  231 ? 2.7763 2.4973 2.5497 0.3058  0.0057  -0.3693 231  PHE E CE2 
13304 C  CZ  . PHE E  231 ? 2.7484 2.4825 2.5167 0.3222  -0.0106 -0.3673 231  PHE E CZ  
13305 N  N   . ASN E  232 ? 3.0637 2.4909 2.6793 0.0808  0.1345  -0.4424 232  ASN E N   
13306 C  CA  . ASN E  232 ? 3.1190 2.4356 2.6835 0.0413  0.1642  -0.4468 232  ASN E CA  
13307 C  C   . ASN E  232 ? 3.1151 2.4579 2.6669 -0.0282 0.1805  -0.4886 232  ASN E C   
13308 O  O   . ASN E  232 ? 3.1748 2.4265 2.6815 -0.0718 0.2075  -0.4946 232  ASN E O   
13309 C  CB  . ASN E  232 ? 3.0581 2.3226 2.6106 0.0426  0.1767  -0.4174 232  ASN E CB  
13310 C  CG  . ASN E  232 ? 3.0523 2.4191 2.6443 0.0275  0.1708  -0.4224 232  ASN E CG  
13311 O  OD1 . ASN E  232 ? 3.0335 2.5133 2.6685 0.0344  0.1521  -0.4402 232  ASN E OD1 
13312 N  ND2 . ASN E  232 ? 3.0833 2.4129 2.6598 0.0084  0.1870  -0.4062 232  ASN E ND2 
13313 N  N   . GLY E  233 ? 3.1232 2.5874 2.7106 -0.0404 0.1650  -0.5168 233  GLY E N   
13314 C  CA  . GLY E  233 ? 3.1638 2.6684 2.7397 -0.1079 0.1788  -0.5599 233  GLY E CA  
13315 C  C   . GLY E  233 ? 3.3309 2.8378 2.8942 -0.1678 0.2008  -0.5708 233  GLY E C   
13316 O  O   . GLY E  233 ? 3.4289 2.8679 2.9465 -0.2287 0.2271  -0.5928 233  GLY E O   
13317 N  N   . ASP E  234 ? 3.3333 2.9157 2.9339 -0.1537 0.1916  -0.5568 234  ASP E N   
13318 C  CA  . ASP E  234 ? 3.3579 2.9607 2.9506 -0.2107 0.2111  -0.5668 234  ASP E CA  
13319 C  C   . ASP E  234 ? 3.2439 3.0194 2.8908 -0.2227 0.1976  -0.5900 234  ASP E C   
13320 O  O   . ASP E  234 ? 3.2324 3.0600 2.8718 -0.2898 0.2139  -0.6184 234  ASP E O   
13321 C  CB  . ASP E  234 ? 3.3781 2.8953 2.9547 -0.1900 0.2203  -0.5270 234  ASP E CB  
13322 C  CG  . ASP E  234 ? 3.3875 2.9828 3.0160 -0.1293 0.1967  -0.5040 234  ASP E CG  
13323 O  OD1 . ASP E  234 ? 3.4195 3.0766 3.0842 -0.0798 0.1713  -0.5034 234  ASP E OD1 
13324 O  OD2 . ASP E  234 ? 3.3635 2.9572 2.9943 -0.1332 0.2043  -0.4871 234  ASP E OD2 
13325 N  N   . GLY E  235 ? 3.2133 3.0795 2.9127 -0.1599 0.1687  -0.5791 235  GLY E N   
13326 C  CA  . GLY E  235 ? 3.1845 3.2167 2.9369 -0.1604 0.1543  -0.6006 235  GLY E CA  
13327 C  C   . GLY E  235 ? 3.0826 3.1578 2.8746 -0.1064 0.1402  -0.5769 235  GLY E C   
13328 O  O   . GLY E  235 ? 3.0459 3.2552 2.8870 -0.0854 0.1237  -0.5899 235  GLY E O   
13329 N  N   . ILE E  236 ? 3.1589 3.1230 2.9289 -0.0830 0.1474  -0.5430 236  ILE E N   
13330 C  CA  . ILE E  236 ? 3.1130 3.1027 2.9140 -0.0344 0.1366  -0.5206 236  ILE E CA  
13331 C  C   . ILE E  236 ? 3.0836 3.0445 2.8985 0.0386  0.1119  -0.4952 236  ILE E C   
13332 O  O   . ILE E  236 ? 3.0608 2.9146 2.8425 0.0524  0.1137  -0.4749 236  ILE E O   
13333 C  CB  . ILE E  236 ? 3.0983 2.9961 2.8665 -0.0546 0.1585  -0.4981 236  ILE E CB  
13334 C  CG1 . ILE E  236 ? 3.1407 3.0601 2.8877 -0.1341 0.1841  -0.5218 236  ILE E CG1 
13335 C  CG2 . ILE E  236 ? 3.0475 2.9790 2.8477 -0.0073 0.1482  -0.4791 236  ILE E CG2 
13336 C  CD1 . ILE E  236 ? 3.1037 3.1857 2.8978 -0.1515 0.1792  -0.5534 236  ILE E CD1 
13337 N  N   . ASP E  237 ? 3.0952 3.1517 2.9573 0.0851  0.0895  -0.4966 237  ASP E N   
13338 C  CA  . ASP E  237 ? 2.9984 3.0289 2.8715 0.1513  0.0659  -0.4715 237  ASP E CA  
13339 C  C   . ASP E  237 ? 2.9293 2.8478 2.7769 0.1737  0.0725  -0.4371 237  ASP E C   
13340 O  O   . ASP E  237 ? 2.9559 2.8700 2.8062 0.1686  0.0834  -0.4306 237  ASP E O   
13341 C  CB  . ASP E  237 ? 2.9562 3.0977 2.8800 0.1966  0.0439  -0.4776 237  ASP E CB  
13342 C  CG  . ASP E  237 ? 2.9777 3.2234 2.9262 0.1988  0.0272  -0.5000 237  ASP E CG  
13343 O  OD1 . ASP E  237 ? 3.1184 3.3671 3.0471 0.1523  0.0364  -0.5186 237  ASP E OD1 
13344 O  OD2 . ASP E  237 ? 2.8798 3.2040 2.8653 0.2472  0.0053  -0.4992 237  ASP E OD2 
13345 N  N   . ASP E  238 ? 2.8028 2.6395 2.6253 0.1973  0.0661  -0.4160 238  ASP E N   
13346 C  CA  . ASP E  238 ? 2.8443 2.5812 2.6402 0.2192  0.0715  -0.3829 238  ASP E CA  
13347 C  C   . ASP E  238 ? 2.9538 2.6993 2.7688 0.2774  0.0489  -0.3619 238  ASP E C   
13348 O  O   . ASP E  238 ? 2.9660 2.7733 2.8070 0.3042  0.0279  -0.3688 238  ASP E O   
13349 C  CB  . ASP E  238 ? 2.9143 2.5536 2.6659 0.2059  0.0820  -0.3739 238  ASP E CB  
13350 C  CG  . ASP E  238 ? 3.0438 2.6554 2.7684 0.1457  0.1068  -0.3943 238  ASP E CG  
13351 O  OD1 . ASP E  238 ? 3.0433 2.6574 2.7646 0.1160  0.1229  -0.3957 238  ASP E OD1 
13352 O  OD2 . ASP E  238 ? 3.1116 2.6982 2.8157 0.1253  0.1110  -0.4099 238  ASP E OD2 
13353 N  N   . PHE E  239 ? 3.0119 2.6935 2.8104 0.2953  0.0537  -0.3349 239  PHE E N   
13354 C  CA  . PHE E  239 ? 2.8937 2.5780 2.7056 0.3417  0.0371  -0.3163 239  PHE E CA  
13355 C  C   . PHE E  239 ? 2.6887 2.3100 2.4756 0.3681  0.0267  -0.2918 239  PHE E C   
13356 O  O   . PHE E  239 ? 2.4084 1.9588 2.1626 0.3606  0.0391  -0.2748 239  PHE E O   
13357 C  CB  . PHE E  239 ? 2.8533 2.5239 2.6644 0.3404  0.0494  -0.3058 239  PHE E CB  
13358 C  CG  . PHE E  239 ? 2.8755 2.6115 2.7090 0.3111  0.0617  -0.3300 239  PHE E CG  
13359 C  CD1 . PHE E  239 ? 2.8160 2.6444 2.6851 0.3114  0.0523  -0.3581 239  PHE E CD1 
13360 C  CD2 . PHE E  239 ? 2.9680 2.6806 2.7862 0.2832  0.0825  -0.3238 239  PHE E CD2 
13361 C  CE1 . PHE E  239 ? 2.7879 2.6880 2.6781 0.2834  0.0641  -0.3822 239  PHE E CE1 
13362 C  CE2 . PHE E  239 ? 3.0458 2.8245 2.8828 0.2525  0.0944  -0.3465 239  PHE E CE2 
13363 C  CZ  . PHE E  239 ? 2.9131 2.7877 2.7868 0.2521  0.0855  -0.3770 239  PHE E CZ  
13364 N  N   . VAL E  240 ? 2.6304 2.2809 2.4314 0.3998  0.0040  -0.2892 240  VAL E N   
13365 C  CA  . VAL E  240 ? 2.4331 2.0387 2.2128 0.4251  -0.0085 -0.2664 240  VAL E CA  
13366 C  C   . VAL E  240 ? 2.4134 2.0148 2.1991 0.4586  -0.0211 -0.2484 240  VAL E C   
13367 O  O   . VAL E  240 ? 2.5133 2.1626 2.3264 0.4754  -0.0318 -0.2577 240  VAL E O   
13368 C  CB  . VAL E  240 ? 2.4313 2.0700 2.2152 0.4298  -0.0247 -0.2759 240  VAL E CB  
13369 C  CG1 . VAL E  240 ? 2.4533 2.0483 2.2118 0.4507  -0.0356 -0.2530 240  VAL E CG1 
13370 C  CG2 . VAL E  240 ? 2.5528 2.2018 2.3314 0.3912  -0.0106 -0.3005 240  VAL E CG2 
13371 N  N   . SER E  241 ? 2.4551 2.0003 2.2136 0.4687  -0.0197 -0.2237 241  SER E N   
13372 C  CA  . SER E  241 ? 2.4050 1.9384 2.1621 0.4927  -0.0286 -0.2077 241  SER E CA  
13373 C  C   . SER E  241 ? 2.5189 2.0089 2.2449 0.5044  -0.0356 -0.1825 241  SER E C   
13374 O  O   . SER E  241 ? 2.8235 2.2815 2.5264 0.4943  -0.0249 -0.1731 241  SER E O   
13375 C  CB  . SER E  241 ? 2.3135 1.8393 2.0728 0.4832  -0.0120 -0.2075 241  SER E CB  
13376 O  OG  . SER E  241 ? 2.2888 1.8055 2.0469 0.5036  -0.0198 -0.1978 241  SER E OG  
13377 N  N   . GLY E  242 ? 2.2786 1.7678 2.0024 0.5262  -0.0531 -0.1716 242  GLY E N   
13378 C  CA  . GLY E  242 ? 2.3414 1.7970 2.0343 0.5335  -0.0600 -0.1479 242  GLY E CA  
13379 C  C   . GLY E  242 ? 2.2244 1.6519 1.8999 0.5291  -0.0481 -0.1341 242  GLY E C   
13380 O  O   . GLY E  242 ? 2.1919 1.6226 1.8789 0.5292  -0.0425 -0.1405 242  GLY E O   
13381 N  N   . VAL E  243 ? 2.3557 1.7623 2.0033 0.5254  -0.0437 -0.1165 243  VAL E N   
13382 C  CA  . VAL E  243 ? 2.3649 1.7553 1.9920 0.5207  -0.0337 -0.1005 243  VAL E CA  
13383 C  C   . VAL E  243 ? 2.3810 1.7636 1.9802 0.5262  -0.0459 -0.0815 243  VAL E C   
13384 O  O   . VAL E  243 ? 2.3000 1.6818 1.8788 0.5258  -0.0420 -0.0688 243  VAL E O   
13385 C  CB  . VAL E  243 ? 2.4354 1.8170 2.0538 0.5112  -0.0145 -0.0956 243  VAL E CB  
13386 C  CG1 . VAL E  243 ? 2.6500 2.0296 2.2558 0.5049  -0.0028 -0.0829 243  VAL E CG1 
13387 C  CG2 . VAL E  243 ? 2.2840 1.6709 1.9245 0.5008  -0.0048 -0.1155 243  VAL E CG2 
13388 N  N   . PRO E  244 ? 2.3743 1.7505 1.9697 0.5315  -0.0602 -0.0789 244  PRO E N   
13389 C  CA  . PRO E  244 ? 2.3677 1.7384 1.9357 0.5329  -0.0748 -0.0621 244  PRO E CA  
13390 C  C   . PRO E  244 ? 2.4209 1.7906 1.9573 0.5217  -0.0682 -0.0442 244  PRO E C   
13391 O  O   . PRO E  244 ? 2.5569 1.9341 2.0699 0.5197  -0.0771 -0.0309 244  PRO E O   
13392 C  CB  . PRO E  244 ? 2.3172 1.6704 1.8869 0.5409  -0.0895 -0.0634 244  PRO E CB  
13393 C  CG  . PRO E  244 ? 2.3113 1.6587 1.9011 0.5418  -0.0785 -0.0784 244  PRO E CG  
13394 C  CD  . PRO E  244 ? 2.3330 1.7046 1.9471 0.5376  -0.0637 -0.0916 244  PRO E CD  
13395 N  N   . ARG E  245 ? 2.4763 1.8454 2.0104 0.5129  -0.0533 -0.0435 245  ARG E N   
13396 C  CA  . ARG E  245 ? 2.5891 1.9702 2.0934 0.5014  -0.0473 -0.0267 245  ARG E CA  
13397 C  C   . ARG E  245 ? 2.7399 2.1424 2.2421 0.5056  -0.0335 -0.0190 245  ARG E C   
13398 O  O   . ARG E  245 ? 2.8967 2.3217 2.3760 0.5000  -0.0282 -0.0039 245  ARG E O   
13399 C  CB  . ARG E  245 ? 2.6187 1.9907 2.1148 0.4868  -0.0404 -0.0289 245  ARG E CB  
13400 C  CG  . ARG E  245 ? 2.6595 2.0005 2.1407 0.4815  -0.0535 -0.0302 245  ARG E CG  
13401 C  CD  . ARG E  245 ? 2.6799 2.0095 2.1429 0.4621  -0.0442 -0.0329 245  ARG E CD  
13402 N  NE  . ARG E  245 ? 2.7470 2.1087 2.1806 0.4424  -0.0368 -0.0177 245  ARG E NE  
13403 C  CZ  . ARG E  245 ? 2.9745 2.3377 2.3722 0.4251  -0.0441 -0.0047 245  ARG E CZ  
13404 N  NH1 . ARG E  245 ? 2.9663 2.2908 2.3499 0.4245  -0.0592 -0.0027 245  ARG E NH1 
13405 N  NH2 . ARG E  245 ? 3.2848 2.6923 2.6590 0.4076  -0.0365 0.0075  245  ARG E NH2 
13406 N  N   . ALA E  246 ? 2.6402 2.0362 2.1632 0.5152  -0.0272 -0.0287 246  ALA E N   
13407 C  CA  . ALA E  246 ? 2.5982 1.9998 2.1146 0.5227  -0.0137 -0.0202 246  ALA E CA  
13408 C  C   . ALA E  246 ? 2.6351 2.0531 2.1306 0.5337  -0.0196 -0.0088 246  ALA E C   
13409 O  O   . ALA E  246 ? 2.5761 2.0013 2.0652 0.5328  -0.0344 -0.0098 246  ALA E O   
13410 C  CB  . ALA E  246 ? 2.5829 1.9636 2.1208 0.5257  -0.0055 -0.0351 246  ALA E CB  
13411 N  N   . ALA E  247 ? 2.8403 2.2660 2.3240 0.5458  -0.0074 0.0028  247  ALA E N   
13412 C  CA  . ALA E  247 ? 2.8549 2.3026 2.3197 0.5617  -0.0099 0.0119  247  ALA E CA  
13413 C  C   . ALA E  247 ? 2.7361 2.2238 2.1812 0.5515  -0.0219 0.0225  247  ALA E C   
13414 O  O   . ALA E  247 ? 2.5573 2.0629 1.9926 0.5549  -0.0323 0.0218  247  ALA E O   
13415 C  CB  . ALA E  247 ? 2.7060 2.1346 2.1789 0.5711  -0.0145 -0.0042 247  ALA E CB  
13416 N  N   . ARG E  248 ? 2.8583 2.3616 2.2950 0.5351  -0.0195 0.0314  248  ARG E N   
13417 C  CA  . ARG E  248 ? 2.8754 2.4146 2.2875 0.5177  -0.0280 0.0413  248  ARG E CA  
13418 C  C   . ARG E  248 ? 2.9544 2.4746 2.3638 0.5056  -0.0452 0.0337  248  ARG E C   
13419 O  O   . ARG E  248 ? 3.0777 2.6246 2.4686 0.5024  -0.0549 0.0398  248  ARG E O   
13420 C  CB  . ARG E  248 ? 2.9228 2.5179 2.3142 0.5304  -0.0254 0.0560  248  ARG E CB  
13421 C  CG  . ARG E  248 ? 2.9061 2.5392 2.2887 0.5348  -0.0117 0.0711  248  ARG E CG  
13422 C  CD  . ARG E  248 ? 2.9718 2.5721 2.3717 0.5558  0.0021  0.0717  248  ARG E CD  
13423 N  NE  . ARG E  248 ? 3.0266 2.6344 2.4224 0.5904  0.0082  0.0790  248  ARG E NE  
13424 C  CZ  . ARG E  248 ? 3.1654 2.8244 2.5452 0.6098  0.0150  0.0979  248  ARG E CZ  
13425 N  NH1 . ARG E  248 ? 3.3378 3.0531 2.7046 0.5931  0.0163  0.1112  248  ARG E NH1 
13426 N  NH2 . ARG E  248 ? 3.1486 2.8049 2.5244 0.6468  0.0208  0.1025  248  ARG E NH2 
13427 N  N   . THR E  249 ? 2.6760 2.1535 2.1038 0.5003  -0.0491 0.0213  249  THR E N   
13428 C  CA  . THR E  249 ? 2.6360 2.0880 2.0637 0.4941  -0.0657 0.0158  249  THR E CA  
13429 C  C   . THR E  249 ? 2.5034 1.9606 1.9391 0.5082  -0.0754 0.0109  249  THR E C   
13430 O  O   . THR E  249 ? 2.5248 1.9713 1.9560 0.5041  -0.0911 0.0108  249  THR E O   
13431 C  CB  . THR E  249 ? 2.6797 2.1370 2.0731 0.4705  -0.0745 0.0276  249  THR E CB  
13432 O  OG1 . THR E  249 ? 2.6552 2.1590 2.0258 0.4679  -0.0777 0.0395  249  THR E OG1 
13433 C  CG2 . THR E  249 ? 2.7285 2.1852 2.1102 0.4518  -0.0632 0.0294  249  THR E CG2 
13434 N  N   . LEU E  250 ? 2.3948 1.8647 1.8404 0.5248  -0.0662 0.0064  250  LEU E N   
13435 C  CA  . LEU E  250 ? 2.3760 1.8470 1.8312 0.5358  -0.0730 -0.0045 250  LEU E CA  
13436 C  C   . LEU E  250 ? 2.3419 1.7845 1.8253 0.5371  -0.0770 -0.0210 250  LEU E C   
13437 O  O   . LEU E  250 ? 2.3500 1.7978 1.8397 0.5392  -0.0890 -0.0290 250  LEU E O   
13438 C  CB  . LEU E  250 ? 2.4019 1.8829 1.8572 0.5537  -0.0593 -0.0079 250  LEU E CB  
13439 C  CG  . LEU E  250 ? 2.7466 2.2539 2.1912 0.5634  -0.0646 -0.0123 250  LEU E CG  
13440 C  CD1 . LEU E  250 ? 2.8840 2.4307 2.3043 0.5507  -0.0790 0.0011  250  LEU E CD1 
13441 C  CD2 . LEU E  250 ? 2.9431 2.4557 2.3814 0.5856  -0.0481 -0.0123 250  LEU E CD2 
13442 N  N   . GLY E  251 ? 2.2310 1.6526 1.7315 0.5351  -0.0672 -0.0268 251  GLY E N   
13443 C  CA  . GLY E  251 ? 2.2236 1.6300 1.7528 0.5363  -0.0691 -0.0442 251  GLY E CA  
13444 C  C   . GLY E  251 ? 2.2142 1.6165 1.7583 0.5408  -0.0577 -0.0594 251  GLY E C   
13445 O  O   . GLY E  251 ? 2.2104 1.6195 1.7442 0.5465  -0.0567 -0.0610 251  GLY E O   
13446 N  N   . MET E  252 ? 2.3368 1.7273 1.9031 0.5362  -0.0482 -0.0725 252  MET E N   
13447 C  CA  . MET E  252 ? 2.3461 1.7258 1.9230 0.5332  -0.0356 -0.0884 252  MET E CA  
13448 C  C   . MET E  252 ? 2.2826 1.6713 1.8891 0.5247  -0.0376 -0.1083 252  MET E C   
13449 O  O   . MET E  252 ? 2.2527 1.6525 1.8723 0.5264  -0.0464 -0.1087 252  MET E O   
13450 C  CB  . MET E  252 ? 2.2870 1.6437 1.8527 0.5328  -0.0149 -0.0800 252  MET E CB  
13451 C  CG  . MET E  252 ? 2.4085 1.7644 1.9466 0.5464  -0.0111 -0.0618 252  MET E CG  
13452 S  SD  . MET E  252 ? 2.4718 1.7982 1.9963 0.5516  0.0127  -0.0495 252  MET E SD  
13453 C  CE  . MET E  252 ? 2.4873 1.7727 2.0151 0.5471  0.0241  -0.0720 252  MET E CE  
13454 N  N   . VAL E  253 ? 2.3016 1.6861 1.9169 0.5154  -0.0284 -0.1266 253  VAL E N   
13455 C  CA  . VAL E  253 ? 2.2632 1.6661 1.9062 0.5030  -0.0268 -0.1480 253  VAL E CA  
13456 C  C   . VAL E  253 ? 2.5594 1.9357 2.1986 0.4853  -0.0041 -0.1567 253  VAL E C   
13457 O  O   . VAL E  253 ? 2.7090 2.0581 2.3308 0.4810  0.0054  -0.1608 253  VAL E O   
13458 C  CB  . VAL E  253 ? 2.2082 1.6447 1.8646 0.5021  -0.0413 -0.1649 253  VAL E CB  
13459 C  CG1 . VAL E  253 ? 2.2657 1.7289 1.9480 0.4847  -0.0352 -0.1904 253  VAL E CG1 
13460 C  CG2 . VAL E  253 ? 2.1757 1.6361 1.8368 0.5194  -0.0643 -0.1537 253  VAL E CG2 
13461 N  N   . TYR E  254 ? 2.6068 1.9875 2.2593 0.4747  0.0054  -0.1596 254  TYR E N   
13462 C  CA  . TYR E  254 ? 2.5003 1.8552 2.1465 0.4535  0.0271  -0.1652 254  TYR E CA  
13463 C  C   . TYR E  254 ? 2.4483 1.8334 2.1173 0.4302  0.0297  -0.1940 254  TYR E C   
13464 O  O   . TYR E  254 ? 2.3517 1.7873 2.0492 0.4328  0.0181  -0.2062 254  TYR E O   
13465 C  CB  . TYR E  254 ? 2.3489 1.6987 1.9934 0.4510  0.0374  -0.1507 254  TYR E CB  
13466 C  CG  . TYR E  254 ? 2.4638 1.7929 2.0841 0.4691  0.0377  -0.1224 254  TYR E CG  
13467 C  CD1 . TYR E  254 ? 2.6145 1.9223 2.2122 0.4853  0.0342  -0.1104 254  TYR E CD1 
13468 C  CD2 . TYR E  254 ? 2.4696 1.8096 2.0900 0.4690  0.0417  -0.1097 254  TYR E CD2 
13469 C  CE1 . TYR E  254 ? 2.7015 2.0046 2.2783 0.5014  0.0343  -0.0854 254  TYR E CE1 
13470 C  CE2 . TYR E  254 ? 2.5445 1.8775 2.1426 0.4822  0.0420  -0.0850 254  TYR E CE2 
13471 C  CZ  . TYR E  254 ? 2.6617 1.9790 2.2385 0.4987  0.0380  -0.0724 254  TYR E CZ  
13472 O  OH  . TYR E  254 ? 2.5688 1.8924 2.1243 0.5112  0.0382  -0.0487 254  TYR E OH  
13473 N  N   . ILE E  255 ? 2.5869 1.9410 2.2411 0.4071  0.0459  -0.2051 255  ILE E N   
13474 C  CA  . ILE E  255 ? 2.6198 2.0030 2.2900 0.3754  0.0527  -0.2335 255  ILE E CA  
13475 C  C   . ILE E  255 ? 2.5593 1.9097 2.2160 0.3480  0.0758  -0.2308 255  ILE E C   
13476 O  O   . ILE E  255 ? 2.6154 1.8973 2.2384 0.3455  0.0908  -0.2156 255  ILE E O   
13477 C  CB  . ILE E  255 ? 2.7763 2.1527 2.4368 0.3618  0.0530  -0.2538 255  ILE E CB  
13478 C  CG1 . ILE E  255 ? 2.7248 2.1475 2.4009 0.3858  0.0285  -0.2563 255  ILE E CG1 
13479 C  CG2 . ILE E  255 ? 2.7584 2.1637 2.4295 0.3205  0.0642  -0.2838 255  ILE E CG2 
13480 C  CD1 . ILE E  255 ? 2.7287 2.1692 2.4024 0.3680  0.0270  -0.2819 255  ILE E CD1 
13481 N  N   . TYR E  256 ? 2.5290 1.9298 2.2105 0.3295  0.0785  -0.2446 256  TYR E N   
13482 C  CA  . TYR E  256 ? 2.8135 2.1961 2.4838 0.2976  0.0998  -0.2436 256  TYR E CA  
13483 C  C   . TYR E  256 ? 2.8927 2.3136 2.5741 0.2551  0.1085  -0.2757 256  TYR E C   
13484 O  O   . TYR E  256 ? 2.9210 2.4150 2.6341 0.2560  0.0950  -0.2991 256  TYR E O   
13485 C  CB  . TYR E  256 ? 2.8129 2.2292 2.5002 0.3075  0.0988  -0.2325 256  TYR E CB  
13486 C  CG  . TYR E  256 ? 2.6803 2.0613 2.3514 0.3397  0.0944  -0.2010 256  TYR E CG  
13487 C  CD1 . TYR E  256 ? 2.6939 2.0207 2.3328 0.3347  0.1103  -0.1755 256  TYR E CD1 
13488 C  CD2 . TYR E  256 ? 2.4612 1.8655 2.1466 0.3735  0.0745  -0.1957 256  TYR E CD2 
13489 C  CE1 . TYR E  256 ? 2.6721 1.9805 2.2967 0.3626  0.1062  -0.1475 256  TYR E CE1 
13490 C  CE2 . TYR E  256 ? 2.4850 1.8643 2.1535 0.3965  0.0715  -0.1690 256  TYR E CE2 
13491 C  CZ  . TYR E  256 ? 2.6230 1.9604 2.2628 0.3910  0.0873  -0.1459 256  TYR E CZ  
13492 O  OH  . TYR E  256 ? 2.6069 1.9327 2.2303 0.4126  0.0842  -0.1200 256  TYR E OH  
13493 N  N   . ASP E  257 ? 2.9047 2.2773 2.5572 0.2168  0.1313  -0.2755 257  ASP E N   
13494 C  CA  . ASP E  257 ? 2.9313 2.3409 2.5890 0.1666  0.1430  -0.3058 257  ASP E CA  
13495 C  C   . ASP E  257 ? 2.8666 2.3737 2.5639 0.1587  0.1391  -0.3198 257  ASP E C   
13496 O  O   . ASP E  257 ? 2.8816 2.3937 2.5841 0.1715  0.1410  -0.3025 257  ASP E O   
13497 C  CB  . ASP E  257 ? 3.1424 2.4654 2.7529 0.1255  0.1698  -0.2979 257  ASP E CB  
13498 C  CG  . ASP E  257 ? 3.3073 2.6631 2.9157 0.0646  0.1841  -0.3303 257  ASP E CG  
13499 O  OD1 . ASP E  257 ? 3.2305 2.6544 2.8636 0.0552  0.1741  -0.3611 257  ASP E OD1 
13500 O  OD2 . ASP E  257 ? 3.4875 2.8053 3.0680 0.0242  0.2053  -0.3241 257  ASP E OD2 
13501 N  N   . GLY E  258 ? 2.8423 2.4333 2.5678 0.1380  0.1340  -0.3531 258  GLY E N   
13502 C  CA  . GLY E  258 ? 2.8718 2.5685 2.6392 0.1364  0.1289  -0.3712 258  GLY E CA  
13503 C  C   . GLY E  258 ? 2.8650 2.5837 2.6243 0.0828  0.1512  -0.3823 258  GLY E C   
13504 O  O   . GLY E  258 ? 2.8702 2.6922 2.6639 0.0697  0.1499  -0.4072 258  GLY E O   
13505 N  N   . LYS E  259 ? 2.7842 2.4087 2.4967 0.0523  0.1718  -0.3634 259  LYS E N   
13506 C  CA  . LYS E  259 ? 2.8610 2.4926 2.5563 -0.0035 0.1944  -0.3684 259  LYS E CA  
13507 C  C   . LYS E  259 ? 2.9216 2.4938 2.5921 0.0021  0.2055  -0.3335 259  LYS E C   
13508 O  O   . LYS E  259 ? 3.0038 2.6301 2.6843 -0.0213 0.2146  -0.3372 259  LYS E O   
13509 C  CB  . LYS E  259 ? 2.9303 2.5022 2.5833 -0.0606 0.2132  -0.3804 259  LYS E CB  
13510 C  CG  . LYS E  259 ? 3.0517 2.6439 2.6861 -0.1296 0.2365  -0.3918 259  LYS E CG  
13511 C  CD  . LYS E  259 ? 3.2639 2.7715 2.8459 -0.1870 0.2570  -0.4008 259  LYS E CD  
13512 C  CE  . LYS E  259 ? 3.3776 2.7271 2.9033 -0.1720 0.2681  -0.3623 259  LYS E CE  
13513 N  NZ  . LYS E  259 ? 3.5020 2.7516 2.9699 -0.2276 0.2909  -0.3710 259  LYS E NZ  
13514 N  N   . ASN E  260 ? 2.9750 2.4460 2.6137 0.0330  0.2049  -0.2997 260  ASN E N   
13515 C  CA  . ASN E  260 ? 3.0629 2.4824 2.6755 0.0392  0.2150  -0.2638 260  ASN E CA  
13516 C  C   . ASN E  260 ? 3.0101 2.4017 2.6267 0.0999  0.1997  -0.2363 260  ASN E C   
13517 O  O   . ASN E  260 ? 3.1315 2.4721 2.7207 0.1093  0.2073  -0.2028 260  ASN E O   
13518 C  CB  . ASN E  260 ? 3.2365 2.5465 2.7889 0.0023  0.2379  -0.2430 260  ASN E CB  
13519 C  CG  . ASN E  260 ? 3.3124 2.5295 2.8349 0.0166  0.2375  -0.2396 260  ASN E CG  
13520 O  OD1 . ASN E  260 ? 2.9842 2.2055 2.5249 0.0633  0.2195  -0.2395 260  ASN E OD1 
13521 N  ND2 . ASN E  260 ? 4.1708 3.3008 3.6443 -0.0255 0.2585  -0.2375 260  ASN E ND2 
13522 N  N   . MET E  261 ? 2.9169 2.3427 2.5641 0.1389  0.1786  -0.2483 261  MET E N   
13523 C  CA  . MET E  261 ? 2.8338 2.2445 2.4860 0.1914  0.1633  -0.2258 261  MET E CA  
13524 C  C   . MET E  261 ? 2.9162 2.2264 2.5231 0.2063  0.1700  -0.1926 261  MET E C   
13525 O  O   . MET E  261 ? 2.9876 2.2681 2.5741 0.2174  0.1761  -0.1622 261  MET E O   
13526 C  CB  . MET E  261 ? 2.8159 2.2784 2.4875 0.2019  0.1620  -0.2189 261  MET E CB  
13527 C  CG  . MET E  261 ? 2.7277 2.2034 2.4162 0.2503  0.1430  -0.2100 261  MET E CG  
13528 S  SD  . MET E  261 ? 2.5845 2.1111 2.3114 0.2750  0.1200  -0.2393 261  MET E SD  
13529 C  CE  . MET E  261 ? 2.6001 2.2276 2.3723 0.2725  0.1175  -0.2684 261  MET E CE  
13530 N  N   . SER E  262 ? 2.8039 2.0680 2.3955 0.2076  0.1688  -0.2003 262  SER E N   
13531 C  CA  . SER E  262 ? 2.7700 1.9424 2.3215 0.2288  0.1738  -0.1747 262  SER E CA  
13532 C  C   . SER E  262 ? 2.6866 1.8621 2.2488 0.2613  0.1563  -0.1842 262  SER E C   
13533 O  O   . SER E  262 ? 2.7027 1.9217 2.2880 0.2502  0.1477  -0.2142 262  SER E O   
13534 C  CB  . SER E  262 ? 2.9591 2.0499 2.4676 0.1911  0.1966  -0.1749 262  SER E CB  
13535 O  OG  . SER E  262 ? 3.1032 2.1016 2.5719 0.2183  0.2024  -0.1504 262  SER E OG  
13536 N  N   . SER E  263 ? 2.7712 1.9049 2.3145 0.2999  0.1516  -0.1583 263  SER E N   
13537 C  CA  . SER E  263 ? 2.7813 1.9230 2.3326 0.3307  0.1347  -0.1644 263  SER E CA  
13538 C  C   . SER E  263 ? 2.9695 2.0641 2.5012 0.3158  0.1423  -0.1849 263  SER E C   
13539 O  O   . SER E  263 ? 3.2555 2.2702 2.7491 0.3046  0.1614  -0.1774 263  SER E O   
13540 C  CB  . SER E  263 ? 2.6049 1.7232 2.1393 0.3724  0.1294  -0.1322 263  SER E CB  
13541 O  OG  . SER E  263 ? 2.5330 1.6714 2.0766 0.3993  0.1119  -0.1379 263  SER E OG  
13542 N  N   . LEU E  264 ? 2.8549 1.9970 2.4102 0.3156  0.1277  -0.2109 264  LEU E N   
13543 C  CA  . LEU E  264 ? 2.8105 1.9225 2.3503 0.2973  0.1339  -0.2363 264  LEU E CA  
13544 C  C   . LEU E  264 ? 2.6936 1.7932 2.2256 0.3329  0.1223  -0.2332 264  LEU E C   
13545 O  O   . LEU E  264 ? 2.7205 1.7485 2.2184 0.3375  0.1351  -0.2336 264  LEU E O   
13546 C  CB  . LEU E  264 ? 2.9129 2.0996 2.4835 0.2640  0.1276  -0.2715 264  LEU E CB  
13547 C  CG  . LEU E  264 ? 3.1400 2.3485 2.7168 0.2186  0.1417  -0.2846 264  LEU E CG  
13548 C  CD1 . LEU E  264 ? 3.1634 2.4594 2.7716 0.1910  0.1334  -0.3213 264  LEU E CD1 
13549 C  CD2 . LEU E  264 ? 3.2225 2.3340 2.7519 0.1855  0.1692  -0.2815 264  LEU E CD2 
13550 N  N   . TYR E  265 ? 2.6631 1.8292 2.2235 0.3582  0.0990  -0.2304 265  TYR E N   
13551 C  CA  . TYR E  265 ? 2.8346 2.0033 2.3890 0.3866  0.0864  -0.2292 265  TYR E CA  
13552 C  C   . TYR E  265 ? 2.6567 1.8662 2.2262 0.4204  0.0672  -0.2043 265  TYR E C   
13553 O  O   . TYR E  265 ? 2.4762 1.7238 2.0679 0.4195  0.0603  -0.1969 265  TYR E O   
13554 C  CB  . TYR E  265 ? 3.0507 2.2650 2.6200 0.3697  0.0766  -0.2614 265  TYR E CB  
13555 C  CG  . TYR E  265 ? 3.3784 2.5523 2.9277 0.3314  0.0965  -0.2909 265  TYR E CG  
13556 C  CD1 . TYR E  265 ? 3.5244 2.6298 3.0386 0.3356  0.1095  -0.2984 265  TYR E CD1 
13557 C  CD2 . TYR E  265 ? 3.3936 2.5991 2.9572 0.2896  0.1031  -0.3134 265  TYR E CD2 
13558 C  CE1 . TYR E  265 ? 3.5676 2.6263 3.0583 0.2970  0.1296  -0.3279 265  TYR E CE1 
13559 C  CE2 . TYR E  265 ? 3.4084 2.5766 2.9494 0.2474  0.1226  -0.3420 265  TYR E CE2 
13560 C  CZ  . TYR E  265 ? 3.4143 2.5037 2.9173 0.2501  0.1361  -0.3494 265  TYR E CZ  
13561 O  OH  . TYR E  265 ? 3.2078 2.2507 2.6834 0.2046  0.1573  -0.3803 265  TYR E OH  
13562 N  N   . ASN E  266 ? 2.8843 2.0843 2.4388 0.4486  0.0602  -0.1927 266  ASN E N   
13563 C  CA  . ASN E  266 ? 2.8063 2.0425 2.3678 0.4758  0.0426  -0.1703 266  ASN E CA  
13564 C  C   . ASN E  266 ? 2.7360 2.0069 2.2995 0.4881  0.0249  -0.1771 266  ASN E C   
13565 O  O   . ASN E  266 ? 2.8680 2.1212 2.4167 0.4877  0.0299  -0.1921 266  ASN E O   
13566 C  CB  . ASN E  266 ? 2.8623 2.0641 2.3994 0.4988  0.0516  -0.1416 266  ASN E CB  
13567 C  CG  . ASN E  266 ? 2.6242 1.8177 2.1640 0.4914  0.0610  -0.1254 266  ASN E CG  
13568 O  OD1 . ASN E  266 ? 2.1395 1.3651 1.7036 0.4746  0.0564  -0.1331 266  ASN E OD1 
13569 N  ND2 . ASN E  266 ? 3.2939 2.4494 2.8087 0.5060  0.0742  -0.1028 266  ASN E ND2 
13570 N  N   . PHE E  267 ? 2.4619 1.7796 2.0410 0.4980  0.0049  -0.1662 267  PHE E N   
13571 C  CA  . PHE E  267 ? 2.4298 1.7803 2.0050 0.5115  -0.0135 -0.1626 267  PHE E CA  
13572 C  C   . PHE E  267 ? 2.2203 1.5771 1.7842 0.5298  -0.0207 -0.1338 267  PHE E C   
13573 O  O   . PHE E  267 ? 2.1829 1.5344 1.7517 0.5294  -0.0176 -0.1207 267  PHE E O   
13574 C  CB  . PHE E  267 ? 2.6614 2.0618 2.2608 0.5034  -0.0325 -0.1752 267  PHE E CB  
13575 C  CG  . PHE E  267 ? 2.7814 2.1921 2.3932 0.4812  -0.0262 -0.2053 267  PHE E CG  
13576 C  CD1 . PHE E  267 ? 2.7600 2.1813 2.3625 0.4748  -0.0274 -0.2238 267  PHE E CD1 
13577 C  CD2 . PHE E  267 ? 2.7668 2.1819 2.3979 0.4636  -0.0180 -0.2173 267  PHE E CD2 
13578 C  CE1 . PHE E  267 ? 2.7927 2.2274 2.4041 0.4487  -0.0203 -0.2542 267  PHE E CE1 
13579 C  CE2 . PHE E  267 ? 2.7915 2.2237 2.4322 0.4376  -0.0114 -0.2465 267  PHE E CE2 
13580 C  CZ  . PHE E  267 ? 2.8416 2.2826 2.4717 0.4290  -0.0124 -0.2652 267  PHE E CZ  
13581 N  N   . THR E  268 ? 2.3234 1.6954 1.8700 0.5427  -0.0289 -0.1259 268  THR E N   
13582 C  CA  . THR E  268 ? 2.3099 1.6960 1.8415 0.5551  -0.0354 -0.1004 268  THR E CA  
13583 C  C   . THR E  268 ? 2.3830 1.8084 1.9095 0.5556  -0.0566 -0.0958 268  THR E C   
13584 O  O   . THR E  268 ? 2.5937 2.0353 2.1164 0.5558  -0.0612 -0.1088 268  THR E O   
13585 C  CB  . THR E  268 ? 2.3552 1.7244 1.8635 0.5720  -0.0206 -0.0903 268  THR E CB  
13586 O  OG1 . THR E  268 ? 2.3090 1.6331 1.8177 0.5711  -0.0006 -0.0936 268  THR E OG1 
13587 C  CG2 . THR E  268 ? 2.3132 1.7073 1.8073 0.5801  -0.0254 -0.0642 268  THR E CG2 
13588 N  N   . GLY E  269 ? 2.4293 1.8677 1.9527 0.5534  -0.0687 -0.0777 269  GLY E N   
13589 C  CA  . GLY E  269 ? 2.4510 1.9194 1.9611 0.5515  -0.0880 -0.0674 269  GLY E CA  
13590 C  C   . GLY E  269 ? 2.5606 2.0523 2.0457 0.5583  -0.0859 -0.0603 269  GLY E C   
13591 O  O   . GLY E  269 ? 2.6997 2.1838 2.1762 0.5692  -0.0702 -0.0581 269  GLY E O   
13592 N  N   . GLU E  270 ? 2.6061 2.1306 2.0783 0.5532  -0.1024 -0.0556 270  GLU E N   
13593 C  CA  . GLU E  270 ? 2.5972 2.1575 2.0467 0.5582  -0.1020 -0.0520 270  GLU E CA  
13594 C  C   . GLU E  270 ? 2.5910 2.1799 2.0151 0.5464  -0.1143 -0.0284 270  GLU E C   
13595 O  O   . GLU E  270 ? 2.4817 2.1133 1.8858 0.5471  -0.1160 -0.0248 270  GLU E O   
13596 C  CB  . GLU E  270 ? 2.6148 2.1998 2.0662 0.5579  -0.1080 -0.0710 270  GLU E CB  
13597 C  CG  . GLU E  270 ? 2.7403 2.2976 2.2102 0.5639  -0.0934 -0.0983 270  GLU E CG  
13598 C  CD  . GLU E  270 ? 2.9876 2.5273 2.4474 0.5822  -0.0721 -0.1065 270  GLU E CD  
13599 O  OE1 . GLU E  270 ? 3.0044 2.5625 2.4470 0.5939  -0.0689 -0.0904 270  GLU E OE1 
13600 O  OE2 . GLU E  270 ? 3.1052 2.6124 2.5725 0.5851  -0.0580 -0.1292 270  GLU E OE2 
13601 N  N   . GLN E  271 ? 2.6330 2.1999 2.0556 0.5342  -0.1221 -0.0141 271  GLN E N   
13602 C  CA  . GLN E  271 ? 2.5443 2.1263 1.9374 0.5166  -0.1319 0.0077  271  GLN E CA  
13603 C  C   . GLN E  271 ? 2.5603 2.1093 1.9525 0.5095  -0.1253 0.0171  271  GLN E C   
13604 O  O   . GLN E  271 ? 2.5617 2.0720 1.9762 0.5140  -0.1234 0.0097  271  GLN E O   
13605 C  CB  . GLN E  271 ? 2.5376 2.1207 1.9193 0.5034  -0.1534 0.0162  271  GLN E CB  
13606 C  CG  . GLN E  271 ? 2.5990 2.1920 1.9422 0.4796  -0.1633 0.0394  271  GLN E CG  
13607 C  CD  . GLN E  271 ? 2.8834 2.4694 2.2111 0.4680  -0.1849 0.0517  271  GLN E CD  
13608 O  OE1 . GLN E  271 ? 2.9162 2.4540 2.2402 0.4642  -0.1937 0.0619  271  GLN E OE1 
13609 N  NE2 . GLN E  271 ? 3.0206 2.6548 2.3380 0.4642  -0.1935 0.0509  271  GLN E NE2 
13610 N  N   . MET E  272 ? 2.8010 2.3727 2.1672 0.4966  -0.1212 0.0313  272  MET E N   
13611 C  CA  . MET E  272 ? 3.0080 2.5559 2.3690 0.4851  -0.1137 0.0385  272  MET E CA  
13612 C  C   . MET E  272 ? 3.2334 2.7327 2.5888 0.4709  -0.1257 0.0429  272  MET E C   
13613 O  O   . MET E  272 ? 3.3504 2.8468 2.6840 0.4579  -0.1413 0.0530  272  MET E O   
13614 C  CB  . MET E  272 ? 2.8421 2.4364 2.1719 0.4687  -0.1086 0.0522  272  MET E CB  
13615 C  CG  . MET E  272 ? 2.8346 2.4821 2.1677 0.4893  -0.0970 0.0501  272  MET E CG  
13616 S  SD  . MET E  272 ? 3.0593 2.6882 2.4174 0.5124  -0.0765 0.0450  272  MET E SD  
13617 C  CE  . MET E  272 ? 3.1981 2.8878 2.5500 0.5411  -0.0661 0.0472  272  MET E CE  
13618 N  N   . ALA E  273 ? 3.0573 2.5177 2.4314 0.4749  -0.1182 0.0355  273  ALA E N   
13619 C  CA  . ALA E  273 ? 2.7111 2.1204 2.0797 0.4666  -0.1263 0.0375  273  ALA E CA  
13620 C  C   . ALA E  273 ? 2.5651 1.9562 1.9405 0.4770  -0.1447 0.0380  273  ALA E C   
13621 O  O   . ALA E  273 ? 2.6191 1.9719 1.9745 0.4695  -0.1567 0.0482  273  ALA E O   
13622 C  CB  . ALA E  273 ? 2.8009 2.2008 2.1267 0.4364  -0.1272 0.0521  273  ALA E CB  
13623 N  N   . ALA E  274 ? 2.4616 1.8785 1.8631 0.4946  -0.1467 0.0272  274  ALA E N   
13624 C  CA  . ALA E  274 ? 2.4693 1.8814 1.8829 0.5061  -0.1634 0.0253  274  ALA E CA  
13625 C  C   . ALA E  274 ? 2.4030 1.7885 1.8503 0.5233  -0.1622 0.0113  274  ALA E C   
13626 O  O   . ALA E  274 ? 2.4024 1.7899 1.8635 0.5364  -0.1762 0.0091  274  ALA E O   
13627 C  CB  . ALA E  274 ? 2.7440 2.2020 2.1692 0.5131  -0.1650 0.0159  274  ALA E CB  
13628 N  N   . TYR E  275 ? 2.5050 1.8750 1.9660 0.5236  -0.1458 0.0015  275  TYR E N   
13629 C  CA  . TYR E  275 ? 2.4587 1.8133 1.9533 0.5382  -0.1416 -0.0150 275  TYR E CA  
13630 C  C   . TYR E  275 ? 2.4202 1.8071 1.9481 0.5503  -0.1423 -0.0320 275  TYR E C   
13631 O  O   . TYR E  275 ? 2.4097 1.8008 1.9615 0.5643  -0.1505 -0.0416 275  TYR E O   
13632 C  CB  . TYR E  275 ? 2.4900 1.8054 1.9780 0.5468  -0.1545 -0.0091 275  TYR E CB  
13633 C  CG  . TYR E  275 ? 2.6862 1.9712 2.1817 0.5472  -0.1414 -0.0193 275  TYR E CG  
13634 C  CD1 . TYR E  275 ? 2.6852 1.9438 2.1495 0.5268  -0.1326 -0.0112 275  TYR E CD1 
13635 C  CD2 . TYR E  275 ? 2.9059 2.1971 2.4396 0.5650  -0.1368 -0.0394 275  TYR E CD2 
13636 C  CE1 . TYR E  275 ? 2.5439 1.7787 2.0141 0.5247  -0.1195 -0.0234 275  TYR E CE1 
13637 C  CE2 . TYR E  275 ? 2.8255 2.0951 2.3664 0.5648  -0.1239 -0.0513 275  TYR E CE2 
13638 C  CZ  . TYR E  275 ? 2.5129 1.7526 2.0219 0.5448  -0.1152 -0.0436 275  TYR E CZ  
13639 O  OH  . TYR E  275 ? 2.5021 1.7241 2.0174 0.5425  -0.1015 -0.0582 275  TYR E OH  
13640 N  N   . PHE E  276 ? 2.3882 1.8002 1.9154 0.5450  -0.1336 -0.0365 276  PHE E N   
13641 C  CA  . PHE E  276 ? 2.5117 1.9464 2.0661 0.5496  -0.1280 -0.0567 276  PHE E CA  
13642 C  C   . PHE E  276 ? 2.2192 1.6452 1.8025 0.5519  -0.1153 -0.0731 276  PHE E C   
13643 O  O   . PHE E  276 ? 2.1348 1.5469 1.7164 0.5460  -0.0983 -0.0734 276  PHE E O   
13644 C  CB  . PHE E  276 ? 2.5532 1.9996 2.0959 0.5448  -0.1159 -0.0591 276  PHE E CB  
13645 C  CG  . PHE E  276 ? 2.4367 1.8959 1.9992 0.5451  -0.1082 -0.0815 276  PHE E CG  
13646 C  CD1 . PHE E  276 ? 2.6233 2.1109 2.1871 0.5447  -0.1196 -0.0898 276  PHE E CD1 
13647 C  CD2 . PHE E  276 ? 2.2248 1.6671 1.8010 0.5420  -0.0887 -0.0944 276  PHE E CD2 
13648 C  CE1 . PHE E  276 ? 2.6766 2.1750 2.2550 0.5397  -0.1109 -0.1137 276  PHE E CE1 
13649 C  CE2 . PHE E  276 ? 2.2675 1.7140 1.8562 0.5365  -0.0800 -0.1161 276  PHE E CE2 
13650 C  CZ  . PHE E  276 ? 2.4721 1.9463 2.0618 0.5346  -0.0906 -0.1273 276  PHE E CZ  
13651 N  N   . GLY E  277 ? 2.2785 1.7205 1.8882 0.5603  -0.1234 -0.0863 277  GLY E N   
13652 C  CA  . GLY E  277 ? 2.2483 1.6936 1.8869 0.5615  -0.1125 -0.1038 277  GLY E CA  
13653 C  C   . GLY E  277 ? 2.2354 1.6724 1.8847 0.5765  -0.1215 -0.1031 277  GLY E C   
13654 O  O   . GLY E  277 ? 2.2128 1.6575 1.8862 0.5782  -0.1116 -0.1188 277  GLY E O   
13655 N  N   . PHE E  278 ? 2.5124 1.9316 2.1423 0.5873  -0.1391 -0.0855 278  PHE E N   
13656 C  CA  . PHE E  278 ? 2.6018 2.0012 2.2373 0.6065  -0.1478 -0.0845 278  PHE E CA  
13657 C  C   . PHE E  278 ? 2.5488 1.9913 2.2241 0.6251  -0.1528 -0.1042 278  PHE E C   
13658 O  O   . PHE E  278 ? 2.6032 2.0443 2.2980 0.6383  -0.1478 -0.1170 278  PHE E O   
13659 C  CB  . PHE E  278 ? 2.6989 2.0677 2.3018 0.6141  -0.1673 -0.0598 278  PHE E CB  
13660 C  CG  . PHE E  278 ? 2.8018 2.1364 2.4040 0.6383  -0.1770 -0.0565 278  PHE E CG  
13661 C  CD1 . PHE E  278 ? 2.9088 2.1917 2.4937 0.6343  -0.1670 -0.0559 278  PHE E CD1 
13662 C  CD2 . PHE E  278 ? 2.7325 2.0867 2.3493 0.6663  -0.1958 -0.0542 278  PHE E CD2 
13663 C  CE1 . PHE E  278 ? 2.8833 2.1245 2.4642 0.6587  -0.1742 -0.0552 278  PHE E CE1 
13664 C  CE2 . PHE E  278 ? 2.7119 2.0284 2.3260 0.6951  -0.2045 -0.0499 278  PHE E CE2 
13665 C  CZ  . PHE E  278 ? 2.8375 2.0922 2.4329 0.6918  -0.1931 -0.0514 278  PHE E CZ  
13666 N  N   . SER E  279 ? 2.5237 2.0116 2.2111 0.6258  -0.1624 -0.1087 279  SER E N   
13667 C  CA  . SER E  279 ? 2.3312 1.8770 2.0564 0.6388  -0.1671 -0.1288 279  SER E CA  
13668 C  C   . SER E  279 ? 2.3094 1.8993 2.0462 0.6153  -0.1588 -0.1458 279  SER E C   
13669 O  O   . SER E  279 ? 2.4456 2.0287 2.1606 0.6015  -0.1605 -0.1373 279  SER E O   
13670 C  CB  . SER E  279 ? 2.3794 1.9422 2.1055 0.6685  -0.1926 -0.1159 279  SER E CB  
13671 O  OG  . SER E  279 ? 2.6750 2.2440 2.3776 0.6602  -0.2058 -0.0990 279  SER E OG  
13672 N  N   . VAL E  280 ? 2.0034 1.6385 1.7726 0.6093  -0.1489 -0.1716 280  VAL E N   
13673 C  CA  . VAL E  280 ? 2.0512 1.7242 1.8299 0.5827  -0.1389 -0.1918 280  VAL E CA  
13674 C  C   . VAL E  280 ? 2.0985 1.8505 1.9130 0.5882  -0.1455 -0.2140 280  VAL E C   
13675 O  O   . VAL E  280 ? 2.0806 1.8567 1.9174 0.6127  -0.1518 -0.2173 280  VAL E O   
13676 C  CB  . VAL E  280 ? 2.0526 1.6942 1.8261 0.5553  -0.1123 -0.2022 280  VAL E CB  
13677 C  CG1 . VAL E  280 ? 2.0167 1.5970 1.7545 0.5496  -0.1064 -0.1813 280  VAL E CG1 
13678 C  CG2 . VAL E  280 ? 2.0862 1.7286 1.8788 0.5601  -0.1021 -0.2104 280  VAL E CG2 
13679 N  N   . ALA E  281 ? 1.9697 1.7659 1.7889 0.5654  -0.1435 -0.2309 281  ALA E N   
13680 C  CA  . ALA E  281 ? 2.0307 1.9159 1.8824 0.5628  -0.1484 -0.2549 281  ALA E CA  
13681 C  C   . ALA E  281 ? 2.1231 2.0283 1.9711 0.5192  -0.1321 -0.2800 281  ALA E C   
13682 O  O   . ALA E  281 ? 2.1441 2.0006 1.9635 0.5017  -0.1246 -0.2753 281  ALA E O   
13683 C  CB  . ALA E  281 ? 2.1386 2.0769 1.9977 0.5931  -0.1766 -0.2428 281  ALA E CB  
13684 N  N   . ALA E  282 ? 2.1979 2.1741 2.0729 0.5008  -0.1252 -0.3083 282  ALA E N   
13685 C  CA  . ALA E  282 ? 2.3017 2.2947 2.1703 0.4532  -0.1074 -0.3360 282  ALA E CA  
13686 C  C   . ALA E  282 ? 2.3742 2.4818 2.2701 0.4440  -0.1177 -0.3603 282  ALA E C   
13687 O  O   . ALA E  282 ? 2.4569 2.6339 2.3845 0.4508  -0.1191 -0.3734 282  ALA E O   
13688 C  CB  . ALA E  282 ? 2.3211 2.2739 2.1864 0.4232  -0.0800 -0.3487 282  ALA E CB  
13689 N  N   . THR E  283 ? 2.4475 2.5829 2.3314 0.4281  -0.1243 -0.3680 283  THR E N   
13690 C  CA  . THR E  283 ? 2.6217 2.8736 2.5278 0.4115  -0.1323 -0.3936 283  THR E CA  
13691 C  C   . THR E  283 ? 2.7161 2.9649 2.5964 0.3732  -0.1257 -0.4108 283  THR E C   
13692 O  O   . THR E  283 ? 2.6925 2.8759 2.5450 0.3818  -0.1290 -0.3934 283  THR E O   
13693 C  CB  . THR E  283 ? 2.5853 2.9158 2.5160 0.4612  -0.1636 -0.3751 283  THR E CB  
13694 O  OG1 . THR E  283 ? 2.7266 3.1805 2.6767 0.4445  -0.1725 -0.3987 283  THR E OG1 
13695 C  CG2 . THR E  283 ? 2.3951 2.6689 2.3006 0.4925  -0.1821 -0.3401 283  THR E CG2 
13696 N  N   . ASP E  284 ? 2.7181 3.0399 2.6065 0.3285  -0.1151 -0.4473 284  ASP E N   
13697 C  CA  . ASP E  284 ? 2.7282 3.0563 2.5924 0.2872  -0.1071 -0.4711 284  ASP E CA  
13698 C  C   . ASP E  284 ? 2.6142 3.0199 2.4844 0.3119  -0.1357 -0.4598 284  ASP E C   
13699 O  O   . ASP E  284 ? 2.6222 3.1459 2.5224 0.3238  -0.1538 -0.4640 284  ASP E O   
13700 C  CB  . ASP E  284 ? 2.7770 3.1654 2.6463 0.2276  -0.0870 -0.5149 284  ASP E CB  
13701 C  CG  . ASP E  284 ? 2.8632 3.2566 2.7047 0.1801  -0.0763 -0.5452 284  ASP E CG  
13702 O  OD1 . ASP E  284 ? 2.9452 3.2483 2.7546 0.1843  -0.0713 -0.5363 284  ASP E OD1 
13703 O  OD2 . ASP E  284 ? 2.8324 3.3240 2.6838 0.1377  -0.0721 -0.5800 284  ASP E OD2 
13704 N  N   . ILE E  285 ? 2.5834 2.9288 2.4246 0.3208  -0.1402 -0.4444 285  ILE E N   
13705 C  CA  . ILE E  285 ? 2.5773 2.9858 2.4191 0.3463  -0.1683 -0.4266 285  ILE E CA  
13706 C  C   . ILE E  285 ? 2.6114 3.0759 2.4380 0.3045  -0.1646 -0.4577 285  ILE E C   
13707 O  O   . ILE E  285 ? 2.5624 3.1138 2.3947 0.3176  -0.1885 -0.4491 285  ILE E O   
13708 C  CB  . ILE E  285 ? 2.5682 2.8887 2.3880 0.3855  -0.1795 -0.3859 285  ILE E CB  
13709 C  CG1 . ILE E  285 ? 2.5192 2.9045 2.3475 0.4266  -0.2138 -0.3539 285  ILE E CG1 
13710 C  CG2 . ILE E  285 ? 2.7230 2.9739 2.5057 0.3604  -0.1638 -0.3963 285  ILE E CG2 
13711 C  CD1 . ILE E  285 ? 2.5895 3.0097 2.4487 0.4682  -0.2296 -0.3341 285  ILE E CD1 
13712 N  N   . ASN E  286 ? 2.7101 3.1244 2.5144 0.2546  -0.1352 -0.4931 286  ASN E N   
13713 C  CA  . ASN E  286 ? 2.7114 3.1600 2.4947 0.2122  -0.1274 -0.5269 286  ASN E CA  
13714 C  C   . ASN E  286 ? 2.7071 3.2152 2.4953 0.1525  -0.1076 -0.5751 286  ASN E C   
13715 O  O   . ASN E  286 ? 2.7121 3.2119 2.4740 0.1054  -0.0898 -0.6116 286  ASN E O   
13716 C  CB  . ASN E  286 ? 2.7492 3.0752 2.4922 0.2053  -0.1086 -0.5292 286  ASN E CB  
13717 C  CG  . ASN E  286 ? 2.8544 3.0600 2.5831 0.1951  -0.0801 -0.5326 286  ASN E CG  
13718 O  OD1 . ASN E  286 ? 2.7894 2.9861 2.5386 0.2092  -0.0801 -0.5176 286  ASN E OD1 
13719 N  ND2 . ASN E  286 ? 2.9103 3.0239 2.6026 0.1717  -0.0554 -0.5524 286  ASN E ND2 
13720 N  N   . GLY E  287 ? 2.6486 3.2196 2.4683 0.1519  -0.1096 -0.5779 287  GLY E N   
13721 C  CA  . GLY E  287 ? 2.6387 3.2908 2.4663 0.0936  -0.0939 -0.6223 287  GLY E CA  
13722 C  C   . GLY E  287 ? 2.6742 3.2284 2.4650 0.0316  -0.0557 -0.6589 287  GLY E C   
13723 O  O   . GLY E  287 ? 2.8050 3.4026 2.5794 -0.0262 -0.0416 -0.7014 287  GLY E O   
13724 N  N   . ASP E  288 ? 2.7835 3.2044 2.5584 0.0418  -0.0380 -0.6428 288  ASP E N   
13725 C  CA  . ASP E  288 ? 2.9472 3.2604 2.6838 -0.0119 -0.0013 -0.6712 288  ASP E CA  
13726 C  C   . ASP E  288 ? 2.8586 3.1387 2.6037 -0.0243 0.0142  -0.6673 288  ASP E C   
13727 O  O   . ASP E  288 ? 2.8593 3.0322 2.5694 -0.0629 0.0444  -0.6816 288  ASP E O   
13728 C  CB  . ASP E  288 ? 3.1125 3.2800 2.8095 0.0069  0.0103  -0.6578 288  ASP E CB  
13729 C  CG  . ASP E  288 ? 3.0807 3.1938 2.7895 0.0762  -0.0072 -0.6064 288  ASP E CG  
13730 O  OD1 . ASP E  288 ? 3.1028 3.2972 2.8478 0.1162  -0.0345 -0.5805 288  ASP E OD1 
13731 O  OD2 . ASP E  288 ? 3.0580 3.0465 2.7376 0.0909  0.0069  -0.5923 288  ASP E OD2 
13732 N  N   . ASP E  289 ? 2.9005 3.2672 2.6889 0.0085  -0.0051 -0.6480 289  ASP E N   
13733 C  CA  . ASP E  289 ? 3.0074 3.3649 2.8101 0.0016  0.0064  -0.6437 289  ASP E CA  
13734 C  C   . ASP E  289 ? 2.9510 3.1597 2.7325 0.0282  0.0184  -0.6124 289  ASP E C   
13735 O  O   . ASP E  289 ? 2.9080 3.0876 2.6915 0.0148  0.0332  -0.6098 289  ASP E O   
13736 C  CB  . ASP E  289 ? 3.1949 3.5825 2.9838 -0.0779 0.0334  -0.6877 289  ASP E CB  
13737 C  CG  . ASP E  289 ? 3.2848 3.8388 3.0969 -0.1091 0.0224  -0.7211 289  ASP E CG  
13738 O  OD1 . ASP E  289 ? 3.3696 3.9348 3.1594 -0.1389 0.0252  -0.7451 289  ASP E OD1 
13739 O  OD2 . ASP E  289 ? 3.2678 3.9473 3.1205 -0.1031 0.0111  -0.7245 289  ASP E OD2 
13740 N  N   . TYR E  290 ? 2.8887 3.0109 2.6495 0.0641  0.0126  -0.5889 290  TYR E N   
13741 C  CA  . TYR E  290 ? 2.8502 2.8496 2.5948 0.0987  0.0190  -0.5547 290  TYR E CA  
13742 C  C   . TYR E  290 ? 2.7971 2.8271 2.5703 0.1657  -0.0108 -0.5163 290  TYR E C   
13743 O  O   . TYR E  290 ? 2.8011 2.8589 2.5758 0.1927  -0.0308 -0.5062 290  TYR E O   
13744 C  CB  . TYR E  290 ? 2.8783 2.7584 2.5762 0.0909  0.0359  -0.5568 290  TYR E CB  
13745 C  CG  . TYR E  290 ? 2.9686 2.7746 2.6286 0.0300  0.0701  -0.5875 290  TYR E CG  
13746 C  CD1 . TYR E  290 ? 3.1034 2.8875 2.7617 0.0000  0.0880  -0.5900 290  TYR E CD1 
13747 C  CD2 . TYR E  290 ? 2.9523 2.7062 2.5746 0.0013  0.0853  -0.6144 290  TYR E CD2 
13748 C  CE1 . TYR E  290 ? 3.1760 2.8827 2.7933 -0.0589 0.1199  -0.6155 290  TYR E CE1 
13749 C  CE2 . TYR E  290 ? 3.0006 2.6726 2.5821 -0.0549 0.1179  -0.6425 290  TYR E CE2 
13750 C  CZ  . TYR E  290 ? 3.0153 2.6607 2.5929 -0.0858 0.1350  -0.6415 290  TYR E CZ  
13751 O  OH  . TYR E  290 ? 3.0303 2.5847 2.5611 -0.1451 0.1681  -0.6671 290  TYR E OH  
13752 N  N   . ALA E  291 ? 2.7948 2.8210 2.5885 0.1894  -0.0130 -0.4963 291  ALA E N   
13753 C  CA  . ALA E  291 ? 2.7899 2.8263 2.6046 0.2502  -0.0377 -0.4606 291  ALA E CA  
13754 C  C   . ALA E  291 ? 2.6805 2.6220 2.4660 0.2784  -0.0408 -0.4336 291  ALA E C   
13755 O  O   . ALA E  291 ? 2.8629 2.7079 2.6163 0.2632  -0.0198 -0.4328 291  ALA E O   
13756 C  CB  . ALA E  291 ? 2.9845 3.0144 2.8189 0.2646  -0.0333 -0.4484 291  ALA E CB  
13757 N  N   . ASP E  292 ? 2.5390 2.5101 2.3342 0.3205  -0.0671 -0.4102 292  ASP E N   
13758 C  CA  . ASP E  292 ? 2.5251 2.4281 2.2939 0.3454  -0.0730 -0.3856 292  ASP E CA  
13759 C  C   . ASP E  292 ? 2.6471 2.5184 2.4226 0.3897  -0.0860 -0.3487 292  ASP E C   
13760 O  O   . ASP E  292 ? 2.8789 2.8003 2.6825 0.4115  -0.0999 -0.3410 292  ASP E O   
13761 C  CB  . ASP E  292 ? 2.7004 2.6609 2.4656 0.3493  -0.0918 -0.3892 292  ASP E CB  
13762 C  CG  . ASP E  292 ? 2.8776 2.8788 2.6359 0.3019  -0.0790 -0.4299 292  ASP E CG  
13763 O  OD1 . ASP E  292 ? 3.0553 2.9886 2.7900 0.2688  -0.0520 -0.4499 292  ASP E OD1 
13764 O  OD2 . ASP E  292 ? 2.7417 2.8414 2.5156 0.2970  -0.0956 -0.4416 292  ASP E OD2 
13765 N  N   . VAL E  293 ? 2.5594 2.3489 2.3076 0.4032  -0.0807 -0.3276 293  VAL E N   
13766 C  CA  . VAL E  293 ? 2.4033 2.1503 2.1501 0.4359  -0.0872 -0.2954 293  VAL E CA  
13767 C  C   . VAL E  293 ? 2.3170 2.0757 2.0557 0.4654  -0.1117 -0.2703 293  VAL E C   
13768 O  O   . VAL E  293 ? 2.3347 2.0847 2.0515 0.4614  -0.1141 -0.2694 293  VAL E O   
13769 C  CB  . VAL E  293 ? 2.3245 1.9825 2.0453 0.4302  -0.0652 -0.2864 293  VAL E CB  
13770 C  CG1 . VAL E  293 ? 2.3006 1.9252 2.0195 0.4589  -0.0713 -0.2558 293  VAL E CG1 
13771 C  CG2 . VAL E  293 ? 2.3678 2.0082 2.0910 0.3980  -0.0407 -0.3081 293  VAL E CG2 
13772 N  N   . PHE E  294 ? 2.3775 2.1536 2.1313 0.4941  -0.1291 -0.2505 294  PHE E N   
13773 C  CA  . PHE E  294 ? 2.3218 2.0971 2.0633 0.5213  -0.1522 -0.2219 294  PHE E CA  
13774 C  C   . PHE E  294 ? 2.2755 1.9874 2.0053 0.5396  -0.1503 -0.1967 294  PHE E C   
13775 O  O   . PHE E  294 ? 2.3971 2.1069 2.1453 0.5512  -0.1487 -0.1965 294  PHE E O   
13776 C  CB  . PHE E  294 ? 2.3653 2.2133 2.1296 0.5409  -0.1760 -0.2193 294  PHE E CB  
13777 C  CG  . PHE E  294 ? 2.4999 2.4261 2.2756 0.5214  -0.1801 -0.2437 294  PHE E CG  
13778 C  CD1 . PHE E  294 ? 2.5759 2.5512 2.3768 0.4997  -0.1679 -0.2753 294  PHE E CD1 
13779 C  CD2 . PHE E  294 ? 2.6828 2.6399 2.4428 0.5214  -0.1961 -0.2360 294  PHE E CD2 
13780 C  CE1 . PHE E  294 ? 2.7339 2.7870 2.5435 0.4767  -0.1707 -0.3002 294  PHE E CE1 
13781 C  CE2 . PHE E  294 ? 2.7862 2.8221 2.5559 0.5006  -0.1994 -0.2605 294  PHE E CE2 
13782 C  CZ  . PHE E  294 ? 2.8486 2.9325 2.6430 0.4776  -0.1865 -0.2933 294  PHE E CZ  
13783 N  N   . ILE E  295 ? 2.1419 1.8089 1.8410 0.5411  -0.1501 -0.1776 295  ILE E N   
13784 C  CA  . ILE E  295 ? 2.0669 1.6778 1.7500 0.5515  -0.1461 -0.1555 295  ILE E CA  
13785 C  C   . ILE E  295 ? 2.0522 1.6555 1.7137 0.5672  -0.1674 -0.1275 295  ILE E C   
13786 O  O   . ILE E  295 ? 2.0845 1.6977 1.7250 0.5618  -0.1747 -0.1201 295  ILE E O   
13787 C  CB  . ILE E  295 ? 2.1281 1.6953 1.7906 0.5375  -0.1250 -0.1561 295  ILE E CB  
13788 C  CG1 . ILE E  295 ? 2.3164 1.8822 1.9939 0.5188  -0.1038 -0.1820 295  ILE E CG1 
13789 C  CG2 . ILE E  295 ? 2.1494 1.6724 1.7968 0.5456  -0.1208 -0.1345 295  ILE E CG2 
13790 C  CD1 . ILE E  295 ? 2.3878 1.9084 2.0426 0.5086  -0.0832 -0.1829 295  ILE E CD1 
13791 N  N   . GLY E  296 ? 2.0656 1.6479 1.7289 0.5850  -0.1760 -0.1126 296  GLY E N   
13792 C  CA  . GLY E  296 ? 2.0668 1.6284 1.7037 0.5971  -0.1950 -0.0843 296  GLY E CA  
13793 C  C   . GLY E  296 ? 2.0436 1.5524 1.6490 0.5880  -0.1864 -0.0670 296  GLY E C   
13794 O  O   . GLY E  296 ? 2.0069 1.4878 1.6165 0.5841  -0.1699 -0.0724 296  GLY E O   
13795 N  N   . ALA E  297 ? 2.2991 1.8024 1.8717 0.5821  -0.1977 -0.0463 297  ALA E N   
13796 C  CA  . ALA E  297 ? 2.3195 1.7847 1.8579 0.5706  -0.1925 -0.0281 297  ALA E CA  
13797 C  C   . ALA E  297 ? 2.3334 1.7776 1.8413 0.5735  -0.2132 -0.0011 297  ALA E C   
13798 O  O   . ALA E  297 ? 2.3765 1.8359 1.8566 0.5618  -0.2227 0.0137  297  ALA E O   
13799 C  CB  . ALA E  297 ? 2.3179 1.8027 1.8416 0.5553  -0.1820 -0.0311 297  ALA E CB  
13800 N  N   . PRO E  298 ? 2.3029 1.7086 1.8120 0.5886  -0.2195 0.0060  298  PRO E N   
13801 C  CA  . PRO E  298 ? 2.3601 1.7362 1.8392 0.5959  -0.2406 0.0327  298  PRO E CA  
13802 C  C   . PRO E  298 ? 2.4239 1.7651 1.8528 0.5707  -0.2414 0.0556  298  PRO E C   
13803 O  O   . PRO E  298 ? 2.4845 1.8041 1.8801 0.5687  -0.2590 0.0808  298  PRO E O   
13804 C  CB  . PRO E  298 ? 2.6544 1.9881 2.1477 0.6207  -0.2412 0.0292  298  PRO E CB  
13805 C  CG  . PRO E  298 ? 2.5391 1.9059 2.0789 0.6274  -0.2244 -0.0020 298  PRO E CG  
13806 C  CD  . PRO E  298 ? 2.2902 1.6756 1.8265 0.6007  -0.2070 -0.0108 298  PRO E CD  
13807 N  N   . LEU E  299 ? 2.5848 1.9248 2.0056 0.5502  -0.2232 0.0490  299  LEU E N   
13808 C  CA  . LEU E  299 ? 2.7253 2.0439 2.0993 0.5226  -0.2219 0.0680  299  LEU E CA  
13809 C  C   . LEU E  299 ? 2.6463 2.0223 2.0095 0.5059  -0.2207 0.0693  299  LEU E C   
13810 O  O   . LEU E  299 ? 2.7608 2.1396 2.0886 0.4812  -0.2173 0.0816  299  LEU E O   
13811 C  CB  . LEU E  299 ? 2.9445 2.2312 2.3134 0.5111  -0.2027 0.0606  299  LEU E CB  
13812 C  CG  . LEU E  299 ? 3.0894 2.3228 2.4721 0.5281  -0.1996 0.0525  299  LEU E CG  
13813 C  CD1 . LEU E  299 ? 3.1951 2.4045 2.5673 0.5102  -0.1801 0.0450  299  LEU E CD1 
13814 C  CD2 . LEU E  299 ? 3.0444 2.2221 2.3988 0.5367  -0.2181 0.0724  299  LEU E CD2 
13815 N  N   . PHE E  300 ? 2.5156 1.9405 1.9077 0.5181  -0.2225 0.0547  300  PHE E N   
13816 C  CA  . PHE E  300 ? 2.5393 2.0185 1.9229 0.5066  -0.2203 0.0513  300  PHE E CA  
13817 C  C   . PHE E  300 ? 2.6236 2.1143 1.9646 0.4878  -0.2371 0.0762  300  PHE E C   
13818 O  O   . PHE E  300 ? 2.7127 2.1901 2.0432 0.4920  -0.2560 0.0920  300  PHE E O   
13819 C  CB  . PHE E  300 ? 2.6489 2.1702 2.0674 0.5209  -0.2203 0.0291  300  PHE E CB  
13820 C  CG  . PHE E  300 ? 2.8824 2.4547 2.2944 0.5126  -0.2147 0.0192  300  PHE E CG  
13821 C  CD1 . PHE E  300 ? 3.1101 2.6891 2.5334 0.5154  -0.1936 0.0015  300  PHE E CD1 
13822 C  CD2 . PHE E  300 ? 2.7968 2.4100 2.1898 0.5038  -0.2302 0.0278  300  PHE E CD2 
13823 C  CE1 . PHE E  300 ? 3.1704 2.7919 2.5866 0.5132  -0.1873 -0.0095 300  PHE E CE1 
13824 C  CE2 . PHE E  300 ? 2.8554 2.5186 2.2427 0.4977  -0.2238 0.0149  300  PHE E CE2 
13825 C  CZ  . PHE E  300 ? 3.0395 2.7047 2.4388 0.5043  -0.2019 -0.0049 300  PHE E CZ  
13826 N  N   . MET E  301 ? 2.6010 2.1214 1.9163 0.4676  -0.2302 0.0805  301  MET E N   
13827 C  CA  . MET E  301 ? 2.6813 2.2258 1.9541 0.4438  -0.2437 0.1020  301  MET E CA  
13828 C  C   . MET E  301 ? 2.6883 2.3071 1.9691 0.4449  -0.2438 0.0885  301  MET E C   
13829 O  O   . MET E  301 ? 2.7949 2.4454 2.0921 0.4519  -0.2270 0.0684  301  MET E O   
13830 C  CB  . MET E  301 ? 2.7344 2.2703 1.9685 0.4155  -0.2360 0.1156  301  MET E CB  
13831 C  CG  . MET E  301 ? 2.7533 2.2170 1.9792 0.4117  -0.2306 0.1220  301  MET E CG  
13832 S  SD  . MET E  301 ? 3.1125 2.5840 2.2883 0.3697  -0.2213 0.1355  301  MET E SD  
13833 C  CE  . MET E  301 ? 3.1245 2.5971 2.2450 0.3378  -0.2429 0.1653  301  MET E CE  
13834 N  N   . ASP E  302 ? 2.6639 2.3086 1.9318 0.4395  -0.2624 0.0994  302  ASP E N   
13835 C  CA  . ASP E  302 ? 2.6830 2.4020 1.9519 0.4358  -0.2641 0.0869  302  ASP E CA  
13836 C  C   . ASP E  302 ? 2.8171 2.5709 2.0375 0.4048  -0.2739 0.1097  302  ASP E C   
13837 O  O   . ASP E  302 ? 2.9024 2.6156 2.0865 0.3846  -0.2825 0.1378  302  ASP E O   
13838 C  CB  . ASP E  302 ? 2.6669 2.4050 1.9596 0.4503  -0.2773 0.0789  302  ASP E CB  
13839 C  CG  . ASP E  302 ? 2.8279 2.6439 2.1155 0.4415  -0.2816 0.0671  302  ASP E CG  
13840 O  OD1 . ASP E  302 ? 2.9307 2.7795 2.2380 0.4491  -0.2648 0.0365  302  ASP E OD1 
13841 O  OD2 . ASP E  302 ? 2.9173 2.7595 2.1788 0.4272  -0.3013 0.0885  302  ASP E OD2 
13842 N  N   . ARG E  303 ? 2.7964 2.6258 2.0142 0.3991  -0.2718 0.0959  303  ARG E N   
13843 C  CA  . ARG E  303 ? 2.8036 2.6845 1.9773 0.3679  -0.2801 0.1135  303  ARG E CA  
13844 C  C   . ARG E  303 ? 2.8649 2.7681 2.0221 0.3573  -0.3030 0.1303  303  ARG E C   
13845 O  O   . ARG E  303 ? 2.7091 2.6402 1.8946 0.3744  -0.3070 0.1126  303  ARG E O   
13846 C  CB  . ARG E  303 ? 2.7732 2.7320 1.9528 0.3704  -0.2646 0.0878  303  ARG E CB  
13847 C  CG  . ARG E  303 ? 2.8847 2.9090 2.0200 0.3369  -0.2699 0.1028  303  ARG E CG  
13848 C  CD  . ARG E  303 ? 2.8542 2.8483 1.9557 0.3111  -0.2671 0.1265  303  ARG E CD  
13849 N  NE  . ARG E  303 ? 2.9273 2.9411 2.0442 0.3250  -0.2457 0.1087  303  ARG E NE  
13850 C  CZ  . ARG E  303 ? 3.0943 3.1075 2.1850 0.3026  -0.2391 0.1220  303  ARG E CZ  
13851 N  NH1 . ARG E  303 ? 3.2912 3.2762 2.3362 0.2618  -0.2509 0.1514  303  ARG E NH1 
13852 N  NH2 . ARG E  303 ? 2.9192 2.9598 2.0263 0.3197  -0.2204 0.1066  303  ARG E NH2 
13853 N  N   . GLY E  304 ? 2.8964 2.7898 2.0045 0.3261  -0.3179 0.1650  304  GLY E N   
13854 C  CA  . GLY E  304 ? 2.9048 2.8191 1.9901 0.3142  -0.3409 0.1876  304  GLY E CA  
13855 C  C   . GLY E  304 ? 2.9499 2.9676 2.0195 0.2935  -0.3431 0.1787  304  GLY E C   
13856 O  O   . GLY E  304 ? 2.8900 2.9643 1.9657 0.2905  -0.3265 0.1542  304  GLY E O   
13857 N  N   . SER E  305 ? 3.3423 3.3884 2.3905 0.2810  -0.3644 0.1996  305  SER E N   
13858 C  CA  . SER E  305 ? 3.4352 3.5856 2.4660 0.2583  -0.3682 0.1920  305  SER E CA  
13859 C  C   . SER E  305 ? 3.5219 3.7012 2.5021 0.2169  -0.3659 0.2099  305  SER E C   
13860 O  O   . SER E  305 ? 3.4547 3.7293 2.4286 0.2022  -0.3590 0.1910  305  SER E O   
13861 C  CB  . SER E  305 ? 3.2950 3.4712 2.3126 0.2530  -0.3929 0.2139  305  SER E CB  
13862 O  OG  . SER E  305 ? 3.1680 3.3315 2.2327 0.2888  -0.3951 0.1956  305  SER E OG  
13863 N  N   . ASP E  306 ? 3.5910 3.6918 2.5344 0.1969  -0.3702 0.2435  306  ASP E N   
13864 C  CA  . ASP E  306 ? 3.5054 3.6270 2.3951 0.1500  -0.3680 0.2628  306  ASP E CA  
13865 C  C   . ASP E  306 ? 3.3727 3.5094 2.2768 0.1524  -0.3440 0.2380  306  ASP E C   
13866 O  O   . ASP E  306 ? 3.3383 3.5022 2.2004 0.1125  -0.3398 0.2502  306  ASP E O   
13867 C  CB  . ASP E  306 ? 3.5240 3.5453 2.3602 0.1227  -0.3829 0.3105  306  ASP E CB  
13868 C  CG  . ASP E  306 ? 3.5643 3.4700 2.4269 0.1596  -0.3835 0.3149  306  ASP E CG  
13869 O  OD1 . ASP E  306 ? 3.4111 3.3040 2.3229 0.1922  -0.3663 0.2833  306  ASP E OD1 
13870 O  OD2 . ASP E  306 ? 3.6887 3.5175 2.5216 0.1576  -0.4013 0.3507  306  ASP E OD2 
13871 N  N   . GLY E  307 ? 3.3758 3.4997 2.3356 0.1963  -0.3283 0.2047  307  GLY E N   
13872 C  CA  . GLY E  307 ? 3.3474 3.4840 2.3224 0.2044  -0.3064 0.1840  307  GLY E CA  
13873 C  C   . GLY E  307 ? 3.2536 3.2935 2.2213 0.2014  -0.3008 0.1987  307  GLY E C   
13874 O  O   . GLY E  307 ? 3.2149 3.2646 2.1958 0.2087  -0.2828 0.1833  307  GLY E O   
13875 N  N   . LYS E  308 ? 3.1428 3.0919 2.0877 0.1916  -0.3155 0.2281  308  LYS E N   
13876 C  CA  . LYS E  308 ? 3.2605 3.1108 2.1967 0.1892  -0.3098 0.2394  308  LYS E CA  
13877 C  C   . LYS E  308 ? 3.2318 3.0234 2.2240 0.2389  -0.3044 0.2207  308  LYS E C   
13878 O  O   . LYS E  308 ? 3.1584 2.9494 2.1788 0.2664  -0.3146 0.2158  308  LYS E O   
13879 C  CB  . LYS E  308 ? 3.3839 3.1568 2.2612 0.1544  -0.3267 0.2803  308  LYS E CB  
13880 C  CG  . LYS E  308 ? 3.5494 3.2273 2.4005 0.1369  -0.3183 0.2913  308  LYS E CG  
13881 C  CD  . LYS E  308 ? 3.5130 3.0959 2.3041 0.1086  -0.3351 0.3314  308  LYS E CD  
13882 C  CE  . LYS E  308 ? 3.3019 2.9373 2.0305 0.0531  -0.3448 0.3562  308  LYS E CE  
13883 N  NZ  . LYS E  308 ? 3.2806 2.9764 1.9821 0.0075  -0.3283 0.3467  308  LYS E NZ  
13884 N  N   . LEU E  309 ? 3.2111 2.9616 2.2184 0.2475  -0.2881 0.2096  309  LEU E N   
13885 C  CA  . LEU E  309 ? 3.0828 2.7768 2.1392 0.2890  -0.2815 0.1927  309  LEU E CA  
13886 C  C   . LEU E  309 ? 3.1845 2.7882 2.2318 0.2973  -0.2974 0.2141  309  LEU E C   
13887 O  O   . LEU E  309 ? 3.3535 2.9046 2.3503 0.2685  -0.3072 0.2432  309  LEU E O   
13888 C  CB  . LEU E  309 ? 3.0071 2.6803 2.0740 0.2904  -0.2610 0.1800  309  LEU E CB  
13889 C  CG  . LEU E  309 ? 2.9753 2.7334 2.0601 0.2964  -0.2437 0.1577  309  LEU E CG  
13890 C  CD1 . LEU E  309 ? 3.0318 2.7704 2.1162 0.2909  -0.2264 0.1534  309  LEU E CD1 
13891 C  CD2 . LEU E  309 ? 2.8516 2.6386 1.9886 0.3385  -0.2382 0.1304  309  LEU E CD2 
13892 N  N   . GLN E  310 ? 2.9137 2.4988 2.0084 0.3374  -0.2992 0.1994  310  GLN E N   
13893 C  CA  . GLN E  310 ? 2.8736 2.3786 1.9674 0.3551  -0.3126 0.2162  310  GLN E CA  
13894 C  C   . GLN E  310 ? 2.8282 2.3095 1.9785 0.3946  -0.3023 0.1903  310  GLN E C   
13895 O  O   . GLN E  310 ? 2.7247 2.2606 1.9182 0.4146  -0.2960 0.1645  310  GLN E O   
13896 C  CB  . GLN E  310 ? 2.9277 2.4552 2.0104 0.3596  -0.3361 0.2357  310  GLN E CB  
13897 C  CG  . GLN E  310 ? 2.9657 2.5877 2.0854 0.3732  -0.3367 0.2120  310  GLN E CG  
13898 C  CD  . GLN E  310 ? 3.0815 2.7274 2.1946 0.3803  -0.3604 0.2305  310  GLN E CD  
13899 O  OE1 . GLN E  310 ? 3.2385 2.8442 2.3064 0.3662  -0.3776 0.2673  310  GLN E OE1 
13900 N  NE2 . GLN E  310 ? 3.0596 2.7700 2.2147 0.4007  -0.3611 0.2058  310  GLN E NE2 
13901 N  N   . GLU E  311 ? 3.0152 2.4142 2.1622 0.4031  -0.2993 0.1959  311  GLU E N   
13902 C  CA  . GLU E  311 ? 2.9915 2.3655 2.1884 0.4382  -0.2902 0.1731  311  GLU E CA  
13903 C  C   . GLU E  311 ? 3.1884 2.5661 2.4108 0.4707  -0.3075 0.1761  311  GLU E C   
13904 O  O   . GLU E  311 ? 3.5160 2.8409 2.7137 0.4786  -0.3238 0.2013  311  GLU E O   
13905 C  CB  . GLU E  311 ? 2.8650 2.1548 2.0467 0.4352  -0.2811 0.1766  311  GLU E CB  
13906 C  CG  . GLU E  311 ? 2.9565 2.2246 2.1880 0.4695  -0.2714 0.1529  311  GLU E CG  
13907 C  CD  . GLU E  311 ? 3.1575 2.3394 2.3706 0.4682  -0.2642 0.1559  311  GLU E CD  
13908 O  OE1 . GLU E  311 ? 3.2027 2.3428 2.3638 0.4353  -0.2632 0.1733  311  GLU E OE1 
13909 O  OE2 . GLU E  311 ? 3.2250 2.3827 2.4738 0.4978  -0.2591 0.1395  311  GLU E OE2 
13910 N  N   . VAL E  312 ? 3.0232 2.4624 2.2931 0.4898  -0.3038 0.1505  312  VAL E N   
13911 C  CA  . VAL E  312 ? 2.9178 2.3794 2.2153 0.5181  -0.3194 0.1496  312  VAL E CA  
13912 C  C   . VAL E  312 ? 2.5399 2.0108 1.8929 0.5454  -0.3078 0.1187  312  VAL E C   
13913 O  O   . VAL E  312 ? 2.5164 2.0013 1.8942 0.5717  -0.3198 0.1175  312  VAL E O   
13914 C  CB  . VAL E  312 ? 3.1518 2.6947 2.4469 0.5080  -0.3305 0.1496  312  VAL E CB  
13915 C  CG1 . VAL E  312 ? 3.1222 2.6599 2.3602 0.4811  -0.3457 0.1844  312  VAL E CG1 
13916 C  CG2 . VAL E  312 ? 3.1758 2.7747 2.4937 0.4976  -0.3110 0.1173  312  VAL E CG2 
13917 N  N   . GLY E  313 ? 2.5957 2.0652 1.9689 0.5401  -0.2851 0.0945  313  GLY E N   
13918 C  CA  . GLY E  313 ? 2.6286 2.1088 2.0506 0.5598  -0.2728 0.0656  313  GLY E CA  
13919 C  C   . GLY E  313 ? 2.5695 2.1201 2.0196 0.5591  -0.2697 0.0417  313  GLY E C   
13920 O  O   . GLY E  313 ? 2.5945 2.1894 2.0335 0.5535  -0.2839 0.0489  313  GLY E O   
13921 N  N   . GLN E  314 ? 2.6371 2.1969 2.1209 0.5624  -0.2506 0.0128  314  GLN E N   
13922 C  CA  . GLN E  314 ? 2.6851 2.2996 2.1908 0.5574  -0.2438 -0.0135 314  GLN E CA  
13923 C  C   . GLN E  314 ? 2.6303 2.2487 2.1771 0.5668  -0.2311 -0.0406 314  GLN E C   
13924 O  O   . GLN E  314 ? 2.6278 2.2069 2.1841 0.5707  -0.2176 -0.0445 314  GLN E O   
13925 C  CB  . GLN E  314 ? 2.7086 2.3303 2.1980 0.5411  -0.2279 -0.0219 314  GLN E CB  
13926 C  CG  . GLN E  314 ? 2.5530 2.2223 2.0565 0.5351  -0.2205 -0.0497 314  GLN E CG  
13927 C  CD  . GLN E  314 ? 2.4400 2.1098 1.9277 0.5270  -0.2032 -0.0590 314  GLN E CD  
13928 O  OE1 . GLN E  314 ? 2.5309 2.1688 2.0257 0.5304  -0.1837 -0.0683 314  GLN E OE1 
13929 N  NE2 . GLN E  314 ? 2.4753 2.1855 1.9411 0.5181  -0.2103 -0.0563 314  GLN E NE2 
13930 N  N   . VAL E  315 ? 2.5645 2.2361 2.1338 0.5665  -0.2349 -0.0601 315  VAL E N   
13931 C  CA  . VAL E  315 ? 2.4346 2.1223 2.0399 0.5665  -0.2212 -0.0899 315  VAL E CA  
13932 C  C   . VAL E  315 ? 2.4822 2.1958 2.0890 0.5466  -0.2064 -0.1173 315  VAL E C   
13933 O  O   . VAL E  315 ? 2.4579 2.2153 2.0552 0.5386  -0.2159 -0.1208 315  VAL E O   
13934 C  CB  . VAL E  315 ? 2.4190 2.1521 2.0505 0.5823  -0.2379 -0.0924 315  VAL E CB  
13935 C  CG1 . VAL E  315 ? 2.4883 2.2522 2.1551 0.5746  -0.2228 -0.1265 315  VAL E CG1 
13936 C  CG2 . VAL E  315 ? 2.2904 1.9850 1.9192 0.6073  -0.2498 -0.0677 315  VAL E CG2 
13937 N  N   . SER E  316 ? 2.5673 2.2511 2.1833 0.5384  -0.1827 -0.1366 316  SER E N   
13938 C  CA  . SER E  316 ? 2.6142 2.3053 2.2289 0.5208  -0.1651 -0.1648 316  SER E CA  
13939 C  C   . SER E  316 ? 2.5191 2.2437 2.1625 0.5088  -0.1593 -0.1941 316  SER E C   
13940 O  O   . SER E  316 ? 2.4535 2.1714 2.1186 0.5125  -0.1551 -0.1971 316  SER E O   
13941 C  CB  . SER E  316 ? 2.6081 2.2413 2.2096 0.5192  -0.1420 -0.1657 316  SER E CB  
13942 O  OG  . SER E  316 ? 2.4940 2.0966 2.1126 0.5210  -0.1307 -0.1670 316  SER E OG  
13943 N  N   . VAL E  317 ? 2.5775 2.3428 2.2196 0.4917  -0.1580 -0.2178 317  VAL E N   
13944 C  CA  . VAL E  317 ? 2.7031 2.5108 2.3681 0.4725  -0.1519 -0.2492 317  VAL E CA  
13945 C  C   . VAL E  317 ? 2.8263 2.5931 2.4796 0.4483  -0.1236 -0.2790 317  VAL E C   
13946 O  O   . VAL E  317 ? 2.7267 2.4859 2.3580 0.4407  -0.1175 -0.2898 317  VAL E O   
13947 C  CB  . VAL E  317 ? 2.6725 2.5645 2.3434 0.4675  -0.1722 -0.2556 317  VAL E CB  
13948 C  CG1 . VAL E  317 ? 2.7442 2.6929 2.4404 0.4457  -0.1667 -0.2881 317  VAL E CG1 
13949 C  CG2 . VAL E  317 ? 2.5753 2.4920 2.2488 0.4958  -0.2007 -0.2195 317  VAL E CG2 
13950 N  N   . SER E  318 ? 2.8598 2.5977 2.5254 0.4365  -0.1057 -0.2922 318  SER E N   
13951 C  CA  . SER E  318 ? 2.8588 2.5406 2.5087 0.4137  -0.0771 -0.3164 318  SER E CA  
13952 C  C   . SER E  318 ? 2.9018 2.6215 2.5669 0.3791  -0.0675 -0.3515 318  SER E C   
13953 O  O   . SER E  318 ? 2.8799 2.6208 2.5683 0.3738  -0.0670 -0.3531 318  SER E O   
13954 C  CB  . SER E  318 ? 2.8167 2.4249 2.4599 0.4248  -0.0620 -0.2985 318  SER E CB  
13955 O  OG  . SER E  318 ? 2.7508 2.3354 2.3793 0.4529  -0.0709 -0.2678 318  SER E OG  
13956 N  N   . LEU E  319 ? 2.8473 2.5802 2.4980 0.3535  -0.0591 -0.3817 319  LEU E N   
13957 C  CA  . LEU E  319 ? 2.8856 2.6589 2.5449 0.3124  -0.0484 -0.4195 319  LEU E CA  
13958 C  C   . LEU E  319 ? 2.8174 2.5048 2.4567 0.2848  -0.0161 -0.4383 319  LEU E C   
13959 O  O   . LEU E  319 ? 2.9320 2.5409 2.5393 0.2848  0.0015  -0.4437 319  LEU E O   
13960 C  CB  . LEU E  319 ? 3.0229 2.8523 2.6728 0.2932  -0.0537 -0.4457 319  LEU E CB  
13961 C  CG  . LEU E  319 ? 3.0671 3.0137 2.7418 0.3008  -0.0837 -0.4401 319  LEU E CG  
13962 C  CD1 . LEU E  319 ? 3.0026 2.9570 2.6859 0.3473  -0.1097 -0.3945 319  LEU E CD1 
13963 C  CD2 . LEU E  319 ? 3.2167 3.2130 2.8763 0.2780  -0.0853 -0.4675 319  LEU E CD2 
13964 N  N   . GLN E  320 ? 2.8026 2.5050 2.4590 0.2630  -0.0082 -0.4469 320  GLN E N   
13965 C  CA  . GLN E  320 ? 2.8329 2.4569 2.4682 0.2309  0.0222  -0.4628 320  GLN E CA  
13966 C  C   . GLN E  320 ? 3.0595 2.6732 2.6703 0.1827  0.0415  -0.5062 320  GLN E C   
13967 O  O   . GLN E  320 ? 3.1316 2.8359 2.7564 0.1588  0.0322  -0.5317 320  GLN E O   
13968 C  CB  . GLN E  320 ? 2.8859 2.5449 2.5475 0.2172  0.0239  -0.4611 320  GLN E CB  
13969 C  CG  . GLN E  320 ? 3.0160 2.5970 2.6541 0.1799  0.0546  -0.4734 320  GLN E CG  
13970 C  CD  . GLN E  320 ? 3.0406 2.6777 2.7061 0.1591  0.0563  -0.4779 320  GLN E CD  
13971 O  OE1 . GLN E  320 ? 2.9971 2.5904 2.6454 0.1199  0.0800  -0.4904 320  GLN E OE1 
13972 N  NE2 . GLN E  320 ? 3.0688 2.8029 2.7753 0.1855  0.0314  -0.4679 320  GLN E NE2 
13973 N  N   . ARG E  321 ? 3.3709 2.8724 2.9427 0.1683  0.0693  -0.5148 321  ARG E N   
13974 C  CA  . ARG E  321 ? 3.4674 2.9315 3.0073 0.1188  0.0936  -0.5577 321  ARG E CA  
13975 C  C   . ARG E  321 ? 3.3232 2.7029 2.8390 0.0814  0.1225  -0.5655 321  ARG E C   
13976 O  O   . ARG E  321 ? 3.1890 2.5122 2.7033 0.1027  0.1271  -0.5342 321  ARG E O   
13977 C  CB  . ARG E  321 ? 3.4595 2.8550 2.9648 0.1365  0.1022  -0.5658 321  ARG E CB  
13978 C  CG  . ARG E  321 ? 3.4028 2.8772 2.9269 0.1727  0.0743  -0.5542 321  ARG E CG  
13979 C  CD  . ARG E  321 ? 3.4741 3.0621 3.0149 0.1383  0.0624  -0.5867 321  ARG E CD  
13980 N  NE  . ARG E  321 ? 3.4964 3.1610 3.0502 0.1678  0.0361  -0.5759 321  ARG E NE  
13981 C  CZ  . ARG E  321 ? 3.3281 3.1002 2.8954 0.1467  0.0215  -0.5977 321  ARG E CZ  
13982 N  NH1 . ARG E  321 ? 3.2563 3.0789 2.8277 0.0953  0.0308  -0.6340 321  ARG E NH1 
13983 N  NH2 . ARG E  321 ? 3.2291 3.0642 2.8043 0.1748  -0.0025 -0.5823 321  ARG E NH2 
13984 N  N   . ALA E  322 ? 3.2681 2.6437 2.7629 0.0211  0.1423  -0.6081 322  ALA E N   
13985 C  CA  . ALA E  322 ? 3.2939 2.5872 2.7588 -0.0249 0.1716  -0.6185 322  ALA E CA  
13986 C  C   . ALA E  322 ? 3.5286 2.6621 2.9458 -0.0040 0.1944  -0.6014 322  ALA E C   
13987 O  O   . ALA E  322 ? 3.6556 2.7103 3.0510 -0.0208 0.2133  -0.5886 322  ALA E O   
13988 C  CB  . ALA E  322 ? 3.2763 2.5968 2.7225 -0.0989 0.1890  -0.6708 322  ALA E CB  
13989 N  N   . SER E  323 ? 3.6233 2.7113 3.0228 0.0334  0.1931  -0.6005 323  SER E N   
13990 C  CA  . SER E  323 ? 3.6675 2.6112 3.0228 0.0626  0.2134  -0.5839 323  SER E CA  
13991 C  C   . SER E  323 ? 3.6850 2.6096 3.0552 0.1183  0.2021  -0.5307 323  SER E C   
13992 O  O   . SER E  323 ? 3.7466 2.5637 3.0837 0.1504  0.2162  -0.5107 323  SER E O   
13993 C  CB  . SER E  323 ? 3.6109 2.5258 2.9449 0.0873  0.2157  -0.6032 323  SER E CB  
13994 O  OG  . SER E  323 ? 3.8551 2.7758 3.1684 0.0323  0.2302  -0.6558 323  SER E OG  
13995 N  N   . GLY E  324 ? 3.6469 2.6736 3.0644 0.1319  0.1774  -0.5084 324  GLY E N   
13996 C  CA  . GLY E  324 ? 3.6184 2.6372 3.0510 0.1764  0.1671  -0.4620 324  GLY E CA  
13997 C  C   . GLY E  324 ? 3.6342 2.7006 3.0881 0.2336  0.1422  -0.4375 324  GLY E C   
13998 O  O   . GLY E  324 ? 3.5472 2.6438 3.0244 0.2637  0.1275  -0.4034 324  GLY E O   
13999 N  N   . ASP E  325 ? 3.7211 2.7963 3.1655 0.2460  0.1380  -0.4552 325  ASP E N   
14000 C  CA  . ASP E  325 ? 3.5935 2.7120 3.0519 0.2956  0.1161  -0.4328 325  ASP E CA  
14001 C  C   . ASP E  325 ? 3.6162 2.8566 3.1189 0.2976  0.0858  -0.4264 325  ASP E C   
14002 O  O   . ASP E  325 ? 3.7830 3.0800 3.3090 0.2667  0.0810  -0.4386 325  ASP E O   
14003 C  CB  . ASP E  325 ? 3.6137 2.7068 3.0459 0.3053  0.1229  -0.4565 325  ASP E CB  
14004 C  CG  . ASP E  325 ? 3.7985 2.7641 3.1836 0.3015  0.1549  -0.4695 325  ASP E CG  
14005 O  OD1 . ASP E  325 ? 3.9770 2.8786 3.3445 0.3437  0.1614  -0.4412 325  ASP E OD1 
14006 O  OD2 . ASP E  325 ? 3.7168 2.6459 3.0805 0.2565  0.1740  -0.5075 325  ASP E OD2 
14007 N  N   . PHE E  326 ? 3.4848 2.7662 2.9969 0.3357  0.0652  -0.4062 326  PHE E N   
14008 C  CA  . PHE E  326 ? 3.4414 2.8259 2.9878 0.3437  0.0355  -0.3962 326  PHE E CA  
14009 C  C   . PHE E  326 ? 3.4285 2.8511 2.9676 0.3609  0.0220  -0.4000 326  PHE E C   
14010 O  O   . PHE E  326 ? 3.6027 2.9818 3.1198 0.3880  0.0275  -0.3890 326  PHE E O   
14011 C  CB  . PHE E  326 ? 3.2559 2.6511 2.8216 0.3729  0.0214  -0.3563 326  PHE E CB  
14012 C  CG  . PHE E  326 ? 3.2822 2.6737 2.8646 0.3545  0.0285  -0.3541 326  PHE E CG  
14013 C  CD1 . PHE E  326 ? 3.2849 2.5961 2.8481 0.3489  0.0514  -0.3470 326  PHE E CD1 
14014 C  CD2 . PHE E  326 ? 3.2245 2.6968 2.8412 0.3448  0.0121  -0.3582 326  PHE E CD2 
14015 C  CE1 . PHE E  326 ? 3.2190 2.5336 2.7966 0.3289  0.0582  -0.3454 326  PHE E CE1 
14016 C  CE2 . PHE E  326 ? 3.1719 2.6502 2.8053 0.3285  0.0191  -0.3588 326  PHE E CE2 
14017 C  CZ  . PHE E  326 ? 3.1450 2.5458 2.7586 0.3181  0.0425  -0.3531 326  PHE E CZ  
14018 N  N   . GLN E  327 ? 3.1060 2.6163 2.6631 0.3458  0.0041  -0.4147 327  GLN E N   
14019 C  CA  . GLN E  327 ? 2.8880 2.4517 2.4409 0.3602  -0.0132 -0.4136 327  GLN E CA  
14020 C  C   . GLN E  327 ? 2.8462 2.4656 2.4208 0.3875  -0.0423 -0.3752 327  GLN E C   
14021 O  O   . GLN E  327 ? 2.8324 2.5182 2.4327 0.3805  -0.0599 -0.3721 327  GLN E O   
14022 C  CB  . GLN E  327 ? 2.9266 2.5545 2.4815 0.3261  -0.0151 -0.4517 327  GLN E CB  
14023 C  CG  . GLN E  327 ? 3.1265 2.6968 2.6574 0.2904  0.0152  -0.4947 327  GLN E CG  
14024 C  CD  . GLN E  327 ? 3.3914 3.0288 2.9180 0.2579  0.0135  -0.5343 327  GLN E CD  
14025 O  OE1 . GLN E  327 ? 3.3722 3.1137 2.9229 0.2521  -0.0104 -0.5313 327  GLN E OE1 
14026 N  NE2 . GLN E  327 ? 3.5565 3.1342 3.0507 0.2375  0.0392  -0.5716 327  GLN E NE2 
14027 N  N   . THR E  328 ? 2.9236 2.5166 2.4857 0.4186  -0.0472 -0.3464 328  THR E N   
14028 C  CA  . THR E  328 ? 2.7109 2.3356 2.2855 0.4417  -0.0709 -0.3085 328  THR E CA  
14029 C  C   . THR E  328 ? 2.6993 2.3801 2.2644 0.4505  -0.0912 -0.2992 328  THR E C   
14030 O  O   . THR E  328 ? 2.9803 2.6508 2.5228 0.4556  -0.0836 -0.3071 328  THR E O   
14031 C  CB  . THR E  328 ? 2.6659 2.2293 2.2313 0.4647  -0.0627 -0.2806 328  THR E CB  
14032 O  OG1 . THR E  328 ? 2.7672 2.2804 2.3391 0.4545  -0.0437 -0.2876 328  THR E OG1 
14033 C  CG2 . THR E  328 ? 2.5538 2.1440 2.1286 0.4827  -0.0853 -0.2451 328  THR E CG2 
14034 N  N   . THR E  329 ? 2.5076 2.2479 2.0883 0.4533  -0.1166 -0.2819 329  THR E N   
14035 C  CA  . THR E  329 ? 2.6301 2.4188 2.1992 0.4626  -0.1391 -0.2616 329  THR E CA  
14036 C  C   . THR E  329 ? 2.5839 2.3640 2.1574 0.4824  -0.1569 -0.2213 329  THR E C   
14037 O  O   . THR E  329 ? 2.5023 2.2495 2.0916 0.4887  -0.1523 -0.2139 329  THR E O   
14038 C  CB  . THR E  329 ? 2.6525 2.5221 2.2293 0.4458  -0.1541 -0.2782 329  THR E CB  
14039 O  OG1 . THR E  329 ? 2.7201 2.6357 2.2852 0.4556  -0.1792 -0.2499 329  THR E OG1 
14040 C  CG2 . THR E  329 ? 2.6371 2.5389 2.2441 0.4387  -0.1605 -0.2847 329  THR E CG2 
14041 N  N   . LYS E  330 ? 2.6516 2.4600 2.2084 0.4898  -0.1765 -0.1960 330  LYS E N   
14042 C  CA  . LYS E  330 ? 2.5026 2.2916 2.0546 0.5052  -0.1919 -0.1580 330  LYS E CA  
14043 C  C   . LYS E  330 ? 2.5373 2.3785 2.0847 0.5071  -0.2202 -0.1371 330  LYS E C   
14044 O  O   . LYS E  330 ? 2.6989 2.5897 2.2322 0.4970  -0.2287 -0.1414 330  LYS E O   
14045 C  CB  . LYS E  330 ? 2.4605 2.2138 1.9859 0.5111  -0.1848 -0.1400 330  LYS E CB  
14046 C  CG  . LYS E  330 ? 2.6420 2.3362 2.1718 0.5173  -0.1614 -0.1459 330  LYS E CG  
14047 C  CD  . LYS E  330 ? 2.9212 2.5990 2.4246 0.5236  -0.1535 -0.1324 330  LYS E CD  
14048 C  CE  . LYS E  330 ? 2.8957 2.5194 2.4026 0.5324  -0.1327 -0.1319 330  LYS E CE  
14049 N  NZ  . LYS E  330 ? 2.8931 2.4908 2.4155 0.5292  -0.1130 -0.1614 330  LYS E NZ  
14050 N  N   . LEU E  331 ? 2.4525 2.2816 2.0101 0.5214  -0.2345 -0.1144 331  LEU E N   
14051 C  CA  . LEU E  331 ? 2.4464 2.3141 1.9986 0.5295  -0.2623 -0.0895 331  LEU E CA  
14052 C  C   . LEU E  331 ? 2.4000 2.2166 1.9267 0.5405  -0.2732 -0.0505 331  LEU E C   
14053 O  O   . LEU E  331 ? 2.3445 2.1093 1.8796 0.5531  -0.2680 -0.0429 331  LEU E O   
14054 C  CB  . LEU E  331 ? 2.4843 2.3862 2.0703 0.5408  -0.2703 -0.0988 331  LEU E CB  
14055 C  CG  . LEU E  331 ? 2.6063 2.5615 2.1898 0.5536  -0.2996 -0.0753 331  LEU E CG  
14056 C  CD1 . LEU E  331 ? 2.5673 2.5898 2.1351 0.5341  -0.3078 -0.0819 331  LEU E CD1 
14057 C  CD2 . LEU E  331 ? 2.6683 2.6645 2.2891 0.5694  -0.3055 -0.0867 331  LEU E CD2 
14058 N  N   . ASN E  332 ? 2.5314 2.3631 2.0246 0.5323  -0.2873 -0.0273 332  ASN E N   
14059 C  CA  . ASN E  332 ? 2.5226 2.3047 1.9833 0.5345  -0.2970 0.0094  332  ASN E CA  
14060 C  C   . ASN E  332 ? 2.5937 2.3707 2.0494 0.5517  -0.3220 0.0390  332  ASN E C   
14061 O  O   . ASN E  332 ? 2.6904 2.5252 2.1563 0.5574  -0.3376 0.0389  332  ASN E O   
14062 C  CB  . ASN E  332 ? 2.5617 2.3638 1.9842 0.5134  -0.2992 0.0212  332  ASN E CB  
14063 C  CG  . ASN E  332 ? 2.5876 2.3785 2.0083 0.5043  -0.2747 0.0007  332  ASN E CG  
14064 O  OD1 . ASN E  332 ? 2.6973 2.4683 2.1449 0.5118  -0.2557 -0.0243 332  ASN E OD1 
14065 N  ND2 . ASN E  332 ? 2.6238 2.4304 2.0110 0.4885  -0.2750 0.0125  332  ASN E ND2 
14066 N  N   . GLY E  333 ? 2.6963 2.4031 2.1344 0.5610  -0.3251 0.0640  333  GLY E N   
14067 C  CA  . GLY E  333 ? 2.6931 2.3763 2.1188 0.5815  -0.3477 0.0954  333  GLY E CA  
14068 C  C   . GLY E  333 ? 2.8437 2.5457 2.2263 0.5684  -0.3691 0.1286  333  GLY E C   
14069 O  O   . GLY E  333 ? 3.0075 2.7420 2.3682 0.5410  -0.3659 0.1270  333  GLY E O   
14070 N  N   . PHE E  334 ? 2.8592 2.5416 2.2282 0.5903  -0.3915 0.1600  334  PHE E N   
14071 C  CA  . PHE E  334 ? 2.8828 2.5839 2.2100 0.5811  -0.4151 0.1967  334  PHE E CA  
14072 C  C   . PHE E  334 ? 2.7962 2.4051 2.0675 0.5735  -0.4231 0.2378  334  PHE E C   
14073 O  O   . PHE E  334 ? 2.7480 2.3660 1.9737 0.5486  -0.4354 0.2656  334  PHE E O   
14074 C  CB  . PHE E  334 ? 2.9653 2.7196 2.3112 0.6116  -0.4378 0.2080  334  PHE E CB  
14075 C  CG  . PHE E  334 ? 3.0695 2.9165 2.4687 0.6163  -0.4306 0.1668  334  PHE E CG  
14076 C  CD1 . PHE E  334 ? 2.9626 2.9006 2.3631 0.5924  -0.4334 0.1525  334  PHE E CD1 
14077 C  CD2 . PHE E  334 ? 3.1489 2.9932 2.5944 0.6411  -0.4199 0.1403  334  PHE E CD2 
14078 C  CE1 . PHE E  334 ? 2.8553 2.8729 2.3000 0.5913  -0.4250 0.1119  334  PHE E CE1 
14079 C  CE2 . PHE E  334 ? 3.0144 2.9425 2.5044 0.6386  -0.4120 0.1016  334  PHE E CE2 
14080 C  CZ  . PHE E  334 ? 2.8614 2.8728 2.3497 0.6127  -0.4142 0.0871  334  PHE E CZ  
14081 N  N   . GLU E  335 ? 2.7486 2.2696 2.0193 0.5916  -0.4159 0.2415  335  GLU E N   
14082 C  CA  . GLU E  335 ? 2.8518 2.2728 2.0662 0.5838  -0.4221 0.2783  335  GLU E CA  
14083 C  C   . GLU E  335 ? 2.7197 2.0817 1.9219 0.5587  -0.3982 0.2636  335  GLU E C   
14084 O  O   . GLU E  335 ? 2.6455 2.0074 1.8890 0.5698  -0.3793 0.2307  335  GLU E O   
14085 C  CB  . GLU E  335 ? 2.9643 2.3232 2.1793 0.6297  -0.4366 0.2991  335  GLU E CB  
14086 C  CG  . GLU E  335 ? 2.7481 2.1451 1.9493 0.6504  -0.4656 0.3327  335  GLU E CG  
14087 C  CD  . GLU E  335 ? 2.7721 2.0827 1.9529 0.6942  -0.4811 0.3651  335  GLU E CD  
14088 O  OE1 . GLU E  335 ? 2.8242 2.1814 2.0229 0.7334  -0.5014 0.3791  335  GLU E OE1 
14089 O  OE2 . GLU E  335 ? 2.8075 2.0050 1.9538 0.6905  -0.4724 0.3754  335  GLU E OE2 
14090 N  N   . VAL E  336 ? 2.7790 2.0944 1.9217 0.5224  -0.3992 0.2894  336  VAL E N   
14091 C  CA  . VAL E  336 ? 2.8024 2.0684 1.9254 0.4932  -0.3781 0.2793  336  VAL E CA  
14092 C  C   . VAL E  336 ? 3.1894 2.3568 2.3137 0.5163  -0.3709 0.2776  336  VAL E C   
14093 O  O   . VAL E  336 ? 3.3998 2.4998 2.5031 0.5409  -0.3857 0.3026  336  VAL E O   
14094 C  CB  . VAL E  336 ? 2.8924 2.1413 1.9472 0.4446  -0.3827 0.3085  336  VAL E CB  
14095 C  CG1 . VAL E  336 ? 2.9080 2.1503 1.9505 0.4091  -0.3596 0.2913  336  VAL E CG1 
14096 C  CG2 . VAL E  336 ? 2.9038 2.2480 1.9531 0.4289  -0.3959 0.3164  336  VAL E CG2 
14097 N  N   . PHE E  337 ? 3.3461 2.5062 2.4955 0.5113  -0.3476 0.2474  337  PHE E N   
14098 C  CA  . PHE E  337 ? 3.2987 2.3749 2.4513 0.5270  -0.3359 0.2381  337  PHE E CA  
14099 C  C   . PHE E  337 ? 3.0721 2.1407 2.2688 0.5812  -0.3433 0.2290  337  PHE E C   
14100 O  O   . PHE E  337 ? 3.0012 1.9986 2.1999 0.6014  -0.3360 0.2223  337  PHE E O   
14101 C  CB  . PHE E  337 ? 3.3596 2.3299 2.4421 0.5026  -0.3386 0.2670  337  PHE E CB  
14102 C  CG  . PHE E  337 ? 3.3848 2.3640 2.4230 0.4450  -0.3281 0.2720  337  PHE E CG  
14103 C  CD1 . PHE E  337 ? 3.3138 2.3725 2.3813 0.4269  -0.3111 0.2453  337  PHE E CD1 
14104 C  CD2 . PHE E  337 ? 3.4976 2.4069 2.4626 0.4089  -0.3349 0.3040  337  PHE E CD2 
14105 C  CE1 . PHE E  337 ? 3.2862 2.3665 2.3152 0.3776  -0.3018 0.2495  337  PHE E CE1 
14106 C  CE2 . PHE E  337 ? 3.4790 2.4095 2.4033 0.3526  -0.3249 0.3070  337  PHE E CE2 
14107 C  CZ  . PHE E  337 ? 3.3736 2.3956 2.3321 0.3388  -0.3087 0.2793  337  PHE E CZ  
14108 N  N   . ALA E  338 ? 2.9057 2.0528 2.1380 0.6045  -0.3567 0.2264  338  ALA E N   
14109 C  CA  . ALA E  338 ? 2.9651 2.1258 2.2420 0.6550  -0.3643 0.2165  338  ALA E CA  
14110 C  C   . ALA E  338 ? 2.8697 2.0638 2.2037 0.6658  -0.3433 0.1744  338  ALA E C   
14111 O  O   . ALA E  338 ? 2.8996 2.0963 2.2697 0.7053  -0.3448 0.1617  338  ALA E O   
14112 C  CB  . ALA E  338 ? 3.0132 2.2598 2.3077 0.6703  -0.3852 0.2262  338  ALA E CB  
14113 N  N   . ARG E  339 ? 2.8477 2.0708 2.1893 0.6325  -0.3240 0.1539  339  ARG E N   
14114 C  CA  . ARG E  339 ? 2.7684 2.0231 2.1588 0.6372  -0.3031 0.1169  339  ARG E CA  
14115 C  C   . ARG E  339 ? 2.7271 2.0614 2.1694 0.6624  -0.3089 0.0978  339  ARG E C   
14116 O  O   . ARG E  339 ? 2.6894 2.0333 2.1711 0.6876  -0.3027 0.0768  339  ARG E O   
14117 C  CB  . ARG E  339 ? 2.7553 1.9389 2.1472 0.6498  -0.2904 0.1075  339  ARG E CB  
14118 C  CG  . ARG E  339 ? 2.8176 1.9315 2.1588 0.6160  -0.2805 0.1199  339  ARG E CG  
14119 C  CD  . ARG E  339 ? 2.9384 1.9949 2.2855 0.6227  -0.2634 0.1023  339  ARG E CD  
14120 N  NE  . ARG E  339 ? 3.1543 2.1429 2.4480 0.5876  -0.2546 0.1139  339  ARG E NE  
14121 C  CZ  . ARG E  339 ? 3.1495 2.0844 2.4365 0.5823  -0.2379 0.0992  339  ARG E CZ  
14122 N  NH1 . ARG E  339 ? 2.9998 1.9422 2.3314 0.6118  -0.2285 0.0730  339  ARG E NH1 
14123 N  NH2 . ARG E  339 ? 3.1581 2.0376 2.3929 0.5444  -0.2300 0.1090  339  ARG E NH2 
14124 N  N   . PHE E  340 ? 2.6473 2.0446 2.0877 0.6526  -0.3208 0.1041  340  PHE E N   
14125 C  CA  . PHE E  340 ? 2.6520 2.1357 2.1372 0.6637  -0.3232 0.0816  340  PHE E CA  
14126 C  C   . PHE E  340 ? 2.5708 2.0757 2.0935 0.6538  -0.2981 0.0444  340  PHE E C   
14127 O  O   . PHE E  340 ? 2.7158 2.2077 2.2266 0.6276  -0.2816 0.0370  340  PHE E O   
14128 C  CB  . PHE E  340 ? 2.7188 2.2620 2.1878 0.6431  -0.3344 0.0902  340  PHE E CB  
14129 C  CG  . PHE E  340 ? 2.7483 2.3828 2.2573 0.6460  -0.3354 0.0642  340  PHE E CG  
14130 C  CD1 . PHE E  340 ? 2.6366 2.3224 2.1601 0.6703  -0.3563 0.0726  340  PHE E CD1 
14131 C  CD2 . PHE E  340 ? 2.7565 2.4255 2.2850 0.6233  -0.3152 0.0319  340  PHE E CD2 
14132 C  CE1 . PHE E  340 ? 2.6432 2.4198 2.2012 0.6671  -0.3563 0.0463  340  PHE E CE1 
14133 C  CE2 . PHE E  340 ? 2.6828 2.4289 2.2427 0.6201  -0.3142 0.0055  340  PHE E CE2 
14134 C  CZ  . PHE E  340 ? 2.6652 2.4687 2.2401 0.6393  -0.3345 0.0113  340  PHE E CZ  
14135 N  N   . GLY E  341 ? 2.4498 1.9909 2.0162 0.6751  -0.2956 0.0223  341  GLY E N   
14136 C  CA  . GLY E  341 ? 2.3703 1.9280 1.9700 0.6649  -0.2722 -0.0111 341  GLY E CA  
14137 C  C   . GLY E  341 ? 2.4352 1.9454 2.0474 0.6784  -0.2596 -0.0195 341  GLY E C   
14138 O  O   . GLY E  341 ? 2.4582 1.9754 2.0920 0.6659  -0.2389 -0.0436 341  GLY E O   
14139 N  N   . SER E  342 ? 2.6005 2.0589 2.1964 0.7028  -0.2707 -0.0003 342  SER E N   
14140 C  CA  . SER E  342 ? 2.5927 2.0059 2.1991 0.7164  -0.2578 -0.0118 342  SER E CA  
14141 C  C   . SER E  342 ? 2.5656 2.0375 2.2239 0.7378  -0.2529 -0.0405 342  SER E C   
14142 O  O   . SER E  342 ? 2.5765 2.0392 2.2535 0.7345  -0.2342 -0.0617 342  SER E O   
14143 C  CB  . SER E  342 ? 2.6543 1.9909 2.2269 0.7390  -0.2705 0.0138  342  SER E CB  
14144 O  OG  . SER E  342 ? 2.7144 1.9963 2.2357 0.7110  -0.2719 0.0382  342  SER E OG  
14145 N  N   . ALA E  343 ? 2.5366 2.0765 2.2177 0.7575  -0.2691 -0.0420 343  ALA E N   
14146 C  CA  . ALA E  343 ? 2.4434 2.0567 2.1740 0.7740  -0.2652 -0.0705 343  ALA E CA  
14147 C  C   . ALA E  343 ? 2.2641 1.9680 2.0138 0.7595  -0.2718 -0.0813 343  ALA E C   
14148 O  O   . ALA E  343 ? 2.1955 1.9169 1.9266 0.7617  -0.2905 -0.0607 343  ALA E O   
14149 C  CB  . ALA E  343 ? 2.4109 2.0234 2.1545 0.8254  -0.2798 -0.0644 343  ALA E CB  
14150 N  N   . ILE E  344 ? 2.2391 2.0007 2.0233 0.7414  -0.2556 -0.1143 344  ILE E N   
14151 C  CA  . ILE E  344 ? 2.1417 1.9875 1.9436 0.7195  -0.2565 -0.1323 344  ILE E CA  
14152 C  C   . ILE E  344 ? 2.4216 2.3500 2.2694 0.7303  -0.2529 -0.1612 344  ILE E C   
14153 O  O   . ILE E  344 ? 2.6100 2.5328 2.4754 0.7178  -0.2324 -0.1835 344  ILE E O   
14154 C  CB  . ILE E  344 ? 2.1266 1.9521 1.9150 0.6735  -0.2356 -0.1461 344  ILE E CB  
14155 C  CG1 . ILE E  344 ? 2.1439 1.8924 1.8887 0.6648  -0.2368 -0.1193 344  ILE E CG1 
14156 C  CG2 . ILE E  344 ? 2.1880 2.0908 1.9878 0.6495  -0.2367 -0.1658 344  ILE E CG2 
14157 C  CD1 . ILE E  344 ? 2.1876 1.9102 1.9182 0.6286  -0.2154 -0.1308 344  ILE E CD1 
14158 N  N   . ALA E  345 ? 2.4337 2.4448 2.3001 0.7531  -0.2728 -0.1600 345  ALA E N   
14159 C  CA  . ALA E  345 ? 2.2629 2.3710 2.1742 0.7660  -0.2718 -0.1871 345  ALA E CA  
14160 C  C   . ALA E  345 ? 2.2681 2.4788 2.1945 0.7355  -0.2737 -0.2081 345  ALA E C   
14161 O  O   . ALA E  345 ? 2.2819 2.5346 2.1992 0.7455  -0.2948 -0.1916 345  ALA E O   
14162 C  CB  . ALA E  345 ? 2.2140 2.3438 2.1384 0.8277  -0.2938 -0.1697 345  ALA E CB  
14163 N  N   . PRO E  346 ? 2.5108 2.7624 2.4560 0.6948  -0.2518 -0.2438 346  PRO E N   
14164 C  CA  . PRO E  346 ? 2.5499 2.9075 2.5105 0.6638  -0.2526 -0.2690 346  PRO E CA  
14165 C  C   . PRO E  346 ? 2.5842 3.0600 2.5783 0.7022  -0.2744 -0.2701 346  PRO E C   
14166 O  O   . PRO E  346 ? 2.6945 3.1966 2.7158 0.7364  -0.2754 -0.2748 346  PRO E O   
14167 C  CB  . PRO E  346 ? 2.7348 3.0966 2.7068 0.6158  -0.2225 -0.3056 346  PRO E CB  
14168 C  CG  . PRO E  346 ? 2.8638 3.1054 2.8153 0.6149  -0.2062 -0.2934 346  PRO E CG  
14169 C  CD  . PRO E  346 ? 2.7187 2.9199 2.6679 0.6710  -0.2246 -0.2624 346  PRO E CD  
14170 N  N   . LEU E  347 ? 2.4482 3.0004 2.4399 0.6986  -0.2920 -0.2660 347  LEU E N   
14171 C  CA  . LEU E  347 ? 2.4049 3.0746 2.4240 0.7405  -0.3169 -0.2597 347  LEU E CA  
14172 C  C   . LEU E  347 ? 2.3468 3.1620 2.3986 0.7073  -0.3110 -0.2997 347  LEU E C   
14173 O  O   . LEU E  347 ? 2.3320 3.2667 2.4109 0.7407  -0.3309 -0.2983 347  LEU E O   
14174 C  CB  . LEU E  347 ? 2.3479 3.0172 2.3408 0.7631  -0.3443 -0.2228 347  LEU E CB  
14175 C  CG  . LEU E  347 ? 2.3559 2.8852 2.3095 0.7879  -0.3511 -0.1818 347  LEU E CG  
14176 C  CD1 . LEU E  347 ? 2.4244 2.9654 2.3501 0.8026  -0.3778 -0.1461 347  LEU E CD1 
14177 C  CD2 . LEU E  347 ? 2.4079 2.8839 2.3716 0.8427  -0.3547 -0.1666 347  LEU E CD2 
14178 N  N   . GLY E  348 ? 2.3136 3.1225 2.3611 0.6425  -0.2840 -0.3348 348  GLY E N   
14179 C  CA  . GLY E  348 ? 2.3790 3.3223 2.4473 0.6006  -0.2788 -0.3724 348  GLY E CA  
14180 C  C   . GLY E  348 ? 2.4103 3.4024 2.4601 0.5849  -0.2945 -0.3659 348  GLY E C   
14181 O  O   . GLY E  348 ? 2.5016 3.4029 2.5163 0.5824  -0.2980 -0.3434 348  GLY E O   
14182 N  N   . ASP E  349 ? 2.2250 3.3713 2.2986 0.5729  -0.3040 -0.3870 349  ASP E N   
14183 C  CA  . ASP E  349 ? 2.2027 3.4202 2.2622 0.5604  -0.3213 -0.3817 349  ASP E CA  
14184 C  C   . ASP E  349 ? 2.1135 3.4017 2.1883 0.6340  -0.3576 -0.3418 349  ASP E C   
14185 O  O   . ASP E  349 ? 2.0647 3.5031 2.1722 0.6513  -0.3715 -0.3512 349  ASP E O   
14186 C  CB  . ASP E  349 ? 2.2486 3.5929 2.3192 0.4954  -0.3084 -0.4304 349  ASP E CB  
14187 C  CG  . ASP E  349 ? 2.3743 3.7515 2.4182 0.4616  -0.3153 -0.4341 349  ASP E CG  
14188 O  OD1 . ASP E  349 ? 2.4858 3.8213 2.5096 0.4979  -0.3367 -0.3944 349  ASP E OD1 
14189 O  OD2 . ASP E  349 ? 2.4439 3.8876 2.4843 0.3958  -0.2983 -0.4779 349  ASP E OD2 
14190 N  N   . LEU E  350 ? 2.1631 3.3406 2.2115 0.6775  -0.3727 -0.2958 350  LEU E N   
14191 C  CA  . LEU E  350 ? 2.0969 3.3056 2.1515 0.7527  -0.4058 -0.2514 350  LEU E CA  
14192 C  C   . LEU E  350 ? 2.0612 3.4289 2.1260 0.7584  -0.4307 -0.2471 350  LEU E C   
14193 O  O   . LEU E  350 ? 2.1005 3.5574 2.1892 0.8179  -0.4546 -0.2268 350  LEU E O   
14194 C  CB  . LEU E  350 ? 2.1037 3.1629 2.1162 0.7797  -0.4157 -0.2048 350  LEU E CB  
14195 C  CG  . LEU E  350 ? 2.0546 3.1099 2.0628 0.8576  -0.4481 -0.1537 350  LEU E CG  
14196 C  CD1 . LEU E  350 ? 2.1484 3.2031 2.1889 0.9127  -0.4476 -0.1549 350  LEU E CD1 
14197 C  CD2 . LEU E  350 ? 2.0747 2.9856 2.0336 0.8683  -0.4559 -0.1103 350  LEU E CD2 
14198 N  N   . ASP E  351 ? 2.0864 3.4949 2.1329 0.6993  -0.4252 -0.2665 351  ASP E N   
14199 C  CA  . ASP E  351 ? 2.1873 3.7468 2.2381 0.6983  -0.4486 -0.2620 351  ASP E CA  
14200 C  C   . ASP E  351 ? 2.1270 3.8301 2.2006 0.6348  -0.4328 -0.3184 351  ASP E C   
14201 O  O   . ASP E  351 ? 2.1472 3.9895 2.2241 0.6218  -0.4488 -0.3227 351  ASP E O   
14202 C  CB  . ASP E  351 ? 2.3893 3.8909 2.3953 0.6850  -0.4598 -0.2338 351  ASP E CB  
14203 C  CG  . ASP E  351 ? 2.5171 3.8999 2.4929 0.6224  -0.4298 -0.2600 351  ASP E CG  
14204 O  OD1 . ASP E  351 ? 2.6270 3.8973 2.6037 0.6167  -0.4069 -0.2713 351  ASP E OD1 
14205 O  OD2 . ASP E  351 ? 2.5752 3.9774 2.5253 0.5819  -0.4296 -0.2678 351  ASP E OD2 
14206 N  N   . GLN E  352 ? 2.0833 3.7596 2.1710 0.5937  -0.4019 -0.3611 352  GLN E N   
14207 C  CA  . GLN E  352 ? 2.1473 3.9507 2.2540 0.5281  -0.3835 -0.4171 352  GLN E CA  
14208 C  C   . GLN E  352 ? 2.4182 4.2555 2.4958 0.4618  -0.3772 -0.4410 352  GLN E C   
14209 O  O   . GLN E  352 ? 2.4474 4.4471 2.5374 0.4352  -0.3854 -0.4631 352  GLN E O   
14210 C  CB  . GLN E  352 ? 2.0276 4.0205 2.1795 0.5632  -0.4029 -0.4211 352  GLN E CB  
14211 C  CG  . GLN E  352 ? 1.9885 3.9674 2.1739 0.6206  -0.4031 -0.4120 352  GLN E CG  
14212 C  CD  . GLN E  352 ? 2.0026 3.9254 2.1950 0.5690  -0.3666 -0.4548 352  GLN E CD  
14213 O  OE1 . GLN E  352 ? 2.1136 3.8777 2.2757 0.5356  -0.3441 -0.4586 352  GLN E OE1 
14214 N  NE2 . GLN E  352 ? 1.9658 4.0255 2.1974 0.5622  -0.3609 -0.4865 352  GLN E NE2 
14215 N  N   . ASP E  353 ? 2.5981 4.2841 2.6363 0.4351  -0.3617 -0.4383 353  ASP E N   
14216 C  CA  . ASP E  353 ? 2.6277 4.3212 2.6345 0.3726  -0.3512 -0.4647 353  ASP E CA  
14217 C  C   . ASP E  353 ? 2.6068 4.2308 2.5977 0.2966  -0.3105 -0.5183 353  ASP E C   
14218 O  O   . ASP E  353 ? 2.6980 4.3149 2.6603 0.2413  -0.2966 -0.5474 353  ASP E O   
14219 C  CB  . ASP E  353 ? 2.7018 4.2862 2.6718 0.3972  -0.3637 -0.4243 353  ASP E CB  
14220 C  CG  . ASP E  353 ? 2.7640 4.1581 2.7169 0.4189  -0.3495 -0.4032 353  ASP E CG  
14221 O  OD1 . ASP E  353 ? 2.7621 4.0942 2.7246 0.4011  -0.3243 -0.4268 353  ASP E OD1 
14222 O  OD2 . ASP E  353 ? 2.7685 4.0783 2.6962 0.4512  -0.3633 -0.3624 353  ASP E OD2 
14223 N  N   . GLY E  354 ? 2.5797 4.1504 2.5860 0.2926  -0.2906 -0.5319 354  GLY E N   
14224 C  CA  . GLY E  354 ? 2.6638 4.1563 2.6515 0.2236  -0.2521 -0.5770 354  GLY E CA  
14225 C  C   . GLY E  354 ? 2.6771 3.9728 2.6367 0.2323  -0.2342 -0.5605 354  GLY E C   
14226 O  O   . GLY E  354 ? 2.7595 3.9720 2.7000 0.1813  -0.2019 -0.5923 354  GLY E O   
14227 N  N   . PHE E  355 ? 2.6011 3.8206 2.5550 0.2939  -0.2540 -0.5111 355  PHE E N   
14228 C  CA  . PHE E  355 ? 2.5948 3.6400 2.5227 0.3060  -0.2397 -0.4921 355  PHE E CA  
14229 C  C   . PHE E  355 ? 2.5467 3.5474 2.4922 0.3756  -0.2575 -0.4466 355  PHE E C   
14230 O  O   . PHE E  355 ? 2.4796 3.5397 2.4369 0.4257  -0.2880 -0.4129 355  PHE E O   
14231 C  CB  . PHE E  355 ? 2.7554 3.7370 2.6453 0.2989  -0.2420 -0.4820 355  PHE E CB  
14232 C  CG  . PHE E  355 ? 2.8093 3.8160 2.6770 0.2312  -0.2213 -0.5299 355  PHE E CG  
14233 C  CD1 . PHE E  355 ? 2.9203 3.8298 2.7668 0.1838  -0.1857 -0.5642 355  PHE E CD1 
14234 C  CD2 . PHE E  355 ? 2.7432 3.8693 2.6087 0.2146  -0.2367 -0.5409 355  PHE E CD2 
14235 C  CE1 . PHE E  355 ? 2.9614 3.8821 2.7830 0.1214  -0.1647 -0.6106 355  PHE E CE1 
14236 C  CE2 . PHE E  355 ? 2.8057 3.9537 2.6485 0.1496  -0.2160 -0.5893 355  PHE E CE2 
14237 C  CZ  . PHE E  355 ? 2.9026 3.9431 2.7226 0.1030  -0.1793 -0.6253 355  PHE E CZ  
14238 N  N   . ASN E  356 ? 2.5107 3.4060 2.4553 0.3778  -0.2379 -0.4460 356  ASN E N   
14239 C  CA  . ASN E  356 ? 2.4909 3.3340 2.4491 0.4386  -0.2506 -0.4082 356  ASN E CA  
14240 C  C   . ASN E  356 ? 2.5318 3.2951 2.4637 0.4781  -0.2693 -0.3636 356  ASN E C   
14241 O  O   . ASN E  356 ? 2.5852 3.2991 2.4851 0.4547  -0.2645 -0.3635 356  ASN E O   
14242 C  CB  . ASN E  356 ? 2.5232 3.2686 2.4810 0.4253  -0.2236 -0.4187 356  ASN E CB  
14243 C  CG  . ASN E  356 ? 2.6935 3.5249 2.6818 0.3980  -0.2097 -0.4541 356  ASN E CG  
14244 O  OD1 . ASN E  356 ? 2.8297 3.7943 2.8496 0.4140  -0.2260 -0.4605 356  ASN E OD1 
14245 N  ND2 . ASN E  356 ? 2.7007 3.4614 2.6783 0.3564  -0.1795 -0.4765 356  ASN E ND2 
14246 N  N   . ASP E  357 ? 2.5025 3.2561 2.4463 0.5379  -0.2903 -0.3269 357  ASP E N   
14247 C  CA  . ASP E  357 ? 2.5225 3.2039 2.4401 0.5769  -0.3100 -0.2811 357  ASP E CA  
14248 C  C   . ASP E  357 ? 2.3785 2.9471 2.2934 0.6100  -0.3042 -0.2590 357  ASP E C   
14249 O  O   . ASP E  357 ? 2.3315 2.8954 2.2695 0.6102  -0.2892 -0.2771 357  ASP E O   
14250 C  CB  . ASP E  357 ? 2.6218 3.4004 2.5488 0.6185  -0.3442 -0.2536 357  ASP E CB  
14251 C  CG  . ASP E  357 ? 2.5875 3.5042 2.5243 0.5846  -0.3494 -0.2804 357  ASP E CG  
14252 O  OD1 . ASP E  357 ? 2.5377 3.4432 2.4521 0.5345  -0.3357 -0.3025 357  ASP E OD1 
14253 O  OD2 . ASP E  357 ? 2.6081 3.6481 2.5750 0.6081  -0.3664 -0.2815 357  ASP E OD2 
14254 N  N   . ILE E  358 ? 2.3600 2.8400 2.2441 0.6341  -0.3154 -0.2210 358  ILE E N   
14255 C  CA  . ILE E  358 ? 2.3185 2.6851 2.1929 0.6577  -0.3081 -0.2016 358  ILE E CA  
14256 C  C   . ILE E  358 ? 2.2696 2.5868 2.1187 0.7005  -0.3329 -0.1541 358  ILE E C   
14257 O  O   . ILE E  358 ? 2.2999 2.6435 2.1281 0.7002  -0.3510 -0.1344 358  ILE E O   
14258 C  CB  . ILE E  358 ? 2.3572 2.6302 2.2088 0.6177  -0.2805 -0.2152 358  ILE E CB  
14259 C  CG1 . ILE E  358 ? 2.5035 2.6928 2.3589 0.6324  -0.2661 -0.2107 358  ILE E CG1 
14260 C  CG2 . ILE E  358 ? 2.3748 2.5957 2.1862 0.6086  -0.2867 -0.1929 358  ILE E CG2 
14261 C  CD1 . ILE E  358 ? 2.4859 2.6244 2.3367 0.5918  -0.2352 -0.2365 358  ILE E CD1 
14262 N  N   . ALA E  359 ? 2.1726 2.4195 2.0222 0.7360  -0.3335 -0.1365 359  ALA E N   
14263 C  CA  . ALA E  359 ? 2.1519 2.3252 1.9705 0.7724  -0.3525 -0.0922 359  ALA E CA  
14264 C  C   . ALA E  359 ? 2.2871 2.3358 2.0760 0.7586  -0.3358 -0.0829 359  ALA E C   
14265 O  O   . ALA E  359 ? 2.2390 2.2546 2.0420 0.7465  -0.3133 -0.1053 359  ALA E O   
14266 C  CB  . ALA E  359 ? 2.1077 2.3000 1.9465 0.8308  -0.3689 -0.0778 359  ALA E CB  
14267 N  N   . ILE E  360 ? 2.4255 2.4118 2.1716 0.7584  -0.3471 -0.0492 360  ILE E N   
14268 C  CA  . ILE E  360 ? 2.3365 2.2130 2.0497 0.7463  -0.3347 -0.0358 360  ILE E CA  
14269 C  C   . ILE E  360 ? 2.4181 2.2276 2.0972 0.7782  -0.3545 0.0064  360  ILE E C   
14270 O  O   . ILE E  360 ? 2.6326 2.4654 2.2908 0.7873  -0.3770 0.0335  360  ILE E O   
14271 C  CB  . ILE E  360 ? 2.2415 2.1056 1.9289 0.7024  -0.3240 -0.0399 360  ILE E CB  
14272 C  CG1 . ILE E  360 ? 2.2618 2.1819 1.9769 0.6711  -0.3041 -0.0813 360  ILE E CG1 
14273 C  CG2 . ILE E  360 ? 2.3053 2.0703 1.9613 0.6910  -0.3110 -0.0269 360  ILE E CG2 
14274 C  CD1 . ILE E  360 ? 2.2931 2.2077 1.9844 0.6343  -0.2940 -0.0887 360  ILE E CD1 
14275 N  N   . ALA E  361 ? 2.2555 1.9791 1.9251 0.7925  -0.3455 0.0119  361  ALA E N   
14276 C  CA  . ALA E  361 ? 2.2864 1.9331 1.9223 0.8242  -0.3615 0.0482  361  ALA E CA  
14277 C  C   . ALA E  361 ? 2.3442 1.8970 1.9280 0.7951  -0.3558 0.0698  361  ALA E C   
14278 O  O   . ALA E  361 ? 2.6238 2.1531 2.2053 0.7621  -0.3343 0.0524  361  ALA E O   
14279 C  CB  . ALA E  361 ? 2.2488 1.8635 1.9071 0.8639  -0.3562 0.0378  361  ALA E CB  
14280 N  N   . ALA E  362 ? 2.4417 1.9447 1.9814 0.8067  -0.3756 0.1093  362  ALA E N   
14281 C  CA  . ALA E  362 ? 2.4807 1.8888 1.9647 0.7811  -0.3723 0.1336  362  ALA E CA  
14282 C  C   . ALA E  362 ? 2.5205 1.8322 1.9781 0.8162  -0.3800 0.1562  362  ALA E C   
14283 O  O   . ALA E  362 ? 2.6687 1.9472 2.0902 0.8342  -0.4017 0.1934  362  ALA E O   
14284 C  CB  . ALA E  362 ? 2.7037 2.1339 2.1496 0.7539  -0.3872 0.1606  362  ALA E CB  
14285 N  N   . PRO E  363 ? 2.6615 1.9223 2.1329 0.8262  -0.3618 0.1349  363  PRO E N   
14286 C  CA  . PRO E  363 ? 2.7836 1.9610 2.2398 0.8695  -0.3675 0.1474  363  PRO E CA  
14287 C  C   . PRO E  363 ? 2.8228 1.8870 2.2075 0.8604  -0.3770 0.1872  363  PRO E C   
14288 O  O   . PRO E  363 ? 2.8748 1.8641 2.2389 0.9014  -0.3864 0.2048  363  PRO E O   
14289 C  CB  . PRO E  363 ? 2.7669 1.9192 2.2490 0.8664  -0.3411 0.1108  363  PRO E CB  
14290 C  CG  . PRO E  363 ? 2.5662 1.8142 2.0922 0.8365  -0.3265 0.0792  363  PRO E CG  
14291 C  CD  . PRO E  363 ? 2.5873 1.8661 2.0882 0.7999  -0.3349 0.0976  363  PRO E CD  
14292 N  N   . TYR E  364 ? 2.7898 1.8389 2.1338 0.8089  -0.3748 0.2023  364  TYR E N   
14293 C  CA  . TYR E  364 ? 2.9394 1.8812 2.2104 0.7897  -0.3812 0.2384  364  TYR E CA  
14294 C  C   . TYR E  364 ? 3.0459 2.0195 2.2820 0.7704  -0.4027 0.2747  364  TYR E C   
14295 O  O   . TYR E  364 ? 3.1893 2.0929 2.3618 0.7370  -0.4061 0.3038  364  TYR E O   
14296 C  CB  . TYR E  364 ? 3.0106 1.8990 2.2546 0.7396  -0.3572 0.2245  364  TYR E CB  
14297 C  CG  . TYR E  364 ? 3.0908 1.9672 2.3729 0.7519  -0.3345 0.1857  364  TYR E CG  
14298 C  CD1 . TYR E  364 ? 3.1362 1.9295 2.4123 0.7895  -0.3320 0.1821  364  TYR E CD1 
14299 C  CD2 . TYR E  364 ? 3.2103 2.1590 2.5333 0.7278  -0.3154 0.1526  364  TYR E CD2 
14300 C  CE1 . TYR E  364 ? 3.0820 1.8724 2.3932 0.7992  -0.3107 0.1447  364  TYR E CE1 
14301 C  CE2 . TYR E  364 ? 3.1771 2.1199 2.5332 0.7366  -0.2949 0.1191  364  TYR E CE2 
14302 C  CZ  . TYR E  364 ? 2.9497 1.8177 2.3007 0.7708  -0.2927 0.1143  364  TYR E CZ  
14303 O  OH  . TYR E  364 ? 2.7182 1.5869 2.1016 0.7779  -0.2719 0.0794  364  TYR E OH  
14304 N  N   . GLY E  365 ? 3.0085 2.0894 2.2831 0.7882  -0.4169 0.2728  365  GLY E N   
14305 C  CA  . GLY E  365 ? 3.0138 2.1390 2.2599 0.7731  -0.4382 0.3049  365  GLY E CA  
14306 C  C   . GLY E  365 ? 3.2177 2.3080 2.4389 0.8188  -0.4650 0.3458  365  GLY E C   
14307 O  O   . GLY E  365 ? 3.3582 2.3747 2.5777 0.8638  -0.4668 0.3513  365  GLY E O   
14308 N  N   . GLY E  366 ? 3.3420 2.4876 2.5420 0.8086  -0.4862 0.3756  366  GLY E N   
14309 C  CA  . GLY E  366 ? 3.3729 2.4979 2.5470 0.8519  -0.5143 0.4199  366  GLY E CA  
14310 C  C   . GLY E  366 ? 3.3667 2.3424 2.4606 0.8446  -0.5197 0.4633  366  GLY E C   
14311 O  O   . GLY E  366 ? 3.4877 2.3792 2.5467 0.8037  -0.5012 0.4566  366  GLY E O   
14312 N  N   . GLU E  367 ? 3.2425 2.1867 2.3033 0.8832  -0.5460 0.5101  367  GLU E N   
14313 C  CA  . GLU E  367 ? 3.3318 2.1216 2.3095 0.8795  -0.5526 0.5558  367  GLU E CA  
14314 C  C   . GLU E  367 ? 3.4300 2.0925 2.4028 0.9031  -0.5333 0.5365  367  GLU E C   
14315 O  O   . GLU E  367 ? 3.5434 2.2278 2.5720 0.9583  -0.5287 0.5088  367  GLU E O   
14316 C  CB  . GLU E  367 ? 3.4566 2.2353 2.4040 0.9282  -0.5849 0.6105  367  GLU E CB  
14317 C  CG  . GLU E  367 ? 3.5278 2.3713 2.5500 0.9983  -0.5880 0.5953  367  GLU E CG  
14318 C  CD  . GLU E  367 ? 3.7975 2.6480 2.8094 1.0300  -0.6094 0.6449  367  GLU E CD  
14319 O  OE1 . GLU E  367 ? 3.7923 2.6521 2.8497 1.0864  -0.6089 0.6402  367  GLU E OE1 
14320 O  OE2 . GLU E  367 ? 3.9639 2.8114 2.9205 0.9980  -0.6267 0.6893  367  GLU E OE2 
14321 N  N   . ASP E  368 ? 3.2659 1.7999 2.1699 0.8580  -0.5211 0.5496  368  ASP E N   
14322 C  CA  . ASP E  368 ? 3.3184 1.7168 2.2028 0.8693  -0.5013 0.5328  368  ASP E CA  
14323 C  C   . ASP E  368 ? 3.3233 1.7804 2.2792 0.8689  -0.4751 0.4709  368  ASP E C   
14324 O  O   . ASP E  368 ? 3.3179 1.6978 2.2828 0.9003  -0.4610 0.4488  368  ASP E O   
14325 C  CB  . ASP E  368 ? 3.4110 1.7553 2.3099 0.9236  -0.5036 0.5486  368  ASP E CB  
14326 C  CG  . ASP E  368 ? 3.6850 1.8665 2.5338 0.9079  -0.4834 0.5487  368  ASP E CG  
14327 O  OD1 . ASP E  368 ? 3.6589 1.7829 2.4804 0.8649  -0.4640 0.5233  368  ASP E OD1 
14328 O  OD2 . ASP E  368 ? 3.9602 2.0709 2.7944 0.9378  -0.4869 0.5745  368  ASP E OD2 
14329 N  N   . LYS E  369 ? 3.4773 2.0680 2.4819 0.8342  -0.4679 0.4426  369  LYS E N   
14330 C  CA  . LYS E  369 ? 3.3333 1.9870 2.4031 0.8285  -0.4435 0.3872  369  LYS E CA  
14331 C  C   . LYS E  369 ? 3.3140 1.9779 2.4400 0.8985  -0.4421 0.3631  369  LYS E C   
14332 O  O   . LYS E  369 ? 3.1884 1.8039 2.3303 0.9061  -0.4213 0.3312  369  LYS E O   
14333 C  CB  . LYS E  369 ? 3.3527 1.9274 2.3882 0.7746  -0.4175 0.3695  369  LYS E CB  
14334 C  CG  . LYS E  369 ? 3.4584 2.0322 2.4381 0.7039  -0.4176 0.3911  369  LYS E CG  
14335 C  CD  . LYS E  369 ? 3.4902 2.0838 2.4776 0.6505  -0.3903 0.3563  369  LYS E CD  
14336 C  CE  . LYS E  369 ? 3.5576 2.0431 2.5292 0.6517  -0.3695 0.3363  369  LYS E CE  
14337 N  NZ  . LYS E  369 ? 3.2830 1.8043 2.2668 0.6027  -0.3438 0.3028  369  LYS E NZ  
14338 N  N   . LYS E  370 ? 3.4090 2.1453 2.5649 0.9496  -0.4649 0.3782  370  LYS E N   
14339 C  CA  . LYS E  370 ? 3.2119 1.9735 2.4202 1.0213  -0.4675 0.3596  370  LYS E CA  
14340 C  C   . LYS E  370 ? 3.2489 2.1551 2.5407 1.0220  -0.4566 0.3119  370  LYS E C   
14341 O  O   . LYS E  370 ? 3.4073 2.3214 2.7429 1.0524  -0.4424 0.2766  370  LYS E O   
14342 C  CB  . LYS E  370 ? 3.1236 1.9119 2.3328 1.0654  -0.4918 0.3979  370  LYS E CB  
14343 C  CG  . LYS E  370 ? 3.2966 1.9496 2.4464 1.0660  -0.4930 0.4370  370  LYS E CG  
14344 C  CD  . LYS E  370 ? 3.4283 2.1240 2.5919 1.1140  -0.5151 0.4723  370  LYS E CD  
14345 C  CE  . LYS E  370 ? 3.4843 2.0497 2.5754 1.1047  -0.5220 0.5231  370  LYS E CE  
14346 N  NZ  . LYS E  370 ? 3.4655 2.0713 2.5727 1.1566  -0.5433 0.5589  370  LYS E NZ  
14347 N  N   . GLY E  371 ? 3.1282 2.1466 2.4401 0.9871  -0.4620 0.3091  371  GLY E N   
14348 C  CA  . GLY E  371 ? 2.9333 2.0771 2.3149 0.9758  -0.4490 0.2637  371  GLY E CA  
14349 C  C   . GLY E  371 ? 2.8888 2.1674 2.3020 0.9840  -0.4682 0.2686  371  GLY E C   
14350 O  O   . GLY E  371 ? 3.1635 2.4609 2.5680 1.0261  -0.4932 0.3003  371  GLY E O   
14351 N  N   . ILE E  372 ? 2.5515 1.9251 2.0002 0.9433  -0.4557 0.2363  372  ILE E N   
14352 C  CA  . ILE E  372 ? 2.5344 2.0410 2.0129 0.9384  -0.4690 0.2319  372  ILE E CA  
14353 C  C   . ILE E  372 ? 2.5686 2.1664 2.1099 0.9248  -0.4489 0.1794  372  ILE E C   
14354 O  O   . ILE E  372 ? 2.6678 2.2309 2.2156 0.8932  -0.4240 0.1522  372  ILE E O   
14355 C  CB  . ILE E  372 ? 2.6477 2.1677 2.0854 0.8879  -0.4754 0.2524  372  ILE E CB  
14356 C  CG1 . ILE E  372 ? 2.9246 2.3508 2.2934 0.8936  -0.4945 0.3067  372  ILE E CG1 
14357 C  CG2 . ILE E  372 ? 2.6939 2.3535 2.1622 0.8804  -0.4871 0.2428  372  ILE E CG2 
14358 C  CD1 . ILE E  372 ? 2.8619 2.3210 2.2253 0.9442  -0.5248 0.3432  372  ILE E CD1 
14359 N  N   . VAL E  373 ? 2.6146 2.3312 2.1995 0.9460  -0.4595 0.1661  373  VAL E N   
14360 C  CA  . VAL E  373 ? 2.5109 2.3247 2.1498 0.9245  -0.4421 0.1177  373  VAL E CA  
14361 C  C   . VAL E  373 ? 2.6433 2.5668 2.2887 0.8972  -0.4525 0.1145  373  VAL E C   
14362 O  O   . VAL E  373 ? 2.8412 2.8263 2.4839 0.9236  -0.4777 0.1389  373  VAL E O   
14363 C  CB  . VAL E  373 ? 2.3059 2.1731 1.9957 0.9704  -0.4408 0.0947  373  VAL E CB  
14364 C  CG1 . VAL E  373 ? 2.2585 2.2325 1.9987 0.9401  -0.4236 0.0465  373  VAL E CG1 
14365 C  CG2 . VAL E  373 ? 2.3182 2.0783 2.0023 0.9936  -0.4271 0.0913  373  VAL E CG2 
14366 N  N   . TYR E  374 ? 2.4215 2.3696 2.0741 0.8458  -0.4328 0.0842  374  TYR E N   
14367 C  CA  . TYR E  374 ? 2.3608 2.4041 2.0163 0.8132  -0.4378 0.0740  374  TYR E CA  
14368 C  C   . TYR E  374 ? 2.3185 2.4650 2.0264 0.8022  -0.4253 0.0275  374  TYR E C   
14369 O  O   . TYR E  374 ? 2.3026 2.4264 2.0342 0.7906  -0.4016 -0.0043 374  TYR E O   
14370 C  CB  . TYR E  374 ? 2.4026 2.4000 2.0242 0.7640  -0.4243 0.0720  374  TYR E CB  
14371 C  CG  . TYR E  374 ? 2.4603 2.3675 2.0259 0.7640  -0.4359 0.1166  374  TYR E CG  
14372 C  CD1 . TYR E  374 ? 2.5784 2.5163 2.1108 0.7609  -0.4592 0.1501  374  TYR E CD1 
14373 C  CD2 . TYR E  374 ? 2.4562 2.2516 1.9992 0.7620  -0.4226 0.1243  374  TYR E CD2 
14374 C  CE1 . TYR E  374 ? 2.5714 2.4269 2.0481 0.7546  -0.4689 0.1912  374  TYR E CE1 
14375 C  CE2 . TYR E  374 ? 2.4787 2.1932 1.9666 0.7548  -0.4316 0.1631  374  TYR E CE2 
14376 C  CZ  . TYR E  374 ? 2.4942 2.2371 1.9484 0.7503  -0.4547 0.1968  374  TYR E CZ  
14377 O  OH  . TYR E  374 ? 2.5636 2.2257 1.9588 0.7376  -0.4630 0.2359  374  TYR E OH  
14378 N  N   . ILE E  375 ? 2.2813 2.5433 2.0046 0.8038  -0.4413 0.0244  375  ILE E N   
14379 C  CA  . ILE E  375 ? 2.2550 2.6288 2.0235 0.7873  -0.4314 -0.0197 375  ILE E CA  
14380 C  C   . ILE E  375 ? 2.4037 2.8188 2.1627 0.7305  -0.4195 -0.0457 375  ILE E C   
14381 O  O   . ILE E  375 ? 2.5711 3.0146 2.3030 0.7197  -0.4349 -0.0261 375  ILE E O   
14382 C  CB  . ILE E  375 ? 2.1160 2.6044 1.9100 0.8274  -0.4566 -0.0091 375  ILE E CB  
14383 C  CG1 . ILE E  375 ? 2.1649 2.5971 1.9600 0.8919  -0.4703 0.0224  375  ILE E CG1 
14384 C  CG2 . ILE E  375 ? 2.1002 2.7078 1.9413 0.8067  -0.4442 -0.0576 375  ILE E CG2 
14385 C  CD1 . ILE E  375 ? 2.2367 2.6043 2.0541 0.8999  -0.4471 -0.0022 375  ILE E CD1 
14386 N  N   . PHE E  376 ? 2.3229 2.7385 2.1014 0.6943  -0.3915 -0.0899 376  PHE E N   
14387 C  CA  . PHE E  376 ? 2.2766 2.7198 2.0456 0.6419  -0.3760 -0.1205 376  PHE E CA  
14388 C  C   . PHE E  376 ? 2.3081 2.8515 2.1131 0.6162  -0.3640 -0.1667 376  PHE E C   
14389 O  O   . PHE E  376 ? 2.3436 2.8883 2.1778 0.6216  -0.3512 -0.1867 376  PHE E O   
14390 C  CB  . PHE E  376 ? 2.1973 2.5304 1.9453 0.6168  -0.3505 -0.1297 376  PHE E CB  
14391 C  CG  . PHE E  376 ? 2.1784 2.4235 1.8875 0.6313  -0.3600 -0.0889 376  PHE E CG  
14392 C  CD1 . PHE E  376 ? 2.2058 2.4625 1.8818 0.6153  -0.3705 -0.0730 376  PHE E CD1 
14393 C  CD2 . PHE E  376 ? 2.1754 2.3309 1.8794 0.6579  -0.3580 -0.0676 376  PHE E CD2 
14394 C  CE1 . PHE E  376 ? 2.2083 2.3897 1.8459 0.6232  -0.3787 -0.0357 376  PHE E CE1 
14395 C  CE2 . PHE E  376 ? 2.2012 2.2770 1.8657 0.6650  -0.3657 -0.0316 376  PHE E CE2 
14396 C  CZ  . PHE E  376 ? 2.1700 2.2596 1.8008 0.6466  -0.3762 -0.0149 376  PHE E CZ  
14397 N  N   . ASN E  377 ? 2.3774 3.0065 2.1780 0.5843  -0.3671 -0.1854 377  ASN E N   
14398 C  CA  . ASN E  377 ? 2.4252 3.1570 2.2537 0.5511  -0.3558 -0.2313 377  ASN E CA  
14399 C  C   . ASN E  377 ? 2.5985 3.2834 2.4138 0.4960  -0.3235 -0.2736 377  ASN E C   
14400 O  O   . ASN E  377 ? 2.8035 3.4208 2.5867 0.4818  -0.3168 -0.2681 377  ASN E O   
14401 C  CB  . ASN E  377 ? 2.3767 3.2438 2.2082 0.5483  -0.3793 -0.2286 377  ASN E CB  
14402 C  CG  . ASN E  377 ? 2.3267 3.2505 2.1727 0.6070  -0.4117 -0.1870 377  ASN E CG  
14403 O  OD1 . ASN E  377 ? 2.3679 3.2522 2.1882 0.6389  -0.4334 -0.1406 377  ASN E OD1 
14404 N  ND2 . ASN E  377 ? 2.2969 3.3148 2.1821 0.6217  -0.4149 -0.2033 377  ASN E ND2 
14405 N  N   . GLY E  378 ? 2.5801 3.2990 2.4186 0.4659  -0.3027 -0.3154 378  GLY E N   
14406 C  CA  . GLY E  378 ? 2.6125 3.2885 2.4359 0.4123  -0.2714 -0.3574 378  GLY E CA  
14407 C  C   . GLY E  378 ? 2.7130 3.4814 2.5278 0.3695  -0.2705 -0.3899 378  GLY E C   
14408 O  O   . GLY E  378 ? 2.6050 3.4946 2.4335 0.3759  -0.2928 -0.3855 378  GLY E O   
14409 N  N   . ARG E  379 ? 2.8440 3.5539 2.6346 0.3257  -0.2433 -0.4238 379  ARG E N   
14410 C  CA  . ARG E  379 ? 2.8322 3.6142 2.6103 0.2768  -0.2353 -0.4645 379  ARG E CA  
14411 C  C   . ARG E  379 ? 2.8713 3.5652 2.6297 0.2300  -0.1969 -0.5085 379  ARG E C   
14412 O  O   . ARG E  379 ? 2.8837 3.4684 2.6385 0.2387  -0.1795 -0.5023 379  ARG E O   
14413 C  CB  . ARG E  379 ? 2.6804 3.4853 2.4340 0.2850  -0.2530 -0.4463 379  ARG E CB  
14414 C  CG  . ARG E  379 ? 2.6422 3.3263 2.3698 0.3121  -0.2514 -0.4149 379  ARG E CG  
14415 C  CD  . ARG E  379 ? 2.6806 3.4018 2.3866 0.3256  -0.2745 -0.3876 379  ARG E CD  
14416 N  NE  . ARG E  379 ? 2.8227 3.4340 2.5030 0.3463  -0.2706 -0.3611 379  ARG E NE  
14417 C  CZ  . ARG E  379 ? 2.8809 3.4995 2.5369 0.3583  -0.2874 -0.3331 379  ARG E CZ  
14418 N  NH1 . ARG E  379 ? 2.8292 3.5558 2.4820 0.3531  -0.3102 -0.3255 379  ARG E NH1 
14419 N  NH2 . ARG E  379 ? 2.8775 3.4014 2.5112 0.3736  -0.2814 -0.3123 379  ARG E NH2 
14420 N  N   . SER E  380 ? 2.6633 3.4053 2.4065 0.1794  -0.1833 -0.5533 380  SER E N   
14421 C  CA  . SER E  380 ? 2.6481 3.3062 2.3679 0.1310  -0.1456 -0.5990 380  SER E CA  
14422 C  C   . SER E  380 ? 2.6625 3.1694 2.3540 0.1511  -0.1296 -0.5847 380  SER E C   
14423 O  O   . SER E  380 ? 2.6980 3.1032 2.3777 0.1359  -0.1021 -0.5997 380  SER E O   
14424 C  CB  . SER E  380 ? 2.6470 3.3758 2.3484 0.0766  -0.1353 -0.6482 380  SER E CB  
14425 O  OG  . SER E  380 ? 2.5872 3.3233 2.2681 0.0904  -0.1471 -0.6380 380  SER E OG  
14426 N  N   . THR E  381 ? 2.6048 3.0994 2.2844 0.1855  -0.1469 -0.5537 381  THR E N   
14427 C  CA  . THR E  381 ? 2.6249 2.9957 2.2781 0.2065  -0.1339 -0.5396 381  THR E CA  
14428 C  C   . THR E  381 ? 2.6312 2.9381 2.2968 0.2533  -0.1440 -0.4915 381  THR E C   
14429 O  O   . THR E  381 ? 2.6391 2.8500 2.2855 0.2733  -0.1345 -0.4757 381  THR E O   
14430 C  CB  . THR E  381 ? 2.7414 3.1393 2.3724 0.2136  -0.1452 -0.5348 381  THR E CB  
14431 O  OG1 . THR E  381 ? 2.9666 3.4551 2.5918 0.1709  -0.1423 -0.5770 381  THR E OG1 
14432 C  CG2 . THR E  381 ? 2.6703 2.9526 2.2699 0.2217  -0.1230 -0.5405 381  THR E CG2 
14433 N  N   . GLY E  382 ? 2.6337 2.9944 2.3305 0.2717  -0.1622 -0.4698 382  GLY E N   
14434 C  CA  . GLY E  382 ? 2.6301 2.9295 2.3373 0.3135  -0.1701 -0.4285 382  GLY E CA  
14435 C  C   . GLY E  382 ? 2.5766 2.9411 2.3021 0.3529  -0.2045 -0.3874 382  GLY E C   
14436 O  O   . GLY E  382 ? 2.6396 3.1125 2.3841 0.3496  -0.2217 -0.3923 382  GLY E O   
14437 N  N   . LEU E  383 ? 2.6733 2.9715 2.3917 0.3906  -0.2143 -0.3466 383  LEU E N   
14438 C  CA  . LEU E  383 ? 2.6631 2.9967 2.3920 0.4307  -0.2450 -0.3042 383  LEU E CA  
14439 C  C   . LEU E  383 ? 2.6048 2.9744 2.3102 0.4371  -0.2663 -0.2823 383  LEU E C   
14440 O  O   . LEU E  383 ? 2.6604 2.9854 2.3376 0.4263  -0.2574 -0.2840 383  LEU E O   
14441 C  CB  . LEU E  383 ? 2.6626 2.9033 2.3905 0.4626  -0.2437 -0.2728 383  LEU E CB  
14442 C  CG  . LEU E  383 ? 2.5616 2.8191 2.2992 0.5056  -0.2716 -0.2317 383  LEU E CG  
14443 C  CD1 . LEU E  383 ? 2.5135 2.8569 2.2882 0.5149  -0.2803 -0.2433 383  LEU E CD1 
14444 C  CD2 . LEU E  383 ? 2.5583 2.7147 2.2872 0.5297  -0.2667 -0.2053 383  LEU E CD2 
14445 N  N   . ASN E  384 ? 2.4777 2.9332 2.1944 0.4560  -0.2945 -0.2610 384  ASN E N   
14446 C  CA  . ASN E  384 ? 2.4421 2.9341 2.1347 0.4643  -0.3181 -0.2323 384  ASN E CA  
14447 C  C   . ASN E  384 ? 2.4363 2.8399 2.1061 0.4949  -0.3281 -0.1858 384  ASN E C   
14448 O  O   . ASN E  384 ? 2.4835 2.8563 2.1637 0.5286  -0.3393 -0.1574 384  ASN E O   
14449 C  CB  . ASN E  384 ? 2.3962 3.0057 2.1060 0.4782  -0.3458 -0.2196 384  ASN E CB  
14450 C  CG  . ASN E  384 ? 2.3964 3.0570 2.0791 0.4788  -0.3692 -0.1933 384  ASN E CG  
14451 O  OD1 . ASN E  384 ? 2.5659 3.1881 2.2185 0.4613  -0.3620 -0.1938 384  ASN E OD1 
14452 N  ND2 . ASN E  384 ? 2.3508 3.1043 2.0434 0.4999  -0.3973 -0.1696 384  ASN E ND2 
14453 N  N   . ALA E  385 ? 2.4885 2.8526 2.1256 0.4818  -0.3229 -0.1806 385  ALA E N   
14454 C  CA  . ALA E  385 ? 2.4978 2.7794 2.1090 0.5017  -0.3288 -0.1409 385  ALA E CA  
14455 C  C   . ALA E  385 ? 2.4429 2.7458 2.0408 0.5283  -0.3612 -0.0920 385  ALA E C   
14456 O  O   . ALA E  385 ? 2.4380 2.6667 2.0193 0.5492  -0.3675 -0.0572 385  ALA E O   
14457 C  CB  . ALA E  385 ? 2.5439 2.7987 2.1240 0.4800  -0.3160 -0.1494 385  ALA E CB  
14458 N  N   . VAL E  386 ? 2.3085 2.7088 1.9093 0.5267  -0.3815 -0.0878 386  VAL E N   
14459 C  CA  . VAL E  386 ? 2.2811 2.7013 1.8655 0.5544  -0.4135 -0.0377 386  VAL E CA  
14460 C  C   . VAL E  386 ? 2.2363 2.6823 1.8533 0.5905  -0.4260 -0.0286 386  VAL E C   
14461 O  O   . VAL E  386 ? 2.2313 2.7536 1.8830 0.5835  -0.4201 -0.0627 386  VAL E O   
14462 C  CB  . VAL E  386 ? 2.4586 2.9746 2.0233 0.5356  -0.4312 -0.0311 386  VAL E CB  
14463 C  CG1 . VAL E  386 ? 2.4615 2.9453 1.9883 0.5079  -0.4227 -0.0301 386  VAL E CG1 
14464 C  CG2 . VAL E  386 ? 2.5761 3.2004 2.1697 0.5123  -0.4244 -0.0771 386  VAL E CG2 
14465 N  N   . PRO E  387 ? 2.3721 2.7557 1.9783 0.6287  -0.4415 0.0141  387  PRO E N   
14466 C  CA  . PRO E  387 ? 2.3401 2.7481 1.9780 0.6701  -0.4530 0.0218  387  PRO E CA  
14467 C  C   . PRO E  387 ? 2.5438 3.0685 2.1885 0.6868  -0.4809 0.0383  387  PRO E C   
14468 O  O   . PRO E  387 ? 2.7641 3.3142 2.3758 0.6817  -0.5002 0.0687  387  PRO E O   
14469 C  CB  . PRO E  387 ? 2.3192 2.6115 1.9330 0.7040  -0.4602 0.0634  387  PRO E CB  
14470 C  CG  . PRO E  387 ? 2.3488 2.5965 1.9111 0.6830  -0.4674 0.0937  387  PRO E CG  
14471 C  CD  . PRO E  387 ? 2.3722 2.6579 1.9345 0.6347  -0.4477 0.0552  387  PRO E CD  
14472 N  N   . SER E  388 ? 2.5649 3.1683 2.2523 0.7065  -0.4832 0.0187  388  SER E N   
14473 C  CA  . SER E  388 ? 2.4376 3.1659 2.1368 0.7279  -0.5102 0.0338  388  SER E CA  
14474 C  C   . SER E  388 ? 2.4083 3.1132 2.1068 0.7934  -0.5352 0.0810  388  SER E C   
14475 O  O   . SER E  388 ? 2.4022 3.2033 2.1049 0.8210  -0.5616 0.1046  388  SER E O   
14476 C  CB  . SER E  388 ? 2.3912 3.2425 2.1370 0.7082  -0.4992 -0.0174 388  SER E CB  
14477 O  OG  . SER E  388 ? 2.4086 3.2324 2.1896 0.7278  -0.4843 -0.0383 388  SER E OG  
14478 N  N   . GLN E  389 ? 2.4934 3.0743 2.1856 0.8201  -0.5271 0.0947  389  GLN E N   
14479 C  CA  . GLN E  389 ? 2.5059 3.0440 2.1923 0.8845  -0.5481 0.1378  389  GLN E CA  
14480 C  C   . GLN E  389 ? 2.4692 2.8425 2.1251 0.8927  -0.5367 0.1561  389  GLN E C   
14481 O  O   . GLN E  389 ? 2.4142 2.7294 2.0794 0.8638  -0.5092 0.1234  389  GLN E O   
14482 C  CB  . GLN E  389 ? 2.4644 3.0842 2.2045 0.9240  -0.5490 0.1154  389  GLN E CB  
14483 C  CG  . GLN E  389 ? 2.4840 3.0866 2.2203 0.9990  -0.5747 0.1599  389  GLN E CG  
14484 C  CD  . GLN E  389 ? 2.4384 3.1601 2.2306 1.0385  -0.5789 0.1367  389  GLN E CD  
14485 O  OE1 . GLN E  389 ? 2.3450 3.1469 2.1780 1.0053  -0.5593 0.0852  389  GLN E OE1 
14486 N  NE2 . GLN E  389 ? 2.5163 3.2488 2.3087 1.1103  -0.6038 0.1748  389  GLN E NE2 
14487 N  N   . ILE E  390 ? 2.6702 2.9689 2.2878 0.9316  -0.5578 0.2088  390  ILE E N   
14488 C  CA  . ILE E  390 ? 2.6682 2.8085 2.2488 0.9385  -0.5494 0.2303  390  ILE E CA  
14489 C  C   . ILE E  390 ? 2.7851 2.8778 2.3740 1.0075  -0.5602 0.2508  390  ILE E C   
14490 O  O   . ILE E  390 ? 3.0899 3.2105 2.6667 1.0533  -0.5877 0.2898  390  ILE E O   
14491 C  CB  . ILE E  390 ? 2.9225 2.9945 2.4375 0.9142  -0.5616 0.2745  390  ILE E CB  
14492 C  CG1 . ILE E  390 ? 2.9897 3.1149 2.4978 0.8492  -0.5498 0.2507  390  ILE E CG1 
14493 C  CG2 . ILE E  390 ? 2.9070 2.8184 2.3815 0.9182  -0.5523 0.2952  390  ILE E CG2 
14494 C  CD1 . ILE E  390 ? 3.0709 3.3323 2.5840 0.8385  -0.5689 0.2549  390  ILE E CD1 
14495 N  N   . LEU E  391 ? 2.5387 2.5636 2.1480 1.0170  -0.5385 0.2242  391  LEU E N   
14496 C  CA  . LEU E  391 ? 2.5121 2.4796 2.1285 1.0820  -0.5441 0.2370  391  LEU E CA  
14497 C  C   . LEU E  391 ? 2.5698 2.3679 2.1253 1.0866  -0.5435 0.2730  391  LEU E C   
14498 O  O   . LEU E  391 ? 2.5572 2.2731 2.0959 1.0446  -0.5210 0.2571  391  LEU E O   
14499 C  CB  . LEU E  391 ? 2.4485 2.4436 2.1204 1.0878  -0.5200 0.1855  391  LEU E CB  
14500 C  CG  . LEU E  391 ? 2.4098 2.5606 2.1428 1.1141  -0.5255 0.1573  391  LEU E CG  
14501 C  CD1 . LEU E  391 ? 2.4023 2.6845 2.1469 1.0735  -0.5331 0.1475  391  LEU E CD1 
14502 C  CD2 . LEU E  391 ? 2.3630 2.5273 2.1420 1.1033  -0.4973 0.1055  391  LEU E CD2 
14503 N  N   . GLU E  392 ? 2.7810 2.5266 2.3020 1.1377  -0.5676 0.3211  392  GLU E N   
14504 C  CA  . GLU E  392 ? 2.8883 2.4692 2.3414 1.1384  -0.5693 0.3601  392  GLU E CA  
14505 C  C   . GLU E  392 ? 2.9058 2.3874 2.3617 1.1949  -0.5624 0.3569  392  GLU E C   
14506 O  O   . GLU E  392 ? 2.9013 2.4463 2.4024 1.2456  -0.5665 0.3485  392  GLU E O   
14507 C  CB  . GLU E  392 ? 3.4008 2.9672 2.7994 1.1519  -0.6001 0.4213  392  GLU E CB  
14508 C  CG  . GLU E  392 ? 3.5471 3.1883 2.9271 1.0901  -0.6065 0.4296  392  GLU E CG  
14509 C  CD  . GLU E  392 ? 3.6451 3.1668 2.9527 1.0398  -0.6025 0.4588  392  GLU E CD  
14510 O  OE1 . GLU E  392 ? 3.7536 3.1313 3.0245 1.0473  -0.5931 0.4704  392  GLU E OE1 
14511 O  OE2 . GLU E  392 ? 3.5971 3.1732 2.8833 0.9910  -0.6082 0.4684  392  GLU E OE2 
14512 N  N   . GLY E  393 ? 3.0988 2.4367 2.5136 1.1705  -0.5446 0.3574  393  GLY E N   
14513 C  CA  . GLY E  393 ? 3.2875 2.5224 2.7035 1.1983  -0.5284 0.3525  393  GLY E CA  
14514 C  C   . GLY E  393 ? 3.3470 2.5055 2.7232 1.2208  -0.5417 0.4031  393  GLY E C   
14515 O  O   . GLY E  393 ? 3.4078 2.5263 2.7283 1.1952  -0.5569 0.4462  393  GLY E O   
14516 N  N   . GLN E  394 ? 3.2915 2.4309 2.6958 1.2697  -0.5358 0.3973  394  GLN E N   
14517 C  CA  . GLN E  394 ? 3.4456 2.5142 2.8195 1.3015  -0.5478 0.4426  394  GLN E CA  
14518 C  C   . GLN E  394 ? 3.7212 2.6233 3.0590 1.3017  -0.5275 0.4429  394  GLN E C   
14519 O  O   . GLN E  394 ? 3.9506 2.7673 3.2524 1.3227  -0.5356 0.4824  394  GLN E O   
14520 C  CB  . GLN E  394 ? 3.4289 2.6136 2.8610 1.3659  -0.5606 0.4409  394  GLN E CB  
14521 C  CG  . GLN E  394 ? 3.2491 2.6138 2.7221 1.3682  -0.5797 0.4351  394  GLN E CG  
14522 C  CD  . GLN E  394 ? 3.3799 2.7649 2.8084 1.3435  -0.6050 0.4846  394  GLN E CD  
14523 O  OE1 . GLN E  394 ? 3.6034 2.8785 2.9749 1.3376  -0.6126 0.5315  394  GLN E OE1 
14524 N  NE2 . GLN E  394 ? 3.2221 2.7512 2.6754 1.3271  -0.6178 0.4735  394  GLN E NE2 
14525 N  N   . TRP E  395 ? 3.6589 2.5142 3.0049 1.2788  -0.5015 0.3998  395  TRP E N   
14526 C  CA  . TRP E  395 ? 3.6881 2.4080 3.0130 1.2842  -0.4794 0.3876  395  TRP E CA  
14527 C  C   . TRP E  395 ? 3.8983 2.4871 3.1522 1.2211  -0.4673 0.3965  395  TRP E C   
14528 O  O   . TRP E  395 ? 3.8496 2.4614 3.1038 1.1776  -0.4575 0.3716  395  TRP E O   
14529 C  CB  . TRP E  395 ? 3.4786 2.2512 2.8669 1.3064  -0.4579 0.3300  395  TRP E CB  
14530 C  CG  . TRP E  395 ? 3.4673 2.3830 2.9239 1.3632  -0.4698 0.3185  395  TRP E CG  
14531 C  CD1 . TRP E  395 ? 3.5954 2.5168 3.0786 1.4238  -0.4711 0.3187  395  TRP E CD1 
14532 C  CD2 . TRP E  395 ? 3.3927 2.4704 2.8962 1.3647  -0.4832 0.3060  395  TRP E CD2 
14533 N  NE1 . TRP E  395 ? 3.5749 2.6584 3.1195 1.4618  -0.4842 0.3065  395  TRP E NE1 
14534 C  CE2 . TRP E  395 ? 3.5091 2.6901 3.0666 1.4248  -0.4916 0.2980  395  TRP E CE2 
14535 C  CE3 . TRP E  395 ? 3.3054 2.4519 2.8095 1.3213  -0.4885 0.2989  395  TRP E CE3 
14536 C  CZ2 . TRP E  395 ? 3.4985 2.8515 3.1090 1.4385  -0.5047 0.2826  395  TRP E CZ2 
14537 C  CZ3 . TRP E  395 ? 3.3137 2.6238 2.8704 1.3367  -0.5013 0.2833  395  TRP E CZ3 
14538 C  CH2 . TRP E  395 ? 3.4174 2.8306 3.0261 1.3928  -0.5091 0.2750  395  TRP E CH2 
14539 N  N   . ALA E  396 ? 4.0970 2.5498 3.2884 1.2160  -0.4682 0.4323  396  ALA E N   
14540 C  CA  . ALA E  396 ? 4.1007 2.4247 3.2170 1.1539  -0.4568 0.4425  396  ALA E CA  
14541 C  C   . ALA E  396 ? 4.1879 2.4508 3.3107 1.1357  -0.4262 0.3932  396  ALA E C   
14542 O  O   . ALA E  396 ? 4.1615 2.4527 3.3380 1.1755  -0.4129 0.3571  396  ALA E O   
14543 C  CB  . ALA E  396 ? 4.1310 2.3224 3.1768 1.1526  -0.4647 0.4926  396  ALA E CB  
14544 N  N   . ALA E  397 ? 4.1266 2.3102 3.1918 1.0728  -0.4151 0.3923  397  ALA E N   
14545 C  CA  . ALA E  397 ? 3.9595 2.0920 3.0242 1.0456  -0.3868 0.3473  397  ALA E CA  
14546 C  C   . ALA E  397 ? 4.1725 2.1457 3.1826 1.0398  -0.3713 0.3517  397  ALA E C   
14547 O  O   . ALA E  397 ? 4.3993 2.2626 3.3290 0.9945  -0.3724 0.3818  397  ALA E O   
14548 C  CB  . ALA E  397 ? 3.7585 1.8959 2.7885 0.9808  -0.3830 0.3427  397  ALA E CB  
14549 N  N   . ARG E  398 ? 4.1190 2.0801 3.1701 1.0833  -0.3564 0.3204  398  ARG E N   
14550 C  CA  . ARG E  398 ? 4.2028 2.0154 3.2063 1.0723  -0.3359 0.3106  398  ARG E CA  
14551 C  C   . ARG E  398 ? 4.0783 1.8380 3.0416 1.0041  -0.3147 0.2837  398  ARG E C   
14552 O  O   . ARG E  398 ? 3.7893 1.6377 2.7769 0.9780  -0.3141 0.2664  398  ARG E O   
14553 C  CB  . ARG E  398 ? 4.2351 2.0637 3.2975 1.1328  -0.3229 0.2756  398  ARG E CB  
14554 C  CG  . ARG E  398 ? 4.1641 2.1162 3.2956 1.2015  -0.3429 0.2856  398  ARG E CG  
14555 C  CD  . ARG E  398 ? 4.1484 2.1660 3.3527 1.2498  -0.3278 0.2371  398  ARG E CD  
14556 N  NE  . ARG E  398 ? 3.9966 2.1536 3.2683 1.3085  -0.3466 0.2421  398  ARG E NE  
14557 C  CZ  . ARG E  398 ? 3.8209 2.0684 3.1620 1.3542  -0.3386 0.2039  398  ARG E CZ  
14558 N  NH1 . ARG E  398 ? 3.7833 1.9966 3.1378 1.3489  -0.3121 0.1579  398  ARG E NH1 
14559 N  NH2 . ARG E  398 ? 3.7412 2.1184 3.1369 1.4033  -0.3572 0.2109  398  ARG E NH2 
14560 N  N   . SER E  399 ? 4.2863 1.8993 3.1852 0.9746  -0.2972 0.2805  399  SER E N   
14561 C  CA  . SER E  399 ? 4.0968 1.6536 2.9492 0.9067  -0.2767 0.2561  399  SER E CA  
14562 C  C   . SER E  399 ? 3.7621 1.4185 2.6840 0.9143  -0.2603 0.2024  399  SER E C   
14563 O  O   . SER E  399 ? 3.7574 1.4529 2.7404 0.9635  -0.2509 0.1712  399  SER E O   
14564 C  CB  . SER E  399 ? 4.2269 1.6143 3.0063 0.8794  -0.2575 0.2527  399  SER E CB  
14565 O  OG  . SER E  399 ? 4.1197 1.4780 2.9365 0.9373  -0.2475 0.2315  399  SER E OG  
14566 N  N   . GLY E  400 ? 3.6788 1.3802 2.5905 0.8661  -0.2575 0.1937  400  GLY E N   
14567 C  CA  . GLY E  400 ? 3.6537 1.4431 2.6210 0.8634  -0.2415 0.1467  400  GLY E CA  
14568 C  C   . GLY E  400 ? 3.6620 1.5903 2.6770 0.8680  -0.2576 0.1523  400  GLY E C   
14569 O  O   . GLY E  400 ? 3.7795 1.7059 2.7511 0.8318  -0.2713 0.1828  400  GLY E O   
14570 N  N   . CYS E  401 ? 3.6020 1.6528 2.7041 0.9107  -0.2563 0.1232  401  CYS E N   
14571 C  CA  . CYS E  401 ? 3.6366 1.8138 2.7802 0.9113  -0.2704 0.1271  401  CYS E CA  
14572 C  C   . CYS E  401 ? 3.5664 1.7870 2.7136 0.9378  -0.2997 0.1695  401  CYS E C   
14573 O  O   . CYS E  401 ? 3.6479 1.8468 2.8018 0.9787  -0.3085 0.1858  401  CYS E O   
14574 C  CB  . CYS E  401 ? 3.7058 2.0013 2.9353 0.9411  -0.2599 0.0838  401  CYS E CB  
14575 S  SG  . CYS E  401 ? 3.8263 2.1766 3.0776 0.8896  -0.2331 0.0411  401  CYS E SG  
14576 N  N   . PRO E  402 ? 3.4805 1.7640 2.6218 0.9160  -0.3150 0.1878  402  PRO E N   
14577 C  CA  . PRO E  402 ? 3.4841 1.8345 2.6376 0.9412  -0.3427 0.2224  402  PRO E CA  
14578 C  C   . PRO E  402 ? 3.3759 1.8463 2.6147 0.9968  -0.3473 0.2010  402  PRO E C   
14579 O  O   . PRO E  402 ? 3.3115 1.8305 2.6020 1.0075  -0.3296 0.1582  402  PRO E O   
14580 C  CB  . PRO E  402 ? 3.3862 1.8213 2.5391 0.8804  -0.3444 0.2291  402  PRO E CB  
14581 C  CG  . PRO E  402 ? 3.3735 1.8428 2.5541 0.8411  -0.3166 0.1871  402  PRO E CG  
14582 C  CD  . PRO E  402 ? 3.4678 1.8133 2.6147 0.8454  -0.2989 0.1716  402  PRO E CD  
14583 N  N   . PRO E  403 ? 3.4509 1.9760 2.7041 1.0310  -0.3710 0.2300  403  PRO E N   
14584 C  CA  . PRO E  403 ? 3.3345 1.9758 2.6645 1.0847  -0.3762 0.2104  403  PRO E CA  
14585 C  C   . PRO E  403 ? 3.0407 1.7980 2.4280 1.0785  -0.3689 0.1714  403  PRO E C   
14586 O  O   . PRO E  403 ? 2.9712 1.7986 2.4189 1.1109  -0.3599 0.1378  403  PRO E O   
14587 C  CB  . PRO E  403 ? 3.5809 2.2666 2.9029 1.1084  -0.4058 0.2541  403  PRO E CB  
14588 C  CG  . PRO E  403 ? 3.5845 2.1444 2.8240 1.0775  -0.4122 0.2972  403  PRO E CG  
14589 C  CD  . PRO E  403 ? 3.5180 2.0115 2.7171 1.0198  -0.3946 0.2820  403  PRO E CD  
14590 N  N   . SER E  404 ? 2.8427 1.6303 2.2161 1.0295  -0.3690 0.1735  404  SER E N   
14591 C  CA  . SER E  404 ? 2.7601 1.6650 2.1924 1.0002  -0.3536 0.1354  404  SER E CA  
14592 C  C   . SER E  404 ? 2.9237 1.9610 2.4182 1.0394  -0.3672 0.1247  404  SER E C   
14593 O  O   . SER E  404 ? 3.0885 2.2086 2.6395 1.0417  -0.3535 0.0862  404  SER E O   
14594 C  CB  . SER E  404 ? 2.7088 1.5840 2.1594 0.9904  -0.3253 0.0950  404  SER E CB  
14595 O  OG  . SER E  404 ? 2.7696 1.5259 2.1605 0.9537  -0.3128 0.1036  404  SER E OG  
14596 N  N   . PHE E  405 ? 2.8456 1.9060 2.3271 1.0679  -0.3942 0.1597  405  PHE E N   
14597 C  CA  . PHE E  405 ? 2.6810 1.8777 2.2162 1.1002  -0.4095 0.1530  405  PHE E CA  
14598 C  C   . PHE E  405 ? 2.4733 1.7803 2.0431 1.0472  -0.3998 0.1281  405  PHE E C   
14599 O  O   . PHE E  405 ? 2.4678 1.7736 2.0079 1.0011  -0.4028 0.1447  405  PHE E O   
14600 C  CB  . PHE E  405 ? 2.7189 1.9138 2.2231 1.1337  -0.4410 0.2013  405  PHE E CB  
14601 C  CG  . PHE E  405 ? 2.5981 1.9431 2.1523 1.1628  -0.4590 0.1979  405  PHE E CG  
14602 C  CD1 . PHE E  405 ? 2.6279 2.0250 2.2223 1.2315  -0.4675 0.1889  405  PHE E CD1 
14603 C  CD2 . PHE E  405 ? 2.5439 1.9816 2.1030 1.1218  -0.4675 0.2034  405  PHE E CD2 
14604 C  CE1 . PHE E  405 ? 2.5907 2.1369 2.2302 1.2552  -0.4841 0.1852  405  PHE E CE1 
14605 C  CE2 . PHE E  405 ? 2.5103 2.0895 2.1126 1.1435  -0.4832 0.1982  405  PHE E CE2 
14606 C  CZ  . PHE E  405 ? 2.5273 2.1637 2.1697 1.2088  -0.4918 0.1897  405  PHE E CZ  
14607 N  N   . GLY E  406 ? 2.4697 1.8700 2.1001 1.0532  -0.3872 0.0872  406  GLY E N   
14608 C  CA  . GLY E  406 ? 2.3939 1.8892 2.0567 1.0051  -0.3752 0.0598  406  GLY E CA  
14609 C  C   . GLY E  406 ? 2.5529 2.0208 2.2256 0.9649  -0.3452 0.0273  406  GLY E C   
14610 O  O   . GLY E  406 ? 2.7209 2.2617 2.4221 0.9291  -0.3327 0.0019  406  GLY E O   
14611 N  N   . TYR E  407 ? 2.8533 2.2174 2.5012 0.9694  -0.3329 0.0274  407  TYR E N   
14612 C  CA  . TYR E  407 ? 2.7268 2.0626 2.3771 0.9284  -0.3053 0.0016  407  TYR E CA  
14613 C  C   . TYR E  407 ? 2.5229 1.9514 2.2318 0.9248  -0.2892 -0.0397 407  TYR E C   
14614 O  O   . TYR E  407 ? 2.4072 1.8473 2.1230 0.8814  -0.2692 -0.0583 407  TYR E O   
14615 C  CB  . TYR E  407 ? 2.6735 1.8933 2.2908 0.9396  -0.2957 0.0046  407  TYR E CB  
14616 C  CG  . TYR E  407 ? 2.7555 1.9479 2.3706 0.8966  -0.2683 -0.0187 407  TYR E CG  
14617 C  CD1 . TYR E  407 ? 2.7022 1.8538 2.2778 0.8464  -0.2613 -0.0048 407  TYR E CD1 
14618 C  CD2 . TYR E  407 ? 2.9670 2.1820 2.6191 0.9066  -0.2496 -0.0541 407  TYR E CD2 
14619 C  CE1 . TYR E  407 ? 2.8610 1.9957 2.4342 0.8098  -0.2372 -0.0237 407  TYR E CE1 
14620 C  CE2 . TYR E  407 ? 3.0479 2.2427 2.6963 0.8672  -0.2253 -0.0728 407  TYR E CE2 
14621 C  CZ  . TYR E  407 ? 3.0322 2.1869 2.6411 0.8201  -0.2196 -0.0565 407  TYR E CZ  
14622 O  OH  . TYR E  407 ? 3.0168 2.1597 2.6220 0.7838  -0.1964 -0.0729 407  TYR E OH  
14623 N  N   . SER E  408 ? 2.5051 2.0023 2.2548 0.9692  -0.2972 -0.0536 408  SER E N   
14624 C  CA  . SER E  408 ? 2.4897 2.0903 2.2941 0.9614  -0.2838 -0.0919 408  SER E CA  
14625 C  C   . SER E  408 ? 2.5076 2.2194 2.3461 0.9926  -0.3034 -0.0930 408  SER E C   
14626 O  O   . SER E  408 ? 2.6233 2.3272 2.4541 1.0430  -0.3249 -0.0703 408  SER E O   
14627 C  CB  . SER E  408 ? 2.5389 2.1226 2.3651 0.9813  -0.2660 -0.1200 408  SER E CB  
14628 O  OG  . SER E  408 ? 2.6549 2.2141 2.4816 1.0446  -0.2799 -0.1117 408  SER E OG  
14629 N  N   . MET E  409 ? 2.3242 2.1390 2.1978 0.9621  -0.2958 -0.1186 409  MET E N   
14630 C  CA  . MET E  409 ? 2.2526 2.1890 2.1603 0.9847  -0.3127 -0.1242 409  MET E CA  
14631 C  C   . MET E  409 ? 2.4116 2.4513 2.3600 0.9457  -0.2952 -0.1642 409  MET E C   
14632 O  O   . MET E  409 ? 2.4458 2.4556 2.3880 0.8960  -0.2731 -0.1798 409  MET E O   
14633 C  CB  . MET E  409 ? 2.2010 2.1469 2.0813 0.9800  -0.3354 -0.0918 409  MET E CB  
14634 C  CG  . MET E  409 ? 2.2105 2.1082 2.0577 0.9216  -0.3258 -0.0850 409  MET E CG  
14635 S  SD  . MET E  409 ? 2.2371 2.1341 2.0455 0.9219  -0.3535 -0.0437 409  MET E SD  
14636 C  CE  . MET E  409 ? 2.3852 2.2652 2.1725 0.8508  -0.3355 -0.0541 409  MET E CE  
14637 N  N   . LYS E  410 ? 2.4858 2.6491 2.4739 0.9687  -0.3056 -0.1795 410  LYS E N   
14638 C  CA  . LYS E  410 ? 2.4766 2.7504 2.5023 0.9302  -0.2907 -0.2184 410  LYS E CA  
14639 C  C   . LYS E  410 ? 2.3012 2.7084 2.3512 0.9427  -0.3105 -0.2210 410  LYS E C   
14640 O  O   . LYS E  410 ? 2.2556 2.6977 2.3136 1.0017  -0.3336 -0.2021 410  LYS E O   
14641 C  CB  . LYS E  410 ? 2.6170 2.9212 2.6772 0.9421  -0.2729 -0.2503 410  LYS E CB  
14642 C  CG  . LYS E  410 ? 2.6823 3.0805 2.7720 0.8891  -0.2528 -0.2897 410  LYS E CG  
14643 C  CD  . LYS E  410 ? 2.7758 3.0934 2.8376 0.8250  -0.2298 -0.2936 410  LYS E CD  
14644 C  CE  . LYS E  410 ? 2.8062 3.2055 2.8809 0.7660  -0.2165 -0.3219 410  LYS E CE  
14645 N  NZ  . LYS E  410 ? 2.9246 3.4464 3.0437 0.7650  -0.2090 -0.3572 410  LYS E NZ  
14646 N  N   . GLY E  411 ? 2.3157 2.7950 2.3744 0.8869  -0.3012 -0.2438 411  GLY E N   
14647 C  CA  . GLY E  411 ? 2.3156 2.9331 2.3968 0.8877  -0.3172 -0.2518 411  GLY E CA  
14648 C  C   . GLY E  411 ? 2.3653 3.0996 2.4806 0.8411  -0.2994 -0.2973 411  GLY E C   
14649 O  O   . GLY E  411 ? 2.3801 3.1066 2.5112 0.8229  -0.2770 -0.3233 411  GLY E O   
14650 N  N   . ALA E  412 ? 2.2822 3.1262 2.4056 0.8175  -0.3089 -0.3072 412  ALA E N   
14651 C  CA  . ALA E  412 ? 2.3051 3.2630 2.4528 0.7616  -0.2924 -0.3510 412  ALA E CA  
14652 C  C   . ALA E  412 ? 2.3161 3.4023 2.5121 0.7891  -0.2927 -0.3760 412  ALA E C   
14653 O  O   . ALA E  412 ? 2.4507 3.6037 2.6655 0.7402  -0.2714 -0.4148 412  ALA E O   
14654 C  CB  . ALA E  412 ? 2.3514 3.2225 2.4787 0.6934  -0.2600 -0.3728 412  ALA E CB  
14655 N  N   . THR E  413 ? 2.1990 3.3204 2.4136 0.8670  -0.3159 -0.3545 413  THR E N   
14656 C  CA  . THR E  413 ? 2.1264 3.3830 2.3892 0.9046  -0.3191 -0.3771 413  THR E CA  
14657 C  C   . THR E  413 ? 2.1052 3.4732 2.3854 0.9685  -0.3525 -0.3554 413  THR E C   
14658 O  O   . THR E  413 ? 2.1790 3.4680 2.4374 1.0259  -0.3740 -0.3128 413  THR E O   
14659 C  CB  . THR E  413 ? 2.1115 3.2912 2.3837 0.9481  -0.3092 -0.3772 413  THR E CB  
14660 O  OG1 . THR E  413 ? 2.2186 3.3167 2.4778 0.8865  -0.2780 -0.3987 413  THR E OG1 
14661 C  CG2 . THR E  413 ? 2.0879 3.4166 2.4115 0.9944  -0.3139 -0.4012 413  THR E CG2 
14662 N  N   . ASP E  414 ? 2.1335 3.6870 2.4508 0.9577  -0.3566 -0.3836 414  ASP E N   
14663 C  CA  . ASP E  414 ? 2.1464 3.8352 2.4841 1.0159  -0.3885 -0.3654 414  ASP E CA  
14664 C  C   . ASP E  414 ? 2.1643 3.9192 2.5411 1.1019  -0.3984 -0.3657 414  ASP E C   
14665 O  O   . ASP E  414 ? 2.0279 3.9360 2.4484 1.0988  -0.3912 -0.4029 414  ASP E O   
14666 C  CB  . ASP E  414 ? 2.0724 3.9367 2.4278 0.9567  -0.3878 -0.3969 414  ASP E CB  
14667 C  CG  . ASP E  414 ? 2.1137 4.1229 2.4859 1.0112  -0.4218 -0.3749 414  ASP E CG  
14668 O  OD1 . ASP E  414 ? 2.1418 4.0821 2.4972 1.0837  -0.4470 -0.3267 414  ASP E OD1 
14669 O  OD2 . ASP E  414 ? 2.1827 4.3758 2.5824 0.9794  -0.4231 -0.4051 414  ASP E OD2 
14670 N  N   . ILE E  415 ? 2.2668 3.9063 2.6259 1.1797  -0.4149 -0.3244 415  ILE E N   
14671 C  CA  . ILE E  415 ? 2.0986 3.7581 2.4874 1.2650  -0.4200 -0.3253 415  ILE E CA  
14672 C  C   . ILE E  415 ? 2.0345 3.8703 2.4591 1.3376  -0.4484 -0.3167 415  ILE E C   
14673 O  O   . ILE E  415 ? 2.0580 3.9678 2.5202 1.4010  -0.4495 -0.3318 415  ILE E O   
14674 C  CB  . ILE E  415 ? 2.3116 3.7676 2.6620 1.3194  -0.4248 -0.2860 415  ILE E CB  
14675 C  CG1 . ILE E  415 ? 2.2896 3.7285 2.6662 1.3797  -0.4146 -0.3040 415  ILE E CG1 
14676 C  CG2 . ILE E  415 ? 2.3375 3.7679 2.6628 1.3848  -0.4594 -0.2319 415  ILE E CG2 
14677 C  CD1 . ILE E  415 ? 2.4203 3.6555 2.7569 1.4251  -0.4149 -0.2726 415  ILE E CD1 
14678 N  N   . ASP E  416 ? 2.0646 3.9789 2.4796 1.3317  -0.4713 -0.2941 416  ASP E N   
14679 C  CA  . ASP E  416 ? 2.0825 4.1694 2.5289 1.4038  -0.5007 -0.2806 416  ASP E CA  
14680 C  C   . ASP E  416 ? 2.0522 4.3588 2.5302 1.3445  -0.5002 -0.3160 416  ASP E C   
14681 O  O   . ASP E  416 ? 2.0542 4.5248 2.5558 1.3923  -0.5262 -0.3039 416  ASP E O   
14682 C  CB  . ASP E  416 ? 2.2764 4.2841 2.6839 1.4627  -0.5332 -0.2169 416  ASP E CB  
14683 C  CG  . ASP E  416 ? 2.4018 4.3765 2.7700 1.3877  -0.5369 -0.2012 416  ASP E CG  
14684 O  OD1 . ASP E  416 ? 2.3388 4.2705 2.6963 1.2953  -0.5103 -0.2332 416  ASP E OD1 
14685 O  OD2 . ASP E  416 ? 2.5834 4.5730 2.9295 1.4228  -0.5661 -0.1564 416  ASP E OD2 
14686 N  N   . LYS E  417 ? 1.9719 4.2855 2.4489 1.2412  -0.4707 -0.3595 417  LYS E N   
14687 C  CA  . LYS E  417 ? 1.9342 4.4461 2.4369 1.1709  -0.4641 -0.4012 417  LYS E CA  
14688 C  C   . LYS E  417 ? 1.9816 4.5885 2.4714 1.1670  -0.4909 -0.3765 417  LYS E C   
14689 O  O   . LYS E  417 ? 1.9382 4.7579 2.4595 1.1552  -0.4998 -0.3983 417  LYS E O   
14690 C  CB  . LYS E  417 ? 2.0059 4.7119 2.5673 1.2039  -0.4617 -0.4377 417  LYS E CB  
14691 C  CG  . LYS E  417 ? 2.0371 4.6742 2.6137 1.1973  -0.4328 -0.4691 417  LYS E CG  
14692 C  CD  . LYS E  417 ? 1.8893 4.4904 2.4512 1.0766  -0.3971 -0.5114 417  LYS E CD  
14693 C  CE  . LYS E  417 ? 1.8448 4.6648 2.4323 1.0064  -0.3909 -0.5550 417  LYS E CE  
14694 N  NZ  . LYS E  417 ? 1.8524 4.6277 2.4201 0.8878  -0.3550 -0.5956 417  LYS E NZ  
14695 N  N   . ASN E  418 ? 2.3801 4.8382 2.8227 1.1736  -0.5037 -0.3318 418  ASN E N   
14696 C  CA  . ASN E  418 ? 2.3832 4.9176 2.8080 1.1684  -0.5292 -0.3049 418  ASN E CA  
14697 C  C   . ASN E  418 ? 2.1961 4.7246 2.5947 1.0551  -0.5104 -0.3334 418  ASN E C   
14698 O  O   . ASN E  418 ? 2.0911 4.6772 2.4708 1.0377  -0.5279 -0.3164 418  ASN E O   
14699 C  CB  . ASN E  418 ? 2.4560 4.8443 2.8411 1.2393  -0.5556 -0.2381 418  ASN E CB  
14700 C  CG  . ASN E  418 ? 2.2218 4.3984 2.5529 1.1843  -0.5409 -0.2239 418  ASN E CG  
14701 O  OD1 . ASN E  418 ? 2.0864 4.1649 2.4113 1.1264  -0.5098 -0.2556 418  ASN E OD1 
14702 N  ND2 . ASN E  418 ? 2.2020 4.3120 2.4929 1.2037  -0.5639 -0.1745 418  ASN E ND2 
14703 N  N   . GLY E  419 ? 2.0634 4.5181 2.4574 0.9797  -0.4749 -0.3752 419  GLY E N   
14704 C  CA  . GLY E  419 ? 2.0778 4.5091 2.4443 0.8742  -0.4533 -0.4055 419  GLY E CA  
14705 C  C   . GLY E  419 ? 2.2814 4.4918 2.5966 0.8485  -0.4431 -0.3827 419  GLY E C   
14706 O  O   . GLY E  419 ? 2.3975 4.5698 2.6871 0.7646  -0.4228 -0.4084 419  GLY E O   
14707 N  N   . TYR E  420 ? 2.3012 4.3656 2.5991 0.9173  -0.4555 -0.3368 420  TYR E N   
14708 C  CA  . TYR E  420 ? 2.3459 4.2113 2.5947 0.8975  -0.4484 -0.3117 420  TYR E CA  
14709 C  C   . TYR E  420 ? 2.2997 4.0025 2.5429 0.9297  -0.4345 -0.3015 420  TYR E C   
14710 O  O   . TYR E  420 ? 2.5165 4.2288 2.7818 1.0048  -0.4463 -0.2857 420  TYR E O   
14711 C  CB  . TYR E  420 ? 2.3855 4.2273 2.6046 0.9412  -0.4807 -0.2580 420  TYR E CB  
14712 C  CG  . TYR E  420 ? 2.2541 4.2524 2.4737 0.9075  -0.4954 -0.2651 420  TYR E CG  
14713 C  CD1 . TYR E  420 ? 2.1826 4.3779 2.4388 0.9452  -0.5172 -0.2662 420  TYR E CD1 
14714 C  CD2 . TYR E  420 ? 2.1270 4.0821 2.3104 0.8388  -0.4870 -0.2723 420  TYR E CD2 
14715 C  CE1 . TYR E  420 ? 2.0805 4.4273 2.3362 0.9112  -0.5304 -0.2737 420  TYR E CE1 
14716 C  CE2 . TYR E  420 ? 2.0587 4.1577 2.2408 0.8048  -0.4990 -0.2821 420  TYR E CE2 
14717 C  CZ  . TYR E  420 ? 2.0685 4.3641 2.2863 0.8392  -0.5208 -0.2825 420  TYR E CZ  
14718 O  OH  . TYR E  420 ? 2.2092 4.6565 2.4247 0.8019  -0.5325 -0.2932 420  TYR E OH  
14719 N  N   . PRO E  421 ? 2.0242 3.5795 2.2376 0.8760  -0.4090 -0.3113 421  PRO E N   
14720 C  CA  . PRO E  421 ? 2.0778 3.4811 2.2830 0.9025  -0.3957 -0.3011 421  PRO E CA  
14721 C  C   . PRO E  421 ? 2.0157 3.3001 2.1911 0.9686  -0.4182 -0.2463 421  PRO E C   
14722 O  O   . PRO E  421 ? 2.0073 3.2650 2.1510 0.9665  -0.4351 -0.2158 421  PRO E O   
14723 C  CB  . PRO E  421 ? 2.0779 3.3734 2.2557 0.8226  -0.3646 -0.3240 421  PRO E CB  
14724 C  CG  . PRO E  421 ? 2.0983 3.4302 2.2532 0.7743  -0.3696 -0.3257 421  PRO E CG  
14725 C  CD  . PRO E  421 ? 2.0488 3.5753 2.2355 0.7885  -0.3895 -0.3354 421  PRO E CD  
14726 N  N   . ASP E  422 ? 2.2030 3.4155 2.3862 1.0250  -0.4173 -0.2353 422  ASP E N   
14727 C  CA  . ASP E  422 ? 2.1656 3.2626 2.3205 1.0924  -0.4371 -0.1859 422  ASP E CA  
14728 C  C   . ASP E  422 ? 2.2716 3.1826 2.3926 1.0723  -0.4169 -0.1794 422  ASP E C   
14729 O  O   . ASP E  422 ? 2.2795 3.1568 2.4005 1.0113  -0.3894 -0.2103 422  ASP E O   
14730 C  CB  . ASP E  422 ? 2.1521 3.3118 2.3393 1.1799  -0.4530 -0.1781 422  ASP E CB  
14731 C  CG  . ASP E  422 ? 2.2843 3.6534 2.5128 1.1973  -0.4698 -0.1918 422  ASP E CG  
14732 O  OD1 . ASP E  422 ? 2.3198 3.8077 2.5878 1.1631  -0.4528 -0.2386 422  ASP E OD1 
14733 O  OD2 . ASP E  422 ? 2.4011 3.8210 2.6208 1.2417  -0.4997 -0.1554 422  ASP E OD2 
14734 N  N   . LEU E  423 ? 2.4021 3.1917 2.4910 1.1233  -0.4307 -0.1376 423  LEU E N   
14735 C  CA  . LEU E  423 ? 2.3643 2.9796 2.4126 1.1022  -0.4155 -0.1247 423  LEU E CA  
14736 C  C   . LEU E  423 ? 2.5319 3.0421 2.5671 1.1697  -0.4216 -0.1010 423  LEU E C   
14737 O  O   . LEU E  423 ? 2.6247 3.1299 2.6472 1.2304  -0.4474 -0.0650 423  LEU E O   
14738 C  CB  . LEU E  423 ? 2.3571 2.9083 2.3577 1.0672  -0.4248 -0.0940 423  LEU E CB  
14739 C  CG  . LEU E  423 ? 2.4489 2.8260 2.4016 1.0557  -0.4158 -0.0707 423  LEU E CG  
14740 C  CD1 . LEU E  423 ? 2.6987 3.0260 2.6573 1.0039  -0.3828 -0.1057 423  LEU E CD1 
14741 C  CD2 . LEU E  423 ? 2.4201 2.7577 2.3273 1.0303  -0.4298 -0.0371 423  LEU E CD2 
14742 N  N   . ILE E  424 ? 2.5722 2.9950 2.6070 1.1584  -0.3974 -0.1208 424  ILE E N   
14743 C  CA  . ILE E  424 ? 2.6203 2.9204 2.6346 1.2104  -0.3977 -0.1032 424  ILE E CA  
14744 C  C   . ILE E  424 ? 2.6093 2.7506 2.5676 1.1736  -0.3898 -0.0796 424  ILE E C   
14745 O  O   . ILE E  424 ? 2.3415 2.4597 2.2931 1.1090  -0.3694 -0.0971 424  ILE E O   
14746 C  CB  . ILE E  424 ? 2.6094 2.9291 2.6614 1.2250  -0.3760 -0.1435 424  ILE E CB  
14747 C  CG1 . ILE E  424 ? 2.9486 3.4431 3.0581 1.2574  -0.3830 -0.1701 424  ILE E CG1 
14748 C  CG2 . ILE E  424 ? 2.4550 2.6450 2.4832 1.2798  -0.3755 -0.1284 424  ILE E CG2 
14749 C  CD1 . ILE E  424 ? 3.0688 3.6076 3.2187 1.2593  -0.3594 -0.2153 424  ILE E CD1 
14750 N  N   . VAL E  425 ? 2.8429 2.8748 2.7589 1.2148  -0.4053 -0.0395 425  VAL E N   
14751 C  CA  . VAL E  425 ? 2.8870 2.7712 2.7451 1.1822  -0.4000 -0.0138 425  VAL E CA  
14752 C  C   . VAL E  425 ? 2.8771 2.6333 2.7115 1.2230  -0.3939 -0.0068 425  VAL E C   
14753 O  O   . VAL E  425 ? 2.8224 2.5538 2.6488 1.2898  -0.4116 0.0152  425  VAL E O   
14754 C  CB  . VAL E  425 ? 2.7468 2.6125 2.5628 1.1784  -0.4248 0.0319  425  VAL E CB  
14755 C  CG1 . VAL E  425 ? 2.8391 2.5578 2.5940 1.1439  -0.4187 0.0572  425  VAL E CG1 
14756 C  CG2 . VAL E  425 ? 2.4854 2.4776 2.3232 1.1351  -0.4289 0.0202  425  VAL E CG2 
14757 N  N   . GLY E  426 ? 2.9313 2.6054 2.7521 1.1837  -0.3686 -0.0253 426  GLY E N   
14758 C  CA  . GLY E  426 ? 2.9201 2.4702 2.7153 1.2116  -0.3588 -0.0245 426  GLY E CA  
14759 C  C   . GLY E  426 ? 3.0416 2.4474 2.7660 1.1946  -0.3646 0.0152  426  GLY E C   
14760 O  O   . GLY E  426 ? 3.1712 2.5637 2.8692 1.1393  -0.3638 0.0293  426  GLY E O   
14761 N  N   . ALA E  427 ? 2.9946 2.2984 2.6902 1.2293  -0.3653 0.0313  427  ALA E N   
14762 C  CA  . ALA E  427 ? 2.9256 2.0860 2.5518 1.2033  -0.3654 0.0662  427  ALA E CA  
14763 C  C   . ALA E  427 ? 3.1173 2.1773 2.7314 1.2048  -0.3419 0.0487  427  ALA E C   
14764 O  O   . ALA E  427 ? 3.4130 2.4202 3.0172 1.2388  -0.3440 0.0620  427  ALA E O   
14765 C  CB  . ALA E  427 ? 2.8409 1.9846 2.4373 1.2268  -0.3912 0.1148  427  ALA E CB  
14766 N  N   . PHE E  428 ? 2.9600 1.9927 2.5733 1.1677  -0.3191 0.0183  428  PHE E N   
14767 C  CA  . PHE E  428 ? 2.9092 1.8699 2.5195 1.1689  -0.2952 -0.0070 428  PHE E CA  
14768 C  C   . PHE E  428 ? 2.9365 1.7464 2.4794 1.1556  -0.2929 0.0208  428  PHE E C   
14769 O  O   . PHE E  428 ? 2.9921 1.7375 2.5307 1.1717  -0.2782 0.0062  428  PHE E O   
14770 C  CB  . PHE E  428 ? 2.8946 1.8722 2.5193 1.1302  -0.2721 -0.0449 428  PHE E CB  
14771 C  CG  . PHE E  428 ? 2.8192 1.7268 2.3915 1.0757  -0.2687 -0.0296 428  PHE E CG  
14772 C  CD1 . PHE E  428 ? 2.8394 1.6222 2.3564 1.0471  -0.2554 -0.0239 428  PHE E CD1 
14773 C  CD2 . PHE E  428 ? 2.7614 1.7474 2.3454 1.0359  -0.2741 -0.0214 428  PHE E CD2 
14774 C  CE1 . PHE E  428 ? 2.8369 1.5750 2.3088 0.9888  -0.2508 -0.0095 428  PHE E CE1 
14775 C  CE2 . PHE E  428 ? 2.8054 1.7510 2.3494 0.9744  -0.2671 -0.0073 428  PHE E CE2 
14776 C  CZ  . PHE E  428 ? 2.7889 1.6159 2.2778 0.9510  -0.2560 -0.0007 428  PHE E CZ  
14777 N  N   . GLY E  429 ? 2.8876 1.6401 2.3761 1.1257  -0.3065 0.0590  429  GLY E N   
14778 C  CA  . GLY E  429 ? 2.9899 1.5972 2.4082 1.1066  -0.3039 0.0852  429  GLY E CA  
14779 C  C   . GLY E  429 ? 3.1142 1.6713 2.5237 1.1531  -0.3130 0.1073  429  GLY E C   
14780 O  O   . GLY E  429 ? 3.1731 1.6024 2.5325 1.1444  -0.3040 0.1169  429  GLY E O   
14781 N  N   . VAL E  430 ? 3.3424 1.9970 2.7978 1.2025  -0.3304 0.1153  430  VAL E N   
14782 C  CA  . VAL E  430 ? 3.4565 2.0821 2.9129 1.2561  -0.3400 0.1353  430  VAL E CA  
14783 C  C   . VAL E  430 ? 3.3762 2.0994 2.9037 1.3092  -0.3339 0.0998  430  VAL E C   
14784 O  O   . VAL E  430 ? 3.5971 2.3332 3.1389 1.3630  -0.3450 0.1145  430  VAL E O   
14785 C  CB  . VAL E  430 ? 3.4091 2.0588 2.8458 1.2709  -0.3701 0.1863  430  VAL E CB  
14786 C  CG1 . VAL E  430 ? 3.3127 1.8404 2.6682 1.2239  -0.3753 0.2258  430  VAL E CG1 
14787 C  CG2 . VAL E  430 ? 3.3844 2.1877 2.8671 1.2709  -0.3850 0.1807  430  VAL E CG2 
14788 N  N   . ASP E  431 ? 3.1821 1.9780 2.7530 1.2948  -0.3167 0.0542  431  ASP E N   
14789 C  CA  . ASP E  431 ? 3.1930 2.0871 2.8300 1.3371  -0.3078 0.0147  431  ASP E CA  
14790 C  C   . ASP E  431 ? 3.2039 2.2237 2.8837 1.3873  -0.3313 0.0282  431  ASP E C   
14791 O  O   . ASP E  431 ? 3.4217 2.4613 3.1239 1.4425  -0.3350 0.0277  431  ASP E O   
14792 C  CB  . ASP E  431 ? 3.3341 2.1372 2.9628 1.3634  -0.2898 -0.0019 431  ASP E CB  
14793 C  CG  . ASP E  431 ? 3.2670 1.9464 2.8495 1.3127  -0.2666 -0.0161 431  ASP E CG  
14794 O  OD1 . ASP E  431 ? 3.1152 1.8331 2.7191 1.2821  -0.2482 -0.0536 431  ASP E OD1 
14795 O  OD2 . ASP E  431 ? 3.4141 1.9590 2.9363 1.3016  -0.2667 0.0106  431  ASP E OD2 
14796 N  N   . ARG E  432 ? 3.0073 2.1178 2.6989 1.3680  -0.3469 0.0383  432  ARG E N   
14797 C  CA  . ARG E  432 ? 2.9952 2.2288 2.7210 1.4087  -0.3711 0.0538  432  ARG E CA  
14798 C  C   . ARG E  432 ? 3.0651 2.4372 2.8313 1.3873  -0.3757 0.0316  432  ARG E C   
14799 O  O   . ARG E  432 ? 3.3563 2.7075 3.1063 1.3369  -0.3683 0.0239  432  ARG E O   
14800 C  CB  . ARG E  432 ? 3.0712 2.2478 2.7487 1.4141  -0.3949 0.1106  432  ARG E CB  
14801 C  CG  . ARG E  432 ? 3.1362 2.3812 2.8370 1.4762  -0.4148 0.1317  432  ARG E CG  
14802 C  CD  . ARG E  432 ? 3.2654 2.4180 2.9580 1.5170  -0.4037 0.1302  432  ARG E CD  
14803 N  NE  . ARG E  432 ? 3.3549 2.3305 2.9778 1.4925  -0.3984 0.1595  432  ARG E NE  
14804 C  CZ  . ARG E  432 ? 3.5502 2.4478 3.1323 1.5158  -0.4142 0.2068  432  ARG E CZ  
14805 N  NH1 . ARG E  432 ? 3.6956 2.6789 3.3010 1.5666  -0.4368 0.2314  432  ARG E NH1 
14806 N  NH2 . ARG E  432 ? 3.5635 2.2992 3.0797 1.4874  -0.4073 0.2298  432  ARG E NH2 
14807 N  N   . ALA E  433 ? 2.8327 2.3488 2.6509 1.4269  -0.3881 0.0210  433  ALA E N   
14808 C  CA  . ALA E  433 ? 2.7311 2.3914 2.5880 1.4121  -0.3966 0.0029  433  ALA E CA  
14809 C  C   . ALA E  433 ? 2.7416 2.5114 2.6155 1.4495  -0.4245 0.0287  433  ALA E C   
14810 O  O   . ALA E  433 ? 2.8166 2.6085 2.7045 1.5004  -0.4309 0.0377  433  ALA E O   
14811 C  CB  . ALA E  433 ? 2.7685 2.5264 2.6831 1.4137  -0.3776 -0.0528 433  ALA E CB  
14812 N  N   . ILE E  434 ? 2.6498 2.4895 2.5211 1.4246  -0.4410 0.0407  434  ILE E N   
14813 C  CA  . ILE E  434 ? 2.7799 2.7214 2.6591 1.4508  -0.4687 0.0696  434  ILE E CA  
14814 C  C   . ILE E  434 ? 2.7033 2.8236 2.6334 1.4394  -0.4754 0.0379  434  ILE E C   
14815 O  O   . ILE E  434 ? 2.5751 2.7019 2.5041 1.3850  -0.4659 0.0187  434  ILE E O   
14816 C  CB  . ILE E  434 ? 2.8838 2.7364 2.7011 1.4295  -0.4863 0.1225  434  ILE E CB  
14817 C  CG1 . ILE E  434 ? 3.0322 2.7018 2.7964 1.4318  -0.4770 0.1498  434  ILE E CG1 
14818 C  CG2 . ILE E  434 ? 2.9814 2.9400 2.8063 1.4593  -0.5147 0.1545  434  ILE E CG2 
14819 C  CD1 . ILE E  434 ? 2.9799 2.5241 2.7050 1.3780  -0.4578 0.1410  434  ILE E CD1 
14820 N  N   . LEU E  435 ? 2.7967 3.0631 2.7707 1.4782  -0.4876 0.0312  435  LEU E N   
14821 C  CA  . LEU E  435 ? 2.6954 3.1513 2.7197 1.4671  -0.4955 0.0007  435  LEU E CA  
14822 C  C   . LEU E  435 ? 2.9938 3.5240 3.0023 1.4631  -0.5238 0.0365  435  LEU E C   
14823 O  O   . LEU E  435 ? 3.2074 3.7556 3.2077 1.5011  -0.5399 0.0707  435  LEU E O   
14824 C  CB  . LEU E  435 ? 2.5565 3.1492 2.6409 1.5055  -0.4898 -0.0338 435  LEU E CB  
14825 C  CG  . LEU E  435 ? 2.4226 3.2296 2.5620 1.4885  -0.4963 -0.0680 435  LEU E CG  
14826 C  CD1 . LEU E  435 ? 2.3692 3.1761 2.5186 1.3947  -0.4647 -0.1116 435  LEU E CD1 
14827 C  CD2 . LEU E  435 ? 2.4193 3.3640 2.6098 1.5349  -0.4955 -0.0913 435  LEU E CD2 
14828 N  N   . TYR E  436 ? 2.9284 3.4917 2.9298 1.3871  -0.5179 0.0262  436  TYR E N   
14829 C  CA  . TYR E  436 ? 2.9586 3.6132 2.9496 1.3692  -0.5404 0.0502  436  TYR E CA  
14830 C  C   . TYR E  436 ? 2.7159 3.5684 2.7619 1.3395  -0.5364 0.0077  436  TYR E C   
14831 O  O   . TYR E  436 ? 2.6964 3.5738 2.7639 1.2767  -0.5097 -0.0379 436  TYR E O   
14832 C  CB  . TYR E  436 ? 2.9865 3.5430 2.9272 1.2998  -0.5349 0.0671  436  TYR E CB  
14833 C  CG  . TYR E  436 ? 2.9761 3.3536 2.8550 1.3226  -0.5431 0.1151  436  TYR E CG  
14834 C  CD1 . TYR E  436 ? 2.9737 3.3342 2.8155 1.3632  -0.5738 0.1701  436  TYR E CD1 
14835 C  CD2 . TYR E  436 ? 3.0215 3.2491 2.8762 1.3002  -0.5199 0.1063  436  TYR E CD2 
14836 C  CE1 . TYR E  436 ? 3.0432 3.2351 2.8235 1.3742  -0.5787 0.2138  436  TYR E CE1 
14837 C  CE2 . TYR E  436 ? 3.0926 3.1587 2.8872 1.3141  -0.5261 0.1480  436  TYR E CE2 
14838 C  CZ  . TYR E  436 ? 3.0595 3.1053 2.8156 1.3515  -0.5559 0.2017  436  TYR E CZ  
14839 O  OH  . TYR E  436 ? 3.3045 3.1865 2.9994 1.3443  -0.5548 0.2411  436  TYR E OH  
14840 N  N   . ARG E  437 ? 2.4145 3.4073 2.4802 1.3827  -0.5630 0.0238  437  ARG E N   
14841 C  CA  . ARG E  437 ? 2.2625 3.4588 2.3789 1.3574  -0.5619 -0.0151 437  ARG E CA  
14842 C  C   . ARG E  437 ? 2.2888 3.5510 2.3863 1.2946  -0.5700 -0.0093 437  ARG E C   
14843 O  O   . ARG E  437 ? 2.4506 3.6757 2.5088 1.3115  -0.5934 0.0385  437  ARG E O   
14844 C  CB  . ARG E  437 ? 2.2792 3.6122 2.4327 1.4442  -0.5856 -0.0048 437  ARG E CB  
14845 C  CG  . ARG E  437 ? 2.3148 3.5981 2.4912 1.4980  -0.5714 -0.0200 437  ARG E CG  
14846 C  CD  . ARG E  437 ? 2.3763 3.7792 2.5816 1.5490  -0.5794 -0.0147 437  ARG E CD  
14847 N  NE  . ARG E  437 ? 2.5809 3.9068 2.7442 1.5884  -0.5983 0.0459  437  ARG E NE  
14848 C  CZ  . ARG E  437 ? 2.6615 4.1110 2.8355 1.6175  -0.6163 0.0665  437  ARG E CZ  
14849 N  NH1 . ARG E  437 ? 2.6247 4.2844 2.8484 1.6078  -0.6168 0.0298  437  ARG E NH1 
14850 N  NH2 . ARG E  437 ? 2.6523 4.0186 2.7864 1.6530  -0.6333 0.1237  437  ARG E NH2 
14851 N  N   . ALA E  438 ? 2.2299 3.5848 2.3521 1.2197  -0.5493 -0.0590 438  ALA E N   
14852 C  CA  . ALA E  438 ? 2.3387 3.7619 2.4450 1.1549  -0.5528 -0.0635 438  ALA E CA  
14853 C  C   . ALA E  438 ? 2.4794 4.0967 2.6096 1.1844  -0.5806 -0.0542 438  ALA E C   
14854 O  O   . ALA E  438 ? 2.5680 4.3319 2.7465 1.2032  -0.5802 -0.0833 438  ALA E O   
14855 C  CB  . ALA E  438 ? 2.2334 3.6770 2.3535 1.0652  -0.5191 -0.1214 438  ALA E CB  
14856 N  N   . ARG E  439 ? 2.8707 3.0941 2.9225 0.9507  -0.2590 -0.3383 439  ARG E N   
14857 C  CA  . ARG E  439 ? 2.6257 2.8820 2.7226 0.9234  -0.2488 -0.3172 439  ARG E CA  
14858 C  C   . ARG E  439 ? 2.6010 2.8852 2.7074 0.8921  -0.2218 -0.2931 439  ARG E C   
14859 O  O   . ARG E  439 ? 2.5742 2.8440 2.6674 0.8774  -0.2203 -0.2945 439  ARG E O   
14860 C  CB  . ARG E  439 ? 2.5035 2.7471 2.6396 0.8969  -0.2775 -0.3216 439  ARG E CB  
14861 C  CG  . ARG E  439 ? 2.4655 2.6782 2.6018 0.9237  -0.3074 -0.3437 439  ARG E CG  
14862 C  CD  . ARG E  439 ? 2.4313 2.6247 2.6039 0.8972  -0.3390 -0.3474 439  ARG E CD  
14863 N  NE  . ARG E  439 ? 2.4155 2.6396 2.6346 0.8627  -0.3350 -0.3245 439  ARG E NE  
14864 C  CZ  . ARG E  439 ? 2.4770 2.6962 2.7321 0.8359  -0.3565 -0.3194 439  ARG E CZ  
14865 N  NH1 . ARG E  439 ? 2.3833 2.5682 2.6386 0.8381  -0.3838 -0.3343 439  ARG E NH1 
14866 N  NH2 . ARG E  439 ? 2.6528 2.9040 2.9447 0.8071  -0.3514 -0.2976 439  ARG E NH2 
14867 N  N   . PRO E  440 ? 2.5840 2.9068 2.7150 0.8815  -0.2015 -0.2708 440  PRO E N   
14868 C  CA  . PRO E  440 ? 2.6325 2.9781 2.7766 0.8484  -0.1801 -0.2492 440  PRO E CA  
14869 C  C   . PRO E  440 ? 2.6806 3.0150 2.8448 0.8071  -0.1943 -0.2515 440  PRO E C   
14870 O  O   . PRO E  440 ? 2.7683 3.0978 2.9545 0.7961  -0.2160 -0.2579 440  PRO E O   
14871 C  CB  . PRO E  440 ? 2.5869 2.9774 2.7622 0.8445  -0.1639 -0.2262 440  PRO E CB  
14872 C  CG  . PRO E  440 ? 2.5830 2.9747 2.7465 0.8893  -0.1665 -0.2348 440  PRO E CG  
14873 C  CD  . PRO E  440 ? 2.5922 2.9399 2.7409 0.9012  -0.1975 -0.2639 440  PRO E CD  
14874 N  N   . VAL E  441 ? 2.5465 2.8769 2.7031 0.7857  -0.1812 -0.2449 441  VAL E N   
14875 C  CA  . VAL E  441 ? 2.5411 2.8584 2.7079 0.7517  -0.1912 -0.2490 441  VAL E CA  
14876 C  C   . VAL E  441 ? 2.6941 3.0389 2.8873 0.7158  -0.1801 -0.2318 441  VAL E C   
14877 O  O   . VAL E  441 ? 2.8008 3.1568 2.9923 0.7096  -0.1595 -0.2182 441  VAL E O   
14878 C  CB  . VAL E  441 ? 2.5021 2.7897 2.6400 0.7552  -0.1871 -0.2572 441  VAL E CB  
14879 C  CG1 . VAL E  441 ? 2.5530 2.8292 2.7013 0.7239  -0.1954 -0.2613 441  VAL E CG1 
14880 C  CG2 . VAL E  441 ? 2.4677 2.7305 2.5791 0.7905  -0.2016 -0.2745 441  VAL E CG2 
14881 N  N   . ILE E  442 ? 2.6878 3.0441 2.9062 0.6922  -0.1950 -0.2313 442  ILE E N   
14882 C  CA  . ILE E  442 ? 2.5656 2.9481 2.8071 0.6569  -0.1904 -0.2181 442  ILE E CA  
14883 C  C   . ILE E  442 ? 2.7604 3.1237 2.9922 0.6305  -0.1933 -0.2265 442  ILE E C   
14884 O  O   . ILE E  442 ? 2.8630 3.2125 3.0926 0.6294  -0.2082 -0.2369 442  ILE E O   
14885 C  CB  . ILE E  442 ? 2.4152 2.8271 2.6885 0.6492  -0.2047 -0.2102 442  ILE E CB  
14886 C  CG1 . ILE E  442 ? 2.3706 2.7948 2.6511 0.6828  -0.2036 -0.2059 442  ILE E CG1 
14887 C  CG2 . ILE E  442 ? 2.4489 2.8929 2.7444 0.6149  -0.2004 -0.1951 442  ILE E CG2 
14888 C  CD1 . ILE E  442 ? 2.4058 2.8541 2.6884 0.6922  -0.1808 -0.1898 442  ILE E CD1 
14889 N  N   . THR E  443 ? 2.8528 3.2143 3.0799 0.6107  -0.1789 -0.2216 443  THR E N   
14890 C  CA  . THR E  443 ? 2.8790 3.2233 3.0964 0.5851  -0.1802 -0.2303 443  THR E CA  
14891 C  C   . THR E  443 ? 3.0221 3.3937 3.2593 0.5526  -0.1872 -0.2242 443  THR E C   
14892 O  O   . THR E  443 ? 3.0809 3.4744 3.3348 0.5397  -0.1811 -0.2112 443  THR E O   
14893 C  CB  . THR E  443 ? 2.7409 3.0596 2.9400 0.5835  -0.1626 -0.2310 443  THR E CB  
14894 O  OG1 . THR E  443 ? 2.6665 2.9606 2.8440 0.6136  -0.1587 -0.2374 443  THR E OG1 
14895 C  CG2 . THR E  443 ? 2.7780 3.0779 2.9674 0.5573  -0.1632 -0.2415 443  THR E CG2 
14896 N  N   . VAL E  444 ? 2.9961 3.3695 3.2325 0.5398  -0.2006 -0.2317 444  VAL E N   
14897 C  CA  . VAL E  444 ? 2.9163 3.3180 3.1666 0.5114  -0.2103 -0.2267 444  VAL E CA  
14898 C  C   . VAL E  444 ? 2.9320 3.3149 3.1596 0.4902  -0.2089 -0.2402 444  VAL E C   
14899 O  O   . VAL E  444 ? 3.0168 3.3768 3.2261 0.4993  -0.2081 -0.2513 444  VAL E O   
14900 C  CB  . VAL E  444 ? 2.7356 3.1622 3.0049 0.5161  -0.2272 -0.2203 444  VAL E CB  
14901 C  CG1 . VAL E  444 ? 2.7272 3.1315 2.9866 0.5332  -0.2334 -0.2295 444  VAL E CG1 
14902 C  CG2 . VAL E  444 ? 2.7303 3.1863 3.0077 0.4873  -0.2377 -0.2153 444  VAL E CG2 
14903 N  N   . ASN E  445 ? 2.8012 3.1939 3.0305 0.4630  -0.2094 -0.2395 445  ASN E N   
14904 C  CA  . ASN E  445 ? 2.7902 3.1660 2.9953 0.4421  -0.2108 -0.2551 445  ASN E CA  
14905 C  C   . ASN E  445 ? 2.8188 3.2310 3.0308 0.4197  -0.2270 -0.2516 445  ASN E C   
14906 O  O   . ASN E  445 ? 2.8432 3.2792 3.0727 0.4000  -0.2334 -0.2428 445  ASN E O   
14907 C  CB  . ASN E  445 ? 2.8312 3.1794 3.0284 0.4283  -0.2006 -0.2608 445  ASN E CB  
14908 C  CG  . ASN E  445 ? 2.8468 3.1549 3.0293 0.4498  -0.1843 -0.2660 445  ASN E CG  
14909 O  OD1 . ASN E  445 ? 2.8312 3.1317 3.0241 0.4546  -0.1736 -0.2559 445  ASN E OD1 
14910 N  ND2 . ASN E  445 ? 2.8814 3.1674 3.0413 0.4634  -0.1820 -0.2789 445  ASN E ND2 
14911 N  N   . ALA E  446 ? 2.8777 3.2982 3.0785 0.4232  -0.2338 -0.2555 446  ALA E N   
14912 C  CA  . ALA E  446 ? 2.8779 3.3352 3.0808 0.4047  -0.2486 -0.2506 446  ALA E CA  
14913 C  C   . ALA E  446 ? 2.9629 3.4055 3.1286 0.3879  -0.2491 -0.2704 446  ALA E C   
14914 O  O   . ALA E  446 ? 2.8358 3.2434 2.9749 0.3977  -0.2379 -0.2862 446  ALA E O   
14915 C  CB  . ALA E  446 ? 2.8085 3.2904 3.0259 0.4193  -0.2564 -0.2377 446  ALA E CB  
14916 N  N   . GLY E  447 ? 3.3018 3.7716 3.4649 0.3637  -0.2627 -0.2698 447  GLY E N   
14917 C  CA  . GLY E  447 ? 3.4349 3.8930 3.5581 0.3479  -0.2666 -0.2910 447  GLY E CA  
14918 C  C   . GLY E  447 ? 3.4072 3.9113 3.5236 0.3390  -0.2813 -0.2832 447  GLY E C   
14919 O  O   . GLY E  447 ? 3.5407 4.0873 3.6891 0.3362  -0.2921 -0.2603 447  GLY E O   
14920 N  N   . LEU E  448 ? 3.1316 3.6278 3.2047 0.3365  -0.2809 -0.3017 448  LEU E N   
14921 C  CA  . LEU E  448 ? 3.0648 3.6072 3.1244 0.3301  -0.2934 -0.2937 448  LEU E CA  
14922 C  C   . LEU E  448 ? 3.1637 3.6901 3.1677 0.3190  -0.2967 -0.3226 448  LEU E C   
14923 O  O   . LEU E  448 ? 3.3315 3.8243 3.3017 0.3336  -0.2819 -0.3418 448  LEU E O   
14924 C  CB  . LEU E  448 ? 3.0000 3.5644 3.0704 0.3531  -0.2858 -0.2748 448  LEU E CB  
14925 C  CG  . LEU E  448 ? 3.0100 3.6304 3.0783 0.3488  -0.2976 -0.2559 448  LEU E CG  
14926 C  CD1 . LEU E  448 ? 3.0148 3.6743 3.1183 0.3322  -0.3162 -0.2355 448  LEU E CD1 
14927 C  CD2 . LEU E  448 ? 2.9936 3.6310 3.0813 0.3709  -0.2894 -0.2343 448  LEU E CD2 
14928 N  N   . GLU E  449 ? 3.1708 3.7207 3.1651 0.2942  -0.3170 -0.3266 449  GLU E N   
14929 C  CA  . GLU E  449 ? 3.2499 3.7876 3.1875 0.2826  -0.3256 -0.3562 449  GLU E CA  
14930 C  C   . GLU E  449 ? 3.2476 3.8443 3.1672 0.2790  -0.3395 -0.3437 449  GLU E C   
14931 O  O   . GLU E  449 ? 3.1915 3.8366 3.1473 0.2685  -0.3538 -0.3162 449  GLU E O   
14932 C  CB  . GLU E  449 ? 3.3684 3.8790 3.3048 0.2536  -0.3420 -0.3756 449  GLU E CB  
14933 C  CG  . GLU E  449 ? 3.4594 3.9130 3.4143 0.2556  -0.3285 -0.3851 449  GLU E CG  
14934 C  CD  . GLU E  449 ? 3.5945 4.0277 3.5610 0.2243  -0.3462 -0.3964 449  GLU E CD  
14935 O  OE1 . GLU E  449 ? 3.5736 3.9772 3.5728 0.2222  -0.3374 -0.3909 449  GLU E OE1 
14936 O  OE2 . GLU E  449 ? 3.6513 4.1002 3.5955 0.2014  -0.3699 -0.4090 449  GLU E OE2 
14937 N  N   . VAL E  450 ? 3.3044 3.8985 3.1675 0.2896  -0.3342 -0.3624 450  VAL E N   
14938 C  CA  . VAL E  450 ? 3.3078 3.9575 3.1425 0.2885  -0.3457 -0.3527 450  VAL E CA  
14939 C  C   . VAL E  450 ? 3.3532 3.9803 3.1181 0.2783  -0.3569 -0.3931 450  VAL E C   
14940 O  O   . VAL E  450 ? 3.3317 3.9231 3.0487 0.2964  -0.3407 -0.4197 450  VAL E O   
14941 C  CB  . VAL E  450 ? 3.3024 3.9821 3.1351 0.3169  -0.3263 -0.3305 450  VAL E CB  
14942 C  CG1 . VAL E  450 ? 3.3212 4.0618 3.1224 0.3161  -0.3372 -0.3177 450  VAL E CG1 
14943 C  CG2 . VAL E  450 ? 3.2727 3.9680 3.1747 0.3260  -0.3193 -0.2939 450  VAL E CG2 
14944 N  N   . TYR E  451 ? 3.4658 4.1129 3.2249 0.2505  -0.3856 -0.3985 451  TYR E N   
14945 C  CA  . TYR E  451 ? 3.6311 4.2570 3.3224 0.2383  -0.4027 -0.4391 451  TYR E CA  
14946 C  C   . TYR E  451 ? 3.7122 4.4042 3.3826 0.2252  -0.4284 -0.4271 451  TYR E C   
14947 O  O   . TYR E  451 ? 3.6978 4.4308 3.4161 0.2048  -0.4475 -0.3998 451  TYR E O   
14948 C  CB  . TYR E  451 ? 3.6005 4.1682 3.3012 0.2119  -0.4178 -0.4674 451  TYR E CB  
14949 C  CG  . TYR E  451 ? 3.5088 4.0969 3.2834 0.1874  -0.4319 -0.4389 451  TYR E CG  
14950 C  CD1 . TYR E  451 ? 3.4043 3.9738 3.2365 0.1956  -0.4125 -0.4188 451  TYR E CD1 
14951 C  CD2 . TYR E  451 ? 3.5390 4.1666 3.3245 0.1575  -0.4647 -0.4322 451  TYR E CD2 
14952 C  CE1 . TYR E  451 ? 3.3796 3.9703 3.2766 0.1771  -0.4227 -0.3924 451  TYR E CE1 
14953 C  CE2 . TYR E  451 ? 3.4670 4.1175 3.3224 0.1374  -0.4756 -0.4039 451  TYR E CE2 
14954 C  CZ  . TYR E  451 ? 3.3955 4.0276 3.3056 0.1484  -0.4532 -0.3842 451  TYR E CZ  
14955 O  OH  . TYR E  451 ? 3.3388 3.9966 3.3159 0.1320  -0.4617 -0.3555 451  TYR E OH  
14956 N  N   . PRO E  452 ? 3.7375 4.4424 3.3350 0.2387  -0.4285 -0.4465 452  PRO E N   
14957 C  CA  . PRO E  452 ? 3.7659 4.4278 3.3024 0.2664  -0.4048 -0.4785 452  PRO E CA  
14958 C  C   . PRO E  452 ? 3.7014 4.3823 3.2576 0.3004  -0.3697 -0.4492 452  PRO E C   
14959 O  O   . PRO E  452 ? 3.5728 4.3090 3.1781 0.3039  -0.3664 -0.4039 452  PRO E O   
14960 C  CB  . PRO E  452 ? 3.7346 4.4228 3.1900 0.2678  -0.4216 -0.5018 452  PRO E CB  
14961 C  CG  . PRO E  452 ? 3.7063 4.4763 3.1901 0.2552  -0.4402 -0.4602 452  PRO E CG  
14962 C  CD  . PRO E  452 ? 3.7231 4.4926 3.2910 0.2285  -0.4533 -0.4364 452  PRO E CD  
14963 N  N   . SER E  453 ? 3.7725 4.4059 3.2924 0.3251  -0.3450 -0.4751 453  SER E N   
14964 C  CA  . SER E  453 ? 3.6012 4.2545 3.1342 0.3580  -0.3127 -0.4493 453  SER E CA  
14965 C  C   . SER E  453 ? 3.5665 4.2855 3.0566 0.3766  -0.3074 -0.4328 453  SER E C   
14966 O  O   . SER E  453 ? 3.4421 4.2096 2.9667 0.3935  -0.2909 -0.3907 453  SER E O   
14967 C  CB  . SER E  453 ? 3.5831 4.1683 3.0921 0.3795  -0.2880 -0.4806 453  SER E CB  
14968 O  OG  . SER E  453 ? 3.6495 4.2000 3.0775 0.3850  -0.2921 -0.5282 453  SER E OG  
14969 N  N   . ILE E  454 ? 3.8320 4.5535 3.2467 0.3742  -0.3218 -0.4649 454  ILE E N   
14970 C  CA  . ILE E  454 ? 3.8848 4.6659 3.2440 0.3961  -0.3144 -0.4546 454  ILE E CA  
14971 C  C   . ILE E  454 ? 4.0338 4.8750 3.3910 0.3720  -0.3465 -0.4366 454  ILE E C   
14972 O  O   . ILE E  454 ? 4.0617 4.8819 3.3855 0.3478  -0.3767 -0.4698 454  ILE E O   
14973 C  CB  . ILE E  454 ? 3.8443 4.5853 3.1091 0.4184  -0.3046 -0.5063 454  ILE E CB  
14974 C  CG1 . ILE E  454 ? 3.8874 4.5543 3.1202 0.3932  -0.3313 -0.5617 454  ILE E CG1 
14975 C  CG2 . ILE E  454 ? 3.7273 4.4397 2.9956 0.4529  -0.2653 -0.5067 454  ILE E CG2 
14976 C  CD1 . ILE E  454 ? 3.9353 4.5513 3.0750 0.4150  -0.3245 -0.6180 454  ILE E CD1 
14977 N  N   . LEU E  455 ? 4.1607 5.0767 3.5578 0.3779  -0.3417 -0.3824 455  LEU E N   
14978 C  CA  . LEU E  455 ? 4.2234 5.2051 3.6258 0.3583  -0.3698 -0.3564 455  LEU E CA  
14979 C  C   . LEU E  455 ? 4.2536 5.2877 3.5739 0.3774  -0.3689 -0.3590 455  LEU E C   
14980 O  O   . LEU E  455 ? 4.3117 5.3836 3.6218 0.4081  -0.3405 -0.3330 455  LEU E O   
14981 C  CB  . LEU E  455 ? 4.0708 5.1031 3.5642 0.3546  -0.3665 -0.2944 455  LEU E CB  
14982 C  CG  . LEU E  455 ? 3.8633 4.8494 3.4371 0.3419  -0.3641 -0.2879 455  LEU E CG  
14983 C  CD1 . LEU E  455 ? 3.7296 4.7661 3.3856 0.3416  -0.3627 -0.2290 455  LEU E CD1 
14984 C  CD2 . LEU E  455 ? 3.8510 4.7964 3.4290 0.3098  -0.3921 -0.3192 455  LEU E CD2 
14985 N  N   . ASN E  456 ? 4.1337 5.1716 3.3956 0.3599  -0.4004 -0.3896 456  ASN E N   
14986 C  CA  . ASN E  456 ? 4.0151 5.1073 3.1938 0.3776  -0.4034 -0.3923 456  ASN E CA  
14987 C  C   . ASN E  456 ? 3.8735 5.0618 3.0941 0.3812  -0.4022 -0.3243 456  ASN E C   
14988 O  O   . ASN E  456 ? 3.7185 4.9283 3.0240 0.3605  -0.4131 -0.2847 456  ASN E O   
14989 C  CB  . ASN E  456 ? 4.0276 5.1015 3.1391 0.3541  -0.4438 -0.4404 456  ASN E CB  
14990 C  CG  . ASN E  456 ? 4.1724 5.2905 3.1798 0.3769  -0.4466 -0.4557 456  ASN E CG  
14991 O  OD1 . ASN E  456 ? 4.2390 5.4353 3.2379 0.3729  -0.4627 -0.4220 456  ASN E OD1 
14992 N  ND2 . ASN E  456 ? 4.2365 5.3047 3.1619 0.4027  -0.4310 -0.5068 456  ASN E ND2 
14993 N  N   . GLN E  457 ? 3.8693 5.1166 3.0291 0.4092  -0.3883 -0.3097 457  GLN E N   
14994 C  CA  . GLN E  457 ? 3.8219 5.1629 3.0196 0.4135  -0.3870 -0.2420 457  GLN E CA  
14995 C  C   . GLN E  457 ? 3.8429 5.2282 3.0350 0.3849  -0.4290 -0.2332 457  GLN E C   
14996 O  O   . GLN E  457 ? 3.8678 5.3228 3.1139 0.3796  -0.4347 -0.1741 457  GLN E O   
14997 C  CB  . GLN E  457 ? 3.9196 5.3162 3.0563 0.4538  -0.3570 -0.2237 457  GLN E CB  
14998 C  CG  . GLN E  457 ? 3.8354 5.3298 3.0182 0.4612  -0.3505 -0.1468 457  GLN E CG  
14999 C  CD  . GLN E  457 ? 3.5518 5.0455 2.8574 0.4487  -0.3435 -0.0966 457  GLN E CD  
15000 O  OE1 . GLN E  457 ? 3.4115 4.8629 2.7578 0.4598  -0.3179 -0.0975 457  GLN E OE1 
15001 N  NE2 . GLN E  457 ? 3.5196 5.0581 2.8838 0.4261  -0.3678 -0.0544 457  GLN E NE2 
15002 N  N   . ASP E  458 ? 3.9146 5.2590 3.0486 0.3649  -0.4601 -0.2894 458  ASP E N   
15003 C  CA  . ASP E  458 ? 3.8119 5.1974 2.9390 0.3356  -0.5039 -0.2844 458  ASP E CA  
15004 C  C   . ASP E  458 ? 3.8402 5.1489 2.9547 0.3036  -0.5356 -0.3445 458  ASP E C   
15005 O  O   . ASP E  458 ? 3.9427 5.2216 2.9672 0.3030  -0.5538 -0.3998 458  ASP E O   
15006 C  CB  . ASP E  458 ? 3.7387 5.1925 2.7727 0.3537  -0.5122 -0.2822 458  ASP E CB  
15007 C  CG  . ASP E  458 ? 3.6827 5.1853 2.7117 0.3237  -0.5592 -0.2730 458  ASP E CG  
15008 O  OD1 . ASP E  458 ? 3.5554 5.1275 2.6507 0.3160  -0.5648 -0.2103 458  ASP E OD1 
15009 O  OD2 . ASP E  458 ? 3.8081 5.2780 2.7695 0.3073  -0.5921 -0.3286 458  ASP E OD2 
15010 N  N   . ASN E  459 ? 3.5925 4.8691 2.7991 0.2777  -0.5421 -0.3325 459  ASN E N   
15011 C  CA  . ASN E  459 ? 3.5643 4.7739 2.7798 0.2442  -0.5710 -0.3780 459  ASN E CA  
15012 C  C   . ASN E  459 ? 3.4594 4.7071 2.7637 0.2118  -0.5972 -0.3375 459  ASN E C   
15013 O  O   . ASN E  459 ? 3.4577 4.6843 2.8487 0.2044  -0.5848 -0.3146 459  ASN E O   
15014 C  CB  . ASN E  459 ? 3.5730 4.6930 2.8103 0.2505  -0.5451 -0.4087 459  ASN E CB  
15015 C  CG  . ASN E  459 ? 3.9093 4.9631 3.1684 0.2147  -0.5731 -0.4473 459  ASN E CG  
15016 O  OD1 . ASN E  459 ? 3.7221 4.7809 2.9490 0.1888  -0.6129 -0.4712 459  ASN E OD1 
15017 N  ND2 . ASN E  459 ? 5.0768 6.0702 4.3924 0.2127  -0.5536 -0.4517 459  ASN E ND2 
15018 N  N   . LYS E  460 ? 3.5017 4.8046 2.7820 0.1934  -0.6343 -0.3306 460  LYS E N   
15019 C  CA  . LYS E  460 ? 3.4084 4.7588 2.7690 0.1650  -0.6606 -0.2888 460  LYS E CA  
15020 C  C   . LYS E  460 ? 3.4967 4.7960 2.8777 0.1266  -0.6938 -0.3258 460  LYS E C   
15021 O  O   . LYS E  460 ? 3.5655 4.8479 2.8786 0.1104  -0.7261 -0.3710 460  LYS E O   
15022 C  CB  . LYS E  460 ? 3.4154 4.8581 2.7435 0.1657  -0.6838 -0.2570 460  LYS E CB  
15023 C  CG  . LYS E  460 ? 3.3215 4.8216 2.6424 0.2023  -0.6501 -0.2105 460  LYS E CG  
15024 C  CD  . LYS E  460 ? 3.3885 4.9742 2.6491 0.2085  -0.6707 -0.1893 460  LYS E CD  
15025 C  CE  . LYS E  460 ? 3.4887 5.0514 2.6258 0.2128  -0.6881 -0.2526 460  LYS E CE  
15026 N  NZ  . LYS E  460 ? 3.4253 5.0745 2.4943 0.2249  -0.7042 -0.2313 460  LYS E NZ  
15027 N  N   . THR E  461 ? 3.5325 4.8077 3.0072 0.1125  -0.6866 -0.3063 461  THR E N   
15028 C  CA  . THR E  461 ? 3.6805 4.9065 3.1844 0.0773  -0.7128 -0.3363 461  THR E CA  
15029 C  C   . THR E  461 ? 3.6755 4.9362 3.2856 0.0558  -0.7232 -0.2902 461  THR E C   
15030 O  O   . THR E  461 ? 3.7246 5.0138 3.3537 0.0242  -0.7622 -0.2877 461  THR E O   
15031 C  CB  . THR E  461 ? 3.7072 4.8382 3.2031 0.0848  -0.6875 -0.3779 461  THR E CB  
15032 O  OG1 . THR E  461 ? 3.8741 4.9718 3.2706 0.1074  -0.6770 -0.4220 461  THR E OG1 
15033 C  CG2 . THR E  461 ? 3.7559 4.8356 3.2824 0.0476  -0.7147 -0.4069 461  THR E CG2 
15034 N  N   . CYS E  462 ? 3.6333 4.8922 3.3133 0.0733  -0.6897 -0.2542 462  CYS E N   
15035 C  CA  . CYS E  462 ? 3.6484 4.9410 3.4271 0.0594  -0.6957 -0.2097 462  CYS E CA  
15036 C  C   . CYS E  462 ? 3.4385 4.8229 3.2330 0.0539  -0.7199 -0.1654 462  CYS E C   
15037 O  O   . CYS E  462 ? 3.3652 4.7932 3.1132 0.0725  -0.7164 -0.1513 462  CYS E O   
15038 C  CB  . CYS E  462 ? 3.7532 5.0270 3.5932 0.0847  -0.6556 -0.1813 462  CYS E CB  
15039 S  SG  . CYS E  462 ? 4.1800 5.4881 3.9925 0.1240  -0.6254 -0.1526 462  CYS E SG  
15040 N  N   . SER E  463 ? 3.3459 4.7632 3.2099 0.0295  -0.7432 -0.1399 463  SER E N   
15041 C  CA  . SER E  463 ? 3.3517 4.8574 3.2380 0.0221  -0.7691 -0.0962 463  SER E CA  
15042 C  C   . SER E  463 ? 3.2606 4.8112 3.1890 0.0523  -0.7426 -0.0414 463  SER E C   
15043 O  O   . SER E  463 ? 3.1743 4.6986 3.1625 0.0682  -0.7132 -0.0234 463  SER E O   
15044 C  CB  . SER E  463 ? 3.2812 4.8106 3.2409 -0.0097 -0.7977 -0.0797 463  SER E CB  
15045 O  OG  . SER E  463 ? 3.1154 4.6121 3.1541 -0.0042 -0.7721 -0.0649 463  SER E OG  
15046 N  N   . LEU E  464 ? 3.1453 4.7638 3.0414 0.0601  -0.7549 -0.0149 464  LEU E N   
15047 C  CA  . LEU E  464 ? 2.9253 4.5944 2.8602 0.0859  -0.7355 0.0415  464  LEU E CA  
15048 C  C   . LEU E  464 ? 3.1042 4.8579 3.0050 0.0823  -0.7636 0.0693  464  LEU E C   
15049 O  O   . LEU E  464 ? 3.1962 4.9556 3.0156 0.0704  -0.7873 0.0342  464  LEU E O   
15050 C  CB  . LEU E  464 ? 2.6905 4.3208 2.5947 0.1176  -0.6953 0.0339  464  LEU E CB  
15051 C  CG  . LEU E  464 ? 2.6361 4.3029 2.5860 0.1453  -0.6709 0.0895  464  LEU E CG  
15052 C  CD1 . LEU E  464 ? 2.5518 4.1975 2.6014 0.1494  -0.6569 0.1162  464  LEU E CD1 
15053 C  CD2 . LEU E  464 ? 2.6502 4.2908 2.5470 0.1719  -0.6393 0.0765  464  LEU E CD2 
15054 N  N   . PRO E  465 ? 3.0444 4.8640 3.0040 0.0931  -0.7629 0.1315  465  PRO E N   
15055 C  CA  . PRO E  465 ? 2.8583 4.7612 2.7802 0.0912  -0.7891 0.1596  465  PRO E CA  
15056 C  C   . PRO E  465 ? 2.8184 4.7304 2.6474 0.1133  -0.7747 0.1481  465  PRO E C   
15057 O  O   . PRO E  465 ? 2.7972 4.7521 2.6404 0.1370  -0.7561 0.1952  465  PRO E O   
15058 C  CB  . PRO E  465 ? 2.7107 4.6714 2.7242 0.1026  -0.7844 0.2312  465  PRO E CB  
15059 C  CG  . PRO E  465 ? 2.7100 4.6243 2.8102 0.0982  -0.7723 0.2320  465  PRO E CG  
15060 C  CD  . PRO E  465 ? 2.8623 4.6866 2.9266 0.1023  -0.7472 0.1767  465  PRO E CD  
15061 N  N   . LYS E  470 ? 3.2234 4.9071 2.8854 0.1209  -0.7310 -0.0279 470  LYS E N   
15062 C  CA  . LYS E  470 ? 3.2160 4.8125 2.8317 0.1257  -0.7124 -0.0868 470  LYS E CA  
15063 C  C   . LYS E  470 ? 3.2296 4.8172 2.8059 0.1627  -0.6721 -0.0831 470  LYS E C   
15064 O  O   . LYS E  470 ? 3.2678 4.9060 2.7830 0.1801  -0.6707 -0.0711 470  LYS E O   
15065 C  CB  . LYS E  470 ? 3.3129 4.8836 2.8430 0.1052  -0.7456 -0.1469 470  LYS E CB  
15066 C  CG  . LYS E  470 ? 3.2722 4.8176 2.8440 0.0656  -0.7803 -0.1674 470  LYS E CG  
15067 C  CD  . LYS E  470 ? 3.1916 4.8115 2.8394 0.0471  -0.8061 -0.1141 470  LYS E CD  
15068 C  CE  . LYS E  470 ? 3.1798 4.8762 2.7709 0.0418  -0.8405 -0.1025 470  LYS E CE  
15069 N  NZ  . LYS E  470 ? 3.0609 4.8324 2.7300 0.0246  -0.8657 -0.0477 470  LYS E NZ  
15070 N  N   . VAL E  471 ? 3.1170 4.6437 2.7305 0.1752  -0.6392 -0.0908 471  VAL E N   
15071 C  CA  . VAL E  471 ? 3.1410 4.6539 2.7288 0.2088  -0.5999 -0.0872 471  VAL E CA  
15072 C  C   . VAL E  471 ? 3.2371 4.6573 2.8114 0.2124  -0.5796 -0.1380 471  VAL E C   
15073 O  O   . VAL E  471 ? 3.2934 4.6632 2.8973 0.1900  -0.5919 -0.1644 471  VAL E O   
15074 C  CB  . VAL E  471 ? 3.0849 4.6372 2.7558 0.2252  -0.5782 -0.0218 471  VAL E CB  
15075 C  CG1 . VAL E  471 ? 3.1881 4.6913 2.9475 0.2169  -0.5699 -0.0171 471  VAL E CG1 
15076 C  CG2 . VAL E  471 ? 3.0210 4.5847 2.6629 0.2588  -0.5433 -0.0064 471  VAL E CG2 
15077 N  N   . SER E  472 ? 3.3306 4.7318 2.8596 0.2416  -0.5479 -0.1496 472  SER E N   
15078 C  CA  . SER E  472 ? 3.3677 4.6852 2.8829 0.2507  -0.5244 -0.1929 472  SER E CA  
15079 C  C   . SER E  472 ? 3.3802 4.6552 2.9876 0.2431  -0.5132 -0.1799 472  SER E C   
15080 O  O   . SER E  472 ? 3.3429 4.6318 3.0065 0.2598  -0.4902 -0.1403 472  SER E O   
15081 C  CB  . SER E  472 ? 3.2587 4.5803 2.7304 0.2873  -0.4884 -0.1899 472  SER E CB  
15082 O  OG  . SER E  472 ? 3.3131 4.6709 2.6906 0.2991  -0.4953 -0.2060 472  SER E OG  
15083 N  N   . CYS E  473 ? 3.4163 4.6393 3.0393 0.2184  -0.5297 -0.2127 473  CYS E N   
15084 C  CA  . CYS E  473 ? 3.4373 4.6252 3.1443 0.2105  -0.5218 -0.2004 473  CYS E CA  
15085 C  C   . CYS E  473 ? 3.4689 4.5704 3.1599 0.2056  -0.5132 -0.2502 473  CYS E C   
15086 O  O   . CYS E  473 ? 3.4744 4.5409 3.0954 0.2006  -0.5219 -0.2969 473  CYS E O   
15087 C  CB  . CYS E  473 ? 3.5116 4.7363 3.2787 0.1836  -0.5508 -0.1744 473  CYS E CB  
15088 S  SG  . CYS E  473 ? 3.9240 5.1473 3.6462 0.1477  -0.5941 -0.2126 473  CYS E SG  
15089 N  N   . PHE E  474 ? 3.5653 4.6322 3.3230 0.2078  -0.4971 -0.2390 474  PHE E N   
15090 C  CA  . PHE E  474 ? 3.7180 4.7056 3.4737 0.2060  -0.4848 -0.2768 474  PHE E CA  
15091 C  C   . PHE E  474 ? 3.7218 4.6954 3.5603 0.1950  -0.4844 -0.2570 474  PHE E C   
15092 O  O   . PHE E  474 ? 3.6605 4.6797 3.5576 0.1967  -0.4864 -0.2144 474  PHE E O   
15093 C  CB  . PHE E  474 ? 3.7038 4.6566 3.4320 0.2375  -0.4504 -0.2879 474  PHE E CB  
15094 C  CG  . PHE E  474 ? 3.5433 4.5268 3.3252 0.2592  -0.4290 -0.2423 474  PHE E CG  
15095 C  CD1 . PHE E  474 ? 3.4690 4.5163 3.2420 0.2731  -0.4262 -0.2087 474  PHE E CD1 
15096 C  CD2 . PHE E  474 ? 3.4471 4.3952 3.2879 0.2659  -0.4129 -0.2326 474  PHE E CD2 
15097 C  CE1 . PHE E  474 ? 3.3693 4.4421 3.1969 0.2909  -0.4094 -0.1656 474  PHE E CE1 
15098 C  CE2 . PHE E  474 ? 3.3312 4.3030 3.2212 0.2848  -0.3973 -0.1935 474  PHE E CE2 
15099 C  CZ  . PHE E  474 ? 3.3392 4.3718 3.2252 0.2961  -0.3963 -0.1599 474  PHE E CZ  
15100 N  N   . ASN E  475 ? 3.8067 4.7165 3.6488 0.1850  -0.4815 -0.2880 475  ASN E N   
15101 C  CA  . ASN E  475 ? 3.6959 4.5887 3.6091 0.1755  -0.4795 -0.2735 475  ASN E CA  
15102 C  C   . ASN E  475 ? 3.6838 4.5368 3.6215 0.2015  -0.4470 -0.2690 475  ASN E C   
15103 O  O   . ASN E  475 ? 3.7743 4.5790 3.6711 0.2152  -0.4295 -0.2976 475  ASN E O   
15104 C  CB  . ASN E  475 ? 3.7261 4.5776 3.6349 0.1470  -0.4973 -0.3047 475  ASN E CB  
15105 C  CG  . ASN E  475 ? 3.8025 4.6932 3.6934 0.1178  -0.5345 -0.3091 475  ASN E CG  
15106 O  OD1 . ASN E  475 ? 3.9103 4.7914 3.7323 0.1125  -0.5482 -0.3412 475  ASN E OD1 
15107 N  ND2 . ASN E  475 ? 3.7397 4.6758 3.6919 0.0999  -0.5517 -0.2770 475  ASN E ND2 
15108 N  N   . VAL E  476 ? 3.6545 4.5274 3.6584 0.2092  -0.4400 -0.2342 476  VAL E N   
15109 C  CA  . VAL E  476 ? 3.6766 4.5135 3.7094 0.2323  -0.4137 -0.2287 476  VAL E CA  
15110 C  C   . VAL E  476 ? 3.7209 4.5308 3.7993 0.2222  -0.4135 -0.2290 476  VAL E C   
15111 O  O   . VAL E  476 ? 3.6660 4.5114 3.7954 0.2150  -0.4235 -0.2017 476  VAL E O   
15112 C  CB  . VAL E  476 ? 3.5853 4.4615 3.6553 0.2530  -0.4057 -0.1899 476  VAL E CB  
15113 C  CG1 . VAL E  476 ? 3.5779 4.4135 3.6753 0.2757  -0.3826 -0.1880 476  VAL E CG1 
15114 C  CG2 . VAL E  476 ? 3.5210 4.4313 3.5492 0.2624  -0.4050 -0.1839 476  VAL E CG2 
15115 N  N   . ARG E  477 ? 3.7634 4.5127 3.8244 0.2229  -0.4011 -0.2579 477  ARG E N   
15116 C  CA  . ARG E  477 ? 3.7372 4.4594 3.8382 0.2150  -0.3977 -0.2573 477  ARG E CA  
15117 C  C   . ARG E  477 ? 3.6294 4.3136 3.7461 0.2422  -0.3711 -0.2555 477  ARG E C   
15118 O  O   . ARG E  477 ? 3.5641 4.2053 3.6442 0.2549  -0.3561 -0.2783 477  ARG E O   
15119 C  CB  . ARG E  477 ? 3.8450 4.5279 3.9189 0.1902  -0.4084 -0.2893 477  ARG E CB  
15120 C  CG  . ARG E  477 ? 3.8784 4.5402 3.9982 0.1786  -0.4060 -0.2836 477  ARG E CG  
15121 C  CD  . ARG E  477 ? 3.9431 4.5720 4.0445 0.1481  -0.4229 -0.3107 477  ARG E CD  
15122 N  NE  . ARG E  477 ? 3.9598 4.5744 4.1110 0.1359  -0.4200 -0.2991 477  ARG E NE  
15123 C  CZ  . ARG E  477 ? 3.9428 4.5022 4.0953 0.1438  -0.4010 -0.3105 477  ARG E CZ  
15124 N  NH1 . ARG E  477 ? 3.8821 4.3938 3.9894 0.1640  -0.3840 -0.3352 477  ARG E NH1 
15125 N  NH2 . ARG E  477 ? 3.9465 4.5015 4.1471 0.1326  -0.3982 -0.2945 477  ARG E NH2 
15126 N  N   . PHE E  478 ? 3.6167 4.3171 3.7863 0.2524  -0.3658 -0.2290 478  PHE E N   
15127 C  CA  . PHE E  478 ? 3.5799 4.2478 3.7667 0.2784  -0.3443 -0.2260 478  PHE E CA  
15128 C  C   . PHE E  478 ? 3.6011 4.2567 3.8247 0.2746  -0.3397 -0.2196 478  PHE E C   
15129 O  O   . PHE E  478 ? 3.6540 4.3482 3.9153 0.2637  -0.3508 -0.1987 478  PHE E O   
15130 C  CB  . PHE E  478 ? 3.5009 4.1982 3.7146 0.3006  -0.3416 -0.2002 478  PHE E CB  
15131 C  CG  . PHE E  478 ? 3.4071 4.1547 3.6673 0.2957  -0.3551 -0.1702 478  PHE E CG  
15132 C  CD1 . PHE E  478 ? 3.4108 4.2079 3.6697 0.2799  -0.3738 -0.1569 478  PHE E CD1 
15133 C  CD2 . PHE E  478 ? 3.3428 4.0894 3.6467 0.3093  -0.3485 -0.1548 478  PHE E CD2 
15134 C  CE1 . PHE E  478 ? 3.3772 4.2217 3.6818 0.2768  -0.3860 -0.1273 478  PHE E CE1 
15135 C  CE2 . PHE E  478 ? 3.3152 4.1077 3.6629 0.3080  -0.3593 -0.1271 478  PHE E CE2 
15136 C  CZ  . PHE E  478 ? 3.3344 4.1759 3.6848 0.2912  -0.3782 -0.1125 478  PHE E CZ  
15137 N  N   . CYS E  479 ? 3.4552 4.0606 3.6694 0.2848  -0.3225 -0.2347 479  CYS E N   
15138 C  CA  . CYS E  479 ? 3.4439 4.0368 3.6897 0.2842  -0.3144 -0.2269 479  CYS E CA  
15139 C  C   . CYS E  479 ? 3.2316 3.8096 3.4936 0.3168  -0.2961 -0.2176 479  CYS E C   
15140 O  O   . CYS E  479 ? 3.1181 3.6746 3.3589 0.3363  -0.2878 -0.2265 479  CYS E O   
15141 C  CB  . CYS E  479 ? 3.5676 4.1138 3.7916 0.2684  -0.3104 -0.2498 479  CYS E CB  
15142 S  SG  . CYS E  479 ? 3.9091 4.4607 4.1117 0.2278  -0.3360 -0.2673 479  CYS E SG  
15143 N  N   . LEU E  480 ? 3.2299 3.8202 3.5293 0.3234  -0.2903 -0.1995 480  LEU E N   
15144 C  CA  . LEU E  480 ? 3.1455 3.7260 3.4593 0.3561  -0.2760 -0.1908 480  LEU E CA  
15145 C  C   . LEU E  480 ? 3.0915 3.6608 3.4239 0.3613  -0.2618 -0.1833 480  LEU E C   
15146 O  O   . LEU E  480 ? 3.1371 3.7358 3.4991 0.3451  -0.2660 -0.1675 480  LEU E O   
15147 C  CB  . LEU E  480 ? 3.0874 3.7096 3.4319 0.3693  -0.2846 -0.1693 480  LEU E CB  
15148 C  CG  . LEU E  480 ? 2.8391 3.4449 3.1881 0.4039  -0.2766 -0.1674 480  LEU E CG  
15149 C  CD1 . LEU E  480 ? 2.6639 3.2339 2.9787 0.4115  -0.2732 -0.1863 480  LEU E CD1 
15150 C  CD2 . LEU E  480 ? 2.8146 3.4582 3.1958 0.4141  -0.2883 -0.1470 480  LEU E CD2 
15151 N  N   . LYS E  481 ? 2.9069 3.4371 3.2234 0.3840  -0.2453 -0.1922 481  LYS E N   
15152 C  CA  . LYS E  481 ? 2.8379 3.3567 3.1673 0.3935  -0.2290 -0.1835 481  LYS E CA  
15153 C  C   . LYS E  481 ? 2.8576 3.3550 3.1770 0.4312  -0.2159 -0.1857 481  LYS E C   
15154 O  O   . LYS E  481 ? 2.8642 3.3335 3.1572 0.4427  -0.2163 -0.2018 481  LYS E O   
15155 C  CB  . LYS E  481 ? 2.9120 3.3950 3.2247 0.3732  -0.2234 -0.1960 481  LYS E CB  
15156 C  CG  . LYS E  481 ? 3.0649 3.5410 3.3961 0.3791  -0.2065 -0.1813 481  LYS E CG  
15157 C  CD  . LYS E  481 ? 3.2434 3.6830 3.5642 0.3546  -0.2047 -0.1919 481  LYS E CD  
15158 C  CE  . LYS E  481 ? 3.3242 3.7103 3.6032 0.3682  -0.1965 -0.2162 481  LYS E CE  
15159 N  NZ  . LYS E  481 ? 3.2992 3.6708 3.5718 0.4041  -0.1779 -0.2101 481  LYS E NZ  
15160 N  N   . ALA E  482 ? 3.0361 3.5489 3.3765 0.4514  -0.2050 -0.1690 482  ALA E N   
15161 C  CA  . ALA E  482 ? 3.0072 3.5021 3.3362 0.4893  -0.1950 -0.1718 482  ALA E CA  
15162 C  C   . ALA E  482 ? 3.0649 3.5591 3.3997 0.5041  -0.1751 -0.1588 482  ALA E C   
15163 O  O   . ALA E  482 ? 3.1432 3.6628 3.5037 0.4872  -0.1699 -0.1409 482  ALA E O   
15164 C  CB  . ALA E  482 ? 2.9600 3.4797 3.3059 0.5096  -0.2050 -0.1651 482  ALA E CB  
15165 N  N   . ASP E  483 ? 2.9896 3.4567 3.3016 0.5358  -0.1646 -0.1662 483  ASP E N   
15166 C  CA  . ASP E  483 ? 2.9188 3.3869 3.2308 0.5557  -0.1441 -0.1525 483  ASP E CA  
15167 C  C   . ASP E  483 ? 2.8753 3.3215 3.1600 0.5970  -0.1397 -0.1631 483  ASP E C   
15168 O  O   . ASP E  483 ? 2.8104 3.2317 3.0760 0.6045  -0.1524 -0.1823 483  ASP E O   
15169 C  CB  . ASP E  483 ? 2.9333 3.3780 3.2390 0.5351  -0.1330 -0.1507 483  ASP E CB  
15170 C  CG  . ASP E  483 ? 3.0323 3.4934 3.3527 0.5464  -0.1118 -0.1259 483  ASP E CG  
15171 O  OD1 . ASP E  483 ? 3.1429 3.6475 3.4917 0.5538  -0.1071 -0.1050 483  ASP E OD1 
15172 O  OD2 . ASP E  483 ? 3.0251 3.4579 3.3305 0.5491  -0.0987 -0.1249 483  ASP E OD2 
15173 N  N   . GLY E  484 ? 2.8802 3.3381 3.1638 0.6241  -0.1221 -0.1490 484  GLY E N   
15174 C  CA  . GLY E  484 ? 2.9021 3.3404 3.1551 0.6655  -0.1178 -0.1592 484  GLY E CA  
15175 C  C   . GLY E  484 ? 2.8879 3.3290 3.1304 0.6831  -0.0934 -0.1429 484  GLY E C   
15176 O  O   . GLY E  484 ? 2.9444 3.4074 3.2112 0.6640  -0.0797 -0.1202 484  GLY E O   
15177 N  N   . LYS E  485 ? 2.8797 3.2994 3.0867 0.7197  -0.0891 -0.1531 485  LYS E N   
15178 C  CA  . LYS E  485 ? 2.8949 3.3158 3.0853 0.7399  -0.0655 -0.1370 485  LYS E CA  
15179 C  C   . LYS E  485 ? 3.0265 3.4535 3.1880 0.7904  -0.0611 -0.1417 485  LYS E C   
15180 O  O   . LYS E  485 ? 3.0441 3.4395 3.1685 0.8141  -0.0704 -0.1626 485  LYS E O   
15181 C  CB  . LYS E  485 ? 2.8720 3.2528 3.0403 0.7298  -0.0639 -0.1451 485  LYS E CB  
15182 C  CG  . LYS E  485 ? 2.9073 3.2928 3.0702 0.7394  -0.0384 -0.1206 485  LYS E CG  
15183 C  CD  . LYS E  485 ? 2.9415 3.2871 3.0930 0.7216  -0.0371 -0.1257 485  LYS E CD  
15184 C  CE  . LYS E  485 ? 2.9731 3.3240 3.1268 0.7274  -0.0119 -0.0965 485  LYS E CE  
15185 N  NZ  . LYS E  485 ? 2.9741 3.2830 3.1190 0.7116  -0.0103 -0.1005 485  LYS E NZ  
15186 N  N   . GLY E  486 ? 3.2263 3.6948 3.4047 0.8075  -0.0471 -0.1220 486  GLY E N   
15187 C  CA  . GLY E  486 ? 3.3121 3.7913 3.4634 0.8583  -0.0410 -0.1262 486  GLY E CA  
15188 C  C   . GLY E  486 ? 3.3387 3.8677 3.5242 0.8661  -0.0305 -0.1054 486  GLY E C   
15189 O  O   . GLY E  486 ? 3.3327 3.8954 3.5609 0.8362  -0.0198 -0.0782 486  GLY E O   
15190 N  N   . VAL E  487 ? 3.4399 3.9721 3.6074 0.9070  -0.0350 -0.1189 487  VAL E N   
15191 C  CA  . VAL E  487 ? 3.3968 3.9743 3.5960 0.9203  -0.0267 -0.1021 487  VAL E CA  
15192 C  C   . VAL E  487 ? 3.4216 3.9858 3.6437 0.9017  -0.0558 -0.1209 487  VAL E C   
15193 O  O   . VAL E  487 ? 3.4582 3.9899 3.6561 0.9254  -0.0756 -0.1497 487  VAL E O   
15194 C  CB  . VAL E  487 ? 3.2858 3.8768 3.4508 0.9812  -0.0105 -0.1034 487  VAL E CB  
15195 C  CG1 . VAL E  487 ? 3.0894 3.7247 3.2893 0.9971  -0.0034 -0.0883 487  VAL E CG1 
15196 C  CG2 . VAL E  487 ? 3.3145 3.9281 3.4607 0.9988  0.0213  -0.0774 487  VAL E CG2 
15197 N  N   . LEU E  488 ? 3.2351 3.8241 3.5048 0.8582  -0.0601 -0.1037 488  LEU E N   
15198 C  CA  . LEU E  488 ? 3.1599 3.7470 3.4575 0.8366  -0.0851 -0.1133 488  LEU E CA  
15199 C  C   . LEU E  488 ? 3.0617 3.7049 3.4132 0.8133  -0.0767 -0.0812 488  LEU E C   
15200 O  O   . LEU E  488 ? 3.0411 3.7146 3.4108 0.7987  -0.0568 -0.0545 488  LEU E O   
15201 C  CB  . LEU E  488 ? 3.1276 3.6766 3.4197 0.7978  -0.1072 -0.1321 488  LEU E CB  
15202 C  CG  . LEU E  488 ? 3.0652 3.6141 3.3669 0.7544  -0.1012 -0.1211 488  LEU E CG  
15203 C  CD1 . LEU E  488 ? 3.0112 3.5386 3.3199 0.7175  -0.1253 -0.1366 488  LEU E CD1 
15204 C  CD2 . LEU E  488 ? 3.0171 3.5385 3.2821 0.7664  -0.0869 -0.1253 488  LEU E CD2 
15205 N  N   . PRO E  489 ? 2.9236 3.5830 3.3048 0.8091  -0.0924 -0.0806 489  PRO E N   
15206 C  CA  . PRO E  489 ? 2.9346 3.6503 3.3698 0.7842  -0.0878 -0.0490 489  PRO E CA  
15207 C  C   . PRO E  489 ? 2.9457 3.6642 3.3995 0.7281  -0.0954 -0.0412 489  PRO E C   
15208 O  O   . PRO E  489 ? 2.9382 3.6137 3.3654 0.7079  -0.1071 -0.0626 489  PRO E O   
15209 C  CB  . PRO E  489 ? 2.8518 3.5733 3.3085 0.7915  -0.1080 -0.0551 489  PRO E CB  
15210 C  CG  . PRO E  489 ? 2.8172 3.4794 3.2374 0.7987  -0.1296 -0.0904 489  PRO E CG  
15211 C  CD  . PRO E  489 ? 2.8775 3.5060 3.2485 0.8262  -0.1164 -0.1062 489  PRO E CD  
15212 N  N   . ARG E  490 ? 2.8744 3.6447 3.3752 0.7037  -0.0889 -0.0100 490  ARG E N   
15213 C  CA  . ARG E  490 ? 2.6995 3.4729 3.2196 0.6494  -0.0999 -0.0041 490  ARG E CA  
15214 C  C   . ARG E  490 ? 2.6150 3.3816 3.1429 0.6221  -0.1288 -0.0182 490  ARG E C   
15215 O  O   . ARG E  490 ? 2.5580 3.2930 3.0679 0.5910  -0.1428 -0.0358 490  ARG E O   
15216 C  CB  . ARG E  490 ? 2.6298 3.4619 3.2013 0.6303  -0.0870 0.0349  490  ARG E CB  
15217 C  CG  . ARG E  490 ? 2.6894 3.5628 3.2758 0.6736  -0.0594 0.0610  490  ARG E CG  
15218 C  CD  . ARG E  490 ? 2.6417 3.5635 3.2732 0.6529  -0.0419 0.1010  490  ARG E CD  
15219 N  NE  . ARG E  490 ? 2.6529 3.6208 3.2993 0.6972  -0.0123 0.1295  490  ARG E NE  
15220 C  CZ  . ARG E  490 ? 2.6146 3.5712 3.2279 0.7341  0.0133  0.1315  490  ARG E CZ  
15221 N  NH1 . ARG E  490 ? 2.6376 3.5375 3.2036 0.7308  0.0119  0.1074  490  ARG E NH1 
15222 N  NH2 . ARG E  490 ? 2.5942 3.5990 3.2209 0.7764  0.0410  0.1590  490  ARG E NH2 
15223 N  N   . LYS E  491 ? 2.5756 3.3724 3.1294 0.6360  -0.1370 -0.0095 491  LYS E N   
15224 C  CA  . LYS E  491 ? 2.5957 3.3997 3.1658 0.6100  -0.1631 -0.0135 491  LYS E CA  
15225 C  C   . LYS E  491 ? 2.6381 3.3941 3.1750 0.6275  -0.1778 -0.0428 491  LYS E C   
15226 O  O   . LYS E  491 ? 2.6209 3.3689 3.1542 0.6665  -0.1766 -0.0480 491  LYS E O   
15227 C  CB  . LYS E  491 ? 2.4904 3.3533 3.1105 0.6159  -0.1649 0.0147  491  LYS E CB  
15228 C  CG  . LYS E  491 ? 2.4760 3.3935 3.1377 0.5987  -0.1512 0.0483  491  LYS E CG  
15229 C  CD  . LYS E  491 ? 2.5734 3.4896 3.2399 0.5443  -0.1642 0.0484  491  LYS E CD  
15230 C  CE  . LYS E  491 ? 2.7021 3.6684 3.4140 0.5245  -0.1530 0.0824  491  LYS E CE  
15231 N  NZ  . LYS E  491 ? 2.7403 3.6994 3.4567 0.4705  -0.1695 0.0792  491  LYS E NZ  
15232 N  N   . LEU E  492 ? 2.6521 3.3752 3.1654 0.5996  -0.1918 -0.0618 492  LEU E N   
15233 C  CA  . LEU E  492 ? 2.5743 3.2586 3.0648 0.6082  -0.2083 -0.0846 492  LEU E CA  
15234 C  C   . LEU E  492 ? 2.5039 3.2104 3.0169 0.5797  -0.2303 -0.0777 492  LEU E C   
15235 O  O   . LEU E  492 ? 2.5173 3.2340 3.0297 0.5422  -0.2369 -0.0761 492  LEU E O   
15236 C  CB  . LEU E  492 ? 2.5779 3.2130 3.0261 0.6018  -0.2061 -0.1083 492  LEU E CB  
15237 C  CG  . LEU E  492 ? 2.6309 3.2445 3.0535 0.6271  -0.1846 -0.1134 492  LEU E CG  
15238 C  CD1 . LEU E  492 ? 2.8033 3.3736 3.1900 0.6140  -0.1834 -0.1327 492  LEU E CD1 
15239 C  CD2 . LEU E  492 ? 2.5841 3.1833 2.9949 0.6748  -0.1819 -0.1216 492  LEU E CD2 
15240 N  N   . ASN E  493 ? 2.5102 3.2232 3.0418 0.5986  -0.2423 -0.0737 493  ASN E N   
15241 C  CA  . ASN E  493 ? 2.4857 3.2241 3.0417 0.5764  -0.2628 -0.0623 493  ASN E CA  
15242 C  C   . ASN E  493 ? 2.4308 3.1340 2.9638 0.5669  -0.2779 -0.0798 493  ASN E C   
15243 O  O   . ASN E  493 ? 2.3729 3.0414 2.8974 0.5924  -0.2829 -0.0924 493  ASN E O   
15244 C  CB  . ASN E  493 ? 2.6124 3.3763 3.2057 0.6021  -0.2680 -0.0451 493  ASN E CB  
15245 C  CG  . ASN E  493 ? 2.6834 3.5012 3.3117 0.6020  -0.2569 -0.0187 493  ASN E CG  
15246 O  OD1 . ASN E  493 ? 2.6185 3.4796 3.2842 0.5915  -0.2676 0.0039  493  ASN E OD1 
15247 N  ND2 . ASN E  493 ? 2.8160 3.6348 3.4350 0.6135  -0.2352 -0.0184 493  ASN E ND2 
15248 N  N   . PHE E  494 ? 2.3736 3.0880 2.8987 0.5309  -0.2864 -0.0793 494  PHE E N   
15249 C  CA  . PHE E  494 ? 2.3316 3.0220 2.8365 0.5201  -0.2981 -0.0916 494  PHE E CA  
15250 C  C   . PHE E  494 ? 2.4231 3.1478 2.9542 0.5066  -0.3168 -0.0729 494  PHE E C   
15251 O  O   . PHE E  494 ? 2.4935 3.2632 3.0467 0.4894  -0.3217 -0.0540 494  PHE E O   
15252 C  CB  . PHE E  494 ? 2.2332 2.9092 2.7036 0.4931  -0.2927 -0.1065 494  PHE E CB  
15253 C  CG  . PHE E  494 ? 2.2388 2.8717 2.6793 0.5071  -0.2766 -0.1260 494  PHE E CG  
15254 C  CD1 . PHE E  494 ? 2.2839 2.9201 2.7260 0.5125  -0.2607 -0.1230 494  PHE E CD1 
15255 C  CD2 . PHE E  494 ? 2.2292 2.8222 2.6429 0.5150  -0.2773 -0.1442 494  PHE E CD2 
15256 C  CE1 . PHE E  494 ? 2.3124 2.9116 2.7272 0.5263  -0.2457 -0.1378 494  PHE E CE1 
15257 C  CE2 . PHE E  494 ? 2.3483 2.9040 2.7351 0.5285  -0.2634 -0.1603 494  PHE E CE2 
15258 C  CZ  . PHE E  494 ? 2.3930 2.9512 2.7789 0.5345  -0.2475 -0.1572 494  PHE E CZ  
15259 N  N   . GLN E  495 ? 2.4710 3.1765 3.0015 0.5136  -0.3279 -0.0756 495  GLN E N   
15260 C  CA  . GLN E  495 ? 2.4514 3.1872 3.0028 0.4994  -0.3448 -0.0562 495  GLN E CA  
15261 C  C   . GLN E  495 ? 2.3104 3.0358 2.8304 0.4796  -0.3468 -0.0663 495  GLN E C   
15262 O  O   . GLN E  495 ? 2.2929 2.9813 2.7988 0.4908  -0.3456 -0.0798 495  GLN E O   
15263 C  CB  . GLN E  495 ? 2.5458 3.2721 3.1309 0.5241  -0.3568 -0.0452 495  GLN E CB  
15264 C  CG  . GLN E  495 ? 2.5430 3.3072 3.1582 0.5107  -0.3738 -0.0178 495  GLN E CG  
15265 C  CD  . GLN E  495 ? 2.4338 3.1805 3.0848 0.5333  -0.3875 -0.0069 495  GLN E CD  
15266 O  OE1 . GLN E  495 ? 2.3838 3.0865 3.0338 0.5590  -0.3865 -0.0237 495  GLN E OE1 
15267 N  NE2 . GLN E  495 ? 2.3516 3.1320 3.0345 0.5237  -0.4019 0.0215  495  GLN E NE2 
15268 N  N   . VAL E  496 ? 2.3775 3.1366 2.8861 0.4514  -0.3505 -0.0600 496  VAL E N   
15269 C  CA  . VAL E  496 ? 2.4458 3.1979 2.9175 0.4337  -0.3494 -0.0719 496  VAL E CA  
15270 C  C   . VAL E  496 ? 2.4284 3.2182 2.9120 0.4231  -0.3636 -0.0497 496  VAL E C   
15271 O  O   . VAL E  496 ? 2.3860 3.2196 2.8929 0.4135  -0.3742 -0.0280 496  VAL E O   
15272 C  CB  . VAL E  496 ? 2.5460 3.3005 2.9860 0.4109  -0.3425 -0.0873 496  VAL E CB  
15273 C  CG1 . VAL E  496 ? 2.6115 3.3539 3.0091 0.3971  -0.3403 -0.1031 496  VAL E CG1 
15274 C  CG2 . VAL E  496 ? 2.5636 3.2850 2.9980 0.4220  -0.3276 -0.1029 496  VAL E CG2 
15275 N  N   . GLU E  497 ? 2.4783 3.2544 2.9484 0.4257  -0.3633 -0.0520 497  GLU E N   
15276 C  CA  . GLU E  497 ? 2.3764 3.1891 2.8535 0.4167  -0.3735 -0.0291 497  GLU E CA  
15277 C  C   . GLU E  497 ? 2.4428 3.2569 2.8711 0.4025  -0.3661 -0.0436 497  GLU E C   
15278 O  O   . GLU E  497 ? 2.5152 3.2904 2.9160 0.4084  -0.3537 -0.0672 497  GLU E O   
15279 C  CB  . GLU E  497 ? 2.3375 3.1392 2.8505 0.4342  -0.3805 -0.0120 497  GLU E CB  
15280 C  CG  . GLU E  497 ? 2.4251 3.2019 2.9767 0.4558  -0.3856 -0.0101 497  GLU E CG  
15281 C  CD  . GLU E  497 ? 2.3750 3.1877 2.9609 0.4551  -0.3950 0.0119  497  GLU E CD  
15282 O  OE1 . GLU E  497 ? 2.4699 3.2667 3.0708 0.4706  -0.3924 0.0051  497  GLU E OE1 
15283 O  OE2 . GLU E  497 ? 2.2338 3.0931 2.8312 0.4409  -0.4042 0.0373  497  GLU E OE2 
15284 N  N   . LEU E  498 ? 2.5086 3.3682 2.9248 0.3860  -0.3736 -0.0293 498  LEU E N   
15285 C  CA  . LEU E  498 ? 2.6340 3.5004 3.0004 0.3754  -0.3675 -0.0419 498  LEU E CA  
15286 C  C   . LEU E  498 ? 2.6133 3.5223 2.9898 0.3765  -0.3734 -0.0112 498  LEU E C   
15287 O  O   . LEU E  498 ? 2.4920 3.4424 2.9007 0.3726  -0.3869 0.0188  498  LEU E O   
15288 C  CB  . LEU E  498 ? 2.6368 3.5180 2.9669 0.3536  -0.3715 -0.0583 498  LEU E CB  
15289 C  CG  . LEU E  498 ? 2.6276 3.4629 2.9239 0.3482  -0.3609 -0.0950 498  LEU E CG  
15290 C  CD1 . LEU E  498 ? 2.5976 3.4020 2.9263 0.3588  -0.3558 -0.0989 498  LEU E CD1 
15291 C  CD2 . LEU E  498 ? 2.6776 3.5319 2.9430 0.3234  -0.3707 -0.1075 498  LEU E CD2 
15292 N  N   . LEU E  499 ? 2.8326 3.7339 3.1843 0.3828  -0.3624 -0.0158 499  LEU E N   
15293 C  CA  . LEU E  499 ? 2.8169 3.7619 3.1759 0.3848  -0.3643 0.0157  499  LEU E CA  
15294 C  C   . LEU E  499 ? 2.8483 3.8068 3.1447 0.3802  -0.3532 0.0001  499  LEU E C   
15295 O  O   . LEU E  499 ? 2.8735 3.7953 3.1390 0.3875  -0.3381 -0.0264 499  LEU E O   
15296 C  CB  . LEU E  499 ? 2.8472 3.7761 3.2495 0.4012  -0.3618 0.0341  499  LEU E CB  
15297 C  CG  . LEU E  499 ? 2.8549 3.7580 3.3154 0.4107  -0.3729 0.0433  499  LEU E CG  
15298 C  CD1 . LEU E  499 ? 2.8346 3.7065 3.3230 0.4254  -0.3702 0.0471  499  LEU E CD1 
15299 C  CD2 . LEU E  499 ? 2.7831 3.7290 3.2880 0.4068  -0.3895 0.0810  499  LEU E CD2 
15300 N  N   . LEU E  500 ? 2.8029 3.8141 3.0792 0.3702  -0.3609 0.0165  500  LEU E N   
15301 C  CA  . LEU E  500 ? 2.8349 3.8645 3.0470 0.3687  -0.3518 0.0028  500  LEU E CA  
15302 C  C   . LEU E  500 ? 2.8603 3.9209 3.0801 0.3832  -0.3406 0.0329  500  LEU E C   
15303 O  O   . LEU E  500 ? 2.9059 4.0008 3.1780 0.3862  -0.3480 0.0755  500  LEU E O   
15304 C  CB  . LEU E  500 ? 2.7644 3.8389 2.9459 0.3519  -0.3672 0.0055  500  LEU E CB  
15305 C  CG  . LEU E  500 ? 2.8590 3.9129 3.0311 0.3337  -0.3803 -0.0216 500  LEU E CG  
15306 C  CD1 . LEU E  500 ? 2.8788 3.9888 3.0382 0.3171  -0.4006 -0.0068 500  LEU E CD1 
15307 C  CD2 . LEU E  500 ? 3.0137 4.0164 3.1300 0.3308  -0.3699 -0.0705 500  LEU E CD2 
15308 N  N   . ASP E  501 ? 2.7672 3.8167 2.9374 0.3928  -0.3224 0.0123  501  ASP E N   
15309 C  CA  . ASP E  501 ? 2.6933 3.7790 2.8645 0.4078  -0.3083 0.0409  501  ASP E CA  
15310 C  C   . ASP E  501 ? 2.6555 3.7372 2.9032 0.4164  -0.3090 0.0752  501  ASP E C   
15311 O  O   . ASP E  501 ? 2.5732 3.7027 2.8600 0.4192  -0.3124 0.1213  501  ASP E O   
15312 C  CB  . ASP E  501 ? 2.7421 3.8989 2.8917 0.4042  -0.3140 0.0703  501  ASP E CB  
15313 C  CG  . ASP E  501 ? 2.9344 4.1320 3.0665 0.4215  -0.2945 0.0941  501  ASP E CG  
15314 O  OD1 . ASP E  501 ? 3.0069 4.1750 3.1137 0.4353  -0.2748 0.0719  501  ASP E OD1 
15315 O  OD2 . ASP E  501 ? 3.0844 4.3461 3.2303 0.4225  -0.2982 0.1379  501  ASP E OD2 
15316 N  N   . LYS E  502 ? 2.8653 3.8884 3.1353 0.4203  -0.3074 0.0529  502  LYS E N   
15317 C  CA  . LYS E  502 ? 2.8774 3.8893 3.2184 0.4276  -0.3128 0.0799  502  LYS E CA  
15318 C  C   . LYS E  502 ? 2.7985 3.8363 3.1536 0.4403  -0.2988 0.1068  502  LYS E C   
15319 O  O   . LYS E  502 ? 2.8293 3.8890 3.2472 0.4421  -0.3071 0.1481  502  LYS E O   
15320 C  CB  . LYS E  502 ? 2.8211 3.7660 3.1756 0.4311  -0.3144 0.0482  502  LYS E CB  
15321 C  CG  . LYS E  502 ? 2.7975 3.7299 3.2231 0.4383  -0.3248 0.0740  502  LYS E CG  
15322 C  CD  . LYS E  502 ? 2.6587 3.5285 3.0951 0.4457  -0.3261 0.0450  502  LYS E CD  
15323 C  CE  . LYS E  502 ? 2.5827 3.4424 3.0893 0.4520  -0.3414 0.0712  502  LYS E CE  
15324 N  NZ  . LYS E  502 ? 2.5226 3.3984 3.0734 0.4462  -0.3613 0.0958  502  LYS E NZ  
15325 N  N   . LEU E  503 ? 2.6369 3.6714 2.9376 0.4497  -0.2778 0.0850  503  LEU E N   
15326 C  CA  . LEU E  503 ? 2.6591 3.7183 2.9707 0.4646  -0.2606 0.1083  503  LEU E CA  
15327 C  C   . LEU E  503 ? 2.6326 3.7588 2.9909 0.4643  -0.2649 0.1674  503  LEU E C   
15328 O  O   . LEU E  503 ? 2.6428 3.7860 3.0487 0.4725  -0.2595 0.1999  503  LEU E O   
15329 C  CB  . LEU E  503 ? 2.7973 3.8606 3.0309 0.4757  -0.2369 0.0799  503  LEU E CB  
15330 C  CG  . LEU E  503 ? 2.9659 3.9712 3.1743 0.4866  -0.2223 0.0395  503  LEU E CG  
15331 C  CD1 . LEU E  503 ? 2.9798 3.9214 3.2042 0.4768  -0.2369 0.0092  503  LEU E CD1 
15332 C  CD2 . LEU E  503 ? 3.0158 4.0177 3.1390 0.4953  -0.2035 0.0043  503  LEU E CD2 
15333 N  N   . LYS E  504 ? 2.6510 3.8174 2.9999 0.4542  -0.2756 0.1843  504  LYS E N   
15334 C  CA  . LYS E  504 ? 2.7435 3.9727 3.1422 0.4522  -0.2827 0.2440  504  LYS E CA  
15335 C  C   . LYS E  504 ? 2.6855 3.8911 3.1704 0.4445  -0.3056 0.2672  504  LYS E C   
15336 O  O   . LYS E  504 ? 2.6783 3.8586 3.1720 0.4347  -0.3232 0.2526  504  LYS E O   
15337 C  CB  . LYS E  504 ? 2.8462 4.1249 3.2027 0.4448  -0.2879 0.2526  504  LYS E CB  
15338 C  CG  . LYS E  504 ? 2.9988 4.3093 3.2698 0.4550  -0.2671 0.2355  504  LYS E CG  
15339 C  CD  . LYS E  504 ? 3.0129 4.3772 3.2968 0.4718  -0.2461 0.2781  504  LYS E CD  
15340 C  CE  . LYS E  504 ? 2.9771 4.3796 3.1706 0.4858  -0.2253 0.2631  504  LYS E CE  
15341 N  NZ  . LYS E  504 ? 2.8933 4.3570 3.0991 0.5051  -0.2018 0.3091  504  LYS E NZ  
15342 N  N   . GLN E  505 ? 2.7642 3.9774 3.3137 0.4496  -0.3060 0.3030  505  GLN E N   
15343 C  CA  . GLN E  505 ? 2.7288 3.9165 3.3616 0.4435  -0.3300 0.3252  505  GLN E CA  
15344 C  C   . GLN E  505 ? 2.8600 4.0872 3.5264 0.4341  -0.3470 0.3641  505  GLN E C   
15345 O  O   . GLN E  505 ? 3.0956 4.3831 3.7320 0.4328  -0.3394 0.3872  505  GLN E O   
15346 C  CB  . GLN E  505 ? 2.5990 3.7934 3.2960 0.4487  -0.3290 0.3598  505  GLN E CB  
15347 C  CG  . GLN E  505 ? 2.5998 3.7535 3.2752 0.4587  -0.3152 0.3250  505  GLN E CG  
15348 C  CD  . GLN E  505 ? 2.5989 3.6745 3.2834 0.4575  -0.3312 0.2819  505  GLN E CD  
15349 O  OE1 . GLN E  505 ? 2.6734 3.7239 3.3890 0.4507  -0.3532 0.2808  505  GLN E OE1 
15350 N  NE2 . GLN E  505 ? 2.5022 3.5406 3.1587 0.4663  -0.3193 0.2473  505  GLN E NE2 
15351 N  N   . LYS E  506 ? 2.7612 3.9533 3.4894 0.4292  -0.3707 0.3708  506  LYS E N   
15352 C  CA  . LYS E  506 ? 2.7308 3.9530 3.5004 0.4220  -0.3887 0.4081  506  LYS E CA  
15353 C  C   . LYS E  506 ? 2.9903 4.2814 3.8031 0.4210  -0.3864 0.4744  506  LYS E C   
15354 O  O   . LYS E  506 ? 3.0354 4.3226 3.9209 0.4211  -0.3950 0.5090  506  LYS E O   
15355 C  CB  . LYS E  506 ? 2.4758 3.6415 3.3083 0.4214  -0.4135 0.4030  506  LYS E CB  
15356 C  CG  . LYS E  506 ? 2.3870 3.5758 3.2572 0.4163  -0.4316 0.4341  506  LYS E CG  
15357 C  CD  . LYS E  506 ? 2.3661 3.5841 3.1713 0.4116  -0.4253 0.4155  506  LYS E CD  
15358 C  CE  . LYS E  506 ? 2.3287 3.5736 3.1748 0.4075  -0.4435 0.4492  506  LYS E CE  
15359 N  NZ  . LYS E  506 ? 2.3743 3.5598 3.2723 0.4127  -0.4625 0.4362  506  LYS E NZ  
15360 N  N   . GLY E  507 ? 3.1708 4.5263 3.9394 0.4198  -0.3758 0.4934  507  GLY E N   
15361 C  CA  . GLY E  507 ? 3.1327 4.5632 3.9332 0.4206  -0.3706 0.5589  507  GLY E CA  
15362 C  C   . GLY E  507 ? 3.0425 4.5294 3.7612 0.4282  -0.3445 0.5557  507  GLY E C   
15363 O  O   . GLY E  507 ? 3.0168 4.5776 3.7372 0.4306  -0.3375 0.6057  507  GLY E O   
15364 N  N   . ALA E  508 ? 2.9039 4.3552 3.5492 0.4335  -0.3299 0.4967  508  ALA E N   
15365 C  CA  . ALA E  508 ? 2.8420 4.3340 3.4013 0.4435  -0.3053 0.4826  508  ALA E CA  
15366 C  C   . ALA E  508 ? 2.9711 4.4957 3.4681 0.4377  -0.3114 0.4717  508  ALA E C   
15367 O  O   . ALA E  508 ? 3.1001 4.6391 3.6333 0.4271  -0.3322 0.4957  508  ALA E O   
15368 C  CB  . ALA E  508 ? 2.8068 4.2427 3.3128 0.4513  -0.2896 0.4222  508  ALA E CB  
15369 N  N   . ILE E  509 ? 2.8824 4.4177 3.2864 0.4450  -0.2948 0.4352  509  ILE E N   
15370 C  CA  . ILE E  509 ? 2.9234 4.4872 3.2584 0.4391  -0.3024 0.4180  509  ILE E CA  
15371 C  C   . ILE E  509 ? 2.8303 4.3254 3.1110 0.4317  -0.3074 0.3456  509  ILE E C   
15372 O  O   . ILE E  509 ? 2.8871 4.3477 3.1170 0.4409  -0.2900 0.3035  509  ILE E O   
15373 C  CB  . ILE E  509 ? 3.0685 4.7028 3.3355 0.4539  -0.2824 0.4346  509  ILE E CB  
15374 C  CG1 . ILE E  509 ? 3.0002 4.6503 3.1806 0.4478  -0.2923 0.4006  509  ILE E CG1 
15375 C  CG2 . ILE E  509 ? 3.0802 4.7011 3.3141 0.4731  -0.2530 0.4152  509  ILE E CG2 
15376 C  CD1 . ILE E  509 ? 2.8691 4.5554 3.0804 0.4322  -0.3188 0.4325  509  ILE E CD1 
15377 N  N   . ARG E  510 ? 2.7024 4.1778 2.9987 0.4156  -0.3307 0.3337  510  ARG E N   
15378 C  CA  . ARG E  510 ? 2.6852 4.0987 2.9438 0.4061  -0.3377 0.2726  510  ARG E CA  
15379 C  C   . ARG E  510 ? 2.8805 4.3189 3.0511 0.4008  -0.3407 0.2438  510  ARG E C   
15380 O  O   . ARG E  510 ? 3.1006 4.6057 3.2504 0.4014  -0.3450 0.2749  510  ARG E O   
15381 C  CB  . ARG E  510 ? 2.5542 3.9390 2.8754 0.3930  -0.3604 0.2764  510  ARG E CB  
15382 C  CG  . ARG E  510 ? 2.5402 3.8526 2.8462 0.3864  -0.3636 0.2205  510  ARG E CG  
15383 C  CD  . ARG E  510 ? 2.5151 3.7704 2.8463 0.3971  -0.3503 0.2040  510  ARG E CD  
15384 N  NE  . ARG E  510 ? 2.4087 3.6610 2.8253 0.4012  -0.3583 0.2434  510  ARG E NE  
15385 C  CZ  . ARG E  510 ? 2.3737 3.5739 2.8281 0.4082  -0.3555 0.2329  510  ARG E CZ  
15386 N  NH1 . ARG E  510 ? 2.4130 3.5632 2.8286 0.4126  -0.3431 0.1871  510  ARG E NH1 
15387 N  NH2 . ARG E  510 ? 2.3043 3.5011 2.8355 0.4109  -0.3669 0.2679  510  ARG E NH2 
15388 N  N   . ARG E  511 ? 2.7857 4.1692 2.9041 0.3956  -0.3397 0.1842  511  ARG E N   
15389 C  CA  . ARG E  511 ? 2.8368 4.2335 2.8679 0.3903  -0.3443 0.1497  511  ARG E CA  
15390 C  C   . ARG E  511 ? 2.7882 4.1413 2.8030 0.3698  -0.3638 0.1057  511  ARG E C   
15391 O  O   . ARG E  511 ? 2.7758 4.1358 2.7212 0.3620  -0.3726 0.0749  511  ARG E O   
15392 C  CB  . ARG E  511 ? 2.9834 4.3644 2.9441 0.4083  -0.3193 0.1178  511  ARG E CB  
15393 C  CG  . ARG E  511 ? 3.0272 4.4633 2.9938 0.4302  -0.2975 0.1623  511  ARG E CG  
15394 C  CD  . ARG E  511 ? 2.9829 4.3878 2.9097 0.4510  -0.2692 0.1339  511  ARG E CD  
15395 N  NE  . ARG E  511 ? 2.9504 4.2860 2.9243 0.4495  -0.2646 0.1143  511  ARG E NE  
15396 C  CZ  . ARG E  511 ? 2.9787 4.2767 2.9320 0.4657  -0.2423 0.0888  511  ARG E CZ  
15397 N  NH1 . ARG E  511 ? 2.9861 4.3075 2.8727 0.4859  -0.2209 0.0786  511  ARG E NH1 
15398 N  NH2 . ARG E  511 ? 3.0462 4.2843 3.0439 0.4635  -0.2410 0.0734  511  ARG E NH2 
15399 N  N   . ALA E  512 ? 2.9316 4.2414 3.0069 0.3614  -0.3714 0.1020  512  ALA E N   
15400 C  CA  . ALA E  512 ? 3.0421 4.3151 3.1091 0.3426  -0.3878 0.0657  512  ALA E CA  
15401 C  C   . ALA E  512 ? 3.0360 4.3166 3.1800 0.3333  -0.4048 0.0949  512  ALA E C   
15402 O  O   . ALA E  512 ? 3.0462 4.3301 3.2539 0.3433  -0.4009 0.1297  512  ALA E O   
15403 C  CB  . ALA E  512 ? 3.0800 4.2766 3.1277 0.3452  -0.3745 0.0168  512  ALA E CB  
15404 N  N   . LEU E  513 ? 2.9768 4.2585 3.1158 0.3146  -0.4244 0.0796  513  LEU E N   
15405 C  CA  . LEU E  513 ? 2.9108 4.1995 3.1177 0.3066  -0.4400 0.1025  513  LEU E CA  
15406 C  C   . LEU E  513 ? 2.9061 4.1921 3.0917 0.2847  -0.4584 0.0755  513  LEU E C   
15407 O  O   . LEU E  513 ? 2.9795 4.2876 3.1048 0.2732  -0.4684 0.0579  513  LEU E O   
15408 C  CB  . LEU E  513 ? 2.8262 4.1804 3.0773 0.3104  -0.4502 0.1600  513  LEU E CB  
15409 C  CG  . LEU E  513 ? 2.8099 4.2351 3.0241 0.3012  -0.4657 0.1801  513  LEU E CG  
15410 C  CD1 . LEU E  513 ? 2.8042 4.2560 3.0476 0.2840  -0.4907 0.1904  513  LEU E CD1 
15411 C  CD2 . LEU E  513 ? 2.7998 4.2789 3.0369 0.3150  -0.4604 0.2333  513  LEU E CD2 
15412 N  N   . PHE E  514 ? 2.8311 4.0897 3.0660 0.2796  -0.4632 0.0721  514  PHE E N   
15413 C  CA  . PHE E  514 ? 2.7810 4.0311 3.0060 0.2585  -0.4782 0.0470  514  PHE E CA  
15414 C  C   . PHE E  514 ? 2.8754 4.1920 3.0923 0.2413  -0.5040 0.0672  514  PHE E C   
15415 O  O   . PHE E  514 ? 2.8729 4.2440 3.1095 0.2473  -0.5105 0.1083  514  PHE E O   
15416 C  CB  . PHE E  514 ? 2.7250 3.9454 3.0129 0.2609  -0.4761 0.0502  514  PHE E CB  
15417 C  CG  . PHE E  514 ? 2.7422 3.8940 3.0294 0.2743  -0.4543 0.0226  514  PHE E CG  
15418 C  CD1 . PHE E  514 ? 2.8073 3.9404 3.1084 0.2958  -0.4381 0.0334  514  PHE E CD1 
15419 C  CD2 . PHE E  514 ? 2.7229 3.8307 2.9975 0.2645  -0.4512 -0.0120 514  PHE E CD2 
15420 C  CE1 . PHE E  514 ? 2.7560 3.8285 3.0555 0.3081  -0.4202 0.0085  514  PHE E CE1 
15421 C  CE2 . PHE E  514 ? 2.7524 3.7997 3.0249 0.2777  -0.4314 -0.0352 514  PHE E CE2 
15422 C  CZ  . PHE E  514 ? 2.7461 3.7762 3.0295 0.2999  -0.4163 -0.0258 514  PHE E CZ  
15423 N  N   . LEU E  515 ? 2.9954 4.3072 3.1857 0.2186  -0.5203 0.0391  515  LEU E N   
15424 C  CA  . LEU E  515 ? 2.9918 4.3637 3.1616 0.1995  -0.5482 0.0501  515  LEU E CA  
15425 C  C   . LEU E  515 ? 2.9347 4.3589 3.1768 0.1966  -0.5633 0.0968  515  LEU E C   
15426 O  O   . LEU E  515 ? 2.9963 4.4833 3.2411 0.1971  -0.5766 0.1319  515  LEU E O   
15427 C  CB  . LEU E  515 ? 3.0528 4.3998 3.1799 0.1740  -0.5646 0.0058  515  LEU E CB  
15428 C  CG  . LEU E  515 ? 3.1880 4.5912 3.2836 0.1512  -0.5980 0.0083  515  LEU E CG  
15429 C  CD1 . LEU E  515 ? 3.2522 4.6894 3.2794 0.1615  -0.5987 0.0103  515  LEU E CD1 
15430 C  CD2 . LEU E  515 ? 3.2175 4.5866 3.2843 0.1236  -0.6164 -0.0359 515  LEU E CD2 
15431 N  N   . TYR E  516 ? 2.9568 4.3582 3.2580 0.1957  -0.5604 0.0995  516  TYR E N   
15432 C  CA  . TYR E  516 ? 2.9552 4.4038 3.3270 0.1957  -0.5731 0.1421  516  TYR E CA  
15433 C  C   . TYR E  516 ? 2.8217 4.2619 3.2521 0.2230  -0.5561 0.1744  516  TYR E C   
15434 O  O   . TYR E  516 ? 2.8231 4.3118 3.3014 0.2291  -0.5660 0.2180  516  TYR E O   
15435 C  CB  . TYR E  516 ? 3.0118 4.4498 3.4170 0.1793  -0.5816 0.1301  516  TYR E CB  
15436 C  CG  . TYR E  516 ? 3.0204 4.5251 3.4792 0.1692  -0.6044 0.1688  516  TYR E CG  
15437 C  CD1 . TYR E  516 ? 2.9660 4.5340 3.4355 0.1734  -0.6180 0.2094  516  TYR E CD1 
15438 C  CD2 . TYR E  516 ? 3.0243 4.5317 3.5262 0.1565  -0.6113 0.1682  516  TYR E CD2 
15439 C  CE1 . TYR E  516 ? 2.9462 4.5768 3.4672 0.1654  -0.6390 0.2467  516  TYR E CE1 
15440 C  CE2 . TYR E  516 ? 2.9779 4.5496 3.5328 0.1486  -0.6313 0.2057  516  TYR E CE2 
15441 C  CZ  . TYR E  516 ? 2.8846 4.5170 3.4486 0.1532  -0.6456 0.2441  516  TYR E CZ  
15442 O  OH  . TYR E  516 ? 2.6468 4.3448 3.2658 0.1463  -0.6657 0.2831  516  TYR E OH  
15443 N  N   . SER E  517 ? 2.5472 3.9257 2.9757 0.2396  -0.5325 0.1538  517  SER E N   
15444 C  CA  . SER E  517 ? 2.5366 3.9000 3.0185 0.2649  -0.5193 0.1799  517  SER E CA  
15445 C  C   . SER E  517 ? 2.6271 4.0269 3.1089 0.2747  -0.5204 0.2144  517  SER E C   
15446 O  O   . SER E  517 ? 2.6882 4.0934 3.2266 0.2914  -0.5185 0.2484  517  SER E O   
15447 C  CB  . SER E  517 ? 2.4621 3.7518 2.9361 0.2788  -0.4966 0.1474  517  SER E CB  
15448 O  OG  . SER E  517 ? 2.4049 3.6757 2.9296 0.3024  -0.4876 0.1691  517  SER E OG  
15449 N  N   . ARG E  518 ? 2.6139 4.0382 3.0339 0.2657  -0.5233 0.2069  518  ARG E N   
15450 C  CA  . ARG E  518 ? 2.5388 4.0041 2.9533 0.2753  -0.5220 0.2420  518  ARG E CA  
15451 C  C   . ARG E  518 ? 2.4892 3.9177 2.9389 0.2971  -0.5030 0.2542  518  ARG E C   
15452 O  O   . ARG E  518 ? 2.3919 3.8505 2.8825 0.3078  -0.5044 0.2985  518  ARG E O   
15453 C  CB  . ARG E  518 ? 2.6074 4.1438 3.0614 0.2717  -0.5422 0.2920  518  ARG E CB  
15454 C  CG  . ARG E  518 ? 2.7136 4.2856 3.1559 0.2499  -0.5650 0.2849  518  ARG E CG  
15455 C  CD  . ARG E  518 ? 2.7759 4.3564 3.1312 0.2329  -0.5722 0.2492  518  ARG E CD  
15456 N  NE  . ARG E  518 ? 2.7580 4.3935 3.1032 0.2116  -0.6009 0.2565  518  ARG E NE  
15457 C  CZ  . ARG E  518 ? 2.6136 4.3203 2.9475 0.2089  -0.6177 0.2918  518  ARG E CZ  
15458 N  NH1 . ARG E  518 ? 2.6388 4.3716 2.9723 0.2265  -0.6068 0.3256  518  ARG E NH1 
15459 N  NH2 . ARG E  518 ? 2.5091 4.2636 2.8345 0.1882  -0.6462 0.2955  518  ARG E NH2 
15460 N  N   . SER E  519 ? 2.5937 3.9564 3.0300 0.3030  -0.4866 0.2157  519  SER E N   
15461 C  CA  . SER E  519 ? 2.7218 4.0438 3.1955 0.3223  -0.4721 0.2231  519  SER E CA  
15462 C  C   . SER E  519 ? 2.7622 4.0263 3.1916 0.3262  -0.4534 0.1785  519  SER E C   
15463 O  O   . SER E  519 ? 2.8191 4.0465 3.2249 0.3189  -0.4509 0.1400  519  SER E O   
15464 C  CB  . SER E  519 ? 2.6863 3.9847 3.2301 0.3317  -0.4770 0.2347  519  SER E CB  
15465 O  OG  . SER E  519 ? 2.6568 3.9128 3.2364 0.3499  -0.4672 0.2395  519  SER E OG  
15466 N  N   . PRO E  520 ? 2.7719 4.0286 3.1921 0.3379  -0.4397 0.1853  520  PRO E N   
15467 C  CA  . PRO E  520 ? 2.7321 3.9390 3.1088 0.3432  -0.4212 0.1454  520  PRO E CA  
15468 C  C   . PRO E  520 ? 2.7006 3.8417 3.0956 0.3481  -0.4155 0.1143  520  PRO E C   
15469 O  O   . PRO E  520 ? 2.7406 3.8386 3.0971 0.3501  -0.4019 0.0777  520  PRO E O   
15470 C  CB  . PRO E  520 ? 2.6670 3.8848 3.0602 0.3575  -0.4102 0.1732  520  PRO E CB  
15471 C  CG  . PRO E  520 ? 2.6910 3.9788 3.1015 0.3546  -0.4211 0.2213  520  PRO E CG  
15472 C  CD  . PRO E  520 ? 2.7379 4.0417 3.1841 0.3453  -0.4408 0.2335  520  PRO E CD  
15473 N  N   . SER E  521 ? 2.4980 3.6314 2.9507 0.3523  -0.4248 0.1295  521  SER E N   
15474 C  CA  . SER E  521 ? 2.3836 3.4600 2.8541 0.3603  -0.4194 0.1035  521  SER E CA  
15475 C  C   . SER E  521 ? 2.4531 3.5401 2.9414 0.3520  -0.4299 0.1018  521  SER E C   
15476 O  O   . SER E  521 ? 2.3727 3.5079 2.8881 0.3464  -0.4441 0.1322  521  SER E O   
15477 C  CB  . SER E  521 ? 2.3195 3.3676 2.8448 0.3796  -0.4189 0.1203  521  SER E CB  
15478 O  OG  . SER E  521 ? 2.2669 3.3513 2.8458 0.3829  -0.4331 0.1629  521  SER E OG  
15479 N  N   . HIS E  522 ? 2.6652 3.7102 3.1404 0.3518  -0.4222 0.0688  522  HIS E N   
15480 C  CA  . HIS E  522 ? 2.7644 3.8182 3.2594 0.3450  -0.4290 0.0670  522  HIS E CA  
15481 C  C   . HIS E  522 ? 2.7024 3.7052 3.2203 0.3629  -0.4182 0.0510  522  HIS E C   
15482 O  O   . HIS E  522 ? 2.5996 3.5559 3.0882 0.3675  -0.4047 0.0216  522  HIS E O   
15483 C  CB  . HIS E  522 ? 2.7406 3.8040 3.1889 0.3212  -0.4319 0.0431  522  HIS E CB  
15484 C  CG  . HIS E  522 ? 2.7588 3.8350 3.2324 0.3118  -0.4390 0.0440  522  HIS E CG  
15485 N  ND1 . HIS E  522 ? 2.6985 3.7346 3.1722 0.3139  -0.4280 0.0202  522  HIS E ND1 
15486 C  CD2 . HIS E  522 ? 2.7594 3.8884 3.2620 0.3007  -0.4554 0.0693  522  HIS E CD2 
15487 C  CE1 . HIS E  522 ? 2.6672 3.7320 3.1706 0.3045  -0.4364 0.0317  522  HIS E CE1 
15488 N  NE2 . HIS E  522 ? 2.7301 3.8513 3.2522 0.2961  -0.4536 0.0608  522  HIS E NE2 
15489 N  N   . SER E  523 ? 2.8276 3.8400 3.3960 0.3752  -0.4239 0.0708  523  SER E N   
15490 C  CA  . SER E  523 ? 2.7234 3.6930 3.3120 0.3957  -0.4143 0.0571  523  SER E CA  
15491 C  C   . SER E  523 ? 2.8187 3.8017 3.4115 0.3877  -0.4121 0.0510  523  SER E C   
15492 O  O   . SER E  523 ? 2.8319 3.8646 3.4388 0.3721  -0.4236 0.0700  523  SER E O   
15493 C  CB  . SER E  523 ? 2.6462 3.6124 3.2878 0.4192  -0.4212 0.0809  523  SER E CB  
15494 O  OG  . SER E  523 ? 2.6988 3.6214 3.3528 0.4426  -0.4122 0.0643  523  SER E OG  
15495 N  N   . LYS E  524 ? 2.8471 3.7886 3.4297 0.3983  -0.3977 0.0270  524  LYS E N   
15496 C  CA  . LYS E  524 ? 2.8697 3.8236 3.4600 0.3915  -0.3930 0.0238  524  LYS E CA  
15497 C  C   . LYS E  524 ? 2.8731 3.7849 3.4701 0.4177  -0.3766 0.0095  524  LYS E C   
15498 O  O   . LYS E  524 ? 2.7576 3.6215 3.3253 0.4269  -0.3661 -0.0142 524  LYS E O   
15499 C  CB  . LYS E  524 ? 2.7641 3.7202 3.3135 0.3615  -0.3930 0.0047  524  LYS E CB  
15500 C  CG  . LYS E  524 ? 2.7336 3.7023 3.2965 0.3509  -0.3893 0.0038  524  LYS E CG  
15501 C  CD  . LYS E  524 ? 2.6910 3.7199 3.3013 0.3459  -0.4023 0.0363  524  LYS E CD  
15502 C  CE  . LYS E  524 ? 2.6476 3.6911 3.2835 0.3414  -0.3955 0.0412  524  LYS E CE  
15503 N  NZ  . LYS E  524 ? 2.6660 3.7047 3.2742 0.3090  -0.3991 0.0234  524  LYS E NZ  
15504 N  N   . ASN E  525 ? 2.8073 3.7401 3.4422 0.4314  -0.3742 0.0252  525  ASN E N   
15505 C  CA  . ASN E  525 ? 2.7004 3.6022 3.3400 0.4585  -0.3574 0.0142  525  ASN E CA  
15506 C  C   . ASN E  525 ? 2.7198 3.6256 3.3441 0.4411  -0.3462 0.0046  525  ASN E C   
15507 O  O   . ASN E  525 ? 2.8936 3.8448 3.5370 0.4194  -0.3527 0.0208  525  ASN E O   
15508 C  CB  . ASN E  525 ? 2.6040 3.5294 3.2917 0.4848  -0.3585 0.0372  525  ASN E CB  
15509 C  CG  . ASN E  525 ? 2.6868 3.5964 3.3922 0.5044  -0.3699 0.0446  525  ASN E CG  
15510 O  OD1 . ASN E  525 ? 2.2774 3.1441 2.9597 0.5101  -0.3711 0.0272  525  ASN E OD1 
15511 N  ND2 . ASN E  525 ? 3.7434 4.6882 4.4933 0.5138  -0.3795 0.0723  525  ASN E ND2 
15512 N  N   . MET E  526 ? 2.4926 3.3522 3.0865 0.4505  -0.3307 -0.0195 526  MET E N   
15513 C  CA  . MET E  526 ? 2.4108 3.2657 2.9866 0.4305  -0.3211 -0.0298 526  MET E CA  
15514 C  C   . MET E  526 ? 2.4224 3.2578 3.0021 0.4568  -0.3002 -0.0332 526  MET E C   
15515 O  O   . MET E  526 ? 2.4775 3.2669 3.0319 0.4792  -0.2901 -0.0520 526  MET E O   
15516 C  CB  . MET E  526 ? 2.4033 3.2215 2.9317 0.4119  -0.3219 -0.0555 526  MET E CB  
15517 C  CG  . MET E  526 ? 2.5133 3.3417 3.0285 0.3769  -0.3250 -0.0612 526  MET E CG  
15518 S  SD  . MET E  526 ? 2.5473 3.3247 3.0045 0.3609  -0.3219 -0.0948 526  MET E SD  
15519 C  CE  . MET E  526 ? 2.6344 3.4235 3.0923 0.3240  -0.3265 -0.0974 526  MET E CE  
15520 N  N   . THR E  527 ? 2.5441 3.4178 3.1562 0.4545  -0.2939 -0.0133 527  THR E N   
15521 C  CA  . THR E  527 ? 2.7001 3.5640 3.3145 0.4744  -0.2717 -0.0127 527  THR E CA  
15522 C  C   . THR E  527 ? 2.7385 3.5863 3.3320 0.4457  -0.2659 -0.0233 527  THR E C   
15523 O  O   . THR E  527 ? 2.7954 3.6739 3.4053 0.4113  -0.2760 -0.0129 527  THR E O   
15524 C  CB  . THR E  527 ? 2.7675 3.6849 3.4311 0.4870  -0.2655 0.0179  527  THR E CB  
15525 O  OG1 . THR E  527 ? 2.8040 3.7265 3.4847 0.5196  -0.2691 0.0247  527  THR E OG1 
15526 C  CG2 . THR E  527 ? 2.7551 3.6702 3.4211 0.5048  -0.2403 0.0227  527  THR E CG2 
15527 N  N   . ILE E  528 ? 2.6099 3.4081 3.1679 0.4593  -0.2519 -0.0442 528  ILE E N   
15528 C  CA  . ILE E  528 ? 2.5810 3.3576 3.1212 0.4376  -0.2437 -0.0533 528  ILE E CA  
15529 C  C   . ILE E  528 ? 2.5928 3.3584 3.1337 0.4661  -0.2188 -0.0477 528  ILE E C   
15530 O  O   . ILE E  528 ? 2.5432 3.2972 3.0768 0.5048  -0.2094 -0.0505 528  ILE E O   
15531 C  CB  . ILE E  528 ? 2.5574 3.2842 3.0510 0.4246  -0.2495 -0.0829 528  ILE E CB  
15532 C  CG1 . ILE E  528 ? 2.5354 3.2160 2.9988 0.4588  -0.2370 -0.1003 528  ILE E CG1 
15533 C  CG2 . ILE E  528 ? 2.6174 3.3571 3.1056 0.4069  -0.2714 -0.0873 528  ILE E CG2 
15534 C  CD1 . ILE E  528 ? 2.5355 3.1703 2.9574 0.4488  -0.2397 -0.1262 528  ILE E CD1 
15535 N  N   . SER E  529 ? 2.6027 3.3709 3.1515 0.4471  -0.2092 -0.0396 529  SER E N   
15536 C  CA  . SER E  529 ? 2.6584 3.4211 3.2086 0.4713  -0.1839 -0.0295 529  SER E CA  
15537 C  C   . SER E  529 ? 2.6464 3.3522 3.1547 0.4691  -0.1761 -0.0522 529  SER E C   
15538 O  O   . SER E  529 ? 2.6721 3.3570 3.1695 0.4350  -0.1863 -0.0641 529  SER E O   
15539 C  CB  . SER E  529 ? 2.8097 3.6200 3.4072 0.4523  -0.1768 0.0027  529  SER E CB  
15540 O  OG  . SER E  529 ? 2.8497 3.6483 3.4494 0.4073  -0.1886 -0.0018 529  SER E OG  
15541 N  N   . ARG E  530 ? 2.8438 3.5237 3.3270 0.5065  -0.1591 -0.0591 530  ARG E N   
15542 C  CA  . ARG E  530 ? 2.9543 3.5829 3.4001 0.5063  -0.1513 -0.0776 530  ARG E CA  
15543 C  C   . ARG E  530 ? 2.9875 3.6228 3.4517 0.4894  -0.1365 -0.0583 530  ARG E C   
15544 O  O   . ARG E  530 ? 3.0355 3.7149 3.5366 0.4933  -0.1253 -0.0289 530  ARG E O   
15545 C  CB  . ARG E  530 ? 3.0042 3.6042 3.4168 0.5510  -0.1401 -0.0903 530  ARG E CB  
15546 C  CG  . ARG E  530 ? 3.0423 3.6483 3.4536 0.5769  -0.1146 -0.0735 530  ARG E CG  
15547 C  CD  . ARG E  530 ? 3.0194 3.5991 3.3935 0.6229  -0.1074 -0.0886 530  ARG E CD  
15548 N  NE  . ARG E  530 ? 3.0595 3.6371 3.4209 0.6450  -0.0829 -0.0755 530  ARG E NE  
15549 C  CZ  . ARG E  530 ? 3.0497 3.6674 3.4297 0.6670  -0.0630 -0.0489 530  ARG E CZ  
15550 N  NH1 . ARG E  530 ? 3.0012 3.6651 3.4166 0.6699  -0.0644 -0.0323 530  ARG E NH1 
15551 N  NH2 . ARG E  530 ? 3.1037 3.7185 3.4686 0.6867  -0.0404 -0.0360 530  ARG E NH2 
15552 N  N   . GLY E  531 ? 3.0502 3.6429 3.4925 0.4696  -0.1369 -0.0729 531  GLY E N   
15553 C  CA  . GLY E  531 ? 3.2167 3.8069 3.6762 0.4553  -0.1227 -0.0546 531  GLY E CA  
15554 C  C   . GLY E  531 ? 3.3635 3.9783 3.8643 0.4100  -0.1350 -0.0392 531  GLY E C   
15555 O  O   . GLY E  531 ? 3.5700 4.1636 4.0794 0.3871  -0.1315 -0.0340 531  GLY E O   
15556 N  N   . GLY E  532 ? 3.1588 3.8174 3.6876 0.3960  -0.1511 -0.0310 532  GLY E N   
15557 C  CA  . GLY E  532 ? 3.1709 3.8595 3.7432 0.3535  -0.1651 -0.0136 532  GLY E CA  
15558 C  C   . GLY E  532 ? 3.3197 3.9680 3.8718 0.3138  -0.1873 -0.0406 532  GLY E C   
15559 O  O   . GLY E  532 ? 3.4519 4.0671 4.0049 0.2937  -0.1849 -0.0425 532  GLY E O   
15560 N  N   . LEU E  533 ? 3.3218 3.9714 3.8540 0.3042  -0.2085 -0.0616 533  LEU E N   
15561 C  CA  . LEU E  533 ? 3.2949 3.9095 3.7996 0.2714  -0.2299 -0.0904 533  LEU E CA  
15562 C  C   . LEU E  533 ? 3.1363 3.7454 3.6032 0.2850  -0.2401 -0.1135 533  LEU E C   
15563 O  O   . LEU E  533 ? 3.1746 3.8115 3.6474 0.3122  -0.2354 -0.1039 533  LEU E O   
15564 C  CB  . LEU E  533 ? 3.3375 3.9825 3.8784 0.2267  -0.2540 -0.0801 533  LEU E CB  
15565 C  CG  . LEU E  533 ? 3.3431 4.0071 3.9376 0.2019  -0.2523 -0.0508 533  LEU E CG  
15566 C  CD1 . LEU E  533 ? 3.2906 3.9944 3.9196 0.1600  -0.2830 -0.0426 533  LEU E CD1 
15567 C  CD2 . LEU E  533 ? 3.4315 4.0339 4.0111 0.1897  -0.2454 -0.0637 533  LEU E CD2 
15568 N  N   . MET E  534 ? 2.9485 3.5205 3.3771 0.2672  -0.2535 -0.1434 534  MET E N   
15569 C  CA  . MET E  534 ? 2.9054 3.4769 3.3008 0.2773  -0.2631 -0.1617 534  MET E CA  
15570 C  C   . MET E  534 ? 3.0230 3.6467 3.4393 0.2558  -0.2865 -0.1512 534  MET E C   
15571 O  O   . MET E  534 ? 3.1637 3.7946 3.5872 0.2209  -0.3049 -0.1543 534  MET E O   
15572 C  CB  . MET E  534 ? 2.9325 3.4499 3.2777 0.2698  -0.2663 -0.1957 534  MET E CB  
15573 C  CG  . MET E  534 ? 2.9199 3.4389 3.2317 0.2826  -0.2728 -0.2111 534  MET E CG  
15574 S  SD  . MET E  534 ? 3.0288 3.4924 3.2830 0.2734  -0.2758 -0.2492 534  MET E SD  
15575 C  CE  . MET E  534 ? 3.1122 3.5191 3.3591 0.2924  -0.2506 -0.2546 534  MET E CE  
15576 N  N   . GLN E  535 ? 2.9343 3.5931 3.3607 0.2766  -0.2875 -0.1388 535  GLN E N   
15577 C  CA  . GLN E  535 ? 2.8275 3.5386 3.2739 0.2603  -0.3091 -0.1259 535  GLN E CA  
15578 C  C   . GLN E  535 ? 2.8143 3.5156 3.2187 0.2570  -0.3224 -0.1470 535  GLN E C   
15579 O  O   . GLN E  535 ? 2.7405 3.4232 3.1232 0.2831  -0.3130 -0.1550 535  GLN E O   
15580 C  CB  . GLN E  535 ? 2.6356 3.3927 3.1223 0.2851  -0.3032 -0.0969 535  GLN E CB  
15581 C  CG  . GLN E  535 ? 2.5623 3.3565 3.1008 0.2802  -0.2970 -0.0677 535  GLN E CG  
15582 C  CD  . GLN E  535 ? 2.4780 3.3126 3.0511 0.3118  -0.2878 -0.0419 535  GLN E CD  
15583 O  OE1 . GLN E  535 ? 2.4200 3.2387 2.9757 0.3429  -0.2808 -0.0492 535  GLN E OE1 
15584 N  NE2 . GLN E  535 ? 2.4747 3.3615 3.0990 0.3043  -0.2888 -0.0115 535  GLN E NE2 
15585 N  N   . CYS E  536 ? 3.0943 3.8105 3.4881 0.2252  -0.3449 -0.1548 536  CYS E N   
15586 C  CA  . CYS E  536 ? 3.1142 3.8262 3.4643 0.2204  -0.3574 -0.1739 536  CYS E CA  
15587 C  C   . CYS E  536 ? 2.9499 3.7233 3.3191 0.2044  -0.3809 -0.1555 536  CYS E C   
15588 O  O   . CYS E  536 ? 2.9505 3.7630 3.3629 0.1885  -0.3912 -0.1339 536  CYS E O   
15589 C  CB  . CYS E  536 ? 3.3573 4.0216 3.6627 0.1999  -0.3627 -0.2072 536  CYS E CB  
15590 S  SG  . CYS E  536 ? 3.7398 4.3781 3.9789 0.2098  -0.3631 -0.2366 536  CYS E SG  
15591 N  N   . GLU E  537 ? 2.8966 3.6823 3.2358 0.2093  -0.3891 -0.1610 537  GLU E N   
15592 C  CA  . GLU E  537 ? 2.8585 3.7043 3.2127 0.1965  -0.4113 -0.1414 537  GLU E CA  
15593 C  C   . GLU E  537 ? 2.9773 3.8236 3.2780 0.1911  -0.4226 -0.1591 537  GLU E C   
15594 O  O   . GLU E  537 ? 3.1527 3.9719 3.4228 0.2121  -0.4083 -0.1705 537  GLU E O   
15595 C  CB  . GLU E  537 ? 2.7663 3.6495 3.1651 0.2214  -0.4050 -0.1087 537  GLU E CB  
15596 C  CG  . GLU E  537 ? 2.7265 3.6678 3.1361 0.2151  -0.4251 -0.0870 537  GLU E CG  
15597 C  CD  . GLU E  537 ? 2.7115 3.6857 3.1717 0.2395  -0.4198 -0.0540 537  GLU E CD  
15598 O  OE1 . GLU E  537 ? 2.7179 3.6895 3.2157 0.2517  -0.4076 -0.0429 537  GLU E OE1 
15599 O  OE2 . GLU E  537 ? 2.7218 3.7247 3.1842 0.2476  -0.4278 -0.0383 537  GLU E OE2 
15600 N  N   . GLU E  538 ? 2.9860 3.8659 3.2756 0.1638  -0.4484 -0.1602 538  GLU E N   
15601 C  CA  . GLU E  538 ? 3.0037 3.8910 3.2379 0.1584  -0.4608 -0.1765 538  GLU E CA  
15602 C  C   . GLU E  538 ? 3.0511 4.0052 3.3021 0.1619  -0.4743 -0.1450 538  GLU E C   
15603 O  O   . GLU E  538 ? 2.9886 3.9876 3.2928 0.1571  -0.4836 -0.1144 538  GLU E O   
15604 C  CB  . GLU E  538 ? 3.0877 3.9600 3.2865 0.1259  -0.4830 -0.2054 538  GLU E CB  
15605 C  CG  . GLU E  538 ? 3.1927 4.0554 3.3184 0.1245  -0.4914 -0.2338 538  GLU E CG  
15606 C  CD  . GLU E  538 ? 3.3210 4.1730 3.4142 0.0911  -0.5200 -0.2622 538  GLU E CD  
15607 O  OE1 . GLU E  538 ? 3.3365 4.1875 3.4697 0.0667  -0.5333 -0.2580 538  GLU E OE1 
15608 O  OE2 . GLU E  538 ? 3.4337 4.2783 3.4617 0.0896  -0.5297 -0.2887 538  GLU E OE2 
15609 N  N   . LEU E  539 ? 3.1334 4.0956 3.3402 0.1718  -0.4741 -0.1504 539  LEU E N   
15610 C  CA  . LEU E  539 ? 3.1216 4.1460 3.3385 0.1760  -0.4861 -0.1194 539  LEU E CA  
15611 C  C   . LEU E  539 ? 3.1080 4.1346 3.2566 0.1782  -0.4888 -0.1372 539  LEU E C   
15612 O  O   . LEU E  539 ? 3.1124 4.0896 3.2163 0.1871  -0.4735 -0.1678 539  LEU E O   
15613 C  CB  . LEU E  539 ? 2.9758 4.0121 3.2419 0.2038  -0.4698 -0.0869 539  LEU E CB  
15614 C  CG  . LEU E  539 ? 2.9713 4.0737 3.2790 0.2067  -0.4835 -0.0444 539  LEU E CG  
15615 C  CD1 . LEU E  539 ? 2.9762 4.1169 3.3249 0.1859  -0.5029 -0.0286 539  LEU E CD1 
15616 C  CD2 . LEU E  539 ? 2.9171 4.0132 3.2697 0.2360  -0.4667 -0.0200 539  LEU E CD2 
15617 N  N   . ILE E  540 ? 2.9669 4.0535 3.1073 0.1719  -0.5075 -0.1164 540  ILE E N   
15618 C  CA  . ILE E  540 ? 2.8807 3.9813 2.9525 0.1733  -0.5129 -0.1305 540  ILE E CA  
15619 C  C   . ILE E  540 ? 2.8380 3.9739 2.9186 0.1982  -0.4998 -0.0969 540  ILE E C   
15620 O  O   . ILE E  540 ? 2.7921 3.9741 2.9259 0.2019  -0.5059 -0.0558 540  ILE E O   
15621 C  CB  . ILE E  540 ? 2.8995 4.0437 2.9455 0.1462  -0.5466 -0.1341 540  ILE E CB  
15622 C  CG1 . ILE E  540 ? 2.9634 4.0683 3.0011 0.1186  -0.5622 -0.1690 540  ILE E CG1 
15623 C  CG2 . ILE E  540 ? 2.9383 4.1038 2.9099 0.1529  -0.5509 -0.1455 540  ILE E CG2 
15624 C  CD1 . ILE E  540 ? 2.9982 4.1416 3.0101 0.0891  -0.6000 -0.1764 540  ILE E CD1 
15625 N  N   . ALA E  541 ? 2.9068 4.0210 2.9387 0.2158  -0.4817 -0.1128 541  ALA E N   
15626 C  CA  . ALA E  541 ? 2.8759 4.0259 2.9079 0.2375  -0.4698 -0.0821 541  ALA E CA  
15627 C  C   . ALA E  541 ? 2.9657 4.1399 2.9195 0.2384  -0.4742 -0.0970 541  ALA E C   
15628 O  O   . ALA E  541 ? 3.0563 4.1958 2.9507 0.2298  -0.4781 -0.1410 541  ALA E O   
15629 C  CB  . ALA E  541 ? 2.8591 3.9659 2.9107 0.2619  -0.4409 -0.0818 541  ALA E CB  
15630 N  N   . TYR E  542 ? 2.9330 4.1667 2.8858 0.2501  -0.4737 -0.0601 542  TYR E N   
15631 C  CA  . TYR E  542 ? 2.9821 4.2477 2.8586 0.2554  -0.4760 -0.0695 542  TYR E CA  
15632 C  C   . TYR E  542 ? 2.8980 4.1863 2.7702 0.2833  -0.4507 -0.0421 542  TYR E C   
15633 O  O   . TYR E  542 ? 2.7942 4.0888 2.7312 0.2949  -0.4385 -0.0057 542  TYR E O   
15634 C  CB  . TYR E  542 ? 3.0241 4.3580 2.8898 0.2389  -0.5061 -0.0488 542  TYR E CB  
15635 C  CG  . TYR E  542 ? 2.9627 4.3619 2.8882 0.2461  -0.5086 0.0133  542  TYR E CG  
15636 C  CD1 . TYR E  542 ? 2.9672 4.3726 2.9753 0.2379  -0.5174 0.0420  542  TYR E CD1 
15637 C  CD2 . TYR E  542 ? 2.8439 4.2989 2.7443 0.2628  -0.5013 0.0449  542  TYR E CD2 
15638 C  CE1 . TYR E  542 ? 2.8040 4.2645 2.8686 0.2456  -0.5205 0.0984  542  TYR E CE1 
15639 C  CE2 . TYR E  542 ? 2.7282 4.2412 2.6872 0.2687  -0.5043 0.1044  542  TYR E CE2 
15640 C  CZ  . TYR E  542 ? 2.6499 4.1628 2.6913 0.2599  -0.5147 0.1299  542  TYR E CZ  
15641 O  OH  . TYR E  542 ? 2.5697 4.1357 2.6712 0.2669  -0.5184 0.1888  542  TYR E OH  
15642 N  N   . LEU E  543 ? 2.9862 4.2858 2.7800 0.2945  -0.4434 -0.0614 543  LEU E N   
15643 C  CA  . LEU E  543 ? 3.0210 4.3537 2.7998 0.3213  -0.4193 -0.0347 543  LEU E CA  
15644 C  C   . LEU E  543 ? 3.0738 4.4937 2.8506 0.3229  -0.4313 0.0127  543  LEU E C   
15645 O  O   . LEU E  543 ? 3.1142 4.5662 2.8614 0.3062  -0.4578 0.0076  543  LEU E O   
15646 C  CB  . LEU E  543 ? 3.2104 4.5122 2.9023 0.3368  -0.4025 -0.0800 543  LEU E CB  
15647 C  CG  . LEU E  543 ? 3.3865 4.7254 3.0489 0.3672  -0.3750 -0.0577 543  LEU E CG  
15648 C  CD1 . LEU E  543 ? 3.3311 4.6540 3.0652 0.3821  -0.3501 -0.0278 543  LEU E CD1 
15649 C  CD2 . LEU E  543 ? 3.5029 4.8129 3.0676 0.3820  -0.3632 -0.1093 543  LEU E CD2 
15650 N  N   . ARG E  544 ? 3.0557 4.5156 2.8650 0.3428  -0.4122 0.0605  544  ARG E N   
15651 C  CA  . ARG E  544 ? 3.1541 4.6997 2.9593 0.3489  -0.4181 0.1107  544  ARG E CA  
15652 C  C   . ARG E  544 ? 3.2577 4.8364 2.9609 0.3629  -0.4120 0.0917  544  ARG E C   
15653 O  O   . ARG E  544 ? 3.4175 4.9542 3.0605 0.3758  -0.3947 0.0476  544  ARG E O   
15654 C  CB  . ARG E  544 ? 2.9917 4.5675 2.8704 0.3649  -0.3995 0.1709  544  ARG E CB  
15655 C  CG  . ARG E  544 ? 2.8095 4.3726 2.7904 0.3535  -0.4109 0.2026  544  ARG E CG  
15656 C  CD  . ARG E  544 ? 2.7513 4.3602 2.7986 0.3672  -0.4002 0.2691  544  ARG E CD  
15657 N  NE  . ARG E  544 ? 2.7607 4.3614 2.9028 0.3583  -0.4141 0.3016  544  ARG E NE  
15658 C  CZ  . ARG E  544 ? 2.8816 4.4185 3.0775 0.3573  -0.4107 0.2867  544  ARG E CZ  
15659 N  NH1 . ARG E  544 ? 2.9480 4.4248 3.1158 0.3630  -0.3944 0.2418  544  ARG E NH1 
15660 N  NH2 . ARG E  544 ? 2.8430 4.3760 3.1195 0.3524  -0.4241 0.3165  544  ARG E NH2 
15661 N  N   . ASP E  545 ? 3.0794 4.7345 2.7617 0.3619  -0.4271 0.1254  545  ASP E N   
15662 C  CA  . ASP E  545 ? 3.0902 4.7903 2.6739 0.3777  -0.4236 0.1147  545  ASP E CA  
15663 C  C   . ASP E  545 ? 3.2272 4.9412 2.7896 0.4109  -0.3848 0.1300  545  ASP E C   
15664 O  O   . ASP E  545 ? 3.1770 4.8897 2.8136 0.4202  -0.3641 0.1683  545  ASP E O   
15665 C  CB  . ASP E  545 ? 3.0493 4.8372 2.6307 0.3717  -0.4462 0.1611  545  ASP E CB  
15666 C  CG  . ASP E  545 ? 3.2029 5.0400 2.6743 0.3882  -0.4462 0.1476  545  ASP E CG  
15667 O  OD1 . ASP E  545 ? 3.3345 5.1521 2.7332 0.3754  -0.4707 0.0953  545  ASP E OD1 
15668 O  OD2 . ASP E  545 ? 3.2096 5.1054 2.6675 0.4144  -0.4224 0.1895  545  ASP E OD2 
15669 N  N   . GLU E  546 ? 3.3681 5.0961 2.8264 0.4294  -0.3761 0.0985  546  GLU E N   
15670 C  CA  . GLU E  546 ? 3.3670 5.1157 2.7914 0.4646  -0.3379 0.1101  546  GLU E CA  
15671 C  C   . GLU E  546 ? 3.2577 5.0956 2.7326 0.4793  -0.3231 0.1929  546  GLU E C   
15672 O  O   . GLU E  546 ? 3.2650 5.1100 2.7833 0.4983  -0.2925 0.2248  546  GLU E O   
15673 C  CB  . GLU E  546 ? 3.3926 5.1447 2.6878 0.4828  -0.3356 0.0594  546  GLU E CB  
15674 C  CG  . GLU E  546 ? 3.2907 5.0647 2.5385 0.5235  -0.2940 0.0654  546  GLU E CG  
15675 C  CD  . GLU E  546 ? 3.2637 5.0330 2.3778 0.5440  -0.2930 0.0082  546  GLU E CD  
15676 O  OE1 . GLU E  546 ? 3.3453 5.0937 2.4037 0.5241  -0.3279 -0.0365 546  GLU E OE1 
15677 O  OE2 . GLU E  546 ? 3.2524 5.0393 2.3179 0.5809  -0.2578 0.0081  546  GLU E OE2 
15678 N  N   . SER E  547 ? 2.9469 4.8554 2.4212 0.4704  -0.3454 0.2314  547  SER E N   
15679 C  CA  . SER E  547 ? 2.9177 4.9160 2.4332 0.4856  -0.3315 0.3124  547  SER E CA  
15680 C  C   . SER E  547 ? 2.8191 4.8124 2.4663 0.4739  -0.3298 0.3680  547  SER E C   
15681 O  O   . SER E  547 ? 2.8020 4.8601 2.4987 0.4863  -0.3155 0.4380  547  SER E O   
15682 C  CB  . SER E  547 ? 2.9697 5.0462 2.4430 0.4802  -0.3573 0.3381  547  SER E CB  
15683 O  OG  . SER E  547 ? 3.0724 5.1653 2.4183 0.4963  -0.3576 0.2935  547  SER E OG  
15684 N  N   . GLU E  548 ? 2.9375 4.8558 2.6419 0.4513  -0.3444 0.3393  548  GLU E N   
15685 C  CA  . GLU E  548 ? 2.9109 4.8155 2.7353 0.4407  -0.3467 0.3841  548  GLU E CA  
15686 C  C   . GLU E  548 ? 2.9092 4.7740 2.7799 0.4546  -0.3177 0.3881  548  GLU E C   
15687 O  O   . GLU E  548 ? 2.8327 4.6945 2.8020 0.4501  -0.3174 0.4324  548  GLU E O   
15688 C  CB  . GLU E  548 ? 2.8277 4.6749 2.6911 0.4124  -0.3759 0.3532  548  GLU E CB  
15689 C  CG  . GLU E  548 ? 2.7425 4.6334 2.5811 0.3955  -0.4081 0.3583  548  GLU E CG  
15690 C  CD  . GLU E  548 ? 2.6121 4.4571 2.5068 0.3695  -0.4345 0.3411  548  GLU E CD  
15691 O  OE1 . GLU E  548 ? 2.6856 4.5696 2.5823 0.3545  -0.4620 0.3552  548  GLU E OE1 
15692 O  OE2 . GLU E  548 ? 2.5769 4.3500 2.5138 0.3654  -0.4272 0.3150  548  GLU E OE2 
15693 N  N   . PHE E  549 ? 3.0381 4.8703 2.8420 0.4714  -0.2951 0.3423  549  PHE E N   
15694 C  CA  . PHE E  549 ? 3.0328 4.8310 2.8781 0.4857  -0.2676 0.3460  549  PHE E CA  
15695 C  C   . PHE E  549 ? 3.0919 4.8908 2.8451 0.5126  -0.2393 0.3113  549  PHE E C   
15696 O  O   . PHE E  549 ? 3.2289 4.9881 2.8972 0.5117  -0.2452 0.2471  549  PHE E O   
15697 C  CB  . PHE E  549 ? 2.9404 4.6472 2.8375 0.4683  -0.2777 0.3079  549  PHE E CB  
15698 C  CG  . PHE E  549 ? 3.0005 4.6411 2.8251 0.4599  -0.2863 0.2303  549  PHE E CG  
15699 C  CD1 . PHE E  549 ? 3.0619 4.6951 2.8653 0.4374  -0.3165 0.2069  549  PHE E CD1 
15700 C  CD2 . PHE E  549 ? 3.0632 4.6492 2.8463 0.4739  -0.2650 0.1833  549  PHE E CD2 
15701 C  CE1 . PHE E  549 ? 3.2212 4.7934 2.9649 0.4272  -0.3263 0.1386  549  PHE E CE1 
15702 C  CE2 . PHE E  549 ? 3.2125 4.7346 2.9334 0.4652  -0.2740 0.1140  549  PHE E CE2 
15703 C  CZ  . PHE E  549 ? 3.2952 4.8100 2.9976 0.4408  -0.3052 0.0920  549  PHE E CZ  
15704 N  N   . ARG E  550 ? 2.9680 4.8143 2.7385 0.5371  -0.2093 0.3554  550  ARG E N   
15705 C  CA  . ARG E  550 ? 3.0062 4.8559 2.6967 0.5677  -0.1777 0.3274  550  ARG E CA  
15706 C  C   . ARG E  550 ? 3.1025 4.8685 2.8048 0.5717  -0.1634 0.2814  550  ARG E C   
15707 O  O   . ARG E  550 ? 3.1674 4.9204 2.7994 0.5967  -0.1388 0.2464  550  ARG E O   
15708 C  CB  . ARG E  550 ? 2.9099 4.8517 2.6171 0.5942  -0.1488 0.3979  550  ARG E CB  
15709 C  CG  . ARG E  550 ? 2.7958 4.7592 2.6313 0.5863  -0.1459 0.4689  550  ARG E CG  
15710 C  CD  . ARG E  550 ? 2.7252 4.7856 2.5758 0.6122  -0.1167 0.5416  550  ARG E CD  
15711 N  NE  . ARG E  550 ? 2.6566 4.7303 2.6322 0.6054  -0.1123 0.6058  550  ARG E NE  
15712 C  CZ  . ARG E  550 ? 2.6218 4.7407 2.6817 0.5900  -0.1285 0.6739  550  ARG E CZ  
15713 N  NH1 . ARG E  550 ? 2.6459 4.8061 2.6792 0.5809  -0.1485 0.6895  550  ARG E NH1 
15714 N  NH2 . ARG E  550 ? 2.5658 4.6880 2.7385 0.5837  -0.1261 0.7269  550  ARG E NH2 
15715 N  N   . ASP E  551 ? 3.1259 4.8358 2.9130 0.5499  -0.1780 0.2807  551  ASP E N   
15716 C  CA  . ASP E  551 ? 3.0909 4.7250 2.9010 0.5527  -0.1662 0.2449  551  ASP E CA  
15717 C  C   . ASP E  551 ? 3.1898 4.7458 2.9327 0.5421  -0.1793 0.1658  551  ASP E C   
15718 O  O   . ASP E  551 ? 3.1215 4.6283 2.8974 0.5163  -0.2045 0.1454  551  ASP E O   
15719 C  CB  . ASP E  551 ? 2.9445 4.5551 2.8708 0.5351  -0.1784 0.2793  551  ASP E CB  
15720 C  CG  . ASP E  551 ? 2.9617 4.5149 2.9215 0.5436  -0.1621 0.2604  551  ASP E CG  
15721 O  OD1 . ASP E  551 ? 3.0281 4.5393 2.9226 0.5571  -0.1466 0.2083  551  ASP E OD1 
15722 O  OD2 . ASP E  551 ? 2.9526 4.5010 3.0058 0.5366  -0.1666 0.2976  551  ASP E OD2 
15723 N  N   . LYS E  552 ? 3.3044 4.8476 2.9537 0.5632  -0.1616 0.1213  552  LYS E N   
15724 C  CA  . LYS E  552 ? 3.3523 4.8180 2.9360 0.5548  -0.1727 0.0456  552  LYS E CA  
15725 C  C   . LYS E  552 ? 3.3421 4.7424 2.9219 0.5708  -0.1495 0.0098  552  LYS E C   
15726 O  O   . LYS E  552 ? 3.3997 4.7372 2.9161 0.5713  -0.1515 -0.0527 552  LYS E O   
15727 C  CB  . LYS E  552 ? 3.3433 4.8319 2.8151 0.5647  -0.1768 0.0119  552  LYS E CB  
15728 C  CG  . LYS E  552 ? 3.2689 4.8046 2.7312 0.5431  -0.2083 0.0294  552  LYS E CG  
15729 C  CD  . LYS E  552 ? 3.2196 4.8572 2.6813 0.5610  -0.1962 0.0933  552  LYS E CD  
15730 C  CE  . LYS E  552 ? 3.2545 4.9411 2.6791 0.5455  -0.2260 0.1016  552  LYS E CE  
15731 N  NZ  . LYS E  552 ? 3.2714 5.0615 2.6945 0.5636  -0.2141 0.1679  552  LYS E NZ  
15732 N  N   . LEU E  553 ? 3.2108 4.6236 2.8613 0.5826  -0.1294 0.0496  553  LEU E N   
15733 C  CA  . LEU E  553 ? 3.2304 4.5911 2.8839 0.6001  -0.1062 0.0240  553  LEU E CA  
15734 C  C   . LEU E  553 ? 3.0578 4.3580 2.7927 0.5804  -0.1185 0.0210  553  LEU E C   
15735 O  O   . LEU E  553 ? 3.0562 4.2928 2.7814 0.5873  -0.1085 -0.0172 553  LEU E O   
15736 C  CB  . LEU E  553 ? 3.2416 4.6634 2.9108 0.6322  -0.0718 0.0697  553  LEU E CB  
15737 C  CG  . LEU E  553 ? 3.1170 4.6099 2.7076 0.6605  -0.0514 0.0812  553  LEU E CG  
15738 C  CD1 . LEU E  553 ? 3.2127 4.6637 2.6882 0.6666  -0.0565 0.0101  553  LEU E CD1 
15739 C  CD2 . LEU E  553 ? 2.9435 4.5229 2.5628 0.6518  -0.0624 0.1431  553  LEU E CD2 
15740 N  N   . THR E  554 ? 2.9212 4.2391 2.7336 0.5581  -0.1398 0.0601  554  THR E N   
15741 C  CA  . THR E  554 ? 2.8386 4.1047 2.7290 0.5419  -0.1525 0.0611  554  THR E CA  
15742 C  C   . THR E  554 ? 2.9267 4.1216 2.7906 0.5214  -0.1728 0.0062  554  THR E C   
15743 O  O   . THR E  554 ? 3.0213 4.2261 2.8829 0.5006  -0.1967 0.0059  554  THR E O   
15744 C  CB  . THR E  554 ? 2.7567 4.0655 2.7352 0.5275  -0.1692 0.1206  554  THR E CB  
15745 O  OG1 . THR E  554 ? 2.7262 4.1032 2.7347 0.5452  -0.1503 0.1759  554  THR E OG1 
15746 C  CG2 . THR E  554 ? 2.6781 3.9310 2.7317 0.5142  -0.1827 0.1183  554  THR E CG2 
15747 N  N   . PRO E  555 ? 2.8066 3.9334 2.6492 0.5271  -0.1635 -0.0388 555  PRO E N   
15748 C  CA  . PRO E  555 ? 2.8224 3.8832 2.6424 0.5073  -0.1815 -0.0880 555  PRO E CA  
15749 C  C   . PRO E  555 ? 2.7424 3.7961 2.6293 0.4820  -0.2076 -0.0701 555  PRO E C   
15750 O  O   . PRO E  555 ? 2.6243 3.6842 2.5845 0.4820  -0.2093 -0.0360 555  PRO E O   
15751 C  CB  . PRO E  555 ? 2.8218 3.8175 2.6357 0.5206  -0.1641 -0.1213 555  PRO E CB  
15752 C  CG  . PRO E  555 ? 2.7857 3.8106 2.6537 0.5390  -0.1461 -0.0800 555  PRO E CG  
15753 C  CD  . PRO E  555 ? 2.7923 3.8995 2.6517 0.5493  -0.1384 -0.0381 555  PRO E CD  
15754 N  N   . ILE E  556 ? 2.8508 3.8904 2.7124 0.4610  -0.2289 -0.0944 556  ILE E N   
15755 C  CA  . ILE E  556 ? 2.7983 3.8387 2.7170 0.4387  -0.2533 -0.0774 556  ILE E CA  
15756 C  C   . ILE E  556 ? 2.7702 3.7382 2.7099 0.4311  -0.2562 -0.1091 556  ILE E C   
15757 O  O   . ILE E  556 ? 2.7825 3.7083 2.6797 0.4216  -0.2608 -0.1514 556  ILE E O   
15758 C  CB  . ILE E  556 ? 2.8348 3.9072 2.7218 0.4201  -0.2753 -0.0808 556  ILE E CB  
15759 C  CG1 . ILE E  556 ? 2.9752 4.1224 2.8342 0.4305  -0.2709 -0.0487 556  ILE E CG1 
15760 C  CG2 . ILE E  556 ? 2.6865 3.7614 2.6376 0.3999  -0.2984 -0.0608 556  ILE E CG2 
15761 C  CD1 . ILE E  556 ? 3.1116 4.2983 2.9394 0.4131  -0.2946 -0.0476 556  ILE E CD1 
15762 N  N   . THR E  557 ? 2.8780 3.8314 2.8833 0.4358  -0.2543 -0.0878 557  THR E N   
15763 C  CA  . THR E  557 ? 2.9356 3.8258 2.9637 0.4319  -0.2562 -0.1124 557  THR E CA  
15764 C  C   . THR E  557 ? 2.8709 3.7609 2.9367 0.4126  -0.2788 -0.1052 557  THR E C   
15765 O  O   . THR E  557 ? 2.6987 3.6238 2.8159 0.4103  -0.2899 -0.0677 557  THR E O   
15766 C  CB  . THR E  557 ? 2.9125 3.7869 2.9885 0.4481  -0.2449 -0.0955 557  THR E CB  
15767 O  OG1 . THR E  557 ? 2.8317 3.7054 2.8729 0.4671  -0.2221 -0.1037 557  THR E OG1 
15768 C  CG2 . THR E  557 ? 2.9580 3.7717 3.0574 0.4453  -0.2487 -0.1178 557  THR E CG2 
15769 N  N   . ILE E  558 ? 2.9748 3.8258 3.0180 0.3995  -0.2854 -0.1393 558  ILE E N   
15770 C  CA  . ILE E  558 ? 2.9588 3.8063 3.0395 0.3834  -0.3036 -0.1342 558  ILE E CA  
15771 C  C   . ILE E  558 ? 3.0067 3.8104 3.1315 0.3925  -0.2987 -0.1357 558  ILE E C   
15772 O  O   . ILE E  558 ? 3.0362 3.7904 3.1411 0.3980  -0.2870 -0.1643 558  ILE E O   
15773 C  CB  . ILE E  558 ? 3.0002 3.8307 3.0417 0.3637  -0.3138 -0.1662 558  ILE E CB  
15774 C  CG1 . ILE E  558 ? 2.9451 3.8216 2.9417 0.3537  -0.3242 -0.1652 558  ILE E CG1 
15775 C  CG2 . ILE E  558 ? 3.0401 3.8637 3.1266 0.3503  -0.3282 -0.1601 558  ILE E CG2 
15776 C  CD1 . ILE E  558 ? 3.0147 3.8797 2.9423 0.3641  -0.3101 -0.1923 558  ILE E CD1 
15777 N  N   . PHE E  559 ? 3.0334 3.8538 3.2163 0.3951  -0.3085 -0.1056 559  PHE E N   
15778 C  CA  . PHE E  559 ? 2.9929 3.7745 3.2160 0.4063  -0.3066 -0.1063 559  PHE E CA  
15779 C  C   . PHE E  559 ? 3.0250 3.7958 3.2728 0.3976  -0.3182 -0.1095 559  PHE E C   
15780 O  O   . PHE E  559 ? 3.2341 4.0422 3.5037 0.3879  -0.3324 -0.0891 559  PHE E O   
15781 C  CB  . PHE E  559 ? 2.8702 3.6704 3.1429 0.4188  -0.3099 -0.0725 559  PHE E CB  
15782 C  CG  . PHE E  559 ? 2.7835 3.5439 3.0964 0.4304  -0.3129 -0.0746 559  PHE E CG  
15783 C  CD1 . PHE E  559 ? 2.8182 3.5357 3.1187 0.4425  -0.3007 -0.0954 559  PHE E CD1 
15784 C  CD2 . PHE E  559 ? 2.7250 3.4907 3.0859 0.4311  -0.3285 -0.0565 559  PHE E CD2 
15785 C  CE1 . PHE E  559 ? 2.8515 3.5334 3.1836 0.4542  -0.3054 -0.0989 559  PHE E CE1 
15786 C  CE2 . PHE E  559 ? 2.7223 3.4494 3.1137 0.4443  -0.3324 -0.0620 559  PHE E CE2 
15787 C  CZ  . PHE E  559 ? 2.8188 3.5045 3.1940 0.4554  -0.3215 -0.0836 559  PHE E CZ  
15788 N  N   . MET E  560 ? 2.8278 3.5507 3.0728 0.4025  -0.3112 -0.1329 560  MET E N   
15789 C  CA  . MET E  560 ? 2.7966 3.5079 3.0652 0.3986  -0.3178 -0.1355 560  MET E CA  
15790 C  C   . MET E  560 ? 2.7278 3.4057 3.0280 0.4184  -0.3149 -0.1346 560  MET E C   
15791 O  O   . MET E  560 ? 2.8592 3.4997 3.1431 0.4295  -0.3032 -0.1515 560  MET E O   
15792 C  CB  . MET E  560 ? 2.9046 3.5913 3.1386 0.3853  -0.3125 -0.1637 560  MET E CB  
15793 C  CG  . MET E  560 ? 2.9626 3.6353 3.2228 0.3848  -0.3144 -0.1649 560  MET E CG  
15794 S  SD  . MET E  560 ? 3.2363 3.8777 3.4639 0.3679  -0.3079 -0.1936 560  MET E SD  
15795 C  CE  . MET E  560 ? 3.1088 3.7373 3.3763 0.3776  -0.3044 -0.1861 560  MET E CE  
15796 N  N   . GLU E  561 ? 2.5565 3.2470 2.8998 0.4241  -0.3261 -0.1157 561  GLU E N   
15797 C  CA  . GLU E  561 ? 2.4745 3.1338 2.8465 0.4446  -0.3271 -0.1161 561  GLU E CA  
15798 C  C   . GLU E  561 ? 2.4732 3.1274 2.8603 0.4477  -0.3286 -0.1188 561  GLU E C   
15799 O  O   . GLU E  561 ? 2.6454 3.3339 3.0459 0.4360  -0.3359 -0.1056 561  GLU E O   
15800 C  CB  . GLU E  561 ? 2.4114 3.0869 2.8253 0.4536  -0.3403 -0.0898 561  GLU E CB  
15801 C  CG  . GLU E  561 ? 2.3618 3.0028 2.8057 0.4750  -0.3466 -0.0918 561  GLU E CG  
15802 C  CD  . GLU E  561 ? 2.3840 3.0400 2.8751 0.4805  -0.3635 -0.0644 561  GLU E CD  
15803 O  OE1 . GLU E  561 ? 2.3182 3.0169 2.8218 0.4678  -0.3691 -0.0398 561  GLU E OE1 
15804 O  OE2 . GLU E  561 ? 2.5610 3.1857 3.0766 0.4972  -0.3723 -0.0669 561  GLU E OE2 
15805 N  N   . TYR E  562 ? 2.3848 2.9999 2.7702 0.4647  -0.3213 -0.1341 562  TYR E N   
15806 C  CA  . TYR E  562 ? 2.4523 3.0648 2.8506 0.4719  -0.3192 -0.1353 562  TYR E CA  
15807 C  C   . TYR E  562 ? 2.5242 3.1039 2.9372 0.5001  -0.3201 -0.1405 562  TYR E C   
15808 O  O   . TYR E  562 ? 2.7036 3.2514 3.1046 0.5114  -0.3183 -0.1523 562  TYR E O   
15809 C  CB  . TYR E  562 ? 2.4510 3.0526 2.8199 0.4601  -0.3055 -0.1518 562  TYR E CB  
15810 C  CG  . TYR E  562 ? 2.4806 3.0399 2.8162 0.4661  -0.2924 -0.1738 562  TYR E CG  
15811 C  CD1 . TYR E  562 ? 2.5501 3.0755 2.8825 0.4873  -0.2836 -0.1841 562  TYR E CD1 
15812 C  CD2 . TYR E  562 ? 2.5208 3.0752 2.8264 0.4527  -0.2883 -0.1840 562  TYR E CD2 
15813 C  CE1 . TYR E  562 ? 2.6104 3.0993 2.9140 0.4933  -0.2721 -0.2017 562  TYR E CE1 
15814 C  CE2 . TYR E  562 ? 2.6334 3.1496 2.9110 0.4598  -0.2757 -0.2026 562  TYR E CE2 
15815 C  CZ  . TYR E  562 ? 2.7098 3.1940 2.9882 0.4792  -0.2681 -0.2103 562  TYR E CZ  
15816 O  OH  . TYR E  562 ? 2.8925 3.3407 3.1446 0.4867  -0.2560 -0.2265 562  TYR E OH  
15817 N  N   . ARG E  563 ? 2.3374 2.9261 2.7757 0.5127  -0.3236 -0.1321 563  ARG E N   
15818 C  CA  . ARG E  563 ? 2.2763 2.8347 2.7254 0.5427  -0.3260 -0.1390 563  ARG E CA  
15819 C  C   . ARG E  563 ? 2.2812 2.8495 2.7371 0.5546  -0.3170 -0.1371 563  ARG E C   
15820 O  O   . ARG E  563 ? 2.3043 2.9066 2.7661 0.5375  -0.3121 -0.1262 563  ARG E O   
15821 C  CB  . ARG E  563 ? 2.3212 2.8799 2.8061 0.5535  -0.3457 -0.1257 563  ARG E CB  
15822 C  CG  . ARG E  563 ? 2.4890 3.0458 2.9786 0.5427  -0.3556 -0.1197 563  ARG E CG  
15823 C  CD  . ARG E  563 ? 2.5711 3.1255 3.1043 0.5538  -0.3765 -0.1037 563  ARG E CD  
15824 N  NE  . ARG E  563 ? 2.5621 3.1096 3.1062 0.5479  -0.3865 -0.0968 563  ARG E NE  
15825 C  CZ  . ARG E  563 ? 2.4657 3.0100 3.0521 0.5529  -0.4065 -0.0799 563  ARG E CZ  
15826 N  NH1 . ARG E  563 ? 2.4554 2.9985 3.0742 0.5656  -0.4189 -0.0709 563  ARG E NH1 
15827 N  NH2 . ARG E  563 ? 2.3829 2.9258 2.9822 0.5456  -0.4140 -0.0702 563  ARG E NH2 
15828 N  N   . LEU E  564 ? 2.4232 2.9631 2.8782 0.5851  -0.3154 -0.1474 564  LEU E N   
15829 C  CA  . LEU E  564 ? 2.5039 3.0534 2.9644 0.6038  -0.3045 -0.1448 564  LEU E CA  
15830 C  C   . LEU E  564 ? 2.5652 3.1126 3.0548 0.6311  -0.3166 -0.1388 564  LEU E C   
15831 O  O   . LEU E  564 ? 2.4670 2.9847 2.9624 0.6442  -0.3324 -0.1465 564  LEU E O   
15832 C  CB  . LEU E  564 ? 2.5518 3.0697 2.9775 0.6216  -0.2880 -0.1635 564  LEU E CB  
15833 C  CG  . LEU E  564 ? 2.6437 3.1683 3.0677 0.6477  -0.2724 -0.1618 564  LEU E CG  
15834 C  CD1 . LEU E  564 ? 2.7386 3.3117 3.1858 0.6316  -0.2622 -0.1400 564  LEU E CD1 
15835 C  CD2 . LEU E  564 ? 2.6842 3.1784 3.0700 0.6611  -0.2569 -0.1781 564  LEU E CD2 
15836 N  N   . ASP E  565 ? 2.7789 3.3575 3.2893 0.6400  -0.3096 -0.1244 565  ASP E N   
15837 C  CA  . ASP E  565 ? 2.8564 3.4296 3.3888 0.6741  -0.3153 -0.1220 565  ASP E CA  
15838 C  C   . ASP E  565 ? 2.7916 3.3370 3.2934 0.7081  -0.3002 -0.1410 565  ASP E C   
15839 O  O   . ASP E  565 ? 2.7552 3.3249 3.2528 0.7153  -0.2799 -0.1339 565  ASP E O   
15840 C  CB  . ASP E  565 ? 2.9131 3.5372 3.4838 0.6700  -0.3136 -0.0952 565  ASP E CB  
15841 C  CG  . ASP E  565 ? 3.0398 3.6570 3.6411 0.7018  -0.3251 -0.0899 565  ASP E CG  
15842 O  OD1 . ASP E  565 ? 3.2115 3.7838 3.7974 0.7345  -0.3289 -0.1110 565  ASP E OD1 
15843 O  OD2 . ASP E  565 ? 2.9330 3.5885 3.5732 0.6950  -0.3315 -0.0652 565  ASP E OD2 
15844 N  N   . TYR E  566 ? 2.7231 3.2195 3.2038 0.7289  -0.3106 -0.1639 566  TYR E N   
15845 C  CA  . TYR E  566 ? 2.6910 3.1597 3.1357 0.7629  -0.2982 -0.1838 566  TYR E CA  
15846 C  C   . TYR E  566 ? 2.6437 3.1253 3.0984 0.7999  -0.2897 -0.1796 566  TYR E C   
15847 O  O   . TYR E  566 ? 2.6187 3.1060 3.0490 0.8229  -0.2683 -0.1830 566  TYR E O   
15848 C  CB  . TYR E  566 ? 2.7946 3.2091 3.2182 0.7776  -0.3171 -0.2093 566  TYR E CB  
15849 C  CG  . TYR E  566 ? 2.9098 3.3138 3.3282 0.7450  -0.3255 -0.2114 566  TYR E CG  
15850 C  CD1 . TYR E  566 ? 2.9071 3.3131 3.3576 0.7243  -0.3465 -0.2014 566  TYR E CD1 
15851 C  CD2 . TYR E  566 ? 2.9294 3.3228 3.3126 0.7370  -0.3117 -0.2211 566  TYR E CD2 
15852 C  CE1 . TYR E  566 ? 2.8185 3.2193 3.2650 0.6978  -0.3521 -0.2012 566  TYR E CE1 
15853 C  CE2 . TYR E  566 ? 2.8334 3.2178 3.2126 0.7105  -0.3182 -0.2228 566  TYR E CE2 
15854 C  CZ  . TYR E  566 ? 2.7237 3.1133 3.1339 0.6918  -0.3377 -0.2129 566  TYR E CZ  
15855 O  OH  . TYR E  566 ? 2.5448 2.9305 2.9519 0.6685  -0.3419 -0.2123 566  TYR E OH  
15856 N  N   . ARG E  567 ? 2.6758 3.1618 3.1666 0.8085  -0.3056 -0.1711 567  ARG E N   
15857 C  CA  . ARG E  567 ? 2.6917 3.1842 3.1933 0.8488  -0.2996 -0.1693 567  ARG E CA  
15858 C  C   . ARG E  567 ? 2.7623 3.3079 3.2691 0.8520  -0.2702 -0.1483 567  ARG E C   
15859 O  O   . ARG E  567 ? 2.8433 3.3905 3.3339 0.8915  -0.2534 -0.1532 567  ARG E O   
15860 C  CB  . ARG E  567 ? 2.6071 3.1035 3.1560 0.8485  -0.3210 -0.1562 567  ARG E CB  
15861 C  CG  . ARG E  567 ? 2.6232 3.0696 3.1772 0.8446  -0.3517 -0.1718 567  ARG E CG  
15862 C  CD  . ARG E  567 ? 2.6134 3.0574 3.2148 0.8545  -0.3715 -0.1592 567  ARG E CD  
15863 N  NE  . ARG E  567 ? 2.6523 3.0541 3.2693 0.8441  -0.4023 -0.1670 567  ARG E NE  
15864 C  CZ  . ARG E  567 ? 2.6141 2.9985 3.2725 0.8537  -0.4251 -0.1595 567  ARG E CZ  
15865 N  NH1 . ARG E  567 ? 2.5311 2.9359 3.2167 0.8762  -0.4197 -0.1457 567  ARG E NH1 
15866 N  NH2 . ARG E  567 ? 2.6216 2.9696 3.2983 0.8409  -0.4533 -0.1634 567  ARG E NH2 
15867 N  N   . THR E  568 ? 2.8039 3.3948 3.3339 0.8115  -0.2642 -0.1239 568  THR E N   
15868 C  CA  . THR E  568 ? 2.8670 3.5101 3.4083 0.8086  -0.2389 -0.1013 568  THR E CA  
15869 C  C   . THR E  568 ? 2.9449 3.5825 3.4492 0.8021  -0.2189 -0.1083 568  THR E C   
15870 O  O   . THR E  568 ? 3.0175 3.6960 3.5316 0.7998  -0.1971 -0.0885 568  THR E O   
15871 C  CB  . THR E  568 ? 2.7737 3.4683 3.3574 0.7672  -0.2446 -0.0723 568  THR E CB  
15872 O  OG1 . THR E  568 ? 2.8246 3.5734 3.4313 0.7698  -0.2236 -0.0469 568  THR E OG1 
15873 C  CG2 . THR E  568 ? 2.7382 3.4264 3.3056 0.7214  -0.2506 -0.0768 568  THR E CG2 
15874 N  N   . ALA E  569 ? 2.7212 3.3113 3.1877 0.7983  -0.2263 -0.1331 569  ALA E N   
15875 C  CA  . ALA E  569 ? 2.6227 3.2013 3.0523 0.7972  -0.2081 -0.1407 569  ALA E CA  
15876 C  C   . ALA E  569 ? 2.7568 3.2949 3.1439 0.8426  -0.2042 -0.1651 569  ALA E C   
15877 O  O   . ALA E  569 ? 2.9363 3.4590 3.2885 0.8459  -0.1915 -0.1732 569  ALA E O   
15878 C  CB  . ALA E  569 ? 2.5616 3.1218 2.9793 0.7560  -0.2174 -0.1481 569  ALA E CB  
15879 N  N   . ALA E  570 ? 2.7051 3.2244 3.0936 0.8783  -0.2161 -0.1773 570  ALA E N   
15880 C  CA  . ALA E  570 ? 2.7371 3.2160 3.0821 0.9243  -0.2163 -0.2039 570  ALA E CA  
15881 C  C   . ALA E  570 ? 2.7219 3.2313 3.0498 0.9594  -0.1846 -0.1931 570  ALA E C   
15882 O  O   . ALA E  570 ? 2.7535 3.3163 3.1123 0.9495  -0.1645 -0.1632 570  ALA E O   
15883 C  CB  . ALA E  570 ? 2.7770 3.2219 3.1311 0.9503  -0.2423 -0.2220 570  ALA E CB  
15884 N  N   . ASP E  571 ? 2.8593 3.3373 3.1379 1.0010  -0.1804 -0.2162 571  ASP E N   
15885 C  CA  . ASP E  571 ? 2.9160 3.4227 3.1712 1.0395  -0.1487 -0.2060 571  ASP E CA  
15886 C  C   . ASP E  571 ? 2.8208 3.3239 3.0702 1.0934  -0.1485 -0.2168 571  ASP E C   
15887 O  O   . ASP E  571 ? 2.7606 3.2331 3.0246 1.0999  -0.1750 -0.2337 571  ASP E O   
15888 C  CB  . ASP E  571 ? 3.1170 3.5975 3.3159 1.0532  -0.1406 -0.2217 571  ASP E CB  
15889 C  CG  . ASP E  571 ? 3.2534 3.7783 3.4385 1.0734  -0.1022 -0.1970 571  ASP E CG  
15890 O  OD1 . ASP E  571 ? 3.3112 3.8899 3.5397 1.0534  -0.0827 -0.1623 571  ASP E OD1 
15891 O  OD2 . ASP E  571 ? 3.2658 3.7741 3.3982 1.1089  -0.0923 -0.2105 571  ASP E OD2 
15892 N  N   . THR E  572 ? 2.8243 3.3593 3.0528 1.1341  -0.1172 -0.2057 572  THR E N   
15893 C  CA  . THR E  572 ? 2.9098 3.4419 3.1245 1.1929  -0.1125 -0.2176 572  THR E CA  
15894 C  C   . THR E  572 ? 2.9563 3.4156 3.1202 1.2261  -0.1412 -0.2654 572  THR E C   
15895 O  O   . THR E  572 ? 2.8395 3.2754 3.0010 1.2641  -0.1534 -0.2844 572  THR E O   
15896 C  CB  . THR E  572 ? 2.9149 3.4977 3.1101 1.2322  -0.0705 -0.1955 572  THR E CB  
15897 O  OG1 . THR E  572 ? 2.9061 3.4839 3.0814 1.2950  -0.0647 -0.2103 572  THR E OG1 
15898 C  CG2 . THR E  572 ? 2.9289 3.4980 3.0671 1.2402  -0.0583 -0.2039 572  THR E CG2 
15899 N  N   . THR E  573 ? 2.9786 3.4006 3.1036 1.2124  -0.1538 -0.2852 573  THR E N   
15900 C  CA  . THR E  573 ? 2.9391 3.2920 3.0188 1.2366  -0.1858 -0.3300 573  THR E CA  
15901 C  C   . THR E  573 ? 2.8528 3.1639 2.9672 1.1969  -0.2265 -0.3434 573  THR E C   
15902 O  O   . THR E  573 ? 2.9935 3.2463 3.0799 1.2080  -0.2580 -0.3781 573  THR E O   
15903 C  CB  . THR E  573 ? 2.8771 3.2148 2.8979 1.2443  -0.1794 -0.3422 573  THR E CB  
15904 O  OG1 . THR E  573 ? 2.7056 3.0521 2.7490 1.1877  -0.1804 -0.3248 573  THR E OG1 
15905 C  CG2 . THR E  573 ? 2.8107 3.1933 2.7969 1.2853  -0.1376 -0.3248 573  THR E CG2 
15906 N  N   . GLY E  574 ? 2.6294 2.9707 2.8042 1.1510  -0.2274 -0.3154 574  GLY E N   
15907 C  CA  . GLY E  574 ? 2.5743 2.8833 2.7840 1.1145  -0.2629 -0.3227 574  GLY E CA  
15908 C  C   . GLY E  574 ? 2.5551 2.8451 2.7546 1.0748  -0.2752 -0.3275 574  GLY E C   
15909 O  O   . GLY E  574 ? 2.5411 2.7957 2.7585 1.0532  -0.3072 -0.3395 574  GLY E O   
15910 N  N   . LEU E  575 ? 2.4787 2.7919 2.6525 1.0656  -0.2501 -0.3166 575  LEU E N   
15911 C  CA  . LEU E  575 ? 2.4728 2.7685 2.6337 1.0324  -0.2581 -0.3208 575  LEU E CA  
15912 C  C   . LEU E  575 ? 2.4969 2.8246 2.7045 0.9778  -0.2539 -0.2933 575  LEU E C   
15913 O  O   . LEU E  575 ? 2.4973 2.8696 2.7174 0.9626  -0.2267 -0.2674 575  LEU E O   
15914 C  CB  . LEU E  575 ? 2.5173 2.8202 2.6287 1.0508  -0.2334 -0.3212 575  LEU E CB  
15915 C  CG  . LEU E  575 ? 2.7076 2.9760 2.7907 1.0363  -0.2479 -0.3370 575  LEU E CG  
15916 C  CD1 . LEU E  575 ? 2.8585 3.0725 2.9292 1.0524  -0.2873 -0.3708 575  LEU E CD1 
15917 C  CD2 . LEU E  575 ? 2.8024 3.0797 2.8356 1.0610  -0.2226 -0.3352 575  LEU E CD2 
15918 N  N   . GLN E  576 ? 2.5859 2.8914 2.8189 0.9484  -0.2816 -0.2986 576  GLN E N   
15919 C  CA  . GLN E  576 ? 2.5107 2.8451 2.7834 0.8992  -0.2802 -0.2752 576  GLN E CA  
15920 C  C   . GLN E  576 ? 2.5247 2.8557 2.7779 0.8716  -0.2719 -0.2742 576  GLN E C   
15921 O  O   . GLN E  576 ? 2.5467 2.8410 2.7725 0.8790  -0.2848 -0.2939 576  GLN E O   
15922 C  CB  . GLN E  576 ? 2.4881 2.8062 2.7986 0.8817  -0.3109 -0.2766 576  GLN E CB  
15923 C  CG  . GLN E  576 ? 2.6611 2.9658 2.9888 0.9133  -0.3259 -0.2837 576  GLN E CG  
15924 C  CD  . GLN E  576 ? 2.8757 3.1620 3.2449 0.8942  -0.3577 -0.2818 576  GLN E CD  
15925 O  OE1 . GLN E  576 ? 2.8731 3.1570 3.2549 0.8599  -0.3686 -0.2763 576  GLN E OE1 
15926 N  NE2 . GLN E  576 ? 3.0261 3.3006 3.4187 0.9177  -0.3717 -0.2844 576  GLN E NE2 
15927 N  N   . PRO E  577 ? 2.4469 2.8141 2.7141 0.8404  -0.2520 -0.2520 577  PRO E N   
15928 C  CA  . PRO E  577 ? 2.6150 2.9754 2.8647 0.8149  -0.2438 -0.2518 577  PRO E CA  
15929 C  C   . PRO E  577 ? 2.7482 3.0854 3.0073 0.7896  -0.2666 -0.2603 577  PRO E C   
15930 O  O   . PRO E  577 ? 2.8599 3.1880 3.1429 0.7891  -0.2897 -0.2637 577  PRO E O   
15931 C  CB  . PRO E  577 ? 2.5440 2.9477 2.8150 0.7859  -0.2226 -0.2266 577  PRO E CB  
15932 C  CG  . PRO E  577 ? 2.5604 2.9961 2.8497 0.8074  -0.2125 -0.2131 577  PRO E CG  
15933 C  CD  . PRO E  577 ? 2.4932 2.9085 2.7922 0.8296  -0.2361 -0.2267 577  PRO E CD  
15934 N  N   . ILE E  578 ? 2.7497 3.0785 2.9930 0.7694  -0.2596 -0.2614 578  ILE E N   
15935 C  CA  . ILE E  578 ? 2.7525 3.0636 3.0033 0.7479  -0.2771 -0.2672 578  ILE E CA  
15936 C  C   . ILE E  578 ? 2.7720 3.0914 3.0149 0.7185  -0.2608 -0.2599 578  ILE E C   
15937 O  O   . ILE E  578 ? 2.8421 3.1633 3.0640 0.7217  -0.2397 -0.2572 578  ILE E O   
15938 C  CB  . ILE E  578 ? 2.4926 2.7638 2.7225 0.7715  -0.2954 -0.2879 578  ILE E CB  
15939 C  CG1 . ILE E  578 ? 2.4771 2.7369 2.7273 0.7498  -0.3162 -0.2888 578  ILE E CG1 
15940 C  CG2 . ILE E  578 ? 2.3759 2.6329 2.5648 0.7864  -0.2788 -0.2952 578  ILE E CG2 
15941 C  CD1 . ILE E  578 ? 2.3239 2.5989 2.6167 0.7349  -0.3333 -0.2776 578  ILE E CD1 
15942 N  N   . LEU E  579 ? 2.6412 2.9653 2.9017 0.6908  -0.2705 -0.2559 579  LEU E N   
15943 C  CA  . LEU E  579 ? 2.3259 2.6546 2.5777 0.6636  -0.2574 -0.2523 579  LEU E CA  
15944 C  C   . LEU E  579 ? 2.2533 2.5515 2.4784 0.6714  -0.2540 -0.2641 579  LEU E C   
15945 O  O   . LEU E  579 ? 2.2184 2.4948 2.4395 0.6892  -0.2693 -0.2740 579  LEU E O   
15946 C  CB  . LEU E  579 ? 2.2587 2.6064 2.5342 0.6355  -0.2680 -0.2439 579  LEU E CB  
15947 C  CG  . LEU E  579 ? 2.2606 2.6444 2.5633 0.6210  -0.2709 -0.2286 579  LEU E CG  
15948 C  CD1 . LEU E  579 ? 2.2529 2.6548 2.5749 0.5975  -0.2833 -0.2197 579  LEU E CD1 
15949 C  CD2 . LEU E  579 ? 2.3130 2.7159 2.6094 0.6070  -0.2520 -0.2218 579  LEU E CD2 
15950 N  N   . ASN E  580 ? 2.2646 2.5604 2.4732 0.6579  -0.2349 -0.2625 580  ASN E N   
15951 C  CA  . ASN E  580 ? 2.3417 2.6111 2.5281 0.6622  -0.2298 -0.2708 580  ASN E CA  
15952 C  C   . ASN E  580 ? 2.5733 2.8395 2.7717 0.6511  -0.2444 -0.2734 580  ASN E C   
15953 O  O   . ASN E  580 ? 2.6626 2.9496 2.8807 0.6310  -0.2503 -0.2666 580  ASN E O   
15954 C  CB  . ASN E  580 ? 2.3232 2.5894 2.4952 0.6469  -0.2074 -0.2673 580  ASN E CB  
15955 C  CG  . ASN E  580 ? 2.3237 2.5614 2.4732 0.6554  -0.1999 -0.2741 580  ASN E CG  
15956 O  OD1 . ASN E  580 ? 2.3390 2.5688 2.4866 0.6411  -0.1983 -0.2775 580  ASN E OD1 
15957 N  ND2 . ASN E  580 ? 2.3101 2.5339 2.4412 0.6813  -0.1948 -0.2755 580  ASN E ND2 
15958 N  N   . GLN E  581 ? 2.6335 2.8774 2.8211 0.6649  -0.2497 -0.2808 581  GLN E N   
15959 C  CA  . GLN E  581 ? 2.4780 2.7223 2.6854 0.6612  -0.2684 -0.2801 581  GLN E CA  
15960 C  C   . GLN E  581 ? 2.3417 2.5952 2.5523 0.6400  -0.2599 -0.2752 581  GLN E C   
15961 O  O   . GLN E  581 ? 2.3273 2.5973 2.5620 0.6297  -0.2721 -0.2673 581  GLN E O   
15962 C  CB  . GLN E  581 ? 2.5798 2.8000 2.7788 0.6841  -0.2809 -0.2886 581  GLN E CB  
15963 C  CG  . GLN E  581 ? 2.5084 2.7100 2.6777 0.6935  -0.2637 -0.2931 581  GLN E CG  
15964 C  CD  . GLN E  581 ? 2.4755 2.6655 2.6496 0.7005  -0.2755 -0.2946 581  GLN E CD  
15965 O  OE1 . GLN E  581 ? 2.5483 2.7481 2.7509 0.6927  -0.2931 -0.2898 581  GLN E OE1 
15966 N  NE2 . GLN E  581 ? 2.4686 2.6405 2.6182 0.7156  -0.2665 -0.2985 581  GLN E NE2 
15967 N  N   . PHE E  582 ? 2.5074 2.7501 2.6944 0.6349  -0.2392 -0.2788 582  PHE E N   
15968 C  CA  . PHE E  582 ? 2.6482 2.8959 2.8342 0.6205  -0.2316 -0.2773 582  PHE E CA  
15969 C  C   . PHE E  582 ? 2.9247 3.1972 3.1159 0.5963  -0.2282 -0.2728 582  PHE E C   
15970 O  O   . PHE E  582 ? 2.9363 3.2217 3.1304 0.5863  -0.2269 -0.2696 582  PHE E O   
15971 C  CB  . PHE E  582 ? 2.7454 2.9679 2.9045 0.6252  -0.2120 -0.2844 582  PHE E CB  
15972 C  CG  . PHE E  582 ? 2.7765 2.9960 2.9344 0.6253  -0.2072 -0.2844 582  PHE E CG  
15973 C  CD1 . PHE E  582 ? 2.8194 3.0430 2.9955 0.6376  -0.2213 -0.2791 582  PHE E CD1 
15974 C  CD2 . PHE E  582 ? 2.6798 2.8926 2.8196 0.6141  -0.1893 -0.2897 582  PHE E CD2 
15975 C  CE1 . PHE E  582 ? 2.7282 2.9548 2.9074 0.6394  -0.2151 -0.2755 582  PHE E CE1 
15976 C  CE2 . PHE E  582 ? 2.6308 2.8423 2.7681 0.6182  -0.1824 -0.2896 582  PHE E CE2 
15977 C  CZ  . PHE E  582 ? 2.6144 2.8358 2.7728 0.6313  -0.1940 -0.2808 582  PHE E CZ  
15978 N  N   . THR E  583 ? 3.1350 3.4176 3.3271 0.5877  -0.2265 -0.2712 583  THR E N   
15979 C  CA  . THR E  583 ? 3.2038 3.5113 3.3993 0.5638  -0.2255 -0.2670 583  THR E CA  
15980 C  C   . THR E  583 ? 2.9646 3.2994 3.1832 0.5579  -0.2375 -0.2567 583  THR E C   
15981 O  O   . THR E  583 ? 2.9208 3.2692 3.1373 0.5421  -0.2326 -0.2549 583  THR E O   
15982 C  CB  . THR E  583 ? 3.1864 3.4809 3.3574 0.5498  -0.2086 -0.2758 583  THR E CB  
15983 O  OG1 . THR E  583 ? 3.2191 3.4809 3.3701 0.5616  -0.1959 -0.2848 583  THR E OG1 
15984 C  CG2 . THR E  583 ? 3.1003 3.4135 3.2643 0.5280  -0.2088 -0.2772 583  THR E CG2 
15985 N  N   . PRO E  584 ? 2.8412 3.1840 3.0845 0.5699  -0.2541 -0.2494 584  PRO E N   
15986 C  CA  . PRO E  584 ? 2.8808 3.2489 3.1476 0.5657  -0.2644 -0.2387 584  PRO E CA  
15987 C  C   . PRO E  584 ? 2.9725 3.3741 3.2553 0.5453  -0.2721 -0.2260 584  PRO E C   
15988 O  O   . PRO E  584 ? 3.0857 3.5130 3.3841 0.5362  -0.2772 -0.2159 584  PRO E O   
15989 C  CB  . PRO E  584 ? 2.8275 3.1832 3.1125 0.5888  -0.2804 -0.2384 584  PRO E CB  
15990 C  CG  . PRO E  584 ? 2.7232 3.0655 3.0090 0.5925  -0.2865 -0.2406 584  PRO E CG  
15991 C  CD  . PRO E  584 ? 2.7655 3.0933 3.0195 0.5879  -0.2665 -0.2502 584  PRO E CD  
15992 N  N   . ALA E  585 ? 2.7823 3.1874 3.0624 0.5400  -0.2727 -0.2240 585  ALA E N   
15993 C  CA  . ALA E  585 ? 2.7708 3.2101 3.0673 0.5259  -0.2809 -0.2083 585  ALA E CA  
15994 C  C   . ALA E  585 ? 2.9111 3.3768 3.1940 0.5041  -0.2758 -0.2063 585  ALA E C   
15995 O  O   . ALA E  585 ? 3.0930 3.5471 3.3503 0.4960  -0.2642 -0.2196 585  ALA E O   
15996 C  CB  . ALA E  585 ? 2.6405 3.0791 2.9309 0.5271  -0.2767 -0.2068 585  ALA E CB  
15997 N  N   . ASN E  586 ? 2.7705 3.2728 3.0732 0.4941  -0.2865 -0.1880 586  ASN E N   
15998 C  CA  . ASN E  586 ? 2.7268 3.2630 3.0169 0.4736  -0.2861 -0.1821 586  ASN E CA  
15999 C  C   . ASN E  586 ? 2.6434 3.1707 2.8919 0.4670  -0.2719 -0.1977 586  ASN E C   
16000 O  O   . ASN E  586 ? 2.6659 3.1652 2.9021 0.4793  -0.2621 -0.2082 586  ASN E O   
16001 C  CB  . ASN E  586 ? 2.8044 3.3786 3.1263 0.4712  -0.2998 -0.1555 586  ASN E CB  
16002 C  CG  . ASN E  586 ? 3.1122 3.6785 3.4494 0.4838  -0.3013 -0.1478 586  ASN E CG  
16003 O  OD1 . ASN E  586 ? 2.8668 3.4157 3.1793 0.4884  -0.2887 -0.1602 586  ASN E OD1 
16004 N  ND2 . ASN E  586 ? 4.0818 4.6593 4.4627 0.4897  -0.3171 -0.1267 586  ASN E ND2 
16005 N  N   . ILE E  587 ? 2.6378 3.1881 2.8634 0.4489  -0.2715 -0.2001 587  ILE E N   
16006 C  CA  . ILE E  587 ? 2.7169 3.2572 2.8988 0.4446  -0.2591 -0.2177 587  ILE E CA  
16007 C  C   . ILE E  587 ? 2.7652 3.3494 2.9334 0.4332  -0.2641 -0.2070 587  ILE E C   
16008 O  O   . ILE E  587 ? 2.7166 3.3374 2.9045 0.4226  -0.2777 -0.1891 587  ILE E O   
16009 C  CB  . ILE E  587 ? 2.7941 3.3017 2.9461 0.4343  -0.2520 -0.2430 587  ILE E CB  
16010 C  CG1 . ILE E  587 ? 2.7944 3.3221 2.9605 0.4162  -0.2641 -0.2374 587  ILE E CG1 
16011 C  CG2 . ILE E  587 ? 2.8739 3.3365 3.0284 0.4497  -0.2413 -0.2541 587  ILE E CG2 
16012 C  CD1 . ILE E  587 ? 2.8739 3.3732 3.0185 0.4023  -0.2597 -0.2581 587  ILE E CD1 
16013 N  N   . SER E  588 ? 2.9425 3.5241 3.0752 0.4378  -0.2521 -0.2174 588  SER E N   
16014 C  CA  . SER E  588 ? 3.0089 3.6330 3.1203 0.4322  -0.2535 -0.2081 588  SER E CA  
16015 C  C   . SER E  588 ? 3.0459 3.6513 3.0972 0.4292  -0.2426 -0.2382 588  SER E C   
16016 O  O   . SER E  588 ? 3.1224 3.6832 3.1532 0.4383  -0.2291 -0.2609 588  SER E O   
16017 C  CB  . SER E  588 ? 3.0741 3.7275 3.2093 0.4473  -0.2493 -0.1810 588  SER E CB  
16018 O  OG  . SER E  588 ? 3.1228 3.7470 3.2481 0.4645  -0.2330 -0.1917 588  SER E OG  
16019 N  N   . ARG E  589 ? 2.8640 3.5032 2.8864 0.4172  -0.2499 -0.2384 589  ARG E N   
16020 C  CA  . ARG E  589 ? 2.8513 3.4796 2.8113 0.4159  -0.2428 -0.2667 589  ARG E CA  
16021 C  C   . ARG E  589 ? 2.9472 3.6345 2.8893 0.4180  -0.2453 -0.2474 589  ARG E C   
16022 O  O   . ARG E  589 ? 2.9932 3.7247 2.9763 0.4202  -0.2510 -0.2111 589  ARG E O   
16023 C  CB  . ARG E  589 ? 2.8658 3.4650 2.8016 0.3941  -0.2545 -0.2953 589  ARG E CB  
16024 C  CG  . ARG E  589 ? 2.9518 3.5095 2.8266 0.3963  -0.2453 -0.3344 589  ARG E CG  
16025 C  CD  . ARG E  589 ? 2.9993 3.5328 2.8545 0.3704  -0.2622 -0.3598 589  ARG E CD  
16026 N  NE  . ARG E  589 ? 3.0687 3.5625 2.8623 0.3722  -0.2574 -0.3989 589  ARG E NE  
16027 C  CZ  . ARG E  589 ? 3.1319 3.5967 2.8997 0.3501  -0.2732 -0.4271 589  ARG E CZ  
16028 N  NH1 . ARG E  589 ? 3.1988 3.6753 3.0002 0.3237  -0.2936 -0.4178 589  ARG E NH1 
16029 N  NH2 . ARG E  589 ? 3.1512 3.5744 2.8615 0.3548  -0.2690 -0.4647 589  ARG E NH2 
16030 N  N   . GLN E  590 ? 2.9863 3.6746 2.8666 0.4185  -0.2414 -0.2710 590  GLN E N   
16031 C  CA  . GLN E  590 ? 3.0525 3.8001 2.9107 0.4253  -0.2402 -0.2509 590  GLN E CA  
16032 C  C   . GLN E  590 ? 3.1772 3.9253 2.9637 0.4175  -0.2470 -0.2823 590  GLN E C   
16033 O  O   . GLN E  590 ? 3.3500 4.0444 3.0963 0.4150  -0.2448 -0.3233 590  GLN E O   
16034 C  CB  . GLN E  590 ? 3.0041 3.7654 2.8643 0.4529  -0.2163 -0.2350 590  GLN E CB  
16035 C  CG  . GLN E  590 ? 3.0390 3.7496 2.8557 0.4701  -0.1958 -0.2706 590  GLN E CG  
16036 C  CD  . GLN E  590 ? 3.0085 3.7365 2.8388 0.4976  -0.1722 -0.2498 590  GLN E CD  
16037 O  OE1 . GLN E  590 ? 2.9525 3.7252 2.8332 0.5016  -0.1728 -0.2080 590  GLN E OE1 
16038 N  NE2 . GLN E  590 ? 3.0642 3.7564 2.8539 0.5167  -0.1521 -0.2777 590  GLN E NE2 
16039 N  N   . ALA E  591 ? 3.0871 3.8956 2.8586 0.4134  -0.2570 -0.2622 591  ALA E N   
16040 C  CA  . ALA E  591 ? 3.1020 3.9206 2.8006 0.4085  -0.2657 -0.2893 591  ALA E CA  
16041 C  C   . ALA E  591 ? 3.1220 3.9964 2.7853 0.4316  -0.2506 -0.2698 591  ALA E C   
16042 O  O   . ALA E  591 ? 3.0881 3.9898 2.7884 0.4499  -0.2327 -0.2352 591  ALA E O   
16043 C  CB  . ALA E  591 ? 3.1367 3.9799 2.8439 0.3794  -0.2963 -0.2848 591  ALA E CB  
16044 N  N   . ASP F  3   ? 3.2945 2.3741 2.3050 -0.9544 -0.2915 -0.2304 113  ASP F N   
16045 C  CA  . ASP F  3   ? 3.3043 2.3061 2.3401 -0.9218 -0.3095 -0.1776 113  ASP F CA  
16046 C  C   . ASP F  3   ? 3.4647 2.4522 2.4394 -0.8954 -0.3520 -0.1067 113  ASP F C   
16047 O  O   . ASP F  3   ? 3.6015 2.5919 2.4821 -0.9164 -0.3480 -0.0598 113  ASP F O   
16048 C  CB  . ASP F  3   ? 3.2331 2.1712 2.2642 -0.9519 -0.2674 -0.1556 113  ASP F CB  
16049 C  CG  . ASP F  3   ? 3.2139 2.0692 2.2884 -0.9190 -0.2818 -0.1173 113  ASP F CG  
16050 O  OD1 . ASP F  3   ? 3.1103 1.9677 2.2407 -0.8722 -0.3165 -0.1303 113  ASP F OD1 
16051 O  OD2 . ASP F  3   ? 3.2985 2.0857 2.3540 -0.9394 -0.2554 -0.0744 113  ASP F OD2 
16052 N  N   . TYR F  4   ? 3.5968 2.5739 2.6253 -0.8462 -0.3918 -0.0968 114  TYR F N   
16053 C  CA  . TYR F  4   ? 3.6359 2.6146 2.6220 -0.8168 -0.4365 -0.0368 114  TYR F CA  
16054 C  C   . TYR F  4   ? 3.5935 2.5336 2.6528 -0.7623 -0.4661 -0.0182 114  TYR F C   
16055 O  O   . TYR F  4   ? 3.4912 2.4466 2.6320 -0.7426 -0.4653 -0.0677 114  TYR F O   
16056 C  CB  . TYR F  4   ? 3.7145 2.7855 2.6738 -0.8237 -0.4623 -0.0665 114  TYR F CB  
16057 C  CG  . TYR F  4   ? 4.1235 3.2149 3.0326 -0.7984 -0.5109 -0.0086 114  TYR F CG  
16058 C  CD1 . TYR F  4   ? 4.3674 3.4583 3.1664 -0.8138 -0.5131 0.0500  114  TYR F CD1 
16059 C  CD2 . TYR F  4   ? 4.2232 3.3407 3.1964 -0.7574 -0.5535 -0.0107 114  TYR F CD2 
16060 C  CE1 . TYR F  4   ? 4.5532 3.6727 3.3054 -0.7856 -0.5619 0.1042  114  TYR F CE1 
16061 C  CE2 . TYR F  4   ? 4.4329 3.5798 3.3693 -0.7331 -0.6008 0.0390  114  TYR F CE2 
16062 C  CZ  . TYR F  4   ? 4.5897 3.7398 3.4144 -0.7458 -0.6076 0.0956  114  TYR F CZ  
16063 O  OH  . TYR F  4   ? 4.6112 3.7999 3.3977 -0.7169 -0.6588 0.1464  114  TYR F OH  
16064 N  N   . PRO F  5   ? 3.7050 2.5957 2.7380 -0.7344 -0.4892 0.0537  115  PRO F N   
16065 C  CA  . PRO F  5   ? 3.6855 2.5406 2.7883 -0.6800 -0.5147 0.0712  115  PRO F CA  
16066 C  C   . PRO F  5   ? 3.5552 2.4804 2.7100 -0.6496 -0.5495 0.0450  115  PRO F C   
16067 O  O   . PRO F  5   ? 3.5147 2.5091 2.6380 -0.6616 -0.5716 0.0402  115  PRO F O   
16068 C  CB  . PRO F  5   ? 3.8806 2.6791 2.9319 -0.6605 -0.5321 0.1580  115  PRO F CB  
16069 C  CG  . PRO F  5   ? 4.0272 2.7992 2.9956 -0.7080 -0.4978 0.1846  115  PRO F CG  
16070 C  CD  . PRO F  5   ? 3.9517 2.8092 2.8905 -0.7498 -0.4857 0.1259  115  PRO F CD  
16071 N  N   . VAL F  6   ? 3.7700 2.6787 3.0076 -0.6098 -0.5524 0.0268  116  VAL F N   
16072 C  CA  . VAL F  6   ? 3.6895 2.6558 2.9935 -0.5783 -0.5758 0.0047  116  VAL F CA  
16073 C  C   . VAL F  6   ? 3.6641 2.5907 3.0245 -0.5212 -0.5900 0.0343  116  VAL F C   
16074 O  O   . VAL F  6   ? 3.5982 2.4650 2.9778 -0.5067 -0.5701 0.0300  116  VAL F O   
16075 C  CB  . VAL F  6   ? 3.5925 2.6001 2.9481 -0.5918 -0.5503 -0.0665 116  VAL F CB  
16076 C  CG1 . VAL F  6   ? 3.3992 2.4425 2.8397 -0.5498 -0.5637 -0.0796 116  VAL F CG1 
16077 C  CG2 . VAL F  6   ? 3.5486 2.6122 2.8605 -0.6422 -0.5420 -0.1008 116  VAL F CG2 
16078 N  N   . ASP F  7   ? 3.4803 2.4447 2.8708 -0.4892 -0.6240 0.0598  117  ASP F N   
16079 C  CA  . ASP F  7   ? 3.3743 2.3167 2.8271 -0.4319 -0.6361 0.0839  117  ASP F CA  
16080 C  C   . ASP F  7   ? 3.0918 2.0962 2.6263 -0.4102 -0.6367 0.0504  117  ASP F C   
16081 O  O   . ASP F  7   ? 3.0528 2.1239 2.5995 -0.4318 -0.6487 0.0315  117  ASP F O   
16082 C  CB  . ASP F  7   ? 3.5582 2.4926 2.9899 -0.4063 -0.6729 0.1503  117  ASP F CB  
16083 C  CG  . ASP F  7   ? 3.7600 2.6222 3.1154 -0.4210 -0.6679 0.1964  117  ASP F CG  
16084 O  OD1 . ASP F  7   ? 3.8185 2.6200 3.1596 -0.4405 -0.6335 0.1777  117  ASP F OD1 
16085 O  OD2 . ASP F  7   ? 3.7715 2.6404 3.0848 -0.4126 -0.6978 0.2524  117  ASP F OD2 
16086 N  N   . LEU F  8   ? 3.0722 2.0552 2.6642 -0.3673 -0.6214 0.0421  118  LEU F N   
16087 C  CA  . LEU F  8   ? 3.0732 2.1075 2.7446 -0.3417 -0.6130 0.0187  118  LEU F CA  
16088 C  C   . LEU F  8   ? 3.1894 2.2092 2.9129 -0.2799 -0.6174 0.0484  118  LEU F C   
16089 O  O   . LEU F  8   ? 3.2353 2.2057 2.9545 -0.2517 -0.6021 0.0459  118  LEU F O   
16090 C  CB  . LEU F  8   ? 3.0573 2.0963 2.7431 -0.3527 -0.5776 -0.0330 118  LEU F CB  
16091 C  CG  . LEU F  8   ? 3.0214 2.1118 2.7849 -0.3328 -0.5607 -0.0558 118  LEU F CG  
16092 C  CD1 . LEU F  8   ? 3.0140 2.0929 2.8244 -0.2707 -0.5465 -0.0435 118  LEU F CD1 
16093 C  CD2 . LEU F  8   ? 2.9911 2.1374 2.7960 -0.3453 -0.5812 -0.0466 118  LEU F CD2 
16094 N  N   . TYR F  9   ? 3.2945 2.3626 3.0719 -0.2593 -0.6375 0.0716  119  TYR F N   
16095 C  CA  . TYR F  9   ? 3.2284 2.2965 3.0661 -0.1998 -0.6380 0.0987  119  TYR F CA  
16096 C  C   . TYR F  9   ? 2.9476 2.0604 2.8617 -0.1783 -0.6098 0.0767  119  TYR F C   
16097 O  O   . TYR F  9   ? 2.8776 2.0419 2.8287 -0.2065 -0.6072 0.0573  119  TYR F O   
16098 C  CB  . TYR F  9   ? 3.3459 2.4446 3.2053 -0.1870 -0.6764 0.1422  119  TYR F CB  
16099 C  CG  . TYR F  9   ? 3.3496 2.4327 3.2558 -0.1246 -0.6794 0.1773  119  TYR F CG  
16100 C  CD1 . TYR F  9   ? 3.4958 2.5103 3.3608 -0.1013 -0.6885 0.2071  119  TYR F CD1 
16101 C  CD2 . TYR F  9   ? 3.2731 2.4085 3.2700 -0.0889 -0.6691 0.1808  119  TYR F CD2 
16102 C  CE1 . TYR F  9   ? 3.4541 2.4540 3.3652 -0.0422 -0.6894 0.2345  119  TYR F CE1 
16103 C  CE2 . TYR F  9   ? 3.3000 2.4265 3.3405 -0.0305 -0.6684 0.2109  119  TYR F CE2 
16104 C  CZ  . TYR F  9   ? 3.3289 2.3883 3.3252 -0.0064 -0.6797 0.2353  119  TYR F CZ  
16105 O  OH  . TYR F  9   ? 3.3290 2.3789 3.3720 0.0539  -0.6772 0.2607  119  TYR F OH  
16106 N  N   . TYR F  10  ? 2.8909 1.9840 2.8293 -0.1271 -0.5867 0.0797  120  TYR F N   
16107 C  CA  . TYR F  10  ? 2.8981 2.0276 2.8991 -0.0977 -0.5533 0.0679  120  TYR F CA  
16108 C  C   . TYR F  10  ? 2.8922 2.0539 2.9676 -0.0502 -0.5533 0.1039  120  TYR F C   
16109 O  O   . TYR F  10  ? 3.0292 2.1650 3.1005 -0.0031 -0.5522 0.1225  120  TYR F O   
16110 C  CB  . TYR F  10  ? 2.9085 2.0069 2.8774 -0.0706 -0.5252 0.0431  120  TYR F CB  
16111 C  CG  . TYR F  10  ? 2.8773 2.0137 2.8897 -0.0500 -0.4890 0.0289  120  TYR F CG  
16112 C  CD1 . TYR F  10  ? 2.8383 1.9938 2.8549 -0.0901 -0.4769 0.0010  120  TYR F CD1 
16113 C  CD2 . TYR F  10  ? 2.9849 2.1379 3.0334 0.0128  -0.4639 0.0459  120  TYR F CD2 
16114 C  CE1 . TYR F  10  ? 2.8581 2.0428 2.9182 -0.0668 -0.4414 -0.0054 120  TYR F CE1 
16115 C  CE2 . TYR F  10  ? 2.9813 2.1677 3.0655 0.0366  -0.4276 0.0428  120  TYR F CE2 
16116 C  CZ  . TYR F  10  ? 2.9145 2.1139 3.0065 -0.0027 -0.4167 0.0192  120  TYR F CZ  
16117 O  OH  . TYR F  10  ? 2.8667 2.0939 2.9979 0.0251  -0.3784 0.0224  120  TYR F OH  
16118 N  N   . LEU F  11  ? 2.6867 1.9064 2.8363 -0.0639 -0.5533 0.1098  121  LEU F N   
16119 C  CA  . LEU F  11  ? 2.6396 1.9020 2.8768 -0.0260 -0.5512 0.1422  121  LEU F CA  
16120 C  C   . LEU F  11  ? 2.6435 1.9314 2.9463 0.0065  -0.5012 0.1431  121  LEU F C   
16121 O  O   . LEU F  11  ? 2.6981 2.0161 3.0508 -0.0212 -0.4823 0.1279  121  LEU F O   
16122 C  CB  . LEU F  11  ? 2.7116 2.0287 2.9995 -0.0637 -0.5851 0.1464  121  LEU F CB  
16123 C  CG  . LEU F  11  ? 2.7274 2.0932 3.1034 -0.0300 -0.5975 0.1807  121  LEU F CG  
16124 C  CD1 . LEU F  11  ? 2.7703 2.0960 3.1043 0.0149  -0.6160 0.2126  121  LEU F CD1 
16125 C  CD2 . LEU F  11  ? 2.8254 2.2563 3.2483 -0.0733 -0.6372 0.1732  121  LEU F CD2 
16126 N  N   . MET F  12  ? 2.6890 1.9639 2.9909 0.0674  -0.4772 0.1614  122  MET F N   
16127 C  CA  . MET F  12  ? 2.6015 1.9004 2.9501 0.1081  -0.4261 0.1708  122  MET F CA  
16128 C  C   . MET F  12  ? 2.5203 1.8670 2.9682 0.1446  -0.4086 0.2088  122  MET F C   
16129 O  O   . MET F  12  ? 2.4972 1.8451 2.9527 0.1708  -0.4288 0.2279  122  MET F O   
16130 C  CB  . MET F  12  ? 2.6853 1.9503 2.9606 0.1552  -0.4066 0.1604  122  MET F CB  
16131 C  CG  . MET F  12  ? 2.8037 2.0952 3.1032 0.1950  -0.3551 0.1688  122  MET F CG  
16132 S  SD  . MET F  12  ? 3.2213 2.5053 3.4622 0.2765  -0.3325 0.1698  122  MET F SD  
16133 C  CE  . MET F  12  ? 3.1516 2.3803 3.2842 0.2484  -0.3669 0.1158  122  MET F CE  
16134 N  N   . ASP F  13  ? 2.4914 1.8760 3.0208 0.1483  -0.3667 0.2211  123  ASP F N   
16135 C  CA  . ASP F  13  ? 2.4840 1.9179 3.1202 0.1825  -0.3368 0.2585  123  ASP F CA  
16136 C  C   . ASP F  13  ? 2.5271 1.9582 3.1394 0.2566  -0.2904 0.2828  123  ASP F C   
16137 O  O   . ASP F  13  ? 2.7564 2.1802 3.3430 0.2750  -0.2520 0.2831  123  ASP F O   
16138 C  CB  . ASP F  13  ? 2.4689 1.9412 3.2148 0.1470  -0.3083 0.2606  123  ASP F CB  
16139 C  CG  . ASP F  13  ? 2.4572 1.9814 3.3263 0.1796  -0.2674 0.3008  123  ASP F CG  
16140 O  OD1 . ASP F  13  ? 2.5879 2.1337 3.4758 0.2122  -0.2804 0.3210  123  ASP F OD1 
16141 O  OD2 . ASP F  13  ? 2.4264 1.9686 3.3793 0.1731  -0.2187 0.3133  123  ASP F OD2 
16142 N  N   . LEU F  14  ? 2.4000 1.8418 3.0207 0.3028  -0.2934 0.3031  124  LEU F N   
16143 C  CA  . LEU F  14  ? 2.3501 1.7962 2.9418 0.3768  -0.2511 0.3211  124  LEU F CA  
16144 C  C   . LEU F  14  ? 2.3135 1.8172 3.0132 0.4120  -0.1950 0.3661  124  LEU F C   
16145 O  O   . LEU F  14  ? 2.4101 1.9307 3.0982 0.4782  -0.1594 0.3872  124  LEU F O   
16146 C  CB  . LEU F  14  ? 2.4550 1.8744 2.9899 0.4121  -0.2804 0.3115  124  LEU F CB  
16147 C  CG  . LEU F  14  ? 2.3919 1.7472 2.8101 0.3984  -0.3173 0.2694  124  LEU F CG  
16148 C  CD1 . LEU F  14  ? 2.4227 1.7502 2.8079 0.4411  -0.3347 0.2634  124  LEU F CD1 
16149 C  CD2 . LEU F  14  ? 2.3916 1.7375 2.7400 0.4146  -0.2896 0.2482  124  LEU F CD2 
16150 N  N   . SER F  15  ? 2.3390 1.8749 3.1464 0.3685  -0.1835 0.3787  125  SER F N   
16151 C  CA  . SER F  15  ? 2.3773 1.9683 3.3077 0.3935  -0.1280 0.4223  125  SER F CA  
16152 C  C   . SER F  15  ? 2.2668 1.8598 3.1757 0.4450  -0.0572 0.4537  125  SER F C   
16153 O  O   . SER F  15  ? 2.2361 1.7942 3.0396 0.4596  -0.0556 0.4380  125  SER F O   
16154 C  CB  . SER F  15  ? 2.4225 2.0448 3.4805 0.3276  -0.1328 0.4187  125  SER F CB  
16155 O  OG  . SER F  15  ? 2.4396 2.0344 3.4864 0.2888  -0.1195 0.4019  125  SER F OG  
16156 N  N   . ALA F  16  ? 2.2004 1.8404 3.2168 0.4726  0.0035  0.5010  126  ALA F N   
16157 C  CA  . ALA F  16  ? 2.2405 1.8905 3.2342 0.5347  0.0767  0.5440  126  ALA F CA  
16158 C  C   . ALA F  16  ? 2.1623 1.7856 3.1529 0.5100  0.1025  0.5482  126  ALA F C   
16159 O  O   . ALA F  16  ? 2.1801 1.7944 3.0894 0.5598  0.1371  0.5667  126  ALA F O   
16160 C  CB  . ALA F  16  ? 2.3714 2.0789 3.4903 0.5671  0.1406  0.5987  126  ALA F CB  
16161 N  N   . SER F  17  ? 2.1463 1.7594 3.2209 0.4360  0.0832  0.5271  127  SER F N   
16162 C  CA  . SER F  17  ? 2.3040 1.8907 3.4002 0.4101  0.1125  0.5301  127  SER F CA  
16163 C  C   . SER F  17  ? 2.2582 1.7997 3.2196 0.4004  0.0711  0.4868  127  SER F C   
16164 O  O   . SER F  17  ? 2.3609 1.8777 3.3364 0.3726  0.0847  0.4787  127  SER F O   
16165 C  CB  . SER F  17  ? 2.5230 2.1179 3.7639 0.3319  0.1058  0.5117  127  SER F CB  
16166 O  OG  . SER F  17  ? 2.5707 2.1683 3.7961 0.2786  0.0270  0.4576  127  SER F OG  
16167 N  N   . MET F  18  ? 2.2700 1.7996 3.1102 0.4217  0.0234  0.4569  128  MET F N   
16168 C  CA  . MET F  18  ? 2.3224 1.8127 3.0454 0.4043  -0.0202 0.4091  128  MET F CA  
16169 C  C   . MET F  18  ? 2.3245 1.8149 2.9332 0.4754  -0.0011 0.4164  128  MET F C   
16170 O  O   . MET F  18  ? 2.3267 1.7917 2.8385 0.4666  -0.0368 0.3736  128  MET F O   
16171 C  CB  . MET F  18  ? 2.3761 1.8473 3.0516 0.3638  -0.0933 0.3619  128  MET F CB  
16172 C  CG  . MET F  18  ? 2.4956 1.9701 3.2566 0.2875  -0.1256 0.3416  128  MET F CG  
16173 S  SD  . MET F  18  ? 2.6757 2.1213 3.4344 0.2253  -0.1302 0.3048  128  MET F SD  
16174 C  CE  . MET F  18  ? 2.9006 2.3041 3.4957 0.2299  -0.1746 0.2612  128  MET F CE  
16175 N  N   . ASP F  19  ? 2.2013 1.7261 2.8206 0.5459  0.0555  0.4680  129  ASP F N   
16176 C  CA  . ASP F  19  ? 2.1809 1.7191 2.6864 0.6190  0.0721  0.4726  129  ASP F CA  
16177 C  C   . ASP F  19  ? 2.4739 2.0029 2.9525 0.6228  0.0914  0.4780  129  ASP F C   
16178 O  O   . ASP F  19  ? 2.5736 2.1064 2.9435 0.6566  0.0737  0.4513  129  ASP F O   
16179 C  CB  . ASP F  19  ? 2.2278 1.8127 2.7487 0.6959  0.1318  0.5298  129  ASP F CB  
16180 C  CG  . ASP F  19  ? 2.2818 1.8938 2.6814 0.7773  0.1503  0.5345  129  ASP F CG  
16181 O  OD1 . ASP F  19  ? 2.2980 1.9122 2.6031 0.8016  0.1112  0.4874  129  ASP F OD1 
16182 O  OD2 . ASP F  19  ? 2.3146 1.9470 2.7155 0.8183  0.2042  0.5848  129  ASP F OD2 
16183 N  N   . ASP F  20  ? 2.7458 2.2638 3.3288 0.5877  0.1259  0.5078  130  ASP F N   
16184 C  CA  . ASP F  20  ? 2.6595 2.1630 3.2368 0.5887  0.1473  0.5158  130  ASP F CA  
16185 C  C   . ASP F  20  ? 2.4212 1.8897 2.9599 0.5238  0.0874  0.4458  130  ASP F C   
16186 O  O   . ASP F  20  ? 2.4560 1.9158 2.9665 0.5295  0.0936  0.4386  130  ASP F O   
16187 C  CB  . ASP F  20  ? 2.6654 2.1619 3.3854 0.5706  0.2101  0.5697  130  ASP F CB  
16188 C  CG  . ASP F  20  ? 2.5449 2.0285 3.3834 0.4891  0.1891  0.5451  130  ASP F CG  
16189 O  OD1 . ASP F  20  ? 2.6909 2.1877 3.5167 0.4751  0.1491  0.5212  130  ASP F OD1 
16190 O  OD2 . ASP F  20  ? 2.3511 1.8146 3.2989 0.4414  0.2123  0.5482  130  ASP F OD2 
16191 N  N   . ASP F  21  ? 2.2855 1.7369 2.8217 0.4660  0.0317  0.3974  131  ASP F N   
16192 C  CA  . ASP F  21  ? 2.3512 1.7710 2.8556 0.3989  -0.0217 0.3346  131  ASP F CA  
16193 C  C   . ASP F  21  ? 2.3932 1.8040 2.7883 0.3991  -0.0781 0.2868  131  ASP F C   
16194 O  O   . ASP F  21  ? 2.6367 2.0211 2.9951 0.3446  -0.1225 0.2357  131  ASP F O   
16195 C  CB  . ASP F  21  ? 2.3711 1.7775 2.9781 0.3217  -0.0360 0.3207  131  ASP F CB  
16196 C  CG  . ASP F  21  ? 2.4443 1.8635 3.1839 0.3252  0.0249  0.3712  131  ASP F CG  
16197 O  OD1 . ASP F  21  ? 2.4547 1.8683 3.2151 0.3520  0.0723  0.3995  131  ASP F OD1 
16198 O  OD2 . ASP F  21  ? 2.5299 1.9660 3.3578 0.3041  0.0276  0.3848  131  ASP F OD2 
16199 N  N   . LEU F  22  ? 2.3437 1.7749 2.6905 0.4589  -0.0736 0.3015  132  LEU F N   
16200 C  CA  . LEU F  22  ? 2.5348 1.9513 2.7934 0.4596  -0.1231 0.2552  132  LEU F CA  
16201 C  C   . LEU F  22  ? 2.7257 2.1321 2.8966 0.4544  -0.1493 0.2054  132  LEU F C   
16202 O  O   . LEU F  22  ? 2.8173 2.1909 2.9516 0.4033  -0.1955 0.1565  132  LEU F O   
16203 C  CB  . LEU F  22  ? 2.6578 2.1029 2.8869 0.5334  -0.1040 0.2776  132  LEU F CB  
16204 C  CG  . LEU F  22  ? 2.6860 2.1139 2.8327 0.5448  -0.1473 0.2291  132  LEU F CG  
16205 C  CD1 . LEU F  22  ? 2.4869 1.8732 2.6625 0.4817  -0.1922 0.2092  132  LEU F CD1 
16206 C  CD2 . LEU F  22  ? 2.8510 2.3150 2.9721 0.6255  -0.1192 0.2492  132  LEU F CD2 
16207 N  N   . ASN F  23  ? 2.7076 2.1457 2.8470 0.5080  -0.1189 0.2194  133  ASN F N   
16208 C  CA  . ASN F  23  ? 2.7509 2.1941 2.8130 0.5108  -0.1443 0.1698  133  ASN F CA  
16209 C  C   . ASN F  23  ? 2.8926 2.3056 2.9790 0.4361  -0.1648 0.1374  133  ASN F C   
16210 O  O   . ASN F  23  ? 3.0135 2.4214 3.0435 0.4156  -0.1973 0.0838  133  ASN F O   
16211 C  CB  . ASN F  23  ? 2.8012 2.2960 2.8299 0.5904  -0.1071 0.1990  133  ASN F CB  
16212 C  CG  . ASN F  23  ? 2.8895 2.3888 2.9979 0.5976  -0.0550 0.2607  133  ASN F CG  
16213 O  OD1 . ASN F  23  ? 2.8338 2.3108 3.0305 0.5645  -0.0337 0.2942  133  ASN F OD1 
16214 N  ND2 . ASN F  23  ? 2.9455 2.4744 3.0301 0.6408  -0.0344 0.2745  133  ASN F ND2 
16215 N  N   . THR F  24  ? 2.7030 2.0994 2.8763 0.3941  -0.1452 0.1643  134  THR F N   
16216 C  CA  . THR F  24  ? 2.4720 1.8419 2.6688 0.3213  -0.1640 0.1281  134  THR F CA  
16217 C  C   . THR F  24  ? 2.4697 1.8065 2.6461 0.2554  -0.2129 0.0886  134  THR F C   
16218 O  O   . THR F  24  ? 2.5345 1.8527 2.6881 0.2010  -0.2386 0.0445  134  THR F O   
16219 C  CB  . THR F  24  ? 2.4010 1.7666 2.7030 0.2997  -0.1251 0.1628  134  THR F CB  
16220 O  OG1 . THR F  24  ? 2.3550 1.7192 2.7237 0.2899  -0.1162 0.1952  134  THR F OG1 
16221 C  CG2 . THR F  24  ? 2.3643 1.7545 2.6865 0.3654  -0.0724 0.2084  134  THR F CG2 
16222 N  N   . ILE F  25  ? 2.4673 1.7984 2.6522 0.2623  -0.2237 0.1072  135  ILE F N   
16223 C  CA  . ILE F  25  ? 2.4765 1.7762 2.6424 0.2083  -0.2689 0.0810  135  ILE F CA  
16224 C  C   . ILE F  25  ? 2.5202 1.8000 2.5954 0.2131  -0.3002 0.0391  135  ILE F C   
16225 O  O   . ILE F  25  ? 2.5759 1.8246 2.6193 0.1576  -0.3330 0.0049  135  ILE F O   
16226 C  CB  . ILE F  25  ? 2.4246 1.7297 2.6411 0.2202  -0.2688 0.1182  135  ILE F CB  
16227 C  CG1 . ILE F  25  ? 2.4004 1.7276 2.7230 0.2052  -0.2379 0.1521  135  ILE F CG1 
16228 C  CG2 . ILE F  25  ? 2.4532 1.7276 2.6449 0.1750  -0.3169 0.0991  135  ILE F CG2 
16229 C  CD1 . ILE F  25  ? 2.4533 1.7711 2.8052 0.1401  -0.2443 0.1240  135  ILE F CD1 
16230 N  N   . LYS F  26  ? 2.6164 1.9161 2.6505 0.2790  -0.2885 0.0391  136  LYS F N   
16231 C  CA  . LYS F  26  ? 2.6840 1.9686 2.6432 0.2839  -0.3164 -0.0100 136  LYS F CA  
16232 C  C   . LYS F  26  ? 2.7938 2.0829 2.7246 0.2528  -0.3248 -0.0537 136  LYS F C   
16233 O  O   . LYS F  26  ? 2.8442 2.1057 2.7350 0.2155  -0.3536 -0.0993 136  LYS F O   
16234 C  CB  . LYS F  26  ? 2.7995 2.1162 2.7235 0.3649  -0.3018 -0.0075 136  LYS F CB  
16235 C  CG  . LYS F  26  ? 2.8447 2.1613 2.7967 0.4012  -0.2902 0.0318  136  LYS F CG  
16236 C  CD  . LYS F  26  ? 2.9574 2.3089 2.8635 0.4819  -0.2757 0.0246  136  LYS F CD  
16237 C  CE  . LYS F  26  ? 2.8582 2.2159 2.7991 0.5213  -0.2570 0.0654  136  LYS F CE  
16238 N  NZ  . LYS F  26  ? 2.8554 2.2530 2.7471 0.6030  -0.2391 0.0557  136  LYS F NZ  
16239 N  N   . GLU F  27  ? 2.8871 2.2089 2.8456 0.2668  -0.2973 -0.0388 137  GLU F N   
16240 C  CA  . GLU F  27  ? 2.8797 2.2097 2.8236 0.2367  -0.3035 -0.0788 137  GLU F CA  
16241 C  C   . GLU F  27  ? 2.8320 2.1261 2.7986 0.1529  -0.3185 -0.0954 137  GLU F C   
16242 O  O   . GLU F  27  ? 2.8891 2.1832 2.8382 0.1160  -0.3282 -0.1370 137  GLU F O   
16243 C  CB  . GLU F  27  ? 2.8924 2.2660 2.8644 0.2830  -0.2673 -0.0527 137  GLU F CB  
16244 C  CG  . GLU F  27  ? 2.9411 2.3657 2.8634 0.3624  -0.2611 -0.0573 137  GLU F CG  
16245 C  CD  . GLU F  27  ? 2.9091 2.3767 2.8495 0.4028  -0.2321 -0.0376 137  GLU F CD  
16246 O  OE1 . GLU F  27  ? 2.8967 2.4160 2.8008 0.4800  -0.2201 -0.0233 137  GLU F OE1 
16247 O  OE2 . GLU F  27  ? 2.8802 2.3314 2.8709 0.3603  -0.2205 -0.0356 137  GLU F OE2 
16248 N  N   . LEU F  28  ? 2.7422 2.0133 2.7469 0.1241  -0.3210 -0.0660 138  LEU F N   
16249 C  CA  . LEU F  28  ? 2.7217 1.9648 2.7347 0.0476  -0.3412 -0.0829 138  LEU F CA  
16250 C  C   . LEU F  28  ? 2.7323 1.9374 2.6901 0.0162  -0.3767 -0.1033 138  LEU F C   
16251 O  O   . LEU F  28  ? 2.7969 1.9822 2.7296 -0.0427 -0.3930 -0.1320 138  LEU F O   
16252 C  CB  . LEU F  28  ? 2.6683 1.9146 2.7516 0.0317  -0.3317 -0.0460 138  LEU F CB  
16253 C  CG  . LEU F  28  ? 2.6145 1.8443 2.7046 -0.0425 -0.3564 -0.0625 138  LEU F CG  
16254 C  CD1 . LEU F  28  ? 2.5845 1.8141 2.6567 -0.0879 -0.3544 -0.1065 138  LEU F CD1 
16255 C  CD2 . LEU F  28  ? 2.5916 1.8395 2.7659 -0.0522 -0.3454 -0.0340 138  LEU F CD2 
16256 N  N   . GLY F  29  ? 2.7120 1.9050 2.6519 0.0557  -0.3853 -0.0879 139  GLY F N   
16257 C  CA  . GLY F  29  ? 2.7300 1.8783 2.6249 0.0330  -0.4144 -0.1038 139  GLY F CA  
16258 C  C   . GLY F  29  ? 2.7348 1.8709 2.5823 0.0142  -0.4225 -0.1559 139  GLY F C   
16259 O  O   . GLY F  29  ? 2.6409 1.7438 2.4638 -0.0437 -0.4380 -0.1746 139  GLY F O   
16260 N  N   . SER F  30  ? 2.7487 1.9173 2.5844 0.0636  -0.4113 -0.1798 140  SER F N   
16261 C  CA  . SER F  30  ? 2.7713 1.9396 2.5733 0.0482  -0.4209 -0.2368 140  SER F CA  
16262 C  C   . SER F  30  ? 2.7983 1.9787 2.6064 -0.0062 -0.4164 -0.2603 140  SER F C   
16263 O  O   . SER F  30  ? 2.8480 2.0062 2.6354 -0.0546 -0.4271 -0.2980 140  SER F O   
16264 C  CB  . SER F  30  ? 2.7428 1.9611 2.5320 0.1183  -0.4133 -0.2598 140  SER F CB  
16265 O  OG  . SER F  30  ? 2.7600 2.0332 2.5706 0.1525  -0.3904 -0.2403 140  SER F OG  
16266 N  N   . ARG F  31  ? 2.7304 1.9430 2.5731 -0.0009 -0.3972 -0.2381 141  ARG F N   
16267 C  CA  . ARG F  31  ? 2.6615 1.8874 2.5158 -0.0488 -0.3897 -0.2635 141  ARG F CA  
16268 C  C   . ARG F  31  ? 2.5403 1.7248 2.3822 -0.1230 -0.4022 -0.2637 141  ARG F C   
16269 O  O   . ARG F  31  ? 2.4250 1.6063 2.2508 -0.1729 -0.4032 -0.2993 141  ARG F O   
16270 C  CB  . ARG F  31  ? 2.6545 1.9162 2.5582 -0.0229 -0.3628 -0.2381 141  ARG F CB  
16271 C  CG  . ARG F  31  ? 2.6094 1.8929 2.5324 -0.0559 -0.3501 -0.2699 141  ARG F CG  
16272 C  CD  . ARG F  31  ? 2.6781 1.9903 2.6577 -0.0183 -0.3193 -0.2411 141  ARG F CD  
16273 N  NE  . ARG F  31  ? 2.6469 1.9814 2.6518 -0.0394 -0.3044 -0.2730 141  ARG F NE  
16274 C  CZ  . ARG F  31  ? 2.7192 2.0751 2.7791 -0.0085 -0.2741 -0.2544 141  ARG F CZ  
16275 N  NH1 . ARG F  31  ? 2.8333 2.1908 2.9275 0.0426  -0.2532 -0.2010 141  ARG F NH1 
16276 N  NH2 . ARG F  31  ? 2.6902 2.0646 2.7755 -0.0272 -0.2612 -0.2873 141  ARG F NH2 
16277 N  N   . LEU F  32  ? 2.6588 1.8177 2.5073 -0.1288 -0.4115 -0.2232 142  LEU F N   
16278 C  CA  . LEU F  32  ? 2.5966 1.7224 2.4227 -0.1912 -0.4280 -0.2177 142  LEU F CA  
16279 C  C   . LEU F  32  ? 2.6271 1.7067 2.4043 -0.2117 -0.4446 -0.2305 142  LEU F C   
16280 O  O   . LEU F  32  ? 2.6040 1.6584 2.3500 -0.2683 -0.4516 -0.2365 142  LEU F O   
16281 C  CB  . LEU F  32  ? 2.6216 1.7452 2.4758 -0.1847 -0.4369 -0.1715 142  LEU F CB  
16282 C  CG  . LEU F  32  ? 2.7341 1.8349 2.5651 -0.2344 -0.4606 -0.1540 142  LEU F CG  
16283 C  CD1 . LEU F  32  ? 2.5907 1.7248 2.4739 -0.2423 -0.4613 -0.1340 142  LEU F CD1 
16284 C  CD2 . LEU F  32  ? 3.0117 2.0702 2.8152 -0.2157 -0.4817 -0.1255 142  LEU F CD2 
16285 N  N   . SER F  33  ? 2.6168 1.6850 2.3881 -0.1664 -0.4478 -0.2366 143  SER F N   
16286 C  CA  . SER F  33  ? 2.6856 1.7036 2.4247 -0.1841 -0.4595 -0.2537 143  SER F CA  
16287 C  C   . SER F  33  ? 2.7026 1.7333 2.4335 -0.2112 -0.4511 -0.3106 143  SER F C   
16288 O  O   . SER F  33  ? 2.6374 1.6422 2.3597 -0.2106 -0.4554 -0.3412 143  SER F O   
16289 C  CB  . SER F  33  ? 2.7743 1.7757 2.5173 -0.1250 -0.4659 -0.2465 143  SER F CB  
16290 O  OG  . SER F  33  ? 2.9395 1.8853 2.6625 -0.1435 -0.4743 -0.2679 143  SER F OG  
16291 N  N   . LYS F  34  ? 2.8461 1.9187 2.5881 -0.2354 -0.4381 -0.3288 144  LYS F N   
16292 C  CA  . LYS F  34  ? 2.9232 2.0196 2.6672 -0.2620 -0.4289 -0.3836 144  LYS F CA  
16293 C  C   . LYS F  34  ? 2.8055 1.9073 2.5429 -0.3256 -0.4174 -0.3896 144  LYS F C   
16294 O  O   . LYS F  34  ? 2.6702 1.7522 2.3903 -0.3775 -0.4122 -0.4137 144  LYS F O   
16295 C  CB  . LYS F  34  ? 2.9980 2.1607 2.7696 -0.2065 -0.4217 -0.4105 144  LYS F CB  
16296 C  CG  . LYS F  34  ? 3.0610 2.2687 2.8481 -0.2309 -0.4118 -0.4645 144  LYS F CG  
16297 C  CD  . LYS F  34  ? 3.1714 2.3607 2.9517 -0.2642 -0.4182 -0.5125 144  LYS F CD  
16298 C  CE  . LYS F  34  ? 3.0393 2.2816 2.8453 -0.2927 -0.4070 -0.5673 144  LYS F CE  
16299 N  NZ  . LYS F  34  ? 2.9552 2.1818 2.7689 -0.3329 -0.4092 -0.6170 144  LYS F NZ  
16300 N  N   . GLU F  35  ? 2.8552 1.9836 2.6095 -0.3230 -0.4105 -0.3691 145  GLU F N   
16301 C  CA  . GLU F  35  ? 2.9732 2.1160 2.7238 -0.3784 -0.3978 -0.3844 145  GLU F CA  
16302 C  C   . GLU F  35  ? 2.9014 2.0018 2.6057 -0.4323 -0.4070 -0.3592 145  GLU F C   
16303 O  O   . GLU F  35  ? 2.8410 1.9511 2.5265 -0.4846 -0.3956 -0.3771 145  GLU F O   
16304 C  CB  . GLU F  35  ? 3.0826 2.2640 2.8754 -0.3581 -0.3862 -0.3758 145  GLU F CB  
16305 C  CG  . GLU F  35  ? 3.0651 2.2877 2.9014 -0.2943 -0.3746 -0.3843 145  GLU F CG  
16306 C  CD  . GLU F  35  ? 3.0094 2.2707 2.8575 -0.2977 -0.3627 -0.4353 145  GLU F CD  
16307 O  OE1 . GLU F  35  ? 3.0191 2.2835 2.8588 -0.3539 -0.3538 -0.4661 145  GLU F OE1 
16308 O  OE2 . GLU F  35  ? 2.9538 2.2493 2.8195 -0.2420 -0.3621 -0.4451 145  GLU F OE2 
16309 N  N   . MET F  36  ? 2.8935 1.9506 2.5770 -0.4176 -0.4264 -0.3176 146  MET F N   
16310 C  CA  . MET F  36  ? 2.9373 1.9580 2.5731 -0.4603 -0.4378 -0.2849 146  MET F CA  
16311 C  C   . MET F  36  ? 2.9634 1.9489 2.5612 -0.5081 -0.4267 -0.2999 146  MET F C   
16312 O  O   . MET F  36  ? 3.0017 1.9781 2.5551 -0.5568 -0.4231 -0.2866 146  MET F O   
16313 C  CB  . MET F  36  ? 3.0024 1.9874 2.6340 -0.4252 -0.4611 -0.2345 146  MET F CB  
16314 C  CG  . MET F  36  ? 3.2867 2.3054 2.9496 -0.3994 -0.4726 -0.2079 146  MET F CG  
16315 S  SD  . MET F  36  ? 3.9692 3.0216 3.6094 -0.4569 -0.4764 -0.2098 146  MET F SD  
16316 C  CE  . MET F  36  ? 3.6516 2.6543 3.2133 -0.4926 -0.4948 -0.1703 146  MET F CE  
16317 N  N   . SER F  37  ? 3.0098 1.9798 2.6263 -0.4953 -0.4194 -0.3294 147  SER F N   
16318 C  CA  . SER F  37  ? 3.2208 2.1546 2.8178 -0.5427 -0.4042 -0.3460 147  SER F CA  
16319 C  C   . SER F  37  ? 3.2848 2.2618 2.8823 -0.5909 -0.3792 -0.3870 147  SER F C   
16320 O  O   . SER F  37  ? 3.5240 2.4765 3.1053 -0.6393 -0.3601 -0.3974 147  SER F O   
16321 C  CB  . SER F  37  ? 3.2535 2.1662 2.8843 -0.5155 -0.4051 -0.3776 147  SER F CB  
16322 O  OG  . SER F  37  ? 3.4565 2.3327 3.0851 -0.5648 -0.3867 -0.3983 147  SER F OG  
16323 N  N   . LYS F  38  ? 3.1279 2.1662 2.7485 -0.5787 -0.3751 -0.4087 148  LYS F N   
16324 C  CA  . LYS F  38  ? 3.2696 2.3543 2.8999 -0.6177 -0.3498 -0.4527 148  LYS F CA  
16325 C  C   . LYS F  38  ? 3.6139 2.6906 3.1884 -0.6749 -0.3389 -0.4341 148  LYS F C   
16326 O  O   . LYS F  38  ? 3.8439 2.9080 3.3946 -0.7239 -0.3168 -0.4448 148  LYS F O   
16327 C  CB  . LYS F  38  ? 3.1656 2.3115 2.8440 -0.5811 -0.3471 -0.4781 148  LYS F CB  
16328 C  CG  . LYS F  38  ? 3.1181 2.2893 2.8451 -0.5227 -0.3533 -0.5008 148  LYS F CG  
16329 C  CD  . LYS F  38  ? 3.2192 2.4097 2.9679 -0.5410 -0.3414 -0.5523 148  LYS F CD  
16330 C  CE  . LYS F  38  ? 3.1733 2.4028 2.9641 -0.4784 -0.3530 -0.5793 148  LYS F CE  
16331 N  NZ  . LYS F  38  ? 3.0012 2.2881 2.8264 -0.4327 -0.3483 -0.5829 148  LYS F NZ  
16332 N  N   . LEU F  39  ? 3.4961 2.5844 3.0505 -0.6692 -0.3532 -0.4073 149  LEU F N   
16333 C  CA  . LEU F  39  ? 3.3914 2.4913 2.8898 -0.7186 -0.3458 -0.3991 149  LEU F CA  
16334 C  C   . LEU F  39  ? 3.6491 2.6962 3.0762 -0.7418 -0.3555 -0.3440 149  LEU F C   
16335 O  O   . LEU F  39  ? 3.7216 2.7811 3.0879 -0.7813 -0.3497 -0.3319 149  LEU F O   
16336 C  CB  . LEU F  39  ? 3.1182 2.2582 2.6304 -0.7050 -0.3597 -0.4005 149  LEU F CB  
16337 C  CG  . LEU F  39  ? 3.1121 2.3079 2.6457 -0.7308 -0.3347 -0.4552 149  LEU F CG  
16338 C  CD1 . LEU F  39  ? 3.1994 2.4265 2.7599 -0.7176 -0.3486 -0.4587 149  LEU F CD1 
16339 C  CD2 . LEU F  39  ? 3.1985 2.4026 2.6665 -0.7913 -0.3124 -0.4675 149  LEU F CD2 
16340 N  N   . THR F  40  ? 3.6047 2.5950 3.0361 -0.7159 -0.3692 -0.3100 150  THR F N   
16341 C  CA  . THR F  40  ? 3.4875 2.4198 2.8576 -0.7332 -0.3755 -0.2517 150  THR F CA  
16342 C  C   . THR F  40  ? 3.2292 2.0950 2.6269 -0.7151 -0.3733 -0.2410 150  THR F C   
16343 O  O   . THR F  40  ? 3.1253 1.9951 2.5815 -0.6748 -0.3810 -0.2691 150  THR F O   
16344 C  CB  . THR F  40  ? 3.5244 2.4590 2.8628 -0.7090 -0.4115 -0.2004 150  THR F CB  
16345 O  OG1 . THR F  40  ? 3.4883 2.3668 2.7654 -0.7209 -0.4172 -0.1381 150  THR F OG1 
16346 C  CG2 . THR F  40  ? 3.5534 2.4858 2.9522 -0.6482 -0.4366 -0.1953 150  THR F CG2 
16347 N  N   . SER F  41  ? 3.2420 2.0474 2.5968 -0.7448 -0.3605 -0.2007 151  SER F N   
16348 C  CA  . SER F  41  ? 3.3807 2.1096 2.7626 -0.7323 -0.3567 -0.1862 151  SER F CA  
16349 C  C   . SER F  41  ? 3.4497 2.1241 2.8075 -0.6956 -0.3856 -0.1173 151  SER F C   
16350 O  O   . SER F  41  ? 3.3758 1.9948 2.7723 -0.6648 -0.3915 -0.1128 151  SER F O   
16351 C  CB  . SER F  41  ? 3.5872 2.2732 2.9555 -0.7895 -0.3158 -0.1854 151  SER F CB  
16352 O  OG  . SER F  41  ? 3.7795 2.4628 3.0666 -0.8256 -0.3044 -0.1342 151  SER F OG  
16353 N  N   . ASN F  42  ? 3.3732 2.0668 2.6704 -0.6971 -0.4044 -0.0674 152  ASN F N   
16354 C  CA  . ASN F  42  ? 3.4234 2.0801 2.7004 -0.6582 -0.4364 -0.0002 152  ASN F CA  
16355 C  C   . ASN F  42  ? 3.4097 2.1188 2.7290 -0.6078 -0.4700 -0.0139 152  ASN F C   
16356 O  O   . ASN F  42  ? 3.2549 2.0214 2.5526 -0.6041 -0.4928 -0.0014 152  ASN F O   
16357 C  CB  . ASN F  42  ? 3.5195 2.1807 2.7093 -0.6828 -0.4427 0.0610  152  ASN F CB  
16358 C  CG  . ASN F  42  ? 3.8626 2.4926 3.0060 -0.7390 -0.4005 0.0697  152  ASN F CG  
16359 O  OD1 . ASN F  42  ? 3.8326 2.5182 2.9292 -0.7785 -0.3854 0.0519  152  ASN F OD1 
16360 N  ND2 . ASN F  42  ? 4.1665 2.7066 3.3286 -0.7442 -0.3770 0.0942  152  ASN F ND2 
16361 N  N   . PHE F  43  ? 3.6033 2.2952 2.9869 -0.5685 -0.4714 -0.0421 153  PHE F N   
16362 C  CA  . PHE F  43  ? 3.4600 2.2000 2.8908 -0.5189 -0.4935 -0.0559 153  PHE F CA  
16363 C  C   . PHE F  43  ? 3.5092 2.1997 2.9698 -0.4650 -0.5104 -0.0242 153  PHE F C   
16364 O  O   . PHE F  43  ? 3.6775 2.3163 3.1643 -0.4529 -0.4972 -0.0437 153  PHE F O   
16365 C  CB  . PHE F  43  ? 3.2274 2.0134 2.7058 -0.5143 -0.4761 -0.1246 153  PHE F CB  
16366 C  CG  . PHE F  43  ? 3.2708 2.0802 2.8036 -0.4535 -0.4885 -0.1348 153  PHE F CG  
16367 C  CD1 . PHE F  43  ? 3.3183 2.1753 2.8686 -0.4286 -0.5063 -0.1151 153  PHE F CD1 
16368 C  CD2 . PHE F  43  ? 3.3895 2.1782 2.9581 -0.4214 -0.4808 -0.1660 153  PHE F CD2 
16369 C  CE1 . PHE F  43  ? 3.4288 2.3082 3.0304 -0.3725 -0.5110 -0.1185 153  PHE F CE1 
16370 C  CE2 . PHE F  43  ? 3.5629 2.3788 3.1724 -0.3617 -0.4889 -0.1721 153  PHE F CE2 
16371 C  CZ  . PHE F  43  ? 3.5889 2.4482 3.2146 -0.3372 -0.5014 -0.1445 153  PHE F CZ  
16372 N  N   . ARG F  44  ? 3.2143 1.9256 2.6769 -0.4328 -0.5394 0.0189  154  ARG F N   
16373 C  CA  . ARG F  44  ? 3.1148 1.7938 2.6139 -0.3753 -0.5557 0.0477  154  ARG F CA  
16374 C  C   . ARG F  44  ? 3.0420 1.7924 2.5842 -0.3378 -0.5737 0.0466  154  ARG F C   
16375 O  O   . ARG F  44  ? 3.1771 1.9831 2.7074 -0.3556 -0.5891 0.0586  154  ARG F O   
16376 C  CB  . ARG F  44  ? 3.3390 1.9611 2.8034 -0.3705 -0.5723 0.1175  154  ARG F CB  
16377 C  CG  . ARG F  44  ? 3.6274 2.1662 3.0573 -0.4057 -0.5483 0.1296  154  ARG F CG  
16378 C  CD  . ARG F  44  ? 3.7554 2.2273 3.1616 -0.3867 -0.5621 0.2065  154  ARG F CD  
16379 N  NE  . ARG F  44  ? 3.7523 2.2771 3.1155 -0.3835 -0.5945 0.2599  154  ARG F NE  
16380 C  CZ  . ARG F  44  ? 3.7159 2.2038 3.0498 -0.3632 -0.6136 0.3348  154  ARG F CZ  
16381 N  NH1 . ARG F  44  ? 3.7742 2.1611 3.1217 -0.3451 -0.5990 0.3679  154  ARG F NH1 
16382 N  NH2 . ARG F  44  ? 3.6794 2.2331 2.9745 -0.3593 -0.6480 0.3750  154  ARG F NH2 
16383 N  N   . LEU F  45  ? 3.0011 1.7529 2.5956 -0.2869 -0.5696 0.0298  155  LEU F N   
16384 C  CA  . LEU F  45  ? 3.0694 1.8866 2.7139 -0.2498 -0.5775 0.0306  155  LEU F CA  
16385 C  C   . LEU F  45  ? 3.2023 2.0002 2.8858 -0.1884 -0.5877 0.0601  155  LEU F C   
16386 O  O   . LEU F  45  ? 3.3986 2.1355 3.0805 -0.1663 -0.5812 0.0571  155  LEU F O   
16387 C  CB  . LEU F  45  ? 3.1019 1.9629 2.7747 -0.2445 -0.5536 -0.0223 155  LEU F CB  
16388 C  CG  . LEU F  45  ? 3.2278 2.0772 2.9276 -0.1963 -0.5376 -0.0516 155  LEU F CG  
16389 C  CD1 . LEU F  45  ? 3.0489 1.9570 2.7727 -0.1884 -0.5177 -0.0910 155  LEU F CD1 
16390 C  CD2 . LEU F  45  ? 3.4301 2.2131 3.1032 -0.2099 -0.5305 -0.0747 155  LEU F CD2 
16391 N  N   . GLY F  46  ? 3.0923 1.9450 2.8182 -0.1620 -0.6018 0.0848  156  GLY F N   
16392 C  CA  . GLY F  46  ? 3.0537 1.9032 2.8258 -0.1023 -0.6096 0.1139  156  GLY F CA  
16393 C  C   . GLY F  46  ? 2.9821 1.8956 2.8176 -0.0641 -0.5950 0.1030  156  GLY F C   
16394 O  O   . GLY F  46  ? 2.9724 1.9240 2.8157 -0.0803 -0.5764 0.0713  156  GLY F O   
16395 N  N   . PHE F  47  ? 3.0511 1.9772 2.9360 -0.0119 -0.6000 0.1320  157  PHE F N   
16396 C  CA  . PHE F  47  ? 2.9715 1.9553 2.9192 0.0289  -0.5785 0.1282  157  PHE F CA  
16397 C  C   . PHE F  47  ? 2.9752 1.9871 2.9844 0.0700  -0.5919 0.1707  157  PHE F C   
16398 O  O   . PHE F  47  ? 3.0041 1.9747 3.0057 0.0918  -0.6098 0.1956  157  PHE F O   
16399 C  CB  . PHE F  47  ? 3.0727 2.0387 3.0108 0.0694  -0.5483 0.0950  157  PHE F CB  
16400 C  CG  . PHE F  47  ? 3.0640 2.0875 3.0581 0.1194  -0.5211 0.1004  157  PHE F CG  
16401 C  CD1 . PHE F  47  ? 3.0979 2.1718 3.1151 0.1064  -0.5000 0.0907  157  PHE F CD1 
16402 C  CD2 . PHE F  47  ? 3.0436 2.0692 3.0697 0.1811  -0.5124 0.1176  157  PHE F CD2 
16403 C  CE1 . PHE F  47  ? 3.0813 2.2040 3.1510 0.1534  -0.4687 0.1043  157  PHE F CE1 
16404 C  CE2 . PHE F  47  ? 3.0647 2.1459 3.1395 0.2280  -0.4813 0.1276  157  PHE F CE2 
16405 C  CZ  . PHE F  47  ? 3.0851 2.2135 3.1809 0.2139  -0.4585 0.1242  157  PHE F CZ  
16406 N  N   . GLY F  48  ? 3.0124 2.0941 3.0902 0.0810  -0.5803 0.1790  158  GLY F N   
16407 C  CA  . GLY F  48  ? 3.0291 2.1527 3.1826 0.1201  -0.5876 0.2152  158  GLY F CA  
16408 C  C   . GLY F  48  ? 2.9548 2.1412 3.1839 0.1438  -0.5517 0.2148  158  GLY F C   
16409 O  O   . GLY F  48  ? 2.9738 2.1823 3.2074 0.1155  -0.5319 0.1937  158  GLY F O   
16410 N  N   . SER F  49  ? 2.8111 2.0254 3.1042 0.1977  -0.5395 0.2408  159  SER F N   
16411 C  CA  . SER F  49  ? 2.7116 1.9834 3.0809 0.2274  -0.4972 0.2494  159  SER F CA  
16412 C  C   . SER F  49  ? 2.7625 2.0982 3.2372 0.2399  -0.5063 0.2826  159  SER F C   
16413 O  O   . SER F  49  ? 2.8106 2.1426 3.2949 0.2529  -0.5406 0.3021  159  SER F O   
16414 C  CB  . SER F  49  ? 2.7394 1.9928 3.0837 0.2908  -0.4585 0.2437  159  SER F CB  
16415 O  OG  . SER F  49  ? 2.8803 2.1035 3.2155 0.3322  -0.4730 0.2536  159  SER F OG  
16416 N  N   . PHE F  50  ? 2.6683 2.0639 3.2295 0.2365  -0.4739 0.2897  160  PHE F N   
16417 C  CA  . PHE F  50  ? 2.7799 2.2476 3.4611 0.2438  -0.4768 0.3158  160  PHE F CA  
16418 C  C   . PHE F  50  ? 2.5751 2.0865 3.3405 0.2736  -0.4137 0.3316  160  PHE F C   
16419 O  O   . PHE F  50  ? 2.3891 1.8814 3.1225 0.2755  -0.3741 0.3223  160  PHE F O   
16420 C  CB  . PHE F  50  ? 2.9757 2.4849 3.6985 0.1787  -0.5182 0.3036  160  PHE F CB  
16421 C  CG  . PHE F  50  ? 2.9425 2.4623 3.6834 0.1306  -0.4943 0.2771  160  PHE F CG  
16422 C  CD1 . PHE F  50  ? 3.0828 2.5511 3.7246 0.0937  -0.5028 0.2467  160  PHE F CD1 
16423 C  CD2 . PHE F  50  ? 2.7977 2.3778 3.6634 0.1219  -0.4603 0.2821  160  PHE F CD2 
16424 C  CE1 . PHE F  50  ? 3.0468 2.5233 3.7102 0.0530  -0.4796 0.2209  160  PHE F CE1 
16425 C  CE2 . PHE F  50  ? 2.7928 2.3745 3.6832 0.0795  -0.4351 0.2577  160  PHE F CE2 
16426 C  CZ  . PHE F  50  ? 2.9134 2.4435 3.7012 0.0466  -0.4460 0.2265  160  PHE F CZ  
16427 N  N   . VAL F  51  ? 2.6288 2.2025 3.5062 0.2988  -0.4032 0.3590  161  VAL F N   
16428 C  CA  . VAL F  51  ? 2.4731 2.0961 3.4506 0.3230  -0.3392 0.3818  161  VAL F CA  
16429 C  C   . VAL F  51  ? 2.4609 2.1640 3.5871 0.2923  -0.3486 0.3906  161  VAL F C   
16430 O  O   . VAL F  51  ? 2.4972 2.2246 3.6877 0.2421  -0.3381 0.3766  161  VAL F O   
16431 C  CB  . VAL F  51  ? 2.4581 2.0815 3.4267 0.4027  -0.2972 0.4076  161  VAL F CB  
16432 C  CG1 . VAL F  51  ? 2.4233 2.0972 3.4870 0.4286  -0.2237 0.4384  161  VAL F CG1 
16433 C  CG2 . VAL F  51  ? 2.5640 2.1158 3.3895 0.4321  -0.2945 0.3880  161  VAL F CG2 
16434 N  N   . GLU F  52  ? 2.3079 2.0544 3.4953 0.3216  -0.3702 0.4092  162  GLU F N   
16435 C  CA  . GLU F  52  ? 2.2681 2.1061 3.6138 0.3024  -0.3759 0.4175  162  GLU F CA  
16436 C  C   . GLU F  52  ? 2.2939 2.1661 3.6703 0.3437  -0.4133 0.4360  162  GLU F C   
16437 O  O   . GLU F  52  ? 2.4022 2.2250 3.6955 0.3963  -0.4135 0.4478  162  GLU F O   
16438 C  CB  . GLU F  52  ? 2.3405 2.2209 3.8031 0.3183  -0.2956 0.4411  162  GLU F CB  
16439 C  CG  . GLU F  52  ? 2.3985 2.3736 4.0437 0.2835  -0.2935 0.4408  162  GLU F CG  
16440 C  CD  . GLU F  52  ? 2.3882 2.3733 4.0638 0.2030  -0.3245 0.3992  162  GLU F CD  
16441 O  OE1 . GLU F  52  ? 2.3814 2.3755 4.0141 0.1690  -0.4000 0.3700  162  GLU F OE1 
16442 O  OE2 . GLU F  52  ? 2.3678 2.3506 4.1082 0.1759  -0.2711 0.3964  162  GLU F OE2 
16443 N  N   . LYS F  53  ? 2.1693 2.1292 3.6727 0.3210  -0.4447 0.4354  163  LYS F N   
16444 C  CA  . LYS F  53  ? 2.2241 2.2308 3.7778 0.3636  -0.4805 0.4560  163  LYS F CA  
16445 C  C   . LYS F  53  ? 2.3015 2.3322 3.9256 0.4315  -0.4149 0.4879  163  LYS F C   
16446 O  O   . LYS F  53  ? 2.2948 2.3784 4.0338 0.4268  -0.3561 0.4975  163  LYS F O   
16447 C  CB  . LYS F  53  ? 2.2833 2.3945 3.9644 0.3230  -0.5322 0.4432  163  LYS F CB  
16448 C  CG  . LYS F  53  ? 2.3230 2.4254 3.9267 0.2654  -0.6075 0.4127  163  LYS F CG  
16449 C  CD  . LYS F  53  ? 2.3564 2.5788 4.0858 0.2373  -0.6653 0.3986  163  LYS F CD  
16450 C  CE  . LYS F  53  ? 2.3039 2.5271 3.9440 0.1861  -0.7421 0.3693  163  LYS F CE  
16451 N  NZ  . LYS F  53  ? 2.3128 2.4595 3.7982 0.2200  -0.7847 0.3957  163  LYS F NZ  
16452 N  N   . PRO F  54  ? 2.3687 2.3604 3.9300 0.4955  -0.4177 0.5045  164  PRO F N   
16453 C  CA  . PRO F  54  ? 2.4017 2.4131 4.0125 0.5643  -0.3500 0.5298  164  PRO F CA  
16454 C  C   . PRO F  54  ? 2.4360 2.5595 4.2247 0.5847  -0.3414 0.5504  164  PRO F C   
16455 O  O   . PRO F  54  ? 2.5830 2.7217 4.3955 0.6472  -0.3388 0.5672  164  PRO F O   
16456 C  CB  . PRO F  54  ? 2.3787 2.3091 3.8648 0.6194  -0.3674 0.5289  164  PRO F CB  
16457 C  CG  . PRO F  54  ? 2.2924 2.1999 3.7341 0.5889  -0.4530 0.5205  164  PRO F CG  
16458 C  CD  . PRO F  54  ? 2.3091 2.2325 3.7507 0.5079  -0.4794 0.5001  164  PRO F CD  
16459 N  N   . VAL F  55  ? 2.3243 2.5286 4.2471 0.5329  -0.3367 0.5454  165  VAL F N   
16460 C  CA  . VAL F  55  ? 2.3029 2.6255 4.4141 0.5443  -0.3285 0.5595  165  VAL F CA  
16461 C  C   . VAL F  55  ? 2.1291 2.5042 4.3700 0.5112  -0.2554 0.5649  165  VAL F C   
16462 O  O   . VAL F  55  ? 2.0725 2.4096 4.2811 0.4580  -0.2416 0.5484  165  VAL F O   
16463 C  CB  . VAL F  55  ? 2.3808 2.7734 4.5564 0.5091  -0.4214 0.5413  165  VAL F CB  
16464 C  CG1 . VAL F  55  ? 2.4508 2.9691 4.8155 0.5376  -0.4188 0.5564  165  VAL F CG1 
16465 C  CG2 . VAL F  55  ? 2.3930 2.7137 4.4183 0.5285  -0.4945 0.5399  165  VAL F CG2 
16466 N  N   . SER F  56  ? 2.0972 2.5571 4.4898 0.5454  -0.2033 0.5903  166  SER F N   
16467 C  CA  . SER F  56  ? 2.0733 2.5980 4.6279 0.5119  -0.1334 0.5999  166  SER F CA  
16468 C  C   . SER F  56  ? 2.0455 2.6273 4.7020 0.4274  -0.1916 0.5593  166  SER F C   
16469 O  O   . SER F  56  ? 2.0499 2.6750 4.7148 0.4148  -0.2792 0.5353  166  SER F O   
16470 C  CB  . SER F  56  ? 2.0862 2.7055 4.7979 0.5628  -0.0774 0.6322  166  SER F CB  
16471 O  OG  . SER F  56  ? 2.0786 2.7303 4.9099 0.5489  0.0193  0.6573  166  SER F OG  
16472 N  N   . PRO F  57  ? 2.0243 2.6098 4.7620 0.3713  -0.1428 0.5507  167  PRO F N   
16473 C  CA  . PRO F  57  ? 2.0269 2.5738 4.7827 0.3830  -0.0346 0.5864  167  PRO F CA  
16474 C  C   . PRO F  57  ? 2.0295 2.4537 4.5958 0.3817  -0.0189 0.5875  167  PRO F C   
16475 O  O   . PRO F  57  ? 2.0375 2.4275 4.6078 0.3912  0.0663  0.6189  167  PRO F O   
16476 C  CB  . PRO F  57  ? 2.0085 2.6274 4.9715 0.3119  -0.0076 0.5680  167  PRO F CB  
16477 C  CG  . PRO F  57  ? 1.9916 2.6287 4.9440 0.2462  -0.1104 0.5057  167  PRO F CG  
16478 C  CD  . PRO F  57  ? 2.0037 2.6473 4.8464 0.2883  -0.1970 0.5007  167  PRO F CD  
16479 N  N   . PHE F  58  ? 2.1312 2.4939 4.5381 0.3710  -0.0986 0.5561  168  PHE F N   
16480 C  CA  . PHE F  58  ? 2.0601 2.3155 4.2988 0.3621  -0.0912 0.5490  168  PHE F CA  
16481 C  C   . PHE F  58  ? 2.0537 2.2491 4.1686 0.4381  -0.0325 0.5871  168  PHE F C   
16482 O  O   . PHE F  58  ? 2.0569 2.1862 4.0814 0.4394  0.0077  0.5950  168  PHE F O   
16483 C  CB  . PHE F  58  ? 2.1390 2.3518 4.2495 0.3300  -0.1889 0.5063  168  PHE F CB  
16484 C  CG  . PHE F  58  ? 2.2245 2.5038 4.4375 0.2589  -0.2523 0.4639  168  PHE F CG  
16485 C  CD1 . PHE F  58  ? 2.2350 2.5579 4.5961 0.2020  -0.2174 0.4470  168  PHE F CD1 
16486 C  CD2 . PHE F  58  ? 2.3392 2.6405 4.5044 0.2507  -0.3453 0.4406  168  PHE F CD2 
16487 C  CE1 . PHE F  58  ? 2.2910 2.6837 4.7495 0.1359  -0.2780 0.3974  168  PHE F CE1 
16488 C  CE2 . PHE F  58  ? 2.3680 2.7432 4.6201 0.1890  -0.4069 0.3986  168  PHE F CE2 
16489 C  CZ  . PHE F  58  ? 2.3245 2.7486 4.7236 0.1305  -0.3750 0.3720  168  PHE F CZ  
16490 N  N   . VAL F  59  ? 2.1322 2.3529 4.2395 0.5038  -0.0288 0.6074  169  VAL F N   
16491 C  CA  . VAL F  59  ? 2.1115 2.2919 4.1139 0.5806  0.0291  0.6371  169  VAL F CA  
16492 C  C   . VAL F  59  ? 2.1724 2.4352 4.3052 0.6324  0.0907  0.6747  169  VAL F C   
16493 O  O   . VAL F  59  ? 2.2833 2.6196 4.5378 0.6281  0.0578  0.6693  169  VAL F O   
16494 C  CB  . VAL F  59  ? 2.1341 2.2457 3.9647 0.6171  -0.0291 0.6143  169  VAL F CB  
16495 C  CG1 . VAL F  59  ? 2.1708 2.2347 3.8764 0.6856  0.0295  0.6306  169  VAL F CG1 
16496 C  CG2 . VAL F  59  ? 2.1143 2.1627 3.8461 0.5569  -0.1032 0.5748  169  VAL F CG2 
16497 N  N   . LYS F  60  ? 2.1649 2.4218 4.2711 0.6845  0.1802  0.7135  170  LYS F N   
16498 C  CA  . LYS F  60  ? 2.2866 2.6212 4.5026 0.7403  0.2475  0.7513  170  LYS F CA  
16499 C  C   . LYS F  60  ? 2.2620 2.6038 4.4267 0.7997  0.2065  0.7359  170  LYS F C   
16500 O  O   . LYS F  60  ? 2.2315 2.4984 4.2322 0.8238  0.1624  0.7097  170  LYS F O   
16501 C  CB  . LYS F  60  ? 2.3271 2.6518 4.4994 0.7905  0.3531  0.7993  170  LYS F CB  
16502 C  CG  . LYS F  60  ? 2.3258 2.6763 4.6307 0.7461  0.4241  0.8361  170  LYS F CG  
16503 C  CD  . LYS F  60  ? 2.3814 2.7393 4.6592 0.8097  0.5375  0.8983  170  LYS F CD  
16504 C  CE  . LYS F  60  ? 2.3931 2.7747 4.8244 0.7684  0.6185  0.9445  170  LYS F CE  
16505 N  NZ  . LYS F  60  ? 2.3429 2.6579 4.7543 0.6975  0.5859  0.9221  170  LYS F NZ  
16506 N  N   . THR F  61  ? 2.2208 2.6536 4.5376 0.8225  0.2227  0.7508  171  THR F N   
16507 C  CA  . THR F  61  ? 2.2458 2.6960 4.5513 0.8768  0.1823  0.7373  171  THR F CA  
16508 C  C   . THR F  61  ? 2.2999 2.7742 4.5864 0.9661  0.2633  0.7635  171  THR F C   
16509 O  O   . THR F  61  ? 2.3550 2.8829 4.7128 1.0131  0.2594  0.7636  171  THR F O   
16510 C  CB  . THR F  61  ? 2.2198 2.7638 4.7084 0.8464  0.1339  0.7304  171  THR F CB  
16511 O  OG1 . THR F  61  ? 2.2012 2.8336 4.8751 0.8160  0.1996  0.7568  171  THR F OG1 
16512 C  CG2 . THR F  61  ? 2.1860 2.6984 4.6419 0.7778  0.0301  0.6934  171  THR F CG2 
16513 N  N   . THR F  62  ? 2.3942 2.8342 4.5835 0.9940  0.3372  0.7854  172  THR F N   
16514 C  CA  . THR F  62  ? 2.4342 2.8935 4.5704 1.0829  0.4131  0.8051  172  THR F CA  
16515 C  C   . THR F  62  ? 2.4282 2.8049 4.3716 1.1306  0.3694  0.7626  172  THR F C   
16516 O  O   . THR F  62  ? 2.4262 2.7188 4.2400 1.0971  0.3186  0.7348  172  THR F O   
16517 C  CB  . THR F  62  ? 2.4320 2.9016 4.5500 1.0956  0.5137  0.8527  172  THR F CB  
16518 O  OG1 . THR F  62  ? 2.4010 2.7850 4.3802 1.0611  0.4893  0.8406  172  THR F OG1 
16519 C  CG2 . THR F  62  ? 2.3904 2.9410 4.7199 1.0512  0.5695  0.8964  172  THR F CG2 
16520 N  N   . PRO F  63  ? 2.4815 2.8815 4.4116 1.2073  0.3900  0.7531  173  PRO F N   
16521 C  CA  . PRO F  63  ? 2.5224 2.8420 4.2925 1.2489  0.3428  0.7031  173  PRO F CA  
16522 C  C   . PRO F  63  ? 2.5418 2.7856 4.1239 1.2527  0.3491  0.6837  173  PRO F C   
16523 O  O   . PRO F  63  ? 2.5542 2.7151 4.0150 1.2493  0.2861  0.6358  173  PRO F O   
16524 C  CB  . PRO F  63  ? 2.5876 2.9627 4.3914 1.3382  0.3965  0.7030  173  PRO F CB  
16525 C  CG  . PRO F  63  ? 2.5878 3.0669 4.5265 1.3489  0.4900  0.7598  173  PRO F CG  
16526 C  CD  . PRO F  63  ? 2.5123 3.0135 4.5789 1.2599  0.4619  0.7844  173  PRO F CD  
16527 N  N   . GLU F  64  ? 2.6485 2.9194 4.2071 1.2599  0.4233  0.7210  174  GLU F N   
16528 C  CA  . GLU F  64  ? 2.5741 2.7848 3.9570 1.2690  0.4274  0.7041  174  GLU F CA  
16529 C  C   . GLU F  64  ? 2.5105 2.6582 3.8646 1.1845  0.3686  0.6952  174  GLU F C   
16530 O  O   . GLU F  64  ? 2.5149 2.5896 3.7274 1.1761  0.3227  0.6537  174  GLU F O   
16531 C  CB  . GLU F  64  ? 2.7025 2.9693 4.0630 1.3189  0.5312  0.7543  174  GLU F CB  
16532 C  CG  . GLU F  64  ? 2.6492 2.8702 3.8364 1.3326  0.5384  0.7447  174  GLU F CG  
16533 C  CD  . GLU F  64  ? 2.7077 2.9897 3.8736 1.3871  0.6429  0.8058  174  GLU F CD  
16534 O  OE1 . GLU F  64  ? 2.7418 3.0995 4.0161 1.4213  0.7144  0.8500  174  GLU F OE1 
16535 O  OE2 . GLU F  64  ? 2.7302 2.9879 3.7730 1.3978  0.6553  0.8125  174  GLU F OE2 
16536 N  N   . GLU F  65  ? 2.4559 2.6336 3.9478 1.1205  0.3695  0.7284  175  GLU F N   
16537 C  CA  . GLU F  65  ? 2.4755 2.6025 3.9514 1.0407  0.3240  0.7204  175  GLU F CA  
16538 C  C   . GLU F  65  ? 2.5878 2.6664 4.0586 0.9877  0.2213  0.6747  175  GLU F C   
16539 O  O   . GLU F  65  ? 2.4080 2.4485 3.8693 0.9182  0.1773  0.6624  175  GLU F O   
16540 C  CB  . GLU F  65  ? 2.4846 2.6650 4.1166 0.9942  0.3734  0.7695  175  GLU F CB  
16541 C  CG  . GLU F  65  ? 2.6037 2.7357 4.2023 0.9332  0.3658  0.7724  175  GLU F CG  
16542 C  CD  . GLU F  65  ? 2.7834 2.9634 4.5278 0.9064  0.4411  0.8271  175  GLU F CD  
16543 O  OE1 . GLU F  65  ? 2.8626 3.1030 4.6713 0.9576  0.5246  0.8746  175  GLU F OE1 
16544 O  OE2 . GLU F  65  ? 2.7734 2.9301 4.5718 0.8343  0.4204  0.8218  175  GLU F OE2 
16545 N  N   . ILE F  66  ? 2.6518 2.7310 4.1284 1.0214  0.1848  0.6516  176  ILE F N   
16546 C  CA  . ILE F  66  ? 2.5874 2.6116 4.0356 0.9831  0.0903  0.6142  176  ILE F CA  
16547 C  C   . ILE F  66  ? 2.6309 2.5611 3.9008 0.9964  0.0567  0.5701  176  ILE F C   
16548 O  O   . ILE F  66  ? 2.6093 2.4774 3.8153 0.9405  -0.0023 0.5462  176  ILE F O   
16549 C  CB  . ILE F  66  ? 2.3838 2.4504 3.9334 1.0149  0.0663  0.6155  176  ILE F CB  
16550 C  CG1 . ILE F  66  ? 2.4181 2.5882 4.1598 0.9939  0.0940  0.6534  176  ILE F CG1 
16551 C  CG2 . ILE F  66  ? 2.3869 2.3914 3.8956 0.9829  -0.0288 0.5855  176  ILE F CG2 
16552 C  CD1 . ILE F  66  ? 2.5953 2.8244 4.4519 1.0317  0.0762  0.6579  176  ILE F CD1 
16553 N  N   . ALA F  67  ? 2.5375 2.4610 3.7291 1.0703  0.0952  0.5549  177  ALA F N   
16554 C  CA  . ALA F  67  ? 2.5176 2.3615 3.5483 1.0861  0.0698  0.5056  177  ALA F CA  
16555 C  C   . ALA F  67  ? 2.5380 2.3694 3.4729 1.0729  0.0983  0.5064  177  ALA F C   
16556 O  O   . ALA F  67  ? 2.4906 2.2570 3.3031 1.0622  0.0641  0.4634  177  ALA F O   
16557 C  CB  . ALA F  67  ? 2.5648 2.4127 3.5520 1.1713  0.0983  0.4787  177  ALA F CB  
16558 N  N   . ASN F  68  ? 2.5028 2.3957 3.4971 1.0744  0.1617  0.5556  178  ASN F N   
16559 C  CA  . ASN F  68  ? 2.4590 2.3442 3.3747 1.0667  0.1933  0.5673  178  ASN F CA  
16560 C  C   . ASN F  68  ? 2.4105 2.3345 3.4483 1.0173  0.2257  0.6209  178  ASN F C   
16561 O  O   . ASN F  68  ? 2.4305 2.4163 3.5344 1.0502  0.3031  0.6718  178  ASN F O   
16562 C  CB  . ASN F  68  ? 2.5291 2.4503 3.3570 1.1518  0.2603  0.5732  178  ASN F CB  
16563 C  CG  . ASN F  68  ? 2.5336 2.4508 3.2746 1.1517  0.2894  0.5894  178  ASN F CG  
16564 O  OD1 . ASN F  68  ? 2.4968 2.3600 3.1862 1.0987  0.2417  0.5652  178  ASN F OD1 
16565 N  ND2 . ASN F  68  ? 2.5841 2.5616 3.3103 1.2136  0.3702  0.6343  178  ASN F ND2 
16566 N  N   . PRO F  69  ? 2.3824 2.2714 3.4559 0.9371  0.1711  0.6095  179  PRO F N   
16567 C  CA  . PRO F  69  ? 2.4194 2.3427 3.6200 0.8846  0.1995  0.6497  179  PRO F CA  
16568 C  C   . PRO F  69  ? 2.6331 2.5540 3.7947 0.8922  0.2604  0.6823  179  PRO F C   
16569 O  O   . PRO F  69  ? 2.7114 2.6597 3.9884 0.8577  0.3010  0.7214  179  PRO F O   
16570 C  CB  . PRO F  69  ? 2.3707 2.2534 3.5911 0.8018  0.1160  0.6148  179  PRO F CB  
16571 C  CG  . PRO F  69  ? 2.3578 2.1684 3.4247 0.8083  0.0589  0.5654  179  PRO F CG  
16572 C  CD  . PRO F  69  ? 2.3793 2.1994 3.3894 0.8906  0.0829  0.5586  179  PRO F CD  
16573 N  N   . CYS F  70  ? 2.6978 2.5900 3.7077 0.9383  0.2695  0.6677  180  CYS F N   
16574 C  CA  . CYS F  70  ? 2.6143 2.5130 3.5795 0.9615  0.3304  0.7061  180  CYS F CA  
16575 C  C   . CYS F  70  ? 2.7476 2.7092 3.7118 1.0456  0.4181  0.7570  180  CYS F C   
16576 O  O   . CYS F  70  ? 2.8547 2.8243 3.7286 1.0929  0.4638  0.7829  180  CYS F O   
16577 C  CB  . CYS F  70  ? 2.5313 2.3780 3.3336 0.9675  0.2914  0.6630  180  CYS F CB  
16578 S  SG  . CYS F  70  ? 2.3809 2.1548 3.1681 0.8715  0.2014  0.6089  180  CYS F SG  
16579 N  N   . SER F  71  ? 2.5109 2.5224 3.5717 1.0684  0.4431  0.7731  181  SER F N   
16580 C  CA  . SER F  71  ? 2.5310 2.6091 3.6008 1.1470  0.5325  0.8236  181  SER F CA  
16581 C  C   . SER F  71  ? 2.5386 2.6451 3.7067 1.1352  0.6151  0.9019  181  SER F C   
16582 O  O   . SER F  71  ? 2.5567 2.6324 3.8046 1.0630  0.5995  0.9096  181  SER F O   
16583 C  CB  . SER F  71  ? 2.5372 2.6630 3.7026 1.1689  0.5365  0.8179  181  SER F CB  
16584 O  OG  . SER F  71  ? 2.6072 2.8026 3.7826 1.2459  0.6278  0.8657  181  SER F OG  
16585 N  N   . SER F  72  ? 2.6744 2.8392 3.8367 1.2084  0.7074  0.9602  182  SER F N   
16586 C  CA  . SER F  72  ? 2.7972 2.9903 4.0559 1.2091  0.8022  1.0466  182  SER F CA  
16587 C  C   . SER F  72  ? 2.7625 2.9075 3.9433 1.1984  0.8099  1.0697  182  SER F C   
16588 O  O   . SER F  72  ? 2.7472 2.9011 4.0042 1.1977  0.8885  1.1446  182  SER F O   
16589 C  CB  . SER F  72  ? 2.8469 3.0567 4.3274 1.1337  0.8104  1.0640  182  SER F CB  
16590 O  OG  . SER F  72  ? 2.9525 3.1735 4.5394 1.1207  0.8986  1.1416  182  SER F OG  
16591 N  N   . ILE F  73  ? 2.6305 2.7246 3.6677 1.1914  0.7329  1.0085  183  ILE F N   
16592 C  CA  . ILE F  73  ? 2.6478 2.7022 3.6062 1.1875  0.7361  1.0258  183  ILE F CA  
16593 C  C   . ILE F  73  ? 2.7827 2.8741 3.5791 1.2889  0.7837  1.0566  183  ILE F C   
16594 O  O   . ILE F  73  ? 2.7884 2.8919 3.5844 1.3209  0.8566  1.1330  183  ILE F O   
16595 C  CB  . ILE F  73  ? 2.5797 2.5659 3.4772 1.1230  0.6315  0.9453  183  ILE F CB  
16596 C  CG1 . ILE F  73  ? 2.4848 2.4455 3.5320 1.0282  0.5835  0.9156  183  ILE F CG1 
16597 C  CG2 . ILE F  73  ? 2.8149 2.7658 3.6440 1.1205  0.6377  0.9634  183  ILE F CG2 
16598 C  CD1 . ILE F  73  ? 2.4231 2.3217 3.4094 0.9657  0.4835  0.8386  183  ILE F CD1 
16599 N  N   . PRO F  74  ? 3.0123 3.1240 3.6722 1.3426  0.7447  0.9979  184  PRO F N   
16600 C  CA  . PRO F  74  ? 2.9676 3.0598 3.5981 1.3226  0.6618  0.9075  184  PRO F CA  
16601 C  C   . PRO F  74  ? 2.8126 2.8455 3.3264 1.2911  0.5696  0.8289  184  PRO F C   
16602 O  O   . PRO F  74  ? 2.8202 2.8488 3.2358 1.3138  0.5734  0.8371  184  PRO F O   
16603 C  CB  . PRO F  74  ? 3.0868 3.2437 3.6335 1.4175  0.7012  0.9037  184  PRO F CB  
16604 C  CG  . PRO F  74  ? 3.1777 3.3729 3.6089 1.4900  0.7606  0.9551  184  PRO F CG  
16605 C  CD  . PRO F  74  ? 3.1569 3.3285 3.6836 1.4471  0.8048  1.0338  184  PRO F CD  
16606 N  N   . TYR F  75  ? 2.6702 2.6611 3.1976 1.2421  0.4908  0.7573  185  TYR F N   
16607 C  CA  . TYR F  75  ? 2.7099 2.6440 3.1347 1.2100  0.4065  0.6807  185  TYR F CA  
16608 C  C   . TYR F  75  ? 2.7787 2.6797 3.2201 1.1821  0.3406  0.6150  185  TYR F C   
16609 O  O   . TYR F  75  ? 2.6828 2.5931 3.2428 1.1602  0.3455  0.6319  185  TYR F O   
16610 C  CB  . TYR F  75  ? 2.6747 2.5587 3.1376 1.1328  0.3784  0.6871  185  TYR F CB  
16611 C  CG  . TYR F  75  ? 2.6873 2.5193 3.0437 1.1015  0.3008  0.6135  185  TYR F CG  
16612 C  CD1 . TYR F  75  ? 2.7531 2.6019 2.9715 1.1546  0.2993  0.5915  185  TYR F CD1 
16613 C  CD2 . TYR F  75  ? 2.6288 2.4017 3.0251 1.0192  0.2307  0.5674  185  TYR F CD2 
16614 C  CE1 . TYR F  75  ? 2.7841 2.5914 2.9185 1.1233  0.2310  0.5220  185  TYR F CE1 
16615 C  CE2 . TYR F  75  ? 2.6022 2.3286 2.9077 0.9885  0.1667  0.5037  185  TYR F CE2 
16616 C  CZ  . TYR F  75  ? 2.6470 2.3904 2.8277 1.0388  0.1679  0.4797  185  TYR F CZ  
16617 O  OH  . TYR F  75  ? 2.5374 2.2402 2.6410 1.0052  0.1062  0.4136  185  TYR F OH  
16618 N  N   . PHE F  76  ? 2.9046 2.7689 3.2317 1.1850  0.2805  0.5410  186  PHE F N   
16619 C  CA  . PHE F  76  ? 2.8571 2.6758 3.1878 1.1599  0.2168  0.4779  186  PHE F CA  
16620 C  C   . PHE F  76  ? 2.7852 2.5342 3.1391 1.0680  0.1483  0.4514  186  PHE F C   
16621 O  O   . PHE F  76  ? 2.7673 2.4888 3.0446 1.0456  0.1221  0.4251  186  PHE F O   
16622 C  CB  . PHE F  76  ? 3.0159 2.8337 3.2171 1.2175  0.1972  0.4086  186  PHE F CB  
16623 C  CG  . PHE F  76  ? 3.1838 2.9460 3.3923 1.1972  0.1388  0.3459  186  PHE F CG  
16624 C  CD1 . PHE F  76  ? 3.1788 2.9586 3.4504 1.2320  0.1561  0.3497  186  PHE F CD1 
16625 C  CD2 . PHE F  76  ? 3.2752 2.9664 3.4327 1.1447  0.0702  0.2862  186  PHE F CD2 
16626 C  CE1 . PHE F  76  ? 3.2352 2.9580 3.5185 1.2176  0.1046  0.2977  186  PHE F CE1 
16627 C  CE2 . PHE F  76  ? 3.2522 2.8847 3.4203 1.1272  0.0218  0.2365  186  PHE F CE2 
16628 C  CZ  . PHE F  76  ? 3.2280 2.8737 3.4586 1.1652  0.0384  0.2434  186  PHE F CZ  
16629 N  N   . CYS F  77  ? 2.7240 2.4518 3.1827 1.0174  0.1198  0.4583  187  CYS F N   
16630 C  CA  . CYS F  77  ? 2.7104 2.3777 3.1853 0.9334  0.0540  0.4327  187  CYS F CA  
16631 C  C   . CYS F  77  ? 2.6383 2.2788 3.1689 0.9121  0.0075  0.4139  187  CYS F C   
16632 O  O   . CYS F  77  ? 2.7328 2.4065 3.3157 0.9567  0.0299  0.4278  187  CYS F O   
16633 C  CB  . CYS F  77  ? 2.8365 2.5145 3.3974 0.8767  0.0702  0.4769  187  CYS F CB  
16634 S  SG  . CYS F  77  ? 3.3433 3.0807 4.0790 0.8704  0.1154  0.5395  187  CYS F SG  
16635 N  N   . LEU F  78  ? 2.5363 2.1181 3.0536 0.8459  -0.0564 0.3842  188  LEU F N   
16636 C  CA  . LEU F  78  ? 2.6698 2.2194 3.2287 0.8232  -0.1069 0.3710  188  LEU F CA  
16637 C  C   . LEU F  78  ? 2.6918 2.2940 3.3919 0.8090  -0.0967 0.4183  188  LEU F C   
16638 O  O   . LEU F  78  ? 2.6799 2.3236 3.4504 0.7828  -0.0670 0.4529  188  LEU F O   
16639 C  CB  . LEU F  78  ? 2.6941 2.1758 3.2043 0.7526  -0.1705 0.3387  188  LEU F CB  
16640 C  CG  . LEU F  78  ? 2.5860 2.0206 2.9718 0.7529  -0.1829 0.2889  188  LEU F CG  
16641 C  CD1 . LEU F  78  ? 2.5333 1.9032 2.8847 0.6802  -0.2416 0.2619  188  LEU F CD1 
16642 C  CD2 . LEU F  78  ? 2.6220 2.0423 2.9461 0.8186  -0.1751 0.2507  188  LEU F CD2 
16643 N  N   . PRO F  79  ? 2.5517 2.1551 3.3037 0.8268  -0.1203 0.4188  189  PRO F N   
16644 C  CA  . PRO F  79  ? 2.4457 2.1077 3.3394 0.8107  -0.1205 0.4576  189  PRO F CA  
16645 C  C   . PRO F  79  ? 2.5516 2.2047 3.4834 0.7275  -0.1700 0.4593  189  PRO F C   
16646 O  O   . PRO F  79  ? 2.7694 2.3629 3.6158 0.6836  -0.2100 0.4311  189  PRO F O   
16647 C  CB  . PRO F  79  ? 2.4286 2.0806 3.3455 0.8518  -0.1463 0.4495  189  PRO F CB  
16648 C  CG  . PRO F  79  ? 2.4804 2.0430 3.2703 0.8549  -0.1831 0.4026  189  PRO F CG  
16649 C  CD  . PRO F  79  ? 2.5486 2.1005 3.2401 0.8639  -0.1480 0.3820  189  PRO F CD  
16650 N  N   . THR F  80  ? 2.3478 2.0677 3.4143 0.7059  -0.1664 0.4891  190  THR F N   
16651 C  CA  . THR F  80  ? 2.3231 2.0522 3.4393 0.6286  -0.2110 0.4860  190  THR F CA  
16652 C  C   . THR F  80  ? 2.3634 2.0643 3.4608 0.6080  -0.2884 0.4717  190  THR F C   
16653 O  O   . THR F  80  ? 2.4890 2.2136 3.6384 0.6467  -0.3024 0.4847  190  THR F O   
16654 C  CB  . THR F  80  ? 2.3247 2.1430 3.6030 0.6119  -0.1789 0.5161  190  THR F CB  
16655 O  OG1 . THR F  80  ? 2.4368 2.2768 3.7335 0.6392  -0.0981 0.5402  190  THR F OG1 
16656 C  CG2 . THR F  80  ? 2.3435 2.1747 3.6700 0.5297  -0.2221 0.5016  190  THR F CG2 
16657 N  N   . PHE F  81  ? 2.4730 2.1237 3.4953 0.5504  -0.3362 0.4481  191  PHE F N   
16658 C  CA  . PHE F  81  ? 2.5076 2.1294 3.5007 0.5270  -0.4078 0.4415  191  PHE F CA  
16659 C  C   . PHE F  81  ? 2.5698 2.2068 3.5710 0.4489  -0.4487 0.4294  191  PHE F C   
16660 O  O   . PHE F  81  ? 2.5738 2.2043 3.5555 0.4105  -0.4261 0.4136  191  PHE F O   
16661 C  CB  . PHE F  81  ? 2.6759 2.2004 3.5356 0.5464  -0.4254 0.4202  191  PHE F CB  
16662 C  CG  . PHE F  81  ? 2.6600 2.1305 3.4153 0.5189  -0.4091 0.3903  191  PHE F CG  
16663 C  CD1 . PHE F  81  ? 2.6570 2.0931 3.3540 0.4533  -0.4474 0.3723  191  PHE F CD1 
16664 C  CD2 . PHE F  81  ? 2.6829 2.1438 3.3972 0.5621  -0.3555 0.3796  191  PHE F CD2 
16665 C  CE1 . PHE F  81  ? 2.6808 2.0732 3.2904 0.4300  -0.4319 0.3434  191  PHE F CE1 
16666 C  CE2 . PHE F  81  ? 2.6386 2.0594 3.2613 0.5413  -0.3439 0.3516  191  PHE F CE2 
16667 C  CZ  . PHE F  81  ? 2.6697 2.0555 3.2448 0.4746  -0.3819 0.3331  191  PHE F CZ  
16668 N  N   . GLY F  82  ? 2.6797 2.3404 3.7094 0.4292  -0.5094 0.4365  192  GLY F N   
16669 C  CA  . GLY F  82  ? 2.6377 2.3244 3.6723 0.3587  -0.5544 0.4210  192  GLY F CA  
16670 C  C   . GLY F  82  ? 2.5925 2.2003 3.4926 0.3150  -0.5720 0.3945  192  GLY F C   
16671 O  O   . GLY F  82  ? 2.5277 2.1379 3.4204 0.2695  -0.5541 0.3713  192  GLY F O   
16672 N  N   . PHE F  83  ? 2.6812 2.2175 3.4815 0.3283  -0.6040 0.3982  193  PHE F N   
16673 C  CA  . PHE F  83  ? 2.6527 2.1136 3.3286 0.2869  -0.6188 0.3744  193  PHE F CA  
16674 C  C   . PHE F  83  ? 2.7185 2.0910 3.3070 0.3219  -0.6289 0.3815  193  PHE F C   
16675 O  O   . PHE F  83  ? 2.6838 2.0531 3.2895 0.3514  -0.6604 0.4096  193  PHE F O   
16676 C  CB  . PHE F  83  ? 2.7315 2.2208 3.3915 0.2243  -0.6713 0.3672  193  PHE F CB  
16677 C  CG  . PHE F  83  ? 2.8321 2.2415 3.3613 0.1924  -0.6955 0.3561  193  PHE F CG  
16678 C  CD1 . PHE F  83  ? 2.8602 2.2198 3.3185 0.1631  -0.6663 0.3234  193  PHE F CD1 
16679 C  CD2 . PHE F  83  ? 2.9460 2.3324 3.4273 0.1936  -0.7449 0.3818  193  PHE F CD2 
16680 C  CE1 . PHE F  83  ? 2.9009 2.1919 3.2490 0.1312  -0.6842 0.3122  193  PHE F CE1 
16681 C  CE2 . PHE F  83  ? 3.0805 2.3919 3.4461 0.1627  -0.7599 0.3766  193  PHE F CE2 
16682 C  CZ  . PHE F  83  ? 3.0075 2.2724 3.3095 0.1294  -0.7286 0.3396  193  PHE F CZ  
16683 N  N   . LYS F  84  ? 2.9414 2.2437 3.4429 0.3183  -0.6027 0.3545  194  LYS F N   
16684 C  CA  . LYS F  84  ? 3.0800 2.2917 3.5027 0.3434  -0.6069 0.3494  194  LYS F CA  
16685 C  C   . LYS F  84  ? 3.0497 2.2001 3.3721 0.2866  -0.6242 0.3272  194  LYS F C   
16686 O  O   . LYS F  84  ? 2.9945 2.1475 3.2856 0.2545  -0.6026 0.2964  194  LYS F O   
16687 C  CB  . LYS F  84  ? 3.1245 2.3152 3.5407 0.3970  -0.5578 0.3288  194  LYS F CB  
16688 C  CG  . LYS F  84  ? 3.1998 2.4409 3.7054 0.4614  -0.5359 0.3517  194  LYS F CG  
16689 C  CD  . LYS F  84  ? 3.3052 2.5267 3.7863 0.5165  -0.4877 0.3271  194  LYS F CD  
16690 C  CE  . LYS F  84  ? 3.4615 2.7350 4.0292 0.5833  -0.4613 0.3495  194  LYS F CE  
16691 N  NZ  . LYS F  84  ? 3.5794 2.8414 4.1146 0.6418  -0.4138 0.3227  194  LYS F NZ  
16692 N  N   . HIS F  85  ? 3.0245 2.1213 3.3002 0.2761  -0.6604 0.3461  195  HIS F N   
16693 C  CA  . HIS F  85  ? 3.0533 2.0827 3.2332 0.2265  -0.6709 0.3294  195  HIS F CA  
16694 C  C   . HIS F  85  ? 3.1192 2.0630 3.2533 0.2518  -0.6440 0.3021  195  HIS F C   
16695 O  O   . HIS F  85  ? 3.0345 1.9231 3.1722 0.2899  -0.6494 0.3187  195  HIS F O   
16696 C  CB  . HIS F  85  ? 3.0830 2.0956 3.2321 0.2044  -0.7175 0.3687  195  HIS F CB  
16697 C  CG  . HIS F  85  ? 3.1365 2.0747 3.1884 0.1568  -0.7221 0.3590  195  HIS F CG  
16698 N  ND1 . HIS F  85  ? 3.0340 1.9814 3.0398 0.1011  -0.7101 0.3220  195  HIS F ND1 
16699 C  CD2 . HIS F  85  ? 3.3250 2.1774 3.3235 0.1569  -0.7330 0.3831  195  HIS F CD2 
16700 C  CE1 . HIS F  85  ? 3.0993 1.9757 3.0273 0.0675  -0.7133 0.3220  195  HIS F CE1 
16701 N  NE2 . HIS F  85  ? 3.2850 2.1002 3.2072 0.0991  -0.7259 0.3605  195  HIS F NE2 
16702 N  N   . ILE F  86  ? 3.2647 2.2006 3.3621 0.2327  -0.6156 0.2571  196  ILE F N   
16703 C  CA  . ILE F  86  ? 3.3095 2.1835 3.3720 0.2581  -0.5906 0.2189  196  ILE F CA  
16704 C  C   . ILE F  86  ? 3.2977 2.0909 3.2894 0.2117  -0.6011 0.2026  196  ILE F C   
16705 O  O   . ILE F  86  ? 3.2903 2.0069 3.2698 0.2287  -0.6032 0.2032  196  ILE F O   
16706 C  CB  . ILE F  86  ? 3.1385 2.0575 3.2024 0.2724  -0.5544 0.1794  196  ILE F CB  
16707 C  CG1 . ILE F  86  ? 3.1100 2.1066 3.2489 0.3181  -0.5361 0.2030  196  ILE F CG1 
16708 C  CG2 . ILE F  86  ? 3.0791 1.9476 3.1054 0.3012  -0.5342 0.1321  196  ILE F CG2 
16709 C  CD1 . ILE F  86  ? 3.0007 2.0412 3.1402 0.3439  -0.4954 0.1766  196  ILE F CD1 
16710 N  N   . LEU F  87  ? 3.2127 2.0205 3.1640 0.1526  -0.6042 0.1879  197  LEU F N   
16711 C  CA  . LEU F  87  ? 3.2734 2.0137 3.1607 0.1045  -0.6053 0.1669  197  LEU F CA  
16712 C  C   . LEU F  87  ? 3.2022 1.9389 3.0543 0.0517  -0.6323 0.2036  197  LEU F C   
16713 O  O   . LEU F  87  ? 3.1361 1.9348 2.9834 0.0159  -0.6384 0.2004  197  LEU F O   
16714 C  CB  . LEU F  87  ? 3.2666 2.0266 3.1291 0.0817  -0.5810 0.1099  197  LEU F CB  
16715 C  CG  . LEU F  87  ? 3.3809 2.0830 3.1887 0.0293  -0.5771 0.0795  197  LEU F CG  
16716 C  CD1 . LEU F  87  ? 3.6715 2.2872 3.4764 0.0489  -0.5720 0.0673  197  LEU F CD1 
16717 C  CD2 . LEU F  87  ? 3.2064 1.9481 3.0004 0.0113  -0.5566 0.0248  197  LEU F CD2 
16718 N  N   . PRO F  88  ? 3.1814 1.8491 3.0083 0.0474  -0.6476 0.2395  198  PRO F N   
16719 C  CA  . PRO F  88  ? 3.0846 1.7445 2.8570 -0.0052 -0.6680 0.2716  198  PRO F CA  
16720 C  C   . PRO F  88  ? 3.1353 1.7778 2.8552 -0.0640 -0.6476 0.2284  198  PRO F C   
16721 O  O   . PRO F  88  ? 3.1302 1.7267 2.8480 -0.0646 -0.6221 0.1849  198  PRO F O   
16722 C  CB  . PRO F  88  ? 3.2256 1.8003 2.9863 0.0148  -0.6787 0.3215  198  PRO F CB  
16723 C  CG  . PRO F  88  ? 3.3787 1.9441 3.2060 0.0843  -0.6748 0.3238  198  PRO F CG  
16724 C  CD  . PRO F  88  ? 3.3875 1.9846 3.2386 0.0960  -0.6462 0.2580  198  PRO F CD  
16725 N  N   . LEU F  89  ? 2.9699 1.6560 2.6505 -0.1132 -0.6597 0.2360  199  LEU F N   
16726 C  CA  . LEU F  89  ? 2.9976 1.6842 2.6369 -0.1683 -0.6386 0.1916  199  LEU F CA  
16727 C  C   . LEU F  89  ? 3.0319 1.6258 2.6300 -0.1942 -0.6209 0.1914  199  LEU F C   
16728 O  O   . LEU F  89  ? 3.1071 1.6510 2.6711 -0.2022 -0.6314 0.2438  199  LEU F O   
16729 C  CB  . LEU F  89  ? 3.0512 1.8042 2.6571 -0.2137 -0.6547 0.1986  199  LEU F CB  
16730 C  CG  . LEU F  89  ? 3.1551 1.9064 2.7077 -0.2332 -0.6832 0.2551  199  LEU F CG  
16731 C  CD1 . LEU F  89  ? 3.2774 1.9863 2.7541 -0.2894 -0.6652 0.2517  199  LEU F CD1 
16732 C  CD2 . LEU F  89  ? 3.1825 2.0332 2.7492 -0.2401 -0.7132 0.2600  199  LEU F CD2 
16733 N  N   . THR F  90  ? 3.1709 1.7442 2.7774 -0.2055 -0.5930 0.1333  200  THR F N   
16734 C  CA  . THR F  90  ? 3.3188 1.8074 2.9062 -0.2329 -0.5713 0.1200  200  THR F CA  
16735 C  C   . THR F  90  ? 3.3353 1.8499 2.9173 -0.2726 -0.5472 0.0524  200  THR F C   
16736 O  O   . THR F  90  ? 3.0351 1.6247 2.6322 -0.2667 -0.5466 0.0172  200  THR F O   
16737 C  CB  . THR F  90  ? 3.2895 1.7085 2.9198 -0.1852 -0.5651 0.1142  200  THR F CB  
16738 O  OG1 . THR F  90  ? 3.3855 1.7182 3.0087 -0.2183 -0.5417 0.0982  200  THR F OG1 
16739 C  CG2 . THR F  90  ? 3.1333 1.5994 2.8075 -0.1432 -0.5581 0.0557  200  THR F CG2 
16740 N  N   . ASN F  91  ? 3.6896 2.1409 3.2574 -0.3123 -0.5251 0.0358  201  ASN F N   
16741 C  CA  . ASN F  91  ? 3.6372 2.1162 3.2069 -0.3518 -0.5025 -0.0299 201  ASN F CA  
16742 C  C   . ASN F  91  ? 3.6158 2.1199 3.2343 -0.3130 -0.4975 -0.0961 201  ASN F C   
16743 O  O   . ASN F  91  ? 3.3789 1.9475 3.0046 -0.3224 -0.4898 -0.1464 201  ASN F O   
16744 C  CB  . ASN F  91  ? 3.6329 2.0396 3.1867 -0.4059 -0.4769 -0.0309 201  ASN F CB  
16745 C  CG  . ASN F  91  ? 3.5390 1.9360 3.0301 -0.4494 -0.4756 0.0301  201  ASN F CG  
16746 O  OD1 . ASN F  91  ? 3.5487 1.8944 3.0162 -0.4369 -0.4861 0.0989  201  ASN F OD1 
16747 N  ND2 . ASN F  91  ? 3.4076 1.8579 2.8696 -0.4975 -0.4623 0.0053  201  ASN F ND2 
16748 N  N   . ASP F  92  ? 3.8153 2.2735 3.4659 -0.2657 -0.5017 -0.0971 202  ASP F N   
16749 C  CA  . ASP F  92  ? 3.7514 2.2374 3.4399 -0.2230 -0.4981 -0.1614 202  ASP F CA  
16750 C  C   . ASP F  92  ? 3.5473 2.1310 3.2379 -0.1895 -0.5057 -0.1695 202  ASP F C   
16751 O  O   . ASP F  92  ? 3.5212 2.1272 3.2206 -0.1464 -0.5180 -0.1300 202  ASP F O   
16752 C  CB  . ASP F  92  ? 3.6839 2.1089 3.4032 -0.1719 -0.5021 -0.1548 202  ASP F CB  
16753 C  CG  . ASP F  92  ? 3.6100 2.0464 3.3627 -0.1404 -0.4943 -0.2357 202  ASP F CG  
16754 O  OD1 . ASP F  92  ? 3.6527 2.1278 3.4072 -0.1678 -0.4857 -0.2960 202  ASP F OD1 
16755 O  OD2 . ASP F  92  ? 3.4888 1.9010 3.2668 -0.0864 -0.4976 -0.2420 202  ASP F OD2 
16756 N  N   . ALA F  93  ? 3.2607 1.9032 2.9500 -0.2085 -0.4961 -0.2186 203  ALA F N   
16757 C  CA  . ALA F  93  ? 3.0263 1.7553 2.7200 -0.1827 -0.4974 -0.2212 203  ALA F CA  
16758 C  C   . ALA F  93  ? 3.0329 1.8050 2.7491 -0.1198 -0.4945 -0.2619 203  ALA F C   
16759 O  O   . ALA F  93  ? 3.0391 1.8712 2.7645 -0.0802 -0.4931 -0.2464 203  ALA F O   
16760 C  CB  . ALA F  93  ? 2.9272 1.6997 2.6079 -0.2336 -0.4871 -0.2458 203  ALA F CB  
16761 N  N   . GLU F  94  ? 3.1427 1.8868 2.8693 -0.1093 -0.4920 -0.3136 204  GLU F N   
16762 C  CA  . GLU F  94  ? 3.1460 1.9356 2.8846 -0.0447 -0.4916 -0.3558 204  GLU F CA  
16763 C  C   . GLU F  94  ? 3.2261 1.9932 2.9744 0.0131  -0.4956 -0.3220 204  GLU F C   
16764 O  O   . GLU F  94  ? 3.2381 2.0576 2.9892 0.0755  -0.4920 -0.3370 204  GLU F O   
16765 C  CB  . GLU F  94  ? 3.1749 1.9508 2.9262 -0.0560 -0.4904 -0.4351 204  GLU F CB  
16766 C  CG  . GLU F  94  ? 3.1318 1.9500 2.8842 -0.1037 -0.4855 -0.4793 204  GLU F CG  
16767 C  CD  . GLU F  94  ? 3.1636 2.0808 2.9071 -0.0705 -0.4844 -0.4841 204  GLU F CD  
16768 O  OE1 . GLU F  94  ? 3.1419 2.1064 2.8810 -0.0018 -0.4868 -0.4883 204  GLU F OE1 
16769 O  OE2 . GLU F  94  ? 3.2391 2.1857 2.9805 -0.1110 -0.4783 -0.4813 204  GLU F OE2 
16770 N  N   . ARG F  95  ? 3.2011 1.8956 2.9535 -0.0036 -0.5015 -0.2735 205  ARG F N   
16771 C  CA  . ARG F  95  ? 3.1693 1.8502 2.9380 0.0503  -0.5057 -0.2318 205  ARG F CA  
16772 C  C   . ARG F  95  ? 3.1057 1.8513 2.8787 0.0695  -0.5065 -0.1793 205  ARG F C   
16773 O  O   . ARG F  95  ? 3.2152 1.9902 3.0082 0.1276  -0.5025 -0.1598 205  ARG F O   
16774 C  CB  . ARG F  95  ? 3.2757 1.8624 3.0513 0.0287  -0.5133 -0.1914 205  ARG F CB  
16775 C  CG  . ARG F  95  ? 3.2427 1.8092 3.0443 0.0868  -0.5181 -0.1535 205  ARG F CG  
16776 C  CD  . ARG F  95  ? 3.2068 1.7828 3.0259 0.1466  -0.5082 -0.2098 205  ARG F CD  
16777 N  NE  . ARG F  95  ? 3.2296 1.7912 3.0775 0.2042  -0.5092 -0.1737 205  ARG F NE  
16778 C  CZ  . ARG F  95  ? 3.3453 1.8208 3.2172 0.2136  -0.5116 -0.1620 205  ARG F CZ  
16779 N  NH1 . ARG F  95  ? 3.4653 1.8564 3.3361 0.1668  -0.5107 -0.1806 205  ARG F NH1 
16780 N  NH2 . ARG F  95  ? 3.3007 1.7735 3.2041 0.2706  -0.5118 -0.1299 205  ARG F NH2 
16781 N  N   . PHE F  96  ? 2.9215 1.6907 2.6818 0.0201  -0.5089 -0.1591 206  PHE F N   
16782 C  CA  . PHE F  96  ? 2.8918 1.7238 2.6674 0.0307  -0.5074 -0.1197 206  PHE F CA  
16783 C  C   . PHE F  96  ? 2.8962 1.7984 2.6833 0.0811  -0.4894 -0.1429 206  PHE F C   
16784 O  O   . PHE F  96  ? 2.8642 1.8055 2.6789 0.1250  -0.4810 -0.1097 206  PHE F O   
16785 C  CB  . PHE F  96  ? 2.9040 1.7471 2.6629 -0.0350 -0.5114 -0.1101 206  PHE F CB  
16786 C  CG  . PHE F  96  ? 2.9672 1.8773 2.7506 -0.0311 -0.5056 -0.0876 206  PHE F CG  
16787 C  CD1 . PHE F  96  ? 3.0680 1.9914 2.8788 -0.0259 -0.5169 -0.0377 206  PHE F CD1 
16788 C  CD2 . PHE F  96  ? 2.8993 1.8600 2.6865 -0.0326 -0.4885 -0.1179 206  PHE F CD2 
16789 C  CE1 . PHE F  96  ? 2.9610 1.9436 2.8079 -0.0272 -0.5090 -0.0228 206  PHE F CE1 
16790 C  CE2 . PHE F  96  ? 2.8129 1.8258 2.6331 -0.0301 -0.4783 -0.0970 206  PHE F CE2 
16791 C  CZ  . PHE F  96  ? 2.8371 1.8592 2.6900 -0.0299 -0.4875 -0.0518 206  PHE F CZ  
16792 N  N   . ASN F  97  ? 2.9045 1.8278 2.6729 0.0768  -0.4821 -0.1976 207  ASN F N   
16793 C  CA  . ASN F  97  ? 2.9324 1.9277 2.7031 0.1291  -0.4659 -0.2156 207  ASN F CA  
16794 C  C   . ASN F  97  ? 3.0212 2.0270 2.7958 0.2020  -0.4593 -0.2171 207  ASN F C   
16795 O  O   . ASN F  97  ? 3.0941 2.1551 2.8800 0.2540  -0.4416 -0.1917 207  ASN F O   
16796 C  CB  . ASN F  97  ? 2.9188 1.9393 2.6691 0.1129  -0.4653 -0.2781 207  ASN F CB  
16797 C  CG  . ASN F  97  ? 3.0012 2.0265 2.7513 0.0485  -0.4650 -0.2778 207  ASN F CG  
16798 O  OD1 . ASN F  97  ? 3.1012 2.1337 2.8658 0.0287  -0.4610 -0.2338 207  ASN F OD1 
16799 N  ND2 . ASN F  97  ? 3.1234 2.1486 2.8622 0.0145  -0.4683 -0.3320 207  ASN F ND2 
16800 N  N   . GLU F  98  ? 3.2728 2.2244 3.0411 0.2072  -0.4697 -0.2466 208  GLU F N   
16801 C  CA  . GLU F  98  ? 3.3859 2.3453 3.1567 0.2766  -0.4628 -0.2595 208  GLU F CA  
16802 C  C   . GLU F  98  ? 3.3289 2.2967 3.1300 0.3130  -0.4537 -0.1940 208  GLU F C   
16803 O  O   . GLU F  98  ? 3.2771 2.2760 3.0816 0.3792  -0.4392 -0.1956 208  GLU F O   
16804 C  CB  . GLU F  98  ? 3.4229 2.3078 3.1939 0.2653  -0.4748 -0.3046 208  GLU F CB  
16805 C  CG  . GLU F  98  ? 3.3599 2.2462 3.1141 0.2387  -0.4811 -0.3831 208  GLU F CG  
16806 C  CD  . GLU F  98  ? 3.3509 2.1437 3.1215 0.2014  -0.4898 -0.4163 208  GLU F CD  
16807 O  OE1 . GLU F  98  ? 3.2345 1.9619 3.0245 0.2107  -0.4906 -0.3802 208  GLU F OE1 
16808 O  OE2 . GLU F  98  ? 3.4124 2.1968 3.1832 0.1630  -0.4939 -0.4770 208  GLU F OE2 
16809 N  N   . ILE F  99  ? 3.2428 2.1910 3.0674 0.2720  -0.4618 -0.1398 209  ILE F N   
16810 C  CA  . ILE F  99  ? 3.0490 2.0141 2.9153 0.3009  -0.4562 -0.0802 209  ILE F CA  
16811 C  C   . ILE F  99  ? 2.8467 1.8885 2.7349 0.3215  -0.4329 -0.0510 209  ILE F C   
16812 O  O   . ILE F  99  ? 2.7570 1.8372 2.6755 0.3751  -0.4125 -0.0219 209  ILE F O   
16813 C  CB  . ILE F  99  ? 2.9656 1.8827 2.8492 0.2496  -0.4802 -0.0391 209  ILE F CB  
16814 C  CG1 . ILE F  99  ? 2.9525 1.7853 2.8211 0.2385  -0.4965 -0.0564 209  ILE F CG1 
16815 C  CG2 . ILE F  99  ? 3.0070 1.9575 2.9445 0.2754  -0.4783 0.0189  209  ILE F CG2 
16816 C  CD1 . ILE F  99  ? 2.9519 1.7364 2.8222 0.1888  -0.5201 -0.0133 209  ILE F CD1 
16817 N  N   . VAL F  100 ? 2.7356 1.7983 2.6139 0.2797  -0.4315 -0.0575 210  VAL F N   
16818 C  CA  . VAL F  100 ? 2.6843 1.8094 2.5923 0.2947  -0.4059 -0.0281 210  VAL F CA  
16819 C  C   . VAL F  100 ? 2.6100 1.7867 2.5008 0.3668  -0.3773 -0.0388 210  VAL F C   
16820 O  O   . VAL F  100 ? 2.5405 1.7642 2.4656 0.4054  -0.3473 0.0022  210  VAL F O   
16821 C  CB  . VAL F  100 ? 2.7368 1.8660 2.6380 0.2346  -0.4106 -0.0408 210  VAL F CB  
16822 C  CG1 . VAL F  100 ? 2.7996 1.9796 2.7487 0.2419  -0.3834 -0.0054 210  VAL F CG1 
16823 C  CG2 . VAL F  100 ? 2.7443 1.8236 2.6417 0.1657  -0.4402 -0.0379 210  VAL F CG2 
16824 N  N   . LYS F  101 ? 2.8433 2.0157 2.6830 0.3873  -0.3849 -0.0938 211  LYS F N   
16825 C  CA  . LYS F  101 ? 2.9543 2.1869 2.7646 0.4591  -0.3621 -0.1094 211  LYS F CA  
16826 C  C   . LYS F  101 ? 2.9421 2.1935 2.7682 0.5245  -0.3408 -0.0801 211  LYS F C   
16827 O  O   . LYS F  101 ? 3.0090 2.3206 2.8370 0.5807  -0.3071 -0.0493 211  LYS F O   
16828 C  CB  . LYS F  101 ? 3.1943 2.4235 2.9519 0.4629  -0.3816 -0.1860 211  LYS F CB  
16829 C  CG  . LYS F  101 ? 3.2580 2.4768 3.0043 0.4004  -0.3994 -0.2199 211  LYS F CG  
16830 C  CD  . LYS F  101 ? 3.4354 2.6269 3.1527 0.3835  -0.4237 -0.2973 211  LYS F CD  
16831 C  CE  . LYS F  101 ? 3.4416 2.6196 3.1576 0.3143  -0.4386 -0.3294 211  LYS F CE  
16832 N  NZ  . LYS F  101 ? 3.4194 2.5680 3.1226 0.2914  -0.4587 -0.4052 211  LYS F NZ  
16833 N  N   . ASN F  102 ? 2.8540 2.0547 2.6949 0.5199  -0.3567 -0.0850 212  ASN F N   
16834 C  CA  . ASN F  102 ? 2.9845 2.2020 2.8410 0.5846  -0.3371 -0.0680 212  ASN F CA  
16835 C  C   . ASN F  102 ? 2.8455 2.0843 2.7707 0.5896  -0.3161 0.0052  212  ASN F C   
16836 O  O   . ASN F  102 ? 2.9133 2.1716 2.8635 0.6421  -0.2959 0.0257  212  ASN F O   
16837 C  CB  . ASN F  102 ? 3.2042 2.3549 3.0579 0.5809  -0.3612 -0.1050 212  ASN F CB  
16838 C  CG  . ASN F  102 ? 3.2763 2.3985 3.0797 0.5636  -0.3827 -0.1828 212  ASN F CG  
16839 O  OD1 . ASN F  102 ? 3.2100 2.3580 2.9836 0.5400  -0.3874 -0.2071 212  ASN F OD1 
16840 N  ND2 . ASN F  102 ? 3.3522 2.4207 3.1550 0.5741  -0.3949 -0.2244 212  ASN F ND2 
16841 N  N   . GLN F  103 ? 2.6347 1.8740 2.5969 0.5361  -0.3196 0.0396  213  GLN F N   
16842 C  CA  . GLN F  103 ? 2.5635 1.8253 2.6045 0.5318  -0.3039 0.1005  213  GLN F CA  
16843 C  C   . GLN F  103 ? 2.5255 1.8553 2.5911 0.5933  -0.2523 0.1384  213  GLN F C   
16844 O  O   . GLN F  103 ? 2.5313 1.8944 2.5695 0.6087  -0.2291 0.1392  213  GLN F O   
16845 C  CB  . GLN F  103 ? 2.5561 1.8054 2.6295 0.4571  -0.3214 0.1157  213  GLN F CB  
16846 C  CG  . GLN F  103 ? 2.6075 1.7948 2.6662 0.3978  -0.3682 0.0969  213  GLN F CG  
16847 C  CD  . GLN F  103 ? 2.7757 1.9447 2.8760 0.4099  -0.3844 0.1229  213  GLN F CD  
16848 O  OE1 . GLN F  103 ? 2.7645 1.9756 2.9284 0.4434  -0.3639 0.1609  213  GLN F OE1 
16849 N  NE2 . GLN F  103 ? 2.8810 1.9877 2.9509 0.3836  -0.4191 0.1048  213  GLN F NE2 
16850 N  N   . LYS F  104 ? 2.6366 1.9886 2.7554 0.6316  -0.2321 0.1728  214  LYS F N   
16851 C  CA  . LYS F  104 ? 2.7317 2.1480 2.8880 0.6878  -0.1765 0.2194  214  LYS F CA  
16852 C  C   . LYS F  104 ? 2.7048 2.1413 2.9706 0.6528  -0.1619 0.2736  214  LYS F C   
16853 O  O   . LYS F  104 ? 2.6985 2.1066 3.0079 0.5952  -0.1994 0.2725  214  LYS F O   
16854 C  CB  . LYS F  104 ? 2.8380 2.2753 2.9817 0.7610  -0.1564 0.2149  214  LYS F CB  
16855 C  CG  . LYS F  104 ? 2.6648 2.0916 2.7069 0.8009  -0.1683 0.1519  214  LYS F CG  
16856 C  CD  . LYS F  104 ? 2.5920 2.0480 2.6262 0.8778  -0.1415 0.1456  214  LYS F CD  
16857 C  CE  . LYS F  104 ? 2.6528 2.0959 2.5946 0.9122  -0.1596 0.0687  214  LYS F CE  
16858 N  NZ  . LYS F  104 ? 2.6746 2.0344 2.6088 0.8578  -0.2136 0.0172  214  LYS F NZ  
16859 N  N   . ILE F  105 ? 2.5791 2.0689 2.8908 0.6892  -0.1054 0.3211  215  ILE F N   
16860 C  CA  . ILE F  105 ? 2.3903 1.9061 2.8208 0.6576  -0.0826 0.3697  215  ILE F CA  
16861 C  C   . ILE F  105 ? 2.4231 1.9634 2.9315 0.6779  -0.0782 0.3923  215  ILE F C   
16862 O  O   . ILE F  105 ? 2.4653 2.0169 2.9405 0.7378  -0.0665 0.3865  215  ILE F O   
16863 C  CB  . ILE F  105 ? 2.2828 1.8400 2.7410 0.6880  -0.0166 0.4163  215  ILE F CB  
16864 C  CG1 . ILE F  105 ? 2.3271 1.8707 2.6860 0.6978  -0.0179 0.3926  215  ILE F CG1 
16865 C  CG2 . ILE F  105 ? 2.2299 1.7977 2.8135 0.6331  -0.0001 0.4505  215  ILE F CG2 
16866 C  CD1 . ILE F  105 ? 2.3338 1.9103 2.5991 0.7831  0.0100  0.3898  215  ILE F CD1 
16867 N  N   . SER F  106 ? 2.4351 1.9872 3.0502 0.6273  -0.0912 0.4121  216  SER F N   
16868 C  CA  . SER F  106 ? 2.3711 1.9650 3.0897 0.6441  -0.0804 0.4415  216  SER F CA  
16869 C  C   . SER F  106 ? 2.3379 1.9862 3.1771 0.6377  -0.0229 0.4903  216  SER F C   
16870 O  O   . SER F  106 ? 2.3191 1.9696 3.1448 0.6427  0.0201  0.5083  216  SER F O   
16871 C  CB  . SER F  106 ? 2.3313 1.9036 3.0804 0.5939  -0.1481 0.4213  216  SER F CB  
16872 O  OG  . SER F  106 ? 2.4070 1.9207 3.0507 0.6006  -0.1927 0.3821  216  SER F OG  
16873 N  N   . ALA F  107 ? 2.2230 1.9157 3.1870 0.6268  -0.0210 0.5124  217  ALA F N   
16874 C  CA  . ALA F  107 ? 2.1645 1.9095 3.2628 0.6154  0.0362  0.5557  217  ALA F CA  
16875 C  C   . ALA F  107 ? 2.1835 1.9766 3.4229 0.5811  0.0114  0.5599  217  ALA F C   
16876 O  O   . ALA F  107 ? 2.2150 2.0075 3.4443 0.5840  -0.0420 0.5403  217  ALA F O   
16877 C  CB  . ALA F  107 ? 2.1996 1.9817 3.3008 0.6914  0.1193  0.6022  217  ALA F CB  
16878 N  N   . ASN F  108 ? 2.1173 1.9536 3.4948 0.5497  0.0519  0.5860  218  ASN F N   
16879 C  CA  . ASN F  108 ? 2.0997 2.0032 3.6423 0.5203  0.0444  0.5936  218  ASN F CA  
16880 C  C   . ASN F  108 ? 2.0986 2.0400 3.7769 0.5087  0.1247  0.6332  218  ASN F C   
16881 O  O   . ASN F  108 ? 2.1740 2.0948 3.8077 0.5461  0.1915  0.6675  218  ASN F O   
16882 C  CB  . ASN F  108 ? 2.1214 2.0193 3.6788 0.4479  -0.0419 0.5475  218  ASN F CB  
16883 C  CG  . ASN F  108 ? 2.2018 2.0683 3.7591 0.3827  -0.0460 0.5247  218  ASN F CG  
16884 O  OD1 . ASN F  108 ? 2.2232 2.1301 3.9146 0.3294  -0.0420 0.5170  218  ASN F OD1 
16885 N  ND2 . ASN F  108 ? 2.2806 2.0776 3.6943 0.3866  -0.0529 0.5092  218  ASN F ND2 
16886 N  N   . ILE F  109 ? 2.0759 2.0733 3.9216 0.4570  0.1190  0.6285  219  ILE F N   
16887 C  CA  . ILE F  109 ? 2.1426 2.1769 4.1450 0.4410  0.1991  0.6652  219  ILE F CA  
16888 C  C   . ILE F  109 ? 2.0999 2.1152 4.1722 0.3585  0.1839  0.6330  219  ILE F C   
16889 O  O   . ILE F  109 ? 2.0681 2.0491 4.1578 0.3520  0.2451  0.6569  219  ILE F O   
16890 C  CB  . ILE F  109 ? 2.1936 2.3204 4.3689 0.4515  0.2241  0.6868  219  ILE F CB  
16891 C  CG1 . ILE F  109 ? 2.3119 2.4572 4.4147 0.5324  0.2293  0.7077  219  ILE F CG1 
16892 C  CG2 . ILE F  109 ? 2.1151 2.2726 4.4453 0.4455  0.3245  0.7352  219  ILE F CG2 
16893 C  CD1 . ILE F  109 ? 2.2406 2.4812 4.5115 0.5472  0.2514  0.7268  219  ILE F CD1 
16894 N  N   . ASP F  110 ? 2.1052 2.1426 4.2138 0.2980  0.1028  0.5783  220  ASP F N   
16895 C  CA  . ASP F  110 ? 2.1464 2.1901 4.3611 0.2165  0.0901  0.5397  220  ASP F CA  
16896 C  C   . ASP F  110 ? 2.2604 2.2273 4.3296 0.1852  0.0461  0.4997  220  ASP F C   
16897 O  O   . ASP F  110 ? 2.2890 2.2299 4.2172 0.1915  -0.0239 0.4729  220  ASP F O   
16898 C  CB  . ASP F  110 ? 2.1215 2.2500 4.4669 0.1682  0.0275  0.4984  220  ASP F CB  
16899 C  CG  . ASP F  110 ? 2.1412 2.2645 4.3602 0.1608  -0.0762 0.4572  220  ASP F CG  
16900 O  OD1 . ASP F  110 ? 2.0974 2.1617 4.1465 0.2078  -0.0922 0.4702  220  ASP F OD1 
16901 O  OD2 . ASP F  110 ? 2.1490 2.3302 4.4413 0.1088  -0.1408 0.4119  220  ASP F OD2 
16902 N  N   . THR F  111 ? 2.2533 2.1827 4.3645 0.1530  0.0924  0.4983  221  THR F N   
16903 C  CA  . THR F  111 ? 2.2525 2.1065 4.2335 0.1334  0.0723  0.4699  221  THR F CA  
16904 C  C   . THR F  111 ? 2.1955 2.0430 4.0865 0.0858  -0.0264 0.4036  221  THR F C   
16905 O  O   . THR F  111 ? 2.1568 1.9478 3.8814 0.1025  -0.0560 0.3931  221  THR F O   
16906 C  CB  . THR F  111 ? 2.2075 2.0374 4.3014 0.0949  0.1344  0.4717  221  THR F CB  
16907 O  OG1 . THR F  111 ? 2.2048 2.0417 4.3844 0.1422  0.2312  0.5437  221  THR F OG1 
16908 C  CG2 . THR F  111 ? 2.2324 1.9850 4.1959 0.0887  0.1281  0.4528  221  THR F CG2 
16909 N  N   . PRO F  112 ? 2.1598 2.0650 4.1475 0.0276  -0.0791 0.3575  222  PRO F N   
16910 C  CA  . PRO F  112 ? 2.2439 2.1457 4.1240 -0.0076 -0.1717 0.3041  222  PRO F CA  
16911 C  C   . PRO F  112 ? 2.3405 2.2457 4.1108 0.0434  -0.2170 0.3253  222  PRO F C   
16912 O  O   . PRO F  112 ? 2.2648 2.2071 4.0898 0.0915  -0.1936 0.3654  222  PRO F O   
16913 C  CB  . PRO F  112 ? 2.2514 2.2322 4.2814 -0.0746 -0.2097 0.2540  222  PRO F CB  
16914 C  CG  . PRO F  112 ? 2.2417 2.2831 4.4513 -0.0573 -0.1530 0.2898  222  PRO F CG  
16915 C  CD  . PRO F  112 ? 2.2394 2.2200 4.4393 -0.0112 -0.0581 0.3481  222  PRO F CD  
16916 N  N   . GLU F  113 ? 2.4737 2.3383 4.0934 0.0325  -0.2794 0.2977  223  GLU F N   
16917 C  CA  . GLU F  113 ? 2.4111 2.2554 3.9124 0.0816  -0.3167 0.3178  223  GLU F CA  
16918 C  C   . GLU F  113 ? 2.3609 2.2355 3.8277 0.0483  -0.4049 0.2865  223  GLU F C   
16919 O  O   . GLU F  113 ? 2.3918 2.3110 3.9187 -0.0112 -0.4390 0.2459  223  GLU F O   
16920 C  CB  . GLU F  113 ? 2.4159 2.1724 3.7549 0.1123  -0.3004 0.3245  223  GLU F CB  
16921 C  CG  . GLU F  113 ? 2.4304 2.1575 3.7846 0.1400  -0.2186 0.3509  223  GLU F CG  
16922 C  CD  . GLU F  113 ? 2.3946 2.1550 3.8262 0.2018  -0.1568 0.4040  223  GLU F CD  
16923 O  OE1 . GLU F  113 ? 2.4169 2.2311 3.9193 0.2187  -0.1724 0.4175  223  GLU F OE1 
16924 O  OE2 . GLU F  113 ? 2.3042 2.0408 3.7249 0.2370  -0.0901 0.4347  223  GLU F OE2 
16925 N  N   . GLY F  114 ? 2.4420 2.2936 3.8116 0.0898  -0.4407 0.3059  224  GLY F N   
16926 C  CA  . GLY F  114 ? 2.5858 2.4609 3.9112 0.0695  -0.5214 0.2900  224  GLY F CA  
16927 C  C   . GLY F  114 ? 2.5575 2.3614 3.7239 0.0415  -0.5558 0.2659  224  GLY F C   
16928 O  O   . GLY F  114 ? 2.5220 2.2901 3.5859 0.0623  -0.5963 0.2789  224  GLY F O   
16929 N  N   . GLY F  115 ? 2.6137 2.3947 3.7650 -0.0055 -0.5361 0.2318  225  GLY F N   
16930 C  CA  . GLY F  115 ? 2.6680 2.3860 3.6755 -0.0343 -0.5619 0.2067  225  GLY F CA  
16931 C  C   . GLY F  115 ? 2.6848 2.4328 3.6423 -0.0685 -0.6369 0.1889  225  GLY F C   
16932 O  O   . GLY F  115 ? 2.7044 2.3983 3.5306 -0.0681 -0.6659 0.1924  225  GLY F O   
16933 N  N   . PHE F  116 ? 2.5004 2.3390 3.5640 -0.0971 -0.6685 0.1705  226  PHE F N   
16934 C  CA  . PHE F  116 ? 2.4828 2.3648 3.4958 -0.1285 -0.7424 0.1519  226  PHE F CA  
16935 C  C   . PHE F  116 ? 2.5530 2.4233 3.4988 -0.0802 -0.7842 0.1993  226  PHE F C   
16936 O  O   . PHE F  116 ? 2.7307 2.5893 3.5688 -0.0939 -0.8345 0.2006  226  PHE F O   
16937 C  CB  . PHE F  116 ? 2.4916 2.4863 3.6450 -0.1671 -0.7683 0.1147  226  PHE F CB  
16938 C  CG  . PHE F  116 ? 2.4949 2.4963 3.7080 -0.2241 -0.7353 0.0587  226  PHE F CG  
16939 C  CD1 . PHE F  116 ? 2.4059 2.3236 3.5229 -0.2425 -0.7020 0.0423  226  PHE F CD1 
16940 C  CD2 . PHE F  116 ? 2.6025 2.6951 3.9760 -0.2598 -0.7376 0.0191  226  PHE F CD2 
16941 C  CE1 . PHE F  116 ? 2.4862 2.4058 3.6631 -0.2911 -0.6698 -0.0086 226  PHE F CE1 
16942 C  CE2 . PHE F  116 ? 2.5967 2.6875 4.0342 -0.3124 -0.7040 -0.0352 226  PHE F CE2 
16943 C  CZ  . PHE F  116 ? 2.5842 2.5861 3.9215 -0.3262 -0.6697 -0.0473 226  PHE F CZ  
16944 N  N   . ASP F  117 ? 2.6355 2.5062 3.6427 -0.0218 -0.7608 0.2403  227  ASP F N   
16945 C  CA  . ASP F  117 ? 2.7492 2.5934 3.6954 0.0300  -0.7926 0.2856  227  ASP F CA  
16946 C  C   . ASP F  117 ? 2.7886 2.5212 3.5733 0.0344  -0.7892 0.2942  227  ASP F C   
16947 O  O   . ASP F  117 ? 2.7474 2.4554 3.4454 0.0412  -0.8346 0.3156  227  ASP F O   
16948 C  CB  . ASP F  117 ? 2.8239 2.6788 3.8620 0.0936  -0.7552 0.3211  227  ASP F CB  
16949 C  CG  . ASP F  117 ? 2.8791 2.8491 4.0603 0.1051  -0.7850 0.3296  227  ASP F CG  
16950 O  OD1 . ASP F  117 ? 2.8715 2.9230 4.1118 0.0562  -0.8207 0.2964  227  ASP F OD1 
16951 O  OD2 . ASP F  117 ? 2.8548 2.8387 4.0931 0.1637  -0.7734 0.3652  227  ASP F OD2 
16952 N  N   . ALA F  118 ? 2.8170 2.4835 3.5643 0.0312  -0.7344 0.2792  228  ALA F N   
16953 C  CA  . ALA F  118 ? 2.8613 2.4283 3.4696 0.0320  -0.7277 0.2794  228  ALA F CA  
16954 C  C   . ALA F  118 ? 2.8001 2.3578 3.3170 -0.0273 -0.7633 0.2538  228  ALA F C   
16955 O  O   . ALA F  118 ? 2.9185 2.4151 3.3261 -0.0272 -0.7839 0.2682  228  ALA F O   
16956 C  CB  . ALA F  118 ? 2.9073 2.4251 3.5073 0.0448  -0.6639 0.2653  228  ALA F CB  
16957 N  N   . ILE F  119 ? 2.6503 2.2665 3.2127 -0.0786 -0.7670 0.2144  229  ILE F N   
16958 C  CA  . ILE F  119 ? 2.6882 2.3057 3.1641 -0.1348 -0.7983 0.1844  229  ILE F CA  
16959 C  C   . ILE F  119 ? 2.7055 2.3590 3.1355 -0.1324 -0.8636 0.2104  229  ILE F C   
16960 O  O   . ILE F  119 ? 2.7630 2.3757 3.0730 -0.1504 -0.8858 0.2176  229  ILE F O   
16961 C  CB  . ILE F  119 ? 2.6683 2.3468 3.2189 -0.1873 -0.7874 0.1300  229  ILE F CB  
16962 C  CG1 . ILE F  119 ? 2.6415 2.2772 3.2331 -0.1829 -0.7194 0.1145  229  ILE F CG1 
16963 C  CG2 . ILE F  119 ? 2.6996 2.3870 3.1575 -0.2436 -0.8193 0.0934  229  ILE F CG2 
16964 C  CD1 . ILE F  119 ? 2.6219 2.3037 3.3007 -0.2307 -0.6995 0.0640  229  ILE F CD1 
16965 N  N   . MET F  120 ? 2.8037 2.5371 3.3304 -0.1076 -0.8938 0.2284  230  MET F N   
16966 C  CA  . MET F  120 ? 2.8072 2.5892 3.2973 -0.0986 -0.9603 0.2566  230  MET F CA  
16967 C  C   . MET F  120 ? 2.8623 2.5568 3.2576 -0.0528 -0.9671 0.3149  230  MET F C   
16968 O  O   . MET F  120 ? 2.8724 2.5510 3.1635 -0.0615 -1.0047 0.3374  230  MET F O   
16969 C  CB  . MET F  120 ? 2.8196 2.7138 3.4507 -0.0774 -0.9896 0.2610  230  MET F CB  
16970 C  CG  . MET F  120 ? 2.9493 2.9034 3.5509 -0.0553 -1.0618 0.2969  230  MET F CG  
16971 S  SD  . MET F  120 ? 3.0299 3.0329 3.5155 -0.1145 -1.1171 0.2652  230  MET F SD  
16972 C  CE  . MET F  120 ? 3.0098 3.1464 3.6430 -0.1665 -1.1263 0.1843  230  MET F CE  
16973 N  N   . GLN F  121 ? 3.0886 2.7247 3.5192 -0.0031 -0.9281 0.3395  231  GLN F N   
16974 C  CA  . GLN F  121 ? 3.3024 2.8518 3.6610 0.0424  -0.9316 0.3890  231  GLN F CA  
16975 C  C   . GLN F  121 ? 3.3802 2.8276 3.6068 0.0131  -0.9126 0.3818  231  GLN F C   
16976 O  O   . GLN F  121 ? 3.4753 2.8653 3.6173 0.0241  -0.9332 0.4201  231  GLN F O   
16977 C  CB  . GLN F  121 ? 3.2418 2.7613 3.6754 0.1021  -0.8919 0.4052  231  GLN F CB  
16978 C  CG  . GLN F  121 ? 3.1256 2.7440 3.6952 0.1378  -0.9080 0.4203  231  GLN F CG  
16979 C  CD  . GLN F  121 ? 3.2325 2.9027 3.8019 0.1578  -0.9740 0.4601  231  GLN F CD  
16980 O  OE1 . GLN F  121 ? 3.3526 2.9542 3.8469 0.1885  -0.9910 0.5025  231  GLN F OE1 
16981 N  NE2 . GLN F  121 ? 3.1867 2.9803 3.8443 0.1415  -1.0115 0.4465  231  GLN F NE2 
16982 N  N   . ALA F  122 ? 3.1872 2.6120 3.4004 -0.0237 -0.8715 0.3351  232  ALA F N   
16983 C  CA  . ALA F  122 ? 3.0728 2.4109 3.1728 -0.0539 -0.8516 0.3224  232  ALA F CA  
16984 C  C   . ALA F  122 ? 3.1206 2.4818 3.1354 -0.1049 -0.8868 0.3181  232  ALA F C   
16985 O  O   . ALA F  122 ? 3.2502 2.5402 3.1627 -0.1230 -0.8813 0.3285  232  ALA F O   
16986 C  CB  . ALA F  122 ? 2.9916 2.3093 3.1082 -0.0727 -0.7995 0.2745  232  ALA F CB  
16987 N  N   . ALA F  123 ? 3.1257 2.5891 3.1829 -0.1293 -0.9210 0.3001  233  ALA F N   
16988 C  CA  . ALA F  123 ? 3.1787 2.6786 3.1507 -0.1761 -0.9553 0.2895  233  ALA F CA  
16989 C  C   . ALA F  123 ? 3.2696 2.7695 3.1747 -0.1496 -1.0033 0.3524  233  ALA F C   
16990 O  O   . ALA F  123 ? 3.3562 2.8059 3.1447 -0.1684 -1.0066 0.3739  233  ALA F O   
16991 C  CB  . ALA F  123 ? 3.1839 2.7988 3.2292 -0.2122 -0.9761 0.2375  233  ALA F CB  
16992 N  N   . VAL F  124 ? 3.2286 2.7852 3.2092 -0.1036 -1.0383 0.3861  234  VAL F N   
16993 C  CA  . VAL F  124 ? 3.3062 2.8798 3.2310 -0.0736 -1.0901 0.4489  234  VAL F CA  
16994 C  C   . VAL F  124 ? 3.4213 2.8654 3.2754 -0.0394 -1.0679 0.5076  234  VAL F C   
16995 O  O   . VAL F  124 ? 3.5030 2.9141 3.2535 -0.0405 -1.0879 0.5543  234  VAL F O   
16996 C  CB  . VAL F  124 ? 3.2349 2.9110 3.2742 -0.0302 -1.1334 0.4663  234  VAL F CB  
16997 C  CG1 . VAL F  124 ? 3.3458 3.0523 3.3251 0.0042  -1.1926 0.5329  234  VAL F CG1 
16998 C  CG2 . VAL F  124 ? 3.1793 2.9793 3.3067 -0.0699 -1.1493 0.3995  234  VAL F CG2 
16999 N  N   . CYS F  125 ? 3.4221 2.7915 3.3316 -0.0085 -1.0244 0.5055  235  CYS F N   
17000 C  CA  . CYS F  125 ? 3.4828 2.7276 3.3430 0.0238  -1.0011 0.5504  235  CYS F CA  
17001 C  C   . CYS F  125 ? 3.4788 2.6393 3.2254 -0.0247 -0.9721 0.5400  235  CYS F C   
17002 O  O   . CYS F  125 ? 3.4323 2.5364 3.1797 -0.0451 -0.9254 0.4963  235  CYS F O   
17003 C  CB  . CYS F  125 ? 3.3527 2.5480 3.2966 0.0646  -0.9594 0.5348  235  CYS F CB  
17004 S  SG  . CYS F  125 ? 3.2368 2.5215 3.3234 0.1279  -0.9813 0.5515  235  CYS F SG  
17005 N  N   . LYS F  126 ? 3.5538 2.7105 3.2032 -0.0414 -0.9987 0.5817  236  LYS F N   
17006 C  CA  . LYS F  126 ? 3.5447 2.6211 3.0881 -0.0864 -0.9680 0.5804  236  LYS F CA  
17007 C  C   . LYS F  126 ? 3.5666 2.5061 3.0907 -0.0598 -0.9350 0.6207  236  LYS F C   
17008 O  O   . LYS F  126 ? 3.6607 2.5233 3.1140 -0.0972 -0.9015 0.6167  236  LYS F O   
17009 C  CB  . LYS F  126 ? 3.6495 2.7760 3.0897 -0.1131 -1.0036 0.6139  236  LYS F CB  
17010 C  CG  . LYS F  126 ? 3.6353 2.8884 3.0746 -0.1562 -1.0294 0.5569  236  LYS F CG  
17011 C  CD  . LYS F  126 ? 3.8731 3.1783 3.1978 -0.1755 -1.0658 0.5919  236  LYS F CD  
17012 C  CE  . LYS F  126 ? 3.8723 3.3007 3.1916 -0.2234 -1.0884 0.5222  236  LYS F CE  
17013 N  NZ  . LYS F  126 ? 3.9562 3.4481 3.1549 -0.2382 -1.1263 0.5526  236  LYS F NZ  
17014 N  N   . GLU F  127 ? 3.4785 2.3875 3.0711 0.0026  -0.9419 0.6556  237  GLU F N   
17015 C  CA  . GLU F  127 ? 3.5267 2.3049 3.1136 0.0329  -0.9134 0.6927  237  GLU F CA  
17016 C  C   . GLU F  127 ? 3.4555 2.1839 3.1174 0.0510  -0.8724 0.6385  237  GLU F C   
17017 O  O   . GLU F  127 ? 3.4796 2.1182 3.1164 0.0276  -0.8310 0.6107  237  GLU F O   
17018 C  CB  . GLU F  127 ? 3.7315 2.5042 3.3383 0.0967  -0.9498 0.7740  237  GLU F CB  
17019 C  CG  . GLU F  127 ? 3.8547 2.6951 3.3846 0.0892  -0.9975 0.8318  237  GLU F CG  
17020 C  CD  . GLU F  127 ? 3.9406 2.8084 3.5080 0.1602  -1.0423 0.9067  237  GLU F CD  
17021 O  OE1 . GLU F  127 ? 3.9607 2.8891 3.4640 0.1655  -1.0864 0.9612  237  GLU F OE1 
17022 O  OE2 . GLU F  127 ? 3.9996 2.8348 3.6601 0.2137  -1.0341 0.9097  237  GLU F OE2 
17023 N  N   . LYS F  128 ? 3.3477 2.1397 3.1029 0.0928  -0.8826 0.6213  238  LYS F N   
17024 C  CA  . LYS F  128 ? 3.3122 2.0676 3.1325 0.1183  -0.8440 0.5739  238  LYS F CA  
17025 C  C   . LYS F  128 ? 3.3069 2.0812 3.1137 0.0697  -0.8121 0.5017  238  LYS F C   
17026 O  O   . LYS F  128 ? 3.4529 2.1815 3.2835 0.0818  -0.7756 0.4597  238  LYS F O   
17027 C  CB  . LYS F  128 ? 3.2118 2.0398 3.1341 0.1760  -0.8594 0.5798  238  LYS F CB  
17028 C  CG  . LYS F  128 ? 3.2562 2.0878 3.2028 0.2284  -0.8976 0.6521  238  LYS F CG  
17029 C  CD  . LYS F  128 ? 3.1990 2.0884 3.2584 0.2913  -0.9025 0.6535  238  LYS F CD  
17030 C  CE  . LYS F  128 ? 3.1568 1.9609 3.2548 0.3324  -0.8574 0.6278  238  LYS F CE  
17031 N  NZ  . LYS F  128 ? 3.0562 1.9136 3.2610 0.3995  -0.8594 0.6363  238  LYS F NZ  
17032 N  N   . ILE F  129 ? 3.1879 2.0316 2.9575 0.0183  -0.8259 0.4848  239  ILE F N   
17033 C  CA  . ILE F  129 ? 3.1993 2.0519 2.9483 -0.0304 -0.7950 0.4214  239  ILE F CA  
17034 C  C   . ILE F  129 ? 3.3375 2.1210 2.9941 -0.0801 -0.7793 0.4203  239  ILE F C   
17035 O  O   . ILE F  129 ? 3.4484 2.1861 3.0925 -0.1023 -0.7432 0.3750  239  ILE F O   
17036 C  CB  . ILE F  129 ? 3.1890 2.1559 2.9668 -0.0579 -0.8120 0.3936  239  ILE F CB  
17037 C  CG1 . ILE F  129 ? 3.0939 2.1146 2.9749 -0.0199 -0.8000 0.3710  239  ILE F CG1 
17038 C  CG2 . ILE F  129 ? 3.2583 2.2298 2.9831 -0.1204 -0.7905 0.3446  239  ILE F CG2 
17039 C  CD1 . ILE F  129 ? 3.2033 2.2531 3.1524 0.0382  -0.8260 0.4157  239  ILE F CD1 
17040 N  N   . GLY F  130 ? 3.4264 2.2070 3.0190 -0.0961 -0.8055 0.4714  240  GLY F N   
17041 C  CA  . GLY F  130 ? 3.6542 2.3641 3.1593 -0.1390 -0.7869 0.4851  240  GLY F CA  
17042 C  C   . GLY F  130 ? 3.6501 2.4123 3.0973 -0.2036 -0.7803 0.4464  240  GLY F C   
17043 O  O   . GLY F  130 ? 3.7701 2.4931 3.1972 -0.2409 -0.7432 0.4030  240  GLY F O   
17044 N  N   . TRP F  131 ? 3.5591 2.4144 2.9824 -0.2168 -0.8169 0.4577  241  TRP F N   
17045 C  CA  . TRP F  131 ? 3.5390 2.4492 2.9052 -0.2766 -0.8123 0.4186  241  TRP F CA  
17046 C  C   . TRP F  131 ? 3.7862 2.6483 3.0440 -0.3092 -0.8030 0.4600  241  TRP F C   
17047 O  O   . TRP F  131 ? 3.9857 2.8266 3.2005 -0.2846 -0.8260 0.5330  241  TRP F O   
17048 C  CB  . TRP F  131 ? 3.5565 2.5898 2.9430 -0.2793 -0.8556 0.4060  241  TRP F CB  
17049 C  CG  . TRP F  131 ? 3.5111 2.5967 3.0093 -0.2555 -0.8574 0.3649  241  TRP F CG  
17050 C  CD1 . TRP F  131 ? 3.5787 2.7043 3.1544 -0.2057 -0.8862 0.3902  241  TRP F CD1 
17051 C  CD2 . TRP F  131 ? 3.3736 2.4776 2.9228 -0.2779 -0.8250 0.2961  241  TRP F CD2 
17052 N  NE1 . TRP F  131 ? 3.5217 2.6887 3.1928 -0.1986 -0.8704 0.3424  241  TRP F NE1 
17053 C  CE2 . TRP F  131 ? 3.3573 2.5095 3.0117 -0.2407 -0.8331 0.2870  241  TRP F CE2 
17054 C  CE3 . TRP F  131 ? 3.3475 2.4341 2.8670 -0.3233 -0.7883 0.2442  241  TRP F CE3 
17055 C  CZ2 . TRP F  131 ? 3.1987 2.3764 2.9238 -0.2466 -0.8036 0.2339  241  TRP F CZ2 
17056 C  CZ3 . TRP F  131 ? 3.2310 2.3452 2.8221 -0.3263 -0.7635 0.1895  241  TRP F CZ3 
17057 C  CH2 . TRP F  131 ? 3.1510 2.3077 2.8414 -0.2878 -0.7702 0.1875  241  TRP F CH2 
17058 N  N   . ARG F  132 ? 3.7986 2.6465 3.0140 -0.3629 -0.7670 0.4165  242  ARG F N   
17059 C  CA  . ARG F  132 ? 3.9834 2.7924 3.0971 -0.4002 -0.7493 0.4518  242  ARG F CA  
17060 C  C   . ARG F  132 ? 4.0090 2.9061 3.0439 -0.4104 -0.7887 0.4830  242  ARG F C   
17061 O  O   . ARG F  132 ? 3.9180 2.9156 2.9829 -0.4016 -0.8277 0.4571  242  ARG F O   
17062 C  CB  . ARG F  132 ? 3.8915 2.6836 2.9880 -0.4562 -0.7018 0.3897  242  ARG F CB  
17063 C  CG  . ARG F  132 ? 3.8354 2.5169 2.9531 -0.4612 -0.6568 0.3878  242  ARG F CG  
17064 C  CD  . ARG F  132 ? 3.7579 2.4436 2.8637 -0.5172 -0.6145 0.3231  242  ARG F CD  
17065 N  NE  . ARG F  132 ? 3.6937 2.2832 2.8259 -0.5273 -0.5728 0.3137  242  ARG F NE  
17066 C  CZ  . ARG F  132 ? 3.5346 2.1101 2.7399 -0.5210 -0.5545 0.2510  242  ARG F CZ  
17067 N  NH1 . ARG F  132 ? 3.4019 2.0472 2.6579 -0.5022 -0.5700 0.2009  242  ARG F NH1 
17068 N  NH2 . ARG F  132 ? 3.5518 2.0459 2.7815 -0.5330 -0.5199 0.2384  242  ARG F NH2 
17069 N  N   . ASN F  133 ? 4.1163 2.9770 3.0502 -0.4292 -0.7767 0.5393  243  ASN F N   
17070 C  CA  . ASN F  133 ? 4.1275 3.0759 2.9662 -0.4393 -0.8113 0.5693  243  ASN F CA  
17071 C  C   . ASN F  133 ? 4.0454 3.0876 2.8638 -0.4911 -0.8070 0.4857  243  ASN F C   
17072 O  O   . ASN F  133 ? 4.0613 3.2122 2.8951 -0.4877 -0.8500 0.4520  243  ASN F O   
17073 C  CB  . ASN F  133 ? 4.2618 3.1453 2.9898 -0.4492 -0.7882 0.6512  243  ASN F CB  
17074 C  CG  . ASN F  133 ? 4.3143 3.1545 3.0294 -0.3898 -0.8170 0.7533  243  ASN F CG  
17075 O  OD1 . ASN F  133 ? 4.2774 3.1512 3.0608 -0.3399 -0.8610 0.7627  243  ASN F OD1 
17076 N  ND2 . ASN F  133 ? 4.3736 3.1405 3.0022 -0.3942 -0.7895 0.8339  243  ASN F ND2 
17077 N  N   . ASP F  134 ? 3.8804 2.8827 2.6725 -0.5400 -0.7541 0.4477  244  ASP F N   
17078 C  CA  . ASP F  134 ? 3.8525 2.9321 2.6215 -0.5906 -0.7409 0.3693  244  ASP F CA  
17079 C  C   . ASP F  134 ? 3.7935 2.8383 2.6532 -0.6093 -0.7008 0.2943  244  ASP F C   
17080 O  O   . ASP F  134 ? 3.8560 2.8386 2.7012 -0.6397 -0.6514 0.2830  244  ASP F O   
17081 C  CB  . ASP F  134 ? 4.0478 3.1268 2.6912 -0.6305 -0.7133 0.3966  244  ASP F CB  
17082 C  CG  . ASP F  134 ? 4.2753 3.3760 2.8200 -0.6027 -0.7492 0.4878  244  ASP F CG  
17083 O  OD1 . ASP F  134 ? 4.4438 3.4513 2.9679 -0.5776 -0.7361 0.5723  244  ASP F OD1 
17084 O  OD2 . ASP F  134 ? 4.2681 3.4808 2.7597 -0.6037 -0.7916 0.4740  244  ASP F OD2 
17085 N  N   . SER F  135 ? 3.7040 2.7930 2.6602 -0.5893 -0.7216 0.2452  245  SER F N   
17086 C  CA  . SER F  135 ? 3.5434 2.6133 2.5848 -0.5986 -0.6881 0.1773  245  SER F CA  
17087 C  C   . SER F  135 ? 3.5569 2.7136 2.6735 -0.5927 -0.7123 0.1206  245  SER F C   
17088 O  O   . SER F  135 ? 3.6383 2.8659 2.7522 -0.5809 -0.7563 0.1316  245  SER F O   
17089 C  CB  . SER F  135 ? 3.5026 2.4812 2.6071 -0.5615 -0.6726 0.2005  245  SER F CB  
17090 O  OG  . SER F  135 ? 3.4716 2.4644 2.6381 -0.5096 -0.7095 0.2264  245  SER F OG  
17091 N  N   . LEU F  136 ? 3.5634 2.7160 2.7532 -0.6000 -0.6824 0.0599  246  LEU F N   
17092 C  CA  . LEU F  136 ? 3.4648 2.6857 2.7412 -0.5948 -0.6938 0.0071  246  LEU F CA  
17093 C  C   . LEU F  136 ? 3.3835 2.5840 2.7496 -0.5407 -0.7069 0.0322  246  LEU F C   
17094 O  O   . LEU F  136 ? 3.3877 2.5352 2.8000 -0.5196 -0.6789 0.0252  246  LEU F O   
17095 C  CB  . LEU F  136 ? 3.3472 2.5751 2.6561 -0.6253 -0.6522 -0.0638 246  LEU F CB  
17096 C  CG  . LEU F  136 ? 3.3749 2.6267 2.6018 -0.6791 -0.6323 -0.0962 246  LEU F CG  
17097 C  CD1 . LEU F  136 ? 3.2148 2.4782 2.4933 -0.7015 -0.5926 -0.1684 246  LEU F CD1 
17098 C  CD2 . LEU F  136 ? 3.5574 2.8910 2.7331 -0.6987 -0.6689 -0.1019 246  LEU F CD2 
17099 N  N   . HIS F  137 ? 3.2950 2.5445 2.6849 -0.5165 -0.7503 0.0602  247  HIS F N   
17100 C  CA  . HIS F  137 ? 3.2961 2.5377 2.7732 -0.4638 -0.7638 0.0870  247  HIS F CA  
17101 C  C   . HIS F  137 ? 3.1907 2.4773 2.7740 -0.4621 -0.7487 0.0337  247  HIS F C   
17102 O  O   . HIS F  137 ? 3.1629 2.5274 2.7946 -0.4724 -0.7719 0.0094  247  HIS F O   
17103 C  CB  . HIS F  137 ? 3.4519 2.7371 2.9203 -0.4388 -0.8158 0.1372  247  HIS F CB  
17104 C  CG  . HIS F  137 ? 3.5176 2.7660 2.8756 -0.4409 -0.8307 0.1958  247  HIS F CG  
17105 N  ND1 . HIS F  137 ? 3.5669 2.8777 2.8746 -0.4374 -0.8786 0.2304  247  HIS F ND1 
17106 C  CD2 . HIS F  137 ? 3.5257 2.6824 2.8176 -0.4450 -0.8024 0.2282  247  HIS F CD2 
17107 C  CE1 . HIS F  137 ? 3.6862 2.9409 2.8953 -0.4363 -0.8766 0.2891  247  HIS F CE1 
17108 N  NE2 . HIS F  137 ? 3.6496 2.8069 2.8523 -0.4435 -0.8286 0.2880  247  HIS F NE2 
17109 N  N   . LEU F  138 ? 3.1932 2.4320 2.8161 -0.4483 -0.7085 0.0148  248  LEU F N   
17110 C  CA  . LEU F  138 ? 3.0881 2.3575 2.8080 -0.4413 -0.6849 -0.0264 248  LEU F CA  
17111 C  C   . LEU F  138 ? 3.1618 2.4169 2.9590 -0.3838 -0.6817 0.0051  248  LEU F C   
17112 O  O   . LEU F  138 ? 3.2859 2.4808 3.0595 -0.3512 -0.6738 0.0352  248  LEU F O   
17113 C  CB  . LEU F  138 ? 2.8111 2.0498 2.5199 -0.4612 -0.6412 -0.0695 248  LEU F CB  
17114 C  CG  . LEU F  138 ? 2.7491 1.9911 2.3745 -0.5154 -0.6350 -0.0991 248  LEU F CG  
17115 C  CD1 . LEU F  138 ? 2.5891 1.8094 2.2255 -0.5278 -0.5914 -0.1435 248  LEU F CD1 
17116 C  CD2 . LEU F  138 ? 2.8111 2.1283 2.4372 -0.5512 -0.6586 -0.1285 248  LEU F CD2 
17117 N  N   . LEU F  139 ? 3.0180 2.3297 2.9120 -0.3724 -0.6846 -0.0050 249  LEU F N   
17118 C  CA  . LEU F  139 ? 2.8793 2.1917 2.8547 -0.3183 -0.6788 0.0260  249  LEU F CA  
17119 C  C   . LEU F  139 ? 2.8027 2.1340 2.8696 -0.3104 -0.6381 -0.0026 249  LEU F C   
17120 O  O   . LEU F  139 ? 2.7797 2.1683 2.9227 -0.3309 -0.6398 -0.0258 249  LEU F O   
17121 C  CB  . LEU F  139 ? 2.9113 2.2800 2.9285 -0.3062 -0.7220 0.0547  249  LEU F CB  
17122 C  CG  . LEU F  139 ? 3.0032 2.3554 3.0570 -0.2465 -0.7297 0.1058  249  LEU F CG  
17123 C  CD1 . LEU F  139 ? 3.1168 2.5283 3.1915 -0.2400 -0.7813 0.1345  249  LEU F CD1 
17124 C  CD2 . LEU F  139 ? 2.9801 2.3421 3.1352 -0.2102 -0.6911 0.1035  249  LEU F CD2 
17125 N  N   . VAL F  140 ? 2.7717 2.0567 2.8331 -0.2805 -0.6012 -0.0016 250  VAL F N   
17126 C  CA  . VAL F  140 ? 2.6650 1.9627 2.8048 -0.2621 -0.5586 -0.0164 250  VAL F CA  
17127 C  C   . VAL F  140 ? 2.7376 2.0609 2.9673 -0.2145 -0.5509 0.0195  250  VAL F C   
17128 O  O   . VAL F  140 ? 2.7514 2.0506 2.9643 -0.1693 -0.5544 0.0533  250  VAL F O   
17129 C  CB  . VAL F  140 ? 2.6187 1.8696 2.7130 -0.2423 -0.5259 -0.0280 250  VAL F CB  
17130 C  CG1 . VAL F  140 ? 2.6352 1.8995 2.8065 -0.2028 -0.4828 -0.0235 250  VAL F CG1 
17131 C  CG2 . VAL F  140 ? 2.7148 1.9555 2.7509 -0.2931 -0.5229 -0.0709 250  VAL F CG2 
17132 N  N   . PHE F  141 ? 2.7206 2.0923 3.0523 -0.2251 -0.5364 0.0096  251  PHE F N   
17133 C  CA  . PHE F  141 ? 2.6876 2.0928 3.1226 -0.1868 -0.5222 0.0417  251  PHE F CA  
17134 C  C   . PHE F  141 ? 2.6267 2.0246 3.1238 -0.1587 -0.4632 0.0458  251  PHE F C   
17135 O  O   . PHE F  141 ? 2.6793 2.0829 3.2137 -0.1892 -0.4399 0.0154  251  PHE F O   
17136 C  CB  . PHE F  141 ? 2.6895 2.1620 3.2095 -0.2217 -0.5501 0.0291  251  PHE F CB  
17137 C  CG  . PHE F  141 ? 2.6071 2.1224 3.2497 -0.1884 -0.5334 0.0592  251  PHE F CG  
17138 C  CD1 . PHE F  141 ? 2.6908 2.2167 3.3356 -0.1471 -0.5550 0.1000  251  PHE F CD1 
17139 C  CD2 . PHE F  141 ? 2.6513 2.1951 3.4143 -0.1984 -0.4924 0.0475  251  PHE F CD2 
17140 C  CE1 . PHE F  141 ? 2.8283 2.3999 3.5918 -0.1165 -0.5363 0.1268  251  PHE F CE1 
17141 C  CE2 . PHE F  141 ? 2.7896 2.3747 3.6734 -0.1705 -0.4710 0.0772  251  PHE F CE2 
17142 C  CZ  . PHE F  141 ? 2.8667 2.4694 3.7500 -0.1296 -0.4932 0.1161  251  PHE F CZ  
17143 N  N   . VAL F  142 ? 2.6120 1.9979 3.1186 -0.0978 -0.4374 0.0842  252  VAL F N   
17144 C  CA  . VAL F  142 ? 2.5478 1.9284 3.0970 -0.0590 -0.3799 0.0995  252  VAL F CA  
17145 C  C   . VAL F  142 ? 2.5399 1.9561 3.1887 -0.0174 -0.3536 0.1424  252  VAL F C   
17146 O  O   . VAL F  142 ? 2.6632 2.0820 3.2941 0.0205  -0.3674 0.1690  252  VAL F O   
17147 C  CB  . VAL F  142 ? 2.5142 1.8523 2.9639 -0.0186 -0.3675 0.1011  252  VAL F CB  
17148 C  CG1 . VAL F  142 ? 2.5341 1.8786 3.0227 0.0336  -0.3107 0.1265  252  VAL F CG1 
17149 C  CG2 . VAL F  142 ? 2.5207 1.8299 2.8901 -0.0626 -0.3850 0.0572  252  VAL F CG2 
17150 N  N   . SER F  143 ? 2.3839 1.8256 3.1433 -0.0244 -0.3120 0.1489  253  SER F N   
17151 C  CA  . SER F  143 ? 2.3490 1.8243 3.2147 0.0149  -0.2717 0.1930  253  SER F CA  
17152 C  C   . SER F  143 ? 2.4442 1.9231 3.4092 0.0068  -0.2131 0.1987  253  SER F C   
17153 O  O   . SER F  143 ? 2.4697 1.9419 3.4601 -0.0459 -0.2178 0.1588  253  SER F O   
17154 C  CB  . SER F  143 ? 2.4109 1.9375 3.3568 -0.0051 -0.3063 0.1956  253  SER F CB  
17155 O  OG  . SER F  143 ? 2.4950 2.0515 3.5160 -0.0712 -0.3250 0.1558  253  SER F OG  
17156 N  N   . ASP F  144 ? 2.6553 2.1428 3.6759 0.0613  -0.1544 0.2497  254  ASP F N   
17157 C  CA  . ASP F  144 ? 2.6853 2.1683 3.8029 0.0636  -0.0887 0.2695  254  ASP F CA  
17158 C  C   . ASP F  144 ? 2.7199 2.2457 4.0075 0.0439  -0.0592 0.2870  254  ASP F C   
17159 O  O   . ASP F  144 ? 2.6979 2.2219 4.0792 0.0653  0.0101  0.3265  254  ASP F O   
17160 C  CB  . ASP F  144 ? 2.5266 1.9908 3.5893 0.1397  -0.0347 0.3196  254  ASP F CB  
17161 C  CG  . ASP F  144 ? 2.4239 1.9190 3.5051 0.2010  -0.0072 0.3732  254  ASP F CG  
17162 O  OD1 . ASP F  144 ? 2.4651 1.9865 3.5557 0.1933  -0.0457 0.3659  254  ASP F OD1 
17163 O  OD2 . ASP F  144 ? 2.3746 1.8703 3.4571 0.2610  0.0538  0.4242  254  ASP F OD2 
17164 N  N   . ALA F  145 ? 2.7424 2.3097 4.0762 0.0041  -0.1095 0.2595  255  ALA F N   
17165 C  CA  . ALA F  145 ? 2.5939 2.2140 4.0998 -0.0210 -0.0896 0.2653  255  ALA F CA  
17166 C  C   . ALA F  145 ? 2.5139 2.1777 4.0474 -0.0853 -0.1630 0.2068  255  ALA F C   
17167 O  O   . ALA F  145 ? 2.5246 2.1728 3.9386 -0.1073 -0.2231 0.1699  255  ALA F O   
17168 C  CB  . ALA F  145 ? 2.5163 2.1701 4.0665 0.0387  -0.0566 0.3255  255  ALA F CB  
17169 N  N   . ASP F  146 ? 2.4030 2.1277 4.0969 -0.1139 -0.1570 0.1998  256  ASP F N   
17170 C  CA  . ASP F  146 ? 2.3567 2.1425 4.0916 -0.1698 -0.2279 0.1448  256  ASP F CA  
17171 C  C   . ASP F  146 ? 2.4824 2.2956 4.1280 -0.1377 -0.2882 0.1624  256  ASP F C   
17172 O  O   . ASP F  146 ? 2.5816 2.3619 4.1388 -0.0765 -0.2737 0.2096  256  ASP F O   
17173 C  CB  . ASP F  146 ? 2.2614 2.1125 4.2073 -0.2059 -0.2021 0.1304  256  ASP F CB  
17174 C  CG  . ASP F  146 ? 2.1663 2.0799 4.1651 -0.2779 -0.2696 0.0523  256  ASP F CG  
17175 O  OD1 . ASP F  146 ? 2.0855 2.0160 3.9642 -0.2857 -0.3455 0.0281  256  ASP F OD1 
17176 O  OD2 . ASP F  146 ? 2.1675 2.1145 4.3296 -0.3260 -0.2451 0.0147  256  ASP F OD2 
17177 N  N   . SER F  147 ? 2.5981 2.4737 4.2668 -0.1775 -0.3578 0.1221  257  SER F N   
17178 C  CA  . SER F  147 ? 2.5619 2.4674 4.1625 -0.1477 -0.4173 0.1410  257  SER F CA  
17179 C  C   . SER F  147 ? 2.2963 2.3069 4.0311 -0.1754 -0.4606 0.1179  257  SER F C   
17180 O  O   . SER F  147 ? 2.1858 2.2441 4.0130 -0.2356 -0.4752 0.0628  257  SER F O   
17181 C  CB  . SER F  147 ? 2.7015 2.5618 4.1200 -0.1582 -0.4758 0.1207  257  SER F CB  
17182 O  OG  . SER F  147 ? 2.8373 2.7170 4.2518 -0.2252 -0.5103 0.0580  257  SER F OG  
17183 N  N   . HIS F  148 ? 2.2648 2.3154 4.0166 -0.1292 -0.4800 0.1570  258  HIS F N   
17184 C  CA  . HIS F  148 ? 2.2809 2.4415 4.1595 -0.1440 -0.5257 0.1413  258  HIS F CA  
17185 C  C   . HIS F  148 ? 2.4219 2.6196 4.2124 -0.1752 -0.6195 0.1024  258  HIS F C   
17186 O  O   . HIS F  148 ? 2.6043 2.7408 4.2249 -0.1579 -0.6512 0.1160  258  HIS F O   
17187 C  CB  . HIS F  148 ? 2.3316 2.5206 4.2508 -0.0768 -0.5142 0.1990  258  HIS F CB  
17188 C  CG  . HIS F  148 ? 2.3962 2.5863 4.4411 -0.0493 -0.4244 0.2357  258  HIS F CG  
17189 N  ND1 . HIS F  148 ? 2.4640 2.7327 4.7115 -0.0810 -0.3940 0.2203  258  HIS F ND1 
17190 C  CD2 . HIS F  148 ? 2.4216 2.5478 4.4184 0.0078  -0.3566 0.2880  258  HIS F CD2 
17191 C  CE1 . HIS F  148 ? 2.4325 2.6808 4.7502 -0.0441 -0.3068 0.2685  258  HIS F CE1 
17192 N  NE2 . HIS F  148 ? 2.4535 2.6188 4.6159 0.0122  -0.2842 0.3101  258  HIS F NE2 
17193 N  N   . PHE F  149 ? 2.3292 2.6313 4.2382 -0.2212 -0.6627 0.0534  259  PHE F N   
17194 C  CA  . PHE F  149 ? 2.2835 2.6462 4.1200 -0.2427 -0.7562 0.0215  259  PHE F CA  
17195 C  C   . PHE F  149 ? 2.2257 2.7102 4.1785 -0.2234 -0.8061 0.0291  259  PHE F C   
17196 O  O   . PHE F  149 ? 2.1982 2.7012 4.2515 -0.1797 -0.7692 0.0725  259  PHE F O   
17197 C  CB  . PHE F  149 ? 2.2427 2.6309 4.0838 -0.3181 -0.7788 -0.0589 259  PHE F CB  
17198 C  CG  . PHE F  149 ? 2.1464 2.5777 4.1846 -0.3641 -0.7307 -0.1058 259  PHE F CG  
17199 C  CD1 . PHE F  149 ? 2.0954 2.4389 4.1594 -0.3740 -0.6473 -0.1025 259  PHE F CD1 
17200 C  CD2 . PHE F  149 ? 2.0949 2.6554 4.2961 -0.3980 -0.7693 -0.1548 259  PHE F CD2 
17201 C  CE1 . PHE F  149 ? 2.0407 2.4132 4.2918 -0.4162 -0.5974 -0.1408 259  PHE F CE1 
17202 C  CE2 . PHE F  149 ? 2.0798 2.6745 4.4750 -0.4450 -0.7209 -0.2017 259  PHE F CE2 
17203 C  CZ  . PHE F  149 ? 2.0545 2.5495 4.4754 -0.4542 -0.6322 -0.1920 259  PHE F CZ  
17204 N  N   . GLY F  150 ? 2.1474 2.7214 4.0844 -0.2521 -0.8904 -0.0125 260  GLY F N   
17205 C  CA  . GLY F  150 ? 2.1722 2.8715 4.2010 -0.2297 -0.9522 -0.0061 260  GLY F CA  
17206 C  C   . GLY F  150 ? 2.1389 2.9286 4.4035 -0.2333 -0.9171 -0.0161 260  GLY F C   
17207 O  O   . GLY F  150 ? 2.1093 2.8965 4.4953 -0.2790 -0.8605 -0.0552 260  GLY F O   
17208 N  N   . MET F  151 ? 2.1484 3.0171 4.4858 -0.1842 -0.9469 0.0210  261  MET F N   
17209 C  CA  . MET F  151 ? 2.1266 3.1088 4.6965 -0.1836 -0.9281 0.0123  261  MET F CA  
17210 C  C   . MET F  151 ? 2.0768 2.9934 4.7464 -0.1680 -0.8169 0.0484  261  MET F C   
17211 O  O   . MET F  151 ? 2.0592 3.0611 4.9276 -0.1647 -0.7859 0.0500  261  MET F O   
17212 C  CB  . MET F  151 ? 2.1386 3.2498 4.8593 -0.2575 -0.9686 -0.0787 261  MET F CB  
17213 C  CG  . MET F  151 ? 2.1969 3.4256 4.8669 -0.2610 -1.0857 -0.1120 261  MET F CG  
17214 S  SD  . MET F  151 ? 2.2257 3.5693 4.9854 -0.3568 -1.1375 -0.2368 261  MET F SD  
17215 C  CE  . MET F  151 ? 2.2842 3.8295 5.1040 -0.3346 -1.2604 -0.2573 261  MET F CE  
17216 N  N   . ASP F  152 ? 2.0588 2.8336 4.5999 -0.1564 -0.7549 0.0786  262  ASP F N   
17217 C  CA  . ASP F  152 ? 2.0608 2.7736 4.6717 -0.1304 -0.6503 0.1226  262  ASP F CA  
17218 C  C   . ASP F  152 ? 2.0228 2.7311 4.6241 -0.0482 -0.6305 0.1938  262  ASP F C   
17219 O  O   . ASP F  152 ? 2.0021 2.7092 4.7122 -0.0225 -0.5501 0.2287  262  ASP F O   
17220 C  CB  . ASP F  152 ? 2.1913 2.7644 4.6615 -0.1399 -0.5973 0.1296  262  ASP F CB  
17221 C  CG  . ASP F  152 ? 2.2645 2.8364 4.8074 -0.2172 -0.5774 0.0650  262  ASP F CG  
17222 O  OD1 . ASP F  152 ? 2.1185 2.7776 4.8633 -0.2572 -0.5621 0.0290  262  ASP F OD1 
17223 O  OD2 . ASP F  152 ? 2.3663 2.8501 4.7720 -0.2385 -0.5752 0.0474  262  ASP F OD2 
17224 N  N   . SER F  153 ? 2.0522 2.7605 4.5324 -0.0057 -0.6991 0.2163  263  SER F N   
17225 C  CA  . SER F  153 ? 2.0602 2.7644 4.5327 0.0742  -0.6862 0.2774  263  SER F CA  
17226 C  C   . SER F  153 ? 2.0618 2.9101 4.7337 0.0894  -0.7044 0.2778  263  SER F C   
17227 O  O   . SER F  153 ? 2.0695 2.9302 4.7649 0.1570  -0.6897 0.3253  263  SER F O   
17228 C  CB  . SER F  153 ? 2.1002 2.7396 4.3751 0.1136  -0.7492 0.3024  263  SER F CB  
17229 O  OG  . SER F  153 ? 2.1356 2.8455 4.3848 0.0821  -0.8443 0.2690  263  SER F OG  
17230 N  N   . LYS F  154 ? 2.0571 3.0178 4.8797 0.0279  -0.7349 0.2210  264  LYS F N   
17231 C  CA  . LYS F  154 ? 2.0564 3.1671 5.0917 0.0354  -0.7501 0.2131  264  LYS F CA  
17232 C  C   . LYS F  154 ? 2.0277 3.1371 5.2005 0.0679  -0.6464 0.2551  264  LYS F C   
17233 O  O   . LYS F  154 ? 2.0315 3.2321 5.3284 0.1109  -0.6467 0.2789  264  LYS F O   
17234 C  CB  . LYS F  154 ? 2.0571 3.2813 5.2351 -0.0465 -0.7917 0.1324  264  LYS F CB  
17235 C  CG  . LYS F  154 ? 2.0563 3.4510 5.4764 -0.0504 -0.8108 0.1106  264  LYS F CG  
17236 C  CD  . LYS F  154 ? 2.0677 3.5746 5.6037 -0.1336 -0.8677 0.0179  264  LYS F CD  
17237 C  CE  . LYS F  154 ? 2.0600 3.7344 5.8747 -0.1513 -0.8665 -0.0141 264  LYS F CE  
17238 N  NZ  . LYS F  154 ? 2.0765 3.8469 5.9257 -0.0791 -0.9167 0.0278  264  LYS F NZ  
17239 N  N   . LEU F  155 ? 2.0046 3.0158 5.1573 0.0509  -0.5556 0.2671  265  LEU F N   
17240 C  CA  . LEU F  155 ? 1.9888 2.9898 5.2459 0.0880  -0.4498 0.3165  265  LEU F CA  
17241 C  C   . LEU F  155 ? 2.0030 2.9600 5.1523 0.1799  -0.4380 0.3787  265  LEU F C   
17242 O  O   . LEU F  155 ? 2.0031 3.0160 5.2716 0.2253  -0.3879 0.4140  265  LEU F O   
17243 C  CB  . LEU F  155 ? 1.9738 2.8683 5.1977 0.0594  -0.3604 0.3242  265  LEU F CB  
17244 C  CG  . LEU F  155 ? 1.9661 2.8729 5.2751 -0.0311 -0.3634 0.2604  265  LEU F CG  
17245 C  CD1 . LEU F  155 ? 1.9591 2.7436 5.2076 -0.0427 -0.2748 0.2812  265  LEU F CD1 
17246 C  CD2 . LEU F  155 ? 1.9625 3.0056 5.5429 -0.0740 -0.3501 0.2272  265  LEU F CD2 
17247 N  N   . ALA F  156 ? 2.0201 2.8791 4.9508 0.2072  -0.4824 0.3895  266  ALA F N   
17248 C  CA  . ALA F  156 ? 2.0413 2.8460 4.8628 0.2915  -0.4731 0.4398  266  ALA F CA  
17249 C  C   . ALA F  156 ? 2.0674 2.9660 4.9478 0.3338  -0.5427 0.4482  266  ALA F C   
17250 O  O   . ALA F  156 ? 2.0886 2.9619 4.9282 0.4082  -0.5262 0.4887  266  ALA F O   
17251 C  CB  . ALA F  156 ? 2.0559 2.7217 4.6357 0.3013  -0.4955 0.4443  266  ALA F CB  
17252 N  N   . GLY F  157 ? 2.0719 3.0810 5.0477 0.2911  -0.6202 0.4088  267  GLY F N   
17253 C  CA  . GLY F  157 ? 2.1042 3.2076 5.1263 0.3332  -0.6969 0.4179  267  GLY F CA  
17254 C  C   . GLY F  157 ? 2.1474 3.2036 4.9885 0.3413  -0.7914 0.4175  267  GLY F C   
17255 O  O   . GLY F  157 ? 2.1880 3.2715 5.0095 0.4008  -0.8421 0.4474  267  GLY F O   
17256 N  N   . ILE F  158 ? 2.1458 3.1300 4.8556 0.2854  -0.8128 0.3876  268  ILE F N   
17257 C  CA  . ILE F  158 ? 2.1924 3.1246 4.7202 0.2861  -0.8940 0.3889  268  ILE F CA  
17258 C  C   . ILE F  158 ? 2.2019 3.2360 4.7732 0.2163  -0.9678 0.3307  268  ILE F C   
17259 O  O   . ILE F  158 ? 2.1710 3.1970 4.7646 0.1473  -0.9423 0.2831  268  ILE F O   
17260 C  CB  . ILE F  158 ? 2.1900 2.9536 4.5163 0.2818  -0.8559 0.4006  268  ILE F CB  
17261 C  CG1 . ILE F  158 ? 2.1752 2.8546 4.4849 0.3423  -0.7701 0.4431  268  ILE F CG1 
17262 C  CG2 . ILE F  158 ? 2.2611 2.9641 4.4051 0.2954  -0.9300 0.4157  268  ILE F CG2 
17263 C  CD1 . ILE F  158 ? 2.1696 2.6965 4.2999 0.3379  -0.7277 0.4481  268  ILE F CD1 
17264 N  N   . VAL F  159 ? 2.2504 3.3862 4.8392 0.2365  -1.0592 0.3321  269  VAL F N   
17265 C  CA  . VAL F  159 ? 2.2707 3.5262 4.9040 0.1773  -1.1376 0.2725  269  VAL F CA  
17266 C  C   . VAL F  159 ? 2.3447 3.5875 4.7980 0.1903  -1.2303 0.2860  269  VAL F C   
17267 O  O   . VAL F  159 ? 2.3779 3.7304 4.8464 0.1514  -1.3063 0.2398  269  VAL F O   
17268 C  CB  . VAL F  159 ? 2.2633 3.7051 5.1359 0.1774  -1.1652 0.2460  269  VAL F CB  
17269 C  CG1 . VAL F  159 ? 2.1967 3.6576 5.2539 0.1392  -1.0724 0.2188  269  VAL F CG1 
17270 C  CG2 . VAL F  159 ? 2.2945 3.7770 5.2021 0.2668  -1.1884 0.3073  269  VAL F CG2 
17271 N  N   . CYS F  160 ? 2.3790 3.4923 4.6631 0.2446  -1.2244 0.3479  270  CYS F N   
17272 C  CA  . CYS F  160 ? 2.4571 3.5365 4.5574 0.2542  -1.2992 0.3692  270  CYS F CA  
17273 C  C   . CYS F  160 ? 2.4478 3.4197 4.3933 0.1915  -1.2782 0.3377  270  CYS F C   
17274 O  O   . CYS F  160 ? 2.4111 3.2447 4.2847 0.1927  -1.2044 0.3528  270  CYS F O   
17275 C  CB  . CYS F  160 ? 2.5083 3.4918 4.5075 0.3378  -1.3001 0.4488  270  CYS F CB  
17276 S  SG  . CYS F  160 ? 2.5370 3.6218 4.6901 0.4308  -1.3248 0.4999  270  CYS F SG  
17277 N  N   . PRO F  161 ? 2.4822 3.5192 4.3760 0.1377  -1.3396 0.2907  271  PRO F N   
17278 C  CA  . PRO F  161 ? 2.5445 3.4877 4.3016 0.0763  -1.3169 0.2549  271  PRO F CA  
17279 C  C   . PRO F  161 ? 2.7015 3.4852 4.2508 0.1063  -1.3023 0.3116  271  PRO F C   
17280 O  O   . PRO F  161 ? 2.8010 3.5531 4.2922 0.1709  -1.3270 0.3769  271  PRO F O   
17281 C  CB  . PRO F  161 ? 2.5255 3.5959 4.2698 0.0279  -1.4005 0.1978  271  PRO F CB  
17282 C  CG  . PRO F  161 ? 2.5274 3.7732 4.4649 0.0440  -1.4474 0.1792  271  PRO F CG  
17283 C  CD  . PRO F  161 ? 2.5296 3.7452 4.5040 0.1291  -1.4312 0.2591  271  PRO F CD  
17284 N  N   . ASN F  162 ? 2.7681 3.4499 4.2138 0.0579  -1.2595 0.2842  272  ASN F N   
17285 C  CA  . ASN F  162 ? 2.8548 3.3879 4.1096 0.0734  -1.2422 0.3260  272  ASN F CA  
17286 C  C   . ASN F  162 ? 2.9216 3.4788 4.0327 0.0591  -1.3158 0.3319  272  ASN F C   
17287 O  O   . ASN F  162 ? 2.8917 3.5179 3.9886 0.0003  -1.3454 0.2732  272  ASN F O   
17288 C  CB  . ASN F  162 ? 2.8488 3.2741 4.0593 0.0300  -1.1669 0.2935  272  ASN F CB  
17289 C  CG  . ASN F  162 ? 2.9744 3.2441 4.0198 0.0531  -1.1362 0.3362  272  ASN F CG  
17290 O  OD1 . ASN F  162 ? 3.0247 3.2495 3.9256 0.0289  -1.1614 0.3368  272  ASN F OD1 
17291 N  ND2 . ASN F  162 ? 2.8936 3.0845 3.9633 0.0991  -1.0794 0.3685  272  ASN F ND2 
17292 N  N   . ASP F  163 ? 2.9271 3.4293 3.9347 0.1146  -1.3433 0.4031  273  ASP F N   
17293 C  CA  . ASP F  163 ? 2.9736 3.4909 3.8346 0.1114  -1.4079 0.4263  273  ASP F CA  
17294 C  C   . ASP F  163 ? 3.0228 3.4264 3.7179 0.0646  -1.3777 0.4139  273  ASP F C   
17295 O  O   . ASP F  163 ? 3.0778 3.5031 3.6481 0.0481  -1.4242 0.4215  273  ASP F O   
17296 C  CB  . ASP F  163 ? 3.0273 3.5133 3.8431 0.1908  -1.4399 0.5156  273  ASP F CB  
17297 C  CG  . ASP F  163 ? 3.0998 3.4264 3.8895 0.2320  -1.3722 0.5612  273  ASP F CG  
17298 O  OD1 . ASP F  163 ? 3.0171 3.2550 3.7946 0.1981  -1.3049 0.5273  273  ASP F OD1 
17299 O  OD2 . ASP F  163 ? 3.2696 3.5626 4.0537 0.3005  -1.3871 0.6287  273  ASP F OD2 
17300 N  N   . GLY F  164 ? 3.0029 3.2927 3.6924 0.0457  -1.3014 0.3967  274  GLY F N   
17301 C  CA  . GLY F  164 ? 3.0116 3.1948 3.5558 0.0041  -1.2695 0.3843  274  GLY F CA  
17302 C  C   . GLY F  164 ? 3.0960 3.1739 3.4959 0.0405  -1.2763 0.4565  274  GLY F C   
17303 O  O   . GLY F  164 ? 3.2520 3.3109 3.5167 0.0134  -1.2975 0.4634  274  GLY F O   
17304 N  N   . LEU F  165 ? 2.9921 3.0005 3.4234 0.1022  -1.2553 0.5103  275  LEU F N   
17305 C  CA  . LEU F  165 ? 3.1120 3.0084 3.4296 0.1410  -1.2549 0.5802  275  LEU F CA  
17306 C  C   . LEU F  165 ? 3.2926 3.0536 3.6151 0.1606  -1.1837 0.5848  275  LEU F C   
17307 O  O   . LEU F  165 ? 3.3362 3.0990 3.7432 0.1504  -1.1384 0.5411  275  LEU F O   
17308 C  CB  . LEU F  165 ? 3.0418 2.9929 3.3905 0.2082  -1.3115 0.6469  275  LEU F CB  
17309 C  CG  . LEU F  165 ? 3.0787 3.1701 3.4034 0.1958  -1.3901 0.6471  275  LEU F CG  
17310 C  CD1 . LEU F  165 ? 3.1620 3.3106 3.5267 0.2711  -1.4456 0.7172  275  LEU F CD1 
17311 C  CD2 . LEU F  165 ? 3.1642 3.2144 3.3166 0.1523  -1.3997 0.6529  275  LEU F CD2 
17312 N  N   . CYS F  166 ? 3.4565 3.1006 3.6876 0.1898  -1.1731 0.6382  276  CYS F N   
17313 C  CA  . CYS F  166 ? 3.5913 3.1046 3.8145 0.2075  -1.1102 0.6372  276  CYS F CA  
17314 C  C   . CYS F  166 ? 3.5701 3.0832 3.9027 0.2800  -1.1016 0.6643  276  CYS F C   
17315 O  O   . CYS F  166 ? 3.5860 3.0884 3.9206 0.3330  -1.1326 0.7241  276  CYS F O   
17316 C  CB  . CYS F  166 ? 3.6972 3.0841 3.7871 0.2011  -1.0989 0.6747  276  CYS F CB  
17317 S  SG  . CYS F  166 ? 4.0157 3.2522 4.0846 0.2006  -1.0224 0.6474  276  CYS F SG  
17318 N  N   . HIS F  167 ? 3.4592 2.9871 3.8841 0.2852  -1.0574 0.6227  277  HIS F N   
17319 C  CA  . HIS F  167 ? 3.2793 2.8145 3.8120 0.3525  -1.0400 0.6404  277  HIS F CA  
17320 C  C   . HIS F  167 ? 3.1742 2.6069 3.6997 0.3687  -0.9721 0.6165  277  HIS F C   
17321 O  O   . HIS F  167 ? 3.1657 2.6370 3.7777 0.3812  -0.9342 0.5874  277  HIS F O   
17322 C  CB  . HIS F  167 ? 3.0555 2.7334 3.7284 0.3537  -1.0517 0.6172  277  HIS F CB  
17323 C  CG  . HIS F  167 ? 2.9378 2.7342 3.6412 0.3520  -1.1245 0.6377  277  HIS F CG  
17324 N  ND1 . HIS F  167 ? 2.9086 2.7227 3.6263 0.4112  -1.1694 0.6970  277  HIS F ND1 
17325 C  CD2 . HIS F  167 ? 2.8712 2.7793 3.5948 0.3004  -1.1619 0.6037  277  HIS F CD2 
17326 C  CE1 . HIS F  167 ? 2.9005 2.8394 3.6412 0.3980  -1.2346 0.7006  277  HIS F CE1 
17327 N  NE2 . HIS F  167 ? 2.9069 2.9058 3.6519 0.3292  -1.2316 0.6405  277  HIS F NE2 
17328 N  N   . LEU F  168 ? 2.9654 2.2723 3.3903 0.3686  -0.9550 0.6277  278  LEU F N   
17329 C  CA  . LEU F  168 ? 2.8020 2.0130 3.2126 0.3856  -0.8968 0.5996  278  LEU F CA  
17330 C  C   . LEU F  168 ? 2.8844 2.0168 3.3092 0.4530  -0.8931 0.6373  278  LEU F C   
17331 O  O   . LEU F  168 ? 2.9805 2.0474 3.3460 0.4590  -0.9184 0.6805  278  LEU F O   
17332 C  CB  . LEU F  168 ? 2.7992 1.9294 3.0985 0.3280  -0.8749 0.5684  278  LEU F CB  
17333 C  CG  . LEU F  168 ? 2.7203 1.9175 3.0063 0.2628  -0.8719 0.5255  278  LEU F CG  
17334 C  CD1 . LEU F  168 ? 2.7527 1.8702 2.9308 0.2105  -0.8514 0.4978  278  LEU F CD1 
17335 C  CD2 . LEU F  168 ? 2.6246 1.8824 3.0021 0.2750  -0.8346 0.4897  278  LEU F CD2 
17336 N  N   . ASP F  169 ? 2.9422 2.0803 3.4468 0.5052  -0.8583 0.6221  279  ASP F N   
17337 C  CA  . ASP F  169 ? 3.1863 2.2577 3.7230 0.5751  -0.8503 0.6491  279  ASP F CA  
17338 C  C   . ASP F  169 ? 3.1441 2.0727 3.6032 0.5739  -0.8163 0.6280  279  ASP F C   
17339 O  O   . ASP F  169 ? 3.0331 1.9133 3.4051 0.5163  -0.8076 0.6033  279  ASP F O   
17340 C  CB  . ASP F  169 ? 3.2462 2.3835 3.8965 0.6312  -0.8205 0.6339  279  ASP F CB  
17341 C  CG  . ASP F  169 ? 2.9726 2.1329 3.6244 0.6095  -0.7689 0.5768  279  ASP F CG  
17342 O  OD1 . ASP F  169 ? 2.8264 1.9286 3.3898 0.5625  -0.7517 0.5437  279  ASP F OD1 
17343 O  OD2 . ASP F  169 ? 2.7508 1.9905 3.4946 0.6416  -0.7436 0.5679  279  ASP F OD2 
17344 N  N   . SER F  170 ? 3.1362 2.0001 3.6350 0.6373  -0.7956 0.6325  280  SER F N   
17345 C  CA  . SER F  170 ? 3.1103 1.8409 3.5536 0.6389  -0.7621 0.6028  280  SER F CA  
17346 C  C   . SER F  170 ? 3.0735 1.8056 3.4914 0.6169  -0.7169 0.5294  280  SER F C   
17347 O  O   . SER F  170 ? 3.0859 1.7251 3.4422 0.5943  -0.6945 0.4924  280  SER F O   
17348 C  CB  . SER F  170 ? 3.1836 1.8506 3.6882 0.7157  -0.7504 0.6188  280  SER F CB  
17349 O  OG  . SER F  170 ? 3.1320 1.8826 3.7278 0.7694  -0.7309 0.6012  280  SER F OG  
17350 N  N   . LYS F  171 ? 3.0223 1.8606 3.4897 0.6235  -0.7024 0.5091  281  LYS F N   
17351 C  CA  . LYS F  171 ? 2.9386 1.7936 3.3801 0.6065  -0.6610 0.4495  281  LYS F CA  
17352 C  C   . LYS F  171 ? 2.9519 1.8353 3.3326 0.5308  -0.6707 0.4365  281  LYS F C   
17353 O  O   . LYS F  171 ? 2.9553 1.8631 3.3160 0.5141  -0.6395 0.3933  281  LYS F O   
17354 C  CB  . LYS F  171 ? 2.9451 1.8972 3.4719 0.6538  -0.6326 0.4415  281  LYS F CB  
17355 C  CG  . LYS F  171 ? 3.1466 2.0751 3.7332 0.7331  -0.6132 0.4424  281  LYS F CG  
17356 C  CD  . LYS F  171 ? 3.1796 2.2122 3.8511 0.7783  -0.5800 0.4385  281  LYS F CD  
17357 C  CE  . LYS F  171 ? 3.2566 2.2682 3.9866 0.8595  -0.5579 0.4351  281  LYS F CE  
17358 N  NZ  . LYS F  171 ? 3.2293 2.3470 4.0437 0.9049  -0.5199 0.4345  281  LYS F NZ  
17359 N  N   . ASN F  172 ? 2.9150 1.7981 3.2645 0.4884  -0.7125 0.4736  282  ASN F N   
17360 C  CA  . ASN F  172 ? 2.9241 1.8406 3.2201 0.4167  -0.7246 0.4618  282  ASN F CA  
17361 C  C   . ASN F  172 ? 2.8391 1.8683 3.1940 0.4062  -0.7135 0.4457  282  ASN F C   
17362 O  O   . ASN F  172 ? 2.7850 1.8324 3.1059 0.3598  -0.6986 0.4130  282  ASN F O   
17363 C  CB  . ASN F  172 ? 2.9602 1.7959 3.1699 0.3769  -0.6999 0.4173  282  ASN F CB  
17364 C  CG  . ASN F  172 ? 3.1362 1.8701 3.2819 0.3570  -0.7164 0.4400  282  ASN F CG  
17365 O  OD1 . ASN F  172 ? 3.1751 1.9147 3.3082 0.3458  -0.7532 0.4916  282  ASN F OD1 
17366 N  ND2 . ASN F  172 ? 3.2439 1.8873 3.3505 0.3528  -0.6884 0.4018  282  ASN F ND2 
17367 N  N   . GLU F  173 ? 2.9246 2.0292 3.3760 0.4496  -0.7180 0.4693  283  GLU F N   
17368 C  CA  . GLU F  173 ? 2.8710 2.0826 3.3993 0.4417  -0.7035 0.4597  283  GLU F CA  
17369 C  C   . GLU F  173 ? 2.7784 2.0787 3.3676 0.4253  -0.7520 0.4921  283  GLU F C   
17370 O  O   . GLU F  173 ? 2.8166 2.1050 3.3994 0.4408  -0.7947 0.5296  283  GLU F O   
17371 C  CB  . GLU F  173 ? 3.0558 2.2969 3.6606 0.5059  -0.6593 0.4540  283  GLU F CB  
17372 C  CG  . GLU F  173 ? 3.1921 2.3538 3.7369 0.5343  -0.6168 0.4188  283  GLU F CG  
17373 C  CD  . GLU F  173 ? 3.2027 2.4013 3.8146 0.6022  -0.5723 0.4134  283  GLU F CD  
17374 O  OE1 . GLU F  173 ? 3.1947 2.4865 3.9023 0.6168  -0.5635 0.4345  283  GLU F OE1 
17375 O  OE2 . GLU F  173 ? 3.1491 2.2874 3.7206 0.6402  -0.5444 0.3849  283  GLU F OE2 
17376 N  N   . TYR F  174 ? 2.6118 2.0044 3.2649 0.3953  -0.7449 0.4769  284  TYR F N   
17377 C  CA  . TYR F  174 ? 2.6331 2.1286 3.3638 0.3799  -0.7899 0.4957  284  TYR F CA  
17378 C  C   . TYR F  174 ? 2.7655 2.3169 3.6081 0.4454  -0.7924 0.5260  284  TYR F C   
17379 O  O   . TYR F  174 ? 2.8076 2.4213 3.7493 0.4657  -0.7542 0.5177  284  TYR F O   
17380 C  CB  . TYR F  174 ? 2.6522 2.2254 3.4352 0.3273  -0.7755 0.4633  284  TYR F CB  
17381 C  CG  . TYR F  174 ? 2.8237 2.5005 3.6675 0.2921  -0.8290 0.4653  284  TYR F CG  
17382 C  CD1 . TYR F  174 ? 2.9277 2.6300 3.7642 0.3100  -0.8901 0.4993  284  TYR F CD1 
17383 C  CD2 . TYR F  174 ? 2.9276 2.6795 3.8401 0.2431  -0.8185 0.4313  284  TYR F CD2 
17384 C  CE1 . TYR F  174 ? 3.0086 2.8194 3.8978 0.2805  -0.9439 0.4956  284  TYR F CE1 
17385 C  CE2 . TYR F  174 ? 2.8913 2.7452 3.8653 0.2090  -0.8693 0.4217  284  TYR F CE2 
17386 C  CZ  . TYR F  174 ? 2.9312 2.8198 3.8904 0.2282  -0.9342 0.4519  284  TYR F CZ  
17387 O  OH  . TYR F  174 ? 2.8262 2.8291 3.8433 0.1966  -0.9896 0.4372  284  TYR F OH  
17388 N  N   . SER F  175 ? 2.9049 2.4326 3.7343 0.4813  -0.8334 0.5643  285  SER F N   
17389 C  CA  . SER F  175 ? 2.8749 2.4512 3.8107 0.5497  -0.8373 0.5942  285  SER F CA  
17390 C  C   . SER F  175 ? 2.7516 2.4733 3.8117 0.5403  -0.8699 0.6009  285  SER F C   
17391 O  O   . SER F  175 ? 2.6110 2.4027 3.7933 0.5846  -0.8508 0.6087  285  SER F O   
17392 C  CB  . SER F  175 ? 3.0650 2.5682 3.9531 0.5928  -0.8720 0.6367  285  SER F CB  
17393 O  OG  . SER F  175 ? 3.0627 2.5868 3.9001 0.5596  -0.9351 0.6630  285  SER F OG  
17394 N  N   . MET F  176 ? 2.7115 2.4854 3.7471 0.4836  -0.9184 0.5942  286  MET F N   
17395 C  CA  . MET F  176 ? 2.6977 2.6176 3.8528 0.4675  -0.9567 0.5899  286  MET F CA  
17396 C  C   . MET F  176 ? 2.7022 2.6783 3.9153 0.4097  -0.9216 0.5418  286  MET F C   
17397 O  O   . MET F  176 ? 2.5986 2.6578 3.8425 0.3573  -0.9582 0.5174  286  MET F O   
17398 C  CB  . MET F  176 ? 2.6619 2.6183 3.7592 0.4461  -1.0362 0.6091  286  MET F CB  
17399 C  CG  . MET F  176 ? 2.7158 2.6010 3.7448 0.5023  -1.0677 0.6658  286  MET F CG  
17400 S  SD  . MET F  176 ? 2.7430 2.6934 3.9187 0.5937  -1.0753 0.7057  286  MET F SD  
17401 C  CE  . MET F  176 ? 2.7422 2.8839 4.0243 0.5746  -1.1529 0.7034  286  MET F CE  
17402 N  N   . SER F  177 ? 2.7611 2.6926 3.9908 0.4211  -0.8487 0.5272  287  SER F N   
17403 C  CA  . SER F  177 ? 2.5558 2.5285 3.8471 0.3753  -0.8039 0.4908  287  SER F CA  
17404 C  C   . SER F  177 ? 2.5631 2.6542 4.0362 0.3923  -0.7843 0.4928  287  SER F C   
17405 O  O   . SER F  177 ? 2.6713 2.8402 4.2340 0.3422  -0.7808 0.4643  287  SER F O   
17406 C  CB  . SER F  177 ? 2.4369 2.3105 3.6530 0.3826  -0.7340 0.4792  287  SER F CB  
17407 O  OG  . SER F  177 ? 2.3985 2.3054 3.6709 0.3419  -0.6888 0.4517  287  SER F OG  
17408 N  N   . THR F  178 ? 2.4309 2.5375 3.9678 0.4615  -0.7691 0.5237  288  THR F N   
17409 C  CA  . THR F  178 ? 2.2950 2.5197 4.0127 0.4832  -0.7498 0.5297  288  THR F CA  
17410 C  C   . THR F  178 ? 2.3264 2.6607 4.1292 0.4860  -0.8273 0.5385  288  THR F C   
17411 O  O   . THR F  178 ? 2.3100 2.7562 4.2757 0.5052  -0.8215 0.5425  288  THR F O   
17412 C  CB  . THR F  178 ? 2.3063 2.5043 4.0560 0.5608  -0.6929 0.5561  288  THR F CB  
17413 O  OG1 . THR F  178 ? 2.3734 2.5388 4.0804 0.6165  -0.7368 0.5850  288  THR F OG1 
17414 C  CG2 . THR F  178 ? 2.2911 2.3806 3.9327 0.5669  -0.6254 0.5468  288  THR F CG2 
17415 N  N   . VAL F  179 ? 2.3798 2.6889 4.0760 0.4694  -0.8985 0.5433  289  VAL F N   
17416 C  CA  . VAL F  179 ? 2.5292 2.9436 4.2833 0.4775  -0.9797 0.5556  289  VAL F CA  
17417 C  C   . VAL F  179 ? 2.5094 2.9973 4.2598 0.4013  -1.0313 0.5148  289  VAL F C   
17418 O  O   . VAL F  179 ? 2.5886 3.2131 4.4503 0.3940  -1.0852 0.5039  289  VAL F O   
17419 C  CB  . VAL F  179 ? 2.6242 2.9643 4.2646 0.5310  -1.0251 0.6031  289  VAL F CB  
17420 C  CG1 . VAL F  179 ? 2.6989 3.1602 4.4286 0.5668  -1.0997 0.6294  289  VAL F CG1 
17421 C  CG2 . VAL F  179 ? 2.6647 2.8956 4.2735 0.5946  -0.9645 0.6282  289  VAL F CG2 
17422 N  N   . LEU F  180 ? 2.3948 2.8034 4.0266 0.3453  -1.0162 0.4871  290  LEU F N   
17423 C  CA  . LEU F  180 ? 2.4174 2.8835 4.0259 0.2736  -1.0630 0.4434  290  LEU F CA  
17424 C  C   . LEU F  180 ? 2.4319 2.9098 4.1118 0.2128  -1.0065 0.3913  290  LEU F C   
17425 O  O   . LEU F  180 ? 2.4404 2.8352 4.1090 0.2200  -0.9307 0.3952  290  LEU F O   
17426 C  CB  . LEU F  180 ? 2.4727 2.8394 3.8819 0.2554  -1.0942 0.4528  290  LEU F CB  
17427 C  CG  . LEU F  180 ? 2.5456 2.8665 3.8679 0.3175  -1.1368 0.5140  290  LEU F CG  
17428 C  CD1 . LEU F  180 ? 2.6736 2.8928 3.8056 0.2919  -1.1566 0.5238  290  LEU F CD1 
17429 C  CD2 . LEU F  180 ? 2.6470 3.1082 4.0608 0.3451  -1.2116 0.5308  290  LEU F CD2 
17430 N  N   . GLU F  181 ? 2.3137 2.8965 4.0661 0.1542  -1.0447 0.3413  291  GLU F N   
17431 C  CA  . GLU F  181 ? 2.2642 2.8534 4.0862 0.0910  -0.9949 0.2885  291  GLU F CA  
17432 C  C   . GLU F  181 ? 2.3190 2.7823 3.9770 0.0566  -0.9681 0.2747  291  GLU F C   
17433 O  O   . GLU F  181 ? 2.3272 2.7146 3.8215 0.0699  -0.9976 0.2975  291  GLU F O   
17434 C  CB  . GLU F  181 ? 2.2634 2.9933 4.1990 0.0334  -1.0478 0.2280  291  GLU F CB  
17435 C  CG  . GLU F  181 ? 2.4005 3.2749 4.5276 0.0567  -1.0729 0.2287  291  GLU F CG  
17436 C  CD  . GLU F  181 ? 2.4736 3.4926 4.7093 -0.0044 -1.1317 0.1577  291  GLU F CD  
17437 O  OE1 . GLU F  181 ? 2.4325 3.4369 4.5736 -0.0590 -1.1598 0.1114  291  GLU F OE1 
17438 O  OE2 . GLU F  181 ? 2.5349 3.6872 4.9531 0.0024  -1.1503 0.1440  291  GLU F OE2 
17439 N  N   . TYR F  182 ? 2.4558 2.8975 4.1673 0.0129  -0.9080 0.2388  292  TYR F N   
17440 C  CA  . TYR F  182 ? 2.5455 2.8950 4.1275 -0.0301 -0.8897 0.2121  292  TYR F CA  
17441 C  C   . TYR F  182 ? 2.5436 2.9501 4.0707 -0.0843 -0.9626 0.1649  292  TYR F C   
17442 O  O   . TYR F  182 ? 2.4882 3.0194 4.1234 -0.1055 -1.0110 0.1332  292  TYR F O   
17443 C  CB  . TYR F  182 ? 2.5846 2.9100 4.2550 -0.0625 -0.8112 0.1852  292  TYR F CB  
17444 C  CG  . TYR F  182 ? 2.5822 2.8665 4.3131 -0.0103 -0.7334 0.2302  292  TYR F CG  
17445 C  CD1 . TYR F  182 ? 2.4968 2.8668 4.4083 0.0074  -0.7071 0.2415  292  TYR F CD1 
17446 C  CD2 . TYR F  182 ? 2.6159 2.7830 4.2253 0.0208  -0.6846 0.2585  292  TYR F CD2 
17447 C  CE1 . TYR F  182 ? 2.3844 2.7212 4.3436 0.0572  -0.6312 0.2845  292  TYR F CE1 
17448 C  CE2 . TYR F  182 ? 2.5183 2.6561 4.1716 0.0716  -0.6143 0.2969  292  TYR F CE2 
17449 C  CZ  . TYR F  182 ? 2.3415 2.5629 4.1653 0.0906  -0.5860 0.3120  292  TYR F CZ  
17450 O  OH  . TYR F  182 ? 2.2553 2.4511 4.1141 0.1439  -0.5118 0.3525  292  TYR F OH  
17451 N  N   . PRO F  183 ? 2.5661 2.8910 3.9261 -0.1060 -0.9726 0.1576  293  PRO F N   
17452 C  CA  . PRO F  183 ? 2.5837 2.9632 3.8819 -0.1591 -1.0338 0.1091  293  PRO F CA  
17453 C  C   . PRO F  183 ? 2.4120 2.8274 3.7991 -0.2275 -1.0080 0.0336  293  PRO F C   
17454 O  O   . PRO F  183 ? 2.3398 2.6921 3.7744 -0.2381 -0.9351 0.0258  293  PRO F O   
17455 C  CB  . PRO F  183 ? 2.6870 2.9533 3.7809 -0.1548 -1.0368 0.1338  293  PRO F CB  
17456 C  CG  . PRO F  183 ? 2.6679 2.8185 3.7432 -0.1278 -0.9599 0.1618  293  PRO F CG  
17457 C  CD  . PRO F  183 ? 2.5786 2.7646 3.7951 -0.0795 -0.9320 0.1935  293  PRO F CD  
17458 N  N   . THR F  184 ? 2.3090 2.8296 3.7196 -0.2718 -1.0692 -0.0230 294  THR F N   
17459 C  CA  . THR F  184 ? 2.2916 2.8501 3.7834 -0.3414 -1.0528 -0.1063 294  THR F CA  
17460 C  C   . THR F  184 ? 2.3150 2.7977 3.6441 -0.3784 -1.0488 -0.1355 294  THR F C   
17461 O  O   . THR F  184 ? 2.4316 2.8525 3.5895 -0.3551 -1.0694 -0.0943 294  THR F O   
17462 C  CB  . THR F  184 ? 2.3278 3.0471 3.9318 -0.3733 -1.1220 -0.1664 294  THR F CB  
17463 O  OG1 . THR F  184 ? 2.4059 3.1688 3.8593 -0.3780 -1.2010 -0.1752 294  THR F OG1 
17464 C  CG2 . THR F  184 ? 2.3199 3.1242 4.0682 -0.3288 -1.1380 -0.1297 294  THR F CG2 
17465 N  N   . ILE F  185 ? 2.2963 2.7833 3.6881 -0.4371 -1.0185 -0.2082 295  ILE F N   
17466 C  CA  . ILE F  185 ? 2.3210 2.7500 3.5732 -0.4756 -1.0143 -0.2460 295  ILE F CA  
17467 C  C   . ILE F  185 ? 2.4044 2.9079 3.5328 -0.4894 -1.0981 -0.2671 295  ILE F C   
17468 O  O   . ILE F  185 ? 2.4422 2.8852 3.3973 -0.4921 -1.1053 -0.2540 295  ILE F O   
17469 C  CB  . ILE F  185 ? 2.2922 2.7190 3.6556 -0.5341 -0.9662 -0.3248 295  ILE F CB  
17470 C  CG1 . ILE F  185 ? 2.2215 2.5593 3.6788 -0.5122 -0.8767 -0.2878 295  ILE F CG1 
17471 C  CG2 . ILE F  185 ? 2.3257 2.7111 3.5528 -0.5756 -0.9680 -0.3740 295  ILE F CG2 
17472 C  CD1 . ILE F  185 ? 2.2334 2.5406 3.7830 -0.5617 -0.8187 -0.3504 295  ILE F CD1 
17473 N  N   . GLY F  186 ? 2.4398 3.0811 3.6554 -0.4962 -1.1621 -0.2976 296  GLY F N   
17474 C  CA  . GLY F  186 ? 2.6176 3.3424 3.7103 -0.4980 -1.2465 -0.3072 296  GLY F CA  
17475 C  C   . GLY F  186 ? 2.5764 3.2403 3.5103 -0.4378 -1.2687 -0.2092 296  GLY F C   
17476 O  O   . GLY F  186 ? 2.6399 3.2857 3.4014 -0.4415 -1.2983 -0.1977 296  GLY F O   
17477 N  N   . GLN F  187 ? 2.6192 3.2489 3.6129 -0.3814 -1.2509 -0.1375 297  GLN F N   
17478 C  CA  . GLN F  187 ? 2.7447 3.3048 3.6051 -0.3219 -1.2655 -0.0454 297  GLN F CA  
17479 C  C   . GLN F  187 ? 2.7199 3.1296 3.4330 -0.3263 -1.2120 -0.0201 297  GLN F C   
17480 O  O   . GLN F  187 ? 2.8889 3.2539 3.4426 -0.3108 -1.2355 0.0229  297  GLN F O   
17481 C  CB  . GLN F  187 ? 2.6969 3.2519 3.6693 -0.2618 -1.2500 0.0146  297  GLN F CB  
17482 C  CG  . GLN F  187 ? 2.7131 3.4236 3.8373 -0.2509 -1.3055 -0.0032 297  GLN F CG  
17483 C  CD  . GLN F  187 ? 2.7432 3.4476 3.9716 -0.1869 -1.2871 0.0599  297  GLN F CD  
17484 O  OE1 . GLN F  187 ? 2.7548 3.3580 3.8966 -0.1352 -1.2665 0.1319  297  GLN F OE1 
17485 N  NE2 . GLN F  187 ? 2.6800 3.4945 4.1021 -0.1914 -1.2916 0.0290  297  GLN F NE2 
17486 N  N   . LEU F  188 ? 2.5121 2.8453 3.2805 -0.3463 -1.1387 -0.0445 298  LEU F N   
17487 C  CA  . LEU F  188 ? 2.5195 2.7212 3.1617 -0.3510 -1.0887 -0.0279 298  LEU F CA  
17488 C  C   . LEU F  188 ? 2.5594 2.7678 3.0697 -0.3993 -1.1110 -0.0702 298  LEU F C   
17489 O  O   . LEU F  188 ? 2.6094 2.7386 2.9698 -0.3921 -1.1053 -0.0343 298  LEU F O   
17490 C  CB  . LEU F  188 ? 2.4534 2.5922 3.1894 -0.3616 -1.0107 -0.0503 298  LEU F CB  
17491 C  CG  . LEU F  188 ? 2.4722 2.5722 3.2959 -0.3058 -0.9713 0.0046  298  LEU F CG  
17492 C  CD1 . LEU F  188 ? 2.4622 2.5221 3.3860 -0.3188 -0.8969 -0.0200 298  LEU F CD1 
17493 C  CD2 . LEU F  188 ? 2.5739 2.5744 3.2720 -0.2564 -0.9637 0.0731  298  LEU F CD2 
17494 N  N   . ILE F  189 ? 2.5714 2.8756 3.1399 -0.4500 -1.1338 -0.1498 299  ILE F N   
17495 C  CA  . ILE F  189 ? 2.8106 3.1354 3.2551 -0.4954 -1.1557 -0.1975 299  ILE F CA  
17496 C  C   . ILE F  189 ? 2.9992 3.3612 3.3002 -0.4704 -1.2205 -0.1474 299  ILE F C   
17497 O  O   . ILE F  189 ? 3.1179 3.4370 3.2619 -0.4842 -1.2198 -0.1376 299  ILE F O   
17498 C  CB  . ILE F  189 ? 2.7757 3.2063 3.3280 -0.5520 -1.1704 -0.3011 299  ILE F CB  
17499 C  CG1 . ILE F  189 ? 2.5878 2.9545 3.2551 -0.5801 -1.0941 -0.3456 299  ILE F CG1 
17500 C  CG2 . ILE F  189 ? 2.8624 3.3475 3.2826 -0.5924 -1.2092 -0.3534 299  ILE F CG2 
17501 C  CD1 . ILE F  189 ? 2.5230 2.9785 3.3192 -0.6369 -1.0988 -0.4498 299  ILE F CD1 
17502 N  N   . ASP F  190 ? 2.8608 3.2991 3.2141 -0.4292 -1.2732 -0.1078 300  ASP F N   
17503 C  CA  . ASP F  190 ? 2.8918 3.3729 3.1170 -0.3979 -1.3378 -0.0526 300  ASP F CA  
17504 C  C   . ASP F  190 ? 2.9377 3.2864 3.0430 -0.3531 -1.3119 0.0438  300  ASP F C   
17505 O  O   . ASP F  190 ? 3.0422 3.3930 3.0095 -0.3346 -1.3487 0.0943  300  ASP F O   
17506 C  CB  . ASP F  190 ? 2.8685 3.4799 3.2020 -0.3639 -1.4035 -0.0418 300  ASP F CB  
17507 C  CG  . ASP F  190 ? 2.9943 3.6771 3.2009 -0.3312 -1.4797 0.0083  300  ASP F CG  
17508 O  OD1 . ASP F  190 ? 3.0748 3.7723 3.1355 -0.3587 -1.4977 -0.0086 300  ASP F OD1 
17509 O  OD2 . ASP F  190 ? 3.0182 3.7454 3.2716 -0.2751 -1.5200 0.0671  300  ASP F OD2 
17510 N  N   . LYS F  191 ? 2.8443 3.0785 2.9974 -0.3355 -1.2479 0.0690  301  LYS F N   
17511 C  CA  . LYS F  191 ? 2.8117 2.9190 2.8683 -0.2953 -1.2208 0.1493  301  LYS F CA  
17512 C  C   . LYS F  191 ? 2.7793 2.7691 2.7591 -0.3265 -1.1562 0.1330  301  LYS F C   
17513 O  O   . LYS F  191 ? 2.8338 2.7230 2.7128 -0.3059 -1.1370 0.1889  301  LYS F O   
17514 C  CB  . LYS F  191 ? 2.7589 2.8310 2.9231 -0.2373 -1.2042 0.1983  301  LYS F CB  
17515 C  CG  . LYS F  191 ? 2.8160 2.9748 3.0210 -0.1874 -1.2683 0.2459  301  LYS F CG  
17516 C  CD  . LYS F  191 ? 2.9371 3.0672 2.9893 -0.1599 -1.3064 0.3165  301  LYS F CD  
17517 C  CE  . LYS F  191 ? 3.0042 3.2378 3.0961 -0.1087 -1.3775 0.3618  301  LYS F CE  
17518 N  NZ  . LYS F  191 ? 3.1343 3.3347 3.0774 -0.0757 -1.4112 0.4415  301  LYS F NZ  
17519 N  N   . LEU F  192 ? 2.7162 2.7172 2.7466 -0.3750 -1.1223 0.0575  302  LEU F N   
17520 C  CA  . LEU F  192 ? 2.7178 2.6224 2.6780 -0.4049 -1.0653 0.0368  302  LEU F CA  
17521 C  C   . LEU F  192 ? 2.7805 2.7017 2.6013 -0.4466 -1.0812 0.0147  302  LEU F C   
17522 O  O   . LEU F  192 ? 2.8058 2.6518 2.5550 -0.4721 -1.0370 0.0011  302  LEU F O   
17523 C  CB  . LEU F  192 ? 2.6109 2.5148 2.6895 -0.4328 -1.0173 -0.0290 302  LEU F CB  
17524 C  CG  . LEU F  192 ? 2.5716 2.4266 2.7632 -0.3925 -0.9759 -0.0027 302  LEU F CG  
17525 C  CD1 . LEU F  192 ? 2.4784 2.3325 2.7741 -0.4217 -0.9259 -0.0624 302  LEU F CD1 
17526 C  CD2 . LEU F  192 ? 2.6390 2.3776 2.7502 -0.3559 -0.9445 0.0552  302  LEU F CD2 
17527 N  N   . VAL F  193 ? 2.8534 2.8787 2.6351 -0.4525 -1.1430 0.0095  303  VAL F N   
17528 C  CA  . VAL F  193 ? 2.9498 3.0035 2.5862 -0.4855 -1.1615 -0.0043 303  VAL F CA  
17529 C  C   . VAL F  193 ? 3.0754 3.1070 2.5842 -0.4469 -1.1939 0.0880  303  VAL F C   
17530 O  O   . VAL F  193 ? 3.2470 3.2283 2.6185 -0.4626 -1.1764 0.1118  303  VAL F O   
17531 C  CB  . VAL F  193 ? 2.9791 3.1761 2.6489 -0.5233 -1.2069 -0.0868 303  VAL F CB  
17532 C  CG1 . VAL F  193 ? 3.0871 3.3192 2.5950 -0.5558 -1.2223 -0.1046 303  VAL F CG1 
17533 C  CG2 . VAL F  193 ? 2.8778 3.0846 2.6867 -0.5617 -1.1683 -0.1757 303  VAL F CG2 
17534 N  N   . GLN F  194 ? 3.1868 3.2536 2.7450 -0.3948 -1.2374 0.1438  304  GLN F N   
17535 C  CA  . GLN F  194 ? 3.2987 3.3273 2.7514 -0.3489 -1.2621 0.2424  304  GLN F CA  
17536 C  C   . GLN F  194 ? 3.3369 3.2057 2.7362 -0.3380 -1.2011 0.2947  304  GLN F C   
17537 O  O   . GLN F  194 ? 3.4730 3.2851 2.7519 -0.3233 -1.2010 0.3637  304  GLN F O   
17538 C  CB  . GLN F  194 ? 3.2404 3.3262 2.7839 -0.2898 -1.3118 0.2892  304  GLN F CB  
17539 C  CG  . GLN F  194 ? 3.2336 3.4900 2.8135 -0.2927 -1.3857 0.2511  304  GLN F CG  
17540 C  CD  . GLN F  194 ? 3.2358 3.5504 2.9174 -0.2315 -1.4324 0.2985  304  GLN F CD  
17541 O  OE1 . GLN F  194 ? 3.2257 3.4474 2.9281 -0.1823 -1.4115 0.3697  304  GLN F OE1 
17542 N  NE2 . GLN F  194 ? 3.2512 3.7242 3.0037 -0.2341 -1.4958 0.2539  304  GLN F NE2 
17543 N  N   . ASN F  195 ? 3.2489 3.0467 2.7392 -0.3440 -1.1486 0.2631  305  ASN F N   
17544 C  CA  . ASN F  195 ? 3.3324 2.9898 2.7846 -0.3394 -1.0902 0.2931  305  ASN F CA  
17545 C  C   . ASN F  195 ? 3.3685 2.9909 2.7855 -0.3962 -1.0401 0.2294  305  ASN F C   
17546 O  O   . ASN F  195 ? 3.4701 2.9865 2.8452 -0.4005 -0.9930 0.2457  305  ASN F O   
17547 C  CB  . ASN F  195 ? 3.3562 2.9597 2.9275 -0.2961 -1.0669 0.3076  305  ASN F CB  
17548 C  CG  . ASN F  195 ? 3.4139 3.0783 3.0565 -0.2418 -1.1165 0.3520  305  ASN F CG  
17549 O  OD1 . ASN F  195 ? 3.5221 3.2084 3.0985 -0.2155 -1.1595 0.4110  305  ASN F OD1 
17550 N  ND2 . ASN F  195 ? 3.3681 3.0638 3.1487 -0.2225 -1.1088 0.3266  305  ASN F ND2 
17551 N  N   . ASN F  196 ? 3.3049 3.0170 2.7445 -0.4392 -1.0498 0.1540  306  ASN F N   
17552 C  CA  . ASN F  196 ? 3.3595 3.0530 2.7765 -0.4923 -1.0050 0.0863  306  ASN F CA  
17553 C  C   . ASN F  196 ? 3.2676 2.8712 2.7598 -0.4861 -0.9469 0.0713  306  ASN F C   
17554 O  O   . ASN F  196 ? 3.2399 2.7511 2.6723 -0.4892 -0.9079 0.0919  306  ASN F O   
17555 C  CB  . ASN F  196 ? 3.5322 3.1937 2.7943 -0.5189 -0.9936 0.1080  306  ASN F CB  
17556 C  CG  . ASN F  196 ? 3.5875 3.2512 2.8252 -0.5749 -0.9525 0.0320  306  ASN F CG  
17557 O  OD1 . ASN F  196 ? 3.4538 3.1792 2.7706 -0.5998 -0.9518 -0.0440 306  ASN F OD1 
17558 N  ND2 . ASN F  196 ? 3.6995 3.2943 2.8362 -0.5950 -0.9150 0.0515  306  ASN F ND2 
17559 N  N   . VAL F  197 ? 3.1208 2.7550 2.7457 -0.4766 -0.9402 0.0355  307  VAL F N   
17560 C  CA  . VAL F  197 ? 3.0058 2.5690 2.7061 -0.4613 -0.8885 0.0260  307  VAL F CA  
17561 C  C   . VAL F  197 ? 3.0889 2.6918 2.8716 -0.4963 -0.8620 -0.0512 307  VAL F C   
17562 O  O   . VAL F  197 ? 3.1319 2.8207 2.9917 -0.5092 -0.8873 -0.0872 307  VAL F O   
17563 C  CB  . VAL F  197 ? 2.9566 2.5069 2.7455 -0.4041 -0.8958 0.0721  307  VAL F CB  
17564 C  CG1 . VAL F  197 ? 2.9065 2.3885 2.7565 -0.3843 -0.8415 0.0638  307  VAL F CG1 
17565 C  CG2 . VAL F  197 ? 3.0741 2.5843 2.7905 -0.3670 -0.9231 0.1476  307  VAL F CG2 
17566 N  N   . LEU F  198 ? 3.1726 2.7144 2.9453 -0.5114 -0.8110 -0.0778 308  LEU F N   
17567 C  CA  . LEU F  198 ? 3.0351 2.5963 2.8925 -0.5362 -0.7766 -0.1429 308  LEU F CA  
17568 C  C   . LEU F  198 ? 2.8355 2.3630 2.8009 -0.4946 -0.7442 -0.1258 308  LEU F C   
17569 O  O   . LEU F  198 ? 2.8206 2.2763 2.7609 -0.4658 -0.7156 -0.0967 308  LEU F O   
17570 C  CB  . LEU F  198 ? 3.0675 2.5915 2.8549 -0.5724 -0.7403 -0.1813 308  LEU F CB  
17571 C  CG  . LEU F  198 ? 3.2158 2.7799 2.8969 -0.6178 -0.7615 -0.2074 308  LEU F CG  
17572 C  CD1 . LEU F  198 ? 3.2189 2.7458 2.8513 -0.6501 -0.7165 -0.2474 308  LEU F CD1 
17573 C  CD2 . LEU F  198 ? 3.3395 3.0036 3.0699 -0.6450 -0.7949 -0.2600 308  LEU F CD2 
17574 N  N   . LEU F  199 ? 2.6661 2.2495 2.7533 -0.4916 -0.7472 -0.1455 309  LEU F N   
17575 C  CA  . LEU F  199 ? 2.6472 2.2118 2.8422 -0.4492 -0.7164 -0.1217 309  LEU F CA  
17576 C  C   . LEU F  199 ? 2.7312 2.2753 2.9913 -0.4616 -0.6620 -0.1625 309  LEU F C   
17577 O  O   . LEU F  199 ? 2.8788 2.4680 3.2085 -0.4980 -0.6567 -0.2147 309  LEU F O   
17578 C  CB  . LEU F  199 ? 2.6473 2.2860 2.9489 -0.4375 -0.7462 -0.1132 309  LEU F CB  
17579 C  CG  . LEU F  199 ? 2.5362 2.1655 2.9496 -0.3898 -0.7159 -0.0785 309  LEU F CG  
17580 C  CD1 . LEU F  199 ? 2.6072 2.1682 2.9535 -0.3376 -0.7080 -0.0200 309  LEU F CD1 
17581 C  CD2 . LEU F  199 ? 2.4919 2.2067 3.0136 -0.3859 -0.7491 -0.0757 309  LEU F CD2 
17582 N  N   . ILE F  200 ? 2.7008 2.1789 2.9404 -0.4297 -0.6224 -0.1404 310  ILE F N   
17583 C  CA  . ILE F  200 ? 2.5727 2.0282 2.8696 -0.4283 -0.5696 -0.1663 310  ILE F CA  
17584 C  C   . ILE F  200 ? 2.5899 2.0483 2.9986 -0.3825 -0.5401 -0.1330 310  ILE F C   
17585 O  O   . ILE F  200 ? 2.6464 2.0793 3.0381 -0.3337 -0.5375 -0.0848 310  ILE F O   
17586 C  CB  . ILE F  200 ? 2.6017 1.9961 2.8085 -0.4189 -0.5455 -0.1657 310  ILE F CB  
17587 C  CG1 . ILE F  200 ? 2.7360 2.1312 2.8428 -0.4690 -0.5648 -0.2007 310  ILE F CG1 
17588 C  CG2 . ILE F  200 ? 2.5748 1.9510 2.8461 -0.4023 -0.4928 -0.1806 310  ILE F CG2 
17589 C  CD1 . ILE F  200 ? 2.7739 2.1155 2.7996 -0.4651 -0.5426 -0.2028 310  ILE F CD1 
17590 N  N   . PHE F  201 ? 2.6452 2.1338 3.1709 -0.3983 -0.5143 -0.1594 311  PHE F N   
17591 C  CA  . PHE F  201 ? 2.6330 2.1246 3.2748 -0.3585 -0.4751 -0.1262 311  PHE F CA  
17592 C  C   . PHE F  201 ? 2.6266 2.0680 3.2685 -0.3274 -0.4187 -0.1158 311  PHE F C   
17593 O  O   . PHE F  201 ? 2.7179 2.1472 3.3692 -0.3548 -0.3960 -0.1557 311  PHE F O   
17594 C  CB  . PHE F  201 ? 2.5509 2.0977 3.3328 -0.3923 -0.4708 -0.1578 311  PHE F CB  
17595 C  CG  . PHE F  201 ? 2.5538 2.1664 3.3609 -0.4086 -0.5257 -0.1599 311  PHE F CG  
17596 C  CD1 . PHE F  201 ? 2.4956 2.1131 3.2683 -0.3671 -0.5520 -0.1066 311  PHE F CD1 
17597 C  CD2 . PHE F  201 ? 2.6193 2.2938 3.4879 -0.4633 -0.5522 -0.2190 311  PHE F CD2 
17598 C  CE1 . PHE F  201 ? 2.4981 2.1821 3.2980 -0.3770 -0.6046 -0.1058 311  PHE F CE1 
17599 C  CE2 . PHE F  201 ? 2.6047 2.3525 3.4970 -0.4750 -0.6077 -0.2229 311  PHE F CE2 
17600 C  CZ  . PHE F  201 ? 2.5057 2.2589 3.3639 -0.4303 -0.6344 -0.1630 311  PHE F CZ  
17601 N  N   . ALA F  202 ? 2.5139 1.9312 3.1444 -0.2673 -0.3969 -0.0638 312  ALA F N   
17602 C  CA  . ALA F  202 ? 2.5026 1.8835 3.1265 -0.2257 -0.3470 -0.0464 312  ALA F CA  
17603 C  C   . ALA F  202 ? 2.5480 1.9401 3.2700 -0.1754 -0.3039 0.0037  312  ALA F C   
17604 O  O   . ALA F  202 ? 2.6284 2.0167 3.3199 -0.1243 -0.3025 0.0459  312  ALA F O   
17605 C  CB  . ALA F  202 ? 2.5300 1.8750 3.0258 -0.1978 -0.3612 -0.0373 312  ALA F CB  
17606 N  N   . VAL F  203 ? 2.3915 1.7960 3.2345 -0.1898 -0.2647 -0.0017 313  VAL F N   
17607 C  CA  . VAL F  203 ? 2.3651 1.7828 3.3172 -0.1491 -0.2168 0.0485  313  VAL F CA  
17608 C  C   . VAL F  203 ? 2.3517 1.7397 3.3442 -0.1187 -0.1519 0.0686  313  VAL F C   
17609 O  O   . VAL F  203 ? 2.3715 1.7313 3.3000 -0.1221 -0.1484 0.0445  313  VAL F O   
17610 C  CB  . VAL F  203 ? 2.3728 1.8362 3.4608 -0.1911 -0.2230 0.0333  313  VAL F CB  
17611 C  CG1 . VAL F  203 ? 2.4427 1.9442 3.4900 -0.2097 -0.2893 0.0226  313  VAL F CG1 
17612 C  CG2 . VAL F  203 ? 2.3925 1.8555 3.5477 -0.2521 -0.2159 -0.0262 313  VAL F CG2 
17613 N  N   . THR F  204 ? 2.4739 1.8704 3.5750 -0.0862 -0.0981 0.1168  314  THR F N   
17614 C  CA  . THR F  204 ? 2.5425 1.9115 3.6978 -0.0530 -0.0299 0.1484  314  THR F CA  
17615 C  C   . THR F  204 ? 2.5997 1.9613 3.8896 -0.1089 -0.0039 0.1119  314  THR F C   
17616 O  O   . THR F  204 ? 2.6634 2.0517 4.0133 -0.1708 -0.0376 0.0624  314  THR F O   
17617 C  CB  . THR F  204 ? 2.5902 1.9697 3.7907 0.0143  0.0229  0.2262  314  THR F CB  
17618 O  OG1 . THR F  204 ? 2.5905 2.0071 3.9029 -0.0084 0.0224  0.2347  314  THR F OG1 
17619 C  CG2 . THR F  204 ? 2.5240 1.9065 3.5840 0.0761  0.0035  0.2539  314  THR F CG2 
17620 N  N   . GLN F  205 ? 2.5618 1.8885 3.9002 -0.0835 0.0566  0.1354  315  GLN F N   
17621 C  CA  . GLN F  205 ? 2.5273 1.8343 3.9958 -0.1322 0.0886  0.0978  315  GLN F CA  
17622 C  C   . GLN F  205 ? 2.6566 1.9923 4.2852 -0.1754 0.1002  0.0885  315  GLN F C   
17623 O  O   . GLN F  205 ? 2.7284 2.0793 4.4229 -0.2456 0.0732  0.0160  315  GLN F O   
17624 C  CB  . GLN F  205 ? 2.5751 1.8378 4.0864 -0.0815 0.1628  0.1480  315  GLN F CB  
17625 C  CG  . GLN F  205 ? 2.6776 1.9203 4.0525 -0.0427 0.1519  0.1467  315  GLN F CG  
17626 C  CD  . GLN F  205 ? 2.7383 1.9400 4.1738 -0.0030 0.2203  0.1831  315  GLN F CD  
17627 O  OE1 . GLN F  205 ? 2.5288 1.7045 4.1146 -0.0232 0.2725  0.1894  315  GLN F OE1 
17628 N  NE2 . GLN F  205 ? 2.8537 2.0506 4.1778 0.0545  0.2201  0.2059  315  GLN F NE2 
17629 N  N   . GLU F  206 ? 2.7723 2.1227 4.4676 -0.1343 0.1405  0.1577  316  GLU F N   
17630 C  CA  . GLU F  206 ? 2.7476 2.1293 4.6163 -0.1726 0.1608  0.1530  316  GLU F CA  
17631 C  C   . GLU F  206 ? 2.6067 2.0492 4.4667 -0.2251 0.0829  0.0952  316  GLU F C   
17632 O  O   . GLU F  206 ? 2.6908 2.1710 4.6992 -0.2723 0.0846  0.0658  316  GLU F O   
17633 C  CB  . GLU F  206 ? 2.6909 2.0802 4.6227 -0.1118 0.2241  0.2455  316  GLU F CB  
17634 C  CG  . GLU F  206 ? 2.5604 1.9839 4.3671 -0.0605 0.1893  0.2843  316  GLU F CG  
17635 C  CD  . GLU F  206 ? 2.5657 1.9582 4.2032 0.0068  0.1907  0.3195  316  GLU F CD  
17636 O  OE1 . GLU F  206 ? 2.6848 2.0341 4.3024 0.0169  0.2183  0.3190  316  GLU F OE1 
17637 O  OE2 . GLU F  206 ? 2.5185 1.9331 4.0485 0.0506  0.1637  0.3443  316  GLU F OE2 
17638 N  N   . GLN F  207 ? 2.2057 1.6607 3.9017 -0.2175 0.0154  0.0783  317  GLN F N   
17639 C  CA  . GLN F  207 ? 2.1752 1.6873 3.8471 -0.2564 -0.0595 0.0361  317  GLN F CA  
17640 C  C   . GLN F  207 ? 2.1202 1.6368 3.7234 -0.3172 -0.1183 -0.0473 317  GLN F C   
17641 O  O   . GLN F  207 ? 2.1189 1.6852 3.6896 -0.3501 -0.1843 -0.0837 317  GLN F O   
17642 C  CB  . GLN F  207 ? 2.2838 1.8069 3.8282 -0.2022 -0.0912 0.0832  317  GLN F CB  
17643 C  CG  . GLN F  207 ? 2.4196 2.0065 4.0306 -0.2041 -0.1192 0.0957  317  GLN F CG  
17644 C  CD  . GLN F  207 ? 2.4725 2.0783 4.2475 -0.1830 -0.0505 0.1444  317  GLN F CD  
17645 O  OE1 . GLN F  207 ? 2.3885 1.9528 4.1877 -0.1430 0.0209  0.1937  317  GLN F OE1 
17646 N  NE2 . GLN F  207 ? 2.5383 2.2110 4.4289 -0.2080 -0.0703 0.1335  317  GLN F NE2 
17647 N  N   . VAL F  208 ? 2.1745 1.6446 3.7574 -0.3307 -0.0945 -0.0770 318  VAL F N   
17648 C  CA  . VAL F  208 ? 2.1262 1.6024 3.6382 -0.3863 -0.1441 -0.1569 318  VAL F CA  
17649 C  C   . VAL F  208 ? 2.0539 1.5745 3.7007 -0.4565 -0.1576 -0.2299 318  VAL F C   
17650 O  O   . VAL F  208 ? 2.0437 1.6155 3.6447 -0.5004 -0.2232 -0.2855 318  VAL F O   
17651 C  CB  . VAL F  208 ? 2.1272 1.5443 3.5755 -0.3735 -0.1126 -0.1663 318  VAL F CB  
17652 C  CG1 . VAL F  208 ? 2.2436 1.6706 3.6338 -0.4340 -0.1547 -0.2529 318  VAL F CG1 
17653 C  CG2 . VAL F  208 ? 2.2054 1.5939 3.5118 -0.3087 -0.1126 -0.1079 318  VAL F CG2 
17654 N  N   . HIS F  209 ? 2.0814 1.5862 3.8994 -0.4667 -0.0953 -0.2304 319  HIS F N   
17655 C  CA  . HIS F  209 ? 2.0901 1.6369 4.0543 -0.5366 -0.1043 -0.3102 319  HIS F CA  
17656 C  C   . HIS F  209 ? 2.2474 1.8822 4.2406 -0.5604 -0.1654 -0.3272 319  HIS F C   
17657 O  O   . HIS F  209 ? 2.3848 2.0783 4.4293 -0.6214 -0.2091 -0.4106 319  HIS F O   
17658 C  CB  . HIS F  209 ? 2.1640 1.6739 4.3251 -0.5372 -0.0191 -0.2930 319  HIS F CB  
17659 C  CG  . HIS F  209 ? 2.2413 1.7833 4.5671 -0.6122 -0.0198 -0.3863 319  HIS F CG  
17660 N  ND1 . HIS F  209 ? 2.1681 1.7862 4.6242 -0.6493 -0.0436 -0.4155 319  HIS F ND1 
17661 C  CD2 . HIS F  209 ? 2.1853 1.6972 4.5738 -0.6566 0.0006  -0.4628 319  HIS F CD2 
17662 C  CE1 . HIS F  209 ? 2.2546 1.8923 4.8361 -0.7121 -0.0397 -0.5078 319  HIS F CE1 
17663 N  NE2 . HIS F  209 ? 2.3435 1.9217 4.8559 -0.7063 -0.0111 -0.5317 319  HIS F NE2 
17664 N  N   . LEU F  210 ? 2.1027 1.7530 4.0620 -0.5101 -0.1708 -0.2518 320  LEU F N   
17665 C  CA  . LEU F  210 ? 2.1596 1.8946 4.1328 -0.5216 -0.2324 -0.2589 320  LEU F CA  
17666 C  C   . LEU F  210 ? 2.1308 1.8898 3.9192 -0.5294 -0.3150 -0.2849 320  LEU F C   
17667 O  O   . LEU F  210 ? 2.0738 1.9005 3.8650 -0.5783 -0.3756 -0.3516 320  LEU F O   
17668 C  CB  . LEU F  210 ? 2.1344 1.8736 4.1421 -0.4607 -0.2016 -0.1682 320  LEU F CB  
17669 C  CG  . LEU F  210 ? 2.1773 2.0044 4.2615 -0.4608 -0.2401 -0.1584 320  LEU F CG  
17670 C  CD1 . LEU F  210 ? 2.2147 2.0296 4.3702 -0.4015 -0.1767 -0.0703 320  LEU F CD1 
17671 C  CD2 . LEU F  210 ? 2.1095 1.9740 4.0360 -0.4507 -0.3264 -0.1617 320  LEU F CD2 
17672 N  N   . TYR F  211 ? 2.1924 1.8979 3.8193 -0.4813 -0.3167 -0.2336 321  TYR F N   
17673 C  CA  . TYR F  211 ? 2.1938 1.9144 3.6502 -0.4827 -0.3876 -0.2428 321  TYR F CA  
17674 C  C   . TYR F  211 ? 2.1765 1.9018 3.5638 -0.5380 -0.4190 -0.3217 321  TYR F C   
17675 O  O   . TYR F  211 ? 2.1069 1.8662 3.3798 -0.5537 -0.4828 -0.3409 321  TYR F O   
17676 C  CB  . TYR F  211 ? 2.2313 1.8888 3.5484 -0.4211 -0.3746 -0.1753 321  TYR F CB  
17677 C  CG  . TYR F  211 ? 2.3274 2.0000 3.6539 -0.3666 -0.3759 -0.1058 321  TYR F CG  
17678 C  CD1 . TYR F  211 ? 2.4438 2.1207 3.9034 -0.3365 -0.3191 -0.0629 321  TYR F CD1 
17679 C  CD2 . TYR F  211 ? 2.4672 2.1461 3.6709 -0.3431 -0.4287 -0.0812 321  TYR F CD2 
17680 C  CE1 . TYR F  211 ? 2.5570 2.2521 4.0253 -0.2848 -0.3166 -0.0025 321  TYR F CE1 
17681 C  CE2 . TYR F  211 ? 2.5604 2.2514 3.7766 -0.2907 -0.4278 -0.0221 321  TYR F CE2 
17682 C  CZ  . TYR F  211 ? 2.6066 2.3087 3.9534 -0.2615 -0.3722 0.0148  321  TYR F CZ  
17683 O  OH  . TYR F  211 ? 2.6296 2.3481 3.9889 -0.2078 -0.3681 0.0705  321  TYR F OH  
17684 N  N   . GLU F  212 ? 2.3849 2.0778 3.8397 -0.5660 -0.3736 -0.3662 322  GLU F N   
17685 C  CA  . GLU F  212 ? 2.3764 2.0797 3.7714 -0.6188 -0.4003 -0.4479 322  GLU F CA  
17686 C  C   . GLU F  212 ? 2.2349 2.0316 3.6906 -0.6739 -0.4556 -0.5201 322  GLU F C   
17687 O  O   . GLU F  212 ? 2.2982 2.1307 3.6494 -0.7075 -0.5063 -0.5729 322  GLU F O   
17688 C  CB  . GLU F  212 ? 2.4589 2.1053 3.9263 -0.6324 -0.3358 -0.4812 322  GLU F CB  
17689 C  CG  . GLU F  212 ? 2.5221 2.1743 3.9171 -0.6812 -0.3567 -0.5657 322  GLU F CG  
17690 C  CD  . GLU F  212 ? 2.6243 2.2192 4.1011 -0.6912 -0.2914 -0.6000 322  GLU F CD  
17691 O  OE1 . GLU F  212 ? 2.6249 2.1721 4.2102 -0.6578 -0.2295 -0.5510 322  GLU F OE1 
17692 O  OE2 . GLU F  212 ? 2.6961 2.2937 4.1273 -0.7293 -0.2998 -0.6730 322  GLU F OE2 
17693 N  N   . ASN F  213 ? 2.1376 1.9809 3.7614 -0.6830 -0.4466 -0.5238 323  ASN F N   
17694 C  CA  . ASN F  213 ? 2.1736 2.1214 3.8618 -0.7313 -0.5064 -0.5932 323  ASN F CA  
17695 C  C   . ASN F  213 ? 2.1812 2.1887 3.7523 -0.7093 -0.5815 -0.5576 323  ASN F C   
17696 O  O   . ASN F  213 ? 2.2243 2.3206 3.7743 -0.7443 -0.6479 -0.6147 323  ASN F O   
17697 C  CB  . ASN F  213 ? 2.2213 2.2053 4.1394 -0.7485 -0.4723 -0.6080 323  ASN F CB  
17698 C  CG  . ASN F  213 ? 2.1778 2.1029 4.2286 -0.7762 -0.3979 -0.6500 323  ASN F CG  
17699 O  OD1 . ASN F  213 ? 2.1588 2.0404 4.3450 -0.7553 -0.3288 -0.6034 323  ASN F OD1 
17700 N  ND2 . ASN F  213 ? 2.2140 2.1361 4.2261 -0.8210 -0.4085 -0.7356 323  ASN F ND2 
17701 N  N   . TYR F  214 ? 2.1476 2.1093 3.6415 -0.6494 -0.5723 -0.4653 324  TYR F N   
17702 C  CA  . TYR F  214 ? 2.3648 2.3637 3.7323 -0.6237 -0.6388 -0.4264 324  TYR F CA  
17703 C  C   . TYR F  214 ? 2.4983 2.4792 3.6776 -0.6395 -0.6756 -0.4487 324  TYR F C   
17704 O  O   . TYR F  214 ? 2.6087 2.6561 3.7088 -0.6527 -0.7434 -0.4650 324  TYR F O   
17705 C  CB  . TYR F  214 ? 2.3862 2.3321 3.7253 -0.5555 -0.6125 -0.3290 324  TYR F CB  
17706 C  CG  . TYR F  214 ? 2.3841 2.3707 3.8896 -0.5336 -0.5905 -0.2966 324  TYR F CG  
17707 C  CD1 . TYR F  214 ? 2.3875 2.4563 4.0628 -0.5767 -0.5985 -0.3529 324  TYR F CD1 
17708 C  CD2 . TYR F  214 ? 2.3416 2.2880 3.8392 -0.4707 -0.5592 -0.2139 324  TYR F CD2 
17709 C  CE1 . TYR F  214 ? 2.4319 2.5411 4.2694 -0.5589 -0.5736 -0.3225 324  TYR F CE1 
17710 C  CE2 . TYR F  214 ? 2.3161 2.3027 3.9647 -0.4494 -0.5335 -0.1823 324  TYR F CE2 
17711 C  CZ  . TYR F  214 ? 2.4579 2.5254 4.2786 -0.4942 -0.5394 -0.2343 324  TYR F CZ  
17712 O  OH  . TYR F  214 ? 2.5094 2.6199 4.4899 -0.4748 -0.5092 -0.2017 324  TYR F OH  
17713 N  N   . ALA F  215 ? 2.4566 2.3530 3.5655 -0.6374 -0.6301 -0.4484 325  ALA F N   
17714 C  CA  . ALA F  215 ? 2.4227 2.2991 3.3625 -0.6548 -0.6544 -0.4699 325  ALA F CA  
17715 C  C   . ALA F  215 ? 2.3450 2.2938 3.2846 -0.7159 -0.6901 -0.5638 325  ALA F C   
17716 O  O   . ALA F  215 ? 2.3934 2.3576 3.1872 -0.7315 -0.7274 -0.5796 325  ALA F O   
17717 C  CB  . ALA F  215 ? 2.4577 2.2382 3.3496 -0.6402 -0.5941 -0.4567 325  ALA F CB  
17718 N  N   . LYS F  216 ? 2.4641 2.4572 3.5651 -0.7511 -0.6761 -0.6280 326  LYS F N   
17719 C  CA  . LYS F  216 ? 2.5980 2.6717 3.7092 -0.8095 -0.7137 -0.7287 326  LYS F CA  
17720 C  C   . LYS F  216 ? 2.7047 2.8867 3.7707 -0.8132 -0.7973 -0.7325 326  LYS F C   
17721 O  O   . LYS F  216 ? 2.9594 3.2048 3.9286 -0.8445 -0.8453 -0.7879 326  LYS F O   
17722 C  CB  . LYS F  216 ? 2.5654 2.6536 3.8799 -0.8464 -0.6734 -0.7997 326  LYS F CB  
17723 C  CG  . LYS F  216 ? 2.5053 2.4915 3.8648 -0.8445 -0.5919 -0.8036 326  LYS F CG  
17724 C  CD  . LYS F  216 ? 2.4580 2.4535 4.0230 -0.8794 -0.5481 -0.8681 326  LYS F CD  
17725 C  CE  . LYS F  216 ? 2.4224 2.3135 4.0170 -0.8627 -0.4612 -0.8528 326  LYS F CE  
17726 N  NZ  . LYS F  216 ? 2.4172 2.3084 4.1638 -0.8760 -0.4045 -0.8878 326  LYS F NZ  
17727 N  N   . LEU F  217 ? 2.3595 2.5696 3.4941 -0.7783 -0.8151 -0.6732 327  LEU F N   
17728 C  CA  . LEU F  217 ? 2.4061 2.7210 3.5010 -0.7720 -0.8962 -0.6667 327  LEU F CA  
17729 C  C   . LEU F  217 ? 2.4391 2.7248 3.3235 -0.7394 -0.9309 -0.6009 327  LEU F C   
17730 O  O   . LEU F  217 ? 2.5126 2.8669 3.2855 -0.7558 -0.9896 -0.6274 327  LEU F O   
17731 C  CB  . LEU F  217 ? 2.3667 2.7186 3.6075 -0.7411 -0.8995 -0.6209 327  LEU F CB  
17732 C  CG  . LEU F  217 ? 2.3363 2.7097 3.8022 -0.7725 -0.8555 -0.6752 327  LEU F CG  
17733 C  CD1 . LEU F  217 ? 2.3063 2.7243 3.9108 -0.7407 -0.8582 -0.6253 327  LEU F CD1 
17734 C  CD2 . LEU F  217 ? 2.3935 2.8631 3.9235 -0.8382 -0.8907 -0.7958 327  LEU F CD2 
17735 N  N   . ILE F  218 ? 2.5920 2.7781 3.4223 -0.6920 -0.8939 -0.5148 328  ILE F N   
17736 C  CA  . ILE F  218 ? 2.6426 2.7844 3.2923 -0.6589 -0.9171 -0.4463 328  ILE F CA  
17737 C  C   . ILE F  218 ? 2.6238 2.7284 3.1318 -0.6905 -0.9063 -0.4808 328  ILE F C   
17738 O  O   . ILE F  218 ? 2.5507 2.5796 3.0677 -0.7004 -0.8470 -0.4975 328  ILE F O   
17739 C  CB  . ILE F  218 ? 2.5888 2.6346 3.2378 -0.6029 -0.8752 -0.3589 328  ILE F CB  
17740 C  CG1 . ILE F  218 ? 2.6539 2.7384 3.4630 -0.5748 -0.8720 -0.3329 328  ILE F CG1 
17741 C  CG2 . ILE F  218 ? 2.6536 2.6591 3.1396 -0.5685 -0.9038 -0.2894 328  ILE F CG2 
17742 C  CD1 . ILE F  218 ? 2.6734 2.6748 3.4873 -0.5169 -0.8295 -0.2530 328  ILE F CD1 
17743 N  N   . PRO F  219 ? 2.5947 2.7529 2.9697 -0.7036 -0.9599 -0.4886 329  PRO F N   
17744 C  CA  . PRO F  219 ? 2.6823 2.8124 2.9217 -0.7349 -0.9458 -0.5215 329  PRO F CA  
17745 C  C   . PRO F  219 ? 2.5788 2.5900 2.7183 -0.7077 -0.9021 -0.4549 329  PRO F C   
17746 O  O   . PRO F  219 ? 2.5686 2.5384 2.6622 -0.6640 -0.9123 -0.3731 329  PRO F O   
17747 C  CB  . PRO F  219 ? 2.8184 3.0425 2.9385 -0.7438 -1.0169 -0.5264 329  PRO F CB  
17748 C  CG  . PRO F  219 ? 2.7248 2.9846 2.8762 -0.6981 -1.0631 -0.4572 329  PRO F CG  
17749 C  CD  . PRO F  219 ? 2.6210 2.8764 2.9661 -0.6882 -1.0354 -0.4667 329  PRO F CD  
17750 N  N   . GLY F  220 ? 2.7217 2.6805 2.8367 -0.7339 -0.8526 -0.4954 330  GLY F N   
17751 C  CA  . GLY F  220 ? 2.7543 2.6113 2.7850 -0.7147 -0.8105 -0.4476 330  GLY F CA  
17752 C  C   . GLY F  220 ? 2.8451 2.6270 2.9708 -0.6781 -0.7627 -0.4113 330  GLY F C   
17753 O  O   . GLY F  220 ? 2.8458 2.5526 2.9312 -0.6698 -0.7192 -0.3985 330  GLY F O   
17754 N  N   . ALA F  221 ? 2.7970 2.6035 3.0469 -0.6542 -0.7693 -0.3939 331  ALA F N   
17755 C  CA  . ALA F  221 ? 2.7661 2.5101 3.1033 -0.6141 -0.7226 -0.3541 331  ALA F CA  
17756 C  C   . ALA F  221 ? 2.7553 2.4714 3.1803 -0.6324 -0.6652 -0.4038 331  ALA F C   
17757 O  O   . ALA F  221 ? 2.6972 2.4626 3.2085 -0.6705 -0.6638 -0.4701 331  ALA F O   
17758 C  CB  . ALA F  221 ? 2.7684 2.5562 3.2185 -0.5856 -0.7426 -0.3227 331  ALA F CB  
17759 N  N   . THR F  222 ? 2.6648 2.3033 3.0708 -0.6036 -0.6182 -0.3735 332  THR F N   
17760 C  CA  . THR F  222 ? 2.5800 2.1832 3.0630 -0.6075 -0.5603 -0.4048 332  THR F CA  
17761 C  C   . THR F  222 ? 2.3759 1.9419 2.9495 -0.5553 -0.5212 -0.3504 332  THR F C   
17762 O  O   . THR F  222 ? 2.3929 1.9600 2.9649 -0.5179 -0.5380 -0.2941 332  THR F O   
17763 C  CB  . THR F  222 ? 2.5822 2.1376 2.9613 -0.6164 -0.5372 -0.4205 332  THR F CB  
17764 O  OG1 . THR F  222 ? 2.6882 2.1885 2.9955 -0.5718 -0.5296 -0.3580 332  THR F OG1 
17765 C  CG2 . THR F  222 ? 2.6770 2.2695 2.9461 -0.6625 -0.5742 -0.4611 332  THR F CG2 
17766 N  N   . VAL F  223 ? 2.3686 1.9030 3.0223 -0.5497 -0.4663 -0.3659 333  VAL F N   
17767 C  CA  . VAL F  223 ? 2.3597 1.8628 3.1001 -0.4987 -0.4214 -0.3135 333  VAL F CA  
17768 C  C   . VAL F  223 ? 2.3592 1.8026 3.0501 -0.4664 -0.3790 -0.2967 333  VAL F C   
17769 O  O   . VAL F  223 ? 2.5116 1.9408 3.1390 -0.4913 -0.3760 -0.3370 333  VAL F O   
17770 C  CB  . VAL F  223 ? 2.3145 1.8412 3.2253 -0.5146 -0.3899 -0.3368 333  VAL F CB  
17771 C  CG1 . VAL F  223 ? 2.4592 2.0516 3.4342 -0.5295 -0.4309 -0.3370 333  VAL F CG1 
17772 C  CG2 . VAL F  223 ? 2.4111 1.9417 3.3562 -0.5661 -0.3756 -0.4155 333  VAL F CG2 
17773 N  N   . GLY F  224 ? 2.3759 1.7919 3.0989 -0.4085 -0.3455 -0.2380 334  GLY F N   
17774 C  CA  . GLY F  224 ? 2.4902 1.8617 3.1689 -0.3686 -0.3091 -0.2182 334  GLY F CA  
17775 C  C   . GLY F  224 ? 2.5490 1.9052 3.3081 -0.3096 -0.2601 -0.1622 334  GLY F C   
17776 O  O   . GLY F  224 ? 2.8403 2.2157 3.6656 -0.2918 -0.2579 -0.1263 334  GLY F O   
17777 N  N   . LEU F  225 ? 2.2029 1.5295 2.9557 -0.2766 -0.2194 -0.1527 335  LEU F N   
17778 C  CA  . LEU F  225 ? 2.2999 1.6130 3.1179 -0.2145 -0.1669 -0.0948 335  LEU F CA  
17779 C  C   . LEU F  225 ? 2.5027 1.8050 3.2190 -0.1516 -0.1682 -0.0538 335  LEU F C   
17780 O  O   . LEU F  225 ? 2.5987 1.8923 3.2146 -0.1556 -0.1911 -0.0799 335  LEU F O   
17781 C  CB  . LEU F  225 ? 2.3554 1.6473 3.2578 -0.2141 -0.1146 -0.1078 335  LEU F CB  
17782 C  CG  . LEU F  225 ? 2.4729 1.7498 3.4577 -0.1511 -0.0521 -0.0407 335  LEU F CG  
17783 C  CD1 . LEU F  225 ? 2.2984 1.5925 3.3899 -0.1524 -0.0368 -0.0064 335  LEU F CD1 
17784 C  CD2 . LEU F  225 ? 2.6047 1.8536 3.6682 -0.1502 -0.0018 -0.0532 335  LEU F CD2 
17785 N  N   . LEU F  226 ? 2.6233 1.9303 3.3716 -0.0940 -0.1408 0.0070  336  LEU F N   
17786 C  CA  . LEU F  226 ? 2.4765 1.7818 3.1377 -0.0275 -0.1387 0.0446  336  LEU F CA  
17787 C  C   . LEU F  226 ? 2.4397 1.7380 3.1198 0.0288  -0.0863 0.0760  336  LEU F C   
17788 O  O   . LEU F  226 ? 2.3444 1.6405 3.1257 0.0494  -0.0358 0.1150  336  LEU F O   
17789 C  CB  . LEU F  226 ? 2.3534 1.6757 3.0286 0.0075  -0.1400 0.0917  336  LEU F CB  
17790 C  CG  . LEU F  226 ? 2.3752 1.6979 2.9397 0.0308  -0.1811 0.0930  336  LEU F CG  
17791 C  CD1 . LEU F  226 ? 2.3969 1.7089 2.8617 0.0648  -0.1834 0.0798  336  LEU F CD1 
17792 C  CD2 . LEU F  226 ? 2.3923 1.7134 2.9247 -0.0300 -0.2372 0.0555  336  LEU F CD2 
17793 N  N   . GLN F  227 ? 2.4869 1.7844 3.0731 0.0559  -0.0976 0.0615  337  GLN F N   
17794 C  CA  . GLN F  227 ? 2.5826 1.8843 3.1687 0.1188  -0.0564 0.0922  337  GLN F CA  
17795 C  C   . GLN F  227 ? 2.6837 2.0062 3.1569 0.1749  -0.0771 0.0992  337  GLN F C   
17796 O  O   . GLN F  227 ? 2.8106 2.1339 3.2122 0.1571  -0.1213 0.0734  337  GLN F O   
17797 C  CB  . GLN F  227 ? 2.6196 1.9092 3.2280 0.0905  -0.0469 0.0513  337  GLN F CB  
17798 C  CG  . GLN F  227 ? 2.6051 1.8734 3.3379 0.0444  -0.0163 0.0414  337  GLN F CG  
17799 C  CD  . GLN F  227 ? 2.5019 1.7574 3.2597 0.0266  -0.0008 0.0017  337  GLN F CD  
17800 O  OE1 . GLN F  227 ? 2.5451 1.8126 3.2242 0.0408  -0.0190 -0.0232 337  GLN F OE1 
17801 N  NE2 . GLN F  227 ? 2.4253 1.6582 3.3016 -0.0043 0.0345  -0.0077 337  GLN F NE2 
17802 N  N   . LYS F  228 ? 2.8173 2.1580 3.2778 0.2454  -0.0442 0.1339  338  LYS F N   
17803 C  CA  . LYS F  228 ? 2.9204 2.2919 3.2755 0.3006  -0.0655 0.1291  338  LYS F CA  
17804 C  C   . LYS F  228 ? 3.0991 2.4699 3.3865 0.2557  -0.1135 0.0567  338  LYS F C   
17805 O  O   . LYS F  228 ? 3.2033 2.5818 3.4129 0.2564  -0.1510 0.0294  338  LYS F O   
17806 C  CB  . LYS F  228 ? 2.7040 2.1048 3.0584 0.3836  -0.0239 0.1761  338  LYS F CB  
17807 C  CG  . LYS F  228 ? 2.5535 1.9592 2.9611 0.4397  0.0302  0.2573  338  LYS F CG  
17808 C  CD  . LYS F  228 ? 2.5538 1.9916 2.9444 0.5262  0.0690  0.3066  338  LYS F CD  
17809 C  CE  . LYS F  228 ? 2.6213 2.0645 3.0606 0.5870  0.1314  0.3967  338  LYS F CE  
17810 N  NZ  . LYS F  228 ? 2.6154 2.0921 3.0293 0.6774  0.1701  0.4529  338  LYS F NZ  
17811 N  N   . ASP F  229 ? 3.0204 2.3808 3.3430 0.2152  -0.1091 0.0236  339  ASP F N   
17812 C  CA  . ASP F  229 ? 2.8496 2.2072 3.1228 0.1593  -0.1483 -0.0453 339  ASP F CA  
17813 C  C   . ASP F  229 ? 2.8173 2.1427 3.1071 0.0800  -0.1708 -0.0695 339  ASP F C   
17814 O  O   . ASP F  229 ? 2.7790 2.0889 3.1302 0.0314  -0.1592 -0.0870 339  ASP F O   
17815 C  CB  . ASP F  229 ? 2.9217 2.2896 3.2247 0.1559  -0.1311 -0.0711 339  ASP F CB  
17816 C  CG  . ASP F  229 ? 3.0622 2.4740 3.3340 0.2358  -0.1204 -0.0536 339  ASP F CG  
17817 O  OD1 . ASP F  229 ? 3.0971 2.5372 3.2953 0.2735  -0.1445 -0.0556 339  ASP F OD1 
17818 O  OD2 . ASP F  229 ? 3.1129 2.5334 3.4356 0.2630  -0.0886 -0.0398 339  ASP F OD2 
17819 N  N   . SER F  230 ? 2.7024 2.0206 2.9388 0.0709  -0.2033 -0.0703 340  SER F N   
17820 C  CA  . SER F  230 ? 2.8770 2.1718 3.1194 0.0068  -0.2293 -0.0838 340  SER F CA  
17821 C  C   . SER F  230 ? 3.0894 2.3733 3.2864 -0.0604 -0.2585 -0.1411 340  SER F C   
17822 O  O   . SER F  230 ? 3.2075 2.4757 3.3864 -0.1103 -0.2862 -0.1521 340  SER F O   
17823 C  CB  . SER F  230 ? 3.0001 2.2895 3.2046 0.0286  -0.2513 -0.0586 340  SER F CB  
17824 O  OG  . SER F  230 ? 3.0917 2.3843 3.2151 0.0538  -0.2717 -0.0789 340  SER F OG  
17825 N  N   . GLY F  231 ? 2.9941 2.2901 3.1761 -0.0622 -0.2508 -0.1755 341  GLY F N   
17826 C  CA  . GLY F  231 ? 2.8031 2.0923 2.9538 -0.1287 -0.2690 -0.2280 341  GLY F CA  
17827 C  C   . GLY F  231 ? 2.4833 1.7653 2.6874 -0.1839 -0.2610 -0.2445 341  GLY F C   
17828 O  O   . GLY F  231 ? 2.4032 1.6823 2.5746 -0.2427 -0.2765 -0.2863 341  GLY F O   
17829 N  N   . ASN F  232 ? 2.6849 1.9668 2.9733 -0.1674 -0.2345 -0.2164 342  ASN F N   
17830 C  CA  . ASN F  232 ? 2.6180 1.8971 2.9619 -0.2254 -0.2309 -0.2445 342  ASN F CA  
17831 C  C   . ASN F  232 ? 2.6664 1.9435 2.9660 -0.2745 -0.2717 -0.2533 342  ASN F C   
17832 O  O   . ASN F  232 ? 2.5983 1.8805 2.8734 -0.3332 -0.2871 -0.2975 342  ASN F O   
17833 C  CB  . ASN F  232 ? 2.1763 1.4531 2.6319 -0.2043 -0.1948 -0.2147 342  ASN F CB  
17834 C  CG  . ASN F  232 ? 2.3258 1.6015 2.8643 -0.2599 -0.1770 -0.2628 342  ASN F CG  
17835 O  OD1 . ASN F  232 ? 2.5912 1.8706 3.1093 -0.3013 -0.1788 -0.3205 342  ASN F OD1 
17836 N  ND2 . ASN F  232 ? 2.1792 1.4512 2.8232 -0.2565 -0.1535 -0.2395 342  ASN F ND2 
17837 N  N   . ILE F  233 ? 2.7369 2.0098 3.0195 -0.2477 -0.2897 -0.2106 343  ILE F N   
17838 C  CA  . ILE F  233 ? 2.7364 2.0101 2.9834 -0.2877 -0.3294 -0.2120 343  ILE F CA  
17839 C  C   . ILE F  233 ? 2.6324 1.8949 2.7789 -0.3242 -0.3558 -0.2417 343  ILE F C   
17840 O  O   . ILE F  233 ? 2.6609 1.9281 2.7709 -0.3734 -0.3833 -0.2580 343  ILE F O   
17841 C  CB  . ILE F  233 ? 2.8126 2.0837 3.0657 -0.2449 -0.3409 -0.1595 343  ILE F CB  
17842 C  CG1 . ILE F  233 ? 2.8991 2.1808 3.2514 -0.2013 -0.3011 -0.1261 343  ILE F CG1 
17843 C  CG2 . ILE F  233 ? 2.7626 2.0437 3.0073 -0.2819 -0.3798 -0.1559 343  ILE F CG2 
17844 C  CD1 . ILE F  233 ? 3.0321 2.3178 3.4008 -0.1539 -0.3017 -0.0749 343  ILE F CD1 
17845 N  N   . LEU F  234 ? 2.4844 1.7370 2.5881 -0.3013 -0.3461 -0.2503 344  LEU F N   
17846 C  CA  . LEU F  234 ? 2.4534 1.6956 2.4766 -0.3391 -0.3621 -0.2814 344  LEU F CA  
17847 C  C   . LEU F  234 ? 2.3967 1.6547 2.4232 -0.3958 -0.3534 -0.3298 344  LEU F C   
17848 O  O   . LEU F  234 ? 2.3792 1.6337 2.3420 -0.4441 -0.3710 -0.3488 344  LEU F O   
17849 C  CB  . LEU F  234 ? 2.6287 1.8680 2.6261 -0.3012 -0.3514 -0.2885 344  LEU F CB  
17850 C  CG  . LEU F  234 ? 2.6148 1.8433 2.6005 -0.2418 -0.3590 -0.2510 344  LEU F CG  
17851 C  CD1 . LEU F  234 ? 2.5968 1.8324 2.5505 -0.2125 -0.3551 -0.2730 344  LEU F CD1 
17852 C  CD2 . LEU F  234 ? 2.6524 1.8529 2.5977 -0.2556 -0.3896 -0.2257 344  LEU F CD2 
17853 N  N   . GLN F  235 ? 2.4152 1.6898 2.5167 -0.3896 -0.3237 -0.3485 345  GLN F N   
17854 C  CA  . GLN F  235 ? 2.5689 1.8598 2.6814 -0.4415 -0.3126 -0.4015 345  GLN F CA  
17855 C  C   . GLN F  235 ? 2.6685 1.9711 2.7654 -0.4922 -0.3384 -0.4130 345  GLN F C   
17856 O  O   . GLN F  235 ? 2.8471 2.1648 2.9048 -0.5431 -0.3418 -0.4564 345  GLN F O   
17857 C  CB  . GLN F  235 ? 2.6636 1.9627 2.8739 -0.4200 -0.2735 -0.4162 345  GLN F CB  
17858 C  CG  . GLN F  235 ? 2.6115 1.9134 2.8280 -0.3776 -0.2487 -0.4189 345  GLN F CG  
17859 C  CD  . GLN F  235 ? 2.5257 1.8321 2.8390 -0.3567 -0.2078 -0.4311 345  GLN F CD  
17860 O  OE1 . GLN F  235 ? 2.4771 1.7804 2.8575 -0.3823 -0.1951 -0.4471 345  GLN F OE1 
17861 N  NE2 . GLN F  235 ? 2.4928 1.8080 2.8187 -0.3081 -0.1873 -0.4245 345  GLN F NE2 
17862 N  N   . LEU F  236 ? 2.4781 1.7814 2.6037 -0.4775 -0.3573 -0.3759 346  LEU F N   
17863 C  CA  . LEU F  236 ? 2.5147 1.8397 2.6196 -0.5197 -0.3906 -0.3837 346  LEU F CA  
17864 C  C   . LEU F  236 ? 2.6582 1.9751 2.6462 -0.5471 -0.4195 -0.3784 346  LEU F C   
17865 O  O   . LEU F  236 ? 2.7169 2.0560 2.6557 -0.5962 -0.4315 -0.4117 346  LEU F O   
17866 C  CB  . LEU F  236 ? 2.4606 1.7913 2.6186 -0.4910 -0.4075 -0.3386 346  LEU F CB  
17867 C  CG  . LEU F  236 ? 2.5117 1.8562 2.7964 -0.4726 -0.3843 -0.3339 346  LEU F CG  
17868 C  CD1 . LEU F  236 ? 2.6491 1.9953 2.9610 -0.4351 -0.4004 -0.2777 346  LEU F CD1 
17869 C  CD2 . LEU F  236 ? 2.6019 1.9835 2.9411 -0.5243 -0.3904 -0.3865 346  LEU F CD2 
17870 N  N   . ILE F  237 ? 2.5485 1.8328 2.4916 -0.5144 -0.4283 -0.3363 347  ILE F N   
17871 C  CA  . ILE F  237 ? 2.4054 1.6711 2.2498 -0.5354 -0.4542 -0.3184 347  ILE F CA  
17872 C  C   . ILE F  237 ? 2.4296 1.6953 2.2144 -0.5777 -0.4380 -0.3584 347  ILE F C   
17873 O  O   . ILE F  237 ? 2.4653 1.7369 2.1760 -0.6185 -0.4532 -0.3613 347  ILE F O   
17874 C  CB  . ILE F  237 ? 2.4208 1.6464 2.2482 -0.4886 -0.4610 -0.2723 347  ILE F CB  
17875 C  CG1 . ILE F  237 ? 2.4288 1.6616 2.3328 -0.4396 -0.4627 -0.2395 347  ILE F CG1 
17876 C  CG2 . ILE F  237 ? 2.6654 1.8660 2.4117 -0.5046 -0.4908 -0.2405 347  ILE F CG2 
17877 C  CD1 . ILE F  237 ? 2.4681 1.6674 2.3599 -0.3883 -0.4669 -0.1998 347  ILE F CD1 
17878 N  N   . ILE F  238 ? 2.6754 1.9401 2.4928 -0.5666 -0.4054 -0.3883 348  ILE F N   
17879 C  CA  . ILE F  238 ? 2.7707 2.0430 2.5462 -0.6055 -0.3855 -0.4307 348  ILE F CA  
17880 C  C   . ILE F  238 ? 2.8933 2.2031 2.6636 -0.6539 -0.3821 -0.4738 348  ILE F C   
17881 O  O   . ILE F  238 ? 2.9821 2.3017 2.6795 -0.6983 -0.3813 -0.4920 348  ILE F O   
17882 C  CB  . ILE F  238 ? 2.5941 1.8688 2.4201 -0.5760 -0.3542 -0.4548 348  ILE F CB  
17883 C  CG1 . ILE F  238 ? 2.6816 1.9286 2.5042 -0.5275 -0.3613 -0.4197 348  ILE F CG1 
17884 C  CG2 . ILE F  238 ? 2.4886 1.7796 2.2847 -0.6164 -0.3315 -0.5026 348  ILE F CG2 
17885 C  CD1 . ILE F  238 ? 2.7184 1.9795 2.5836 -0.4919 -0.3373 -0.4417 348  ILE F CD1 
17886 N  N   . SER F  239 ? 2.9306 2.2633 2.7797 -0.6466 -0.3781 -0.4918 349  SER F N   
17887 C  CA  . SER F  239 ? 2.9757 2.3481 2.8310 -0.6911 -0.3780 -0.5415 349  SER F CA  
17888 C  C   . SER F  239 ? 3.1061 2.5003 2.9167 -0.7116 -0.4199 -0.5226 349  SER F C   
17889 O  O   . SER F  239 ? 3.1793 2.6166 2.9970 -0.7459 -0.4280 -0.5659 349  SER F O   
17890 C  CB  . SER F  239 ? 2.8633 2.2475 2.8369 -0.6768 -0.3526 -0.5744 349  SER F CB  
17891 O  OG  . SER F  239 ? 2.9638 2.3348 3.0073 -0.6354 -0.3612 -0.5307 349  SER F OG  
17892 N  N   . ALA F  240 ? 2.8878 2.2570 2.6552 -0.6889 -0.4476 -0.4617 350  ALA F N   
17893 C  CA  . ALA F  240 ? 2.9923 2.3829 2.7017 -0.7039 -0.4899 -0.4354 350  ALA F CA  
17894 C  C   . ALA F  240 ? 3.0485 2.4206 2.6365 -0.7258 -0.4978 -0.4098 350  ALA F C   
17895 O  O   . ALA F  240 ? 3.3159 2.7107 2.8370 -0.7413 -0.5307 -0.3878 350  ALA F O   
17896 C  CB  . ALA F  240 ? 2.9436 2.3211 2.7002 -0.6597 -0.5156 -0.3804 350  ALA F CB  
17897 N  N   . TYR F  241 ? 2.9289 2.2649 2.4908 -0.7278 -0.4672 -0.4128 351  TYR F N   
17898 C  CA  . TYR F  241 ? 3.0652 2.3797 2.5247 -0.7545 -0.4632 -0.3925 351  TYR F CA  
17899 C  C   . TYR F  241 ? 3.1398 2.4971 2.5456 -0.8058 -0.4449 -0.4423 351  TYR F C   
17900 O  O   . TYR F  241 ? 3.3466 2.6907 2.6722 -0.8333 -0.4291 -0.4320 351  TYR F O   
17901 C  CB  . TYR F  241 ? 3.1524 2.4148 2.6222 -0.7364 -0.4374 -0.3807 351  TYR F CB  
17902 C  CG  . TYR F  241 ? 3.3889 2.6090 2.7739 -0.7540 -0.4350 -0.3418 351  TYR F CG  
17903 C  CD1 . TYR F  241 ? 3.3737 2.5553 2.7240 -0.7330 -0.4640 -0.2779 351  TYR F CD1 
17904 C  CD2 . TYR F  241 ? 3.5811 2.7971 2.9311 -0.7901 -0.4000 -0.3678 351  TYR F CD2 
17905 C  CE1 . TYR F  241 ? 3.4928 2.6258 2.7751 -0.7483 -0.4568 -0.2387 351  TYR F CE1 
17906 C  CE2 . TYR F  241 ? 3.6454 2.8173 2.9293 -0.8089 -0.3914 -0.3299 351  TYR F CE2 
17907 C  CZ  . TYR F  241 ? 3.5995 2.7260 2.8501 -0.7878 -0.4192 -0.2642 351  TYR F CZ  
17908 O  OH  . TYR F  241 ? 3.6714 2.7449 2.8647 -0.8059 -0.4060 -0.2229 351  TYR F OH  
17909 N  N   . GLU F  242 ? 3.1399 2.5482 2.5940 -0.8191 -0.4436 -0.4976 352  GLU F N   
17910 C  CA  . GLU F  242 ? 3.4196 2.8763 2.8268 -0.8658 -0.4262 -0.5550 352  GLU F CA  
17911 C  C   . GLU F  242 ? 3.5509 3.0348 2.8371 -0.8922 -0.4527 -0.5274 352  GLU F C   
17912 O  O   . GLU F  242 ? 3.7364 3.2391 2.9408 -0.9282 -0.4303 -0.5453 352  GLU F O   
17913 C  CB  . GLU F  242 ? 3.4754 2.9776 2.9707 -0.8714 -0.4240 -0.6213 352  GLU F CB  
17914 C  CG  . GLU F  242 ? 3.3404 2.8157 2.9559 -0.8410 -0.3937 -0.6417 352  GLU F CG  
17915 C  CD  . GLU F  242 ? 3.4345 2.9421 3.1522 -0.8428 -0.3912 -0.6953 352  GLU F CD  
17916 O  OE1 . GLU F  242 ? 3.6226 3.1767 3.3246 -0.8668 -0.4198 -0.7188 352  GLU F OE1 
17917 O  OE2 . GLU F  242 ? 3.3264 2.8144 3.1435 -0.8192 -0.3608 -0.7136 352  GLU F OE2 
17918 N  N   . GLU F  243 ? 3.3082 2.7987 2.5814 -0.8719 -0.4991 -0.4809 353  GLU F N   
17919 C  CA  . GLU F  243 ? 3.3739 2.8955 2.5331 -0.8863 -0.5314 -0.4444 353  GLU F CA  
17920 C  C   . GLU F  243 ? 3.5903 3.1926 2.6967 -0.9276 -0.5308 -0.5101 353  GLU F C   
17921 O  O   . GLU F  243 ? 3.5960 3.2528 2.7677 -0.9327 -0.5478 -0.5685 353  GLU F O   
17922 C  CB  . GLU F  243 ? 3.3448 2.8089 2.4120 -0.8892 -0.5142 -0.3796 353  GLU F CB  
17923 C  CG  . GLU F  243 ? 3.2832 2.6677 2.4009 -0.8505 -0.5130 -0.3250 353  GLU F CG  
17924 C  CD  . GLU F  243 ? 3.5711 2.8964 2.6045 -0.8550 -0.5003 -0.2595 353  GLU F CD  
17925 O  OE1 . GLU F  243 ? 3.7473 3.0199 2.8049 -0.8580 -0.4638 -0.2615 353  GLU F OE1 
17926 O  OE2 . GLU F  243 ? 3.7728 3.1068 2.7192 -0.8555 -0.5261 -0.2067 353  GLU F OE2 
17927 N  N   . LEU F  244 ? 3.8979 3.5091 2.8902 -0.9576 -0.5085 -0.5033 354  LEU F N   
17928 C  CA  . LEU F  244 ? 3.9248 3.6169 2.8446 -0.9962 -0.5042 -0.5640 354  LEU F CA  
17929 C  C   . LEU F  244 ? 3.9246 3.6952 2.8135 -0.9923 -0.5637 -0.5711 354  LEU F C   
17930 O  O   . LEU F  244 ? 3.8506 3.7022 2.7137 -1.0196 -0.5698 -0.6436 354  LEU F O   
17931 C  CB  . LEU F  244 ? 3.7500 3.4632 2.7561 -1.0172 -0.4648 -0.6616 354  LEU F CB  
17932 C  CG  . LEU F  244 ? 3.5379 3.1989 2.5693 -1.0254 -0.4054 -0.6705 354  LEU F CG  
17933 C  CD1 . LEU F  244 ? 3.3462 3.0354 2.4675 -1.0402 -0.3711 -0.7667 354  LEU F CD1 
17934 C  CD2 . LEU F  244 ? 3.6428 3.3023 2.5450 -1.0532 -0.3770 -0.6376 354  LEU F CD2 
17935 N  N   . GLU G  12  ? 4.2163 3.9212 2.5763 -1.0818 -0.9282 0.8914  10   GLU G N   
17936 C  CA  . GLU G  12  ? 4.2460 3.8710 2.5502 -1.0500 -0.8987 0.8208  10   GLU G CA  
17937 C  C   . GLU G  12  ? 4.2778 3.6311 2.3708 -1.0174 -0.8499 0.6837  10   GLU G C   
17938 O  O   . GLU G  12  ? 4.3066 3.5781 2.3695 -0.9516 -0.8083 0.6079  10   GLU G O   
17939 C  CB  . GLU G  12  ? 4.3607 4.0521 2.5870 -1.1960 -0.9524 0.8882  10   GLU G CB  
17940 C  CG  . GLU G  12  ? 4.1171 4.0890 2.5717 -1.2069 -0.9904 1.0253  10   GLU G CG  
17941 C  CD  . GLU G  12  ? 3.9253 3.9762 2.5510 -1.0798 -0.9487 1.0081  10   GLU G CD  
17942 O  OE1 . GLU G  12  ? 3.9144 3.8110 2.4542 -1.0165 -0.9034 0.8954  10   GLU G OE1 
17943 O  OE2 . GLU G  12  ? 3.8540 4.1202 2.6978 -1.0430 -0.9582 1.1106  10   GLU G OE2 
17944 N  N   . LEU G  13  ? 4.1720 3.3871 2.1189 -1.0623 -0.8524 0.6567  11   LEU G N   
17945 C  CA  . LEU G  13  ? 4.1697 3.1196 1.9111 -1.0292 -0.8004 0.5360  11   LEU G CA  
17946 C  C   . LEU G  13  ? 4.1104 3.0299 1.9696 -0.8486 -0.7357 0.4607  11   LEU G C   
17947 O  O   . LEU G  13  ? 4.2064 2.9434 1.9397 -0.7916 -0.6827 0.3638  11   LEU G O   
17948 C  CB  . LEU G  13  ? 4.2871 3.0967 1.8413 -1.1274 -0.8191 0.5344  11   LEU G CB  
17949 C  CG  . LEU G  13  ? 4.4641 3.2896 1.8707 -1.3267 -0.8865 0.6095  11   LEU G CG  
17950 C  CD1 . LEU G  13  ? 4.6555 3.3226 1.8672 -1.4174 -0.8981 0.5984  11   LEU G CD1 
17951 C  CD2 . LEU G  13  ? 4.6217 3.3388 1.8552 -1.4051 -0.8816 0.5732  11   LEU G CD2 
17952 N  N   . VAL G  14  ? 4.0360 3.1307 2.1293 -0.7603 -0.7363 0.5070  12   VAL G N   
17953 C  CA  . VAL G  14  ? 3.9966 3.0735 2.2009 -0.6003 -0.6786 0.4410  12   VAL G CA  
17954 C  C   . VAL G  14  ? 4.0655 3.1498 2.3164 -0.5243 -0.6422 0.3923  12   VAL G C   
17955 O  O   . VAL G  14  ? 4.0428 3.0184 2.2609 -0.4265 -0.5891 0.3065  12   VAL G O   
17956 C  CB  . VAL G  14  ? 3.8037 3.0614 2.2350 -0.5373 -0.6860 0.5065  12   VAL G CB  
17957 C  CG1 . VAL G  14  ? 3.7511 2.9928 2.2888 -0.3834 -0.6276 0.4393  12   VAL G CG1 
17958 C  CG2 . VAL G  14  ? 3.8320 3.0825 2.2150 -0.6105 -0.7206 0.5535  12   VAL G CG2 
17959 N  N   . LYS G  15  ? 4.1389 3.3579 2.4680 -0.5695 -0.6708 0.4511  13   LYS G N   
17960 C  CA  . LYS G  15  ? 4.0186 3.2670 2.4115 -0.4993 -0.6398 0.4144  13   LYS G CA  
17961 C  C   . LYS G  15  ? 4.1754 3.2433 2.3604 -0.5307 -0.6170 0.3359  13   LYS G C   
17962 O  O   . LYS G  15  ? 4.1172 3.1566 2.3243 -0.4447 -0.5740 0.2755  13   LYS G O   
17963 C  CB  . LYS G  15  ? 3.8997 3.3507 2.4447 -0.5375 -0.6762 0.5093  13   LYS G CB  
17964 C  CG  . LYS G  15  ? 3.7544 3.3849 2.5065 -0.5040 -0.6905 0.5974  13   LYS G CG  
17965 C  CD  . LYS G  15  ? 3.5017 3.3296 2.4010 -0.5392 -0.7209 0.7016  13   LYS G CD  
17966 C  CE  . LYS G  15  ? 3.2752 3.2700 2.3846 -0.4866 -0.7191 0.7876  13   LYS G CE  
17967 N  NZ  . LYS G  15  ? 3.1128 3.3014 2.3782 -0.5048 -0.7384 0.8962  13   LYS G NZ  
17968 N  N   . ARG G  16  ? 4.3865 3.3267 2.3625 -0.6540 -0.6414 0.3362  14   ARG G N   
17969 C  CA  . ARG G  16  ? 4.5069 3.2686 2.2713 -0.6964 -0.6162 0.2690  14   ARG G CA  
17970 C  C   . ARG G  16  ? 4.5336 3.0958 2.1838 -0.5999 -0.5465 0.1660  14   ARG G C   
17971 O  O   . ARG G  16  ? 4.5722 3.0119 2.1027 -0.5833 -0.5058 0.1039  14   ARG G O   
17972 C  CB  . ARG G  16  ? 4.6605 3.3364 2.2193 -0.8706 -0.6612 0.3037  14   ARG G CB  
17973 C  CG  . ARG G  16  ? 4.5869 3.4533 2.2256 -0.9826 -0.7295 0.4075  14   ARG G CG  
17974 C  CD  . ARG G  16  ? 4.3889 3.3143 2.0768 -0.9596 -0.7188 0.3969  14   ARG G CD  
17975 N  NE  . ARG G  16  ? 4.4419 3.1484 1.9049 -0.9771 -0.6752 0.3056  14   ARG G NE  
17976 C  CZ  . ARG G  16  ? 4.4032 3.1142 1.8615 -0.9603 -0.6566 0.2783  14   ARG G CZ  
17977 N  NH1 . ARG G  16  ? 4.1959 3.1159 1.8596 -0.9279 -0.6801 0.3344  14   ARG G NH1 
17978 N  NH2 . ARG G  16  ? 4.6422 3.1438 1.8875 -0.9738 -0.6103 0.1964  14   ARG G NH2 
17979 N  N   . LYS G  17  ? 4.6188 3.1494 2.3045 -0.5346 -0.5295 0.1510  15   LYS G N   
17980 C  CA  . LYS G  17  ? 4.7123 3.0682 2.3025 -0.4373 -0.4626 0.0643  15   LYS G CA  
17981 C  C   . LYS G  17  ? 4.6271 3.0561 2.3638 -0.2946 -0.4174 0.0236  15   LYS G C   
17982 O  O   . LYS G  17  ? 4.7223 3.0191 2.3600 -0.2316 -0.3605 -0.0442 15   LYS G O   
17983 C  CB  . LYS G  17  ? 4.7187 3.0278 2.3049 -0.4163 -0.4621 0.0668  15   LYS G CB  
17984 C  CG  . LYS G  17  ? 4.7062 2.8575 2.2196 -0.3054 -0.3933 -0.0107 15   LYS G CG  
17985 C  CD  . LYS G  17  ? 4.7397 2.8086 2.1975 -0.3132 -0.3959 -0.0073 15   LYS G CD  
17986 C  CE  . LYS G  17  ? 4.9505 2.8500 2.1685 -0.4564 -0.4160 0.0001  15   LYS G CE  
17987 N  NZ  . LYS G  17  ? 4.9654 2.7654 2.1119 -0.4643 -0.4142 -0.0012 15   LYS G NZ  
17988 N  N   . ARG G  18  ? 4.4774 3.1123 2.4427 -0.2445 -0.4383 0.0669  16   ARG G N   
17989 C  CA  . ARG G  18  ? 4.3843 3.0938 2.4842 -0.1215 -0.3986 0.0316  16   ARG G CA  
17990 C  C   . ARG G  18  ? 4.3297 3.0255 2.3820 -0.1289 -0.3827 0.0056  16   ARG G C   
17991 O  O   . ARG G  18  ? 4.2783 2.9526 2.3474 -0.0357 -0.3351 -0.0471 16   ARG G O   
17992 C  CB  . ARG G  18  ? 4.2589 3.1738 2.5942 -0.0802 -0.4212 0.0864  16   ARG G CB  
17993 C  CG  . ARG G  18  ? 4.1426 3.1363 2.6122 0.0347  -0.3823 0.0528  16   ARG G CG  
17994 C  CD  . ARG G  18  ? 4.0023 3.1779 2.6827 0.0634  -0.3986 0.1087  16   ARG G CD  
17995 N  NE  . ARG G  18  ? 3.8479 3.0756 2.6369 0.1703  -0.3578 0.0709  16   ARG G NE  
17996 C  CZ  . ARG G  18  ? 3.8485 3.1279 2.6841 0.2004  -0.3411 0.0540  16   ARG G CZ  
17997 N  NH1 . ARG G  18  ? 4.1714 3.4570 2.9590 0.1367  -0.3608 0.0705  16   ARG G NH1 
17998 N  NH2 . ARG G  18  ? 3.6126 2.9387 2.5372 0.2880  -0.3061 0.0220  16   ARG G NH2 
17999 N  N   . ILE G  19  ? 4.3809 3.0982 2.3762 -0.2409 -0.4231 0.0460  17   ILE G N   
18000 C  CA  . ILE G  19  ? 4.4831 3.1975 2.4382 -0.2549 -0.4118 0.0260  17   ILE G CA  
18001 C  C   . ILE G  19  ? 4.6370 3.1459 2.3964 -0.2277 -0.3531 -0.0542 17   ILE G C   
18002 O  O   . ILE G  19  ? 4.6582 3.1664 2.4334 -0.1586 -0.3133 -0.0956 17   ILE G O   
18003 C  CB  . ILE G  19  ? 4.7055 3.4780 2.6217 -0.3936 -0.4701 0.0911  17   ILE G CB  
18004 C  CG1 . ILE G  19  ? 4.5417 3.5332 2.6725 -0.4035 -0.5191 0.1808  17   ILE G CG1 
18005 C  CG2 . ILE G  19  ? 4.7697 3.5274 2.6284 -0.4145 -0.4581 0.0678  17   ILE G CG2 
18006 C  CD1 . ILE G  19  ? 4.5291 3.6132 2.6497 -0.5353 -0.5794 0.2621  17   ILE G CD1 
18007 N  N   . GLU G  20  ? 4.6932 3.0217 2.2627 -0.2799 -0.3425 -0.0747 18   GLU G N   
18008 C  CA  . GLU G  20  ? 4.7330 2.8457 2.1051 -0.2485 -0.2755 -0.1469 18   GLU G CA  
18009 C  C   . GLU G  20  ? 4.8038 2.9058 2.2515 -0.0951 -0.2156 -0.1926 18   GLU G C   
18010 O  O   . GLU G  20  ? 4.8848 2.8579 2.2228 -0.0376 -0.1516 -0.2458 18   GLU G O   
18011 C  CB  . GLU G  20  ? 4.6948 2.6035 1.8353 -0.3465 -0.2749 -0.1546 18   GLU G CB  
18012 C  CG  . GLU G  20  ? 4.7441 2.6133 1.7411 -0.5092 -0.3190 -0.1240 18   GLU G CG  
18013 C  CD  . GLU G  20  ? 4.7815 2.5891 1.6839 -0.5193 -0.2860 -0.1603 18   GLU G CD  
18014 O  OE1 . GLU G  20  ? 4.8165 2.5060 1.6561 -0.4205 -0.2112 -0.2237 18   GLU G OE1 
18015 O  OE2 . GLU G  20  ? 4.8089 2.6936 1.7037 -0.6248 -0.3339 -0.1208 18   GLU G OE2 
18016 N  N   . ALA G  21  ? 4.7614 2.9983 2.3915 -0.0294 -0.2329 -0.1688 19   ALA G N   
18017 C  CA  . ALA G  21  ? 4.6327 2.9005 2.3599 0.1097  -0.1843 -0.2029 19   ALA G CA  
18018 C  C   . ALA G  21  ? 4.4170 2.8374 2.2935 0.1705  -0.1776 -0.2057 19   ALA G C   
18019 O  O   . ALA G  21  ? 4.3132 2.7287 2.2119 0.2703  -0.1270 -0.2425 19   ALA G O   
18020 C  CB  . ALA G  21  ? 4.5652 2.9083 2.4146 0.1486  -0.2035 -0.1788 19   ALA G CB  
18021 N  N   . ILE G  22  ? 4.2206 2.7804 2.1996 0.1110  -0.2269 -0.1625 20   ILE G N   
18022 C  CA  . ILE G  22  ? 4.0861 2.7738 2.1848 0.1549  -0.2204 -0.1654 20   ILE G CA  
18023 C  C   . ILE G  22  ? 4.1945 2.7785 2.1534 0.1482  -0.1833 -0.2065 20   ILE G C   
18024 O  O   . ILE G  22  ? 4.1551 2.7839 2.1657 0.2254  -0.1473 -0.2346 20   ILE G O   
18025 C  CB  . ILE G  22  ? 4.0148 2.8640 2.2480 0.0915  -0.2779 -0.1026 20   ILE G CB  
18026 C  CG1 . ILE G  22  ? 3.9273 2.8899 2.3201 0.1219  -0.3000 -0.0634 20   ILE G CG1 
18027 C  CG2 . ILE G  22  ? 3.9444 2.8982 2.2669 0.1204  -0.2702 -0.1069 20   ILE G CG2 
18028 C  CD1 . ILE G  22  ? 3.8309 2.8735 2.3573 0.2349  -0.2660 -0.0886 20   ILE G CD1 
18029 N  N   . ARG G  23  ? 4.4816 2.9242 2.2549 0.0512  -0.1901 -0.2094 21   ARG G N   
18030 C  CA  . ARG G  23  ? 4.5932 2.9120 2.2087 0.0373  -0.1485 -0.2503 21   ARG G CA  
18031 C  C   . ARG G  23  ? 4.7055 2.9119 2.2553 0.1505  -0.0698 -0.3046 21   ARG G C   
18032 O  O   . ARG G  23  ? 4.6983 2.9118 2.2468 0.2076  -0.0276 -0.3325 21   ARG G O   
18033 C  CB  . ARG G  23  ? 4.6071 2.7697 2.0110 -0.0961 -0.1665 -0.2448 21   ARG G CB  
18034 C  CG  . ARG G  23  ? 4.7035 2.6831 1.8993 -0.1098 -0.1083 -0.2956 21   ARG G CG  
18035 C  CD  . ARG G  23  ? 4.9025 2.7032 1.8632 -0.2513 -0.1221 -0.2936 21   ARG G CD  
18036 N  NE  . ARG G  23  ? 4.7625 2.6823 1.7610 -0.3803 -0.2010 -0.2364 21   ARG G NE  
18037 C  CZ  . ARG G  23  ? 4.7914 2.7251 1.7365 -0.4486 -0.2119 -0.2331 21   ARG G CZ  
18038 N  NH1 . ARG G  23  ? 4.8645 2.6953 1.7129 -0.3998 -0.1471 -0.2878 21   ARG G NH1 
18039 N  NH2 . ARG G  23  ? 4.8046 2.8618 1.7962 -0.5648 -0.2867 -0.1700 21   ARG G NH2 
18040 N  N   . GLY G  24  ? 4.8465 2.9538 2.3437 0.1853  -0.0479 -0.3149 22   GLY G N   
18041 C  CA  . GLY G  24  ? 4.9106 2.9274 2.3636 0.3012  0.0275  -0.3539 22   GLY G CA  
18042 C  C   . GLY G  24  ? 4.5962 2.7911 2.2544 0.4173  0.0370  -0.3497 22   GLY G C   
18043 O  O   . GLY G  24  ? 4.5002 2.6627 2.1450 0.5172  0.0994  -0.3740 22   GLY G O   
18044 N  N   . GLN G  25  ? 4.5161 2.8972 2.3589 0.4044  -0.0203 -0.3154 23   GLN G N   
18045 C  CA  . GLN G  25  ? 4.4534 3.0011 2.4796 0.4984  -0.0133 -0.3119 23   GLN G CA  
18046 C  C   . GLN G  25  ? 4.3965 3.0363 2.4752 0.5181  -0.0014 -0.3210 23   GLN G C   
18047 O  O   . GLN G  25  ? 4.3436 3.0199 2.4558 0.6067  0.0436  -0.3394 23   GLN G O   
18048 C  CB  . GLN G  25  ? 4.4084 3.0983 2.5964 0.4768  -0.0693 -0.2735 23   GLN G CB  
18049 C  CG  . GLN G  25  ? 4.2451 3.0925 2.6071 0.5615  -0.0617 -0.2708 23   GLN G CG  
18050 C  CD  . GLN G  25  ? 4.0610 3.0387 2.5736 0.5333  -0.1097 -0.2328 23   GLN G CD  
18051 O  OE1 . GLN G  25  ? 4.0336 3.0298 2.5549 0.4534  -0.1516 -0.2008 23   GLN G OE1 
18052 N  NE2 . GLN G  25  ? 3.9551 3.0245 2.5843 0.5982  -0.1007 -0.2320 23   GLN G NE2 
18053 N  N   . ILE G  26  ? 4.2829 2.9685 2.3710 0.4341  -0.0423 -0.3033 24   ILE G N   
18054 C  CA  . ILE G  26  ? 4.1143 2.8955 2.2596 0.4446  -0.0373 -0.3085 24   ILE G CA  
18055 C  C   . ILE G  26  ? 4.2287 2.9033 2.2467 0.4911  0.0274  -0.3479 24   ILE G C   
18056 O  O   . ILE G  26  ? 4.1111 2.8708 2.1979 0.5626  0.0577  -0.3594 24   ILE G O   
18057 C  CB  . ILE G  26  ? 4.1500 2.9745 2.3009 0.3380  -0.0907 -0.2782 24   ILE G CB  
18058 C  CG1 . ILE G  26  ? 4.0606 3.0049 2.3547 0.3055  -0.1461 -0.2298 24   ILE G CG1 
18059 C  CG2 . ILE G  26  ? 4.1567 3.0672 2.3535 0.3461  -0.0835 -0.2853 24   ILE G CG2 
18060 C  CD1 . ILE G  26  ? 4.0910 3.0954 2.4063 0.2056  -0.1984 -0.1854 24   ILE G CD1 
18061 N  N   . LEU G  27  ? 4.4435 2.9268 2.2677 0.4488  0.0527  -0.3667 25   LEU G N   
18062 C  CA  . LEU G  27  ? 4.5811 2.9381 2.2677 0.4973  0.1263  -0.4027 25   LEU G CA  
18063 C  C   . LEU G  27  ? 4.3846 2.7510 2.1144 0.6259  0.1846  -0.4129 25   LEU G C   
18064 O  O   . LEU G  27  ? 4.3253 2.7007 2.0452 0.6986  0.2402  -0.4273 25   LEU G O   
18065 C  CB  . LEU G  27  ? 4.9457 3.0704 2.3976 0.4204  0.1473  -0.4212 25   LEU G CB  
18066 C  CG  . LEU G  27  ? 5.0067 3.1083 2.3831 0.2805  0.0934  -0.4079 25   LEU G CG  
18067 C  CD1 . LEU G  27  ? 5.2971 3.1526 2.4195 0.1994  0.1191  -0.4285 25   LEU G CD1 
18068 C  CD2 . LEU G  27  ? 4.9199 3.1079 2.3317 0.2716  0.0941  -0.4125 25   LEU G CD2 
18069 N  N   . SER G  28  ? 4.3735 2.7486 2.1560 0.6556  0.1727  -0.4002 26   SER G N   
18070 C  CA  . SER G  28  ? 4.4749 2.8808 2.3120 0.7748  0.2225  -0.4011 26   SER G CA  
18071 C  C   . SER G  28  ? 4.4037 3.0361 2.4387 0.8298  0.2052  -0.3851 26   SER G C   
18072 O  O   . SER G  28  ? 4.4057 3.0914 2.4786 0.9240  0.2537  -0.3843 26   SER G O   
18073 C  CB  . SER G  28  ? 4.4827 2.8259 2.3094 0.7847  0.2141  -0.3919 26   SER G CB  
18074 O  OG  . SER G  28  ? 4.2524 2.7200 2.2114 0.7344  0.1418  -0.3679 26   SER G OG  
18075 N  N   . LYS G  29  ? 4.2995 3.0660 2.4577 0.7710  0.1398  -0.3682 27   LYS G N   
18076 C  CA  . LYS G  29  ? 4.0940 3.0579 2.4209 0.8103  0.1256  -0.3560 27   LYS G CA  
18077 C  C   . LYS G  29  ? 4.1562 3.1646 2.4731 0.8306  0.1550  -0.3674 27   LYS G C   
18078 O  O   . LYS G  29  ? 4.0600 3.1959 2.4701 0.8952  0.1742  -0.3618 27   LYS G O   
18079 C  CB  . LYS G  29  ? 3.9266 2.9970 2.3704 0.7422  0.0586  -0.3340 27   LYS G CB  
18080 C  CG  . LYS G  29  ? 4.0351 3.0908 2.5146 0.7308  0.0310  -0.3178 27   LYS G CG  
18081 C  CD  . LYS G  29  ? 3.9594 3.1118 2.5488 0.6664  -0.0264 -0.2898 27   LYS G CD  
18082 C  CE  . LYS G  29  ? 3.7614 3.0771 2.5043 0.7029  -0.0312 -0.2816 27   LYS G CE  
18083 N  NZ  . LYS G  29  ? 3.7211 3.0723 2.5184 0.7663  -0.0154 -0.2823 27   LYS G NZ  
18084 N  N   . LEU G  30  ? 4.2315 3.1396 2.4320 0.7717  0.1587  -0.3814 28   LEU G N   
18085 C  CA  . LEU G  30  ? 4.1190 3.0438 2.2854 0.7910  0.1941  -0.3949 28   LEU G CA  
18086 C  C   . LEU G  30  ? 4.0801 2.8864 2.1279 0.8708  0.2760  -0.4108 28   LEU G C   
18087 O  O   . LEU G  30  ? 3.9951 2.8011 2.0013 0.8956  0.3168  -0.4211 28   LEU G O   
18088 C  CB  . LEU G  30  ? 4.1127 2.9790 2.1987 0.6894  0.1647  -0.4012 28   LEU G CB  
18089 C  CG  . LEU G  30  ? 3.9933 2.9764 2.1934 0.6106  0.0895  -0.3760 28   LEU G CG  
18090 C  CD1 . LEU G  30  ? 4.1981 3.1107 2.2990 0.5086  0.0638  -0.3754 28   LEU G CD1 
18091 C  CD2 . LEU G  30  ? 3.8465 3.0190 2.2087 0.6476  0.0781  -0.3654 28   LEU G CD2 
18092 N  N   . ARG G  31  ? 4.1606 2.8662 2.1544 0.9144  0.3045  -0.4100 29   ARG G N   
18093 C  CA  . ARG G  31  ? 4.2847 2.8477 2.1498 0.9922  0.3905  -0.4203 29   ARG G CA  
18094 C  C   . ARG G  31  ? 4.5603 2.9432 2.2371 0.9414  0.4273  -0.4481 29   ARG G C   
18095 O  O   . ARG G  31  ? 4.7699 3.0917 2.3692 1.0037  0.5020  -0.4567 29   ARG G O   
18096 C  CB  . ARG G  31  ? 4.2178 2.9236 2.1856 1.1051  0.4371  -0.4011 29   ARG G CB  
18097 C  CG  . ARG G  31  ? 4.4626 3.0625 2.3520 1.2089  0.5230  -0.3918 29   ARG G CG  
18098 C  CD  . ARG G  31  ? 4.4791 3.2624 2.5044 1.2967  0.5567  -0.3522 29   ARG G CD  
18099 N  NE  . ARG G  31  ? 4.3302 3.3240 2.5214 1.3253  0.5107  -0.3330 29   ARG G NE  
18100 C  CZ  . ARG G  31  ? 4.2517 3.3202 2.5303 1.3804  0.5149  -0.2964 29   ARG G CZ  
18101 N  NH1 . ARG G  31  ? 4.2600 3.2129 2.4800 1.4195  0.5635  -0.2729 29   ARG G NH1 
18102 N  NH2 . ARG G  31  ? 4.1291 3.3862 2.5479 1.3927  0.4715  -0.2822 29   ARG G NH2 
18103 N  N   . LEU G  32  ? 4.6164 2.9169 2.2170 0.8241  0.3756  -0.4583 30   LEU G N   
18104 C  CA  . LEU G  32  ? 4.7849 2.9295 2.2076 0.7474  0.3944  -0.4828 30   LEU G CA  
18105 C  C   . LEU G  32  ? 4.9202 2.8421 2.1567 0.6719  0.3962  -0.4964 30   LEU G C   
18106 O  O   . LEU G  32  ? 4.8228 2.7601 2.1032 0.6348  0.3446  -0.4810 30   LEU G O   
18107 C  CB  . LEU G  32  ? 4.5613 2.8331 2.0597 0.6557  0.3242  -0.4753 30   LEU G CB  
18108 C  CG  . LEU G  32  ? 4.4408 2.8941 2.0727 0.7087  0.3301  -0.4692 30   LEU G CG  
18109 C  CD1 . LEU G  32  ? 4.4014 2.9545 2.0897 0.6108  0.2622  -0.4603 30   LEU G CD1 
18110 C  CD2 . LEU G  32  ? 4.7510 3.1097 2.2695 0.7783  0.4215  -0.4896 30   LEU G CD2 
18111 N  N   . ALA G  33  ? 5.2037 2.9130 2.2236 0.6459  0.4585  -0.5250 31   ALA G N   
18112 C  CA  . ALA G  33  ? 5.3342 2.8132 2.1432 0.5503  0.4606  -0.5413 31   ALA G CA  
18113 C  C   . ALA G  33  ? 5.3833 2.8519 2.1236 0.3974  0.3947  -0.5411 31   ALA G C   
18114 O  O   . ALA G  33  ? 5.4389 2.8158 2.0850 0.2912  0.3509  -0.5350 31   ALA G O   
18115 C  CB  . ALA G  33  ? 5.4840 2.7847 2.1760 0.5819  0.5545  -0.5445 31   ALA G CB  
18116 N  N   . SER G  34  ? 5.3496 2.9210 2.1394 0.3816  0.3845  -0.5423 32   SER G N   
18117 C  CA  . SER G  34  ? 5.3872 2.9603 2.1148 0.2404  0.3258  -0.5370 32   SER G CA  
18118 C  C   . SER G  34  ? 5.2110 3.0240 2.1354 0.2517  0.2794  -0.5167 32   SER G C   
18119 O  O   . SER G  34  ? 5.0775 2.9909 2.1082 0.3616  0.3195  -0.5222 32   SER G O   
18120 C  CB  . SER G  34  ? 5.5597 2.8911 2.0205 0.1804  0.3908  -0.5737 32   SER G CB  
18121 O  OG  . SER G  34  ? 5.4418 2.7837 1.9405 0.2847  0.4718  -0.5847 32   SER G OG  
18122 N  N   . PRO G  35  ? 5.1342 3.0460 2.1104 0.1389  0.1961  -0.4883 33   PRO G N   
18123 C  CA  . PRO G  35  ? 4.9086 3.0329 2.0573 0.1391  0.1528  -0.4669 33   PRO G CA  
18124 C  C   . PRO G  35  ? 5.0794 3.1579 2.1374 0.1468  0.2038  -0.4956 33   PRO G C   
18125 O  O   . PRO G  35  ? 5.4212 3.2914 2.2573 0.1108  0.2587  -0.5276 33   PRO G O   
18126 C  CB  . PRO G  35  ? 4.7915 2.9810 1.9654 0.0032  0.0616  -0.4247 33   PRO G CB  
18127 C  CG  . PRO G  35  ? 4.8281 2.9223 1.9416 -0.0299 0.0448  -0.4142 33   PRO G CG  
18128 C  CD  . PRO G  35  ? 5.1842 3.0429 2.0915 0.0124  0.1323  -0.4633 33   PRO G CD  
18129 N  N   . PRO G  36  ? 4.8475 3.1084 2.0623 0.1883  0.1899  -0.4854 34   PRO G N   
18130 C  CA  . PRO G  36  ? 4.9845 3.2171 2.1225 0.1940  0.2356  -0.5098 34   PRO G CA  
18131 C  C   . PRO G  36  ? 5.1733 3.3337 2.1761 0.0503  0.1996  -0.5070 34   PRO G C   
18132 O  O   . PRO G  36  ? 5.2051 3.3724 2.1994 -0.0554 0.1310  -0.4774 34   PRO G O   
18133 C  CB  . PRO G  36  ? 4.6672 3.1363 2.0280 0.2616  0.2134  -0.4914 34   PRO G CB  
18134 C  CG  . PRO G  36  ? 4.5069 3.1208 2.0367 0.2328  0.1329  -0.4513 34   PRO G CG  
18135 C  CD  . PRO G  36  ? 4.5953 3.0888 2.0566 0.2301  0.1355  -0.4516 34   PRO G CD  
18136 N  N   . SER G  37  ? 5.2536 3.3534 2.1519 0.0459  0.2474  -0.5337 35   SER G N   
18137 C  CA  . SER G  37  ? 5.3284 3.3248 2.0560 -0.0912 0.2288  -0.5383 35   SER G CA  
18138 C  C   . SER G  37  ? 5.2577 3.4440 2.1143 -0.1499 0.1612  -0.5066 35   SER G C   
18139 O  O   . SER G  37  ? 5.4138 3.5772 2.1867 -0.2829 0.1116  -0.4877 35   SER G O   
18140 C  CB  . SER G  37  ? 5.5136 3.2944 2.0137 -0.0724 0.3297  -0.5889 35   SER G CB  
18141 O  OG  . SER G  37  ? 5.7016 3.2977 2.0890 -0.0383 0.3897  -0.6070 35   SER G OG  
18142 N  N   . GLU G  40  ? 4.0775 3.2222 1.7452 -0.2599 -0.1172 -0.3185 38   GLU G N   
18143 C  CA  . GLU G  40  ? 4.0136 3.1978 1.6485 -0.3737 -0.1644 -0.2841 38   GLU G CA  
18144 C  C   . GLU G  40  ? 3.9183 3.2788 1.7266 -0.3304 -0.1783 -0.2657 38   GLU G C   
18145 O  O   . GLU G  40  ? 3.8253 3.2276 1.7051 -0.2255 -0.1351 -0.2981 38   GLU G O   
18146 C  CB  . GLU G  40  ? 4.0229 3.0305 1.4141 -0.4415 -0.1243 -0.3266 38   GLU G CB  
18147 C  CG  . GLU G  40  ? 4.0741 3.1164 1.4103 -0.5313 -0.1445 -0.3152 38   GLU G CG  
18148 C  CD  . GLU G  40  ? 4.0507 3.1222 1.3980 -0.4530 -0.0865 -0.3593 38   GLU G CD  
18149 O  OE1 . GLU G  40  ? 3.9323 3.0653 1.3925 -0.3265 -0.0467 -0.3820 38   GLU G OE1 
18150 O  OE2 . GLU G  40  ? 4.1510 3.1949 1.3957 -0.5263 -0.0851 -0.3656 38   GLU G OE2 
18151 N  N   . VAL G  41  ? 4.0247 3.4902 1.8995 -0.4121 -0.2380 -0.2093 39   VAL G N   
18152 C  CA  . VAL G  41  ? 3.8339 3.4723 1.8871 -0.3874 -0.2630 -0.1746 39   VAL G CA  
18153 C  C   . VAL G  41  ? 3.7668 3.5122 2.0137 -0.3028 -0.2713 -0.1507 39   VAL G C   
18154 O  O   . VAL G  41  ? 3.6833 3.3799 1.9334 -0.2337 -0.2424 -0.1798 39   VAL G O   
18155 C  CB  . VAL G  41  ? 3.6890 3.3347 1.7061 -0.3502 -0.2184 -0.2217 39   VAL G CB  
18156 C  CG1 . VAL G  41  ? 3.5608 3.3732 1.7471 -0.3275 -0.2401 -0.1906 39   VAL G CG1 
18157 C  CG2 . VAL G  41  ? 3.7769 3.3105 1.5968 -0.4431 -0.2100 -0.2412 39   VAL G CG2 
18158 N  N   . PRO G  42  ? 3.9834 3.8641 2.3821 -0.3185 -0.3124 -0.0902 40   PRO G N   
18159 C  CA  . PRO G  42  ? 3.9890 3.9437 2.4080 -0.4063 -0.3571 -0.0338 40   PRO G CA  
18160 C  C   . PRO G  42  ? 4.1233 4.1074 2.5572 -0.4972 -0.4157 0.0454  40   PRO G C   
18161 O  O   . PRO G  42  ? 4.1464 4.1429 2.6488 -0.4746 -0.4273 0.0735  40   PRO G O   
18162 C  CB  . PRO G  42  ? 3.7186 3.8027 2.3077 -0.3475 -0.3542 -0.0139 40   PRO G CB  
18163 C  CG  . PRO G  42  ? 3.6425 3.7312 2.3175 -0.2482 -0.3242 -0.0392 40   PRO G CG  
18164 C  CD  . PRO G  42  ? 3.7917 3.7634 2.3604 -0.2369 -0.3076 -0.0752 40   PRO G CD  
18165 N  N   . PRO G  43  ? 4.2205 4.2267 2.5955 -0.6010 -0.4532 0.0865  41   PRO G N   
18166 C  CA  . PRO G  43  ? 4.1299 4.1939 2.5330 -0.6933 -0.5137 0.1771  41   PRO G CA  
18167 C  C   . PRO G  43  ? 3.8774 4.0887 2.4942 -0.6514 -0.5358 0.2559  41   PRO G C   
18168 O  O   . PRO G  43  ? 3.8261 4.0947 2.4979 -0.6979 -0.5767 0.3351  41   PRO G O   
18169 C  CB  . PRO G  43  ? 4.1783 4.2494 2.4790 -0.8077 -0.5445 0.2020  41   PRO G CB  
18170 C  CG  . PRO G  43  ? 4.1817 4.2609 2.4888 -0.7551 -0.5069 0.1484  41   PRO G CG  
18171 C  CD  . PRO G  43  ? 4.2502 4.2461 2.5412 -0.6408 -0.4442 0.0605  41   PRO G CD  
18172 N  N   . GLY G  44  ? 5.3538 5.7514 1.8623 0.1381  -0.5825 0.2754  42   GLY G N   
18173 C  CA  . GLY G  44  ? 4.8844 5.3058 1.5388 0.1654  -0.6227 0.3592  42   GLY G CA  
18174 C  C   . GLY G  44  ? 4.6679 5.0823 1.4716 0.1780  -0.5712 0.3351  42   GLY G C   
18175 O  O   . GLY G  44  ? 4.5429 4.9475 1.3565 0.1645  -0.5319 0.2371  42   GLY G O   
18176 N  N   . PRO G  45  ? 4.8525 5.2616 1.7771 0.2050  -0.5707 0.4228  43   PRO G N   
18177 C  CA  . PRO G  45  ? 4.5656 4.9276 1.6837 0.2039  -0.5210 0.3949  43   PRO G CA  
18178 C  C   . PRO G  45  ? 4.6071 4.9176 1.7019 0.1970  -0.4091 0.3796  43   PRO G C   
18179 O  O   . PRO G  45  ? 4.6162 4.9149 1.6167 0.2037  -0.3609 0.4488  43   PRO G O   
18180 C  CB  . PRO G  45  ? 4.4240 4.7765 1.6705 0.2299  -0.5515 0.4966  43   PRO G CB  
18181 C  CG  . PRO G  45  ? 4.7907 5.1622 1.8945 0.2453  -0.5805 0.5954  43   PRO G CG  
18182 C  CD  . PRO G  45  ? 4.9947 5.4082 1.9310 0.2263  -0.6209 0.5400  43   PRO G CD  
18183 N  N   . LEU G  46  ? 4.6301 4.9129 1.8179 0.1835  -0.3680 0.2916  44   LEU G N   
18184 C  CA  . LEU G  46  ? 4.7386 4.9791 1.9216 0.1793  -0.2653 0.2659  44   LEU G CA  
18185 C  C   . LEU G  46  ? 4.8107 5.0192 2.0927 0.1923  -0.2151 0.3569  44   LEU G C   
18186 O  O   . LEU G  46  ? 4.7578 4.9648 2.1369 0.2040  -0.2596 0.4227  44   LEU G O   
18187 C  CB  . LEU G  46  ? 4.4133 4.6293 1.6895 0.1649  -0.2451 0.1581  44   LEU G CB  
18188 C  CG  . LEU G  46  ? 4.0345 4.2456 1.5002 0.1630  -0.2875 0.1445  44   LEU G CG  
18189 C  CD1 . LEU G  46  ? 3.9040 4.0734 1.5123 0.1718  -0.2253 0.1796  44   LEU G CD1 
18190 C  CD2 . LEU G  46  ? 4.0228 4.2326 1.5123 0.1413  -0.3089 0.0338  44   LEU G CD2 
18191 N  N   . PRO G  47  ? 4.7045 4.8882 1.9668 0.1904  -0.1224 0.3602  45   PRO G N   
18192 C  CA  . PRO G  47  ? 4.4418 4.6007 1.7772 0.1971  -0.0751 0.4520  45   PRO G CA  
18193 C  C   . PRO G  47  ? 3.9127 4.0431 1.4469 0.2012  -0.0947 0.4639  45   PRO G C   
18194 O  O   . PRO G  47  ? 3.8461 3.9660 1.4807 0.1963  -0.0949 0.3895  45   PRO G O   
18195 C  CB  . PRO G  47  ? 4.3422 4.4910 1.6448 0.1915  0.0261  0.4234  45   PRO G CB  
18196 C  CG  . PRO G  47  ? 4.2785 4.4270 1.5635 0.1860  0.0301  0.3052  45   PRO G CG  
18197 C  CD  . PRO G  47  ? 4.6408 4.8185 1.8249 0.1827  -0.0549 0.2786  45   PRO G CD  
18198 N  N   . GLU G  48  ? 3.8587 3.9731 1.4451 0.2103  -0.1095 0.5596  46   GLU G N   
18199 C  CA  . GLU G  48  ? 3.8340 3.9182 1.5991 0.2167  -0.1272 0.5784  46   GLU G CA  
18200 C  C   . GLU G  48  ? 3.8248 3.8759 1.6934 0.2076  -0.0503 0.5698  46   GLU G C   
18201 O  O   . GLU G  48  ? 3.7618 3.7851 1.7740 0.2109  -0.0577 0.5836  46   GLU G O   
18202 C  CB  . GLU G  48  ? 3.8046 3.8749 1.5840 0.2317  -0.1719 0.6822  46   GLU G CB  
18203 C  CG  . GLU G  48  ? 3.8056 3.9138 1.5183 0.2460  -0.2620 0.6941  46   GLU G CG  
18204 C  CD  . GLU G  48  ? 3.8285 3.9162 1.5934 0.2680  -0.3119 0.7911  46   GLU G CD  
18205 O  OE1 . GLU G  48  ? 3.8119 3.8502 1.6297 0.2679  -0.2711 0.8578  46   GLU G OE1 
18206 O  OE2 . GLU G  48  ? 3.8656 3.9864 1.6242 0.2854  -0.3931 0.8001  46   GLU G OE2 
18207 N  N   . ALA G  49  ? 3.7664 3.8238 1.5668 0.1976  0.0226  0.5466  47   ALA G N   
18208 C  CA  . ALA G  49  ? 3.7373 3.7745 1.6435 0.1901  0.0909  0.5284  47   ALA G CA  
18209 C  C   . ALA G  49  ? 3.7532 3.7843 1.7552 0.1896  0.0822  0.4366  47   ALA G C   
18210 O  O   . ALA G  49  ? 3.5085 3.5179 1.6451 0.1874  0.1004  0.4310  47   ALA G O   
18211 C  CB  . ALA G  49  ? 3.7247 3.7796 1.5370 0.1837  0.1722  0.5297  47   ALA G CB  
18212 N  N   . VAL G  50  ? 3.9810 4.0296 1.9126 0.1894  0.0536  0.3647  48   VAL G N   
18213 C  CA  . VAL G  50  ? 3.7169 3.7562 1.7381 0.1857  0.0386  0.2825  48   VAL G CA  
18214 C  C   . VAL G  50  ? 3.6491 3.6937 1.7521 0.1884  -0.0396 0.2855  48   VAL G C   
18215 O  O   . VAL G  50  ? 3.7488 3.7841 1.9606 0.1843  -0.0495 0.2374  48   VAL G O   
18216 C  CB  . VAL G  50  ? 3.8157 3.8635 1.7357 0.1804  0.0479  0.1968  48   VAL G CB  
18217 C  CG1 . VAL G  50  ? 3.9869 4.0335 1.8302 0.1833  0.1307  0.1906  48   VAL G CG1 
18218 C  CG2 . VAL G  50  ? 4.0369 4.1142 1.8366 0.1782  -0.0191 0.1908  48   VAL G CG2 
18219 N  N   . LEU G  51  ? 3.6522 3.7149 1.7073 0.1966  -0.0944 0.3431  49   LEU G N   
18220 C  CA  . LEU G  51  ? 3.4964 3.5687 1.6472 0.2051  -0.1644 0.3554  49   LEU G CA  
18221 C  C   . LEU G  51  ? 3.5949 3.6345 1.8858 0.2127  -0.1480 0.4001  49   LEU G C   
18222 O  O   . LEU G  51  ? 3.6226 3.6646 2.0275 0.2187  -0.1847 0.3852  49   LEU G O   
18223 C  CB  . LEU G  51  ? 3.6419 3.7442 1.7040 0.2167  -0.2298 0.4086  49   LEU G CB  
18224 C  CG  . LEU G  51  ? 3.9542 4.0985 1.8892 0.2083  -0.2705 0.3571  49   LEU G CG  
18225 C  CD1 . LEU G  51  ? 4.1786 4.3570 2.0324 0.2225  -0.3404 0.4213  49   LEU G CD1 
18226 C  CD2 . LEU G  51  ? 3.6614 3.8228 1.6751 0.1959  -0.3026 0.2686  49   LEU G CD2 
18227 N  N   . ALA G  52  ? 3.7563 3.7679 2.0410 0.2109  -0.0926 0.4528  50   ALA G N   
18228 C  CA  . ALA G  52  ? 3.6490 3.6254 2.0655 0.2125  -0.0716 0.4834  50   ALA G CA  
18229 C  C   . ALA G  52  ? 3.5331 3.5026 2.0450 0.2031  -0.0385 0.4142  50   ALA G C   
18230 O  O   . ALA G  52  ? 3.5257 3.4783 2.1588 0.2060  -0.0475 0.4109  50   ALA G O   
18231 C  CB  . ALA G  52  ? 3.6745 3.6267 2.0602 0.2067  -0.0213 0.5562  50   ALA G CB  
18232 N  N   . LEU G  53  ? 3.4977 3.4779 1.9534 0.1935  0.0007  0.3590  51   LEU G N   
18233 C  CA  . LEU G  53  ? 3.4339 3.4067 1.9718 0.1868  0.0249  0.2924  51   LEU G CA  
18234 C  C   . LEU G  53  ? 3.3700 3.3560 1.9587 0.1863  -0.0302 0.2422  51   LEU G C   
18235 O  O   . LEU G  53  ? 3.4152 3.3921 2.1146 0.1841  -0.0298 0.2178  51   LEU G O   
18236 C  CB  . LEU G  53  ? 3.5104 3.4865 1.9735 0.1812  0.0782  0.2461  51   LEU G CB  
18237 C  CG  . LEU G  53  ? 3.4403 3.4090 1.9168 0.1798  0.1510  0.2697  51   LEU G CG  
18238 C  CD1 . LEU G  53  ? 3.5435 3.5198 1.9488 0.1799  0.1674  0.3459  51   LEU G CD1 
18239 C  CD2 . LEU G  53  ? 3.5103 3.4818 1.9388 0.1807  0.1980  0.2065  51   LEU G CD2 
18240 N  N   . TYR G  54  ? 3.2936 3.3063 1.8023 0.1866  -0.0784 0.2269  52   TYR G N   
18241 C  CA  . TYR G  54  ? 3.2889 3.3241 1.8488 0.1817  -0.1308 0.1771  52   TYR G CA  
18242 C  C   . TYR G  54  ? 3.2676 3.3123 1.9370 0.1945  -0.1734 0.2132  52   TYR G C   
18243 O  O   . TYR G  54  ? 3.2346 3.2912 2.0002 0.1903  -0.1919 0.1757  52   TYR G O   
18244 C  CB  . TYR G  54  ? 3.6682 3.7359 2.1133 0.1763  -0.1755 0.1519  52   TYR G CB  
18245 C  CG  . TYR G  54  ? 3.7439 3.8433 2.2415 0.1654  -0.2316 0.0984  52   TYR G CG  
18246 C  CD1 . TYR G  54  ? 3.6519 3.7389 2.1874 0.1458  -0.2136 0.0246  52   TYR G CD1 
18247 C  CD2 . TYR G  54  ? 3.9149 4.0585 2.4284 0.1743  -0.3030 0.1244  52   TYR G CD2 
18248 C  CE1 . TYR G  54  ? 3.7816 3.8998 2.3702 0.1302  -0.2629 -0.0220 52   TYR G CE1 
18249 C  CE2 . TYR G  54  ? 3.9008 4.0847 2.4719 0.1618  -0.3538 0.0763  52   TYR G CE2 
18250 C  CZ  . TYR G  54  ? 3.8528 4.0241 2.4613 0.1371  -0.3325 0.0030  52   TYR G CZ  
18251 O  OH  . TYR G  54  ? 3.8389 4.0523 2.5107 0.1192  -0.3813 -0.0425 52   TYR G OH  
18252 N  N   . ASN G  55  ? 3.2279 3.2657 1.8847 0.2109  -0.1874 0.2866  53   ASN G N   
18253 C  CA  . ASN G  55  ? 3.2376 3.2740 2.0025 0.2283  -0.2213 0.3214  53   ASN G CA  
18254 C  C   . ASN G  55  ? 3.3574 3.3576 2.2312 0.2264  -0.1778 0.3194  53   ASN G C   
18255 O  O   . ASN G  55  ? 3.2817 3.2827 2.2599 0.2379  -0.1998 0.3207  53   ASN G O   
18256 C  CB  . ASN G  55  ? 3.2681 3.2967 1.9850 0.2475  -0.2494 0.4031  53   ASN G CB  
18257 C  CG  . ASN G  55  ? 3.6083 3.6851 2.2585 0.2572  -0.3177 0.4094  53   ASN G CG  
18258 O  OD1 . ASN G  55  ? 3.4842 3.5994 2.0973 0.2435  -0.3380 0.3499  53   ASN G OD1 
18259 N  ND2 . ASN G  55  ? 4.6412 4.7145 3.2766 0.2802  -0.3559 0.4829  53   ASN G ND2 
18260 N  N   . SER G  56  ? 3.5473 3.5207 2.3999 0.2131  -0.1172 0.3147  54   SER G N   
18261 C  CA  . SER G  56  ? 3.3517 3.2971 2.3020 0.2086  -0.0786 0.3095  54   SER G CA  
18262 C  C   . SER G  56  ? 3.1205 3.0763 2.1255 0.1971  -0.0647 0.2404  54   SER G C   
18263 O  O   . SER G  56  ? 3.0278 2.9691 2.1227 0.1952  -0.0464 0.2313  54   SER G O   
18264 C  CB  . SER G  56  ? 3.3066 3.2269 2.2216 0.1997  -0.0220 0.3425  54   SER G CB  
18265 O  OG  . SER G  56  ? 3.4230 3.3286 2.2901 0.2061  -0.0297 0.4135  54   SER G OG  
18266 N  N   . THR G  57  ? 3.0322 3.0094 1.9822 0.1880  -0.0732 0.1920  55   THR G N   
18267 C  CA  . THR G  57  ? 2.9976 2.9771 1.9993 0.1751  -0.0604 0.1306  55   THR G CA  
18268 C  C   . THR G  57  ? 3.1554 3.1646 2.2328 0.1749  -0.1070 0.1067  55   THR G C   
18269 O  O   . THR G  57  ? 3.2915 3.2996 2.4480 0.1669  -0.0943 0.0757  55   THR G O   
18270 C  CB  . THR G  57  ? 3.0268 3.0047 1.9408 0.1630  -0.0429 0.0848  55   THR G CB  
18271 O  OG1 . THR G  57  ? 3.2085 3.1707 2.0438 0.1672  -0.0009 0.1109  55   THR G OG1 
18272 C  CG2 . THR G  57  ? 2.9565 2.9189 1.9260 0.1505  -0.0155 0.0322  55   THR G CG2 
18273 N  N   . ARG G  58  ? 3.3344 3.3756 2.3917 0.1842  -0.1605 0.1233  56   ARG G N   
18274 C  CA  . ARG G  58  ? 3.3511 3.4338 2.4899 0.1864  -0.2059 0.1039  56   ARG G CA  
18275 C  C   . ARG G  58  ? 3.4103 3.4903 2.6502 0.2068  -0.2111 0.1359  56   ARG G C   
18276 O  O   . ARG G  58  ? 3.4444 3.5610 2.7692 0.2105  -0.2370 0.1164  56   ARG G O   
18277 C  CB  . ARG G  58  ? 3.3190 3.4462 2.4032 0.1909  -0.2662 0.1096  56   ARG G CB  
18278 C  CG  . ARG G  58  ? 3.2795 3.4133 2.2611 0.1691  -0.2699 0.0673  56   ARG G CG  
18279 C  CD  . ARG G  58  ? 3.2679 3.4594 2.2185 0.1680  -0.3395 0.0600  56   ARG G CD  
18280 N  NE  . ARG G  58  ? 3.3131 3.5150 2.2004 0.1922  -0.3720 0.1232  56   ARG G NE  
18281 C  CZ  . ARG G  58  ? 3.3696 3.5987 2.3230 0.2181  -0.4135 0.1685  56   ARG G CZ  
18282 N  NH1 . ARG G  58  ? 3.3604 3.6148 2.4459 0.2236  -0.4243 0.1530  56   ARG G NH1 
18283 N  NH2 . ARG G  58  ? 3.4717 3.7024 2.3592 0.2400  -0.4424 0.2306  56   ARG G NH2 
18284 N  N   . ASP G  59  ? 3.3386 3.3768 2.5733 0.2188  -0.1859 0.1822  57   ASP G N   
18285 C  CA  . ASP G  59  ? 3.2348 3.2578 2.5535 0.2397  -0.1925 0.2141  57   ASP G CA  
18286 C  C   . ASP G  59  ? 3.2488 3.2529 2.6428 0.2301  -0.1518 0.1856  57   ASP G C   
18287 O  O   . ASP G  59  ? 3.3070 3.2712 2.6941 0.2237  -0.1128 0.2009  57   ASP G O   
18288 C  CB  . ASP G  59  ? 3.1804 3.1622 2.4516 0.2522  -0.1882 0.2789  57   ASP G CB  
18289 C  CG  . ASP G  59  ? 3.1554 3.1111 2.5074 0.2761  -0.2022 0.3137  57   ASP G CG  
18290 O  OD1 . ASP G  59  ? 3.2002 3.1689 2.6457 0.2840  -0.2065 0.2836  57   ASP G OD1 
18291 O  OD2 . ASP G  59  ? 3.1992 3.1178 2.5196 0.2868  -0.2064 0.3717  57   ASP G OD2 
18292 N  N   . ARG G  60  ? 3.1859 3.2242 2.6544 0.2280  -0.1616 0.1457  58   ARG G N   
18293 C  CA  . ARG G  60  ? 3.1262 3.1532 2.6609 0.2190  -0.1262 0.1187  58   ARG G CA  
18294 C  C   . ARG G  60  ? 3.2238 3.2597 2.8508 0.2411  -0.1401 0.1230  58   ARG G C   
18295 O  O   . ARG G  60  ? 3.3196 3.4036 3.0056 0.2468  -0.1613 0.0986  58   ARG G O   
18296 C  CB  . ARG G  60  ? 3.1020 3.1556 2.6425 0.1948  -0.1146 0.0683  58   ARG G CB  
18297 C  CG  . ARG G  60  ? 3.1822 3.2926 2.7442 0.1903  -0.1545 0.0420  58   ARG G CG  
18298 C  CD  . ARG G  60  ? 3.2026 3.3499 2.8657 0.1888  -0.1521 0.0152  58   ARG G CD  
18299 N  NE  . ARG G  60  ? 3.1439 3.3406 2.8296 0.1667  -0.1696 -0.0224 58   ARG G NE  
18300 C  CZ  . ARG G  60  ? 3.0280 3.2737 2.8025 0.1628  -0.1725 -0.0441 58   ARG G CZ  
18301 N  NH1 . ARG G  60  ? 2.9956 3.2463 2.8373 0.1835  -0.1585 -0.0352 58   ARG G NH1 
18302 N  NH2 . ARG G  60  ? 2.9845 3.2750 2.7813 0.1367  -0.1880 -0.0762 58   ARG G NH2 
18303 N  N   . VAL G  61  ? 3.0029 2.9923 2.6453 0.2528  -0.1262 0.1521  59   VAL G N   
18304 C  CA  . VAL G  61  ? 2.9138 2.8971 2.6410 0.2725  -0.1284 0.1468  59   VAL G CA  
18305 C  C   . VAL G  61  ? 2.8831 2.8413 2.6313 0.2553  -0.0862 0.1246  59   VAL G C   
18306 O  O   . VAL G  61  ? 2.8399 2.8285 2.6291 0.2475  -0.0727 0.0862  59   VAL G O   
18307 C  CB  . VAL G  61  ? 2.8674 2.8092 2.6030 0.2997  -0.1498 0.1938  59   VAL G CB  
18308 C  CG1 . VAL G  61  ? 2.8486 2.7804 2.6749 0.3240  -0.1515 0.1794  59   VAL G CG1 
18309 C  CG2 . VAL G  61  ? 2.9295 2.8982 2.6325 0.3171  -0.1948 0.2235  59   VAL G CG2 
18310 N  N   . ALA G  62  ? 2.8108 2.7179 2.5304 0.2476  -0.0662 0.1510  60   ALA G N   
18311 C  CA  . ALA G  62  ? 2.6328 2.5182 2.3667 0.2296  -0.0310 0.1356  60   ALA G CA  
18312 C  C   . ALA G  62  ? 2.6012 2.4818 2.4057 0.2407  -0.0288 0.1105  60   ALA G C   
18313 O  O   . ALA G  62  ? 2.5909 2.4416 2.4087 0.2304  -0.0091 0.1057  60   ALA G O   
18314 C  CB  . ALA G  62  ? 2.5917 2.5051 2.2996 0.2073  -0.0077 0.1078  60   ALA G CB  
18315 N  N   . ALA G  74  ? 2.9862 2.3372 2.5085 0.0557  0.3048  -0.2268 72   ALA G N   
18316 C  CA  . ALA G  74  ? 2.9140 2.3080 2.4149 0.0956  0.3181  -0.2095 72   ALA G CA  
18317 C  C   . ALA G  74  ? 3.1312 2.5207 2.5652 0.1052  0.3184  -0.2536 72   ALA G C   
18318 O  O   . ALA G  74  ? 3.2117 2.5338 2.6136 0.1018  0.3256  -0.2992 72   ALA G O   
18319 C  CB  . ALA G  74  ? 2.8158 2.2971 2.3399 0.0925  0.3017  -0.1708 72   ALA G CB  
18320 N  N   . ASP G  75  ? 3.3621 2.8202 2.7715 0.1161  0.3107  -0.2403 73   ASP G N   
18321 C  CA  . ASP G  75  ? 3.3447 2.8086 2.6823 0.1283  0.3142  -0.2717 73   ASP G CA  
18322 C  C   . ASP G  75  ? 3.3529 2.8321 2.6539 0.0939  0.2754  -0.3048 73   ASP G C   
18323 O  O   . ASP G  75  ? 3.1106 2.6540 2.4159 0.0836  0.2485  -0.2837 73   ASP G O   
18324 C  CB  . ASP G  75  ? 3.1436 2.6714 2.4737 0.1543  0.3258  -0.2347 73   ASP G CB  
18325 C  CG  . ASP G  75  ? 3.0609 2.5833 2.4281 0.1891  0.3627  -0.2063 73   ASP G CG  
18326 O  OD1 . ASP G  75  ? 3.1043 2.6484 2.5322 0.1893  0.3596  -0.1664 73   ASP G OD1 
18327 O  OD2 . ASP G  75  ? 3.0466 2.5474 2.3824 0.2170  0.3945  -0.2251 73   ASP G OD2 
18328 N  N   . TYR G  76  ? 3.4408 2.8602 2.7080 0.0770  0.2708  -0.3579 74   TYR G N   
18329 C  CA  . TYR G  76  ? 3.4611 2.8965 2.6916 0.0428  0.2303  -0.3954 74   TYR G CA  
18330 C  C   . TYR G  76  ? 3.3835 2.8290 2.5177 0.0559  0.2280  -0.4269 74   TYR G C   
18331 O  O   . TYR G  76  ? 3.4590 2.9352 2.5551 0.0317  0.1886  -0.4502 74   TYR G O   
18332 C  CB  . TYR G  76  ? 3.5635 2.9302 2.8120 0.0076  0.2202  -0.4392 74   TYR G CB  
18333 C  CG  . TYR G  76  ? 3.6271 3.0040 2.9633 -0.0214 0.2089  -0.4096 74   TYR G CG  
18334 C  CD1 . TYR G  76  ? 3.5952 3.0399 2.9635 -0.0540 0.1700  -0.4029 74   TYR G CD1 
18335 C  CD2 . TYR G  76  ? 3.6363 2.9586 3.0233 -0.0145 0.2384  -0.3866 74   TYR G CD2 
18336 C  CE1 . TYR G  76  ? 3.4602 2.9211 2.9073 -0.0803 0.1655  -0.3768 74   TYR G CE1 
18337 C  CE2 . TYR G  76  ? 3.5163 2.8506 2.9745 -0.0423 0.2314  -0.3566 74   TYR G CE2 
18338 C  CZ  . TYR G  76  ? 3.4374 2.8424 2.9246 -0.0759 0.1974  -0.3534 74   TYR G CZ  
18339 O  OH  . TYR G  76  ? 3.3637 2.7872 2.9208 -0.1031 0.1963  -0.3244 74   TYR G OH  
18340 N  N   . TYR G  77  ? 3.3989 2.8261 2.4933 0.0937  0.2691  -0.4267 75   TYR G N   
18341 C  CA  . TYR G  77  ? 3.5845 3.0201 2.5783 0.1065  0.2741  -0.4576 75   TYR G CA  
18342 C  C   . TYR G  77  ? 3.6992 3.2198 2.6687 0.1105  0.2543  -0.4138 75   TYR G C   
18343 O  O   . TYR G  77  ? 3.7220 3.2896 2.7557 0.1063  0.2390  -0.3639 75   TYR G O   
18344 C  CB  . TYR G  77  ? 3.5147 2.9089 2.4809 0.1474  0.3306  -0.4711 75   TYR G CB  
18345 C  CG  . TYR G  77  ? 3.5558 2.8528 2.5325 0.1483  0.3503  -0.5217 75   TYR G CG  
18346 C  CD1 . TYR G  77  ? 3.6064 2.8473 2.5022 0.1394  0.3485  -0.5950 75   TYR G CD1 
18347 C  CD2 . TYR G  77  ? 3.6466 2.9038 2.7112 0.1582  0.3696  -0.4960 75   TYR G CD2 
18348 C  CE1 . TYR G  77  ? 3.6988 2.8389 2.6065 0.1401  0.3669  -0.6437 75   TYR G CE1 
18349 C  CE2 . TYR G  77  ? 3.7122 2.8711 2.7894 0.1607  0.3875  -0.5372 75   TYR G CE2 
18350 C  CZ  . TYR G  77  ? 3.6747 2.7714 2.6760 0.1516  0.3869  -0.6123 75   TYR G CZ  
18351 O  OH  . TYR G  77  ? 3.6928 2.6801 2.7085 0.1537  0.4049  -0.6563 75   TYR G OH  
18352 N  N   . ALA G  78  ? 3.7105 3.2468 2.5817 0.1194  0.2559  -0.4331 76   ALA G N   
18353 C  CA  . ALA G  78  ? 3.5560 3.1628 2.3888 0.1211  0.2338  -0.3934 76   ALA G CA  
18354 C  C   . ALA G  78  ? 3.4395 3.0773 2.2796 0.1534  0.2769  -0.3416 76   ALA G C   
18355 O  O   . ALA G  78  ? 3.4851 3.0964 2.3314 0.1787  0.3267  -0.3479 76   ALA G O   
18356 C  CB  . ALA G  78  ? 3.6304 3.2431 2.3451 0.1122  0.2114  -0.4345 76   ALA G CB  
18357 N  N   . LYS G  79  ? 3.2223 2.9175 2.0666 0.1521  0.2564  -0.2894 77   LYS G N   
18358 C  CA  . LYS G  79  ? 3.1154 2.8451 1.9728 0.1743  0.2906  -0.2352 77   LYS G CA  
18359 C  C   . LYS G  79  ? 3.1262 2.8945 1.8934 0.1755  0.2799  -0.2127 77   LYS G C   
18360 O  O   . LYS G  79  ? 3.1489 2.9395 1.8970 0.1592  0.2299  -0.2033 77   LYS G O   
18361 C  CB  . LYS G  79  ? 3.0015 2.7553 1.9641 0.1703  0.2786  -0.1850 77   LYS G CB  
18362 C  CG  . LYS G  79  ? 2.9744 2.6958 2.0197 0.1629  0.2770  -0.2019 77   LYS G CG  
18363 C  CD  . LYS G  79  ? 3.1315 2.8161 2.1928 0.1848  0.3264  -0.2181 77   LYS G CD  
18364 C  CE  . LYS G  79  ? 3.1391 2.7881 2.2791 0.1774  0.3230  -0.2261 77   LYS G CE  
18365 N  NZ  . LYS G  79  ? 3.2746 2.8836 2.4360 0.2030  0.3674  -0.2380 77   LYS G NZ  
18366 N  N   . GLU G  80  ? 3.1515 2.9311 1.8655 0.1958  0.3275  -0.2013 78   GLU G N   
18367 C  CA  . GLU G  80  ? 3.2547 3.0705 1.8752 0.1973  0.3251  -0.1728 78   GLU G CA  
18368 C  C   . GLU G  80  ? 3.4018 3.2561 2.0783 0.1961  0.3194  -0.0968 78   GLU G C   
18369 O  O   . GLU G  80  ? 3.4167 3.2820 2.1597 0.2065  0.3579  -0.0656 78   GLU G O   
18370 C  CB  . GLU G  80  ? 3.3327 3.1484 1.8712 0.2182  0.3844  -0.1928 78   GLU G CB  
18371 C  CG  . GLU G  80  ? 3.3991 3.2542 1.8305 0.2189  0.3888  -0.1589 78   GLU G CG  
18372 C  CD  . GLU G  80  ? 3.4809 3.3393 1.8238 0.2396  0.4516  -0.1869 78   GLU G CD  
18373 O  OE1 . GLU G  80  ? 3.4753 3.2964 1.8288 0.2539  0.4824  -0.2457 78   GLU G OE1 
18374 O  OE2 . GLU G  80  ? 3.4694 3.3663 1.7329 0.2428  0.4725  -0.1494 78   GLU G OE2 
18375 N  N   . VAL G  81  ? 3.6101 3.4843 2.2624 0.1838  0.2700  -0.0675 79   VAL G N   
18376 C  CA  . VAL G  81  ? 3.5952 3.4923 2.3082 0.1812  0.2559  -0.0001 79   VAL G CA  
18377 C  C   . VAL G  81  ? 3.5328 3.4549 2.1705 0.1864  0.2783  0.0505  79   VAL G C   
18378 O  O   . VAL G  81  ? 3.4885 3.4201 2.0183 0.1855  0.2617  0.0478  79   VAL G O   
18379 C  CB  . VAL G  81  ? 3.6207 3.5226 2.3670 0.1692  0.1898  0.0061  79   VAL G CB  
18380 C  CG1 . VAL G  81  ? 3.4759 3.3922 2.2781 0.1701  0.1767  0.0727  79   VAL G CG1 
18381 C  CG2 . VAL G  81  ? 3.5629 3.4456 2.3899 0.1606  0.1743  -0.0382 79   VAL G CG2 
18382 N  N   . THR G  82  ? 3.4514 3.3866 2.1459 0.1894  0.3147  0.0987  80   THR G N   
18383 C  CA  . THR G  82  ? 3.4721 3.4313 2.1153 0.1891  0.3394  0.1580  80   THR G CA  
18384 C  C   . THR G  82  ? 3.3970 3.3588 2.1380 0.1802  0.3324  0.2181  80   THR G C   
18385 O  O   . THR G  82  ? 3.4683 3.4207 2.3133 0.1779  0.3277  0.2079  80   THR G O   
18386 C  CB  . THR G  82  ? 3.4330 3.4117 2.0356 0.2003  0.4103  0.1489  80   THR G CB  
18387 O  OG1 . THR G  82  ? 3.2067 3.1836 1.9121 0.2075  0.4424  0.1292  80   THR G OG1 
18388 C  CG2 . THR G  82  ? 3.4397 3.4116 1.9219 0.2095  0.4182  0.0903  80   THR G CG2 
18389 N  N   . ARG G  83  ? 3.3397 3.3111 2.0433 0.1740  0.3314  0.2812  81   ARG G N   
18390 C  CA  . ARG G  83  ? 3.1698 3.1334 1.9595 0.1629  0.3220  0.3384  81   ARG G CA  
18391 C  C   . ARG G  83  ? 3.2242 3.2087 1.9942 0.1539  0.3708  0.3983  81   ARG G C   
18392 O  O   . ARG G  83  ? 3.3956 3.4027 2.0676 0.1578  0.4045  0.4046  81   ARG G O   
18393 C  CB  . ARG G  83  ? 3.1062 3.0478 1.8936 0.1621  0.2581  0.3649  81   ARG G CB  
18394 C  CG  . ARG G  83  ? 3.2151 3.1605 1.8988 0.1622  0.2475  0.4180  81   ARG G CG  
18395 C  CD  . ARG G  83  ? 3.2191 3.1411 1.9225 0.1656  0.1854  0.4553  81   ARG G CD  
18396 N  NE  . ARG G  83  ? 3.5935 3.5156 2.2030 0.1658  0.1782  0.5208  81   ARG G NE  
18397 C  CZ  . ARG G  83  ? 3.5654 3.4662 2.1756 0.1725  0.1281  0.5694  81   ARG G CZ  
18398 N  NH1 . ARG G  83  ? 3.3843 3.2652 2.0881 0.1809  0.0830  0.5548  81   ARG G NH1 
18399 N  NH2 . ARG G  83  ? 3.6864 3.5868 2.2027 0.1727  0.1247  0.6343  81   ARG G NH2 
18400 N  N   . VAL G  84  ? 2.9245 2.9027 1.7892 0.1396  0.3753  0.4410  82   VAL G N   
18401 C  CA  . VAL G  84  ? 2.9036 2.9010 1.7732 0.1234  0.4191  0.5038  82   VAL G CA  
18402 C  C   . VAL G  84  ? 2.9131 2.8751 1.8496 0.1061  0.3872  0.5591  82   VAL G C   
18403 O  O   . VAL G  84  ? 2.8774 2.8182 1.9111 0.1025  0.3614  0.5406  82   VAL G O   
18404 C  CB  . VAL G  84  ? 2.8530 2.8909 1.7921 0.1203  0.4768  0.4889  82   VAL G CB  
18405 C  CG1 . VAL G  84  ? 2.9778 3.0520 1.8338 0.1378  0.5253  0.4550  82   VAL G CG1 
18406 C  CG2 . VAL G  84  ? 2.7910 2.8187 1.8358 0.1241  0.4563  0.4431  82   VAL G CG2 
18407 N  N   . LEU G  85  ? 3.1437 3.0958 2.0259 0.0953  0.3904  0.6269  83   LEU G N   
18408 C  CA  . LEU G  85  ? 3.2164 3.1231 2.1585 0.0793  0.3620  0.6831  83   LEU G CA  
18409 C  C   . LEU G  85  ? 3.2602 3.1777 2.3030 0.0511  0.4008  0.7096  83   LEU G C   
18410 O  O   . LEU G  85  ? 3.2392 3.2086 2.3007 0.0456  0.4518  0.6941  83   LEU G O   
18411 C  CB  . LEU G  85  ? 3.3503 3.2367 2.1974 0.0779  0.3497  0.7526  83   LEU G CB  
18412 C  CG  . LEU G  85  ? 3.4380 3.3175 2.1860 0.1036  0.3013  0.7352  83   LEU G CG  
18413 C  CD1 . LEU G  85  ? 3.6851 3.5551 2.3273 0.1016  0.2968  0.8121  83   LEU G CD1 
18414 C  CD2 . LEU G  85  ? 3.2812 3.1221 2.0999 0.1179  0.2375  0.7073  83   LEU G CD2 
18415 N  N   . MET G  86  ? 3.3406 3.2090 2.4535 0.0336  0.3748  0.7487  84   MET G N   
18416 C  CA  . MET G  86  ? 3.2430 3.1161 2.4594 0.0013  0.4014  0.7713  84   MET G CA  
18417 C  C   . MET G  86  ? 3.2220 3.0962 2.4118 -0.0270 0.4377  0.8542  84   MET G C   
18418 O  O   . MET G  86  ? 3.2684 3.1381 2.3531 -0.0195 0.4422  0.8961  84   MET G O   
18419 C  CB  . MET G  86  ? 3.1804 2.9955 2.4930 -0.0055 0.3551  0.7583  84   MET G CB  
18420 C  CG  . MET G  86  ? 3.3318 3.0716 2.6326 -0.0084 0.3181  0.8130  84   MET G CG  
18421 S  SD  . MET G  86  ? 3.2706 2.9406 2.6968 -0.0233 0.2795  0.7993  84   MET G SD  
18422 C  CE  . MET G  86  ? 3.5840 3.1638 2.9789 -0.0203 0.2457  0.8751  84   MET G CE  
18423 N  N   . VAL G  87  ? 3.4512 3.3339 2.7373 -0.0628 0.4631  0.8801  85   VAL G N   
18424 C  CA  . VAL G  87  ? 3.7691 3.6569 3.0514 -0.0983 0.5028  0.9609  85   VAL G CA  
18425 C  C   . VAL G  87  ? 3.8833 3.6778 3.1919 -0.1163 0.4624  1.0153  85   VAL G C   
18426 O  O   . VAL G  87  ? 3.8765 3.6165 3.2593 -0.1147 0.4171  0.9843  85   VAL G O   
18427 C  CB  . VAL G  87  ? 3.8131 3.7672 3.1965 -0.1313 0.5520  0.9608  85   VAL G CB  
18428 C  CG1 . VAL G  87  ? 3.9617 3.9331 3.3407 -0.1713 0.6007  1.0465  85   VAL G CG1 
18429 C  CG2 . VAL G  87  ? 3.7381 3.7771 3.1080 -0.1053 0.5874  0.9014  85   VAL G CG2 
18430 N  N   . GLU G  88  ? 3.9676 3.7413 3.2138 -0.1326 0.4807  1.0975  86   GLU G N   
18431 C  CA  . GLU G  88  ? 3.9394 3.6165 3.2075 -0.1491 0.4464  1.1599  86   GLU G CA  
18432 C  C   . GLU G  88  ? 4.0129 3.6636 3.4177 -0.1963 0.4536  1.1699  86   GLU G C   
18433 O  O   . GLU G  88  ? 4.0579 3.7735 3.5390 -0.2158 0.4825  1.1316  86   GLU G O   
18434 C  CB  . GLU G  88  ? 3.9442 3.6114 3.1085 -0.1582 0.4703  1.2529  86   GLU G CB  
18435 C  CG  . GLU G  88  ? 3.9315 3.6527 2.9523 -0.1210 0.4792  1.2405  86   GLU G CG  
18436 C  CD  . GLU G  88  ? 4.1379 3.8774 3.0524 -0.1372 0.5216  1.3297  86   GLU G CD  
18437 O  OE1 . GLU G  88  ? 4.2193 3.9280 3.1776 -0.1790 0.5458  1.4065  86   GLU G OE1 
18438 O  OE2 . GLU G  88  ? 4.2325 4.0167 3.0172 -0.1102 0.5312  1.3226  86   GLU G OE2 
18439 N  N   . THR G  89  ? 3.9783 3.5307 3.4163 -0.2150 0.4246  1.2224  87   THR G N   
18440 C  CA  . THR G  89  ? 3.9167 3.4336 3.4784 -0.2670 0.4307  1.2380  87   THR G CA  
18441 C  C   . THR G  89  ? 3.8289 3.4016 3.4077 -0.3188 0.4954  1.3047  87   THR G C   
18442 O  O   . THR G  89  ? 3.7184 3.2726 3.4043 -0.3704 0.5048  1.3225  87   THR G O   
18443 C  CB  . THR G  89  ? 3.9077 3.2919 3.4991 -0.2708 0.3825  1.2739  87   THR G CB  
18444 O  OG1 . THR G  89  ? 3.9153 3.2570 3.4064 -0.2584 0.3820  1.3582  87   THR G OG1 
18445 C  CG2 . THR G  89  ? 3.6850 3.0245 3.2975 -0.2261 0.3232  1.1955  87   THR G CG2 
18446 N  N   . HIS G  90  ? 3.7719 3.4144 3.2490 -0.3079 0.5405  1.3397  88   HIS G N   
18447 C  CA  . HIS G  90  ? 3.8198 3.5381 3.3082 -0.3517 0.6117  1.3964  88   HIS G CA  
18448 C  C   . HIS G  90  ? 3.6853 3.5256 3.2209 -0.3462 0.6494  1.3273  88   HIS G C   
18449 O  O   . HIS G  90  ? 3.6097 3.4566 3.2012 -0.3251 0.6160  1.2458  88   HIS G O   
18450 C  CB  . HIS G  90  ? 4.0837 3.8114 3.4285 -0.3407 0.6427  1.4721  88   HIS G CB  
18451 C  CG  . HIS G  90  ? 4.2405 3.8495 3.5266 -0.3314 0.5953  1.5351  88   HIS G CG  
18452 N  ND1 . HIS G  90  ? 4.1318 3.6773 3.3765 -0.2806 0.5281  1.4942  88   HIS G ND1 
18453 C  CD2 . HIS G  90  ? 4.4116 3.9548 3.6786 -0.3651 0.6053  1.6393  88   HIS G CD2 
18454 C  CE1 . HIS G  90  ? 4.3238 3.7716 3.5288 -0.2794 0.4969  1.5693  88   HIS G CE1 
18455 N  NE2 . HIS G  90  ? 4.4655 3.9047 3.6800 -0.3302 0.5422  1.6596  88   HIS G NE2 
18456 N  N   . ASN G  91  ? 3.7550 3.6932 3.2698 -0.3634 0.7206  1.3611  89   ASN G N   
18457 C  CA  . ASN G  91  ? 3.6605 3.7198 3.2086 -0.3486 0.7628  1.3010  89   ASN G CA  
18458 C  C   . ASN G  91  ? 3.5866 3.6688 3.2892 -0.3693 0.7423  1.2459  89   ASN G C   
18459 O  O   . ASN G  91  ? 3.5709 3.6974 3.2938 -0.3348 0.7300  1.1678  89   ASN G O   
18460 C  CB  . ASN G  91  ? 3.4909 3.5710 2.9265 -0.2837 0.7513  1.2359  89   ASN G CB  
18461 C  CG  . ASN G  91  ? 3.8694 3.9665 3.1502 -0.2655 0.7869  1.2818  89   ASN G CG  
18462 O  OD1 . ASN G  91  ? 4.2223 4.3573 3.4835 -0.2978 0.8435  1.3546  89   ASN G OD1 
18463 N  ND2 . ASN G  91  ? 3.7302 3.8034 2.8983 -0.2156 0.7542  1.2394  89   ASN G ND2 
18464 N  N   . GLU G  92  ? 3.5467 3.5958 3.3565 -0.4276 0.7365  1.2875  90   GLU G N   
18465 C  CA  . GLU G  92  ? 3.4854 3.5687 3.4473 -0.4615 0.7229  1.2486  90   GLU G CA  
18466 C  C   . GLU G  92  ? 3.3523 3.3721 3.3461 -0.4354 0.6509  1.1688  90   GLU G C   
18467 O  O   . GLU G  92  ? 3.1359 3.2010 3.2353 -0.4497 0.6369  1.1199  90   GLU G O   
18468 C  CB  . GLU G  92  ? 3.3819 3.6142 3.3996 -0.4590 0.7789  1.2240  90   GLU G CB  
18469 C  CG  . GLU G  92  ? 3.1799 3.4941 3.1831 -0.4876 0.8591  1.2989  90   GLU G CG  
18470 C  CD  . GLU G  92  ? 3.0422 3.5057 3.0890 -0.4694 0.9168  1.2672  90   GLU G CD  
18471 O  OE1 . GLU G  92  ? 3.1690 3.6619 3.2296 -0.4252 0.8935  1.1892  90   GLU G OE1 
18472 O  OE2 . GLU G  92  ? 2.9405 3.4923 3.0105 -0.4982 0.9871  1.3222  90   GLU G OE2 
18473 N  N   . ILE G  93  ? 3.3308 3.2524 3.2380 -0.3977 0.6043  1.1553  91   ILE G N   
18474 C  CA  . ILE G  93  ? 3.1969 3.0564 3.1344 -0.3746 0.5397  1.0836  91   ILE G CA  
18475 C  C   . ILE G  93  ? 3.2635 3.0282 3.2882 -0.4191 0.5011  1.0968  91   ILE G C   
18476 O  O   . ILE G  93  ? 3.2423 2.9540 3.3014 -0.4061 0.4500  1.0368  91   ILE G O   
18477 C  CB  . ILE G  93  ? 3.2344 3.0397 3.0517 -0.3150 0.5084  1.0626  91   ILE G CB  
18478 C  CG1 . ILE G  93  ? 3.2290 3.1191 2.9497 -0.2786 0.5508  1.0571  91   ILE G CG1 
18479 C  CG2 . ILE G  93  ? 3.1963 2.9678 3.0385 -0.2836 0.4535  0.9802  91   ILE G CG2 
18480 C  CD1 . ILE G  93  ? 3.1187 3.1149 2.8902 -0.2685 0.5782  0.9999  91   ILE G CD1 
18481 N  N   . TYR G  94  ? 3.3526 3.0945 3.4156 -0.4736 0.5266  1.1723  92   TYR G N   
18482 C  CA  . TYR G  94  ? 3.3223 2.9492 3.4514 -0.5161 0.4915  1.1959  92   TYR G CA  
18483 C  C   . TYR G  94  ? 3.2921 2.9544 3.5600 -0.5853 0.5002  1.1946  92   TYR G C   
18484 O  O   . TYR G  94  ? 3.2813 2.8549 3.6188 -0.6147 0.4577  1.1740  92   TYR G O   
18485 C  CB  . TYR G  94  ? 3.3219 2.8674 3.3863 -0.5289 0.5058  1.2922  92   TYR G CB  
18486 C  CG  . TYR G  94  ? 3.3186 2.9546 3.3519 -0.5547 0.5770  1.3667  92   TYR G CG  
18487 C  CD1 . TYR G  94  ? 3.2520 2.9557 3.1655 -0.5082 0.6096  1.3756  92   TYR G CD1 
18488 C  CD2 . TYR G  94  ? 3.4589 3.1145 3.5830 -0.6276 0.6132  1.4259  92   TYR G CD2 
18489 C  CE1 . TYR G  94  ? 3.3832 3.1727 3.2622 -0.5298 0.6794  1.4398  92   TYR G CE1 
18490 C  CE2 . TYR G  94  ? 3.4570 3.2032 3.5552 -0.6515 0.6840  1.4950  92   TYR G CE2 
18491 C  CZ  . TYR G  94  ? 3.4230 3.2361 3.3955 -0.6006 0.7184  1.5010  92   TYR G CZ  
18492 O  OH  . TYR G  94  ? 3.3429 3.2486 3.2841 -0.6228 0.7933  1.5663  92   TYR G OH  
18493 N  N   . ASP G  95  ? 3.2931 3.0844 3.6058 -0.6118 0.5534  1.2137  93   ASP G N   
18494 C  CA  . ASP G  95  ? 3.2345 3.0745 3.6880 -0.6813 0.5609  1.2165  93   ASP G CA  
18495 C  C   . ASP G  95  ? 3.1322 3.0034 3.6625 -0.6764 0.5156  1.1244  93   ASP G C   
18496 O  O   . ASP G  95  ? 3.1325 3.0426 3.7830 -0.7342 0.5094  1.1164  93   ASP G O   
18497 C  CB  . ASP G  95  ? 3.1861 3.1696 3.6706 -0.7060 0.6342  1.2648  93   ASP G CB  
18498 C  CG  . ASP G  95  ? 3.2200 3.2429 3.8496 -0.7914 0.6492  1.2986  93   ASP G CG  
18499 O  OD1 . ASP G  95  ? 3.2656 3.1816 3.9544 -0.8370 0.6066  1.2999  93   ASP G OD1 
18500 O  OD2 . ASP G  95  ? 3.2621 3.4236 3.9498 -0.8133 0.7042  1.3228  93   ASP G OD2 
18501 N  N   . LYS G  96  ? 2.9780 2.8355 3.4423 -0.6121 0.4827  1.0568  94   LYS G N   
18502 C  CA  . LYS G  96  ? 2.9768 2.8639 3.4975 -0.6027 0.4406  0.9722  94   LYS G CA  
18503 C  C   . LYS G  96  ? 3.1730 2.9325 3.6717 -0.5850 0.3781  0.9209  94   LYS G C   
18504 O  O   . LYS G  96  ? 3.1787 2.9313 3.7483 -0.6078 0.3395  0.8662  94   LYS G O   
18505 C  CB  . LYS G  96  ? 2.9039 2.8957 3.3782 -0.5432 0.4573  0.9291  94   LYS G CB  
18506 C  CG  . LYS G  96  ? 2.8412 2.9709 3.3446 -0.5510 0.5205  0.9650  94   LYS G CG  
18507 C  CD  . LYS G  96  ? 2.8047 3.0289 3.4489 -0.6016 0.5200  0.9540  94   LYS G CD  
18508 C  CE  . LYS G  96  ? 2.7380 3.1161 3.4130 -0.5867 0.5774  0.9671  94   LYS G CE  
18509 N  NZ  . LYS G  96  ? 2.8139 3.2173 3.4438 -0.5949 0.6445  1.0418  94   LYS G NZ  
18510 N  N   . PHE G  97  ? 3.2718 2.9353 3.6754 -0.5445 0.3669  0.9363  95   PHE G N   
18511 C  CA  . PHE G  97  ? 3.2694 2.8267 3.6493 -0.5145 0.3120  0.8814  95   PHE G CA  
18512 C  C   . PHE G  97  ? 3.3966 2.8120 3.7602 -0.5266 0.2960  0.9290  95   PHE G C   
18513 O  O   . PHE G  97  ? 3.6232 2.9809 4.0629 -0.5847 0.2894  0.9520  95   PHE G O   
18514 C  CB  . PHE G  97  ? 3.1985 2.7812 3.4851 -0.4409 0.3047  0.8394  95   PHE G CB  
18515 C  CG  . PHE G  97  ? 3.2372 2.9546 3.5229 -0.4229 0.3323  0.8131  95   PHE G CG  
18516 C  CD1 . PHE G  97  ? 3.1145 2.8854 3.4544 -0.4234 0.3101  0.7469  95   PHE G CD1 
18517 C  CD2 . PHE G  97  ? 3.3061 3.0948 3.5361 -0.4054 0.3810  0.8556  95   PHE G CD2 
18518 C  CE1 . PHE G  97  ? 3.0241 2.9127 3.3690 -0.4041 0.3341  0.7271  95   PHE G CE1 
18519 C  CE2 . PHE G  97  ? 3.2005 3.1059 3.4356 -0.3857 0.4080  0.8291  95   PHE G CE2 
18520 C  CZ  . PHE G  97  ? 3.0301 2.9837 3.3265 -0.3841 0.3837  0.7667  95   PHE G CZ  
18521 N  N   . LYS G  98  ? 3.3881 2.7466 3.6571 -0.4713 0.2864  0.9415  96   LYS G N   
18522 C  CA  . LYS G  98  ? 3.5466 2.7837 3.7802 -0.4689 0.2773  1.0046  96   LYS G CA  
18523 C  C   . LYS G  98  ? 3.7651 2.8675 4.0350 -0.4638 0.2263  0.9667  96   LYS G C   
18524 O  O   . LYS G  98  ? 3.8550 2.8731 4.0699 -0.4189 0.2038  0.9806  96   LYS G O   
18525 C  CB  . LYS G  98  ? 3.6362 2.8716 3.9022 -0.5305 0.3171  1.0958  96   LYS G CB  
18526 C  CG  . LYS G  98  ? 3.6059 2.7009 3.8537 -0.5400 0.3054  1.1686  96   LYS G CG  
18527 C  CD  . LYS G  98  ? 3.5643 2.6603 3.8600 -0.6125 0.3467  1.2567  96   LYS G CD  
18528 C  CE  . LYS G  98  ? 3.7601 2.6990 4.0538 -0.6293 0.3309  1.3294  96   LYS G CE  
18529 N  NZ  . LYS G  98  ? 3.9120 2.8443 4.2583 -0.7068 0.3720  1.4195  96   LYS G NZ  
18530 N  N   . GLN G  99  ? 3.9331 3.0154 4.2939 -0.5060 0.2061  0.9156  97   GLN G N   
18531 C  CA  . GLN G  99  ? 4.0626 3.0009 4.4652 -0.5140 0.1655  0.8907  97   GLN G CA  
18532 C  C   . GLN G  99  ? 3.9435 2.8656 4.3539 -0.4793 0.1254  0.7869  97   GLN G C   
18533 O  O   . GLN G  99  ? 3.9462 2.7449 4.3762 -0.4699 0.0932  0.7602  97   GLN G O   
18534 C  CB  . GLN G  99  ? 4.1389 3.0321 4.6407 -0.5976 0.1686  0.9136  97   GLN G CB  
18535 C  CG  . GLN G  99  ? 4.1433 3.0966 4.6618 -0.6492 0.2170  1.0055  97   GLN G CG  
18536 C  CD  . GLN G  99  ? 3.9876 3.0904 4.5663 -0.6903 0.2403  0.9814  97   GLN G CD  
18537 O  OE1 . GLN G  99  ? 4.0089 3.1731 4.6064 -0.6760 0.2183  0.8991  97   GLN G OE1 
18538 N  NE2 . GLN G  99  ? 3.8940 3.0601 4.5048 -0.7406 0.2858  1.0560  97   GLN G NE2 
18539 N  N   . SER G  100 ? 3.7842 2.8225 4.1820 -0.4605 0.1277  0.7282  98   SER G N   
18540 C  CA  . SER G  100 ? 3.7196 2.7422 4.1170 -0.4280 0.0925  0.6347  98   SER G CA  
18541 C  C   . SER G  100 ? 3.7208 2.6773 4.0530 -0.3582 0.0762  0.6293  98   SER G C   
18542 O  O   . SER G  100 ? 3.6151 2.6411 3.8824 -0.3100 0.0855  0.6277  98   SER G O   
18543 C  CB  . SER G  100 ? 3.5614 2.7210 3.9527 -0.4197 0.0991  0.5829  98   SER G CB  
18544 O  OG  . SER G  100 ? 3.5520 2.7953 3.8764 -0.3802 0.1269  0.6135  98   SER G OG  
18545 N  N   . THR G  101 ? 3.8293 2.6505 4.1839 -0.3528 0.0513  0.6264  99   THR G N   
18546 C  CA  . THR G  101 ? 3.7851 2.5373 4.0918 -0.2877 0.0353  0.6362  99   THR G CA  
18547 C  C   . THR G  101 ? 3.7047 2.5097 3.9760 -0.2294 0.0206  0.5600  99   THR G C   
18548 O  O   . THR G  101 ? 3.6341 2.4178 3.8632 -0.1721 0.0104  0.5698  99   THR G O   
18549 C  CB  . THR G  101 ? 3.8362 2.4283 4.1884 -0.2923 0.0108  0.6401  99   THR G CB  
18550 O  OG1 . THR G  101 ? 3.8228 2.3803 4.2228 -0.3038 -0.0115 0.5472  99   THR G OG1 
18551 C  CG2 . THR G  101 ? 3.8799 2.4101 4.2713 -0.3551 0.0259  0.7207  99   THR G CG2 
18552 N  N   . HIS G  102 ? 3.7210 2.5968 4.0099 -0.2437 0.0182  0.4880  100  HIS G N   
18553 C  CA  . HIS G  102 ? 3.7005 2.6292 3.9576 -0.1950 0.0076  0.4167  100  HIS G CA  
18554 C  C   . HIS G  102 ? 3.6409 2.7048 3.8527 -0.1839 0.0291  0.4200  100  HIS G C   
18555 O  O   . HIS G  102 ? 3.4611 2.5878 3.6607 -0.1664 0.0246  0.3585  100  HIS G O   
18556 C  CB  . HIS G  102 ? 3.6498 2.5587 3.9474 -0.2136 -0.0118 0.3309  100  HIS G CB  
18557 C  CG  . HIS G  102 ? 3.7844 2.5534 4.1237 -0.2174 -0.0337 0.3100  100  HIS G CG  
18558 N  ND1 . HIS G  102 ? 3.7952 2.5006 4.1258 -0.1623 -0.0500 0.2658  100  HIS G ND1 
18559 C  CD2 . HIS G  102 ? 3.9226 2.6007 4.3172 -0.2697 -0.0410 0.3254  100  HIS G CD2 
18560 C  CE1 . HIS G  102 ? 3.9705 2.5467 4.3468 -0.1763 -0.0659 0.2529  100  HIS G CE1 
18561 N  NE2 . HIS G  102 ? 4.0303 2.5833 4.4448 -0.2434 -0.0619 0.2885  100  HIS G NE2 
18562 N  N   . SER G  103 ? 3.7526 2.8593 3.9365 -0.1931 0.0541  0.4906  101  SER G N   
18563 C  CA  . SER G  103 ? 3.5239 2.7510 3.6668 -0.1827 0.0773  0.4920  101  SER G CA  
18564 C  C   . SER G  103 ? 3.5237 2.7686 3.6134 -0.1723 0.1006  0.5680  101  SER G C   
18565 O  O   . SER G  103 ? 3.5420 2.7167 3.6338 -0.1857 0.1022  0.6288  101  SER G O   
18566 C  CB  . SER G  103 ? 3.3732 2.6771 3.5609 -0.2302 0.0912  0.4759  101  SER G CB  
18567 O  OG  . SER G  103 ? 3.2963 2.5879 3.5230 -0.2412 0.0664  0.4050  101  SER G OG  
18568 N  N   . ILE G  104 ? 3.4760 2.8127 3.5139 -0.1483 0.1185  0.5635  102  ILE G N   
18569 C  CA  . ILE G  104 ? 3.4928 2.8635 3.4669 -0.1373 0.1434  0.6243  102  ILE G CA  
18570 C  C   . ILE G  104 ? 3.4455 2.9267 3.4099 -0.1488 0.1775  0.6174  102  ILE G C   
18571 O  O   . ILE G  104 ? 3.2920 2.8274 3.2599 -0.1332 0.1735  0.5605  102  ILE G O   
18572 C  CB  . ILE G  104 ? 3.3958 2.7531 3.3021 -0.0822 0.1249  0.6214  102  ILE G CB  
18573 C  CG1 . ILE G  104 ? 3.5340 2.7869 3.4411 -0.0696 0.1001  0.6626  102  ILE G CG1 
18574 C  CG2 . ILE G  104 ? 3.3717 2.8010 3.2013 -0.0680 0.1511  0.6520  102  ILE G CG2 
18575 C  CD1 . ILE G  104 ? 3.5287 2.7777 3.3725 -0.0172 0.0795  0.6731  102  ILE G CD1 
18576 N  N   . TYR G  105 ? 3.6259 3.1404 3.5797 -0.1747 0.2128  0.6768  103  TYR G N   
18577 C  CA  . TYR G  105 ? 3.5103 3.1302 3.4617 -0.1830 0.2505  0.6747  103  TYR G CA  
18578 C  C   . TYR G  105 ? 3.4814 3.1372 3.3408 -0.1552 0.2773  0.7084  103  TYR G C   
18579 O  O   . TYR G  105 ? 3.6088 3.2210 3.4220 -0.1557 0.2815  0.7660  103  TYR G O   
18580 C  CB  . TYR G  105 ? 3.5612 3.2107 3.5863 -0.2388 0.2766  0.7096  103  TYR G CB  
18581 C  CG  . TYR G  105 ? 3.6602 3.2618 3.7721 -0.2741 0.2462  0.6810  103  TYR G CG  
18582 C  CD1 . TYR G  105 ? 3.5456 3.1991 3.7092 -0.2809 0.2330  0.6212  103  TYR G CD1 
18583 C  CD2 . TYR G  105 ? 3.8146 3.3147 3.9531 -0.3002 0.2290  0.7130  103  TYR G CD2 
18584 C  CE1 . TYR G  105 ? 3.5803 3.1911 3.8145 -0.3148 0.2026  0.5897  103  TYR G CE1 
18585 C  CE2 . TYR G  105 ? 3.8176 3.2665 4.0319 -0.3338 0.2006  0.6798  103  TYR G CE2 
18586 C  CZ  . TYR G  105 ? 3.7269 3.2338 3.9861 -0.3419 0.1870  0.6158  103  TYR G CZ  
18587 O  OH  . TYR G  105 ? 3.7956 3.2524 4.1219 -0.3771 0.1563  0.5779  103  TYR G OH  
18588 N  N   . MET G  106 ? 3.4852 3.2174 3.3149 -0.1310 0.2945  0.6725  104  MET G N   
18589 C  CA  . MET G  106 ? 3.5447 3.3126 3.2816 -0.1026 0.3182  0.6883  104  MET G CA  
18590 C  C   . MET G  106 ? 3.4588 3.3209 3.2047 -0.1092 0.3662  0.6853  104  MET G C   
18591 O  O   . MET G  106 ? 3.4749 3.3820 3.2821 -0.1124 0.3674  0.6444  104  MET G O   
18592 C  CB  . MET G  106 ? 3.6216 3.3778 3.3048 -0.0578 0.2876  0.6382  104  MET G CB  
18593 C  CG  . MET G  106 ? 3.6562 3.3302 3.3434 -0.0445 0.2401  0.6339  104  MET G CG  
18594 S  SD  . MET G  106 ? 3.6830 3.3612 3.3412 0.0007  0.2056  0.5653  104  MET G SD  
18595 C  CE  . MET G  106 ? 3.3780 3.1016 3.1082 -0.0102 0.2114  0.5038  104  MET G CE  
18596 N  N   . PHE G  107 ? 3.4377 3.3318 3.1215 -0.1086 0.4061  0.7290  105  PHE G N   
18597 C  CA  . PHE G  107 ? 3.5500 3.5353 3.2461 -0.1131 0.4592  0.7310  105  PHE G CA  
18598 C  C   . PHE G  107 ? 3.6753 3.6902 3.2608 -0.0794 0.4873  0.7285  105  PHE G C   
18599 O  O   . PHE G  107 ? 3.6260 3.5975 3.1226 -0.0672 0.4745  0.7533  105  PHE G O   
18600 C  CB  . PHE G  107 ? 3.6485 3.6596 3.4035 -0.1604 0.4948  0.7927  105  PHE G CB  
18601 C  CG  . PHE G  107 ? 3.5035 3.5274 3.3835 -0.1961 0.4804  0.7791  105  PHE G CG  
18602 C  CD1 . PHE G  107 ? 3.3341 3.2771 3.2580 -0.2150 0.4320  0.7720  105  PHE G CD1 
18603 C  CD2 . PHE G  107 ? 3.4734 3.5928 3.4278 -0.2093 0.5144  0.7713  105  PHE G CD2 
18604 C  CE1 . PHE G  107 ? 3.2521 3.2072 3.2829 -0.2500 0.4160  0.7539  105  PHE G CE1 
18605 C  CE2 . PHE G  107 ? 3.3870 3.5257 3.4546 -0.2438 0.4957  0.7582  105  PHE G CE2 
18606 C  CZ  . PHE G  107 ? 3.3244 3.3799 3.4260 -0.2661 0.4458  0.7479  105  PHE G CZ  
18607 N  N   . PHE G  108 ? 3.7743 3.8632 3.3661 -0.0632 0.5240  0.6968  106  PHE G N   
18608 C  CA  . PHE G  108 ? 3.7217 3.8408 3.2128 -0.0305 0.5545  0.6810  106  PHE G CA  
18609 C  C   . PHE G  108 ? 3.5270 3.7349 3.0432 -0.0339 0.6213  0.6925  106  PHE G C   
18610 O  O   . PHE G  108 ? 3.5433 3.7981 3.1666 -0.0567 0.6375  0.7021  106  PHE G O   
18611 C  CB  . PHE G  108 ? 3.6034 3.7085 3.0673 0.0068  0.5256  0.6099  106  PHE G CB  
18612 C  CG  . PHE G  108 ? 3.5396 3.5709 2.9818 0.0142  0.4641  0.5943  106  PHE G CG  
18613 C  CD1 . PHE G  108 ? 3.7264 3.7228 3.0658 0.0310  0.4452  0.6012  106  PHE G CD1 
18614 C  CD2 . PHE G  108 ? 3.3157 3.3187 2.8404 0.0058  0.4252  0.5710  106  PHE G CD2 
18615 C  CE1 . PHE G  108 ? 3.7172 3.6562 3.0480 0.0408  0.3893  0.5874  106  PHE G CE1 
18616 C  CE2 . PHE G  108 ? 3.3163 3.2583 2.8263 0.0160  0.3739  0.5544  106  PHE G CE2 
18617 C  CZ  . PHE G  108 ? 3.5114 3.4236 2.9301 0.0343  0.3563  0.5636  106  PHE G CZ  
18618 N  N   . GLN G  109 ? 3.0897 3.3248 2.5071 -0.0100 0.6599  0.6887  107  GLN G N   
18619 C  CA  . GLN G  109 ? 2.8683 3.1902 2.2968 -0.0042 0.7299  0.6935  107  GLN G CA  
18620 C  C   . GLN G  109 ? 2.9083 3.2536 2.3192 0.0398  0.7413  0.6227  107  GLN G C   
18621 O  O   . GLN G  109 ? 3.0616 3.3630 2.3773 0.0666  0.7193  0.5842  107  GLN G O   
18622 C  CB  . GLN G  109 ? 2.8771 3.2155 2.2003 -0.0100 0.7751  0.7428  107  GLN G CB  
18623 C  CG  . GLN G  109 ? 2.9174 3.2393 2.2646 -0.0563 0.7768  0.8237  107  GLN G CG  
18624 C  CD  . GLN G  109 ? 2.9913 3.3284 2.2215 -0.0613 0.8214  0.8775  107  GLN G CD  
18625 O  OE1 . GLN G  109 ? 3.0680 3.4229 2.1863 -0.0287 0.8450  0.8488  107  GLN G OE1 
18626 N  NE2 . GLN G  109 ? 3.0180 3.3455 2.2698 -0.1038 0.8331  0.9562  107  GLN G NE2 
18627 N  N   . THR G  110 ? 2.8864 3.3011 2.3928 0.0468  0.7747  0.6070  108  THR G N   
18628 C  CA  . THR G  110 ? 2.8593 3.2915 2.3609 0.0906  0.7880  0.5437  108  THR G CA  
18629 C  C   . THR G  110 ? 2.8729 3.3331 2.2724 0.1195  0.8459  0.5286  108  THR G C   
18630 O  O   . THR G  110 ? 2.8418 3.2855 2.1977 0.1574  0.8491  0.4699  108  THR G O   
18631 C  CB  . THR G  110 ? 2.8241 3.3247 2.4643 0.0933  0.8034  0.5362  108  THR G CB  
18632 O  OG1 . THR G  110 ? 2.8614 3.3482 2.5941 0.0566  0.7568  0.5597  108  THR G OG1 
18633 C  CG2 . THR G  110 ? 2.6818 3.1725 2.3294 0.1375  0.7949  0.4720  108  THR G CG2 
18634 N  N   . SER G  111 ? 2.8361 3.3352 2.1937 0.1012  0.8926  0.5795  109  SER G N   
18635 C  CA  . SER G  111 ? 2.8577 3.3879 2.1074 0.1278  0.9521  0.5647  109  SER G CA  
18636 C  C   . SER G  111 ? 2.8589 3.3148 1.9605 0.1468  0.9184  0.5271  109  SER G C   
18637 O  O   . SER G  111 ? 2.8157 3.2827 1.8248 0.1776  0.9559  0.4865  109  SER G O   
18638 C  CB  . SER G  111 ? 2.8426 3.4306 2.0747 0.0982  1.0077  0.6359  109  SER G CB  
18639 O  OG  . SER G  111 ? 2.6362 3.2995 2.0164 0.0752  1.0363  0.6707  109  SER G OG  
18640 N  N   . GLU G  112 ? 2.8763 3.2593 1.9568 0.1298  0.8480  0.5363  110  GLU G N   
18641 C  CA  . GLU G  112 ? 2.8661 3.1851 1.8236 0.1455  0.8061  0.5003  110  GLU G CA  
18642 C  C   . GLU G  112 ? 2.7595 3.0304 1.7547 0.1642  0.7553  0.4359  110  GLU G C   
18643 O  O   . GLU G  112 ? 2.7873 3.0173 1.6912 0.1816  0.7300  0.3899  110  GLU G O   
18644 C  CB  . GLU G  112 ? 2.8645 3.1384 1.7676 0.1179  0.7616  0.5571  110  GLU G CB  
18645 C  CG  . GLU G  112 ? 3.1412 3.4534 2.0114 0.0928  0.8074  0.6338  110  GLU G CG  
18646 C  CD  . GLU G  112 ? 3.1485 3.4065 1.9665 0.0691  0.7607  0.6945  110  GLU G CD  
18647 O  OE1 . GLU G  112 ? 2.9255 3.1221 1.7282 0.0766  0.6933  0.6719  110  GLU G OE1 
18648 O  OE2 . GLU G  112 ? 3.1515 3.4294 1.9478 0.0437  0.7926  0.7672  110  GLU G OE2 
18649 N  N   . LEU G  113 ? 2.7793 3.0566 1.9048 0.1583  0.7392  0.4327  111  LEU G N   
18650 C  CA  . LEU G  113 ? 2.7719 3.0073 1.9341 0.1745  0.6957  0.3772  111  LEU G CA  
18651 C  C   . LEU G  113 ? 2.7354 2.9837 1.8831 0.2112  0.7318  0.3178  111  LEU G C   
18652 O  O   . LEU G  113 ? 2.7555 2.9556 1.8462 0.2283  0.7070  0.2652  111  LEU G O   
18653 C  CB  . LEU G  113 ? 2.7717 3.0131 2.0674 0.1569  0.6687  0.3938  111  LEU G CB  
18654 C  CG  . LEU G  113 ? 2.7198 2.9193 2.0310 0.1262  0.6160  0.4308  111  LEU G CG  
18655 C  CD1 . LEU G  113 ? 2.6661 2.8754 2.1040 0.1086  0.5942  0.4393  111  LEU G CD1 
18656 C  CD2 . LEU G  113 ? 2.7182 2.8537 1.9576 0.1354  0.5635  0.3990  111  LEU G CD2 
18657 N  N   . ARG G  114 ? 2.8499 3.1630 2.0539 0.2240  0.7911  0.3250  112  ARG G N   
18658 C  CA  . ARG G  114 ? 3.0238 3.3488 2.2243 0.2643  0.8312  0.2705  112  ARG G CA  
18659 C  C   . ARG G  114 ? 3.4361 3.7525 2.4974 0.2834  0.8679  0.2393  112  ARG G C   
18660 O  O   . ARG G  114 ? 3.6920 4.0253 2.7435 0.3185  0.9165  0.1968  112  ARG G O   
18661 C  CB  . ARG G  114 ? 2.8964 3.3028 2.2148 0.2753  0.8818  0.2906  112  ARG G CB  
18662 C  CG  . ARG G  114 ? 2.7569 3.1718 2.2096 0.2629  0.8425  0.3060  112  ARG G CG  
18663 C  CD  . ARG G  114 ? 2.7281 3.2282 2.2997 0.2802  0.8874  0.3178  112  ARG G CD  
18664 N  NE  . ARG G  114 ? 2.8941 3.4730 2.5044 0.2537  0.9274  0.3747  112  ARG G NE  
18665 C  CZ  . ARG G  114 ? 3.1475 3.8206 2.8650 0.2623  0.9727  0.3947  112  ARG G CZ  
18666 N  NH1 . ARG G  114 ? 3.0741 3.7720 2.8689 0.3015  0.9816  0.3632  112  ARG G NH1 
18667 N  NH2 . ARG G  114 ? 3.2950 4.0393 3.0468 0.2314  1.0090  0.4491  112  ARG G NH2 
18668 N  N   . GLU G  115 ? 3.5024 3.7924 2.4546 0.2630  0.8449  0.2585  113  GLU G N   
18669 C  CA  . GLU G  115 ? 3.4095 3.6847 2.2133 0.2780  0.8662  0.2239  113  GLU G CA  
18670 C  C   . GLU G  115 ? 3.5475 3.7470 2.2747 0.2781  0.8031  0.1753  113  GLU G C   
18671 O  O   . GLU G  115 ? 3.6942 3.8695 2.3272 0.2987  0.8159  0.1156  113  GLU G O   
18672 C  CB  . GLU G  115 ? 3.1461 3.4571 1.8669 0.2559  0.8899  0.2851  113  GLU G CB  
18673 C  CG  . GLU G  115 ? 3.2656 3.5864 1.8333 0.2741  0.9325  0.2541  113  GLU G CG  
18674 C  CD  . GLU G  115 ? 3.6417 3.9972 2.1220 0.2501  0.9534  0.3238  113  GLU G CD  
18675 O  OE1 . GLU G  115 ? 3.5526 3.9118 2.0938 0.2185  0.9280  0.3945  113  GLU G OE1 
18676 O  OE2 . GLU G  115 ? 4.0823 4.4582 2.4307 0.2623  0.9955  0.3082  113  GLU G OE2 
18677 N  N   . ALA G  116 ? 3.3839 3.5477 2.1537 0.2552  0.7363  0.1967  114  ALA G N   
18678 C  CA  . ALA G  116 ? 3.3954 3.4973 2.1195 0.2542  0.6757  0.1505  114  ALA G CA  
18679 C  C   . ALA G  116 ? 3.3672 3.4376 2.1616 0.2728  0.6706  0.0924  114  ALA G C   
18680 O  O   . ALA G  116 ? 3.4188 3.4443 2.1547 0.2818  0.6520  0.0328  114  ALA G O   
18681 C  CB  . ALA G  116 ? 3.2526 3.3333 2.0057 0.2271  0.6110  0.1939  114  ALA G CB  
18682 N  N   . VAL G  117 ? 3.4081 3.5010 2.3272 0.2770  0.6852  0.1105  115  VAL G N   
18683 C  CA  . VAL G  117 ? 3.4528 3.5188 2.4444 0.2966  0.6835  0.0665  115  VAL G CA  
18684 C  C   . VAL G  117 ? 3.4775 3.5937 2.5362 0.3232  0.7473  0.0708  115  VAL G C   
18685 O  O   . VAL G  117 ? 3.4996 3.6614 2.6624 0.3158  0.7531  0.1149  115  VAL G O   
18686 C  CB  . VAL G  117 ? 3.2559 3.3019 2.3402 0.2781  0.6290  0.0838  115  VAL G CB  
18687 C  CG1 . VAL G  117 ? 3.1426 3.1558 2.2880 0.2970  0.6252  0.0423  115  VAL G CG1 
18688 C  CG2 . VAL G  117 ? 3.1863 3.1965 2.2162 0.2539  0.5696  0.0863  115  VAL G CG2 
18689 N  N   . PRO G  118 ? 3.4399 3.5523 2.4466 0.3549  0.7955  0.0244  116  PRO G N   
18690 C  CA  . PRO G  118 ? 3.3800 3.5508 2.4579 0.3853  0.8608  0.0306  116  PRO G CA  
18691 C  C   . PRO G  118 ? 3.2852 3.4577 2.4978 0.4000  0.8498  0.0332  116  PRO G C   
18692 O  O   . PRO G  118 ? 3.1032 3.3436 2.4180 0.3987  0.8672  0.0783  116  PRO G O   
18693 C  CB  . PRO G  118 ? 3.5337 3.6798 2.5150 0.4192  0.9070  -0.0338 116  PRO G CB  
18694 C  CG  . PRO G  118 ? 3.5909 3.6909 2.4320 0.3963  0.8715  -0.0551 116  PRO G CG  
18695 C  CD  . PRO G  118 ? 3.4508 3.5124 2.3285 0.3638  0.7948  -0.0352 116  PRO G CD  
18696 N  N   . GLU G  119 ? 3.5010 3.6020 2.7167 0.4117  0.8195  -0.0119 117  GLU G N   
18697 C  CA  . GLU G  119 ? 3.5062 3.6048 2.8394 0.4288  0.8095  -0.0075 117  GLU G CA  
18698 C  C   . GLU G  119 ? 3.2605 3.3396 2.6393 0.3940  0.7436  0.0206  117  GLU G C   
18699 O  O   . GLU G  119 ? 3.1312 3.1555 2.4453 0.3709  0.7007  0.0025  117  GLU G O   
18700 C  CB  . GLU G  119 ? 3.6740 3.7019 2.9907 0.4641  0.8213  -0.0693 117  GLU G CB  
18701 C  CG  . GLU G  119 ? 3.6425 3.6679 3.0763 0.4904  0.8190  -0.0614 117  GLU G CG  
18702 C  CD  . GLU G  119 ? 3.6703 3.6230 3.0893 0.5313  0.8422  -0.1196 117  GLU G CD  
18703 O  OE1 . GLU G  119 ? 3.5706 3.4750 2.8862 0.5368  0.8603  -0.1725 117  GLU G OE1 
18704 O  OE2 . GLU G  119 ? 3.7680 3.7092 3.2774 0.5577  0.8407  -0.1125 117  GLU G OE2 
18705 N  N   . PRO G  120 ? 3.1586 3.2851 2.6476 0.3897  0.7334  0.0622  118  PRO G N   
18706 C  CA  . PRO G  120 ? 3.1718 3.2798 2.6992 0.3582  0.6733  0.0840  118  PRO G CA  
18707 C  C   . PRO G  120 ? 3.4075 3.4385 2.9216 0.3618  0.6386  0.0474  118  PRO G C   
18708 O  O   . PRO G  120 ? 3.4299 3.4377 2.9482 0.3339  0.5904  0.0561  118  PRO G O   
18709 C  CB  . PRO G  120 ? 3.0075 3.1851 2.6545 0.3604  0.6770  0.1262  118  PRO G CB  
18710 C  CG  . PRO G  120 ? 3.0174 3.2658 2.6831 0.3787  0.7362  0.1409  118  PRO G CG  
18711 C  CD  . PRO G  120 ? 3.1695 3.3766 2.7531 0.4116  0.7753  0.0911  118  PRO G CD  
18712 N  N   . VAL G  121 ? 3.3744 3.3636 2.8753 0.3950  0.6636  0.0068  119  VAL G N   
18713 C  CA  . VAL G  121 ? 3.1987 3.1095 2.6896 0.3943  0.6331  -0.0256 119  VAL G CA  
18714 C  C   . VAL G  121 ? 3.1388 2.9965 2.5294 0.3692  0.6079  -0.0607 119  VAL G C   
18715 O  O   . VAL G  121 ? 3.0870 2.8972 2.4734 0.3492  0.5677  -0.0738 119  VAL G O   
18716 C  CB  . VAL G  121 ? 3.0827 2.9570 2.5998 0.4384  0.6676  -0.0556 119  VAL G CB  
18717 C  CG1 . VAL G  121 ? 3.1943 2.9944 2.7301 0.4342  0.6342  -0.0707 119  VAL G CG1 
18718 C  CG2 . VAL G  121 ? 2.9495 2.8964 2.5625 0.4696  0.7000  -0.0202 119  VAL G CG2 
18719 N  N   . LEU G  122 ? 3.0841 2.9554 2.3934 0.3688  0.6302  -0.0745 120  LEU G N   
18720 C  CA  . LEU G  122 ? 3.1062 2.9379 2.3173 0.3454  0.6019  -0.1055 120  LEU G CA  
18721 C  C   . LEU G  122 ? 3.0632 2.9085 2.2811 0.3084  0.5493  -0.0731 120  LEU G C   
18722 O  O   . LEU G  122 ? 3.0878 2.8977 2.2533 0.2881  0.5125  -0.0976 120  LEU G O   
18723 C  CB  . LEU G  122 ? 3.2407 3.0944 2.3583 0.3540  0.6377  -0.1193 120  LEU G CB  
18724 C  CG  . LEU G  122 ? 3.3513 3.1962 2.4522 0.3945  0.6975  -0.1574 120  LEU G CG  
18725 C  CD1 . LEU G  122 ? 3.3174 3.1962 2.3183 0.3991  0.7341  -0.1648 120  LEU G CD1 
18726 C  CD2 . LEU G  122 ? 3.5263 3.2833 2.6037 0.4052  0.6893  -0.2213 120  LEU G CD2 
18727 N  N   . LEU G  123 ? 3.0547 2.9512 2.3397 0.2995  0.5442  -0.0211 121  LEU G N   
18728 C  CA  . LEU G  123 ? 3.1448 3.0505 2.4393 0.2685  0.4980  0.0077  121  LEU G CA  
18729 C  C   . LEU G  123 ? 3.1569 3.0256 2.4921 0.2570  0.4589  -0.0067 121  LEU G C   
18730 O  O   . LEU G  123 ? 2.9036 2.7679 2.3048 0.2677  0.4648  -0.0037 121  LEU G O   
18731 C  CB  . LEU G  123 ? 3.1414 3.1047 2.4997 0.2609  0.5054  0.0619  121  LEU G CB  
18732 C  CG  . LEU G  123 ? 3.1732 3.1507 2.5252 0.2329  0.4728  0.0979  121  LEU G CG  
18733 C  CD1 . LEU G  123 ? 3.2084 3.1655 2.6064 0.2161  0.4255  0.0980  121  LEU G CD1 
18734 C  CD2 . LEU G  123 ? 3.1520 3.1155 2.4030 0.2267  0.4659  0.0906  121  LEU G CD2 
18735 N  N   . SER G  124 ? 3.2666 3.1138 2.5635 0.2354  0.4190  -0.0193 122  SER G N   
18736 C  CA  . SER G  124 ? 3.1041 2.9244 2.4371 0.2205  0.3836  -0.0318 122  SER G CA  
18737 C  C   . SER G  124 ? 3.1217 2.9682 2.4907 0.2007  0.3489  -0.0001 122  SER G C   
18738 O  O   . SER G  124 ? 3.1564 3.0093 2.5894 0.1961  0.3390  0.0137  122  SER G O   
18739 C  CB  . SER G  124 ? 3.0579 2.8351 2.3314 0.2110  0.3652  -0.0789 122  SER G CB  
18740 O  OG  . SER G  124 ? 3.1140 2.9060 2.3222 0.1998  0.3441  -0.0790 122  SER G OG  
18741 N  N   . ARG G  125 ? 3.0989 2.9588 2.4259 0.1906  0.3299  0.0120  123  ARG G N   
18742 C  CA  . ARG G  125 ? 2.9027 2.7792 2.2633 0.1759  0.2971  0.0388  123  ARG G CA  
18743 C  C   . ARG G  125 ? 2.9655 2.8644 2.3007 0.1749  0.3022  0.0762  123  ARG G C   
18744 O  O   . ARG G  125 ? 3.2077 3.1060 2.4704 0.1783  0.3079  0.0741  123  ARG G O   
18745 C  CB  . ARG G  125 ? 2.7699 2.6328 2.1154 0.1634  0.2569  0.0155  123  ARG G CB  
18746 C  CG  . ARG G  125 ? 2.7568 2.6357 2.1394 0.1542  0.2244  0.0391  123  ARG G CG  
18747 C  CD  . ARG G  125 ? 2.8502 2.7272 2.2329 0.1448  0.1873  0.0148  123  ARG G CD  
18748 N  NE  . ARG G  125 ? 2.9691 2.8616 2.3968 0.1418  0.1603  0.0337  123  ARG G NE  
18749 C  CZ  . ARG G  125 ? 2.9498 2.8482 2.4391 0.1369  0.1550  0.0291  123  ARG G CZ  
18750 N  NH1 . ARG G  125 ? 3.0066 2.8972 2.5188 0.1325  0.1725  0.0123  123  ARG G NH1 
18751 N  NH2 . ARG G  125 ? 2.8412 2.7511 2.3667 0.1378  0.1331  0.0416  123  ARG G NH2 
18752 N  N   . ALA G  126 ? 2.7953 2.7121 2.1868 0.1681  0.2996  0.1106  124  ALA G N   
18753 C  CA  . ALA G  126 ? 2.8517 2.7841 2.2313 0.1624  0.3055  0.1524  124  ALA G CA  
18754 C  C   . ALA G  126 ? 2.7817 2.7084 2.2102 0.1497  0.2723  0.1729  124  ALA G C   
18755 O  O   . ALA G  126 ? 2.7385 2.6748 2.2322 0.1427  0.2745  0.1832  124  ALA G O   
18756 C  CB  . ALA G  126 ? 2.8864 2.8484 2.2926 0.1661  0.3483  0.1745  124  ALA G CB  
18757 N  N   . GLU G  127 ? 2.6478 2.5596 2.0449 0.1483  0.2405  0.1774  125  GLU G N   
18758 C  CA  . GLU G  127 ? 2.6285 2.5285 2.0700 0.1421  0.2085  0.1916  125  GLU G CA  
18759 C  C   . GLU G  127 ? 2.6197 2.5104 2.0417 0.1378  0.2049  0.2384  125  GLU G C   
18760 O  O   . GLU G  127 ? 2.6864 2.5768 2.0395 0.1427  0.2047  0.2532  125  GLU G O   
18761 C  CB  . GLU G  127 ? 2.6820 2.5750 2.1202 0.1472  0.1726  0.1627  125  GLU G CB  
18762 C  CG  . GLU G  127 ? 2.7506 2.6455 2.1154 0.1533  0.1610  0.1499  125  GLU G CG  
18763 C  CD  . GLU G  127 ? 2.6859 2.5851 2.0643 0.1544  0.1257  0.1182  125  GLU G CD  
18764 O  OE1 . GLU G  127 ? 2.6121 2.5128 2.0535 0.1538  0.1103  0.1139  125  GLU G OE1 
18765 O  OE2 . GLU G  127 ? 2.8238 2.7282 2.1511 0.1547  0.1142  0.0956  125  GLU G OE2 
18766 N  N   . LEU G  128 ? 2.6159 2.4963 2.0953 0.1270  0.2013  0.2618  126  LEU G N   
18767 C  CA  . LEU G  128 ? 2.6965 2.5581 2.1698 0.1188  0.1989  0.3108  126  LEU G CA  
18768 C  C   . LEU G  128 ? 2.8790 2.7087 2.3567 0.1279  0.1569  0.3169  126  LEU G C   
18769 O  O   . LEU G  128 ? 2.8863 2.7030 2.4206 0.1296  0.1369  0.2952  126  LEU G O   
18770 C  CB  . LEU G  128 ? 2.6258 2.4885 2.1652 0.0988  0.2156  0.3303  126  LEU G CB  
18771 C  CG  . LEU G  128 ? 2.7110 2.5453 2.2618 0.0830  0.2138  0.3820  126  LEU G CG  
18772 C  CD1 . LEU G  128 ? 3.0753 2.9221 2.5579 0.0816  0.2397  0.4232  126  LEU G CD1 
18773 C  CD2 . LEU G  128 ? 2.6885 2.5264 2.3160 0.0582  0.2248  0.3898  126  LEU G CD2 
18774 N  N   . ARG G  129 ? 3.1133 2.9330 2.5313 0.1360  0.1438  0.3471  127  ARG G N   
18775 C  CA  . ARG G  129 ? 3.0503 2.8460 2.4710 0.1511  0.1011  0.3564  127  ARG G CA  
18776 C  C   . ARG G  129 ? 2.9570 2.7128 2.3781 0.1469  0.0948  0.4163  127  ARG G C   
18777 O  O   . ARG G  129 ? 3.0703 2.8274 2.4454 0.1354  0.1193  0.4578  127  ARG G O   
18778 C  CB  . ARG G  129 ? 3.1040 2.9221 2.4552 0.1662  0.0802  0.3434  127  ARG G CB  
18779 C  CG  . ARG G  129 ? 2.9718 2.8208 2.3222 0.1669  0.0853  0.2850  127  ARG G CG  
18780 C  CD  . ARG G  129 ? 3.0456 2.9138 2.3477 0.1785  0.0521  0.2663  127  ARG G CD  
18781 N  NE  . ARG G  129 ? 3.0490 2.9386 2.3632 0.1748  0.0546  0.2105  127  ARG G NE  
18782 C  CZ  . ARG G  129 ? 3.1589 3.0698 2.4516 0.1785  0.0249  0.1818  127  ARG G CZ  
18783 N  NH1 . ARG G  129 ? 3.0918 3.0119 2.3484 0.1891  -0.0126 0.2036  127  ARG G NH1 
18784 N  NH2 . ARG G  129 ? 3.2947 3.2182 2.6044 0.1702  0.0308  0.1338  127  ARG G NH2 
18785 N  N   . LEU G  130 ? 2.7212 2.4397 2.1952 0.1568  0.0642  0.4215  128  LEU G N   
18786 C  CA  . LEU G  130 ? 2.7693 2.4355 2.2528 0.1535  0.0556  0.4787  128  LEU G CA  
18787 C  C   . LEU G  130 ? 2.9486 2.5928 2.4184 0.1827  0.0115  0.5001  128  LEU G C   
18788 O  O   . LEU G  130 ? 3.0065 2.6882 2.4390 0.2011  -0.0098 0.4797  128  LEU G O   
18789 C  CB  . LEU G  130 ? 2.7724 2.3995 2.3403 0.1381  0.0609  0.4703  128  LEU G CB  
18790 C  CG  . LEU G  130 ? 2.7297 2.3867 2.3306 0.1130  0.0938  0.4393  128  LEU G CG  
18791 C  CD1 . LEU G  130 ? 2.7903 2.4043 2.4671 0.0956  0.0907  0.4343  128  LEU G CD1 
18792 C  CD2 . LEU G  130 ? 2.7245 2.4131 2.2814 0.0932  0.1320  0.4710  128  LEU G CD2 
18793 N  N   . LEU G  131 ? 2.9890 2.5723 2.4923 0.1872  -0.0045 0.5418  129  LEU G N   
18794 C  CA  . LEU G  131 ? 2.9436 2.5038 2.4468 0.2207  -0.0490 0.5654  129  LEU G CA  
18795 C  C   . LEU G  131 ? 2.9721 2.4602 2.5576 0.2297  -0.0636 0.5732  129  LEU G C   
18796 O  O   . LEU G  131 ? 2.9994 2.4296 2.5987 0.2090  -0.0490 0.6147  129  LEU G O   
18797 C  CB  . LEU G  131 ? 3.0491 2.6053 2.4649 0.2239  -0.0571 0.6343  129  LEU G CB  
18798 C  CG  . LEU G  131 ? 3.1880 2.7384 2.5869 0.2616  -0.1087 0.6637  129  LEU G CG  
18799 C  CD1 . LEU G  131 ? 3.3746 2.8413 2.8134 0.2736  -0.1266 0.7236  129  LEU G CD1 
18800 C  CD2 . LEU G  131 ? 3.0384 2.6314 2.4888 0.2881  -0.1384 0.6002  129  LEU G CD2 
18801 N  N   . ARG G  132 ? 2.9807 2.4725 2.6222 0.2599  -0.0912 0.5325  130  ARG G N   
18802 C  CA  . ARG G  132 ? 3.0062 2.4309 2.7282 0.2754  -0.1046 0.5257  130  ARG G CA  
18803 C  C   . ARG G  132 ? 3.1449 2.5199 2.8687 0.3096  -0.1416 0.5834  130  ARG G C   
18804 O  O   . ARG G  132 ? 3.3092 2.7251 2.9906 0.3340  -0.1694 0.6056  130  ARG G O   
18805 C  CB  . ARG G  132 ? 2.9934 2.4535 2.7764 0.2936  -0.1100 0.4504  130  ARG G CB  
18806 C  CG  . ARG G  132 ? 3.1137 2.5193 2.9757 0.3268  -0.1311 0.4353  130  ARG G CG  
18807 C  CD  . ARG G  132 ? 2.9977 2.4632 2.9062 0.3503  -0.1364 0.3670  130  ARG G CD  
18808 N  NE  . ARG G  132 ? 3.2445 2.6682 3.2291 0.3896  -0.1545 0.3491  130  ARG G NE  
18809 C  CZ  . ARG G  132 ? 3.3021 2.6998 3.3412 0.3896  -0.1384 0.2951  130  ARG G CZ  
18810 N  NH1 . ARG G  132 ? 3.2800 2.6386 3.3864 0.4306  -0.1531 0.2775  130  ARG G NH1 
18811 N  NH2 . ARG G  132 ? 3.2702 2.6826 3.2955 0.3508  -0.1081 0.2581  130  ARG G NH2 
18812 N  N   . LEU G  133 ? 3.2077 2.4913 2.9813 0.3109  -0.1442 0.6083  131  LEU G N   
18813 C  CA  . LEU G  133 ? 3.4110 2.6313 3.2001 0.3474  -0.1796 0.6646  131  LEU G CA  
18814 C  C   . LEU G  133 ? 3.4316 2.6016 3.3167 0.3837  -0.1973 0.6251  131  LEU G C   
18815 O  O   . LEU G  133 ? 3.3639 2.5485 3.2766 0.4330  -0.2323 0.6281  131  LEU G O   
18816 C  CB  . LEU G  133 ? 3.6322 2.7712 3.3919 0.3199  -0.1682 0.7445  131  LEU G CB  
18817 C  CG  . LEU G  133 ? 3.6841 2.8585 3.3406 0.2988  -0.1585 0.8105  131  LEU G CG  
18818 C  CD1 . LEU G  133 ? 3.6212 2.8622 3.2374 0.2543  -0.1146 0.7778  131  LEU G CD1 
18819 C  CD2 . LEU G  133 ? 3.7277 2.8097 3.3692 0.2857  -0.1576 0.9012  131  LEU G CD2 
18820 N  N   . LYS G  134 ? 3.5517 2.6664 3.4894 0.3615  -0.1743 0.5858  132  LYS G N   
18821 C  CA  . LYS G  134 ? 3.6451 2.7000 3.6689 0.3951  -0.1864 0.5446  132  LYS G CA  
18822 C  C   . LYS G  134 ? 3.4648 2.6041 3.5224 0.4322  -0.1957 0.4780  132  LYS G C   
18823 O  O   . LYS G  134 ? 3.3842 2.6097 3.4178 0.4119  -0.1775 0.4328  132  LYS G O   
18824 C  CB  . LYS G  134 ? 3.6282 2.6213 3.6884 0.3559  -0.1587 0.5041  132  LYS G CB  
18825 C  CG  . LYS G  134 ? 3.6676 2.5461 3.8020 0.3797  -0.1705 0.4919  132  LYS G CG  
18826 C  CD  . LYS G  134 ? 3.5970 2.4102 3.7528 0.3279  -0.1464 0.4634  132  LYS G CD  
18827 C  CE  . LYS G  134 ? 3.7299 2.4083 3.9517 0.3449  -0.1586 0.4594  132  LYS G CE  
18828 N  NZ  . LYS G  134 ? 3.7278 2.3416 3.9695 0.2876  -0.1395 0.4321  132  LYS G NZ  
18829 N  N   . LEU G  135 ? 3.4282 2.5426 3.5473 0.4874  -0.2228 0.4739  133  LEU G N   
18830 C  CA  . LEU G  135 ? 3.2652 2.4662 3.4270 0.5261  -0.2325 0.4187  133  LEU G CA  
18831 C  C   . LEU G  135 ? 3.1965 2.3628 3.4424 0.5531  -0.2215 0.3498  133  LEU G C   
18832 O  O   . LEU G  135 ? 3.0501 2.2973 3.3324 0.5759  -0.2176 0.2937  133  LEU G O   
18833 C  CB  . LEU G  135 ? 3.3258 2.5629 3.4931 0.5755  -0.2762 0.4680  133  LEU G CB  
18834 C  CG  . LEU G  135 ? 3.3568 2.5008 3.5671 0.6227  -0.3084 0.5254  133  LEU G CG  
18835 C  CD1 . LEU G  135 ? 3.3027 2.4493 3.6173 0.6839  -0.3201 0.4773  133  LEU G CD1 
18836 C  CD2 . LEU G  135 ? 3.2876 2.4603 3.4417 0.6381  -0.3475 0.6083  133  LEU G CD2 
18837 N  N   . LYS G  136 ? 3.4277 2.4774 3.7040 0.5491  -0.2145 0.3502  134  LYS G N   
18838 C  CA  . LYS G  136 ? 3.3924 2.3955 3.7435 0.5781  -0.2045 0.2824  134  LYS G CA  
18839 C  C   . LYS G  136 ? 3.2920 2.2883 3.6283 0.5283  -0.1690 0.2172  134  LYS G C   
18840 O  O   . LYS G  136 ? 3.2072 2.1937 3.4906 0.4718  -0.1557 0.2383  134  LYS G O   
18841 C  CB  . LYS G  136 ? 3.3716 2.2383 3.7714 0.6102  -0.2231 0.3180  134  LYS G CB  
18842 C  CG  . LYS G  136 ? 3.2721 2.1416 3.6954 0.6685  -0.2628 0.3836  134  LYS G CG  
18843 C  CD  . LYS G  136 ? 3.3394 2.0608 3.8077 0.6978  -0.2806 0.4275  134  LYS G CD  
18844 C  CE  . LYS G  136 ? 3.4642 2.1941 3.9523 0.7579  -0.3245 0.5011  134  LYS G CE  
18845 N  NZ  . LYS G  136 ? 3.6563 2.2338 4.1902 0.7908  -0.3437 0.5523  134  LYS G NZ  
18846 N  N   . VAL G  137 ? 3.2729 2.2800 3.6574 0.5516  -0.1539 0.1378  135  VAL G N   
18847 C  CA  . VAL G  137 ? 3.2919 2.3017 3.6632 0.5122  -0.1236 0.0670  135  VAL G CA  
18848 C  C   . VAL G  137 ? 3.4057 2.5161 3.7115 0.4633  -0.1079 0.0687  135  VAL G C   
18849 O  O   . VAL G  137 ? 3.4172 2.6050 3.6958 0.4679  -0.1172 0.1064  135  VAL G O   
18850 C  CB  . VAL G  137 ? 3.3713 2.2501 3.7483 0.4804  -0.1211 0.0660  135  VAL G CB  
18851 C  CG1 . VAL G  137 ? 3.3693 2.2359 3.7562 0.4644  -0.0981 -0.0253 135  VAL G CG1 
18852 C  CG2 . VAL G  137 ? 3.5552 2.3173 3.9856 0.5243  -0.1441 0.1017  135  VAL G CG2 
18853 N  N   . GLU G  138 ? 3.5417 2.6508 3.8224 0.4174  -0.0859 0.0266  136  GLU G N   
18854 C  CA  . GLU G  138 ? 3.4246 2.6241 3.6507 0.3751  -0.0693 0.0224  136  GLU G CA  
18855 C  C   . GLU G  138 ? 3.3807 2.5349 3.5814 0.3181  -0.0594 0.0222  136  GLU G C   
18856 O  O   . GLU G  138 ? 3.4768 2.5404 3.7046 0.3095  -0.0621 0.0016  136  GLU G O   
18857 C  CB  . GLU G  138 ? 3.2942 2.5820 3.5247 0.3872  -0.0504 -0.0446 136  GLU G CB  
18858 C  CG  . GLU G  138 ? 3.3537 2.6068 3.5950 0.3762  -0.0338 -0.1154 136  GLU G CG  
18859 C  CD  . GLU G  138 ? 3.2947 2.6219 3.5508 0.4032  -0.0145 -0.1795 136  GLU G CD  
18860 O  OE1 . GLU G  138 ? 3.2083 2.6150 3.4766 0.4292  -0.0144 -0.1683 136  GLU G OE1 
18861 O  OE2 . GLU G  138 ? 3.3409 2.6491 3.5955 0.3963  0.0009  -0.2417 136  GLU G OE2 
18862 N  N   . GLN G  139 ? 3.1299 2.3485 3.2828 0.2791  -0.0485 0.0432  137  GLN G N   
18863 C  CA  . GLN G  139 ? 3.2148 2.4124 3.3505 0.2246  -0.0394 0.0453  137  GLN G CA  
18864 C  C   . GLN G  139 ? 3.2084 2.5041 3.3049 0.1986  -0.0219 0.0267  137  GLN G C   
18865 O  O   . GLN G  139 ? 3.1365 2.5074 3.2118 0.2165  -0.0168 0.0283  137  GLN G O   
18866 C  CB  . GLN G  139 ? 3.2899 2.4362 3.4166 0.2000  -0.0459 0.1205  137  GLN G CB  
18867 C  CG  . GLN G  139 ? 3.5056 2.5295 3.6745 0.2051  -0.0607 0.1368  137  GLN G CG  
18868 C  CD  . GLN G  139 ? 3.5703 2.5563 3.7440 0.2444  -0.0783 0.1986  137  GLN G CD  
18869 O  OE1 . GLN G  139 ? 3.5977 2.6502 3.7532 0.2788  -0.0841 0.2104  137  GLN G OE1 
18870 N  NE2 . GLN G  139 ? 3.5212 2.3995 3.7198 0.2377  -0.0892 0.2405  137  GLN G NE2 
18871 N  N   . HIS G  140 ? 3.2178 2.5103 3.3087 0.1551  -0.0149 0.0094  138  HIS G N   
18872 C  CA  . HIS G  140 ? 2.9935 2.3700 3.0530 0.1298  -0.0006 -0.0081 138  HIS G CA  
18873 C  C   . HIS G  140 ? 2.8934 2.2822 2.9398 0.0895  0.0048  0.0427  138  HIS G C   
18874 O  O   . HIS G  140 ? 2.9933 2.3241 3.0633 0.0605  -0.0011 0.0603  138  HIS G O   
18875 C  CB  . HIS G  140 ? 3.0114 2.3883 3.0760 0.1157  0.0010  -0.0747 138  HIS G CB  
18876 C  CG  . HIS G  140 ? 2.8528 2.3182 2.8839 0.0995  0.0134  -0.0934 138  HIS G CG  
18877 N  ND1 . HIS G  140 ? 2.7739 2.3057 2.7839 0.1248  0.0251  -0.1080 138  HIS G ND1 
18878 C  CD2 . HIS G  140 ? 2.8220 2.3201 2.8410 0.0607  0.0145  -0.0969 138  HIS G CD2 
18879 C  CE1 . HIS G  140 ? 2.7305 2.3240 2.7128 0.1031  0.0340  -0.1173 138  HIS G CE1 
18880 N  NE2 . HIS G  140 ? 2.7721 2.3494 2.7596 0.0665  0.0265  -0.1106 138  HIS G NE2 
18881 N  N   . VAL G  141 ? 2.6187 2.0828 2.6319 0.0869  0.0177  0.0645  139  VAL G N   
18882 C  CA  . VAL G  141 ? 2.6357 2.1192 2.6350 0.0598  0.0279  0.1181  139  VAL G CA  
18883 C  C   . VAL G  141 ? 2.6426 2.1997 2.6292 0.0368  0.0415  0.1043  139  VAL G C   
18884 O  O   . VAL G  141 ? 2.8279 2.4370 2.7936 0.0525  0.0470  0.0757  139  VAL G O   
18885 C  CB  . VAL G  141 ? 2.6179 2.1161 2.5848 0.0836  0.0311  0.1635  139  VAL G CB  
18886 C  CG1 . VAL G  141 ? 2.6425 2.1708 2.5872 0.0580  0.0486  0.2123  139  VAL G CG1 
18887 C  CG2 . VAL G  141 ? 2.7769 2.2023 2.7589 0.1072  0.0134  0.1869  139  VAL G CG2 
18888 N  N   . GLU G  142 ? 2.5851 2.1485 2.5889 -0.0003 0.0470  0.1282  140  GLU G N   
18889 C  CA  . GLU G  142 ? 2.5694 2.2068 2.5687 -0.0196 0.0596  0.1280  140  GLU G CA  
18890 C  C   . GLU G  142 ? 2.5618 2.2265 2.5537 -0.0303 0.0795  0.1842  140  GLU G C   
18891 O  O   . GLU G  142 ? 2.5821 2.2048 2.5862 -0.0436 0.0814  0.2238  140  GLU G O   
18892 C  CB  . GLU G  142 ? 2.6644 2.3046 2.6993 -0.0552 0.0478  0.1011  140  GLU G CB  
18893 C  CG  . GLU G  142 ? 2.8027 2.4183 2.8363 -0.0471 0.0306  0.0398  140  GLU G CG  
18894 C  CD  . GLU G  142 ? 2.9569 2.5728 3.0192 -0.0861 0.0144  0.0114  140  GLU G CD  
18895 O  OE1 . GLU G  142 ? 2.9426 2.5919 3.0325 -0.1193 0.0160  0.0409  140  GLU G OE1 
18896 O  OE2 . GLU G  142 ? 3.0838 2.6705 3.1420 -0.0840 -0.0001 -0.0422 140  GLU G OE2 
18897 N  N   . LEU G  143 ? 2.4616 2.1946 2.4327 -0.0238 0.0965  0.1882  141  LEU G N   
18898 C  CA  . LEU G  143 ? 2.4206 2.1876 2.3779 -0.0274 0.1211  0.2335  141  LEU G CA  
18899 C  C   . LEU G  143 ? 2.4812 2.3103 2.4728 -0.0518 0.1332  0.2390  141  LEU G C   
18900 O  O   . LEU G  143 ? 2.7301 2.5941 2.7324 -0.0520 0.1247  0.2067  141  LEU G O   
18901 C  CB  . LEU G  143 ? 2.3553 2.1466 2.2597 0.0056  0.1325  0.2322  141  LEU G CB  
18902 C  CG  . LEU G  143 ? 2.3084 2.1296 2.1846 0.0073  0.1600  0.2720  141  LEU G CG  
18903 C  CD1 . LEU G  143 ? 2.3873 2.1656 2.2568 -0.0027 0.1620  0.3173  141  LEU G CD1 
18904 C  CD2 . LEU G  143 ? 2.2446 2.0849 2.0680 0.0374  0.1666  0.2580  141  LEU G CD2 
18905 N  N   . TYR G  144 ? 2.5724 2.4203 2.5824 -0.0715 0.1536  0.2826  142  TYR G N   
18906 C  CA  . TYR G  144 ? 2.6018 2.5171 2.6590 -0.0948 0.1658  0.2930  142  TYR G CA  
18907 C  C   . TYR G  144 ? 2.5854 2.5496 2.6268 -0.0848 0.2035  0.3305  142  TYR G C   
18908 O  O   . TYR G  144 ? 2.5652 2.5051 2.5548 -0.0666 0.2183  0.3504  142  TYR G O   
18909 C  CB  . TYR G  144 ? 2.8201 2.7187 2.9404 -0.1401 0.1535  0.3051  142  TYR G CB  
18910 C  CG  . TYR G  144 ? 2.9901 2.8484 3.1292 -0.1531 0.1171  0.2588  142  TYR G CG  
18911 C  CD1 . TYR G  144 ? 2.9442 2.8536 3.1129 -0.1666 0.1002  0.2275  142  TYR G CD1 
18912 C  CD2 . TYR G  144 ? 3.0542 2.8242 3.1796 -0.1498 0.0994  0.2458  142  TYR G CD2 
18913 C  CE1 . TYR G  144 ? 2.8492 2.7234 3.0244 -0.1790 0.0681  0.1809  142  TYR G CE1 
18914 C  CE2 . TYR G  144 ? 2.9434 2.6748 3.0829 -0.1591 0.0701  0.1971  142  TYR G CE2 
18915 C  CZ  . TYR G  144 ? 2.7713 2.5553 2.9312 -0.1751 0.0553  0.1631  142  TYR G CZ  
18916 O  OH  . TYR G  144 ? 2.7372 2.4846 2.9006 -0.1850 0.0271  0.1106  142  TYR G OH  
18917 N  N   . GLN G  145 ? 2.7276 2.7652 2.8142 -0.0956 0.2187  0.3386  143  GLN G N   
18918 C  CA  . GLN G  145 ? 2.7872 2.8807 2.8689 -0.0844 0.2594  0.3691  143  GLN G CA  
18919 C  C   . GLN G  145 ? 2.7682 2.9132 2.9247 -0.1217 0.2757  0.4043  143  GLN G C   
18920 O  O   . GLN G  145 ? 2.8317 2.9899 3.0517 -0.1534 0.2512  0.3956  143  GLN G O   
18921 C  CB  . GLN G  145 ? 2.7671 2.9105 2.8385 -0.0517 0.2684  0.3454  143  GLN G CB  
18922 C  CG  . GLN G  145 ? 2.8040 2.9948 2.8604 -0.0307 0.3131  0.3669  143  GLN G CG  
18923 C  CD  . GLN G  145 ? 2.8316 3.0667 2.8945 0.0001  0.3204  0.3450  143  GLN G CD  
18924 O  OE1 . GLN G  145 ? 2.9257 3.1480 2.9862 0.0084  0.2919  0.3156  143  GLN G OE1 
18925 N  NE2 . GLN G  145 ? 2.7521 3.0382 2.8231 0.0183  0.3607  0.3604  143  GLN G NE2 
18926 N  N   . LYS G  146 ? 2.6752 2.8532 2.8237 -0.1198 0.3177  0.4429  144  LYS G N   
18927 C  CA  . LYS G  146 ? 2.6745 2.9076 2.8963 -0.1573 0.3407  0.4827  144  LYS G CA  
18928 C  C   . LYS G  146 ? 2.6619 2.9968 2.9526 -0.1513 0.3531  0.4762  144  LYS G C   
18929 O  O   . LYS G  146 ? 2.5825 2.9579 2.8479 -0.1124 0.3808  0.4699  144  LYS G O   
18930 C  CB  . LYS G  146 ? 2.6841 2.9165 2.8647 -0.1570 0.3854  0.5293  144  LYS G CB  
18931 C  CG  . LYS G  146 ? 2.6413 2.9305 2.8979 -0.2001 0.4151  0.5773  144  LYS G CG  
18932 C  CD  . LYS G  146 ? 2.6241 2.9178 2.8251 -0.1960 0.4650  0.6245  144  LYS G CD  
18933 C  CE  . LYS G  146 ? 2.6106 2.9719 2.8920 -0.2405 0.5018  0.6755  144  LYS G CE  
18934 N  NZ  . LYS G  146 ? 2.6035 2.9879 2.8280 -0.2343 0.5595  0.7222  144  LYS G NZ  
18935 N  N   . TYR G  147 ? 2.7689 3.1444 3.1489 -0.1895 0.3310  0.4772  145  TYR G N   
18936 C  CA  . TYR G  147 ? 2.7578 3.2399 3.2191 -0.1878 0.3362  0.4769  145  TYR G CA  
18937 C  C   . TYR G  147 ? 2.8261 3.3700 3.3883 -0.2406 0.3456  0.5128  145  TYR G C   
18938 O  O   . TYR G  147 ? 2.8855 3.3827 3.4737 -0.2875 0.3175  0.5149  145  TYR G O   
18939 C  CB  . TYR G  147 ? 2.6677 3.1533 3.1406 -0.1798 0.2872  0.4341  145  TYR G CB  
18940 C  CG  . TYR G  147 ? 2.6591 3.1255 3.0613 -0.1252 0.2885  0.4061  145  TYR G CG  
18941 C  CD1 . TYR G  147 ? 2.5692 3.1087 2.9960 -0.0896 0.3091  0.4086  145  TYR G CD1 
18942 C  CD2 . TYR G  147 ? 2.8550 3.2299 3.1722 -0.1093 0.2699  0.3783  145  TYR G CD2 
18943 C  CE1 . TYR G  147 ? 2.6107 3.1232 2.9757 -0.0432 0.3106  0.3846  145  TYR G CE1 
18944 C  CE2 . TYR G  147 ? 2.8673 3.2256 3.1260 -0.0654 0.2717  0.3543  145  TYR G CE2 
18945 C  CZ  . TYR G  147 ? 2.7428 3.1652 3.0237 -0.0342 0.2919  0.3578  145  TYR G CZ  
18946 O  OH  . TYR G  147 ? 2.7343 3.1310 2.9598 0.0060  0.2938  0.3353  145  TYR G OH  
18947 N  N   . SER G  148 ? 2.7580 3.4064 3.3813 -0.2333 0.3863  0.5396  146  SER G N   
18948 C  CA  . SER G  148 ? 2.6247 3.3558 3.3590 -0.2829 0.4016  0.5768  146  SER G CA  
18949 C  C   . SER G  148 ? 2.7172 3.3919 3.4382 -0.3269 0.4227  0.6168  146  SER G C   
18950 O  O   . SER G  148 ? 2.7088 3.4245 3.5209 -0.3829 0.4243  0.6458  146  SER G O   
18951 C  CB  . SER G  148 ? 2.5200 3.2918 3.3444 -0.3205 0.3464  0.5561  146  SER G CB  
18952 O  OG  . SER G  148 ? 2.4900 3.3571 3.4343 -0.3693 0.3601  0.5908  146  SER G OG  
18953 N  N   . GLN G  149 ? 2.7754 3.3568 3.3863 -0.3040 0.4368  0.6210  147  GLN G N   
18954 C  CA  . GLN G  149 ? 2.7116 3.2243 3.2895 -0.3367 0.4543  0.6632  147  GLN G CA  
18955 C  C   . GLN G  149 ? 2.6541 3.0977 3.2780 -0.3937 0.4088  0.6626  147  GLN G C   
18956 O  O   . GLN G  149 ? 2.6763 3.0703 3.3017 -0.4319 0.4225  0.7061  147  GLN G O   
18957 C  CB  . GLN G  149 ? 2.8241 3.4203 3.4409 -0.3538 0.5191  0.7199  147  GLN G CB  
18958 C  CG  . GLN G  149 ? 2.8289 3.4839 3.3905 -0.2959 0.5705  0.7178  147  GLN G CG  
18959 C  CD  . GLN G  149 ? 2.9507 3.6862 3.5392 -0.3110 0.6406  0.7725  147  GLN G CD  
18960 O  OE1 . GLN G  149 ? 3.0032 3.7322 3.6296 -0.3653 0.6534  0.8208  147  GLN G OE1 
18961 N  NE2 . GLN G  149 ? 2.9658 3.7762 3.5355 -0.2632 0.6889  0.7650  147  GLN G NE2 
18962 N  N   . ASN G  150 ? 2.5973 3.0314 3.2543 -0.4000 0.3553  0.6140  148  ASN G N   
18963 C  CA  . ASN G  150 ? 2.6573 3.0217 3.3549 -0.4520 0.3094  0.6007  148  ASN G CA  
18964 C  C   . ASN G  150 ? 2.6190 2.9251 3.2734 -0.4282 0.2556  0.5360  148  ASN G C   
18965 O  O   . ASN G  150 ? 2.6656 2.8653 3.2917 -0.4426 0.2241  0.5164  148  ASN G O   
18966 C  CB  . ASN G  150 ? 2.7225 3.1770 3.5509 -0.5118 0.3034  0.6151  148  ASN G CB  
18967 C  CG  . ASN G  150 ? 2.8312 3.2110 3.7034 -0.5695 0.2525  0.5926  148  ASN G CG  
18968 O  OD1 . ASN G  150 ? 3.0083 3.2621 3.8266 -0.5757 0.2390  0.5905  148  ASN G OD1 
18969 N  ND2 . ASN G  150 ? 2.7496 3.2065 3.7212 -0.6106 0.2221  0.5738  148  ASN G ND2 
18970 N  N   . SER G  151 ? 2.4641 2.8383 3.1135 -0.3904 0.2471  0.5040  149  SER G N   
18971 C  CA  . SER G  151 ? 2.4653 2.7998 3.0737 -0.3685 0.2006  0.4460  149  SER G CA  
18972 C  C   . SER G  151 ? 2.4782 2.7480 2.9774 -0.3112 0.2103  0.4302  149  SER G C   
18973 O  O   . SER G  151 ? 2.4463 2.7366 2.9056 -0.2778 0.2506  0.4550  149  SER G O   
18974 C  CB  . SER G  151 ? 2.4343 2.8748 3.0942 -0.3597 0.1824  0.4247  149  SER G CB  
18975 O  OG  . SER G  151 ? 2.5659 2.9704 3.1719 -0.3347 0.1433  0.3736  149  SER G OG  
18976 N  N   . TRP G  152 ? 2.7329 2.9267 3.1850 -0.3013 0.1731  0.3858  150  TRP G N   
18977 C  CA  . TRP G  152 ? 2.8097 2.9442 3.1686 -0.2521 0.1762  0.3667  150  TRP G CA  
18978 C  C   . TRP G  152 ? 2.8162 2.9632 3.1511 -0.2281 0.1462  0.3161  150  TRP G C   
18979 O  O   . TRP G  152 ? 2.9051 3.0479 3.2682 -0.2533 0.1099  0.2840  150  TRP G O   
18980 C  CB  . TRP G  152 ? 2.9169 2.9391 3.2370 -0.2582 0.1658  0.3676  150  TRP G CB  
18981 C  CG  . TRP G  152 ? 3.0905 3.0904 3.4336 -0.2880 0.1909  0.4228  150  TRP G CG  
18982 C  CD1 . TRP G  152 ? 3.2203 3.1927 3.6277 -0.3416 0.1804  0.4401  150  TRP G CD1 
18983 C  CD2 . TRP G  152 ? 3.0881 3.0902 3.3862 -0.2686 0.2313  0.4695  150  TRP G CD2 
18984 N  NE1 . TRP G  152 ? 3.2779 3.2350 3.6854 -0.3571 0.2139  0.5002  150  TRP G NE1 
18985 C  CE2 . TRP G  152 ? 3.1948 3.1722 3.5312 -0.3118 0.2456  0.5190  150  TRP G CE2 
18986 C  CE3 . TRP G  152 ? 2.9319 2.9529 3.1582 -0.2213 0.2562  0.4731  150  TRP G CE3 
18987 C  CZ2 . TRP G  152 ? 3.1008 3.0764 3.3995 -0.3071 0.2854  0.5750  150  TRP G CZ2 
18988 C  CZ3 . TRP G  152 ? 2.9129 2.9314 3.1005 -0.2165 0.2931  0.5222  150  TRP G CZ3 
18989 C  CH2 . TRP G  152 ? 2.9671 2.9655 3.1878 -0.2582 0.3081  0.5742  150  TRP G CH2 
18990 N  N   . ARG G  153 ? 2.4556 2.6162 2.7353 -0.1814 0.1618  0.3089  151  ARG G N   
18991 C  CA  . ARG G  153 ? 2.4673 2.6410 2.7191 -0.1571 0.1395  0.2692  151  ARG G CA  
18992 C  C   . ARG G  153 ? 2.4728 2.5758 2.6464 -0.1242 0.1381  0.2458  151  ARG G C   
18993 O  O   . ARG G  153 ? 2.4406 2.5146 2.5750 -0.1043 0.1621  0.2648  151  ARG G O   
18994 C  CB  . ARG G  153 ? 2.4607 2.7206 2.7303 -0.1327 0.1565  0.2810  151  ARG G CB  
18995 C  CG  . ARG G  153 ? 2.4675 2.8137 2.8254 -0.1623 0.1470  0.2961  151  ARG G CG  
18996 C  CD  . ARG G  153 ? 2.4588 2.7949 2.8430 -0.2004 0.0997  0.2654  151  ARG G CD  
18997 N  NE  . ARG G  153 ? 2.4702 2.8035 2.8096 -0.1798 0.0715  0.2279  151  ARG G NE  
18998 C  CZ  . ARG G  153 ? 2.4429 2.8515 2.8088 -0.1757 0.0514  0.2247  151  ARG G CZ  
18999 N  NH1 . ARG G  153 ? 2.4755 2.9729 2.9216 -0.1887 0.0548  0.2541  151  ARG G NH1 
19000 N  NH2 . ARG G  153 ? 2.4481 2.8478 2.7623 -0.1579 0.0282  0.1950  151  ARG G NH2 
19001 N  N   . TYR G  154 ? 2.6125 2.6947 2.7645 -0.1199 0.1095  0.2041  152  TYR G N   
19002 C  CA  . TYR G  154 ? 2.5594 2.5817 2.6508 -0.0931 0.1050  0.1771  152  TYR G CA  
19003 C  C   . TYR G  154 ? 2.4438 2.4823 2.4907 -0.0550 0.1291  0.1855  152  TYR G C   
19004 O  O   . TYR G  154 ? 2.3765 2.4717 2.4332 -0.0440 0.1428  0.1979  152  TYR G O   
19005 C  CB  . TYR G  154 ? 2.5747 2.5912 2.6548 -0.0968 0.0754  0.1309  152  TYR G CB  
19006 C  CG  . TYR G  154 ? 2.5440 2.5028 2.5757 -0.0741 0.0705  0.0989  152  TYR G CG  
19007 C  CD1 . TYR G  154 ? 2.5854 2.4750 2.6212 -0.0830 0.0580  0.0821  152  TYR G CD1 
19008 C  CD2 . TYR G  154 ? 2.4932 2.4675 2.4820 -0.0437 0.0788  0.0860  152  TYR G CD2 
19009 C  CE1 . TYR G  154 ? 2.6207 2.4664 2.6225 -0.0582 0.0548  0.0526  152  TYR G CE1 
19010 C  CE2 . TYR G  154 ? 2.5227 2.4564 2.4777 -0.0244 0.0760  0.0576  152  TYR G CE2 
19011 C  CZ  . TYR G  154 ? 2.6770 2.5506 2.6403 -0.0298 0.0643  0.0404  152  TYR G CZ  
19012 O  OH  . TYR G  154 ? 2.8557 2.6968 2.7949 -0.0064 0.0629  0.0119  152  TYR G OH  
19013 N  N   . LEU G  155 ? 2.4275 2.4145 2.4289 -0.0344 0.1326  0.1775  153  LEU G N   
19014 C  CA  . LEU G  155 ? 2.3394 2.3331 2.2961 -0.0025 0.1508  0.1785  153  LEU G CA  
19015 C  C   . LEU G  155 ? 2.3246 2.2882 2.2463 0.0150  0.1372  0.1436  153  LEU G C   
19016 O  O   . LEU G  155 ? 2.4019 2.3889 2.3167 0.0208  0.1315  0.1221  153  LEU G O   
19017 C  CB  . LEU G  155 ? 2.2983 2.2736 2.2328 0.0050  0.1720  0.2093  153  LEU G CB  
19018 C  CG  . LEU G  155 ? 2.2851 2.3009 2.2495 -0.0085 0.1962  0.2464  153  LEU G CG  
19019 C  CD1 . LEU G  155 ? 2.2760 2.2732 2.2005 0.0015  0.2189  0.2747  153  LEU G CD1 
19020 C  CD2 . LEU G  155 ? 2.2342 2.3121 2.2159 0.0032  0.2104  0.2446  153  LEU G CD2 
19021 N  N   . SER G  156 ? 2.3223 2.2382 2.2242 0.0240  0.1323  0.1407  154  SER G N   
19022 C  CA  . SER G  156 ? 2.3078 2.2037 2.1857 0.0426  0.1223  0.1094  154  SER G CA  
19023 C  C   . SER G  156 ? 2.4665 2.3115 2.3589 0.0400  0.1039  0.0956  154  SER G C   
19024 O  O   . SER G  156 ? 2.5225 2.3399 2.4408 0.0213  0.0978  0.1110  154  SER G O   
19025 C  CB  . SER G  156 ? 2.2280 2.1244 2.0691 0.0650  0.1339  0.1166  154  SER G CB  
19026 O  OG  . SER G  156 ? 2.2467 2.1175 2.0766 0.0672  0.1365  0.1451  154  SER G OG  
19027 N  N   . ASN G  157 ? 2.6173 2.4490 2.4979 0.0592  0.0963  0.0663  155  ASN G N   
19028 C  CA  . ASN G  157 ? 2.6987 2.4823 2.5967 0.0650  0.0805  0.0463  155  ASN G CA  
19029 C  C   . ASN G  157 ? 2.6000 2.3782 2.4864 0.0949  0.0780  0.0363  155  ASN G C   
19030 O  O   . ASN G  157 ? 2.4781 2.2948 2.3447 0.1053  0.0867  0.0287  155  ASN G O   
19031 C  CB  . ASN G  157 ? 2.8816 2.6666 2.7917 0.0541  0.0717  0.0042  155  ASN G CB  
19032 C  CG  . ASN G  157 ? 3.0561 2.7834 2.9870 0.0612  0.0578  -0.0225 155  ASN G CG  
19033 O  OD1 . ASN G  157 ? 3.0780 2.8020 3.0065 0.0857  0.0578  -0.0518 155  ASN G OD1 
19034 N  ND2 . ASN G  157 ? 3.1528 2.8344 3.1096 0.0397  0.0473  -0.0133 155  ASN G ND2 
19035 N  N   . ARG G  158 ? 2.5950 2.3250 2.4993 0.1082  0.0647  0.0375  156  ARG G N   
19036 C  CA  . ARG G  158 ? 2.5590 2.2894 2.4640 0.1389  0.0578  0.0308  156  ARG G CA  
19037 C  C   . ARG G  158 ? 2.5825 2.2554 2.5208 0.1555  0.0420  0.0210  156  ARG G C   
19038 O  O   . ARG G  158 ? 2.6290 2.2485 2.5785 0.1461  0.0342  0.0480  156  ARG G O   
19039 C  CB  . ARG G  158 ? 2.5612 2.3029 2.4387 0.1461  0.0577  0.0703  156  ARG G CB  
19040 C  CG  . ARG G  158 ? 2.5507 2.3119 2.4283 0.1740  0.0470  0.0625  156  ARG G CG  
19041 C  CD  . ARG G  158 ? 2.6035 2.3899 2.4403 0.1736  0.0487  0.0903  156  ARG G CD  
19042 N  NE  . ARG G  158 ? 2.6160 2.4343 2.4277 0.1542  0.0699  0.0862  156  ARG G NE  
19043 C  CZ  . ARG G  158 ? 2.5664 2.4040 2.3391 0.1509  0.0781  0.1021  156  ARG G CZ  
19044 N  NH1 . ARG G  158 ? 2.5339 2.3670 2.2807 0.1627  0.0650  0.1228  156  ARG G NH1 
19045 N  NH2 . ARG G  158 ? 2.4669 2.3275 2.2248 0.1377  0.0984  0.0966  156  ARG G NH2 
19046 N  N   . LEU G  159 ? 2.6186 2.3019 2.5764 0.1805  0.0395  -0.0162 157  LEU G N   
19047 C  CA  . LEU G  159 ? 2.6567 2.2872 2.6519 0.2060  0.0260  -0.0290 157  LEU G CA  
19048 C  C   . LEU G  159 ? 2.6494 2.2784 2.6525 0.2355  0.0108  0.0042  157  LEU G C   
19049 O  O   . LEU G  159 ? 2.6127 2.2962 2.5958 0.2401  0.0116  0.0162  157  LEU G O   
19050 C  CB  . LEU G  159 ? 2.7799 2.4290 2.7960 0.2227  0.0342  -0.0880 157  LEU G CB  
19051 C  CG  . LEU G  159 ? 2.7059 2.3522 2.7108 0.1987  0.0444  -0.1296 157  LEU G CG  
19052 C  CD1 . LEU G  159 ? 2.6414 2.3549 2.6086 0.1746  0.0591  -0.1304 157  LEU G CD1 
19053 C  CD2 . LEU G  159 ? 2.7297 2.3674 2.7586 0.2241  0.0501  -0.1864 157  LEU G CD2 
19054 N  N   . LEU G  160 ? 2.6240 2.1876 2.6564 0.2551  -0.0057 0.0194  158  LEU G N   
19055 C  CA  . LEU G  160 ? 2.6831 2.2380 2.7208 0.2834  -0.0262 0.0609  158  LEU G CA  
19056 C  C   . LEU G  160 ? 2.8764 2.4179 2.9696 0.3289  -0.0392 0.0359  158  LEU G C   
19057 O  O   . LEU G  160 ? 2.9635 2.4598 3.0905 0.3374  -0.0342 -0.0015 158  LEU G O   
19058 C  CB  . LEU G  160 ? 2.6690 2.1559 2.6912 0.2692  -0.0359 0.1182  158  LEU G CB  
19059 C  CG  . LEU G  160 ? 2.6554 2.1688 2.6226 0.2366  -0.0254 0.1599  158  LEU G CG  
19060 C  CD1 . LEU G  160 ? 2.6421 2.1771 2.5973 0.1980  -0.0022 0.1370  158  LEU G CD1 
19061 C  CD2 . LEU G  160 ? 2.7056 2.1575 2.6601 0.2308  -0.0352 0.2231  158  LEU G CD2 
19062 N  N   . ALA G  161 ? 2.7682 2.3513 2.8722 0.3594  -0.0569 0.0552  159  ALA G N   
19063 C  CA  . ALA G  161 ? 2.6601 2.2552 2.8256 0.4077  -0.0700 0.0350  159  ALA G CA  
19064 C  C   . ALA G  161 ? 2.7081 2.2534 2.8915 0.4401  -0.1025 0.0883  159  ALA G C   
19065 O  O   . ALA G  161 ? 2.7655 2.3119 2.9035 0.4285  -0.1179 0.1424  159  ALA G O   
19066 C  CB  . ALA G  161 ? 2.6005 2.3004 2.7769 0.4170  -0.0676 0.0127  159  ALA G CB  
19067 N  N   . PRO G  162 ? 2.8068 2.3076 3.0543 0.4835  -0.1130 0.0750  160  PRO G N   
19068 C  CA  . PRO G  162 ? 2.8691 2.3141 3.1375 0.5186  -0.1463 0.1313  160  PRO G CA  
19069 C  C   . PRO G  162 ? 2.8487 2.3733 3.1235 0.5473  -0.1758 0.1621  160  PRO G C   
19070 O  O   . PRO G  162 ? 2.9345 2.4995 3.2775 0.5938  -0.1886 0.1422  160  PRO G O   
19071 C  CB  . PRO G  162 ? 3.0124 2.3933 3.3560 0.5609  -0.1448 0.0949  160  PRO G CB  
19072 C  CG  . PRO G  162 ? 2.9657 2.4151 3.3344 0.5619  -0.1155 0.0179  160  PRO G CG  
19073 C  CD  . PRO G  162 ? 2.8967 2.3901 3.1964 0.5032  -0.0930 0.0076  160  PRO G CD  
19074 N  N   . SER G  163 ? 2.7748 2.3261 2.9806 0.5204  -0.1874 0.2087  161  SER G N   
19075 C  CA  . SER G  163 ? 2.7727 2.3967 2.9727 0.5420  -0.2212 0.2393  161  SER G CA  
19076 C  C   . SER G  163 ? 2.8355 2.3981 3.0324 0.5727  -0.2583 0.3103  161  SER G C   
19077 O  O   . SER G  163 ? 2.8691 2.3527 3.0163 0.5504  -0.2546 0.3565  161  SER G O   
19078 C  CB  . SER G  163 ? 2.7611 2.4465 2.8811 0.4983  -0.2145 0.2464  161  SER G CB  
19079 O  OG  . SER G  163 ? 2.7714 2.5155 2.8733 0.5149  -0.2525 0.2796  161  SER G OG  
19080 N  N   . ASP G  164 ? 3.1103 2.7142 3.3635 0.6235  -0.2943 0.3222  162  ASP G N   
19081 C  CA  . ASP G  164 ? 3.2926 2.8390 3.5532 0.6622  -0.3342 0.3923  162  ASP G CA  
19082 C  C   . ASP G  164 ? 3.2518 2.7993 3.4115 0.6366  -0.3553 0.4619  162  ASP G C   
19083 O  O   . ASP G  164 ? 3.3457 2.8220 3.4867 0.6545  -0.3795 0.5311  162  ASP G O   
19084 C  CB  . ASP G  164 ? 3.3870 2.9984 3.7355 0.7244  -0.3710 0.3882  162  ASP G CB  
19085 C  CG  . ASP G  164 ? 3.3335 2.9538 3.7838 0.7552  -0.3462 0.3175  162  ASP G CG  
19086 O  OD1 . ASP G  164 ? 3.4487 2.9673 3.9398 0.7783  -0.3351 0.3133  162  ASP G OD1 
19087 O  OD2 . ASP G  164 ? 3.1714 2.8991 3.6603 0.7555  -0.3366 0.2656  162  ASP G OD2 
19088 N  N   . SER G  165 ? 3.0654 2.6886 3.1582 0.5965  -0.3456 0.4457  163  SER G N   
19089 C  CA  . SER G  165 ? 3.1892 2.8243 3.1786 0.5725  -0.3616 0.5011  163  SER G CA  
19090 C  C   . SER G  165 ? 3.1995 2.7983 3.1138 0.5157  -0.3166 0.4984  163  SER G C   
19091 O  O   . SER G  165 ? 3.0402 2.6329 2.9804 0.4918  -0.2781 0.4445  163  SER G O   
19092 C  CB  . SER G  165 ? 3.1522 2.9050 3.1206 0.5727  -0.3894 0.4830  163  SER G CB  
19093 O  OG  . SER G  165 ? 3.0687 2.8811 3.0471 0.5413  -0.3569 0.4123  163  SER G OG  
19094 N  N   . PRO G  166 ? 3.3481 2.9256 3.1695 0.4944  -0.3196 0.5576  164  PRO G N   
19095 C  CA  . PRO G  166 ? 3.2533 2.8130 3.0082 0.4423  -0.2748 0.5543  164  PRO G CA  
19096 C  C   . PRO G  166 ? 3.1267 2.7693 2.8623 0.4165  -0.2543 0.4904  164  PRO G C   
19097 O  O   . PRO G  166 ? 3.1218 2.8374 2.8259 0.4218  -0.2780 0.4806  164  PRO G O   
19098 C  CB  . PRO G  166 ? 3.3182 2.8607 2.9753 0.4333  -0.2870 0.6317  164  PRO G CB  
19099 C  CG  . PRO G  166 ? 3.3721 2.9586 3.0252 0.4748  -0.3429 0.6591  164  PRO G CG  
19100 C  CD  . PRO G  166 ? 3.4640 3.0355 3.2349 0.5179  -0.3626 0.6332  164  PRO G CD  
19101 N  N   . GLU G  167 ? 3.0095 2.6388 2.7655 0.3876  -0.2126 0.4471  165  GLU G N   
19102 C  CA  . GLU G  167 ? 2.9347 2.6310 2.6815 0.3645  -0.1906 0.3880  165  GLU G CA  
19103 C  C   . GLU G  167 ? 2.9654 2.6553 2.6421 0.3230  -0.1532 0.3949  165  GLU G C   
19104 O  O   . GLU G  167 ? 3.1290 2.7616 2.7920 0.3064  -0.1337 0.4298  165  GLU G O   
19105 C  CB  . GLU G  167 ? 2.8781 2.5794 2.7076 0.3687  -0.1737 0.3276  165  GLU G CB  
19106 C  CG  . GLU G  167 ? 2.9419 2.6681 2.8479 0.4119  -0.2041 0.3106  165  GLU G CG  
19107 C  CD  . GLU G  167 ? 2.8946 2.7132 2.7974 0.4200  -0.2288 0.2923  165  GLU G CD  
19108 O  OE1 . GLU G  167 ? 2.7928 2.6664 2.7415 0.4169  -0.2170 0.2385  165  GLU G OE1 
19109 O  OE2 . GLU G  167 ? 3.0215 2.8592 2.8747 0.4272  -0.2607 0.3322  165  GLU G OE2 
19110 N  N   . TRP G  168 ? 2.8761 2.6263 2.5144 0.3063  -0.1429 0.3609  166  TRP G N   
19111 C  CA  . TRP G  168 ? 2.9575 2.7126 2.5309 0.2733  -0.1072 0.3618  166  TRP G CA  
19112 C  C   . TRP G  168 ? 2.9600 2.7375 2.5702 0.2552  -0.0773 0.3043  166  TRP G C   
19113 O  O   . TRP G  168 ? 2.9669 2.7902 2.5998 0.2599  -0.0858 0.2613  166  TRP G O   
19114 C  CB  . TRP G  168 ? 2.9288 2.7267 2.4164 0.2709  -0.1202 0.3711  166  TRP G CB  
19115 C  CG  . TRP G  168 ? 2.8819 2.6686 2.2860 0.2481  -0.0888 0.4009  166  TRP G CG  
19116 C  CD1 . TRP G  168 ? 2.8704 2.6649 2.2585 0.2234  -0.0454 0.3772  166  TRP G CD1 
19117 C  CD2 . TRP G  168 ? 2.8693 2.6413 2.1949 0.2504  -0.0969 0.4610  166  TRP G CD2 
19118 N  NE1 . TRP G  168 ? 2.8697 2.6585 2.1803 0.2110  -0.0228 0.4155  166  TRP G NE1 
19119 C  CE2 . TRP G  168 ? 2.8493 2.6240 2.1156 0.2254  -0.0524 0.4677  166  TRP G CE2 
19120 C  CE3 . TRP G  168 ? 3.0378 2.7966 2.3373 0.2728  -0.1370 0.5127  166  TRP G CE3 
19121 C  CZ2 . TRP G  168 ? 2.8852 2.6524 2.0638 0.2196  -0.0425 0.5222  166  TRP G CZ2 
19122 C  CZ3 . TRP G  168 ? 3.1963 2.9431 2.4035 0.2663  -0.1309 0.5709  166  TRP G CZ3 
19123 C  CH2 . TRP G  168 ? 3.0814 2.8337 2.2272 0.2387  -0.0819 0.5742  166  TRP G CH2 
19124 N  N   . LEU G  169 ? 3.0344 2.7821 2.6533 0.2334  -0.0439 0.3067  167  LEU G N   
19125 C  CA  . LEU G  169 ? 2.9642 2.7304 2.6132 0.2162  -0.0166 0.2606  167  LEU G CA  
19126 C  C   . LEU G  169 ? 2.9283 2.7129 2.5239 0.1932  0.0153  0.2629  167  LEU G C   
19127 O  O   . LEU G  169 ? 3.0104 2.7941 2.5443 0.1898  0.0200  0.2966  167  LEU G O   
19128 C  CB  . LEU G  169 ? 3.0584 2.7834 2.7675 0.2105  -0.0073 0.2547  167  LEU G CB  
19129 C  CG  . LEU G  169 ? 3.1804 2.9055 2.9550 0.2302  -0.0225 0.2168  167  LEU G CG  
19130 C  CD1 . LEU G  169 ? 3.2917 2.9999 3.0849 0.2628  -0.0569 0.2386  167  LEU G CD1 
19131 C  CD2 . LEU G  169 ? 3.2426 2.9303 3.0614 0.2176  -0.0078 0.1993  167  LEU G CD2 
19132 N  N   . SER G  170 ? 2.9383 2.7408 2.5570 0.1795  0.0385  0.2274  168  SER G N   
19133 C  CA  . SER G  170 ? 2.9997 2.8216 2.5802 0.1634  0.0698  0.2248  168  SER G CA  
19134 C  C   . SER G  170 ? 2.9055 2.7347 2.5308 0.1501  0.0910  0.1991  168  SER G C   
19135 O  O   . SER G  170 ? 2.9705 2.8065 2.6364 0.1538  0.0820  0.1673  168  SER G O   
19136 C  CB  . SER G  170 ? 2.9913 2.8445 2.5237 0.1681  0.0662  0.2014  168  SER G CB  
19137 O  OG  . SER G  170 ? 3.1285 3.0021 2.6980 0.1720  0.0539  0.1603  168  SER G OG  
19138 N  N   . PHE G  171 ? 2.6224 2.4561 2.2397 0.1353  0.1194  0.2145  169  PHE G N   
19139 C  CA  . PHE G  171 ? 2.4604 2.3081 2.1174 0.1229  0.1369  0.1966  169  PHE G CA  
19140 C  C   . PHE G  171 ? 2.4013 2.2772 2.0302 0.1212  0.1650  0.1913  169  PHE G C   
19141 O  O   . PHE G  171 ? 2.5691 2.4507 2.1670 0.1186  0.1851  0.2170  169  PHE G O   
19142 C  CB  . PHE G  171 ? 2.4998 2.3292 2.1957 0.1061  0.1411  0.2206  169  PHE G CB  
19143 C  CG  . PHE G  171 ? 2.5813 2.3768 2.3175 0.1078  0.1163  0.2109  169  PHE G CG  
19144 C  CD1 . PHE G  171 ? 2.6070 2.4089 2.3812 0.1042  0.1113  0.1753  169  PHE G CD1 
19145 C  CD2 . PHE G  171 ? 2.6228 2.3785 2.3561 0.1151  0.0986  0.2373  169  PHE G CD2 
19146 C  CE1 . PHE G  171 ? 2.6062 2.3754 2.4142 0.1083  0.0920  0.1596  169  PHE G CE1 
19147 C  CE2 . PHE G  171 ? 2.6419 2.3601 2.4164 0.1213  0.0776  0.2250  169  PHE G CE2 
19148 C  CZ  . PHE G  171 ? 2.6404 2.3654 2.4521 0.1182  0.0757  0.1827  169  PHE G CZ  
19149 N  N   . ASP G  172 ? 2.5355 2.4275 2.1760 0.1237  0.1687  0.1590  170  ASP G N   
19150 C  CA  . ASP G  172 ? 2.4818 2.3917 2.1011 0.1268  0.1939  0.1495  170  ASP G CA  
19151 C  C   . ASP G  172 ? 2.5042 2.4328 2.1544 0.1190  0.2174  0.1681  170  ASP G C   
19152 O  O   . ASP G  172 ? 2.6672 2.6074 2.3610 0.1127  0.2147  0.1607  170  ASP G O   
19153 C  CB  . ASP G  172 ? 2.6133 2.5275 2.2423 0.1299  0.1885  0.1152  170  ASP G CB  
19154 C  CG  . ASP G  172 ? 2.7521 2.6682 2.3502 0.1364  0.2093  0.1010  170  ASP G CG  
19155 O  OD1 . ASP G  172 ? 2.8211 2.7445 2.4074 0.1407  0.2347  0.1150  170  ASP G OD1 
19156 O  OD2 . ASP G  172 ? 2.7810 2.6907 2.3703 0.1371  0.2015  0.0747  170  ASP G OD2 
19157 N  N   . VAL G  173 ? 2.6090 2.5473 2.2370 0.1191  0.2406  0.1930  171  VAL G N   
19158 C  CA  . VAL G  173 ? 2.6753 2.6438 2.3413 0.1119  0.2656  0.2129  171  VAL G CA  
19159 C  C   . VAL G  173 ? 2.6530 2.6425 2.2965 0.1279  0.2986  0.2054  171  VAL G C   
19160 O  O   . VAL G  173 ? 2.5702 2.5887 2.2228 0.1279  0.3283  0.2275  171  VAL G O   
19161 C  CB  . VAL G  173 ? 2.9136 2.8828 2.5881 0.0960  0.2718  0.2526  171  VAL G CB  
19162 C  CG1 . VAL G  173 ? 3.0937 3.0369 2.8073 0.0798  0.2414  0.2570  171  VAL G CG1 
19163 C  CG2 . VAL G  173 ? 2.9369 2.8913 2.5419 0.1031  0.2794  0.2690  171  VAL G CG2 
19164 N  N   . THR G  174 ? 2.8106 2.7852 2.4292 0.1415  0.2954  0.1733  172  THR G N   
19165 C  CA  . THR G  174 ? 2.8329 2.8135 2.4275 0.1595  0.3261  0.1596  172  THR G CA  
19166 C  C   . THR G  174 ? 2.7050 2.7216 2.3580 0.1661  0.3488  0.1716  172  THR G C   
19167 O  O   . THR G  174 ? 2.6624 2.7030 2.3131 0.1788  0.3836  0.1802  172  THR G O   
19168 C  CB  . THR G  174 ? 2.9710 2.9204 2.5388 0.1673  0.3142  0.1225  172  THR G CB  
19169 O  OG1 . THR G  174 ? 3.1852 3.1129 2.7026 0.1618  0.2919  0.1117  172  THR G OG1 
19170 C  CG2 . THR G  174 ? 2.9377 2.8807 2.4839 0.1871  0.3459  0.1039  172  THR G CG2 
19171 N  N   . GLY G  175 ? 2.7098 2.7359 2.4157 0.1590  0.3295  0.1723  173  GLY G N   
19172 C  CA  . GLY G  175 ? 2.7559 2.8237 2.5217 0.1653  0.3431  0.1867  173  GLY G CA  
19173 C  C   . GLY G  175 ? 2.8023 2.9153 2.6046 0.1549  0.3605  0.2184  173  GLY G C   
19174 O  O   . GLY G  175 ? 2.8958 3.0544 2.7440 0.1661  0.3833  0.2314  173  GLY G O   
19175 N  N   . VAL G  176 ? 2.7313 2.8337 2.5195 0.1335  0.3505  0.2336  174  VAL G N   
19176 C  CA  . VAL G  176 ? 2.8304 2.9714 2.6534 0.1173  0.3687  0.2680  174  VAL G CA  
19177 C  C   . VAL G  176 ? 2.8437 2.9992 2.6258 0.1320  0.4115  0.2781  174  VAL G C   
19178 O  O   . VAL G  176 ? 2.8634 3.0729 2.6863 0.1346  0.4445  0.2983  174  VAL G O   
19179 C  CB  . VAL G  176 ? 2.8046 2.9181 2.6289 0.0884  0.3422  0.2837  174  VAL G CB  
19180 C  CG1 . VAL G  176 ? 2.7888 2.9362 2.6486 0.0664  0.3633  0.3235  174  VAL G CG1 
19181 C  CG2 . VAL G  176 ? 2.7575 2.8602 2.6213 0.0750  0.3042  0.2678  174  VAL G CG2 
19182 N  N   . VAL G  177 ? 2.7157 2.8290 2.4167 0.1416  0.4116  0.2630  175  VAL G N   
19183 C  CA  . VAL G  177 ? 2.5852 2.7092 2.2295 0.1545  0.4509  0.2687  175  VAL G CA  
19184 C  C   . VAL G  177 ? 2.5862 2.7366 2.2425 0.1843  0.4871  0.2482  175  VAL G C   
19185 O  O   . VAL G  177 ? 2.5936 2.7823 2.2441 0.1950  0.5316  0.2600  175  VAL G O   
19186 C  CB  . VAL G  177 ? 2.6023 2.6764 2.1534 0.1574  0.4340  0.2526  175  VAL G CB  
19187 C  CG1 . VAL G  177 ? 2.6316 2.7175 2.1101 0.1698  0.4734  0.2556  175  VAL G CG1 
19188 C  CG2 . VAL G  177 ? 2.6276 2.6757 2.1764 0.1339  0.3983  0.2767  175  VAL G CG2 
19189 N  N   . ARG G  178 ? 2.6545 2.7843 2.3297 0.1994  0.4712  0.2188  176  ARG G N   
19190 C  CA  . ARG G  178 ? 2.7113 2.8528 2.4000 0.2320  0.5031  0.1990  176  ARG G CA  
19191 C  C   . ARG G  178 ? 2.8451 3.0594 2.6184 0.2392  0.5316  0.2269  176  ARG G C   
19192 O  O   . ARG G  178 ? 3.0127 3.2556 2.7903 0.2664  0.5761  0.2220  176  ARG G O   
19193 C  CB  . ARG G  178 ? 2.6343 2.7353 2.3338 0.2423  0.4768  0.1716  176  ARG G CB  
19194 C  CG  . ARG G  178 ? 2.6905 2.7963 2.4193 0.2777  0.5052  0.1570  176  ARG G CG  
19195 C  CD  . ARG G  178 ? 2.8000 2.8524 2.5262 0.2847  0.4803  0.1332  176  ARG G CD  
19196 N  NE  . ARG G  178 ? 2.9735 2.9621 2.6198 0.2821  0.4743  0.0965  176  ARG G NE  
19197 C  CZ  . ARG G  178 ? 3.0573 3.0156 2.6704 0.2567  0.4382  0.0877  176  ARG G CZ  
19198 N  NH1 . ARG G  178 ? 3.0462 3.0252 2.6942 0.2343  0.4078  0.1101  176  ARG G NH1 
19199 N  NH2 . ARG G  178 ? 2.9926 2.9023 2.5405 0.2541  0.4321  0.0536  176  ARG G NH2 
19200 N  N   . GLN G  179 ? 2.8277 3.0761 2.6719 0.2154  0.5065  0.2538  177  GLN G N   
19201 C  CA  . GLN G  179 ? 2.7524 3.0805 2.6878 0.2178  0.5274  0.2812  177  GLN G CA  
19202 C  C   . GLN G  179 ? 2.7840 3.1589 2.7214 0.2043  0.5658  0.3103  177  GLN G C   
19203 O  O   . GLN G  179 ? 2.8038 3.2514 2.8055 0.2160  0.6017  0.3277  177  GLN G O   
19204 C  CB  . GLN G  179 ? 2.7147 3.0654 2.7207 0.1918  0.4843  0.2968  177  GLN G CB  
19205 C  CG  . GLN G  179 ? 2.8970 3.2107 2.9008 0.2031  0.4491  0.2743  177  GLN G CG  
19206 C  CD  . GLN G  179 ? 3.0371 3.3720 3.0936 0.1751  0.4059  0.2858  177  GLN G CD  
19207 O  OE1 . GLN G  179 ? 3.0139 3.3898 3.1164 0.1461  0.4005  0.3082  177  GLN G OE1 
19208 N  NE2 . GLN G  179 ? 3.0950 3.4009 3.1425 0.1813  0.3754  0.2696  177  GLN G NE2 
19209 N  N   . TRP G  180 ? 2.7901 3.1281 2.6612 0.1804  0.5597  0.3194  178  TRP G N   
19210 C  CA  . TRP G  180 ? 2.7664 3.1440 2.6326 0.1630  0.5956  0.3547  178  TRP G CA  
19211 C  C   . TRP G  180 ? 2.7051 3.0990 2.5125 0.1934  0.6518  0.3437  178  TRP G C   
19212 O  O   . TRP G  180 ? 2.6966 3.1502 2.5225 0.1872  0.6965  0.3736  178  TRP G O   
19213 C  CB  . TRP G  180 ? 2.8123 3.1388 2.6245 0.1299  0.5675  0.3734  178  TRP G CB  
19214 C  CG  . TRP G  180 ? 2.8263 3.1487 2.7063 0.0946  0.5255  0.3916  178  TRP G CG  
19215 C  CD1 . TRP G  180 ? 2.8501 3.2122 2.8232 0.0870  0.5074  0.3905  178  TRP G CD1 
19216 C  CD2 . TRP G  180 ? 2.8287 3.1026 2.6870 0.0630  0.4952  0.4115  178  TRP G CD2 
19217 N  NE1 . TRP G  180 ? 2.7817 3.1215 2.7873 0.0502  0.4683  0.4031  178  TRP G NE1 
19218 C  CE2 . TRP G  180 ? 2.8365 3.1185 2.7761 0.0363  0.4617  0.4160  178  TRP G CE2 
19219 C  CE3 . TRP G  180 ? 2.8815 3.1047 2.6587 0.0564  0.4912  0.4263  178  TRP G CE3 
19220 C  CZ2 . TRP G  180 ? 2.8836 3.1178 2.8281 0.0045  0.4281  0.4302  178  TRP G CZ2 
19221 C  CZ3 . TRP G  180 ? 2.9114 3.0895 2.6984 0.0273  0.4565  0.4468  178  TRP G CZ3 
19222 C  CH2 . TRP G  180 ? 2.9134 3.0937 2.7843 0.0022  0.4271  0.4465  178  TRP G CH2 
19223 N  N   . LEU G  181 ? 2.6247 2.9671 2.3612 0.2239  0.6520  0.3001  179  LEU G N   
19224 C  CA  . LEU G  181 ? 2.6284 2.9801 2.3042 0.2555  0.7051  0.2789  179  LEU G CA  
19225 C  C   . LEU G  181 ? 2.6148 3.0256 2.3695 0.2908  0.7463  0.2709  179  LEU G C   
19226 O  O   . LEU G  181 ? 2.8251 3.2662 2.5516 0.3166  0.8025  0.2608  179  LEU G O   
19227 C  CB  . LEU G  181 ? 2.6884 2.9594 2.2625 0.2721  0.6873  0.2301  179  LEU G CB  
19228 C  CG  . LEU G  181 ? 2.8614 3.0911 2.3236 0.2532  0.6730  0.2317  179  LEU G CG  
19229 C  CD1 . LEU G  181 ? 2.9202 3.1420 2.4034 0.2142  0.6306  0.2729  179  LEU G CD1 
19230 C  CD2 . LEU G  181 ? 2.8365 2.9943 2.2205 0.2667  0.6469  0.1792  179  LEU G CD2 
19231 N  N   . SER G  182 ? 2.5381 2.9682 2.3896 0.2948  0.7198  0.2753  180  SER G N   
19232 C  CA  . SER G  182 ? 2.6596 3.1557 2.6025 0.3298  0.7533  0.2764  180  SER G CA  
19233 C  C   . SER G  182 ? 2.8117 3.4133 2.8484 0.3114  0.7802  0.3228  180  SER G C   
19234 O  O   . SER G  182 ? 3.0054 3.6800 3.1121 0.3428  0.8241  0.3267  180  SER G O   
19235 C  CB  . SER G  182 ? 2.5253 3.0010 2.5290 0.3433  0.7105  0.2661  180  SER G CB  
19236 O  OG  . SER G  182 ? 2.5165 3.0070 2.5704 0.3034  0.6606  0.2939  180  SER G OG  
19237 N  N   . ARG G  183 ? 2.7345 3.3456 2.7787 0.2615  0.7563  0.3577  181  ARG G N   
19238 C  CA  . ARG G  183 ? 2.6389 3.3456 2.7759 0.2337  0.7779  0.4038  181  ARG G CA  
19239 C  C   . ARG G  183 ? 2.6388 3.3713 2.7194 0.2235  0.8345  0.4251  181  ARG G C   
19240 O  O   . ARG G  183 ? 2.5796 3.2442 2.5419 0.2183  0.8348  0.4153  181  ARG G O   
19241 C  CB  . ARG G  183 ? 2.5999 3.2970 2.7817 0.1815  0.7211  0.4299  181  ARG G CB  
19242 C  CG  . ARG G  183 ? 2.7555 3.4170 2.9667 0.1868  0.6618  0.4077  181  ARG G CG  
19243 C  CD  . ARG G  183 ? 2.9252 3.5645 3.1598 0.1359  0.6077  0.4242  181  ARG G CD  
19244 N  NE  . ARG G  183 ? 2.7608 3.3494 2.9883 0.1411  0.5531  0.3974  181  ARG G NE  
19245 C  CZ  . ARG G  183 ? 2.6563 3.2898 2.9640 0.1457  0.5260  0.3974  181  ARG G CZ  
19246 N  NH1 . ARG G  183 ? 2.8183 3.5522 3.2286 0.1468  0.5450  0.4216  181  ARG G NH1 
19247 N  NH2 . ARG G  183 ? 2.5806 3.1645 2.8665 0.1491  0.4798  0.3751  181  ARG G NH2 
19248 N  N   . GLY G  184 ? 2.8262 3.6641 2.9938 0.2202  0.8824  0.4566  182  GLY G N   
19249 C  CA  . GLY G  184 ? 3.0017 3.8813 3.1303 0.2049  0.9412  0.4868  182  GLY G CA  
19250 C  C   . GLY G  184 ? 3.0462 3.9259 3.1865 0.1410  0.9224  0.5389  182  GLY G C   
19251 O  O   . GLY G  184 ? 2.9893 3.9140 3.1134 0.1206  0.9722  0.5766  182  GLY G O   
19252 N  N   . GLY G  185 ? 3.0010 3.8295 3.1690 0.1088  0.8537  0.5424  183  GLY G N   
19253 C  CA  . GLY G  185 ? 2.9805 3.7902 3.1599 0.0494  0.8304  0.5869  183  GLY G CA  
19254 C  C   . GLY G  185 ? 2.9265 3.6574 2.9697 0.0401  0.8355  0.5986  183  GLY G C   
19255 O  O   . GLY G  185 ? 2.9682 3.6071 2.9256 0.0525  0.7933  0.5687  183  GLY G O   
19256 N  N   . GLU G  186 ? 2.8246 3.5958 2.8482 0.0180  0.8867  0.6448  184  GLU G N   
19257 C  CA  . GLU G  186 ? 2.8444 3.5513 2.7314 0.0120  0.8958  0.6632  184  GLU G CA  
19258 C  C   . GLU G  186 ? 2.8923 3.5193 2.7653 -0.0336 0.8421  0.6974  184  GLU G C   
19259 O  O   . GLU G  186 ? 3.0317 3.6101 2.8030 -0.0436 0.8471  0.7267  184  GLU G O   
19260 C  CB  . GLU G  186 ? 2.9252 3.7080 2.7868 0.0072  0.9760  0.7036  184  GLU G CB  
19261 C  CG  . GLU G  186 ? 2.7496 3.6014 2.6003 0.0603  1.0373  0.6647  184  GLU G CG  
19262 C  CD  . GLU G  186 ? 2.7118 3.6232 2.4962 0.0604  1.1182  0.6974  184  GLU G CD  
19263 O  OE1 . GLU G  186 ? 2.7506 3.6368 2.4739 0.0215  1.1223  0.7512  184  GLU G OE1 
19264 O  OE2 . GLU G  186 ? 2.6920 3.6741 2.4836 0.1011  1.1791  0.6702  184  GLU G OE2 
19265 N  N   . ILE G  187 ? 2.7667 3.3772 2.7355 -0.0595 0.7906  0.6940  185  ILE G N   
19266 C  CA  . ILE G  187 ? 2.7469 3.2726 2.7077 -0.0978 0.7382  0.7176  185  ILE G CA  
19267 C  C   . ILE G  187 ? 2.9003 3.3829 2.9084 -0.0926 0.6730  0.6712  185  ILE G C   
19268 O  O   . ILE G  187 ? 2.8069 3.3465 2.9198 -0.0988 0.6648  0.6568  185  ILE G O   
19269 C  CB  . ILE G  187 ? 2.6170 3.1729 2.6579 -0.1566 0.7548  0.7813  185  ILE G CB  
19270 C  CG1 . ILE G  187 ? 2.6580 3.1133 2.7006 -0.1925 0.6959  0.7975  185  ILE G CG1 
19271 C  CG2 . ILE G  187 ? 2.5704 3.2314 2.7565 -0.1739 0.7713  0.7811  185  ILE G CG2 
19272 C  CD1 . ILE G  187 ? 2.7030 3.0640 2.6146 -0.1777 0.6796  0.8100  185  ILE G CD1 
19273 N  N   . GLU G  188 ? 3.1306 3.5190 3.0611 -0.0801 0.6271  0.6487  186  GLU G N   
19274 C  CA  . GLU G  188 ? 3.1783 3.5191 3.1377 -0.0749 0.5674  0.6053  186  GLU G CA  
19275 C  C   . GLU G  188 ? 3.2861 3.5287 3.1977 -0.0908 0.5238  0.6164  186  GLU G C   
19276 O  O   . GLU G  188 ? 3.4794 3.6931 3.3465 -0.1078 0.5374  0.6626  186  GLU G O   
19277 C  CB  . GLU G  188 ? 3.0941 3.4345 3.0099 -0.0256 0.5624  0.5496  186  GLU G CB  
19278 C  CG  . GLU G  188 ? 3.0318 3.4604 3.0034 -0.0026 0.6009  0.5352  186  GLU G CG  
19279 C  CD  . GLU G  188 ? 2.9930 3.4704 3.0849 -0.0196 0.5777  0.5301  186  GLU G CD  
19280 O  OE1 . GLU G  188 ? 3.0961 3.5308 3.2167 -0.0466 0.5286  0.5257  186  GLU G OE1 
19281 O  OE2 . GLU G  188 ? 2.8359 3.3966 2.9930 -0.0041 0.6079  0.5289  186  GLU G OE2 
19282 N  N   . GLY G  189 ? 3.1745 3.3664 3.0951 -0.0833 0.4725  0.5763  187  GLY G N   
19283 C  CA  . GLY G  189 ? 3.2677 3.3690 3.1509 -0.0908 0.4314  0.5813  187  GLY G CA  
19284 C  C   . GLY G  189 ? 3.2199 3.2837 3.1351 -0.0856 0.3814  0.5332  187  GLY G C   
19285 O  O   . GLY G  189 ? 3.0931 3.1997 3.0540 -0.0783 0.3760  0.4988  187  GLY G O   
19286 N  N   . PHE G  190 ? 3.3729 3.3566 3.2621 -0.0877 0.3455  0.5334  188  PHE G N   
19287 C  CA  . PHE G  190 ? 3.1950 3.1353 3.1055 -0.0818 0.3002  0.4886  188  PHE G CA  
19288 C  C   . PHE G  190 ? 3.2651 3.1400 3.2178 -0.1133 0.2738  0.5057  188  PHE G C   
19289 O  O   . PHE G  190 ? 3.4798 3.3341 3.4402 -0.1391 0.2881  0.5565  188  PHE G O   
19290 C  CB  . PHE G  190 ? 3.0953 2.9999 2.9323 -0.0428 0.2807  0.4591  188  PHE G CB  
19291 C  CG  . PHE G  190 ? 3.1126 3.0659 2.9100 -0.0132 0.3005  0.4322  188  PHE G CG  
19292 C  CD1 . PHE G  190 ? 3.0032 2.9793 2.8259 -0.0007 0.2890  0.3870  188  PHE G CD1 
19293 C  CD2 . PHE G  190 ? 3.3733 3.3448 3.1040 0.0019  0.3306  0.4519  188  PHE G CD2 
19294 C  CE1 . PHE G  190 ? 3.0290 3.0384 2.8187 0.0261  0.3070  0.3638  188  PHE G CE1 
19295 C  CE2 . PHE G  190 ? 3.4596 3.4656 3.1542 0.0290  0.3489  0.4217  188  PHE G CE2 
19296 C  CZ  . PHE G  190 ? 3.2467 3.2680 2.9744 0.0410  0.3369  0.3784  188  PHE G CZ  
19297 N  N   . ARG G  191 ? 2.8882 2.7263 2.8661 -0.1109 0.2366  0.4623  189  ARG G N   
19298 C  CA  . ARG G  191 ? 2.8650 2.6295 2.8816 -0.1358 0.2088  0.4655  189  ARG G CA  
19299 C  C   . ARG G  191 ? 2.8847 2.5967 2.8799 -0.1068 0.1738  0.4183  189  ARG G C   
19300 O  O   . ARG G  191 ? 2.9238 2.6706 2.9119 -0.0873 0.1661  0.3724  189  ARG G O   
19301 C  CB  . ARG G  191 ? 2.9081 2.6981 3.0089 -0.1792 0.2032  0.4563  189  ARG G CB  
19302 C  CG  . ARG G  191 ? 2.9175 2.6254 3.0573 -0.2027 0.1686  0.4380  189  ARG G CG  
19303 C  CD  . ARG G  191 ? 2.8819 2.6243 3.0927 -0.2388 0.1525  0.4050  189  ARG G CD  
19304 N  NE  . ARG G  191 ? 2.8538 2.5146 3.0873 -0.2528 0.1165  0.3676  189  ARG G NE  
19305 C  CZ  . ARG G  191 ? 2.8631 2.5361 3.1451 -0.2823 0.0925  0.3262  189  ARG G CZ  
19306 N  NH1 . ARG G  191 ? 2.8420 2.6111 3.1606 -0.3006 0.0973  0.3219  189  ARG G NH1 
19307 N  NH2 . ARG G  191 ? 2.8952 2.4854 3.1884 -0.2917 0.0624  0.2875  189  ARG G NH2 
19308 N  N   . LEU G  192 ? 2.9758 2.6054 2.9639 -0.1031 0.1543  0.4320  190  LEU G N   
19309 C  CA  . LEU G  192 ? 3.0258 2.6065 3.0023 -0.0728 0.1237  0.3892  190  LEU G CA  
19310 C  C   . LEU G  192 ? 3.1481 2.6464 3.1747 -0.0935 0.1004  0.3814  190  LEU G C   
19311 O  O   . LEU G  192 ? 3.3097 2.7379 3.3356 -0.0949 0.0947  0.4214  190  LEU G O   
19312 C  CB  . LEU G  192 ? 2.9774 2.5402 2.8922 -0.0342 0.1200  0.4088  190  LEU G CB  
19313 C  CG  . LEU G  192 ? 2.9526 2.4951 2.8569 0.0033  0.0939  0.3621  190  LEU G CG  
19314 C  CD1 . LEU G  192 ? 3.0388 2.6207 2.8818 0.0361  0.0974  0.3654  190  LEU G CD1 
19315 C  CD2 . LEU G  192 ? 2.9873 2.4414 2.9149 0.0124  0.0689  0.3703  190  LEU G CD2 
19316 N  N   . SER G  193 ? 3.0265 2.5294 3.0930 -0.1088 0.0860  0.3299  191  SER G N   
19317 C  CA  . SER G  193 ? 3.0069 2.4282 3.1166 -0.1260 0.0622  0.3057  191  SER G CA  
19318 C  C   . SER G  193 ? 2.8538 2.2468 2.9474 -0.0862 0.0419  0.2478  191  SER G C   
19319 O  O   . SER G  193 ? 2.8237 2.2501 2.8758 -0.0470 0.0454  0.2408  191  SER G O   
19320 C  CB  . SER G  193 ? 3.0709 2.5187 3.2347 -0.1757 0.0588  0.2865  191  SER G CB  
19321 O  OG  . SER G  193 ? 3.0477 2.5744 3.2031 -0.1687 0.0571  0.2414  191  SER G OG  
19322 N  N   . ALA G  194 ? 2.7814 2.1152 2.9093 -0.0972 0.0220  0.2037  192  ALA G N   
19323 C  CA  . ALA G  194 ? 2.7736 2.0812 2.8914 -0.0597 0.0074  0.1457  192  ALA G CA  
19324 C  C   . ALA G  194 ? 2.8266 2.1712 2.9517 -0.0767 -0.0002 0.0806  192  ALA G C   
19325 O  O   . ALA G  194 ? 3.0884 2.4932 3.2222 -0.1107 0.0038  0.0833  192  ALA G O   
19326 C  CB  . ALA G  194 ? 2.8096 2.0040 2.9535 -0.0465 -0.0084 0.1461  192  ALA G CB  
19327 N  N   . HIS G  195 ? 2.7854 2.0982 2.9064 -0.0507 -0.0111 0.0224  193  HIS G N   
19328 C  CA  . HIS G  195 ? 2.7674 2.1157 2.8809 -0.0625 -0.0181 -0.0418 193  HIS G CA  
19329 C  C   . HIS G  195 ? 2.8042 2.1113 2.9540 -0.1131 -0.0350 -0.0622 193  HIS G C   
19330 O  O   . HIS G  195 ? 2.8442 2.0610 3.0293 -0.1286 -0.0438 -0.0498 193  HIS G O   
19331 C  CB  . HIS G  195 ? 2.8446 2.1700 2.9424 -0.0201 -0.0201 -0.0989 193  HIS G CB  
19332 C  CG  . HIS G  195 ? 2.9750 2.3406 3.0510 -0.0284 -0.0240 -0.1648 193  HIS G CG  
19333 N  ND1 . HIS G  195 ? 2.9453 2.4059 2.9912 -0.0394 -0.0178 -0.1645 193  HIS G ND1 
19334 C  CD2 . HIS G  195 ? 3.1124 2.4348 3.1872 -0.0259 -0.0332 -0.2326 193  HIS G CD2 
19335 C  CE1 . HIS G  195 ? 3.0062 2.4835 3.0299 -0.0448 -0.0246 -0.2247 193  HIS G CE1 
19336 N  NE2 . HIS G  195 ? 3.1148 2.5111 3.1528 -0.0374 -0.0330 -0.2699 193  HIS G NE2 
19337 N  N   . CYS G  196 ? 2.7939 2.1686 2.9362 -0.1405 -0.0417 -0.0917 194  CYS G N   
19338 C  CA  . CYS G  196 ? 2.8707 2.2253 3.0446 -0.1918 -0.0635 -0.1218 194  CYS G CA  
19339 C  C   . CYS G  196 ? 2.8664 2.2321 3.0063 -0.1849 -0.0770 -0.2016 194  CYS G C   
19340 O  O   . CYS G  196 ? 2.7660 2.2191 2.8681 -0.1747 -0.0731 -0.2141 194  CYS G O   
19341 C  CB  . CYS G  196 ? 2.8997 2.3377 3.0986 -0.2339 -0.0636 -0.0819 194  CYS G CB  
19342 S  SG  . CYS G  196 ? 3.1186 2.6027 3.3289 -0.2278 -0.0338 0.0106  194  CYS G SG  
19343 N  N   . SER G  197 ? 3.0946 2.3691 3.2448 -0.1899 -0.0916 -0.2555 195  SER G N   
19344 C  CA  . SER G  197 ? 2.9980 2.2732 3.1089 -0.1815 -0.1015 -0.3380 195  SER G CA  
19345 C  C   . SER G  197 ? 3.2300 2.5186 3.3514 -0.2404 -0.1310 -0.3737 195  SER G C   
19346 O  O   . SER G  197 ? 3.4299 2.6369 3.5945 -0.2775 -0.1489 -0.3865 195  SER G O   
19347 C  CB  . SER G  197 ? 2.9834 2.1519 3.0977 -0.1466 -0.0981 -0.3841 195  SER G CB  
19348 O  OG  . SER G  197 ? 3.1149 2.1746 3.2813 -0.1760 -0.1130 -0.3794 195  SER G OG  
19349 N  N   . CYS G  198 ? 3.1517 2.5425 3.2355 -0.2504 -0.1384 -0.3875 196  CYS G N   
19350 C  CA  . CYS G  198 ? 3.1664 2.5866 3.2535 -0.3038 -0.1722 -0.4253 196  CYS G CA  
19351 C  C   . CYS G  198 ? 3.0523 2.5334 3.0638 -0.2897 -0.1791 -0.4840 196  CYS G C   
19352 O  O   . CYS G  198 ? 2.9560 2.4567 2.9193 -0.2409 -0.1539 -0.4915 196  CYS G O   
19353 C  CB  . CYS G  198 ? 3.1603 2.6642 3.2936 -0.3431 -0.1814 -0.3621 196  CYS G CB  
19354 S  SG  . CYS G  198 ? 3.0505 2.6951 3.1445 -0.3139 -0.1663 -0.3186 196  CYS G SG  
19355 N  N   . ASP G  208 ? 3.4592 2.2930 3.8491 -0.3684 -0.1519 -0.2177 206  ASP G N   
19356 C  CA  . ASP G  208 ? 3.5219 2.2977 3.8863 -0.2983 -0.1353 -0.2100 206  ASP G CA  
19357 C  C   . ASP G  208 ? 3.4059 2.2568 3.7526 -0.2677 -0.1101 -0.1261 206  ASP G C   
19358 O  O   . ASP G  208 ? 3.3081 2.2744 3.6157 -0.2497 -0.0993 -0.1240 206  ASP G O   
19359 C  CB  . ASP G  208 ? 3.6170 2.4100 3.9295 -0.2513 -0.1362 -0.2949 206  ASP G CB  
19360 C  CG  . ASP G  208 ? 3.7349 2.4061 4.0536 -0.2008 -0.1337 -0.3287 206  ASP G CG  
19361 O  OD1 . ASP G  208 ? 3.7728 2.3695 4.1224 -0.1816 -0.1274 -0.2694 206  ASP G OD1 
19362 O  OD2 . ASP G  208 ? 3.7082 2.3607 4.0002 -0.1780 -0.1372 -0.4140 206  ASP G OD2 
19363 N  N   . ILE G  209 ? 3.5809 2.3612 3.9534 -0.2631 -0.1016 -0.0568 207  ILE G N   
19364 C  CA  . ILE G  209 ? 3.5808 2.4180 3.9317 -0.2365 -0.0794 0.0239  207  ILE G CA  
19365 C  C   . ILE G  209 ? 3.7901 2.5645 4.1219 -0.1693 -0.0762 0.0333  207  ILE G C   
19366 O  O   . ILE G  209 ? 3.9433 2.5958 4.3033 -0.1575 -0.0879 0.0190  207  ILE G O   
19367 C  CB  . ILE G  209 ? 3.5903 2.4128 3.9794 -0.2865 -0.0705 0.1067  207  ILE G CB  
19368 C  CG1 . ILE G  209 ? 3.6790 2.4158 4.1288 -0.3499 -0.0896 0.0841  207  ILE G CG1 
19369 C  CG2 . ILE G  209 ? 3.4833 2.4441 3.8595 -0.3068 -0.0521 0.1444  207  ILE G CG2 
19370 C  CD1 . ILE G  209 ? 3.6755 2.3499 4.1700 -0.3918 -0.0806 0.1678  207  ILE G CD1 
19371 N  N   . ASN G  210 ? 3.7365 2.5932 4.0250 -0.1253 -0.0619 0.0574  208  ASN G N   
19372 C  CA  . ASN G  210 ? 3.7897 2.6103 4.0631 -0.0604 -0.0617 0.0680  208  ASN G CA  
19373 C  C   . ASN G  210 ? 3.7965 2.6879 4.0348 -0.0430 -0.0470 0.1421  208  ASN G C   
19374 O  O   . ASN G  210 ? 3.7215 2.6604 3.9538 -0.0813 -0.0347 0.1924  208  ASN G O   
19375 C  CB  . ASN G  210 ? 3.6198 2.4715 3.8742 -0.0163 -0.0633 -0.0126 208  ASN G CB  
19376 C  CG  . ASN G  210 ? 3.5161 2.3163 3.7894 -0.0386 -0.0750 -0.0945 208  ASN G CG  
19377 O  OD1 . ASN G  210 ? 3.6299 2.3124 3.9385 -0.0355 -0.0865 -0.1149 208  ASN G OD1 
19378 N  ND2 . ASN G  210 ? 3.4184 2.3041 3.6652 -0.0600 -0.0731 -0.1429 208  ASN G ND2 
19379 N  N   . GLY G  211 ? 3.8083 2.7106 4.0245 0.0156  -0.0483 0.1465  209  GLY G N   
19380 C  CA  . GLY G  211 ? 3.6443 2.6185 3.8187 0.0363  -0.0383 0.2028  209  GLY G CA  
19381 C  C   . GLY G  211 ? 3.5752 2.4864 3.7478 0.0453  -0.0431 0.2839  209  GLY G C   
19382 O  O   . GLY G  211 ? 3.5266 2.4177 3.6916 0.0953  -0.0550 0.3010  209  GLY G O   
19383 N  N   . PHE G  212 ? 3.7481 2.6334 3.9292 -0.0034 -0.0342 0.3373  210  PHE G N   
19384 C  CA  . PHE G  212 ? 3.9283 2.7562 4.1001 -0.0032 -0.0348 0.4244  210  PHE G CA  
19385 C  C   . PHE G  212 ? 3.9900 2.6806 4.2182 -0.0206 -0.0489 0.4305  210  PHE G C   
19386 O  O   . PHE G  212 ? 3.9746 2.6341 4.2363 -0.0788 -0.0420 0.4376  210  PHE G O   
19387 C  CB  . PHE G  212 ? 4.0578 2.9507 4.2008 -0.0464 -0.0094 0.4851  210  PHE G CB  
19388 C  CG  . PHE G  212 ? 4.0256 3.0454 4.1168 -0.0332 0.0068  0.4724  210  PHE G CG  
19389 C  CD1 . PHE G  212 ? 3.9179 3.0114 4.0174 -0.0456 0.0136  0.4081  210  PHE G CD1 
19390 C  CD2 . PHE G  212 ? 4.0024 3.0642 4.0337 -0.0099 0.0144  0.5260  210  PHE G CD2 
19391 C  CE1 . PHE G  212 ? 3.7856 2.9841 3.8410 -0.0330 0.0287  0.3985  210  PHE G CE1 
19392 C  CE2 . PHE G  212 ? 3.8574 3.0252 3.8420 0.0011  0.0293  0.5096  210  PHE G CE2 
19393 C  CZ  . PHE G  212 ? 3.7656 2.9980 3.7655 -0.0102 0.0373  0.4470  210  PHE G CZ  
19394 N  N   . THR G  213 ? 4.1955 2.8038 4.4401 0.0300  -0.0695 0.4267  211  THR G N   
19395 C  CA  . THR G  213 ? 4.3538 2.8177 4.6549 0.0214  -0.0840 0.4253  211  THR G CA  
19396 C  C   . THR G  213 ? 4.4971 2.8785 4.7999 0.0031  -0.0845 0.5275  211  THR G C   
19397 O  O   . THR G  213 ? 4.5477 2.7988 4.9000 -0.0144 -0.0944 0.5377  211  THR G O   
19398 C  CB  . THR G  213 ? 4.2787 2.6863 4.6052 0.0888  -0.1038 0.3733  211  THR G CB  
19399 O  OG1 . THR G  213 ? 4.2531 2.6800 4.5527 0.1460  -0.1143 0.4279  211  THR G OG1 
19400 C  CG2 . THR G  213 ? 4.0749 2.5657 4.3961 0.1036  -0.0988 0.2745  211  THR G CG2 
19401 N  N   . THR G  214 ? 4.4707 2.9205 4.7179 0.0054  -0.0732 0.6024  212  THR G N   
19402 C  CA  . THR G  214 ? 4.4862 2.8716 4.7213 -0.0145 -0.0694 0.7069  212  THR G CA  
19403 C  C   . THR G  214 ? 4.3983 2.8434 4.6217 -0.0864 -0.0378 0.7461  212  THR G C   
19404 O  O   . THR G  214 ? 4.2398 2.8069 4.4380 -0.1014 -0.0193 0.7129  212  THR G O   
19405 C  CB  . THR G  214 ? 4.4337 2.8528 4.6067 0.0408  -0.0798 0.7694  212  THR G CB  
19406 O  OG1 . THR G  214 ? 4.4855 2.8980 4.6730 0.1102  -0.1064 0.7173  212  THR G OG1 
19407 C  CG2 . THR G  214 ? 4.4487 2.7651 4.6149 0.0343  -0.0854 0.8762  212  THR G CG2 
19408 N  N   . GLY G  215 ? 4.4296 2.7871 4.6762 -0.1301 -0.0305 0.8198  213  GLY G N   
19409 C  CA  . GLY G  215 ? 4.4156 2.8237 4.6620 -0.1998 0.0024  0.8693  213  GLY G CA  
19410 C  C   . GLY G  215 ? 4.4659 2.9379 4.6369 -0.1976 0.0261  0.9627  213  GLY G C   
19411 O  O   . GLY G  215 ? 4.4409 2.9708 4.6103 -0.2527 0.0600  1.0033  213  GLY G O   
19412 N  N   . ARG G  216 ? 4.4369 2.9061 4.5454 -0.1360 0.0096  0.9974  214  ARG G N   
19413 C  CA  . ARG G  216 ? 4.3356 2.8735 4.3575 -0.1319 0.0303  1.0789  214  ARG G CA  
19414 C  C   . ARG G  216 ? 4.2394 2.9318 4.2094 -0.1262 0.0525  1.0355  214  ARG G C   
19415 O  O   . ARG G  216 ? 4.1319 2.8957 4.0349 -0.1383 0.0812  1.0913  214  ARG G O   
19416 C  CB  . ARG G  216 ? 4.2535 2.7410 4.2235 -0.0681 -0.0012 1.1300  214  ARG G CB  
19417 C  CG  . ARG G  216 ? 4.2568 2.5828 4.2786 -0.0598 -0.0275 1.1736  214  ARG G CG  
19418 C  CD  . ARG G  216 ? 4.2042 2.4972 4.1748 0.0088  -0.0616 1.2282  214  ARG G CD  
19419 N  NE  . ARG G  216 ? 4.2538 2.3874 4.2679 0.0165  -0.0835 1.2910  214  ARG G NE  
19420 C  CZ  . ARG G  216 ? 4.2573 2.3381 4.2389 0.0721  -0.1158 1.3577  214  ARG G CZ  
19421 N  NH1 . ARG G  216 ? 4.2375 2.4188 4.1414 0.1211  -0.1318 1.3670  214  ARG G NH1 
19422 N  NH2 . ARG G  216 ? 4.3776 2.3039 4.4060 0.0784  -0.1345 1.4156  214  ARG G NH2 
19423 N  N   . ARG G  217 ? 4.2611 3.0022 4.2578 -0.1062 0.0409  0.9380  215  ARG G N   
19424 C  CA  . ARG G  217 ? 4.0663 2.9411 4.0230 -0.0958 0.0572  0.8871  215  ARG G CA  
19425 C  C   . ARG G  217 ? 4.0383 2.9651 3.9080 -0.0421 0.0469  0.9060  215  ARG G C   
19426 O  O   . ARG G  217 ? 3.8236 2.8474 3.6590 -0.0236 0.0532  0.8570  215  ARG G O   
19427 C  CB  . ARG G  217 ? 3.9733 2.9276 3.9297 -0.1519 0.1013  0.9093  215  ARG G CB  
19428 C  CG  . ARG G  217 ? 3.6453 2.7130 3.6045 -0.1523 0.1153  0.8353  215  ARG G CG  
19429 C  CD  . ARG G  217 ? 3.5764 2.7460 3.4971 -0.1780 0.1602  0.8709  215  ARG G CD  
19430 N  NE  . ARG G  217 ? 3.6611 2.8129 3.6262 -0.2384 0.1881  0.9289  215  ARG G NE  
19431 C  CZ  . ARG G  217 ? 3.6145 2.8492 3.5617 -0.2677 0.2332  0.9695  215  ARG G CZ  
19432 N  NH1 . ARG G  217 ? 3.5640 2.8969 3.4449 -0.2397 0.2549  0.9548  215  ARG G NH1 
19433 N  NH2 . ARG G  217 ? 3.5811 2.8004 3.5798 -0.3257 0.2585  1.0234  215  ARG G NH2 
19434 N  N   . GLY G  218 ? 4.0896 2.9511 3.9241 -0.0174 0.0283  0.9766  216  GLY G N   
19435 C  CA  . GLY G  218 ? 3.9669 2.8728 3.7185 0.0315  0.0109  1.0009  216  GLY G CA  
19436 C  C   . GLY G  218 ? 3.9463 2.8061 3.7187 0.0919  -0.0366 0.9759  216  GLY G C   
19437 O  O   . GLY G  218 ? 3.7817 2.6750 3.4927 0.1333  -0.0588 1.0008  216  GLY G O   
19438 N  N   . ASP G  219 ? 4.0412 2.8291 3.9000 0.0987  -0.0529 0.9251  217  ASP G N   
19439 C  CA  . ASP G  219 ? 3.9471 2.6988 3.8377 0.1599  -0.0933 0.8936  217  ASP G CA  
19440 C  C   . ASP G  219 ? 3.7069 2.5576 3.5984 0.1872  -0.0977 0.8043  217  ASP G C   
19441 O  O   . ASP G  219 ? 3.6420 2.5225 3.5227 0.2393  -0.1264 0.7939  217  ASP G O   
19442 C  CB  . ASP G  219 ? 3.9136 2.5390 3.8939 0.1585  -0.1057 0.8749  217  ASP G CB  
19443 C  CG  . ASP G  219 ? 3.8169 2.4080 3.8411 0.2257  -0.1421 0.8348  217  ASP G CG  
19444 O  OD1 . ASP G  219 ? 3.6798 2.3180 3.7372 0.2419  -0.1422 0.7452  217  ASP G OD1 
19445 O  OD2 . ASP G  219 ? 3.9056 2.4258 3.9328 0.2637  -0.1697 0.8956  217  ASP G OD2 
19446 N  N   . LEU G  220 ? 3.4581 2.3630 3.3657 0.1519  -0.0707 0.7426  218  LEU G N   
19447 C  CA  . LEU G  220 ? 3.3221 2.3133 3.2334 0.1729  -0.0719 0.6603  218  LEU G CA  
19448 C  C   . LEU G  220 ? 3.2669 2.3682 3.1018 0.1728  -0.0591 0.6656  218  LEU G C   
19449 O  O   . LEU G  220 ? 3.1499 2.3180 2.9770 0.2011  -0.0691 0.6152  218  LEU G O   
19450 C  CB  . LEU G  220 ? 3.2946 2.2892 3.2572 0.1380  -0.0528 0.5916  218  LEU G CB  
19451 C  CG  . LEU G  220 ? 3.1662 2.2277 3.1452 0.1596  -0.0550 0.5041  218  LEU G CG  
19452 C  CD1 . LEU G  220 ? 3.1730 2.2001 3.1878 0.2147  -0.0839 0.4772  218  LEU G CD1 
19453 C  CD2 . LEU G  220 ? 3.1598 2.2203 3.1799 0.1219  -0.0389 0.4463  218  LEU G CD2 
19454 N  N   . ALA G  221 ? 3.4018 2.5227 3.1814 0.1408  -0.0354 0.7233  219  ALA G N   
19455 C  CA  . ALA G  221 ? 3.3230 2.5415 3.0263 0.1398  -0.0193 0.7236  219  ALA G CA  
19456 C  C   . ALA G  221 ? 3.5423 2.7531 3.1722 0.1283  -0.0093 0.8111  219  ALA G C   
19457 O  O   . ALA G  221 ? 3.7994 2.9337 3.4440 0.1113  -0.0077 0.8728  219  ALA G O   
19458 C  CB  . ALA G  221 ? 3.2263 2.5090 2.9409 0.1053  0.0161  0.6742  219  ALA G CB  
19459 N  N   . THR G  222 ? 3.5613 2.8502 3.1082 0.1361  -0.0011 0.8155  220  THR G N   
19460 C  CA  . THR G  222 ? 3.7014 2.9966 3.1590 0.1301  0.0082  0.8936  220  THR G CA  
19461 C  C   . THR G  222 ? 3.7028 3.0174 3.1487 0.0803  0.0616  0.9215  220  THR G C   
19462 O  O   . THR G  222 ? 3.4676 2.8558 2.9009 0.0658  0.0930  0.8785  220  THR G O   
19463 C  CB  . THR G  222 ? 3.6486 3.0199 3.0182 0.1580  -0.0061 0.8786  220  THR G CB  
19464 O  OG1 . THR G  222 ? 3.8335 3.2214 3.1030 0.1465  0.0116  0.9475  220  THR G OG1 
19465 C  CG2 . THR G  222 ? 3.4261 2.8754 2.7997 0.1516  0.0155  0.7973  220  THR G CG2 
19466 N  N   . ILE G  223 ? 3.9889 3.2381 3.4440 0.0546  0.0725  0.9958  221  ILE G N   
19467 C  CA  . ILE G  223 ? 4.0273 3.2961 3.4769 0.0048  0.1241  1.0365  221  ILE G CA  
19468 C  C   . ILE G  223 ? 4.0926 3.3638 3.4399 0.0032  0.1367  1.1258  221  ILE G C   
19469 O  O   . ILE G  223 ? 4.1309 3.3483 3.4410 0.0308  0.1001  1.1753  221  ILE G O   
19470 C  CB  . ILE G  223 ? 4.0640 3.2556 3.6149 -0.0348 0.1310  1.0518  221  ILE G CB  
19471 C  CG1 . ILE G  223 ? 3.8518 3.0299 3.4931 -0.0276 0.1098  0.9637  221  ILE G CG1 
19472 C  CG2 . ILE G  223 ? 4.1019 3.3345 3.6642 -0.0900 0.1859  1.0845  221  ILE G CG2 
19473 C  CD1 . ILE G  223 ? 3.6671 2.9421 3.3183 -0.0365 0.1343  0.8933  221  ILE G CD1 
19474 N  N   . HIS G  224 ? 4.1389 3.4774 3.4393 -0.0270 0.1895  1.1468  222  HIS G N   
19475 C  CA  . HIS G  224 ? 4.3441 3.6932 3.5455 -0.0390 0.2160  1.2345  222  HIS G CA  
19476 C  C   . HIS G  224 ? 4.4881 3.8386 3.5771 0.0049  0.1778  1.2626  222  HIS G C   
19477 O  O   . HIS G  224 ? 4.6112 3.9577 3.6096 -0.0014 0.1905  1.3441  222  HIS G O   
19478 C  CB  . HIS G  224 ? 4.4595 3.7252 3.7071 -0.0783 0.2284  1.3205  222  HIS G CB  
19479 C  CG  . HIS G  224 ? 4.4977 3.6494 3.7879 -0.0564 0.1732  1.3477  222  HIS G CG  
19480 N  ND1 . HIS G  224 ? 4.6013 3.7171 3.8140 -0.0170 0.1333  1.4005  222  HIS G ND1 
19481 C  CD2 . HIS G  224 ? 4.4076 3.4735 3.8110 -0.0655 0.1505  1.3265  222  HIS G CD2 
19482 C  CE1 . HIS G  224 ? 4.5943 3.6064 3.8774 0.0003  0.0901  1.4131  222  HIS G CE1 
19483 N  NE2 . HIS G  224 ? 4.5115 3.4885 3.9084 -0.0288 0.1012  1.3661  222  HIS G NE2 
19484 N  N   . GLY G  225 ? 4.3085 3.6700 3.4008 0.0474  0.1307  1.1985  223  GLY G N   
19485 C  CA  . GLY G  225 ? 4.3224 3.6993 3.3179 0.0882  0.0887  1.2151  223  GLY G CA  
19486 C  C   . GLY G  225 ? 4.1247 3.5961 3.0550 0.1045  0.0936  1.1415  223  GLY G C   
19487 O  O   . GLY G  225 ? 3.9209 3.4415 2.8832 0.0886  0.1298  1.0785  223  GLY G O   
19488 N  N   . MET G  226 ? 4.0365 3.5311 2.8741 0.1368  0.0536  1.1519  224  MET G N   
19489 C  CA  . MET G  226 ? 3.9105 3.4837 2.6907 0.1533  0.0476  1.0770  224  MET G CA  
19490 C  C   . MET G  226 ? 3.9243 3.4994 2.8060 0.1728  0.0151  0.9925  224  MET G C   
19491 O  O   . MET G  226 ? 3.9095 3.4274 2.8938 0.1793  -0.0066 0.9933  224  MET G O   
19492 C  CB  . MET G  226 ? 4.0121 3.6121 2.6652 0.1785  0.0083  1.1106  224  MET G CB  
19493 C  CG  . MET G  226 ? 4.1430 3.6929 2.8235 0.2117  -0.0604 1.1541  224  MET G CG  
19494 S  SD  . MET G  226 ? 4.5146 4.1112 3.0435 0.2408  -0.1135 1.1913  224  MET G SD  
19495 C  CE  . MET G  226 ? 4.2185 3.9031 2.7308 0.2483  -0.1233 1.0699  224  MET G CE  
19496 N  N   . ASN G  227 ? 4.1407 3.7807 2.9911 0.1815  0.0138  0.9181  225  ASN G N   
19497 C  CA  . ASN G  227 ? 4.0728 3.7271 3.0112 0.1940  -0.0058 0.8345  225  ASN G CA  
19498 C  C   . ASN G  227 ? 3.9227 3.5521 2.9700 0.1718  0.0293  0.8071  225  ASN G C   
19499 O  O   . ASN G  227 ? 3.7461 3.3634 2.8835 0.1820  0.0092  0.7583  225  ASN G O   
19500 C  CB  . ASN G  227 ? 4.0991 3.7324 3.0812 0.2287  -0.0719 0.8348  225  ASN G CB  
19501 C  CG  . ASN G  227 ? 4.2590 3.9284 3.1402 0.2514  -0.1158 0.8573  225  ASN G CG  
19502 O  OD1 . ASN G  227 ? 4.3439 4.0633 3.1231 0.2423  -0.1005 0.8423  225  ASN G OD1 
19503 N  ND2 . ASN G  227 ? 4.2918 3.9369 3.2013 0.2825  -0.1721 0.8914  225  ASN G ND2 
19504 N  N   . ARG G  228 ? 3.9599 3.5876 2.9986 0.1407  0.0815  0.8386  226  ARG G N   
19505 C  CA  . ARG G  228 ? 3.7859 3.3950 2.9248 0.1150  0.1124  0.8211  226  ARG G CA  
19506 C  C   . ARG G  228 ? 3.6642 3.3260 2.8347 0.1140  0.1309  0.7380  226  ARG G C   
19507 O  O   . ARG G  228 ? 3.7495 3.4600 2.8548 0.1268  0.1325  0.7012  226  ARG G O   
19508 C  CB  . ARG G  228 ? 3.7102 3.3151 2.8324 0.0802  0.1625  0.8832  226  ARG G CB  
19509 C  CG  . ARG G  228 ? 3.5486 3.2217 2.5743 0.0734  0.2071  0.8841  226  ARG G CG  
19510 C  CD  . ARG G  228 ? 3.5553 3.2321 2.5744 0.0381  0.2606  0.9491  226  ARG G CD  
19511 N  NE  . ARG G  228 ? 3.6617 3.4079 2.5856 0.0357  0.3084  0.9475  226  ARG G NE  
19512 C  CZ  . ARG G  228 ? 3.8317 3.6029 2.7303 0.0082  0.3640  1.0014  226  ARG G CZ  
19513 N  NH1 . ARG G  228 ? 3.7774 3.5076 2.7428 -0.0237 0.3758  1.0636  226  ARG G NH1 
19514 N  NH2 . ARG G  228 ? 3.9655 3.8026 2.7744 0.0116  0.4095  0.9915  226  ARG G NH2 
19515 N  N   . PRO G  229 ? 3.4527 3.1023 2.7212 0.0984  0.1429  0.7075  227  PRO G N   
19516 C  CA  . PRO G  229 ? 3.4353 3.1301 2.7380 0.0995  0.1563  0.6338  227  PRO G CA  
19517 C  C   . PRO G  229 ? 3.3414 3.0963 2.5811 0.0936  0.2003  0.6211  227  PRO G C   
19518 O  O   . PRO G  229 ? 3.2576 3.0274 2.4745 0.0740  0.2407  0.6628  227  PRO G O   
19519 C  CB  . PRO G  229 ? 3.4584 3.1297 2.8641 0.0764  0.1671  0.6247  227  PRO G CB  
19520 C  CG  . PRO G  229 ? 3.4351 3.0333 2.8741 0.0772  0.1363  0.6666  227  PRO G CG  
19521 C  CD  . PRO G  229 ? 3.3844 2.9698 2.7384 0.0835  0.1332  0.7339  227  PRO G CD  
19522 N  N   . PHE G  230 ? 3.2215 3.0104 2.4352 0.1110  0.1938  0.5621  228  PHE G N   
19523 C  CA  . PHE G  230 ? 3.1845 3.0225 2.3387 0.1117  0.2326  0.5376  228  PHE G CA  
19524 C  C   . PHE G  230 ? 2.9216 2.7807 2.1260 0.1177  0.2359  0.4685  228  PHE G C   
19525 O  O   . PHE G  230 ? 2.8979 2.7404 2.1528 0.1254  0.2014  0.4367  228  PHE G O   
19526 C  CB  . PHE G  230 ? 3.3400 3.1909 2.3778 0.1278  0.2189  0.5407  228  PHE G CB  
19527 C  CG  . PHE G  230 ? 3.3543 3.2039 2.3846 0.1473  0.1703  0.4927  228  PHE G CG  
19528 C  CD1 . PHE G  230 ? 3.4472 3.2679 2.5050 0.1587  0.1188  0.5100  228  PHE G CD1 
19529 C  CD2 . PHE G  230 ? 3.2844 3.1621 2.2864 0.1542  0.1770  0.4306  228  PHE G CD2 
19530 C  CE1 . PHE G  230 ? 3.4327 3.2642 2.4941 0.1752  0.0758  0.4668  228  PHE G CE1 
19531 C  CE2 . PHE G  230 ? 3.2867 3.1672 2.2889 0.1663  0.1333  0.3879  228  PHE G CE2 
19532 C  CZ  . PHE G  230 ? 3.3367 3.2000 2.3709 0.1761  0.0830  0.4064  228  PHE G CZ  
19533 N  N   . LEU G  231 ? 2.7575 2.6540 1.9475 0.1158  0.2801  0.4474  229  LEU G N   
19534 C  CA  . LEU G  231 ? 2.6935 2.6078 1.9280 0.1222  0.2887  0.3896  229  LEU G CA  
19535 C  C   . LEU G  231 ? 2.6923 2.6164 1.8509 0.1394  0.2856  0.3446  229  LEU G C   
19536 O  O   . LEU G  231 ? 2.7201 2.6658 1.8124 0.1443  0.3206  0.3415  229  LEU G O   
19537 C  CB  . LEU G  231 ? 2.6627 2.6107 1.9451 0.1122  0.3375  0.3955  229  LEU G CB  
19538 C  CG  . LEU G  231 ? 2.6935 2.6602 2.0248 0.1213  0.3486  0.3448  229  LEU G CG  
19539 C  CD1 . LEU G  231 ? 2.7756 2.7195 2.1766 0.1179  0.3098  0.3232  229  LEU G CD1 
19540 C  CD2 . LEU G  231 ? 2.7182 2.7277 2.0988 0.1148  0.3953  0.3585  229  LEU G CD2 
19541 N  N   . LEU G  232 ? 2.7555 2.6649 1.9261 0.1472  0.2454  0.3069  230  LEU G N   
19542 C  CA  . LEU G  232 ? 2.7675 2.6820 1.8755 0.1578  0.2360  0.2601  230  LEU G CA  
19543 C  C   . LEU G  232 ? 2.7154 2.6385 1.8485 0.1615  0.2685  0.2150  230  LEU G C   
19544 O  O   . LEU G  232 ? 2.6651 2.5855 1.8789 0.1588  0.2678  0.2017  230  LEU G O   
19545 C  CB  . LEU G  232 ? 2.8193 2.7220 1.9444 0.1614  0.1818  0.2393  230  LEU G CB  
19546 C  CG  . LEU G  232 ? 2.8775 2.7867 1.9378 0.1662  0.1598  0.1956  230  LEU G CG  
19547 C  CD1 . LEU G  232 ? 3.1534 3.0710 2.1047 0.1697  0.1568  0.2184  230  LEU G CD1 
19548 C  CD2 . LEU G  232 ? 2.8222 2.7316 1.9286 0.1673  0.1094  0.1765  230  LEU G CD2 
19549 N  N   . LEU G  233 ? 3.0599 2.9911 2.1208 0.1695  0.2966  0.1914  231  LEU G N   
19550 C  CA  . LEU G  233 ? 3.2422 3.1755 2.3225 0.1784  0.3316  0.1511  231  LEU G CA  
19551 C  C   . LEU G  233 ? 3.4103 3.3231 2.4370 0.1835  0.3155  0.0938  231  LEU G C   
19552 O  O   . LEU G  233 ? 3.6141 3.5250 2.5569 0.1822  0.2948  0.0858  231  LEU G O   
19553 C  CB  . LEU G  233 ? 3.4228 3.3822 2.4759 0.1862  0.3891  0.1677  231  LEU G CB  
19554 C  CG  . LEU G  233 ? 3.3190 3.3053 2.4244 0.1759  0.4114  0.2259  231  LEU G CG  
19555 C  CD1 . LEU G  233 ? 3.2674 3.2896 2.3356 0.1836  0.4712  0.2400  231  LEU G CD1 
19556 C  CD2 . LEU G  233 ? 3.1651 3.1555 2.3849 0.1703  0.4065  0.2282  231  LEU G CD2 
19557 N  N   . MET G  234 ? 3.1927 3.0894 2.2681 0.1873  0.3227  0.0554  232  MET G N   
19558 C  CA  . MET G  234 ? 3.0453 2.9142 2.0818 0.1881  0.3114  -0.0017 232  MET G CA  
19559 C  C   . MET G  234 ? 2.9858 2.8388 2.0467 0.2031  0.3553  -0.0299 232  MET G C   
19560 O  O   . MET G  234 ? 2.9242 2.7701 2.0660 0.2040  0.3576  -0.0288 232  MET G O   
19561 C  CB  . MET G  234 ? 2.9721 2.8293 2.0557 0.1738  0.2638  -0.0176 232  MET G CB  
19562 C  CG  . MET G  234 ? 3.0042 2.8798 2.0838 0.1649  0.2192  0.0122  232  MET G CG  
19563 S  SD  . MET G  234 ? 3.0351 2.9104 2.1901 0.1518  0.1722  -0.0051 232  MET G SD  
19564 C  CE  . MET G  234 ? 3.0648 2.9639 2.2134 0.1528  0.1291  0.0374  232  MET G CE  
19565 N  N   . ALA G  235 ? 3.1412 2.9889 2.1306 0.2172  0.3904  -0.0544 233  ALA G N   
19566 C  CA  . ALA G  235 ? 3.1011 2.9344 2.1135 0.2389  0.4373  -0.0795 233  ALA G CA  
19567 C  C   . ALA G  235 ? 3.2464 3.0341 2.1856 0.2446  0.4421  -0.1446 233  ALA G C   
19568 O  O   . ALA G  235 ? 3.5191 3.2962 2.3820 0.2300  0.4106  -0.1686 233  ALA G O   
19569 C  CB  . ALA G  235 ? 3.1054 2.9816 2.1162 0.2561  0.4895  -0.0471 233  ALA G CB  
19570 N  N   . THR G  236 ? 3.2230 2.9822 2.1884 0.2669  0.4802  -0.1745 234  THR G N   
19571 C  CA  . THR G  236 ? 3.3593 3.0621 2.2629 0.2742  0.4897  -0.2421 234  THR G CA  
19572 C  C   . THR G  236 ? 3.6594 3.3732 2.4910 0.3016  0.5447  -0.2621 234  THR G C   
19573 O  O   . THR G  236 ? 3.7818 3.5267 2.6625 0.3275  0.5917  -0.2368 234  THR G O   
19574 C  CB  . THR G  236 ? 3.0994 2.7490 2.0786 0.2828  0.4951  -0.2653 234  THR G CB  
19575 O  OG1 . THR G  236 ? 3.0357 2.6751 2.0681 0.2541  0.4459  -0.2527 234  THR G OG1 
19576 C  CG2 . THR G  236 ? 3.1761 2.7567 2.0957 0.2923  0.5109  -0.3372 234  THR G CG2 
19577 N  N   . PRO G  237 ? 3.5020 3.1969 2.2187 0.2970  0.5412  -0.3083 235  PRO G N   
19578 C  CA  . PRO G  237 ? 3.4535 3.1623 2.0891 0.3238  0.5979  -0.3309 235  PRO G CA  
19579 C  C   . PRO G  237 ? 3.4477 3.1197 2.1277 0.3608  0.6514  -0.3682 235  PRO G C   
19580 O  O   . PRO G  237 ? 3.4037 3.0187 2.1499 0.3628  0.6386  -0.3917 235  PRO G O   
19581 C  CB  . PRO G  237 ? 3.5149 3.1967 2.0179 0.3066  0.5701  -0.3853 235  PRO G CB  
19582 C  CG  . PRO G  237 ? 3.4124 3.1015 1.9312 0.2696  0.4974  -0.3610 235  PRO G CG  
19583 C  CD  . PRO G  237 ? 3.3654 3.0365 2.0186 0.2655  0.4831  -0.3390 235  PRO G CD  
19584 N  N   . LEU G  238 ? 3.4560 3.1634 2.1014 0.3919  0.7143  -0.3702 236  LEU G N   
19585 C  CA  . LEU G  238 ? 3.4335 3.1104 2.1168 0.4350  0.7707  -0.4090 236  LEU G CA  
19586 C  C   . LEU G  238 ? 3.5396 3.1243 2.1486 0.4396  0.7670  -0.4983 236  LEU G C   
19587 O  O   . LEU G  238 ? 3.6534 3.1801 2.3133 0.4693  0.7937  -0.5353 236  LEU G O   
19588 C  CB  . LEU G  238 ? 3.3966 3.1431 2.0567 0.4672  0.8424  -0.3932 236  LEU G CB  
19589 C  CG  . LEU G  238 ? 3.2094 3.0510 1.9493 0.4643  0.8589  -0.3077 236  LEU G CG  
19590 C  CD1 . LEU G  238 ? 3.1433 3.0318 1.8078 0.4275  0.8318  -0.2627 236  LEU G CD1 
19591 C  CD2 . LEU G  238 ? 3.0708 2.9672 1.8440 0.5081  0.9396  -0.3051 236  LEU G CD2 
19592 N  N   . GLU G  239 ? 3.4201 2.9888 1.9101 0.4101  0.7319  -0.5334 237  GLU G N   
19593 C  CA  . GLU G  239 ? 3.4091 2.8898 1.8231 0.4053  0.7199  -0.6229 237  GLU G CA  
19594 C  C   . GLU G  239 ? 3.4313 2.8354 1.9332 0.3876  0.6782  -0.6393 237  GLU G C   
19595 O  O   . GLU G  239 ? 3.3929 2.7082 1.8787 0.3952  0.6857  -0.7096 237  GLU G O   
19596 C  CB  . GLU G  239 ? 3.4630 2.9586 1.7393 0.3711  0.6785  -0.6464 237  GLU G CB  
19597 C  CG  . GLU G  239 ? 3.5017 3.0767 1.6829 0.3833  0.7159  -0.6179 237  GLU G CG  
19598 C  CD  . GLU G  239 ? 3.5010 3.1204 1.5992 0.3445  0.6574  -0.5863 237  GLU G CD  
19599 O  OE1 . GLU G  239 ? 3.5201 3.1192 1.6532 0.3105  0.5888  -0.5816 237  GLU G OE1 
19600 O  OE2 . GLU G  239 ? 3.5219 3.1987 1.5226 0.3490  0.6808  -0.5633 237  GLU G OE2 
19601 N  N   . ARG G  240 ? 3.5882 3.0222 2.1820 0.3636  0.6365  -0.5756 238  ARG G N   
19602 C  CA  . ARG G  240 ? 3.5522 2.9233 2.2307 0.3445  0.6002  -0.5817 238  ARG G CA  
19603 C  C   . ARG G  240 ? 3.3968 2.7403 2.1841 0.3822  0.6402  -0.5637 238  ARG G C   
19604 O  O   . ARG G  240 ? 3.4979 2.7527 2.3065 0.3929  0.6494  -0.6097 238  ARG G O   
19605 C  CB  . ARG G  240 ? 3.3199 2.7384 2.0465 0.3050  0.5415  -0.5241 238  ARG G CB  
19606 C  CG  . ARG G  240 ? 3.3308 2.7961 1.9650 0.2748  0.5008  -0.5222 238  ARG G CG  
19607 C  CD  . ARG G  240 ? 3.5659 2.9747 2.1198 0.2470  0.4655  -0.5969 238  ARG G CD  
19608 N  NE  . ARG G  240 ? 3.7001 3.1613 2.1676 0.2204  0.4209  -0.5907 238  ARG G NE  
19609 C  CZ  . ARG G  240 ? 3.9051 3.3868 2.2470 0.2282  0.4341  -0.6164 238  ARG G CZ  
19610 N  NH1 . ARG G  240 ? 3.8461 3.3019 2.1346 0.2623  0.4953  -0.6553 238  ARG G NH1 
19611 N  NH2 . ARG G  240 ? 4.0227 3.5534 2.2912 0.2041  0.3867  -0.6023 238  ARG G NH2 
19612 N  N   . ALA G  241 ? 3.1428 2.5607 2.0018 0.4021  0.6621  -0.4954 239  ALA G N   
19613 C  CA  . ALA G  241 ? 3.1030 2.5100 2.0747 0.4363  0.6903  -0.4676 239  ALA G CA  
19614 C  C   . ALA G  241 ? 3.1956 2.5470 2.1552 0.4849  0.7472  -0.5220 239  ALA G C   
19615 O  O   . ALA G  241 ? 3.3804 2.6594 2.4035 0.5044  0.7536  -0.5362 239  ALA G O   
19616 C  CB  . ALA G  241 ? 3.0072 2.5155 2.0466 0.4472  0.7045  -0.3915 239  ALA G CB  
19617 N  N   . GLN G  242 ? 3.1546 2.5369 2.0322 0.5066  0.7906  -0.5521 240  GLN G N   
19618 C  CA  . GLN G  242 ? 3.2108 2.5428 2.0685 0.5566  0.8501  -0.6119 240  GLN G CA  
19619 C  C   . GLN G  242 ? 3.3321 2.5444 2.1176 0.5429  0.8325  -0.6983 240  GLN G C   
19620 O  O   . GLN G  242 ? 3.3906 2.5132 2.2244 0.5689  0.8481  -0.7320 240  GLN G O   
19621 C  CB  . GLN G  242 ? 3.3692 2.7771 2.1520 0.5813  0.9052  -0.6196 240  GLN G CB  
19622 C  CG  . GLN G  242 ? 3.2147 2.7418 2.0717 0.5913  0.9269  -0.5362 240  GLN G CG  
19623 C  CD  . GLN G  242 ? 3.2334 2.8375 2.0130 0.6097  0.9841  -0.5401 240  GLN G CD  
19624 O  OE1 . GLN G  242 ? 3.3740 2.9426 2.0395 0.6211  1.0120  -0.6087 240  GLN G OE1 
19625 N  NE2 . GLN G  242 ? 3.1374 2.8480 1.9762 0.6101  1.0025  -0.4668 240  GLN G NE2 
19626 N  N   . ALA G  252 ? 3.2350 2.0186 3.5829 0.7403  0.0770  -0.2809 250  ALA G N   
19627 C  CA  . ALA G  252 ? 3.3150 2.1063 3.6474 0.7111  0.0655  -0.2749 250  ALA G CA  
19628 C  C   . ALA G  252 ? 3.2622 2.0760 3.6076 0.6893  0.0712  -0.2893 250  ALA G C   
19629 O  O   . ALA G  252 ? 3.0646 1.8671 3.4268 0.6737  0.0745  -0.2803 250  ALA G O   
19630 C  CB  . ALA G  252 ? 3.2372 2.0006 3.5711 0.7051  0.0612  -0.2412 250  ALA G CB  
19631 N  N   . LEU G  253 ? 3.2339 2.0786 3.5740 0.6884  0.0678  -0.3131 251  LEU G N   
19632 C  CA  . LEU G  253 ? 3.0048 1.8761 3.3637 0.6700  0.0674  -0.3263 251  LEU G CA  
19633 C  C   . LEU G  253 ? 2.8095 1.6885 3.1565 0.6403  0.0503  -0.3212 251  LEU G C   
19634 O  O   . LEU G  253 ? 2.4941 1.3695 2.8183 0.6361  0.0363  -0.3139 251  LEU G O   
19635 C  CB  . LEU G  253 ? 2.6931 1.5954 3.0563 0.6863  0.0697  -0.3502 251  LEU G CB  
19636 C  CG  . LEU G  253 ? 2.6786 1.5853 3.0576 0.7218  0.0886  -0.3612 251  LEU G CG  
19637 C  CD1 . LEU G  253 ? 2.6742 1.6164 3.0559 0.7426  0.0932  -0.3859 251  LEU G CD1 
19638 C  CD2 . LEU G  253 ? 2.7665 1.6736 3.1988 0.7195  0.1021  -0.3559 251  LEU G CD2 
19639 N  N   . ASP G  254 ? 2.9368 1.8309 3.3074 0.6191  0.0484  -0.3280 252  ASP G N   
19640 C  CA  . ASP G  254 ? 2.9022 1.8063 3.2688 0.5917  0.0334  -0.3259 252  ASP G CA  
19641 C  C   . ASP G  254 ? 2.7997 1.7403 3.1741 0.5792  0.0158  -0.3421 252  ASP G C   
19642 O  O   . ASP G  254 ? 2.4991 1.4498 2.8613 0.5928  0.0095  -0.3494 252  ASP G O   
19643 C  CB  . ASP G  254 ? 3.0415 1.9326 3.4313 0.5734  0.0402  -0.3246 252  ASP G CB  
19644 C  CG  . ASP G  254 ? 2.9554 1.8557 3.3903 0.5696  0.0494  -0.3400 252  ASP G CG  
19645 O  OD1 . ASP G  254 ? 3.1058 2.0327 3.5557 0.5830  0.0496  -0.3523 252  ASP G OD1 
19646 O  OD2 . ASP G  254 ? 2.7792 1.6605 3.2412 0.5527  0.0573  -0.3406 252  ASP G OD2 
19647 N  N   . THR G  255 ? 2.6587 1.6167 3.0556 0.5537  0.0064  -0.3490 253  THR G N   
19648 C  CA  . THR G  255 ? 2.3717 1.3648 2.7833 0.5403  -0.0151 -0.3624 253  THR G CA  
19649 C  C   . THR G  255 ? 2.3818 1.3964 2.8225 0.5535  -0.0116 -0.3766 253  THR G C   
19650 O  O   . THR G  255 ? 2.2236 1.2615 2.6689 0.5550  -0.0287 -0.3846 253  THR G O   
19651 C  CB  . THR G  255 ? 2.1891 1.1965 2.6253 0.5102  -0.0257 -0.3685 253  THR G CB  
19652 O  OG1 . THR G  255 ? 2.2185 1.2202 2.6904 0.5013  -0.0105 -0.3769 253  THR G OG1 
19653 C  CG2 . THR G  255 ? 2.1762 1.1668 2.5883 0.5035  -0.0271 -0.3554 253  THR G CG2 
19654 N  N   . ASN G  256 ? 2.7144 1.7226 3.1796 0.5657  0.0092  -0.3795 254  ASN G N   
19655 C  CA  . ASN G  256 ? 2.6447 1.6828 3.1518 0.5820  0.0145  -0.3938 254  ASN G CA  
19656 C  C   . ASN G  256 ? 2.5980 1.6381 3.0765 0.6169  0.0191  -0.3953 254  ASN G C   
19657 O  O   . ASN G  256 ? 2.5849 1.6554 3.0954 0.6376  0.0237  -0.4071 254  ASN G O   
19658 C  CB  . ASN G  256 ? 2.9208 1.9552 3.4751 0.5834  0.0358  -0.3977 254  ASN G CB  
19659 C  CG  . ASN G  256 ? 2.8499 1.8748 3.4375 0.5457  0.0346  -0.4005 254  ASN G CG  
19660 O  OD1 . ASN G  256 ? 2.8983 1.9408 3.4982 0.5212  0.0174  -0.4081 254  ASN G OD1 
19661 N  ND2 . ASN G  256 ? 2.7378 1.7314 3.3418 0.5399  0.0533  -0.3950 254  ASN G ND2 
19662 N  N   . TYR G  257 ? 2.5451 1.5559 2.9708 0.6240  0.0185  -0.3854 255  TYR G N   
19663 C  CA  . TYR G  257 ? 2.7530 1.7577 3.1497 0.6530  0.0230  -0.3911 255  TYR G CA  
19664 C  C   . TYR G  257 ? 2.7112 1.7034 3.0709 0.6385  -0.0016 -0.3885 255  TYR G C   
19665 O  O   . TYR G  257 ? 2.5687 1.5591 2.9104 0.6526  -0.0097 -0.3986 255  TYR G O   
19666 C  CB  . TYR G  257 ? 2.9939 1.9738 3.3742 0.6762  0.0443  -0.3875 255  TYR G CB  
19667 C  CG  . TYR G  257 ? 3.0424 2.0069 3.3845 0.6985  0.0438  -0.3963 255  TYR G CG  
19668 C  CD1 . TYR G  257 ? 2.9834 1.9647 3.3289 0.7299  0.0550  -0.4151 255  TYR G CD1 
19669 C  CD2 . TYR G  257 ? 3.0040 1.9387 3.3089 0.6893  0.0298  -0.3890 255  TYR G CD2 
19670 C  CE1 . TYR G  257 ? 3.1223 2.0843 3.4279 0.7493  0.0525  -0.4297 255  TYR G CE1 
19671 C  CE2 . TYR G  257 ? 2.8958 1.8124 3.1629 0.7072  0.0219  -0.4034 255  TYR G CE2 
19672 C  CZ  . TYR G  257 ? 3.1194 2.0462 3.3828 0.7362  0.0335  -0.4254 255  TYR G CZ  
19673 O  OH  . TYR G  257 ? 3.3198 2.2215 3.5344 0.7548  0.0242  -0.4452 255  TYR G OH  
19674 N  N   . CYS G  258 ? 2.6091 1.5925 2.9599 0.6118  -0.0146 -0.3763 256  CYS G N   
19675 C  CA  . CYS G  258 ? 2.5789 1.5545 2.9010 0.5979  -0.0420 -0.3739 256  CYS G CA  
19676 C  C   . CYS G  258 ? 2.4534 1.4532 2.7891 0.5807  -0.0691 -0.3810 256  CYS G C   
19677 O  O   . CYS G  258 ? 2.2613 1.2541 2.5735 0.5736  -0.0969 -0.3831 256  CYS G O   
19678 C  CB  . CYS G  258 ? 2.4764 1.4405 2.7912 0.5816  -0.0456 -0.3581 256  CYS G CB  
19679 S  SG  . CYS G  258 ? 2.6004 1.5308 2.8796 0.5999  -0.0457 -0.3510 256  CYS G SG  
19680 N  N   . PHE G  259 ? 2.4896 1.5164 2.8653 0.5739  -0.0661 -0.3860 257  PHE G N   
19681 C  CA  . PHE G  259 ? 2.4801 1.5328 2.8783 0.5587  -0.0943 -0.3930 257  PHE G CA  
19682 C  C   . PHE G  259 ? 2.5921 1.6575 3.0074 0.5820  -0.0936 -0.4034 257  PHE G C   
19683 O  O   . PHE G  259 ? 2.5388 1.6163 2.9642 0.5766  -0.1206 -0.4079 257  PHE G O   
19684 C  CB  . PHE G  259 ? 2.3376 1.4152 2.7778 0.5327  -0.0978 -0.3945 257  PHE G CB  
19685 C  CG  . PHE G  259 ? 2.3648 1.4356 2.7915 0.5098  -0.1058 -0.3864 257  PHE G CG  
19686 C  CD1 . PHE G  259 ? 2.3500 1.3928 2.7478 0.5169  -0.0867 -0.3742 257  PHE G CD1 
19687 C  CD2 . PHE G  259 ? 2.5975 1.6923 3.0463 0.4842  -0.1325 -0.3915 257  PHE G CD2 
19688 C  CE1 . PHE G  259 ? 2.1384 1.1776 2.5292 0.5018  -0.0928 -0.3660 257  PHE G CE1 
19689 C  CE2 . PHE G  259 ? 2.4531 1.5454 2.8936 0.4683  -0.1379 -0.3857 257  PHE G CE2 
19690 C  CZ  . PHE G  259 ? 2.2695 1.3341 2.6810 0.4785  -0.1172 -0.3725 257  PHE G CZ  
19691 N  N   . SER G  260 ? 2.7782 1.8427 3.2011 0.6103  -0.0642 -0.4070 258  SER G N   
19692 C  CA  . SER G  260 ? 2.8374 1.9179 3.2800 0.6409  -0.0581 -0.4168 258  SER G CA  
19693 C  C   . SER G  260 ? 2.8942 1.9436 3.2905 0.6675  -0.0526 -0.4222 258  SER G C   
19694 O  O   . SER G  260 ? 2.9927 2.0501 3.3992 0.6952  -0.0492 -0.4309 258  SER G O   
19695 C  CB  . SER G  260 ? 2.9000 2.0068 3.3870 0.6608  -0.0303 -0.4213 258  SER G CB  
19696 O  OG  . SER G  260 ? 2.9677 2.0514 3.4297 0.6728  -0.0045 -0.4183 258  SER G OG  
19697 N  N   . SER G  261 ? 2.9349 1.9496 3.2848 0.6611  -0.0525 -0.4193 259  SER G N   
19698 C  CA  . SER G  261 ? 2.9393 1.9203 3.2451 0.6828  -0.0509 -0.4305 259  SER G CA  
19699 C  C   . SER G  261 ? 2.9270 1.8771 3.1896 0.6590  -0.0835 -0.4282 259  SER G C   
19700 O  O   . SER G  261 ? 2.8643 1.8209 3.1304 0.6304  -0.0985 -0.4155 259  SER G O   
19701 C  CB  . SER G  261 ? 2.9868 1.9580 3.2819 0.7081  -0.0187 -0.4359 259  SER G CB  
19702 O  OG  . SER G  261 ? 3.0978 2.0598 3.3867 0.6895  -0.0162 -0.4226 259  SER G OG  
19703 N  N   . THR G  262 ? 3.0604 1.9759 3.2815 0.6736  -0.0957 -0.4427 260  THR G N   
19704 C  CA  . THR G  262 ? 3.2332 2.1135 3.4065 0.6557  -0.1325 -0.4447 260  THR G CA  
19705 C  C   . THR G  262 ? 3.2288 2.0765 3.3580 0.6673  -0.1255 -0.4521 260  THR G C   
19706 O  O   . THR G  262 ? 3.2773 2.0932 3.3689 0.6926  -0.1196 -0.4726 260  THR G O   
19707 C  CB  . THR G  262 ? 3.2469 2.0999 3.3962 0.6628  -0.1578 -0.4581 260  THR G CB  
19708 O  OG1 . THR G  262 ? 3.1439 2.0290 3.3386 0.6555  -0.1664 -0.4506 260  THR G OG1 
19709 C  CG2 . THR G  262 ? 3.2456 2.0594 3.3425 0.6425  -0.2026 -0.4602 260  THR G CG2 
19710 N  N   . GLU G  263 ? 2.8951 1.7490 3.0275 0.6511  -0.1274 -0.4367 261  GLU G N   
19711 C  CA  . GLU G  263 ? 2.7740 1.5986 2.8681 0.6631  -0.1250 -0.4402 261  GLU G CA  
19712 C  C   . GLU G  263 ? 2.6943 1.4768 2.7272 0.6524  -0.1703 -0.4453 261  GLU G C   
19713 O  O   . GLU G  263 ? 2.5538 1.3424 2.5897 0.6274  -0.2023 -0.4352 261  GLU G O   
19714 C  CB  . GLU G  263 ? 2.7662 1.6126 2.8950 0.6554  -0.1061 -0.4184 261  GLU G CB  
19715 C  CG  . GLU G  263 ? 3.0364 1.8559 3.1354 0.6747  -0.0992 -0.4192 261  GLU G CG  
19716 C  CD  . GLU G  263 ? 3.2679 2.0854 3.3642 0.7082  -0.0672 -0.4374 261  GLU G CD  
19717 O  OE1 . GLU G  263 ? 3.2234 2.0724 3.3636 0.7151  -0.0403 -0.4397 261  GLU G OE1 
19718 O  OE2 . GLU G  263 ? 3.4761 2.2609 3.5216 0.7303  -0.0709 -0.4504 261  GLU G OE2 
19719 N  N   . LYS G  264 ? 2.7456 1.4827 2.7172 0.6727  -0.1759 -0.4628 262  LYS G N   
19720 C  CA  . LYS G  264 ? 2.7025 1.3893 2.6029 0.6647  -0.2212 -0.4669 262  LYS G CA  
19721 C  C   . LYS G  264 ? 2.7399 1.4224 2.6319 0.6635  -0.2284 -0.4479 262  LYS G C   
19722 O  O   . LYS G  264 ? 2.7840 1.4316 2.6261 0.6534  -0.2710 -0.4429 262  LYS G O   
19723 C  CB  . LYS G  264 ? 2.8931 1.5199 2.7136 0.6877  -0.2280 -0.4994 262  LYS G CB  
19724 C  CG  . LYS G  264 ? 3.1144 1.6734 2.8434 0.6777  -0.2802 -0.5080 262  LYS G CG  
19725 C  CD  . LYS G  264 ? 3.1636 1.7281 2.9055 0.6462  -0.3215 -0.4938 262  LYS G CD  
19726 C  CE  . LYS G  264 ? 3.2346 1.7266 2.8811 0.6341  -0.3786 -0.5000 262  LYS G CE  
19727 N  NZ  . LYS G  264 ? 3.1017 1.6012 2.7608 0.6034  -0.4238 -0.4843 262  LYS G NZ  
19728 N  N   . ASN G  265 ? 2.9238 1.6375 2.8637 0.6745  -0.1905 -0.4349 263  ASN G N   
19729 C  CA  . ASN G  265 ? 2.7909 1.5004 2.7325 0.6786  -0.1922 -0.4126 263  ASN G CA  
19730 C  C   . ASN G  265 ? 2.4714 1.2268 2.4836 0.6550  -0.1865 -0.3832 263  ASN G C   
19731 O  O   . ASN G  265 ? 2.3775 1.1619 2.4208 0.6329  -0.1917 -0.3820 263  ASN G O   
19732 C  CB  . ASN G  265 ? 3.0258 1.7328 2.9705 0.7084  -0.1557 -0.4166 263  ASN G CB  
19733 C  CG  . ASN G  265 ? 3.1240 1.7756 2.9761 0.7365  -0.1658 -0.4453 263  ASN G CG  
19734 O  OD1 . ASN G  265 ? 3.2459 1.8444 3.0195 0.7371  -0.2045 -0.4487 263  ASN G OD1 
19735 N  ND2 . ASN G  265 ? 2.9951 1.6553 2.8480 0.7612  -0.1318 -0.4680 263  ASN G ND2 
19736 N  N   . CYS G  266 ? 2.4936 1.2522 2.5270 0.6622  -0.1756 -0.3593 264  CYS G N   
19737 C  CA  . CYS G  266 ? 2.4685 1.2621 2.5609 0.6451  -0.1667 -0.3319 264  CYS G CA  
19738 C  C   . CYS G  266 ? 2.4816 1.3143 2.6336 0.6331  -0.1272 -0.3322 264  CYS G C   
19739 O  O   . CYS G  266 ? 2.6620 1.4990 2.8445 0.6438  -0.0915 -0.3247 264  CYS G O   
19740 C  CB  . CYS G  266 ? 2.6873 1.4674 2.7876 0.6621  -0.1603 -0.3047 264  CYS G CB  
19741 S  SG  . CYS G  266 ? 2.7253 1.5412 2.8974 0.6481  -0.1385 -0.2718 264  CYS G SG  
19742 N  N   . CYS G  267 ? 2.2471 1.1027 2.4096 0.6123  -0.1381 -0.3408 265  CYS G N   
19743 C  CA  . CYS G  267 ? 2.3741 1.2614 2.5796 0.6005  -0.1111 -0.3421 265  CYS G CA  
19744 C  C   . CYS G  267 ? 2.0034 0.9165 2.2334 0.5764  -0.1234 -0.3311 265  CYS G C   
19745 O  O   . CYS G  267 ? 1.9953 0.9082 2.2090 0.5671  -0.1595 -0.3291 265  CYS G O   
19746 C  CB  . CYS G  267 ? 2.6955 1.5860 2.8903 0.6029  -0.1151 -0.3641 265  CYS G CB  
19747 S  SG  . CYS G  267 ? 3.3298 2.2545 3.5701 0.5968  -0.0891 -0.3681 265  CYS G SG  
19748 N  N   . VAL G  268 ? 2.1078 1.0401 2.3730 0.5679  -0.0967 -0.3264 266  VAL G N   
19749 C  CA  . VAL G  268 ? 2.0414 0.9978 2.3282 0.5467  -0.1069 -0.3220 266  VAL G CA  
19750 C  C   . VAL G  268 ? 1.9857 0.9655 2.2774 0.5301  -0.1315 -0.3380 266  VAL G C   
19751 O  O   . VAL G  268 ? 1.9794 0.9682 2.2841 0.5305  -0.1193 -0.3482 266  VAL G O   
19752 C  CB  . VAL G  268 ? 2.1292 1.0866 2.4423 0.5441  -0.0733 -0.3146 266  VAL G CB  
19753 C  CG1 . VAL G  268 ? 2.1684 1.1207 2.4898 0.5521  -0.0479 -0.3232 266  VAL G CG1 
19754 C  CG2 . VAL G  268 ? 2.1359 1.1193 2.4707 0.5216  -0.0847 -0.3197 266  VAL G CG2 
19755 N  N   . ARG G  269 ? 1.9158 0.9059 2.2007 0.5173  -0.1696 -0.3391 267  ARG G N   
19756 C  CA  . ARG G  269 ? 1.8556 0.8639 2.1449 0.5023  -0.2007 -0.3522 267  ARG G CA  
19757 C  C   . ARG G  269 ? 2.2091 1.2511 2.5374 0.4824  -0.2029 -0.3548 267  ARG G C   
19758 O  O   . ARG G  269 ? 2.5371 1.5856 2.8798 0.4787  -0.1922 -0.3472 267  ARG G O   
19759 C  CB  . ARG G  269 ? 1.8694 0.8645 2.1264 0.4989  -0.2487 -0.3540 267  ARG G CB  
19760 C  CG  . ARG G  269 ? 1.9272 0.8815 2.1380 0.5176  -0.2529 -0.3549 267  ARG G CG  
19761 C  CD  . ARG G  269 ? 1.9597 0.8998 2.1610 0.5319  -0.2303 -0.3674 267  ARG G CD  
19762 N  NE  . ARG G  269 ? 2.0210 0.9211 2.1791 0.5525  -0.2278 -0.3718 267  ARG G NE  
19763 C  CZ  . ARG G  269 ? 2.0629 0.9455 2.2074 0.5717  -0.2064 -0.3848 267  ARG G CZ  
19764 N  NH1 . ARG G  269 ? 2.0487 0.9517 2.2226 0.5746  -0.1855 -0.3913 267  ARG G NH1 
19765 N  NH2 . ARG G  269 ? 2.1241 0.9682 2.2245 0.5907  -0.2079 -0.3923 267  ARG G NH2 
19766 N  N   . GLN G  270 ? 2.1125 1.1742 2.4592 0.4714  -0.2179 -0.3667 268  GLN G N   
19767 C  CA  . GLN G  270 ? 1.7447 0.8388 2.1319 0.4516  -0.2239 -0.3738 268  GLN G CA  
19768 C  C   . GLN G  270 ? 1.7183 0.8294 2.1109 0.4367  -0.2645 -0.3749 268  GLN G C   
19769 O  O   . GLN G  270 ? 1.7274 0.8307 2.0977 0.4362  -0.3027 -0.3748 268  GLN G O   
19770 C  CB  . GLN G  270 ? 1.8573 0.9687 2.2699 0.4467  -0.2316 -0.3857 268  GLN G CB  
19771 C  CG  . GLN G  270 ? 2.0845 1.2294 2.5451 0.4251  -0.2389 -0.3966 268  GLN G CG  
19772 C  CD  . GLN G  270 ? 2.2377 1.4024 2.7315 0.4216  -0.2543 -0.4075 268  GLN G CD  
19773 O  OE1 . GLN G  270 ? 2.4777 1.6297 2.9568 0.4386  -0.2563 -0.4062 268  GLN G OE1 
19774 N  NE2 . GLN G  270 ? 1.8785 1.0737 2.4209 0.4011  -0.2650 -0.4198 268  GLN G NE2 
19775 N  N   . LEU G  271 ? 2.0662 1.1970 2.4876 0.4256  -0.2575 -0.3777 269  LEU G N   
19776 C  CA  . LEU G  271 ? 1.9971 1.1492 2.4322 0.4136  -0.2955 -0.3815 269  LEU G CA  
19777 C  C   . LEU G  271 ? 1.8987 1.0764 2.3759 0.3992  -0.2831 -0.3940 269  LEU G C   
19778 O  O   . LEU G  271 ? 1.7080 0.8752 2.1883 0.4055  -0.2458 -0.3909 269  LEU G O   
19779 C  CB  . LEU G  271 ? 1.7355 0.8716 2.1462 0.4273  -0.3023 -0.3678 269  LEU G CB  
19780 C  CG  . LEU G  271 ? 1.6961 0.8546 2.1239 0.4195  -0.3435 -0.3715 269  LEU G CG  
19781 C  CD1 . LEU G  271 ? 1.7571 0.9244 2.1821 0.4042  -0.4003 -0.3798 269  LEU G CD1 
19782 C  CD2 . LEU G  271 ? 1.7314 0.8742 2.1395 0.4379  -0.3493 -0.3556 269  LEU G CD2 
19783 N  N   . TYR G  272 ? 1.7687 0.9757 2.2778 0.3803  -0.3150 -0.4090 270  TYR G N   
19784 C  CA  . TYR G  272 ? 1.5842 0.8176 2.1364 0.3633  -0.3117 -0.4267 270  TYR G CA  
19785 C  C   . TYR G  272 ? 1.5876 0.8408 2.1524 0.3592  -0.3464 -0.4319 270  TYR G C   
19786 O  O   . TYR G  272 ? 1.9616 1.2251 2.5255 0.3533  -0.3970 -0.4314 270  TYR G O   
19787 C  CB  . TYR G  272 ? 1.8652 1.1219 2.4537 0.3452  -0.3297 -0.4415 270  TYR G CB  
19788 C  CG  . TYR G  272 ? 1.9211 1.2075 2.5577 0.3232  -0.3344 -0.4645 270  TYR G CG  
19789 C  CD1 . TYR G  272 ? 1.6287 0.9080 2.2792 0.3171  -0.2921 -0.4759 270  TYR G CD1 
19790 C  CD2 . TYR G  272 ? 2.0605 1.3780 2.7272 0.3070  -0.3831 -0.4765 270  TYR G CD2 
19791 C  CE1 . TYR G  272 ? 1.5806 0.8832 2.2718 0.2944  -0.2947 -0.5016 270  TYR G CE1 
19792 C  CE2 . TYR G  272 ? 1.9745 1.3202 2.6859 0.2853  -0.3867 -0.5015 270  TYR G CE2 
19793 C  CZ  . TYR G  272 ? 1.7523 1.0907 2.4747 0.2786  -0.3405 -0.5155 270  TYR G CZ  
19794 O  OH  . TYR G  272 ? 2.0736 1.4372 2.8359 0.2536  -0.3419 -0.5450 270  TYR G OH  
19795 N  N   . ILE G  273 ? 1.5729 0.8278 2.1494 0.3639  -0.3213 -0.4373 271  ILE G N   
19796 C  CA  . ILE G  273 ? 1.6217 0.8957 2.2137 0.3675  -0.3490 -0.4429 271  ILE G CA  
19797 C  C   . ILE G  273 ? 1.5886 0.8950 2.2277 0.3475  -0.3561 -0.4724 271  ILE G C   
19798 O  O   . ILE G  273 ? 1.6554 0.9563 2.3068 0.3434  -0.3140 -0.4856 271  ILE G O   
19799 C  CB  . ILE G  273 ? 1.7571 1.0108 2.3326 0.3938  -0.3161 -0.4284 271  ILE G CB  
19800 C  CG1 . ILE G  273 ? 1.7362 0.9608 2.2684 0.4110  -0.3166 -0.4016 271  ILE G CG1 
19801 C  CG2 . ILE G  273 ? 1.7185 0.9980 2.3205 0.4027  -0.3413 -0.4373 271  ILE G CG2 
19802 C  CD1 . ILE G  273 ? 1.6443 0.8522 2.1659 0.4386  -0.2929 -0.3832 271  ILE G CD1 
19803 N  N   . ASP G  274 ? 1.5140 0.8498 2.1773 0.3334  -0.4116 -0.4840 272  ASP G N   
19804 C  CA  . ASP G  274 ? 1.5240 0.8949 2.2348 0.3129  -0.4252 -0.5156 272  ASP G CA  
19805 C  C   . ASP G  274 ? 1.5598 0.9476 2.2866 0.3271  -0.4365 -0.5276 272  ASP G C   
19806 O  O   . ASP G  274 ? 1.6474 1.0304 2.3584 0.3445  -0.4684 -0.5105 272  ASP G O   
19807 C  CB  . ASP G  274 ? 1.5211 0.9151 2.2542 0.2871  -0.4827 -0.5222 272  ASP G CB  
19808 C  CG  . ASP G  274 ? 1.5876 1.0184 2.3696 0.2573  -0.4884 -0.5568 272  ASP G CG  
19809 O  OD1 . ASP G  274 ? 1.6335 1.0793 2.4330 0.2578  -0.4683 -0.5820 272  ASP G OD1 
19810 O  OD2 . ASP G  274 ? 1.7056 1.1515 2.5084 0.2329  -0.5121 -0.5603 272  ASP G OD2 
19811 N  N   . PHE G  275 ? 1.5486 0.9559 2.3073 0.3203  -0.4110 -0.5592 273  PHE G N   
19812 C  CA  . PHE G  275 ? 1.5968 1.0261 2.3776 0.3397  -0.4152 -0.5768 273  PHE G CA  
19813 C  C   . PHE G  275 ? 1.7027 1.1714 2.5156 0.3220  -0.4840 -0.5992 273  PHE G C   
19814 O  O   . PHE G  275 ? 1.7768 1.2828 2.5852 0.3346  -0.5087 -0.5836 273  PHE G O   
19815 C  CB  . PHE G  275 ? 1.6320 1.0619 2.4279 0.3403  -0.3569 -0.6062 273  PHE G CB  
19816 C  CG  . PHE G  275 ? 1.5924 0.9724 2.3517 0.3567  -0.2955 -0.5828 273  PHE G CG  
19817 C  CD1 . PHE G  275 ? 1.7228 1.0823 2.4654 0.3953  -0.2673 -0.5615 273  PHE G CD1 
19818 C  CD2 . PHE G  275 ? 1.5815 0.9350 2.3248 0.3343  -0.2697 -0.5805 273  PHE G CD2 
19819 C  CE1 . PHE G  275 ? 1.8196 1.1272 2.5260 0.4085  -0.2150 -0.5391 273  PHE G CE1 
19820 C  CE2 . PHE G  275 ? 1.6237 0.9270 2.3317 0.3482  -0.2191 -0.5605 273  PHE G CE2 
19821 C  CZ  . PHE G  275 ? 1.7874 1.0648 2.4746 0.3842  -0.1922 -0.5398 273  PHE G CZ  
19822 N  N   . ARG G  276 ? 1.8216 1.3098 2.6516 0.2798  -0.5097 -0.6181 274  ARG G N   
19823 C  CA  . ARG G  276 ? 1.8312 1.4020 2.6614 0.2363  -0.5641 -0.6077 274  ARG G CA  
19824 C  C   . ARG G  276 ? 1.7934 1.3508 2.5944 0.2316  -0.6260 -0.5677 274  ARG G C   
19825 O  O   . ARG G  276 ? 1.6713 1.2950 2.4580 0.2075  -0.6705 -0.5426 274  ARG G O   
19826 C  CB  . ARG G  276 ? 2.0162 1.6232 2.8708 0.1862  -0.5684 -0.6328 274  ARG G CB  
19827 C  CG  . ARG G  276 ? 1.9421 1.5773 2.8168 0.1758  -0.5153 -0.6751 274  ARG G CG  
19828 C  CD  . ARG G  276 ? 1.9905 1.7286 2.8647 0.1546  -0.5235 -0.6774 274  ARG G CD  
19829 N  NE  . ARG G  276 ? 2.0323 1.8549 2.9115 0.0930  -0.5746 -0.6681 274  ARG G NE  
19830 C  CZ  . ARG G  276 ? 2.1538 2.0263 3.0198 0.0726  -0.6363 -0.6284 274  ARG G CZ  
19831 N  NH1 . ARG G  276 ? 2.4115 2.2595 3.2549 0.1069  -0.6551 -0.5956 274  ARG G NH1 
19832 N  NH2 . ARG G  276 ? 1.8647 1.8121 2.7380 0.0141  -0.6812 -0.6193 274  ARG G NH2 
19833 N  N   . LYS G  277 ? 1.8602 1.3320 2.6488 0.2538  -0.6290 -0.5615 275  LYS G N   
19834 C  CA  . LYS G  277 ? 1.7900 1.2307 2.5469 0.2483  -0.6856 -0.5312 275  LYS G CA  
19835 C  C   . LYS G  277 ? 1.6994 1.0995 2.4151 0.2835  -0.6919 -0.5045 275  LYS G C   
19836 O  O   . LYS G  277 ? 1.6174 1.0303 2.2996 0.2675  -0.7450 -0.4751 275  LYS G O   
19837 C  CB  . LYS G  277 ? 1.9603 1.3853 2.7091 0.2445  -0.6668 -0.5162 275  LYS G CB  
19838 C  CG  . LYS G  277 ? 2.1111 1.5055 2.8241 0.2420  -0.7157 -0.4855 275  LYS G CG  
19839 C  CD  . LYS G  277 ? 2.1276 1.5473 2.8502 0.2012  -0.7880 -0.4800 275  LYS G CD  
19840 C  CE  . LYS G  277 ? 1.9518 1.3297 2.6342 0.2025  -0.8316 -0.4469 275  LYS G CE  
19841 N  NZ  . LYS G  277 ? 1.6101 0.9383 2.2381 0.2272  -0.8407 -0.4314 275  LYS G NZ  
19842 N  N   . ASP G  278 ? 1.5160 0.9027 2.2167 0.3156  -0.6286 -0.4957 276  ASP G N   
19843 C  CA  . ASP G  278 ? 1.5107 0.8661 2.1680 0.3428  -0.6282 -0.4670 276  ASP G CA  
19844 C  C   . ASP G  278 ? 1.5399 0.9115 2.2157 0.3742  -0.6158 -0.4683 276  ASP G C   
19845 O  O   . ASP G  278 ? 1.5423 0.8949 2.1884 0.3982  -0.6198 -0.4416 276  ASP G O   
19846 C  CB  . ASP G  278 ? 1.5847 0.9129 2.2064 0.3525  -0.5693 -0.4508 276  ASP G CB  
19847 C  CG  . ASP G  278 ? 1.9802 1.2987 2.5902 0.3324  -0.5787 -0.4483 276  ASP G CG  
19848 O  OD1 . ASP G  278 ? 2.1223 1.4380 2.7287 0.3154  -0.6397 -0.4452 276  ASP G OD1 
19849 O  OD2 . ASP G  278 ? 2.1051 1.4169 2.7109 0.3345  -0.5272 -0.4479 276  ASP G OD2 
19850 N  N   . LEU G  279 ? 1.7856 1.2063 2.5055 0.3717  -0.5955 -0.4938 277  LEU G N   
19851 C  CA  . LEU G  279 ? 1.8112 1.2855 2.5433 0.3954  -0.5676 -0.4847 277  LEU G CA  
19852 C  C   . LEU G  279 ? 1.8481 1.4315 2.5981 0.3631  -0.5822 -0.4879 277  LEU G C   
19853 O  O   . LEU G  279 ? 1.8508 1.5013 2.5997 0.3749  -0.5844 -0.4640 277  LEU G O   
19854 C  CB  . LEU G  279 ? 1.9253 1.3578 2.6801 0.4310  -0.4941 -0.5071 277  LEU G CB  
19855 C  CG  . LEU G  279 ? 1.9283 1.3159 2.6341 0.4441  -0.4537 -0.4705 277  LEU G CG  
19856 C  CD1 . LEU G  279 ? 1.9112 1.2820 2.6169 0.4556  -0.3754 -0.4746 277  LEU G CD1 
19857 C  CD2 . LEU G  279 ? 1.8756 1.2622 2.5652 0.4749  -0.4835 -0.4363 277  LEU G CD2 
19858 N  N   . GLY G  280 ? 1.9348 1.5464 2.7019 0.3220  -0.5921 -0.5139 278  GLY G N   
19859 C  CA  . GLY G  280 ? 2.0429 1.7626 2.8265 0.2884  -0.6020 -0.5205 278  GLY G CA  
19860 C  C   . GLY G  280 ? 2.2837 2.0286 3.0969 0.3149  -0.5375 -0.5526 278  GLY G C   
19861 O  O   . GLY G  280 ? 2.4232 2.2605 3.2444 0.3146  -0.5345 -0.5462 278  GLY G O   
19862 N  N   . TRP G  281 ? 2.3919 2.0567 3.2204 0.3370  -0.4855 -0.5874 279  TRP G N   
19863 C  CA  . TRP G  281 ? 2.3510 2.0139 3.2024 0.3647  -0.4207 -0.6221 279  TRP G CA  
19864 C  C   . TRP G  281 ? 2.3236 1.9815 3.1895 0.3260  -0.3998 -0.6701 279  TRP G C   
19865 O  O   . TRP G  281 ? 2.3841 1.9642 3.2520 0.3202  -0.3874 -0.6863 279  TRP G O   
19866 C  CB  . TRP G  281 ? 2.3048 1.8714 3.1577 0.4227  -0.3752 -0.6190 279  TRP G CB  
19867 C  CG  . TRP G  281 ? 2.2414 1.8232 3.0828 0.4624  -0.3878 -0.5719 279  TRP G CG  
19868 C  CD1 . TRP G  281 ? 2.2461 1.9150 3.0736 0.4491  -0.4357 -0.5332 279  TRP G CD1 
19869 C  CD2 . TRP G  281 ? 2.1710 1.6840 3.0132 0.5175  -0.3535 -0.5549 279  TRP G CD2 
19870 N  NE1 . TRP G  281 ? 2.2438 1.9045 3.0627 0.4916  -0.4333 -0.4934 279  TRP G NE1 
19871 C  CE2 . TRP G  281 ? 2.2057 1.7724 3.0347 0.5350  -0.3830 -0.5054 279  TRP G CE2 
19872 C  CE3 . TRP G  281 ? 2.1031 1.5528 2.9116 0.5185  -0.2886 -0.5432 279  TRP G CE3 
19873 C  CZ2 . TRP G  281 ? 2.0660 1.5941 2.8933 0.5848  -0.3629 -0.4736 279  TRP G CZ2 
19874 C  CZ3 . TRP G  281 ? 2.0470 1.4692 2.8322 0.5529  -0.2617 -0.4998 279  TRP G CZ3 
19875 C  CH2 . TRP G  281 ? 2.0786 1.5381 2.8776 0.5870  -0.2985 -0.4685 279  TRP G CH2 
19876 N  N   . LYS G  282 ? 2.3703 2.1177 3.2451 0.2974  -0.3960 -0.6916 280  LYS G N   
19877 C  CA  . LYS G  282 ? 2.3769 2.1327 3.2614 0.2555  -0.3747 -0.7386 280  LYS G CA  
19878 C  C   . LYS G  282 ? 2.5565 2.2856 3.4490 0.2844  -0.3041 -0.7834 280  LYS G C   
19879 O  O   . LYS G  282 ? 2.8179 2.5629 3.7124 0.2486  -0.2811 -0.8275 280  LYS G O   
19880 C  CB  . LYS G  282 ? 2.3511 2.2260 3.2353 0.1953  -0.4204 -0.7346 280  LYS G CB  
19881 C  CG  . LYS G  282 ? 2.5090 2.3937 3.3998 0.1363  -0.4222 -0.7678 280  LYS G CG  
19882 C  CD  . LYS G  282 ? 2.3900 2.3911 3.2807 0.0745  -0.4788 -0.7512 280  LYS G CD  
19883 C  CE  . LYS G  282 ? 2.1835 2.2932 3.0723 0.0724  -0.4686 -0.7585 280  LYS G CE  
19884 N  NZ  . LYS G  282 ? 2.0891 2.3187 2.9770 0.0065  -0.5252 -0.7398 280  LYS G NZ  
19885 N  N   . TRP G  283 ? 2.4701 2.1566 3.3656 0.3477  -0.2698 -0.7724 281  TRP G N   
19886 C  CA  . TRP G  283 ? 2.3394 1.9857 3.2424 0.3850  -0.2017 -0.8116 281  TRP G CA  
19887 C  C   . TRP G  283 ? 2.2445 1.7667 3.1333 0.3965  -0.1584 -0.8180 281  TRP G C   
19888 O  O   . TRP G  283 ? 2.1574 1.6404 3.0248 0.4120  -0.0994 -0.8287 281  TRP G O   
19889 C  CB  . TRP G  283 ? 2.3590 2.0415 3.2711 0.4464  -0.1866 -0.7832 281  TRP G CB  
19890 C  CG  . TRP G  283 ? 2.3534 1.9830 3.2641 0.4882  -0.2024 -0.7323 281  TRP G CG  
19891 C  CD1 . TRP G  283 ? 2.3575 2.0271 3.2567 0.4768  -0.2615 -0.6816 281  TRP G CD1 
19892 C  CD2 . TRP G  283 ? 2.2635 1.7986 3.1636 0.5340  -0.1568 -0.7132 281  TRP G CD2 
19893 N  NE1 . TRP G  283 ? 2.3829 1.9831 3.2786 0.5219  -0.2564 -0.6473 281  TRP G NE1 
19894 C  CE2 . TRP G  283 ? 2.3295 1.8560 3.2192 0.5514  -0.1910 -0.6575 281  TRP G CE2 
19895 C  CE3 . TRP G  283 ? 2.1835 1.6526 3.0500 0.5429  -0.0885 -0.7149 281  TRP G CE3 
19896 C  CZ2 . TRP G  283 ? 2.1706 1.6351 3.0219 0.5755  -0.1564 -0.6072 281  TRP G CZ2 
19897 C  CZ3 . TRP G  283 ? 2.1809 1.5821 3.0092 0.5703  -0.0585 -0.6625 281  TRP G CZ3 
19898 C  CH2 . TRP G  283 ? 2.1690 1.5731 2.9923 0.5856  -0.0909 -0.6105 281  TRP G CH2 
19899 N  N   . ILE G  284 ? 2.2085 1.6939 3.0758 0.3719  -0.1823 -0.7804 282  ILE G N   
19900 C  CA  . ILE G  284 ? 2.1270 1.5349 2.9490 0.3618  -0.1423 -0.7522 282  ILE G CA  
19901 C  C   . ILE G  284 ? 2.1895 1.6011 3.0123 0.3033  -0.1529 -0.7771 282  ILE G C   
19902 O  O   . ILE G  284 ? 2.2350 1.6736 3.0713 0.2777  -0.2007 -0.7659 282  ILE G O   
19903 C  CB  . ILE G  284 ? 1.8802 1.2539 2.6760 0.3831  -0.1544 -0.6914 282  ILE G CB  
19904 C  CG1 . ILE G  284 ? 1.8913 1.2644 2.6867 0.4384  -0.1425 -0.6641 282  ILE G CG1 
19905 C  CG2 . ILE G  284 ? 1.8288 1.1331 2.5808 0.3691  -0.1183 -0.6699 282  ILE G CG2 
19906 C  CD1 . ILE G  284 ? 1.8303 1.1715 2.5953 0.4563  -0.1508 -0.6078 282  ILE G CD1 
19907 N  N   . HIS G  285 ? 1.9019 1.2830 2.7074 0.2824  -0.1090 -0.8082 283  HIS G N   
19908 C  CA  . HIS G  285 ? 1.8828 1.2747 2.6912 0.2237  -0.1174 -0.8337 283  HIS G CA  
19909 C  C   . HIS G  285 ? 1.7560 1.1043 2.5434 0.2132  -0.1191 -0.7928 283  HIS G C   
19910 O  O   . HIS G  285 ? 1.7027 1.0839 2.5094 0.1828  -0.1573 -0.7861 283  HIS G O   
19911 C  CB  . HIS G  285 ? 2.5061 1.8752 3.2957 0.2020  -0.0706 -0.8808 283  HIS G CB  
19912 C  CG  . HIS G  285 ? 2.6124 2.0393 3.4237 0.2047  -0.0670 -0.9321 283  HIS G CG  
19913 N  ND1 . HIS G  285 ? 2.5746 2.0207 3.4010 0.2602  -0.0623 -0.9286 283  HIS G ND1 
19914 C  CD2 . HIS G  285 ? 2.5008 1.9783 3.3193 0.1580  -0.0655 -0.9896 283  HIS G CD2 
19915 C  CE1 . HIS G  285 ? 2.5022 2.0109 3.3480 0.2521  -0.0571 -0.9852 283  HIS G CE1 
19916 N  NE2 . HIS G  285 ? 2.5150 2.0432 3.3523 0.1875  -0.0585 -1.0241 283  HIS G NE2 
19917 N  N   . GLU G  286 ? 1.8269 1.1029 2.5747 0.2390  -0.0789 -0.7661 284  GLU G N   
19918 C  CA  . GLU G  286 ? 1.8444 1.0818 2.5712 0.2321  -0.0767 -0.7318 284  GLU G CA  
19919 C  C   . GLU G  286 ? 2.0985 1.2888 2.7918 0.2787  -0.0599 -0.6851 284  GLU G C   
19920 O  O   . GLU G  286 ? 2.2278 1.3764 2.8971 0.3096  -0.0264 -0.6826 284  GLU G O   
19921 C  CB  . GLU G  286 ? 1.8784 1.0707 2.5854 0.1979  -0.0448 -0.7548 284  GLU G CB  
19922 C  CG  . GLU G  286 ? 2.0293 1.2710 2.7651 0.1423  -0.0614 -0.7979 284  GLU G CG  
19923 C  CD  . GLU G  286 ? 1.8120 1.1065 2.5824 0.1177  -0.1069 -0.7833 284  GLU G CD  
19924 O  OE1 . GLU G  286 ? 1.8057 1.0813 2.5705 0.1380  -0.1141 -0.7441 284  GLU G OE1 
19925 O  OE2 . GLU G  286 ? 1.7717 1.1275 2.5725 0.0781  -0.1354 -0.8106 284  GLU G OE2 
19926 N  N   . PRO G  287 ? 2.0644 1.2613 2.7542 0.2841  -0.0829 -0.6488 285  PRO G N   
19927 C  CA  . PRO G  287 ? 1.7210 0.9651 2.4402 0.2546  -0.1240 -0.6503 285  PRO G CA  
19928 C  C   . PRO G  287 ? 1.6617 0.9654 2.4109 0.2598  -0.1723 -0.6514 285  PRO G C   
19929 O  O   . PRO G  287 ? 1.7147 1.0267 2.4650 0.2865  -0.1725 -0.6520 285  PRO G O   
19930 C  CB  . PRO G  287 ? 1.7176 0.9322 2.4117 0.2677  -0.1205 -0.6112 285  PRO G CB  
19931 C  CG  . PRO G  287 ? 1.7493 0.9283 2.4083 0.3093  -0.0993 -0.5822 285  PRO G CG  
19932 C  CD  . PRO G  287 ? 1.9071 1.0609 2.5602 0.3188  -0.0672 -0.6050 285  PRO G CD  
19933 N  N   . LYS G  288 ? 1.6701 1.0131 2.4451 0.2356  -0.2151 -0.6519 286  LYS G N   
19934 C  CA  . LYS G  288 ? 1.9192 1.3095 2.7178 0.2370  -0.2704 -0.6498 286  LYS G CA  
19935 C  C   . LYS G  288 ? 1.9110 1.2919 2.6913 0.2538  -0.2973 -0.6087 286  LYS G C   
19936 O  O   . LYS G  288 ? 1.5975 1.0076 2.3940 0.2447  -0.3491 -0.6037 286  LYS G O   
19937 C  CB  . LYS G  288 ? 1.9361 1.3771 2.7746 0.1930  -0.3046 -0.6835 286  LYS G CB  
19938 C  CG  . LYS G  288 ? 1.8498 1.3077 2.7004 0.1701  -0.2786 -0.7314 286  LYS G CG  
19939 C  CD  . LYS G  288 ? 1.7318 1.2444 2.6118 0.1132  -0.3070 -0.7618 286  LYS G CD  
19940 C  CE  . LYS G  288 ? 1.7566 1.2854 2.6358 0.0847  -0.2735 -0.8118 286  LYS G CE  
19941 N  NZ  . LYS G  288 ? 1.7537 1.3470 2.6509 0.0189  -0.2988 -0.8347 286  LYS G NZ  
19942 N  N   . GLY G  289 ? 2.0465 1.3831 2.7884 0.2773  -0.2623 -0.5801 287  GLY G N   
19943 C  CA  . GLY G  289 ? 1.7304 1.0536 2.4461 0.2923  -0.2768 -0.5456 287  GLY G CA  
19944 C  C   . GLY G  289 ? 1.7669 1.0455 2.4508 0.3022  -0.2316 -0.5281 287  GLY G C   
19945 O  O   . GLY G  289 ? 1.6977 0.9621 2.3904 0.2860  -0.2035 -0.5443 287  GLY G O   
19946 N  N   . TYR G  290 ? 1.8646 1.1191 2.5112 0.3267  -0.2253 -0.4974 288  TYR G N   
19947 C  CA  . TYR G  290 ? 1.8191 1.0313 2.4355 0.3376  -0.1852 -0.4812 288  TYR G CA  
19948 C  C   . TYR G  290 ? 1.6330 0.8346 2.2170 0.3570  -0.1949 -0.4530 288  TYR G C   
19949 O  O   . TYR G  290 ? 1.6117 0.8314 2.1915 0.3623  -0.2303 -0.4454 288  TYR G O   
19950 C  CB  . TYR G  290 ? 1.6832 0.8568 2.2808 0.3521  -0.1425 -0.4797 288  TYR G CB  
19951 C  CG  . TYR G  290 ? 1.6958 0.8593 2.2710 0.3821  -0.1406 -0.4572 288  TYR G CG  
19952 C  CD1 . TYR G  290 ? 1.6705 0.8682 2.2653 0.3871  -0.1708 -0.4629 288  TYR G CD1 
19953 C  CD2 . TYR G  290 ? 1.7350 0.8568 2.2749 0.4058  -0.1114 -0.4311 288  TYR G CD2 
19954 C  CE1 . TYR G  290 ? 1.6826 0.8752 2.2646 0.4155  -0.1724 -0.4422 288  TYR G CE1 
19955 C  CE2 . TYR G  290 ? 1.7473 0.8631 2.2740 0.4333  -0.1111 -0.4098 288  TYR G CE2 
19956 C  CZ  . TYR G  290 ? 1.7206 0.8728 2.2696 0.4383  -0.1416 -0.4149 288  TYR G CZ  
19957 O  OH  . TYR G  290 ? 1.7336 0.8839 2.2762 0.4671  -0.1446 -0.3926 288  TYR G OH  
19958 N  N   . HIS G  291 ? 1.6969 0.8662 2.2578 0.3665  -0.1651 -0.4403 289  HIS G N   
19959 C  CA  . HIS G  291 ? 1.7055 0.8604 2.2342 0.3850  -0.1671 -0.4179 289  HIS G CA  
19960 C  C   . HIS G  291 ? 1.7417 0.8627 2.2379 0.4093  -0.1409 -0.3970 289  HIS G C   
19961 O  O   . HIS G  291 ? 1.7790 0.8652 2.2594 0.4194  -0.1064 -0.3889 289  HIS G O   
19962 C  CB  . HIS G  291 ? 1.7676 0.9127 2.2980 0.3836  -0.1533 -0.4190 289  HIS G CB  
19963 C  CG  . HIS G  291 ? 1.9159 1.0953 2.4811 0.3664  -0.1833 -0.4343 289  HIS G CG  
19964 N  ND1 . HIS G  291 ? 1.8830 1.0887 2.4920 0.3416  -0.1951 -0.4570 289  HIS G ND1 
19965 C  CD2 . HIS G  291 ? 1.9821 1.1718 2.5472 0.3720  -0.2039 -0.4307 289  HIS G CD2 
19966 C  CE1 . HIS G  291 ? 1.8610 1.0944 2.5000 0.3326  -0.2243 -0.4647 289  HIS G CE1 
19967 N  NE2 . HIS G  291 ? 2.0756 1.2984 2.6875 0.3524  -0.2296 -0.4484 289  HIS G NE2 
19968 N  N   . ALA G  292 ? 1.6978 0.8290 2.1876 0.4197  -0.1619 -0.3878 290  ALA G N   
19969 C  CA  . ALA G  292 ? 1.7309 0.8349 2.1979 0.4451  -0.1422 -0.3657 290  ALA G CA  
19970 C  C   . ALA G  292 ? 1.7476 0.8323 2.1843 0.4585  -0.1415 -0.3482 290  ALA G C   
19971 O  O   . ALA G  292 ? 1.9799 1.0326 2.3989 0.4772  -0.1123 -0.3315 290  ALA G O   
19972 C  CB  . ALA G  292 ? 1.7177 0.8432 2.1971 0.4536  -0.1682 -0.3629 290  ALA G CB  
19973 N  N   . ASN G  293 ? 2.2092 1.3097 2.6393 0.4506  -0.1747 -0.3528 291  ASN G N   
19974 C  CA  . ASN G  293 ? 2.0371 1.1180 2.4366 0.4628  -0.1775 -0.3424 291  ASN G CA  
19975 C  C   . ASN G  293 ? 2.0216 1.0858 2.4019 0.4823  -0.1832 -0.3237 291  ASN G C   
19976 O  O   . ASN G  293 ? 2.2900 1.3622 2.6838 0.4883  -0.1876 -0.3170 291  ASN G O   
19977 C  CB  . ASN G  293 ? 1.7738 0.8321 2.1662 0.4694  -0.1398 -0.3412 291  ASN G CB  
19978 C  CG  . ASN G  293 ? 1.7534 0.8297 2.1690 0.4523  -0.1401 -0.3591 291  ASN G CG  
19979 O  OD1 . ASN G  293 ? 1.7200 0.8255 2.1553 0.4356  -0.1705 -0.3717 291  ASN G OD1 
19980 N  ND2 . ASN G  293 ? 1.7754 0.8352 2.1932 0.4573  -0.1104 -0.3603 291  ASN G ND2 
19981 N  N   . PHE G  294 ? 1.9095 0.9511 2.2609 0.4944  -0.1853 -0.3163 292  PHE G N   
19982 C  CA  . PHE G  294 ? 2.0644 1.0878 2.3971 0.5132  -0.1965 -0.2991 292  PHE G CA  
19983 C  C   . PHE G  294 ? 2.2138 1.2070 2.5175 0.5264  -0.1850 -0.2964 292  PHE G C   
19984 O  O   . PHE G  294 ? 2.0345 1.0245 2.3327 0.5220  -0.1728 -0.3089 292  PHE G O   
19985 C  CB  . PHE G  294 ? 2.0531 1.0881 2.3754 0.5078  -0.2524 -0.3012 292  PHE G CB  
19986 C  CG  . PHE G  294 ? 2.0111 1.0425 2.3088 0.4940  -0.2875 -0.3173 292  PHE G CG  
19987 C  CD1 . PHE G  294 ? 2.0023 1.0594 2.3203 0.4738  -0.3005 -0.3329 292  PHE G CD1 
19988 C  CD2 . PHE G  294 ? 2.0331 1.0310 2.2858 0.5028  -0.3090 -0.3173 292  PHE G CD2 
19989 C  CE1 . PHE G  294 ? 2.1504 1.2010 2.4481 0.4642  -0.3329 -0.3445 292  PHE G CE1 
19990 C  CE2 . PHE G  294 ? 2.0694 1.0557 2.2953 0.4926  -0.3396 -0.3324 292  PHE G CE2 
19991 C  CZ  . PHE G  294 ? 2.1602 1.1735 2.4106 0.4741  -0.3508 -0.3441 292  PHE G CZ  
19992 N  N   . CYS G  295 ? 2.4765 1.4482 2.7640 0.5455  -0.1908 -0.2799 293  CYS G N   
19993 C  CA  . CYS G  295 ? 2.3168 1.2570 2.5743 0.5609  -0.1861 -0.2791 293  CYS G CA  
19994 C  C   . CYS G  295 ? 2.3682 1.2893 2.5804 0.5626  -0.2384 -0.2847 293  CYS G C   
19995 O  O   . CYS G  295 ? 2.1809 1.1002 2.3849 0.5673  -0.2715 -0.2713 293  CYS G O   
19996 C  CB  . CYS G  295 ? 2.1337 1.0548 2.4011 0.5833  -0.1579 -0.2557 293  CYS G CB  
19997 S  SG  . CYS G  295 ? 2.3546 1.2773 2.6595 0.5836  -0.1008 -0.2474 293  CYS G SG  
19998 N  N   . LEU G  296 ? 2.4522 1.3549 2.6315 0.5604  -0.2476 -0.3044 294  LEU G N   
19999 C  CA  . LEU G  296 ? 2.4863 1.3537 2.6066 0.5623  -0.2967 -0.3140 294  LEU G CA  
20000 C  C   . LEU G  296 ? 2.3436 1.1745 2.4252 0.5787  -0.2824 -0.3285 294  LEU G C   
20001 O  O   . LEU G  296 ? 2.2283 1.0705 2.3277 0.5789  -0.2504 -0.3416 294  LEU G O   
20002 C  CB  . LEU G  296 ? 2.3238 1.2016 2.4368 0.5404  -0.3332 -0.3286 294  LEU G CB  
20003 C  CG  . LEU G  296 ? 2.2120 1.0525 2.2666 0.5349  -0.3981 -0.3322 294  LEU G CG  
20004 C  CD1 . LEU G  296 ? 2.2968 1.0816 2.2838 0.5427  -0.4122 -0.3511 294  LEU G CD1 
20005 C  CD2 . LEU G  296 ? 2.2933 1.1229 2.3367 0.5452  -0.4232 -0.3096 294  LEU G CD2 
20006 N  N   . GLY G  297 ? 2.3588 1.1436 2.3839 0.5947  -0.3083 -0.3265 295  GLY G N   
20007 C  CA  . GLY G  297 ? 2.5832 1.3271 2.5601 0.6134  -0.2985 -0.3446 295  GLY G CA  
20008 C  C   . GLY G  297 ? 2.8266 1.5238 2.7510 0.6365  -0.3147 -0.3334 295  GLY G C   
20009 O  O   . GLY G  297 ? 2.8554 1.5627 2.8031 0.6431  -0.3176 -0.3036 295  GLY G O   
20010 N  N   . PRO G  298 ? 2.7269 1.3685 2.5743 0.6516  -0.3261 -0.3563 296  PRO G N   
20011 C  CA  . PRO G  298 ? 2.7737 1.3583 2.5511 0.6762  -0.3444 -0.3472 296  PRO G CA  
20012 C  C   . PRO G  298 ? 2.7679 1.3639 2.5733 0.7021  -0.2978 -0.3393 296  PRO G C   
20013 O  O   . PRO G  298 ? 2.7313 1.3648 2.5902 0.7028  -0.2531 -0.3518 296  PRO G O   
20014 C  CB  . PRO G  298 ? 2.8014 1.3131 2.4705 0.6785  -0.3748 -0.3829 296  PRO G CB  
20015 C  CG  . PRO G  298 ? 2.6912 1.2366 2.3987 0.6704  -0.3435 -0.4104 296  PRO G CG  
20016 C  CD  . PRO G  298 ? 2.5323 1.1527 2.3417 0.6476  -0.3282 -0.3911 296  PRO G CD  
20017 N  N   . CYS G  299 ? 2.7102 1.2679 2.4733 0.7251  -0.3128 -0.3141 297  CYS G N   
20018 C  CA  . CYS G  299 ? 2.8095 1.3803 2.5895 0.7465  -0.2729 -0.2967 297  CYS G CA  
20019 C  C   . CYS G  299 ? 3.0671 1.6443 2.7532 0.7308  -0.2779 -0.2771 297  CYS G C   
20020 O  O   . CYS G  299 ? 3.1787 1.7888 2.8551 0.7129  -0.2909 -0.2260 297  CYS G O   
20021 C  CB  . CYS G  299 ? 2.8973 1.5089 2.7661 0.7485  -0.2560 -0.2505 297  CYS G CB  
20022 S  SG  . CYS G  299 ? 3.2614 1.9452 3.2491 0.7177  -0.2239 -0.2532 297  CYS G SG  
20023 N  N   . PRO G  300 ? 3.1168 1.6664 2.7311 0.7371  -0.2676 -0.3160 298  PRO G N   
20024 C  CA  . PRO G  300 ? 3.1311 1.6871 2.6477 0.7193  -0.2698 -0.3026 298  PRO G CA  
20025 C  C   . PRO G  300 ? 3.2906 1.8941 2.8243 0.7279  -0.2225 -0.2806 298  PRO G C   
20026 O  O   . PRO G  300 ? 3.4251 2.0510 3.0425 0.7476  -0.1876 -0.2787 298  PRO G O   
20027 C  CB  . PRO G  300 ? 3.1220 1.6140 2.5494 0.7247  -0.2825 -0.3646 298  PRO G CB  
20028 C  CG  . PRO G  300 ? 2.9351 1.4046 2.4327 0.7571  -0.2662 -0.4079 298  PRO G CG  
20029 C  CD  . PRO G  300 ? 2.9448 1.4578 2.5624 0.7623  -0.2529 -0.3752 298  PRO G CD  
20030 N  N   . TYR G  301 ? 3.3270 1.9473 2.7758 0.7081  -0.2235 -0.2625 299  TYR G N   
20031 C  CA  . TYR G  301 ? 3.4844 2.1563 2.9369 0.7095  -0.1827 -0.2362 299  TYR G CA  
20032 C  C   . TYR G  301 ? 3.4711 2.1345 2.9045 0.7348  -0.1450 -0.2901 299  TYR G C   
20033 O  O   . TYR G  301 ? 3.5140 2.2108 2.8991 0.7309  -0.1183 -0.2862 299  TYR G O   
20034 C  CB  . TYR G  301 ? 3.6939 2.3947 3.0585 0.6759  -0.1979 -0.1968 299  TYR G CB  
20035 C  CG  . TYR G  301 ? 3.7163 2.4321 3.0880 0.6503  -0.2394 -0.1428 299  TYR G CG  
20036 C  CD1 . TYR G  301 ? 3.6104 2.3740 3.0712 0.6518  -0.2320 -0.0785 299  TYR G CD1 
20037 C  CD2 . TYR G  301 ? 3.7379 2.4209 3.0269 0.6247  -0.2858 -0.1545 299  TYR G CD2 
20038 C  CE1 . TYR G  301 ? 3.5163 2.3029 2.9890 0.6338  -0.2672 -0.0269 299  TYR G CE1 
20039 C  CE2 . TYR G  301 ? 3.6901 2.4002 2.9884 0.6002  -0.3238 -0.1009 299  TYR G CE2 
20040 C  CZ  . TYR G  301 ? 3.5472 2.3135 2.9401 0.6075  -0.3130 -0.0368 299  TYR G CZ  
20041 O  OH  . TYR G  301 ? 3.5014 2.3036 2.9090 0.5885  -0.3482 0.0187  299  TYR G OH  
20042 N  N   . ALA G  326 ? 3.5296 2.4267 3.2668 0.6360  -0.4054 0.1332  324  ALA G N   
20043 C  CA  . ALA G  326 ? 3.5592 2.3934 3.2730 0.6358  -0.4140 0.0585  324  ALA G CA  
20044 C  C   . ALA G  326 ? 3.6013 2.4056 3.4071 0.6717  -0.3742 0.0228  324  ALA G C   
20045 O  O   . ALA G  326 ? 3.6912 2.5120 3.5780 0.6888  -0.3706 0.0342  324  ALA G O   
20046 C  CB  . ALA G  326 ? 3.5076 2.3499 3.2004 0.6142  -0.4637 0.0570  324  ALA G CB  
20047 N  N   . PRO G  327 ? 3.5071 2.2724 3.2985 0.6818  -0.3432 -0.0188 325  PRO G N   
20048 C  CA  . PRO G  327 ? 3.3722 2.1124 3.2454 0.7100  -0.3058 -0.0520 325  PRO G CA  
20049 C  C   . PRO G  327 ? 3.2740 1.9858 3.1739 0.7134  -0.3245 -0.0983 325  PRO G C   
20050 O  O   . PRO G  327 ? 3.2933 1.9720 3.1317 0.7005  -0.3512 -0.1385 325  PRO G O   
20051 C  CB  . PRO G  327 ? 3.4195 2.1355 3.2511 0.7135  -0.2767 -0.0850 325  PRO G CB  
20052 C  CG  . PRO G  327 ? 3.5618 2.3024 3.3095 0.6916  -0.2874 -0.0510 325  PRO G CG  
20053 C  CD  . PRO G  327 ? 3.6111 2.3629 3.3116 0.6672  -0.3378 -0.0321 325  PRO G CD  
20054 N  N   . CYS G  328 ? 3.1322 1.8547 3.1226 0.7300  -0.3106 -0.0923 326  CYS G N   
20055 C  CA  . CYS G  328 ? 2.9320 1.6514 2.9583 0.7239  -0.3219 -0.1285 326  CYS G CA  
20056 C  C   . CYS G  328 ? 2.7742 1.5238 2.8625 0.7077  -0.2637 -0.1580 326  CYS G C   
20057 O  O   . CYS G  328 ? 2.7612 1.5103 2.8823 0.7192  -0.2236 -0.1481 326  CYS G O   
20058 C  CB  . CYS G  328 ? 3.0438 1.8099 3.1243 0.7224  -0.3336 -0.0937 326  CYS G CB  
20059 S  SG  . CYS G  328 ? 3.2239 2.0190 3.2420 0.7074  -0.3935 -0.0477 326  CYS G SG  
20060 N  N   . CYS G  329 ? 2.5238 1.2957 2.6211 0.6808  -0.2646 -0.1905 327  CYS G N   
20061 C  CA  . CYS G  329 ? 2.5112 1.3144 2.6589 0.6623  -0.2177 -0.2125 327  CYS G CA  
20062 C  C   . CYS G  329 ? 2.5695 1.4124 2.7823 0.6532  -0.1927 -0.1943 327  CYS G C   
20063 O  O   . CYS G  329 ? 2.4543 1.3235 2.6774 0.6354  -0.2079 -0.2032 327  CYS G O   
20064 C  CB  . CYS G  329 ? 2.6076 1.4119 2.7254 0.6414  -0.2348 -0.2494 327  CYS G CB  
20065 S  SG  . CYS G  329 ? 2.8396 1.6775 3.0038 0.6226  -0.1865 -0.2716 327  CYS G SG  
20066 N  N   . VAL G  330 ? 2.5892 1.4307 2.8409 0.6671  -0.1552 -0.1696 328  VAL G N   
20067 C  CA  . VAL G  330 ? 2.1665 1.0312 2.4667 0.6643  -0.1273 -0.1533 328  VAL G CA  
20068 C  C   . VAL G  330 ? 2.1312 0.9937 2.4501 0.6514  -0.0799 -0.1692 328  VAL G C   
20069 O  O   . VAL G  330 ? 2.1731 1.0155 2.4844 0.6553  -0.0618 -0.1767 328  VAL G O   
20070 C  CB  . VAL G  330 ? 2.2195 1.0757 2.5424 0.6924  -0.1221 -0.1086 328  VAL G CB  
20071 C  CG1 . VAL G  330 ? 2.2653 1.1280 2.5652 0.7061  -0.1758 -0.0870 328  VAL G CG1 
20072 C  CG2 . VAL G  330 ? 2.3137 1.1361 2.6364 0.7094  -0.1006 -0.0936 328  VAL G CG2 
20073 N  N   . PRO G  331 ? 2.1309 1.0099 2.4675 0.6384  -0.0633 -0.1753 329  PRO G N   
20074 C  CA  . PRO G  331 ? 2.1148 0.9818 2.4531 0.6274  -0.0274 -0.1898 329  PRO G CA  
20075 C  C   . PRO G  331 ? 2.4485 1.2757 2.7887 0.6476  0.0033  -0.1681 329  PRO G C   
20076 O  O   . PRO G  331 ? 2.8582 1.6730 3.2073 0.6689  0.0059  -0.1392 329  PRO G O   
20077 C  CB  . PRO G  331 ? 2.0450 0.9348 2.3943 0.6115  -0.0286 -0.2014 329  PRO G CB  
20078 C  CG  . PRO G  331 ? 2.2264 1.1329 2.5898 0.6257  -0.0497 -0.1814 329  PRO G CG  
20079 C  CD  . PRO G  331 ? 2.0793 0.9875 2.4289 0.6334  -0.0838 -0.1736 329  PRO G CD  
20080 N  N   . GLN G  332 ? 2.4171 1.2229 2.7474 0.6433  0.0218  -0.1812 330  GLN G N   
20081 C  CA  . GLN G  332 ? 2.2594 1.0202 2.5845 0.6600  0.0404  -0.1660 330  GLN G CA  
20082 C  C   . GLN G  332 ? 2.3854 1.1268 2.7073 0.6485  0.0507  -0.1788 330  GLN G C   
20083 O  O   . GLN G  332 ? 2.8071 1.5135 3.1286 0.6626  0.0541  -0.1634 330  GLN G O   
20084 C  CB  . GLN G  332 ? 2.3416 1.0889 2.6644 0.6647  0.0456  -0.1738 330  GLN G CB  
20085 C  CG  . GLN G  332 ? 2.4184 1.1203 2.7453 0.6798  0.0525  -0.1589 330  GLN G CG  
20086 C  CD  . GLN G  332 ? 2.4755 1.1713 2.8117 0.6879  0.0558  -0.1658 330  GLN G CD  
20087 O  OE1 . GLN G  332 ? 2.4421 1.1650 2.7739 0.6845  0.0565  -0.1864 330  GLN G OE1 
20088 N  NE2 . GLN G  332 ? 2.5380 1.2025 2.9001 0.6972  0.0571  -0.1486 330  GLN G NE2 
20089 N  N   . ALA G  333 ? 2.3330 1.0957 2.6576 0.6225  0.0510  -0.2077 331  ALA G N   
20090 C  CA  . ALA G  333 ? 2.3797 1.1270 2.7098 0.6058  0.0577  -0.2245 331  ALA G CA  
20091 C  C   . ALA G  333 ? 2.1083 0.8918 2.4438 0.5878  0.0507  -0.2400 331  ALA G C   
20092 O  O   . ALA G  333 ? 2.0572 0.8816 2.3981 0.5738  0.0378  -0.2520 331  ALA G O   
20093 C  CB  . ALA G  333 ? 2.5218 1.2628 2.8659 0.5885  0.0623  -0.2448 331  ALA G CB  
20094 N  N   . LEU G  334 ? 2.3415 1.1090 2.6784 0.5896  0.0562  -0.2409 332  LEU G N   
20095 C  CA  . LEU G  334 ? 2.3615 1.1618 2.7097 0.5738  0.0497  -0.2577 332  LEU G CA  
20096 C  C   . LEU G  334 ? 2.4039 1.1779 2.7573 0.5575  0.0600  -0.2800 332  LEU G C   
20097 O  O   . LEU G  334 ? 2.1947 0.9182 2.5426 0.5643  0.0716  -0.2769 332  LEU G O   
20098 C  CB  . LEU G  334 ? 2.2426 1.0588 2.5959 0.5953  0.0448  -0.2391 332  LEU G CB  
20099 C  CG  . LEU G  334 ? 2.0832 0.9362 2.4437 0.6022  0.0258  -0.2231 332  LEU G CG  
20100 C  CD1 . LEU G  334 ? 2.1518 0.9774 2.5020 0.6277  0.0315  -0.1943 332  LEU G CD1 
20101 C  CD2 . LEU G  334 ? 2.0500 0.9381 2.4318 0.6097  0.0105  -0.2176 332  LEU G CD2 
20102 N  N   . GLU G  335 ? 2.2350 1.0424 2.6042 0.5339  0.0524  -0.3036 333  GLU G N   
20103 C  CA  . GLU G  335 ? 2.0958 0.8836 2.4752 0.5123  0.0604  -0.3299 333  GLU G CA  
20104 C  C   . GLU G  335 ? 2.0879 0.8916 2.4763 0.5126  0.0596  -0.3422 333  GLU G C   
20105 O  O   . GLU G  335 ? 2.0339 0.8875 2.4355 0.5124  0.0434  -0.3411 333  GLU G O   
20106 C  CB  . GLU G  335 ? 2.4340 1.2499 2.8345 0.4792  0.0510  -0.3523 333  GLU G CB  
20107 C  CG  . GLU G  335 ? 2.5286 1.3314 2.9293 0.4805  0.0538  -0.3444 333  GLU G CG  
20108 C  CD  . GLU G  335 ? 2.1834 1.0182 2.6143 0.4528  0.0449  -0.3661 333  GLU G CD  
20109 O  OE1 . GLU G  335 ? 1.9977 0.8601 2.4497 0.4289  0.0359  -0.3879 333  GLU G OE1 
20110 O  OE2 . GLU G  335 ? 2.0323 0.8661 2.4711 0.4567  0.0466  -0.3618 333  GLU G OE2 
20111 N  N   . PRO G  336 ? 2.2214 0.9821 2.6061 0.5136  0.0752  -0.3558 334  PRO G N   
20112 C  CA  . PRO G  336 ? 2.2512 1.0251 2.6460 0.5179  0.0776  -0.3712 334  PRO G CA  
20113 C  C   . PRO G  336 ? 2.3538 1.1728 2.7757 0.4810  0.0647  -0.4034 334  PRO G C   
20114 O  O   . PRO G  336 ? 2.3860 1.2167 2.8187 0.4514  0.0569  -0.4159 334  PRO G O   
20115 C  CB  . PRO G  336 ? 2.2547 0.9574 2.6334 0.5299  0.0986  -0.3792 334  PRO G CB  
20116 C  CG  . PRO G  336 ? 2.2835 0.9471 2.6574 0.5086  0.1020  -0.3827 334  PRO G CG  
20117 C  CD  . PRO G  336 ? 2.3834 1.0772 2.7568 0.5125  0.0902  -0.3583 334  PRO G CD  
20118 N  N   . LEU G  337 ? 2.3889 1.2366 2.8281 0.4846  0.0611  -0.4175 335  LEU G N   
20119 C  CA  . LEU G  337 ? 2.0654 0.9608 2.5359 0.4511  0.0444  -0.4497 335  LEU G CA  
20120 C  C   . LEU G  337 ? 2.0707 0.9503 2.5484 0.4509  0.0599  -0.4793 335  LEU G C   
20121 O  O   . LEU G  337 ? 2.0866 0.9718 2.5678 0.4819  0.0663  -0.4738 335  LEU G O   
20122 C  CB  . LEU G  337 ? 1.9473 0.9125 2.4426 0.4506  0.0120  -0.4423 335  LEU G CB  
20123 C  CG  . LEU G  337 ? 1.8966 0.9144 2.4295 0.4198  -0.0120 -0.4758 335  LEU G CG  
20124 C  CD1 . LEU G  337 ? 1.8771 0.9003 2.4195 0.3833  -0.0196 -0.4920 335  LEU G CD1 
20125 C  CD2 . LEU G  337 ? 1.8312 0.9098 2.3879 0.4244  -0.0499 -0.4690 335  LEU G CD2 
20126 N  N   . PRO G  338 ? 2.0937 0.9559 2.5768 0.4177  0.0669  -0.5123 336  PRO G N   
20127 C  CA  . PRO G  338 ? 2.2936 1.1441 2.7830 0.4136  0.0813  -0.5472 336  PRO G CA  
20128 C  C   . PRO G  338 ? 2.1994 1.1266 2.7303 0.3970  0.0579  -0.5709 336  PRO G C   
20129 O  O   . PRO G  338 ? 1.9966 0.9744 2.5533 0.3670  0.0299  -0.5765 336  PRO G O   
20130 C  CB  . PRO G  338 ? 2.4978 1.3010 2.9773 0.3770  0.0940  -0.5735 336  PRO G CB  
20131 C  CG  . PRO G  338 ? 2.1279 0.9604 2.6223 0.3508  0.0745  -0.5618 336  PRO G CG  
20132 C  CD  . PRO G  338 ? 2.0933 0.9400 2.5768 0.3841  0.0651  -0.5195 336  PRO G CD  
20133 N  N   . ILE G  339 ? 2.3760 1.3127 2.9166 0.4192  0.0678  -0.5864 337  ILE G N   
20134 C  CA  . ILE G  339 ? 2.0602 1.0715 2.6447 0.4071  0.0442  -0.6130 337  ILE G CA  
20135 C  C   . ILE G  339 ? 2.3431 1.3407 2.9310 0.3987  0.0678  -0.6597 337  ILE G C   
20136 O  O   . ILE G  339 ? 2.4673 1.3942 3.0209 0.4151  0.1028  -0.6656 337  ILE G O   
20137 C  CB  . ILE G  339 ? 1.9884 1.0463 2.5941 0.4450  0.0268  -0.5891 337  ILE G CB  
20138 C  CG1 . ILE G  339 ? 2.1256 1.1460 2.7165 0.4944  0.0613  -0.5800 337  ILE G CG1 
20139 C  CG2 . ILE G  339 ? 1.9423 1.0078 2.5373 0.4510  0.0049  -0.5457 337  ILE G CG2 
20140 C  CD1 . ILE G  339 ? 2.0340 1.1073 2.6543 0.5332  0.0449  -0.5567 337  ILE G CD1 
20141 N  N   . VAL G  340 ? 2.4218 1.4866 3.0498 0.3724  0.0462  -0.6957 338  VAL G N   
20142 C  CA  . VAL G  340 ? 2.4063 1.4739 3.0410 0.3604  0.0667  -0.7475 338  VAL G CA  
20143 C  C   . VAL G  340 ? 2.3013 1.4532 2.9836 0.3744  0.0450  -0.7676 338  VAL G C   
20144 O  O   . VAL G  340 ? 2.2245 1.4458 2.9438 0.3501  0.0009  -0.7724 338  VAL G O   
20145 C  CB  . VAL G  340 ? 2.2013 1.2699 2.8367 0.2995  0.0630  -0.7844 338  VAL G CB  
20146 C  CG1 . VAL G  340 ? 2.1444 1.2266 2.7849 0.2833  0.0827  -0.8422 338  VAL G CG1 
20147 C  CG2 . VAL G  340 ? 2.3252 1.3106 2.9175 0.2872  0.0843  -0.7689 338  VAL G CG2 
20148 N  N   . TYR G  341 ? 2.2629 1.4094 2.9454 0.4164  0.0737  -0.7793 339  TYR G N   
20149 C  CA  . TYR G  341 ? 2.2644 1.4969 2.9958 0.4352  0.0574  -0.8042 339  TYR G CA  
20150 C  C   . TYR G  341 ? 2.5294 1.7496 3.2529 0.4548  0.1028  -0.8482 339  TYR G C   
20151 O  O   . TYR G  341 ? 2.8685 2.0008 3.5444 0.4666  0.1450  -0.8477 339  TYR G O   
20152 C  CB  . TYR G  341 ? 2.2322 1.4963 2.9846 0.4850  0.0374  -0.7572 339  TYR G CB  
20153 C  CG  . TYR G  341 ? 2.3977 1.6038 3.1223 0.5429  0.0795  -0.7227 339  TYR G CG  
20154 C  CD1 . TYR G  341 ? 2.3399 1.4644 3.0165 0.5503  0.0951  -0.6793 339  TYR G CD1 
20155 C  CD2 . TYR G  341 ? 2.6764 1.9164 3.4252 0.5930  0.1021  -0.7334 339  TYR G CD2 
20156 C  CE1 . TYR G  341 ? 2.4162 1.4876 3.0672 0.6038  0.1288  -0.6478 339  TYR G CE1 
20157 C  CE2 . TYR G  341 ? 2.6908 1.8789 3.4163 0.6497  0.1391  -0.6982 339  TYR G CE2 
20158 C  CZ  . TYR G  341 ? 2.5644 1.6656 3.2398 0.6539  0.1503  -0.6557 339  TYR G CZ  
20159 O  OH  . TYR G  341 ? 2.6707 1.7205 3.3223 0.7111  0.1819  -0.6218 339  TYR G OH  
20160 N  N   . TYR G  342 ? 2.5335 1.8435 3.3018 0.4596  0.0921  -0.8890 340  TYR G N   
20161 C  CA  . TYR G  342 ? 2.8071 2.1238 3.5710 0.4800  0.1363  -0.9367 340  TYR G CA  
20162 C  C   . TYR G  342 ? 2.6027 1.9564 3.3927 0.5550  0.1522  -0.9152 340  TYR G C   
20163 O  O   . TYR G  342 ? 2.4345 1.8449 3.2624 0.5811  0.1167  -0.8779 340  TYR G O   
20164 C  CB  . TYR G  342 ? 2.8891 2.2953 3.6820 0.4319  0.1205  -1.0061 340  TYR G CB  
20165 C  CG  . TYR G  342 ? 2.7987 2.1634 3.5568 0.3608  0.1259  -1.0391 340  TYR G CG  
20166 C  CD1 . TYR G  342 ? 2.6750 2.0256 3.4313 0.3133  0.0888  -1.0138 340  TYR G CD1 
20167 C  CD2 . TYR G  342 ? 2.5595 1.9047 3.2863 0.3415  0.1680  -1.0948 340  TYR G CD2 
20168 C  CE1 . TYR G  342 ? 2.6289 1.9533 3.3588 0.2491  0.0928  -1.0399 340  TYR G CE1 
20169 C  CE2 . TYR G  342 ? 2.6250 1.9381 3.3196 0.2727  0.1704  -1.1232 340  TYR G CE2 
20170 C  CZ  . TYR G  342 ? 2.5823 1.8883 3.2812 0.2268  0.1323  -1.0940 340  TYR G CZ  
20171 O  OH  . TYR G  342 ? 2.4923 1.7759 3.1633 0.1592  0.1341  -1.1179 340  TYR G OH  
20172 N  N   . VAL G  343 ? 2.7644 2.0871 3.5331 0.5907  0.2051  -0.9389 341  VAL G N   
20173 C  CA  . VAL G  343 ? 2.9494 2.3150 3.7448 0.6661  0.2291  -0.9225 341  VAL G CA  
20174 C  C   . VAL G  343 ? 3.0935 2.5241 3.9016 0.6701  0.2600  -0.9918 341  VAL G C   
20175 O  O   . VAL G  343 ? 3.0409 2.3942 3.8002 0.6770  0.3091  -1.0199 341  VAL G O   
20176 C  CB  . VAL G  343 ? 3.0042 2.2576 3.7524 0.7199  0.2690  -0.8740 341  VAL G CB  
20177 C  CG1 . VAL G  343 ? 3.0357 2.3452 3.8182 0.8002  0.2940  -0.8535 341  VAL G CG1 
20178 C  CG2 . VAL G  343 ? 2.7468 1.9437 3.4752 0.7097  0.2409  -0.8114 341  VAL G CG2 
20179 N  N   . GLY G  344 ? 2.9504 2.5261 3.8193 0.6667  0.2296  -1.0218 342  GLY G N   
20180 C  CA  . GLY G  344 ? 2.8583 2.5192 3.7373 0.6606  0.2556  -1.0942 342  GLY G CA  
20181 C  C   . GLY G  344 ? 2.7373 2.3496 3.5714 0.5822  0.2626  -1.1513 342  GLY G C   
20182 O  O   . GLY G  344 ? 2.5969 2.2709 3.4494 0.5194  0.2183  -1.1793 342  GLY G O   
20183 N  N   . ARG G  345 ? 2.7758 2.2772 3.5482 0.5852  0.3156  -1.1680 343  ARG G N   
20184 C  CA  . ARG G  345 ? 2.7551 2.1977 3.4774 0.5111  0.3239  -1.2149 343  ARG G CA  
20185 C  C   . ARG G  345 ? 2.6671 1.9511 3.3312 0.4992  0.3320  -1.1754 343  ARG G C   
20186 O  O   . ARG G  345 ? 2.6923 1.9230 3.3152 0.4369  0.3347  -1.2053 343  ARG G O   
20187 C  CB  . ARG G  345 ? 3.1642 2.6214 3.8550 0.5140  0.3758  -1.2831 343  ARG G CB  
20188 C  CG  . ARG G  345 ? 3.1040 2.7276 3.8464 0.5431  0.3802  -1.3205 343  ARG G CG  
20189 C  CD  . ARG G  345 ? 3.0661 2.7042 3.7675 0.5405  0.4346  -1.3897 343  ARG G CD  
20190 N  NE  . ARG G  345 ? 2.8457 2.6466 3.5930 0.5859  0.4482  -1.4151 343  ARG G NE  
20191 C  CZ  . ARG G  345 ? 2.8630 2.6682 3.6202 0.6754  0.4897  -1.3928 343  ARG G CZ  
20192 N  NH1 . ARG G  345 ? 2.9253 2.5720 3.6451 0.7290  0.5209  -1.3476 343  ARG G NH1 
20193 N  NH2 . ARG G  345 ? 2.8655 2.8433 3.6683 0.7119  0.4990  -1.4136 343  ARG G NH2 
20194 N  N   . LYS G  346 ? 2.6341 1.8518 3.2933 0.5547  0.3336  -1.1092 344  LYS G N   
20195 C  CA  . LYS G  346 ? 2.7365 1.8119 3.3363 0.5522  0.3432  -1.0736 344  LYS G CA  
20196 C  C   . LYS G  346 ? 2.9485 2.0219 3.5630 0.5227  0.2965  -1.0208 344  LYS G C   
20197 O  O   . LYS G  346 ? 3.0309 2.1410 3.6788 0.5613  0.2759  -0.9704 344  LYS G O   
20198 C  CB  . LYS G  346 ? 2.8184 1.8160 3.3905 0.6356  0.3801  -1.0398 344  LYS G CB  
20199 C  CG  . LYS G  346 ? 3.1081 2.1211 3.6732 0.6815  0.4274  -1.0858 344  LYS G CG  
20200 C  CD  . LYS G  346 ? 3.1949 2.1221 3.7293 0.7675  0.4614  -1.0513 344  LYS G CD  
20201 C  CE  . LYS G  346 ? 3.2486 2.2026 3.7805 0.8215  0.5097  -1.0949 344  LYS G CE  
20202 N  NZ  . LYS G  346 ? 3.4189 2.3078 3.8935 0.7837  0.5375  -1.1665 344  LYS G NZ  
20203 N  N   . PRO G  347 ? 2.9254 1.9609 3.5156 0.4562  0.2793  -1.0294 345  PRO G N   
20204 C  CA  . PRO G  347 ? 2.4799 1.5100 3.0791 0.4326  0.2396  -0.9784 345  PRO G CA  
20205 C  C   . PRO G  347 ? 2.5476 1.4686 3.1008 0.4680  0.2542  -0.9270 345  PRO G C   
20206 O  O   . PRO G  347 ? 2.9144 1.7381 3.4155 0.4683  0.2825  -0.9413 345  PRO G O   
20207 C  CB  . PRO G  347 ? 2.4592 1.4952 3.0498 0.3516  0.2228  -1.0118 345  PRO G CB  
20208 C  CG  . PRO G  347 ? 2.8451 1.8259 3.3915 0.3376  0.2632  -1.0649 345  PRO G CG  
20209 C  CD  . PRO G  347 ? 3.1474 2.1534 3.7025 0.3975  0.2952  -1.0873 345  PRO G CD  
20210 N  N   . LYS G  348 ? 2.5485 1.4869 3.1196 0.4960  0.2316  -0.8695 346  LYS G N   
20211 C  CA  . LYS G  348 ? 2.7146 1.5655 3.2455 0.5292  0.2406  -0.8191 346  LYS G CA  
20212 C  C   . LYS G  348 ? 2.7173 1.5722 3.2485 0.4922  0.2069  -0.7828 346  LYS G C   
20213 O  O   . LYS G  348 ? 2.4859 1.4185 3.0570 0.4850  0.1738  -0.7623 346  LYS G O   
20214 C  CB  . LYS G  348 ? 2.6099 1.4760 3.1550 0.6027  0.2505  -0.7806 346  LYS G CB  
20215 C  CG  . LYS G  348 ? 2.7306 1.5907 3.2747 0.6512  0.2887  -0.8117 346  LYS G CG  
20216 C  CD  . LYS G  348 ? 2.7459 1.6213 3.3059 0.7278  0.2987  -0.7661 346  LYS G CD  
20217 C  CE  . LYS G  348 ? 2.9182 1.7907 3.4782 0.7833  0.3395  -0.7957 346  LYS G CE  
20218 N  NZ  . LYS G  348 ? 3.0798 1.8317 3.5760 0.7861  0.3681  -0.8268 346  LYS G NZ  
20219 N  N   . VAL G  349 ? 2.7101 1.4828 3.1985 0.4693  0.2138  -0.7779 347  VAL G N   
20220 C  CA  . VAL G  349 ? 2.4891 1.2588 2.9738 0.4418  0.1888  -0.7427 347  VAL G CA  
20221 C  C   . VAL G  349 ? 2.5179 1.2405 2.9784 0.4913  0.1938  -0.6905 347  VAL G C   
20222 O  O   . VAL G  349 ? 2.6208 1.2554 3.0421 0.5112  0.2141  -0.6876 347  VAL G O   
20223 C  CB  . VAL G  349 ? 2.5327 1.2502 2.9925 0.3880  0.1920  -0.7670 347  VAL G CB  
20224 C  CG1 . VAL G  349 ? 2.5297 1.2579 2.9945 0.3626  0.1676  -0.7325 347  VAL G CG1 
20225 C  CG2 . VAL G  349 ? 2.6282 1.3909 3.1080 0.3391  0.1903  -0.8218 347  VAL G CG2 
20226 N  N   . GLU G  350 ? 2.3928 1.1734 2.8773 0.5093  0.1722  -0.6511 348  GLU G N   
20227 C  CA  . GLU G  350 ? 2.4267 1.1768 2.8921 0.5544  0.1748  -0.6014 348  GLU G CA  
20228 C  C   . GLU G  350 ? 2.3393 1.1077 2.8036 0.5316  0.1499  -0.5676 348  GLU G C   
20229 O  O   . GLU G  350 ? 2.2578 1.0807 2.7463 0.4911  0.1261  -0.5774 348  GLU G O   
20230 C  CB  . GLU G  350 ? 2.4767 1.2778 2.9701 0.6058  0.1763  -0.5823 348  GLU G CB  
20231 C  CG  . GLU G  350 ? 2.6431 1.4325 3.1408 0.6380  0.2048  -0.6149 348  GLU G CG  
20232 C  CD  . GLU G  350 ? 2.6562 1.4881 3.1809 0.7000  0.2110  -0.5877 348  GLU G CD  
20233 O  OE1 . GLU G  350 ? 2.8400 1.6629 3.3681 0.7384  0.2379  -0.6092 348  GLU G OE1 
20234 O  OE2 . GLU G  350 ? 2.5369 1.4121 3.0800 0.7117  0.1896  -0.5450 348  GLU G OE2 
20235 N  N   . GLN G  351 ? 2.3736 1.0974 2.8108 0.5607  0.1541  -0.5290 349  GLN G N   
20236 C  CA  . GLN G  351 ? 2.3221 1.0543 2.7524 0.5447  0.1362  -0.4981 349  GLN G CA  
20237 C  C   . GLN G  351 ? 2.3685 1.1202 2.7991 0.5871  0.1303  -0.4533 349  GLN G C   
20238 O  O   . GLN G  351 ? 2.3732 1.0802 2.7862 0.6298  0.1447  -0.4350 349  GLN G O   
20239 C  CB  . GLN G  351 ? 2.3881 1.0439 2.7871 0.5283  0.1452  -0.4992 349  GLN G CB  
20240 C  CG  . GLN G  351 ? 2.3646 1.0329 2.7609 0.5113  0.1295  -0.4726 349  GLN G CG  
20241 C  CD  . GLN G  351 ? 2.4325 1.0292 2.8087 0.4958  0.1378  -0.4742 349  GLN G CD  
20242 O  OE1 . GLN G  351 ? 2.4984 1.0253 2.8575 0.5061  0.1535  -0.4861 349  GLN G OE1 
20243 N  NE2 . GLN G  351 ? 2.4528 1.0667 2.8360 0.4711  0.1263  -0.4635 349  GLN G NE2 
20244 N  N   . LEU G  352 ? 2.5712 1.3891 3.0239 0.5751  0.1059  -0.4368 350  LEU G N   
20245 C  CA  . LEU G  352 ? 2.3843 1.2249 2.8396 0.6075  0.0970  -0.3952 350  LEU G CA  
20246 C  C   . LEU G  352 ? 2.3069 1.1066 2.7306 0.6067  0.0974  -0.3687 350  LEU G C   
20247 O  O   . LEU G  352 ? 2.2053 0.9940 2.6196 0.5720  0.0927  -0.3800 350  LEU G O   
20248 C  CB  . LEU G  352 ? 2.2024 1.1256 2.6948 0.5928  0.0650  -0.3928 350  LEU G CB  
20249 C  CG  . LEU G  352 ? 2.2803 1.2582 2.8147 0.5933  0.0548  -0.4197 350  LEU G CG  
20250 C  CD1 . LEU G  352 ? 2.1925 1.2450 2.7605 0.5772  0.0105  -0.4168 350  LEU G CD1 
20251 C  CD2 . LEU G  352 ? 2.6379 1.6100 3.1824 0.6448  0.0765  -0.4086 350  LEU G CD2 
20252 N  N   . SER G  353 ? 2.5530 1.3354 2.9658 0.6466  0.1017  -0.3335 351  SER G N   
20253 C  CA  . SER G  353 ? 2.6790 1.4231 3.0658 0.6508  0.1009  -0.3088 351  SER G CA  
20254 C  C   . SER G  353 ? 2.4700 1.2633 2.8654 0.6449  0.0821  -0.2842 351  SER G C   
20255 O  O   . SER G  353 ? 2.2431 1.0821 2.6610 0.6636  0.0713  -0.2660 351  SER G O   
20256 C  CB  . SER G  353 ? 3.0339 1.7267 3.4071 0.6971  0.1107  -0.2870 351  SER G CB  
20257 O  OG  . SER G  353 ? 3.1513 1.8830 3.5451 0.7364  0.1081  -0.2647 351  SER G OG  
20258 N  N   . ASN G  354 ? 2.5501 1.3336 2.9314 0.6197  0.0770  -0.2850 352  ASN G N   
20259 C  CA  . ASN G  354 ? 2.4629 1.2811 2.8464 0.6130  0.0606  -0.2670 352  ASN G CA  
20260 C  C   . ASN G  354 ? 2.4408 1.3268 2.8521 0.5946  0.0357  -0.2769 352  ASN G C   
20261 O  O   . ASN G  354 ? 2.4354 1.3547 2.8653 0.6130  0.0216  -0.2598 352  ASN G O   
20262 C  CB  . ASN G  354 ? 2.4532 1.2586 2.8300 0.6501  0.0615  -0.2285 352  ASN G CB  
20263 C  CG  . ASN G  354 ? 2.6739 1.4136 3.0262 0.6658  0.0737  -0.2181 352  ASN G CG  
20264 O  OD1 . ASN G  354 ? 2.8798 1.6036 3.2210 0.6550  0.0717  -0.2142 352  ASN G OD1 
20265 N  ND2 . ASN G  354 ? 2.8975 1.5997 3.2473 0.6926  0.0822  -0.2151 352  ASN G ND2 
20266 N  N   . MET G  355 ? 2.2454 1.1528 2.6626 0.5589  0.0237  -0.3033 353  MET G N   
20267 C  CA  . MET G  355 ? 2.1141 1.0811 2.5561 0.5396  -0.0089 -0.3163 353  MET G CA  
20268 C  C   . MET G  355 ? 1.8972 0.8791 2.3316 0.5169  -0.0264 -0.3207 353  MET G C   
20269 O  O   . MET G  355 ? 1.8617 0.8732 2.2986 0.5160  -0.0548 -0.3135 353  MET G O   
20270 C  CB  . MET G  355 ? 2.3409 1.3273 2.8061 0.5207  -0.0121 -0.3485 353  MET G CB  
20271 C  CG  . MET G  355 ? 2.3412 1.3202 2.8187 0.5459  0.0037  -0.3502 353  MET G CG  
20272 S  SD  . MET G  355 ? 3.0576 2.0847 3.5629 0.5764  -0.0207 -0.3275 353  MET G SD  
20273 C  CE  . MET G  355 ? 2.6423 1.7350 3.1757 0.5425  -0.0727 -0.3525 353  MET G CE  
20274 N  N   . ILE G  356 ? 1.9091 0.8684 2.3349 0.5003  -0.0121 -0.3336 354  ILE G N   
20275 C  CA  . ILE G  356 ? 1.8803 0.8546 2.3041 0.4834  -0.0251 -0.3392 354  ILE G CA  
20276 C  C   . ILE G  356 ? 1.9082 0.8559 2.3076 0.5035  -0.0142 -0.3160 354  ILE G C   
20277 O  O   . ILE G  356 ? 2.0875 0.9922 2.4732 0.5157  0.0101  -0.3071 354  ILE G O   
20278 C  CB  . ILE G  356 ? 1.8847 0.8514 2.3204 0.4591  -0.0165 -0.3627 354  ILE G CB  
20279 C  CG1 . ILE G  356 ? 1.8517 0.8519 2.3172 0.4355  -0.0320 -0.3890 354  ILE G CG1 
20280 C  CG2 . ILE G  356 ? 1.8675 0.8448 2.3039 0.4514  -0.0242 -0.3642 354  ILE G CG2 
20281 C  CD1 . ILE G  356 ? 1.8918 0.8655 2.3596 0.4377  -0.0115 -0.4003 354  ILE G CD1 
20282 N  N   . VAL G  357 ? 1.8792 0.8494 2.2737 0.5064  -0.0355 -0.3086 355  VAL G N   
20283 C  CA  . VAL G  357 ? 1.9062 0.8542 2.2806 0.5251  -0.0274 -0.2904 355  VAL G CA  
20284 C  C   . VAL G  357 ? 1.9196 0.8608 2.2900 0.5174  -0.0196 -0.3017 355  VAL G C   
20285 O  O   . VAL G  357 ? 2.0768 1.0459 2.4535 0.5038  -0.0382 -0.3161 355  VAL G O   
20286 C  CB  . VAL G  357 ? 1.8865 0.8553 2.2558 0.5317  -0.0568 -0.2816 355  VAL G CB  
20287 C  CG1 . VAL G  357 ? 1.9161 0.8626 2.2664 0.5477  -0.0504 -0.2698 355  VAL G CG1 
20288 C  CG2 . VAL G  357 ? 1.8884 0.8640 2.2680 0.5454  -0.0658 -0.2665 355  VAL G CG2 
20289 N  N   . ARG G  358 ? 1.9701 0.8740 2.3325 0.5291  0.0050  -0.2945 356  ARG G N   
20290 C  CA  . ARG G  358 ? 1.9656 0.8644 2.3324 0.5258  0.0121  -0.3053 356  ARG G CA  
20291 C  C   . ARG G  358 ? 1.9948 0.8882 2.3463 0.5464  0.0125  -0.2948 356  ARG G C   
20292 O  O   . ARG G  358 ? 1.9921 0.9087 2.3432 0.5442  -0.0001 -0.3054 356  ARG G O   
20293 C  CB  . ARG G  358 ? 2.2157 1.0774 2.5906 0.5242  0.0319  -0.3076 356  ARG G CB  
20294 C  CG  . ARG G  358 ? 2.3039 1.1666 2.7000 0.5185  0.0368  -0.3212 356  ARG G CG  
20295 C  CD  . ARG G  358 ? 2.2264 1.1301 2.6498 0.4949  0.0231  -0.3444 356  ARG G CD  
20296 N  NE  . ARG G  358 ? 2.3821 1.2841 2.8255 0.4696  0.0233  -0.3588 356  ARG G NE  
20297 C  CZ  . ARG G  358 ? 2.2542 1.1895 2.7301 0.4453  0.0110  -0.3802 356  ARG G CZ  
20298 N  NH1 . ARG G  358 ? 1.8944 0.8669 2.3866 0.4460  -0.0039 -0.3870 356  ARG G NH1 
20299 N  NH2 . ARG G  358 ? 2.3134 1.2431 2.8067 0.4219  0.0130  -0.3955 356  ARG G NH2 
20300 N  N   . SER G  359 ? 2.0235 0.8841 2.3635 0.5678  0.0255  -0.2749 357  SER G N   
20301 C  CA  . SER G  359 ? 2.0466 0.8981 2.3763 0.5884  0.0271  -0.2663 357  SER G CA  
20302 C  C   . SER G  359 ? 2.0425 0.8988 2.3645 0.5982  0.0120  -0.2501 357  SER G C   
20303 O  O   . SER G  359 ? 2.0282 0.8916 2.3549 0.5944  0.0043  -0.2407 357  SER G O   
20304 C  CB  . SER G  359 ? 2.1002 0.9127 2.4318 0.6062  0.0456  -0.2551 357  SER G CB  
20305 O  OG  . SER G  359 ? 2.1052 0.9146 2.4554 0.5942  0.0532  -0.2717 357  SER G OG  
20306 N  N   . CYS G  360 ? 2.1868 1.0397 2.4997 0.6123  0.0043  -0.2494 358  CYS G N   
20307 C  CA  . CYS G  360 ? 2.2425 1.0951 2.5473 0.6227  -0.0194 -0.2366 358  CYS G CA  
20308 C  C   . CYS G  360 ? 2.4495 1.2756 2.7482 0.6473  -0.0148 -0.2272 358  CYS G C   
20309 O  O   . CYS G  360 ? 2.5828 1.4036 2.8770 0.6541  -0.0036 -0.2431 358  CYS G O   
20310 C  CB  . CYS G  360 ? 2.1614 1.0363 2.4472 0.6103  -0.0548 -0.2559 358  CYS G CB  
20311 S  SG  . CYS G  360 ? 2.1634 1.0735 2.4606 0.5817  -0.0699 -0.2679 358  CYS G SG  
20312 N  N   . LYS G  361 ? 2.5675 1.3793 2.8682 0.6634  -0.0263 -0.2007 359  LYS G N   
20313 C  CA  . LYS G  361 ? 2.7706 1.5551 3.0634 0.6892  -0.0311 -0.1866 359  LYS G CA  
20314 C  C   . LYS G  361 ? 2.9353 1.7133 3.1900 0.7004  -0.0765 -0.1798 359  LYS G C   
20315 O  O   . LYS G  361 ? 2.9866 1.7820 3.2300 0.6877  -0.1026 -0.1838 359  LYS G O   
20316 C  CB  . LYS G  361 ? 2.5653 1.3250 2.8871 0.7037  -0.0058 -0.1515 359  LYS G CB  
20317 C  CG  . LYS G  361 ? 2.5455 1.3094 2.8818 0.7065  -0.0095 -0.1208 359  LYS G CG  
20318 C  CD  . LYS G  361 ? 2.7031 1.4304 3.0514 0.7268  0.0121  -0.0848 359  LYS G CD  
20319 C  CE  . LYS G  361 ? 2.6862 1.4179 3.0416 0.7368  0.0093  -0.0568 359  LYS G CE  
20320 N  NZ  . LYS G  361 ? 2.5654 1.2533 2.9130 0.7604  0.0129  -0.0280 359  LYS G NZ  
20321 N  N   . CYS G  362 ? 2.8553 1.6011 3.0768 0.7270  -0.0906 -0.1691 360  CYS G N   
20322 C  CA  . CYS G  362 ? 2.7173 1.4381 2.8745 0.7442  -0.1373 -0.1570 360  CYS G CA  
20323 C  C   . CYS G  362 ? 2.8791 1.5759 3.0370 0.7720  -0.1410 -0.1062 360  CYS G C   
20324 O  O   . CYS G  362 ? 3.1242 1.8177 3.2745 0.7780  -0.1167 -0.0920 360  CYS G O   
20325 C  CB  . CYS G  362 ? 2.8663 1.5541 2.9408 0.7559  -0.1565 -0.1923 360  CYS G CB  
20326 S  SG  . CYS G  362 ? 3.2968 2.0106 3.3698 0.7267  -0.1547 -0.2437 360  CYS G SG  
20327 N  N   . SER G  363 ? 2.8499 1.5582 3.0196 0.7754  -0.1633 -0.0697 361  SER G N   
20328 C  CA  . SER G  363 ? 3.1382 1.8646 3.3162 0.7821  -0.1570 -0.0059 361  SER G CA  
20329 C  C   . SER G  363 ? 3.2412 2.0013 3.3865 0.7751  -0.1956 0.0302  361  SER G C   
20330 O  O   . SER G  363 ? 3.1136 1.8735 3.2316 0.7665  -0.2283 0.0034  361  SER G O   
20331 C  CB  . SER G  363 ? 3.3071 2.0187 3.5736 0.7988  -0.1255 0.0155  361  SER G CB  
20332 O  OG  . SER G  363 ? 3.4480 2.1993 3.7618 0.7791  -0.1139 0.0050  361  SER G OG  
20333 O  OXT . SER G  363 ? 3.4207 2.2124 3.5654 0.7755  -0.1965 0.0900  361  SER G OXT 
20334 N  N   . LYS H  7   ? 3.4004 1.7338 2.7308 0.4798  -0.7654 -0.3157 5    LYS H N   
20335 C  CA  . LYS H  7   ? 3.5618 1.7960 2.7900 0.4818  -0.7661 -0.3609 5    LYS H CA  
20336 C  C   . LYS H  7   ? 3.8501 2.0020 3.0034 0.4480  -0.8259 -0.3833 5    LYS H C   
20337 O  O   . LYS H  7   ? 4.0913 2.1614 3.1276 0.4267  -0.8486 -0.4054 5    LYS H O   
20338 C  CB  . LYS H  7   ? 3.3868 1.6307 2.5302 0.4635  -0.7593 -0.3393 5    LYS H CB  
20339 C  CG  . LYS H  7   ? 3.4090 1.5751 2.4758 0.4854  -0.7295 -0.3889 5    LYS H CG  
20340 C  CD  . LYS H  7   ? 3.5989 1.7617 2.5522 0.4494  -0.7413 -0.3699 5    LYS H CD  
20341 C  CE  . LYS H  7   ? 3.6141 1.7327 2.4666 0.3896  -0.8104 -0.3597 5    LYS H CE  
20342 N  NZ  . LYS H  7   ? 3.7296 1.8514 2.4679 0.3468  -0.8250 -0.3377 5    LYS H NZ  
20343 N  N   . THR H  8   ? 3.5627 1.7338 2.7803 0.4404  -0.8526 -0.3774 6    THR H N   
20344 C  CA  . THR H  8   ? 3.4811 1.5881 2.6387 0.4025  -0.9121 -0.3889 6    THR H CA  
20345 C  C   . THR H  8   ? 3.2158 1.4123 2.4871 0.4095  -0.8843 -0.3896 6    THR H C   
20346 O  O   . THR H  8   ? 3.0116 1.2598 2.3458 0.3963  -0.9085 -0.3662 6    THR H O   
20347 C  CB  . THR H  8   ? 3.4711 1.6219 2.5890 0.3430  -0.9704 -0.3378 6    THR H CB  
20348 O  OG1 . THR H  8   ? 3.8022 2.0027 2.8777 0.3285  -0.9587 -0.3027 6    THR H OG1 
20349 C  CG2 . THR H  8   ? 3.2965 1.3465 2.3047 0.2958  -1.0359 -0.3533 6    THR H CG2 
20350 N  N   . ILE H  9   ? 3.3581 1.5693 2.6522 0.4297  -0.8344 -0.4161 7    ILE H N   
20351 C  CA  . ILE H  9   ? 3.4272 1.6968 2.8010 0.4303  -0.8154 -0.4198 7    ILE H CA  
20352 C  C   . ILE H  9   ? 3.4778 1.8578 2.9793 0.4446  -0.7723 -0.4063 7    ILE H C   
20353 O  O   . ILE H  9   ? 3.4009 1.8323 2.9695 0.4616  -0.7193 -0.4173 7    ILE H O   
20354 C  CB  . ILE H  9   ? 3.1791 1.4103 2.5116 0.3909  -0.8858 -0.4083 7    ILE H CB  
20355 C  CG1 . ILE H  9   ? 3.1166 1.2429 2.3323 0.3763  -0.9133 -0.4259 7    ILE H CG1 
20356 C  CG2 . ILE H  9   ? 3.1346 1.4339 2.5587 0.3914  -0.8727 -0.4052 7    ILE H CG2 
20357 C  CD1 . ILE H  9   ? 3.2656 1.3055 2.3596 0.3506  -0.9580 -0.4224 7    ILE H CD1 
20358 N  N   . ASP H  10  ? 3.2225 1.6358 2.7560 0.4356  -0.7961 -0.3816 8    ASP H N   
20359 C  CA  . ASP H  10  ? 2.7845 1.2972 2.4316 0.4471  -0.7546 -0.3693 8    ASP H CA  
20360 C  C   . ASP H  10  ? 2.7345 1.2966 2.4408 0.4297  -0.7634 -0.3692 8    ASP H C   
20361 O  O   . ASP H  10  ? 2.6507 1.1830 2.3302 0.4206  -0.7777 -0.3813 8    ASP H O   
20362 C  CB  . ASP H  10  ? 2.7099 1.2642 2.4065 0.4780  -0.6755 -0.3783 8    ASP H CB  
20363 C  CG  . ASP H  10  ? 2.9043 1.4239 2.5596 0.4971  -0.6684 -0.3710 8    ASP H CG  
20364 O  OD1 . ASP H  10  ? 3.1473 1.6312 2.7602 0.4885  -0.7200 -0.3515 8    ASP H OD1 
20365 O  OD2 . ASP H  10  ? 2.8944 1.4202 2.5591 0.5207  -0.6153 -0.3815 8    ASP H OD2 
20366 N  N   . MET H  11  ? 2.9936 1.6279 2.7793 0.4268  -0.7548 -0.3555 9    MET H N   
20367 C  CA  . MET H  11  ? 2.7134 1.3934 2.5527 0.4085  -0.7705 -0.3544 9    MET H CA  
20368 C  C   . MET H  11  ? 2.3741 1.1370 2.3076 0.4204  -0.7057 -0.3577 9    MET H C   
20369 O  O   . MET H  11  ? 2.3260 1.1118 2.2852 0.4407  -0.6484 -0.3582 9    MET H O   
20370 C  CB  . MET H  11  ? 3.0081 1.6893 2.8461 0.3854  -0.8369 -0.3351 9    MET H CB  
20371 C  CG  . MET H  11  ? 3.4774 2.0718 3.2177 0.3608  -0.9138 -0.3253 9    MET H CG  
20372 S  SD  . MET H  11  ? 4.0806 2.6782 3.8257 0.3375  -0.9858 -0.2935 9    MET H SD  
20373 C  CE  . MET H  11  ? 3.6322 2.2359 3.3837 0.3745  -0.9505 -0.2771 9    MET H CE  
20374 N  N   . GLU H  12  ? 2.6618 1.4642 2.6421 0.4040  -0.7206 -0.3581 10   GLU H N   
20375 C  CA  . GLU H  12  ? 2.6571 1.5330 2.7205 0.4062  -0.6757 -0.3597 10   GLU H CA  
20376 C  C   . GLU H  12  ? 2.3236 1.2373 2.4251 0.4001  -0.6932 -0.3486 10   GLU H C   
20377 O  O   . GLU H  12  ? 2.2157 1.1860 2.3821 0.4002  -0.6604 -0.3512 10   GLU H O   
20378 C  CB  . GLU H  12  ? 3.1250 2.0201 3.2182 0.3928  -0.6866 -0.3670 10   GLU H CB  
20379 C  CG  . GLU H  12  ? 2.8141 1.7676 2.9768 0.3982  -0.6299 -0.3729 10   GLU H CG  
20380 C  CD  . GLU H  12  ? 2.6158 1.5927 2.8151 0.3828  -0.6540 -0.3770 10   GLU H CD  
20381 O  OE1 . GLU H  12  ? 2.5666 1.5658 2.7900 0.3636  -0.6980 -0.3730 10   GLU H OE1 
20382 O  OE2 . GLU H  12  ? 2.4049 1.3758 2.6099 0.3910  -0.6328 -0.3836 10   GLU H OE2 
20383 N  N   . LEU H  13  ? 2.5038 1.3813 2.5625 0.3947  -0.7480 -0.3362 11   LEU H N   
20384 C  CA  . LEU H  13  ? 2.6073 1.5143 2.6989 0.3962  -0.7676 -0.3220 11   LEU H CA  
20385 C  C   . LEU H  13  ? 2.6556 1.5900 2.7776 0.4246  -0.7064 -0.3152 11   LEU H C   
20386 O  O   . LEU H  13  ? 2.8397 1.8143 3.0081 0.4344  -0.7014 -0.3043 11   LEU H O   
20387 C  CB  . LEU H  13  ? 2.6883 1.5381 2.7168 0.3822  -0.8491 -0.3036 11   LEU H CB  
20388 C  CG  . LEU H  13  ? 2.4785 1.3414 2.5204 0.3933  -0.8792 -0.2749 11   LEU H CG  
20389 C  CD1 . LEU H  13  ? 2.3939 1.3306 2.5163 0.3918  -0.8816 -0.2721 11   LEU H CD1 
20390 C  CD2 . LEU H  13  ? 2.6459 1.4802 2.6039 0.3575  -0.9493 -0.2453 11   LEU H CD2 
20391 N  N   . VAL H  14  ? 2.3479 1.2604 2.4460 0.4396  -0.6601 -0.3198 12   VAL H N   
20392 C  CA  . VAL H  14  ? 2.1708 1.1063 2.2995 0.4638  -0.5998 -0.3108 12   VAL H CA  
20393 C  C   . VAL H  14  ? 2.2364 1.2340 2.4401 0.4625  -0.5521 -0.3158 12   VAL H C   
20394 O  O   . VAL H  14  ? 2.4177 1.4419 2.6582 0.4783  -0.5206 -0.3039 12   VAL H O   
20395 C  CB  . VAL H  14  ? 2.2028 1.1036 2.2960 0.4762  -0.5608 -0.3176 12   VAL H CB  
20396 C  CG1 . VAL H  14  ? 2.1934 1.1117 2.3169 0.4992  -0.5032 -0.3045 12   VAL H CG1 
20397 C  CG2 . VAL H  14  ? 2.4218 1.2506 2.4297 0.4757  -0.6118 -0.3177 12   VAL H CG2 
20398 N  N   . LYS H  15  ? 2.1980 1.2153 2.4227 0.4443  -0.5483 -0.3323 13   LYS H N   
20399 C  CA  . LYS H  15  ? 1.9291 0.9967 2.2160 0.4389  -0.5115 -0.3396 13   LYS H CA  
20400 C  C   . LYS H  15  ? 1.9246 1.0234 2.2468 0.4366  -0.5416 -0.3369 13   LYS H C   
20401 O  O   . LYS H  15  ? 2.0112 1.1421 2.3776 0.4448  -0.5032 -0.3374 13   LYS H O   
20402 C  CB  . LYS H  15  ? 1.8914 0.9702 2.1905 0.4209  -0.5123 -0.3550 13   LYS H CB  
20403 C  CG  . LYS H  15  ? 1.8968 0.9483 2.1674 0.4280  -0.4826 -0.3585 13   LYS H CG  
20404 C  CD  . LYS H  15  ? 1.8615 0.9282 2.1526 0.4148  -0.4870 -0.3703 13   LYS H CD  
20405 C  CE  . LYS H  15  ? 1.8704 0.9124 2.1397 0.4275  -0.4550 -0.3741 13   LYS H CE  
20406 N  NZ  . LYS H  15  ? 1.8487 0.9069 2.1445 0.4192  -0.4602 -0.3829 13   LYS H NZ  
20407 N  N   . ARG H  16  ? 1.9182 1.0027 2.2185 0.4268  -0.6116 -0.3331 14   ARG H N   
20408 C  CA  . ARG H  16  ? 1.9190 1.0341 2.2551 0.4279  -0.6467 -0.3287 14   ARG H CA  
20409 C  C   . ARG H  16  ? 1.9400 1.0621 2.2829 0.4580  -0.6334 -0.3063 14   ARG H C   
20410 O  O   . ARG H  16  ? 1.9269 1.0918 2.3179 0.4711  -0.6332 -0.3020 14   ARG H O   
20411 C  CB  . ARG H  16  ? 2.0832 1.1737 2.3900 0.4062  -0.7330 -0.3245 14   ARG H CB  
20412 C  CG  . ARG H  16  ? 2.1161 1.2135 2.4351 0.3776  -0.7542 -0.3422 14   ARG H CG  
20413 C  CD  . ARG H  16  ? 2.4257 1.5821 2.8177 0.3752  -0.7284 -0.3587 14   ARG H CD  
20414 N  NE  . ARG H  16  ? 2.3854 1.5698 2.8120 0.3888  -0.7506 -0.3522 14   ARG H NE  
20415 C  CZ  . ARG H  16  ? 2.0616 1.2958 2.5512 0.3918  -0.7352 -0.3689 14   ARG H CZ  
20416 N  NH1 . ARG H  16  ? 1.9241 1.1795 2.4441 0.3758  -0.7018 -0.3926 14   ARG H NH1 
20417 N  NH2 . ARG H  16  ? 2.0623 1.3647 2.5720 0.3964  -0.7393 -0.3510 14   ARG H NH2 
20418 N  N   . LYS H  17  ? 2.1403 1.2247 2.4389 0.4721  -0.6222 -0.2907 15   LYS H N   
20419 C  CA  . LYS H  17  ? 2.2447 1.3384 2.5525 0.5036  -0.6053 -0.2630 15   LYS H CA  
20420 C  C   . LYS H  17  ? 2.1579 1.2826 2.5161 0.5195  -0.5262 -0.2667 15   LYS H C   
20421 O  O   . LYS H  17  ? 2.0631 1.2164 2.4558 0.5459  -0.5080 -0.2471 15   LYS H O   
20422 C  CB  . LYS H  17  ? 2.2789 1.3178 2.5223 0.5117  -0.6177 -0.2469 15   LYS H CB  
20423 C  CG  . LYS H  17  ? 2.4593 1.4575 2.6418 0.5010  -0.7037 -0.2292 15   LYS H CG  
20424 C  CD  . LYS H  17  ? 2.6825 1.6179 2.7932 0.5093  -0.7133 -0.2162 15   LYS H CD  
20425 C  CE  . LYS H  17  ? 2.4600 1.3849 2.4922 0.4748  -0.7846 -0.1888 15   LYS H CE  
20426 N  NZ  . LYS H  17  ? 2.5069 1.3715 2.4568 0.4729  -0.7906 -0.1817 15   LYS H NZ  
20427 N  N   . ARG H  18  ? 2.0019 1.1193 2.3619 0.5047  -0.4801 -0.2871 16   ARG H N   
20428 C  CA  . ARG H  18  ? 1.9937 1.1295 2.3927 0.5116  -0.4115 -0.2912 16   ARG H CA  
20429 C  C   . ARG H  18  ? 2.0803 1.2575 2.5284 0.5060  -0.4118 -0.3069 16   ARG H C   
20430 O  O   . ARG H  18  ? 2.0056 1.1983 2.4865 0.5233  -0.3709 -0.3029 16   ARG H O   
20431 C  CB  . ARG H  18  ? 1.8920 1.0094 2.2761 0.4962  -0.3734 -0.3046 16   ARG H CB  
20432 C  CG  . ARG H  18  ? 2.2444 1.3721 2.6600 0.4948  -0.3132 -0.3117 16   ARG H CG  
20433 C  CD  . ARG H  18  ? 2.2505 1.3558 2.6644 0.5190  -0.2646 -0.2906 16   ARG H CD  
20434 N  NE  . ARG H  18  ? 2.1162 1.2197 2.5517 0.5173  -0.2135 -0.2973 16   ARG H NE  
20435 C  CZ  . ARG H  18  ? 2.1889 1.2652 2.6219 0.5355  -0.1679 -0.2813 16   ARG H CZ  
20436 N  NH1 . ARG H  18  ? 2.7038 1.7602 3.1222 0.5574  -0.1654 -0.2563 16   ARG H NH1 
20437 N  NH2 . ARG H  18  ? 2.0926 1.1571 2.5353 0.5315  -0.1290 -0.2904 16   ARG H NH2 
20438 N  N   . ILE H  19  ? 2.0539 1.2457 2.5068 0.4826  -0.4580 -0.3258 17   ILE H N   
20439 C  CA  . ILE H  19  ? 1.9282 1.1601 2.4297 0.4754  -0.4634 -0.3457 17   ILE H CA  
20440 C  C   . ILE H  19  ? 1.9435 1.2059 2.4758 0.5034  -0.4801 -0.3334 17   ILE H C   
20441 O  O   . ILE H  19  ? 1.7822 1.0735 2.3570 0.5164  -0.4459 -0.3439 17   ILE H O   
20442 C  CB  . ILE H  19  ? 1.7542 0.9929 2.2550 0.4450  -0.5183 -0.3642 17   ILE H CB  
20443 C  CG1 . ILE H  19  ? 1.7236 0.9460 2.2070 0.4245  -0.4929 -0.3736 17   ILE H CG1 
20444 C  CG2 . ILE H  19  ? 1.7521 1.0339 2.3065 0.4392  -0.5350 -0.3858 17   ILE H CG2 
20445 C  CD1 . ILE H  19  ? 1.8800 1.1102 2.3679 0.3973  -0.5419 -0.3875 17   ILE H CD1 
20446 N  N   . GLU H  20  ? 2.2947 1.5529 2.8052 0.5153  -0.5336 -0.3088 18   GLU H N   
20447 C  CA  . GLU H  20  ? 2.3129 1.6169 2.8576 0.5478  -0.5534 -0.2863 18   GLU H CA  
20448 C  C   . GLU H  20  ? 2.1323 1.4402 2.6904 0.5830  -0.4932 -0.2634 18   GLU H C   
20449 O  O   . GLU H  20  ? 1.8850 1.2435 2.4865 0.6150  -0.4860 -0.2484 18   GLU H O   
20450 C  CB  . GLU H  20  ? 2.3281 1.6474 2.8307 0.5348  -0.6270 -0.2516 18   GLU H CB  
20451 C  CG  . GLU H  20  ? 2.1209 1.4716 2.6053 0.4845  -0.6817 -0.2597 18   GLU H CG  
20452 C  CD  . GLU H  20  ? 2.2183 1.6625 2.7534 0.4739  -0.6748 -0.2677 18   GLU H CD  
20453 O  OE1 . GLU H  20  ? 2.3215 1.8320 2.8887 0.5001  -0.6472 -0.2484 18   GLU H OE1 
20454 O  OE2 . GLU H  20  ? 2.2336 1.6876 2.7767 0.4405  -0.6964 -0.2925 18   GLU H OE2 
20455 N  N   . ALA H  21  ? 2.2291 1.4893 2.7540 0.5798  -0.4498 -0.2580 19   ALA H N   
20456 C  CA  . ALA H  21  ? 2.3384 1.5930 2.8771 0.6100  -0.3901 -0.2359 19   ALA H CA  
20457 C  C   . ALA H  21  ? 2.3566 1.6081 2.9222 0.6070  -0.3254 -0.2596 19   ALA H C   
20458 O  O   . ALA H  21  ? 2.2963 1.5517 2.8859 0.6364  -0.2811 -0.2451 19   ALA H O   
20459 C  CB  . ALA H  21  ? 2.4046 1.6105 2.8981 0.6093  -0.3767 -0.2178 19   ALA H CB  
20460 N  N   . ILE H  22  ? 2.4401 1.6817 2.9986 0.5723  -0.3214 -0.2930 20   ILE H N   
20461 C  CA  . ILE H  22  ? 2.2823 1.5209 2.8611 0.5647  -0.2714 -0.3169 20   ILE H CA  
20462 C  C   . ILE H  22  ? 1.9702 1.2543 2.5962 0.5792  -0.2795 -0.3332 20   ILE H C   
20463 O  O   . ILE H  22  ? 1.8544 1.1348 2.4995 0.5968  -0.2315 -0.3390 20   ILE H O   
20464 C  CB  . ILE H  22  ? 1.9395 1.1657 2.5020 0.5246  -0.2736 -0.3431 20   ILE H CB  
20465 C  CG1 . ILE H  22  ? 1.7733 0.9583 2.2952 0.5183  -0.2501 -0.3285 20   ILE H CG1 
20466 C  CG2 . ILE H  22  ? 2.1921 1.4221 2.7777 0.5122  -0.2389 -0.3714 20   ILE H CG2 
20467 C  CD1 . ILE H  22  ? 1.8022 0.9521 2.3164 0.5343  -0.1889 -0.3159 20   ILE H CD1 
20468 N  N   . ARG H  23  ? 2.0503 1.3754 2.6936 0.5745  -0.3419 -0.3409 21   ARG H N   
20469 C  CA  . ARG H  23  ? 1.8707 1.2522 2.5652 0.5915  -0.3562 -0.3583 21   ARG H CA  
20470 C  C   . ARG H  23  ? 1.8969 1.3031 2.6183 0.6408  -0.3231 -0.3326 21   ARG H C   
20471 O  O   . ARG H  23  ? 1.9726 1.3935 2.7246 0.6577  -0.2807 -0.3515 21   ARG H O   
20472 C  CB  . ARG H  23  ? 1.9608 1.3820 2.6648 0.5833  -0.4394 -0.3580 21   ARG H CB  
20473 C  CG  . ARG H  23  ? 1.9861 1.5015 2.7310 0.5924  -0.4550 -0.3595 21   ARG H CG  
20474 C  CD  . ARG H  23  ? 2.0311 1.6175 2.7410 0.5485  -0.5236 -0.3289 21   ARG H CD  
20475 N  NE  . ARG H  23  ? 1.9770 1.5367 2.6663 0.5002  -0.5614 -0.3534 21   ARG H NE  
20476 C  CZ  . ARG H  23  ? 1.9870 1.6013 2.6940 0.4648  -0.5737 -0.3777 21   ARG H CZ  
20477 N  NH1 . ARG H  23  ? 2.0225 1.7208 2.7644 0.4721  -0.5488 -0.3856 21   ARG H NH1 
20478 N  NH2 . ARG H  23  ? 1.9766 1.5643 2.6669 0.4231  -0.6103 -0.3931 21   ARG H NH2 
20479 N  N   . GLY H  24  ? 2.1705 1.5802 2.8791 0.6650  -0.3407 -0.2880 22   GLY H N   
20480 C  CA  . GLY H  24  ? 2.4020 1.8409 3.1395 0.7144  -0.3097 -0.2548 22   GLY H CA  
20481 C  C   . GLY H  24  ? 2.2878 1.6669 3.0115 0.7258  -0.2328 -0.2496 22   GLY H C   
20482 O  O   . GLY H  24  ? 1.9638 1.3583 2.7153 0.7673  -0.1945 -0.2318 22   GLY H O   
20483 N  N   . GLN H  25  ? 2.1301 1.4441 2.8106 0.6920  -0.2109 -0.2624 23   GLN H N   
20484 C  CA  . GLN H  25  ? 2.0648 1.3188 2.7242 0.7007  -0.1458 -0.2549 23   GLN H CA  
20485 C  C   . GLN H  25  ? 1.9991 1.2393 2.6690 0.6985  -0.1042 -0.2904 23   GLN H C   
20486 O  O   . GLN H  25  ? 2.0291 1.2475 2.7035 0.7326  -0.0592 -0.2805 23   GLN H O   
20487 C  CB  . GLN H  25  ? 1.9581 1.1601 2.5698 0.6676  -0.1411 -0.2553 23   GLN H CB  
20488 C  CG  . GLN H  25  ? 2.1449 1.2845 2.7289 0.6789  -0.0846 -0.2413 23   GLN H CG  
20489 C  CD  . GLN H  25  ? 2.0703 1.1707 2.6140 0.6457  -0.0801 -0.2487 23   GLN H CD  
20490 O  OE1 . GLN H  25  ? 1.9320 1.0480 2.4699 0.6111  -0.1077 -0.2725 23   GLN H OE1 
20491 N  NE2 . GLN H  25  ? 2.4243 1.4761 2.9417 0.6594  -0.0475 -0.2269 23   GLN H NE2 
20492 N  N   . ILE H  26  ? 1.8815 1.1310 2.5524 0.6595  -0.1211 -0.3318 24   ILE H N   
20493 C  CA  . ILE H  26  ? 1.9260 1.1624 2.6046 0.6514  -0.0872 -0.3701 24   ILE H CA  
20494 C  C   . ILE H  26  ? 2.1153 1.3916 2.8358 0.6940  -0.0725 -0.3743 24   ILE H C   
20495 O  O   . ILE H  26  ? 2.4196 1.6597 3.1331 0.7133  -0.0232 -0.3847 24   ILE H O   
20496 C  CB  . ILE H  26  ? 1.8622 1.1212 2.5477 0.6039  -0.1197 -0.4109 24   ILE H CB  
20497 C  CG1 . ILE H  26  ? 1.8278 1.0530 2.4743 0.5685  -0.1294 -0.4027 24   ILE H CG1 
20498 C  CG2 . ILE H  26  ? 2.1282 1.3770 2.8235 0.5928  -0.0872 -0.4533 24   ILE H CG2 
20499 C  CD1 . ILE H  26  ? 1.7952 1.0436 2.4504 0.5250  -0.1621 -0.4355 24   ILE H CD1 
20500 N  N   . LEU H  27  ? 2.0872 1.4391 2.8490 0.7125  -0.1171 -0.3658 25   LEU H N   
20501 C  CA  . LEU H  27  ? 2.2403 1.6501 3.0500 0.7582  -0.1040 -0.3683 25   LEU H CA  
20502 C  C   . LEU H  27  ? 2.3578 1.7423 3.1647 0.8096  -0.0578 -0.3249 25   LEU H C   
20503 O  O   . LEU H  27  ? 2.5866 1.9794 3.4140 0.8468  -0.0171 -0.3331 25   LEU H O   
20504 C  CB  . LEU H  27  ? 2.3019 1.8106 3.1556 0.7691  -0.1707 -0.3616 25   LEU H CB  
20505 C  CG  . LEU H  27  ? 2.2272 1.7684 3.0914 0.7267  -0.2221 -0.4059 25   LEU H CG  
20506 C  CD1 . LEU H  27  ? 2.4895 2.1376 3.3772 0.7320  -0.2882 -0.3823 25   LEU H CD1 
20507 C  CD2 . LEU H  27  ? 2.0860 1.6306 2.9684 0.7152  -0.1872 -0.4632 25   LEU H CD2 
20508 N  N   . SER H  28  ? 2.1860 1.5383 2.9665 0.8142  -0.0624 -0.2798 26   SER H N   
20509 C  CA  . SER H  28  ? 2.3495 1.6802 3.1290 0.8649  -0.0236 -0.2350 26   SER H CA  
20510 C  C   . SER H  28  ? 2.3962 1.6286 3.1260 0.8683  0.0344  -0.2478 26   SER H C   
20511 O  O   . SER H  28  ? 2.4784 1.6906 3.2065 0.9181  0.0713  -0.2328 26   SER H O   
20512 C  CB  . SER H  28  ? 2.2748 1.6094 3.0440 0.8684  -0.0530 -0.1837 26   SER H CB  
20513 O  OG  . SER H  28  ? 2.1234 1.3907 2.8405 0.8254  -0.0542 -0.1926 26   SER H OG  
20514 N  N   . LYS H  29  ? 2.3768 1.5491 3.0614 0.8195  0.0373  -0.2752 27   LYS H N   
20515 C  CA  . LYS H  29  ? 2.3867 1.4673 3.0187 0.8203  0.0797  -0.2889 27   LYS H CA  
20516 C  C   . LYS H  29  ? 2.4435 1.5135 3.0818 0.8298  0.1074  -0.3313 27   LYS H C   
20517 O  O   . LYS H  29  ? 2.6080 1.6096 3.2112 0.8569  0.1401  -0.3366 27   LYS H O   
20518 C  CB  . LYS H  29  ? 2.3720 1.4074 2.9623 0.7660  0.0713  -0.3041 27   LYS H CB  
20519 C  CG  . LYS H  29  ? 2.3396 1.3687 2.9127 0.7611  0.0537  -0.2658 27   LYS H CG  
20520 C  CD  . LYS H  29  ? 2.2443 1.2369 2.7807 0.7130  0.0494  -0.2827 27   LYS H CD  
20521 C  CE  . LYS H  29  ? 2.2119 1.1903 2.7275 0.7143  0.0401  -0.2476 27   LYS H CE  
20522 N  NZ  . LYS H  29  ? 2.2012 1.1465 2.6835 0.6745  0.0406  -0.2633 27   LYS H NZ  
20523 N  N   . LEU H  30  ? 2.5220 1.6580 3.2030 0.8097  0.0892  -0.3650 28   LEU H N   
20524 C  CA  . LEU H  30  ? 2.4651 1.6050 3.1597 0.8202  0.1153  -0.4085 28   LEU H CA  
20525 C  C   . LEU H  30  ? 2.4785 1.6737 3.2171 0.8846  0.1312  -0.3915 28   LEU H C   
20526 O  O   . LEU H  30  ? 2.7253 1.9334 3.4794 0.9026  0.1569  -0.4273 28   LEU H O   
20527 C  CB  . LEU H  30  ? 2.3917 1.5861 3.1151 0.7705  0.0853  -0.4569 28   LEU H CB  
20528 C  CG  . LEU H  30  ? 2.4843 1.6374 3.1722 0.7076  0.0700  -0.4766 28   LEU H CG  
20529 C  CD1 . LEU H  30  ? 2.6664 1.8857 3.3901 0.6657  0.0322  -0.5196 28   LEU H CD1 
20530 C  CD2 . LEU H  30  ? 2.4677 1.5278 3.1038 0.6978  0.1108  -0.4959 28   LEU H CD2 
20531 N  N   . ARG H  31  ? 2.3730 1.6065 3.1334 0.9200  0.1166  -0.3369 29   ARG H N   
20532 C  CA  . ARG H  31  ? 2.5757 1.8817 3.3873 0.9845  0.1267  -0.3091 29   ARG H CA  
20533 C  C   . ARG H  31  ? 2.6522 2.0669 3.5293 0.9815  0.1065  -0.3425 29   ARG H C   
20534 O  O   . ARG H  31  ? 3.0709 2.5315 3.9819 1.0269  0.1357  -0.3528 29   ARG H O   
20535 C  CB  . ARG H  31  ? 2.7220 1.9601 3.4978 1.0408  0.1765  -0.3087 29   ARG H CB  
20536 C  CG  . ARG H  31  ? 2.7707 2.0693 3.5812 1.1182  0.1819  -0.2616 29   ARG H CG  
20537 C  CD  . ARG H  31  ? 3.0101 2.2470 3.7839 1.1707  0.2092  -0.2843 29   ARG H CD  
20538 N  NE  . ARG H  31  ? 3.1688 2.2911 3.8800 1.1581  0.1990  -0.2888 29   ARG H NE  
20539 C  CZ  . ARG H  31  ? 3.2424 2.3553 3.9646 1.1871  0.1699  -0.2607 29   ARG H CZ  
20540 N  NH1 . ARG H  31  ? 3.1931 2.4046 3.9874 1.2287  0.1438  -0.2291 29   ARG H NH1 
20541 N  NH2 . ARG H  31  ? 3.3518 2.3637 4.0342 1.1701  0.1634  -0.2659 29   ARG H NH2 
20542 N  N   . LEU H  32  ? 2.3279 1.7870 3.2186 0.9310  0.0526  -0.3621 30   LEU H N   
20543 C  CA  . LEU H  32  ? 2.1878 1.7536 3.1310 0.9241  0.0175  -0.3998 30   LEU H CA  
20544 C  C   . LEU H  32  ? 2.2603 1.9247 3.2395 0.9289  -0.0527 -0.3623 30   LEU H C   
20545 O  O   . LEU H  32  ? 2.4982 2.1272 3.4490 0.9077  -0.0842 -0.3276 30   LEU H O   
20546 C  CB  . LEU H  32  ? 2.1782 1.7139 3.0997 0.8613  0.0037  -0.4620 30   LEU H CB  
20547 C  CG  . LEU H  32  ? 2.2573 1.7176 3.1458 0.8505  0.0618  -0.5087 30   LEU H CG  
20548 C  CD1 . LEU H  32  ? 2.1976 1.6455 3.0725 0.7843  0.0396  -0.5633 30   LEU H CD1 
20549 C  CD2 . LEU H  32  ? 2.7228 2.2382 3.6477 0.9020  0.1005  -0.5298 30   LEU H CD2 
20550 N  N   . ALA H  33  ? 2.2981 2.0925 3.3346 0.9578  -0.0789 -0.3686 31   ALA H N   
20551 C  CA  . ALA H  33  ? 2.3828 2.2893 3.4193 0.9384  -0.1487 -0.3206 31   ALA H CA  
20552 C  C   . ALA H  33  ? 2.2373 2.1872 3.2394 0.8601  -0.1995 -0.3459 31   ALA H C   
20553 O  O   . ALA H  33  ? 2.0644 2.0369 3.0323 0.8171  -0.2595 -0.3102 31   ALA H O   
20554 C  CB  . ALA H  33  ? 2.4262 2.4755 3.4983 0.9809  -0.1415 -0.2776 31   ALA H CB  
20555 N  N   . SER H  34  ? 2.4374 2.3929 3.4454 0.8399  -0.1768 -0.4068 32   SER H N   
20556 C  CA  . SER H  34  ? 2.4418 2.4429 3.4235 0.7662  -0.2210 -0.4323 32   SER H CA  
20557 C  C   . SER H  34  ? 2.4794 2.3978 3.4609 0.7482  -0.1830 -0.5066 32   SER H C   
20558 O  O   . SER H  34  ? 2.5449 2.4096 3.5490 0.7938  -0.1202 -0.5413 32   SER H O   
20559 C  CB  . SER H  34  ? 2.6020 2.7711 3.5932 0.7497  -0.2448 -0.4140 32   SER H CB  
20560 O  OG  . SER H  34  ? 2.7574 2.9716 3.7840 0.7951  -0.1853 -0.4456 32   SER H OG  
20561 N  N   . PRO H  35  ? 2.3459 2.2477 3.3012 0.6824  -0.2198 -0.5306 33   PRO H N   
20562 C  CA  . PRO H  35  ? 2.4722 2.3082 3.4258 0.6559  -0.1883 -0.5982 33   PRO H CA  
20563 C  C   . PRO H  35  ? 2.6022 2.5122 3.5734 0.6623  -0.1496 -0.6401 33   PRO H C   
20564 O  O   . PRO H  35  ? 2.7395 2.7840 3.7174 0.6548  -0.1708 -0.6200 33   PRO H O   
20565 C  CB  . PRO H  35  ? 2.2844 2.1330 3.2110 0.5821  -0.2492 -0.5982 33   PRO H CB  
20566 C  CG  . PRO H  35  ? 2.1625 2.0077 3.0705 0.5837  -0.2990 -0.5381 33   PRO H CG  
20567 C  CD  . PRO H  35  ? 2.1547 2.0792 3.0785 0.6310  -0.2921 -0.4938 33   PRO H CD  
20568 N  N   . PRO H  36  ? 2.5483 2.3755 3.5241 0.6740  -0.0926 -0.6992 34   PRO H N   
20569 C  CA  . PRO H  36  ? 2.6157 2.5018 3.6024 0.6840  -0.0487 -0.7465 34   PRO H CA  
20570 C  C   . PRO H  36  ? 2.7101 2.6961 3.6814 0.6097  -0.0829 -0.7718 34   PRO H C   
20571 O  O   . PRO H  36  ? 2.6395 2.6379 3.5937 0.5502  -0.1393 -0.7554 34   PRO H O   
20572 C  CB  . PRO H  36  ? 2.5573 2.2994 3.5420 0.7066  0.0152  -0.8026 34   PRO H CB  
20573 C  CG  . PRO H  36  ? 2.4901 2.1313 3.4486 0.6654  -0.0101 -0.7901 34   PRO H CG  
20574 C  CD  . PRO H  36  ? 2.5068 2.1814 3.4737 0.6748  -0.0661 -0.7264 34   PRO H CD  
20575 N  N   . SER H  37  ? 2.7847 2.8419 3.7620 0.6151  -0.0461 -0.8130 35   SER H N   
20576 C  CA  . SER H  37  ? 2.6491 2.8178 3.6131 0.5462  -0.0736 -0.8371 35   SER H CA  
20577 C  C   . SER H  37  ? 2.6344 2.7199 3.5770 0.4941  -0.0571 -0.8990 35   SER H C   
20578 O  O   . SER H  37  ? 2.7145 2.6929 3.6532 0.5215  0.0025  -0.9480 35   SER H O   
20579 C  CB  . SER H  37  ? 2.5050 2.7981 3.4822 0.5731  -0.0394 -0.8557 35   SER H CB  
20580 O  OG  . SER H  37  ? 2.4957 2.7088 3.4738 0.6162  0.0382  -0.9189 35   SER H OG  
20581 N  N   . GLN H  38  ? 2.6428 2.7833 3.5711 0.4163  -0.1111 -0.8951 36   GLN H N   
20582 C  CA  . GLN H  38  ? 2.7139 2.7930 3.6239 0.3571  -0.1070 -0.9426 36   GLN H CA  
20583 C  C   . GLN H  38  ? 2.7447 2.9435 3.6433 0.2956  -0.1141 -0.9775 36   GLN H C   
20584 O  O   . GLN H  38  ? 2.7572 2.9420 3.6409 0.2308  -0.1253 -1.0075 36   GLN H O   
20585 C  CB  . GLN H  38  ? 2.7578 2.7854 3.6636 0.3194  -0.1635 -0.9059 36   GLN H CB  
20586 C  CG  . GLN H  38  ? 2.8965 2.8304 3.7904 0.2753  -0.1528 -0.9449 36   GLN H CG  
20587 C  CD  . GLN H  38  ? 2.8500 2.7533 3.7440 0.2428  -0.2105 -0.9045 36   GLN H CD  
20588 O  OE1 . GLN H  38  ? 2.7878 2.7330 3.6853 0.2500  -0.2596 -0.8511 36   GLN H OE1 
20589 N  NE2 . GLN H  38  ? 2.7855 2.6143 3.6742 0.2078  -0.2040 -0.9296 36   GLN H NE2 
20590 N  N   . GLY H  39  ? 2.6209 2.9429 3.5272 0.3153  -0.1054 -0.9733 37   GLY H N   
20591 C  CA  . GLY H  39  ? 2.5773 3.0226 3.4719 0.2641  -0.1040 -1.0084 37   GLY H CA  
20592 C  C   . GLY H  39  ? 2.7199 3.1185 3.6035 0.2977  -0.0218 -1.0823 37   GLY H C   
20593 O  O   . GLY H  39  ? 2.7357 3.2148 3.6020 0.2572  -0.0051 -1.1285 37   GLY H O   
20594 N  N   . GLU H  40  ? 2.8445 3.1071 3.7354 0.3707  0.0290  -1.0933 38   GLU H N   
20595 C  CA  . GLU H  40  ? 2.8463 3.0149 3.7234 0.4100  0.1096  -1.1635 38   GLU H CA  
20596 C  C   . GLU H  40  ? 2.7811 2.7953 3.6350 0.3746  0.1233  -1.2005 38   GLU H C   
20597 O  O   . GLU H  40  ? 2.7542 2.6628 3.5885 0.3946  0.1857  -1.2606 38   GLU H O   
20598 C  CB  . GLU H  40  ? 2.7476 2.8601 3.6503 0.5164  0.1568  -1.1462 38   GLU H CB  
20599 C  CG  . GLU H  40  ? 2.5831 2.6370 3.4749 0.5746  0.2486  -1.2210 38   GLU H CG  
20600 C  CD  . GLU H  40  ? 2.6008 2.5897 3.5242 0.6921  0.3028  -1.2032 38   GLU H CD  
20601 O  OE1 . GLU H  40  ? 2.6964 2.6886 3.6534 0.7400  0.2778  -1.1316 38   GLU H OE1 
20602 O  OE2 . GLU H  40  ? 2.6958 2.6246 3.5957 0.7298  0.3704  -1.2485 38   GLU H OE2 
20603 N  N   . VAL H  41  ? 2.7020 2.7088 3.5552 0.3160  0.0652  -1.1681 39   VAL H N   
20604 C  CA  . VAL H  41  ? 2.8523 2.7242 3.6889 0.2830  0.0736  -1.1927 39   VAL H CA  
20605 C  C   . VAL H  41  ? 2.8913 2.8376 3.7089 0.1852  0.0391  -1.2141 39   VAL H C   
20606 O  O   . VAL H  41  ? 2.7209 2.7969 3.5485 0.1456  -0.0179 -1.1768 39   VAL H O   
20607 C  CB  . VAL H  41  ? 2.8702 2.6625 3.7261 0.3077  0.0405  -1.1337 39   VAL H CB  
20608 C  CG1 . VAL H  41  ? 2.8717 2.5345 3.7132 0.2747  0.0502  -1.1556 39   VAL H CG1 
20609 C  CG2 . VAL H  41  ? 2.9769 2.7201 3.8534 0.4019  0.0702  -1.1053 39   VAL H CG2 
20610 N  N   . PRO H  42  ? 3.0766 2.9500 3.8657 0.1406  0.0701  -1.2713 40   PRO H N   
20611 C  CA  . PRO H  42  ? 2.9634 2.9166 3.7358 0.0449  0.0369  -1.2881 40   PRO H CA  
20612 C  C   . PRO H  42  ? 2.9195 2.8360 3.7048 0.0019  -0.0144 -1.2472 40   PRO H C   
20613 O  O   . PRO H  42  ? 2.8466 2.6323 3.6301 0.0166  0.0052  -1.2512 40   PRO H O   
20614 C  CB  . PRO H  42  ? 2.9703 2.8562 3.7014 0.0195  0.0993  -1.3709 40   PRO H CB  
20615 C  CG  . PRO H  42  ? 3.0236 2.7501 3.7487 0.0960  0.1568  -1.3820 40   PRO H CG  
20616 C  CD  . PRO H  42  ? 3.1570 2.8741 3.9252 0.1731  0.1374  -1.3228 40   PRO H CD  
20617 N  N   . PRO H  43  ? 3.1407 3.1714 3.9403 -0.0501 -0.0807 -1.2051 41   PRO H N   
20618 C  CA  . PRO H  43  ? 3.1658 3.1678 3.9801 -0.0888 -0.1295 -1.1663 41   PRO H CA  
20619 C  C   . PRO H  43  ? 3.0939 3.0728 3.8885 -0.1631 -0.1181 -1.2076 41   PRO H C   
20620 O  O   . PRO H  43  ? 3.1089 3.1687 3.8825 -0.2202 -0.1120 -1.2449 41   PRO H O   
20621 C  CB  . PRO H  43  ? 3.1758 3.3118 4.0089 -0.1194 -0.2018 -1.1113 41   PRO H CB  
20622 C  CG  . PRO H  43  ? 3.2261 3.4827 4.0457 -0.1375 -0.1903 -1.1382 41   PRO H CG  
20623 C  CD  . PRO H  43  ? 3.1927 3.3836 3.9985 -0.0695 -0.1161 -1.1844 41   PRO H CD  
20624 N  N   . GLY H  44  ? 3.2960 4.1992 3.1181 -0.1900 -0.0867 0.8018  42   GLY H N   
20625 C  CA  . GLY H  44  ? 3.2102 4.1490 3.0214 -0.2098 -0.0878 0.8091  42   GLY H CA  
20626 C  C   . GLY H  44  ? 3.1390 4.0161 2.8793 -0.1741 -0.0404 0.7181  42   GLY H C   
20627 O  O   . GLY H  44  ? 2.9834 3.7725 2.7455 -0.1504 -0.0438 0.7018  42   GLY H O   
20628 N  N   . PRO H  45  ? 3.0927 4.0146 2.7521 -0.1689 0.0043  0.6567  43   PRO H N   
20629 C  CA  . PRO H  45  ? 2.8887 3.7584 2.4831 -0.1396 0.0461  0.5728  43   PRO H CA  
20630 C  C   . PRO H  45  ? 2.7063 3.4207 2.3132 -0.0825 0.0569  0.5223  43   PRO H C   
20631 O  O   . PRO H  45  ? 2.6504 3.3164 2.2611 -0.0572 0.0640  0.5027  43   PRO H O   
20632 C  CB  . PRO H  45  ? 2.9220 3.8779 2.4432 -0.1471 0.0871  0.5234  43   PRO H CB  
20633 C  CG  . PRO H  45  ? 2.9271 3.9335 2.4782 -0.1585 0.0742  0.5640  43   PRO H CG  
20634 C  CD  . PRO H  45  ? 3.0371 4.0643 2.6658 -0.1902 0.0190  0.6607  43   PRO H CD  
20635 N  N   . LEU H  46  ? 2.7574 3.3995 2.3713 -0.0653 0.0570  0.5042  44   LEU H N   
20636 C  CA  . LEU H  46  ? 2.8926 3.3959 2.5091 -0.0149 0.0710  0.4519  44   LEU H CA  
20637 C  C   . LEU H  46  ? 2.8028 3.2892 2.3640 -0.0044 0.1014  0.3951  44   LEU H C   
20638 O  O   . LEU H  46  ? 2.8242 3.3022 2.4076 -0.0119 0.0891  0.4137  44   LEU H O   
20639 C  CB  . LEU H  46  ? 2.8707 3.3001 2.5695 -0.0049 0.0352  0.4955  44   LEU H CB  
20640 C  CG  . LEU H  46  ? 2.8033 3.2318 2.5629 -0.0127 0.0011  0.5488  44   LEU H CG  
20641 C  CD1 . LEU H  46  ? 2.6221 3.0230 2.4763 -0.0210 -0.0433 0.6112  44   LEU H CD1 
20642 C  CD2 . LEU H  46  ? 2.7949 3.1232 2.5380 0.0278  0.0177  0.4982  44   LEU H CD2 
20643 N  N   . PRO H  47  ? 2.5468 3.0242 2.0432 0.0135  0.1389  0.3272  45   PRO H N   
20644 C  CA  . PRO H  47  ? 2.6149 3.0884 2.0584 0.0171  0.1648  0.2758  45   PRO H CA  
20645 C  C   . PRO H  47  ? 2.7225 3.0874 2.1829 0.0473  0.1649  0.2560  45   PRO H C   
20646 O  O   . PRO H  47  ? 2.8179 3.0895 2.3048 0.0795  0.1624  0.2463  45   PRO H O   
20647 C  CB  . PRO H  47  ? 2.5076 2.9806 1.8955 0.0354  0.2010  0.2086  45   PRO H CB  
20648 C  CG  . PRO H  47  ? 2.4264 2.8530 1.8440 0.0573  0.1952  0.2165  45   PRO H CG  
20649 C  CD  . PRO H  47  ? 2.4102 2.8829 1.8853 0.0303  0.1574  0.2962  45   PRO H CD  
20650 N  N   . GLU H  48  ? 2.8372 3.2198 2.2810 0.0344  0.1677  0.2505  46   GLU H N   
20651 C  CA  . GLU H  48  ? 2.8619 3.1534 2.3169 0.0615  0.1725  0.2278  46   GLU H CA  
20652 C  C   . GLU H  48  ? 2.8266 3.0481 2.2292 0.0938  0.2052  0.1530  46   GLU H C   
20653 O  O   . GLU H  48  ? 2.8011 2.9473 2.2069 0.1166  0.2121  0.1303  46   GLU H O   
20654 C  CB  . GLU H  48  ? 2.7689 3.1071 2.2289 0.0343  0.1618  0.2529  46   GLU H CB  
20655 C  CG  . GLU H  48  ? 2.6272 3.0185 2.1573 0.0052  0.1236  0.3343  46   GLU H CG  
20656 C  CD  . GLU H  48  ? 2.6573 3.0746 2.2067 -0.0150 0.1107  0.3611  46   GLU H CD  
20657 O  OE1 . GLU H  48  ? 2.7289 3.1437 2.2248 -0.0154 0.1312  0.3183  46   GLU H OE1 
20658 O  OE2 . GLU H  48  ? 2.6308 3.0706 2.2543 -0.0312 0.0778  0.4273  46   GLU H OE2 
20659 N  N   . ALA H  49  ? 2.7293 2.9771 2.0893 0.0956  0.2248  0.1163  47   ALA H N   
20660 C  CA  . ALA H  49  ? 2.5857 2.7642 1.9087 0.1267  0.2512  0.0505  47   ALA H CA  
20661 C  C   . ALA H  49  ? 2.6100 2.6994 1.9582 0.1590  0.2486  0.0465  47   ALA H C   
20662 O  O   . ALA H  49  ? 2.6341 2.6412 1.9690 0.1854  0.2606  0.0088  47   ALA H O   
20663 C  CB  . ALA H  49  ? 2.5900 2.8296 1.8693 0.1187  0.2731  0.0109  47   ALA H CB  
20664 N  N   . VAL H  50  ? 2.5289 2.6357 1.9121 0.1540  0.2311  0.0865  48   VAL H N   
20665 C  CA  . VAL H  50  ? 2.5274 2.5499 1.9345 0.1803  0.2245  0.0856  48   VAL H CA  
20666 C  C   . VAL H  50  ? 2.5617 2.5249 2.0123 0.1888  0.2067  0.1112  48   VAL H C   
20667 O  O   . VAL H  50  ? 2.5918 2.4705 2.0521 0.2132  0.2063  0.0962  48   VAL H O   
20668 C  CB  . VAL H  50  ? 2.5266 2.5877 1.9547 0.1718  0.2120  0.1155  48   VAL H CB  
20669 C  CG1 . VAL H  50  ? 2.4885 2.6161 1.8797 0.1653  0.2337  0.0867  48   VAL H CG1 
20670 C  CG2 . VAL H  50  ? 2.5799 2.7037 2.0552 0.1429  0.1820  0.1830  48   VAL H CG2 
20671 N  N   . LEU H  51  ? 2.6332 2.6409 2.1119 0.1686  0.1923  0.1482  49   LEU H N   
20672 C  CA  . LEU H  51  ? 2.7543 2.7085 2.2832 0.1795  0.1784  0.1682  49   LEU H CA  
20673 C  C   . LEU H  51  ? 2.8588 2.7490 2.3616 0.2018  0.2002  0.1229  49   LEU H C   
20674 O  O   . LEU H  51  ? 3.0138 2.8364 2.5472 0.2222  0.1985  0.1187  49   LEU H O   
20675 C  CB  . LEU H  51  ? 2.9732 2.9992 2.5496 0.1497  0.1538  0.2268  49   LEU H CB  
20676 C  CG  . LEU H  51  ? 3.1613 3.2444 2.7857 0.1254  0.1226  0.2878  49   LEU H CG  
20677 C  CD1 . LEU H  51  ? 3.2728 3.4207 2.9516 0.0952  0.0950  0.3494  49   LEU H CD1 
20678 C  CD2 . LEU H  51  ? 3.0925 3.0994 2.7618 0.1476  0.1080  0.2944  49   LEU H CD2 
20679 N  N   . ALA H  52  ? 2.6769 2.5895 2.1258 0.1971  0.2205  0.0880  50   ALA H N   
20680 C  CA  . ALA H  52  ? 2.5904 2.4420 2.0128 0.2167  0.2397  0.0458  50   ALA H CA  
20681 C  C   . ALA H  52  ? 2.5700 2.3440 1.9694 0.2434  0.2522  0.0072  50   ALA H C   
20682 O  O   . ALA H  52  ? 2.5628 2.2726 1.9572 0.2618  0.2618  -0.0158 50   ALA H O   
20683 C  CB  . ALA H  52  ? 2.6103 2.5057 1.9862 0.2017  0.2533  0.0208  50   ALA H CB  
20684 N  N   . LEU H  53  ? 2.5642 2.3484 1.9499 0.2435  0.2518  0.0017  51   LEU H N   
20685 C  CA  . LEU H  53  ? 2.5512 2.2647 1.9220 0.2651  0.2580  -0.0256 51   LEU H CA  
20686 C  C   . LEU H  53  ? 2.5999 2.2561 2.0074 0.2770  0.2446  -0.0083 51   LEU H C   
20687 O  O   . LEU H  53  ? 2.6746 2.2606 2.0698 0.2945  0.2526  -0.0342 51   LEU H O   
20688 C  CB  . LEU H  53  ? 2.5311 2.2769 1.8903 0.2611  0.2581  -0.0283 51   LEU H CB  
20689 C  CG  . LEU H  53  ? 2.6187 2.3732 1.9383 0.2657  0.2777  -0.0710 51   LEU H CG  
20690 C  CD1 . LEU H  53  ? 2.9028 2.7119 2.2257 0.2589  0.2776  -0.0649 51   LEU H CD1 
20691 C  CD2 . LEU H  53  ? 2.4109 2.0798 1.7122 0.2871  0.2854  -0.1044 51   LEU H CD2 
20692 N  N   . TYR H  54  ? 2.3978 2.0850 1.8518 0.2658  0.2231  0.0353  52   TYR H N   
20693 C  CA  . TYR H  54  ? 2.4588 2.0903 1.9557 0.2768  0.2077  0.0498  52   TYR H CA  
20694 C  C   . TYR H  54  ? 2.7367 2.3309 2.2550 0.2889  0.2146  0.0406  52   TYR H C   
20695 O  O   . TYR H  54  ? 2.7818 2.3087 2.3127 0.3063  0.2157  0.0242  52   TYR H O   
20696 C  CB  . TYR H  54  ? 2.3800 2.0585 1.9309 0.2591  0.1791  0.1033  52   TYR H CB  
20697 C  CG  . TYR H  54  ? 2.4140 2.0340 2.0160 0.2689  0.1583  0.1186  52   TYR H CG  
20698 C  CD1 . TYR H  54  ? 2.5103 2.0788 2.0985 0.2777  0.1534  0.1044  52   TYR H CD1 
20699 C  CD2 . TYR H  54  ? 2.3018 1.9177 1.9704 0.2688  0.1419  0.1468  52   TYR H CD2 
20700 C  CE1 . TYR H  54  ? 2.4553 1.9674 2.0884 0.2849  0.1330  0.1142  52   TYR H CE1 
20701 C  CE2 . TYR H  54  ? 2.2651 1.8238 1.9863 0.2790  0.1224  0.1554  52   TYR H CE2 
20702 C  CZ  . TYR H  54  ? 2.2653 1.7711 1.9652 0.2864  0.1182  0.1371  52   TYR H CZ  
20703 O  OH  . TYR H  54  ? 2.2427 1.6886 1.9927 0.2949  0.0976  0.1414  52   TYR H OH  
20704 N  N   . ASN H  55  ? 2.8581 2.4981 2.3801 0.2791  0.2200  0.0494  53   ASN H N   
20705 C  CA  . ASN H  55  ? 2.9739 2.5883 2.5217 0.2900  0.2277  0.0437  53   ASN H CA  
20706 C  C   . ASN H  55  ? 3.0304 2.5916 2.5284 0.3069  0.2533  -0.0052 53   ASN H C   
20707 O  O   . ASN H  55  ? 2.9753 2.4973 2.4923 0.3218  0.2626  -0.0182 53   ASN H O   
20708 C  CB  . ASN H  55  ? 2.9421 2.6271 2.5100 0.2701  0.2222  0.0737  53   ASN H CB  
20709 C  CG  . ASN H  55  ? 2.9022 2.6373 2.5372 0.2522  0.1926  0.1314  53   ASN H CG  
20710 O  OD1 . ASN H  55  ? 2.5497 2.2660 2.2183 0.2550  0.1753  0.1491  53   ASN H OD1 
20711 N  ND2 . ASN H  55  ? 3.4855 3.2864 3.1411 0.2304  0.1836  0.1642  53   ASN H ND2 
20712 N  N   . SER H  56  ? 2.9915 2.5530 2.4309 0.3044  0.2644  -0.0318 54   SER H N   
20713 C  CA  . SER H  56  ? 2.7979 2.3108 2.1928 0.3165  0.2838  -0.0724 54   SER H CA  
20714 C  C   . SER H  56  ? 2.8082 2.2560 2.1882 0.3300  0.2847  -0.0924 54   SER H C   
20715 O  O   . SER H  56  ? 2.9067 2.3094 2.2614 0.3395  0.2983  -0.1198 54   SER H O   
20716 C  CB  . SER H  56  ? 2.6139 2.1536 1.9622 0.3073  0.2923  -0.0916 54   SER H CB  
20717 O  OG  . SER H  56  ? 2.4834 2.0444 1.8215 0.3019  0.2853  -0.0886 54   SER H OG  
20718 N  N   . THR H  57  ? 2.6904 2.1357 2.0857 0.3281  0.2688  -0.0766 55   THR H N   
20719 C  CA  . THR H  57  ? 2.5495 1.9336 1.9316 0.3373  0.2656  -0.0925 55   THR H CA  
20720 C  C   . THR H  57  ? 2.5141 1.8578 1.9335 0.3477  0.2622  -0.0926 55   THR H C   
20721 O  O   . THR H  57  ? 2.6358 1.9227 2.0337 0.3560  0.2677  -0.1187 55   THR H O   
20722 C  CB  . THR H  57  ? 2.6047 2.0023 1.9902 0.3299  0.2485  -0.0748 55   THR H CB  
20723 O  OG1 . THR H  57  ? 2.7901 2.2337 2.2259 0.3202  0.2305  -0.0350 55   THR H OG1 
20724 C  CG2 . THR H  57  ? 2.5694 1.9991 1.9190 0.3241  0.2563  -0.0855 55   THR H CG2 
20725 N  N   . ARG H  58  ? 2.4726 1.8456 1.9505 0.3462  0.2519  -0.0639 56   ARG H N   
20726 C  CA  . ARG H  58  ? 2.4541 1.7872 1.9777 0.3595  0.2507  -0.0693 56   ARG H CA  
20727 C  C   . ARG H  58  ? 2.5833 1.9018 2.0950 0.3709  0.2766  -0.0981 56   ARG H C   
20728 O  O   . ARG H  58  ? 2.8596 2.1377 2.3940 0.3850  0.2847  -0.1187 56   ARG H O   
20729 C  CB  . ARG H  58  ? 2.5706 1.9394 2.1736 0.3543  0.2283  -0.0254 56   ARG H CB  
20730 C  CG  . ARG H  58  ? 2.5178 1.9037 2.1408 0.3408  0.1998  0.0086  56   ARG H CG  
20731 C  CD  . ARG H  58  ? 2.5233 1.9206 2.2362 0.3384  0.1738  0.0486  56   ARG H CD  
20732 N  NE  . ARG H  58  ? 2.5301 1.9920 2.2802 0.3281  0.1711  0.0816  56   ARG H NE  
20733 C  CZ  . ARG H  58  ? 2.5290 1.9984 2.3636 0.3308  0.1564  0.1096  56   ARG H CZ  
20734 N  NH1 . ARG H  58  ? 2.5169 1.9295 2.4100 0.3464  0.1447  0.1034  56   ARG H NH1 
20735 N  NH2 . ARG H  58  ? 2.5491 2.0821 2.4131 0.3173  0.1520  0.1434  56   ARG H NH2 
20736 N  N   . ASP H  59  ? 2.6967 2.0488 2.1744 0.3643  0.2899  -0.1015 57   ASP H N   
20737 C  CA  . ASP H  59  ? 2.9478 2.2926 2.4104 0.3716  0.3134  -0.1248 57   ASP H CA  
20738 C  C   . ASP H  59  ? 2.9399 2.2378 2.3381 0.3743  0.3269  -0.1617 57   ASP H C   
20739 O  O   . ASP H  59  ? 2.9889 2.2922 2.3385 0.3652  0.3282  -0.1683 57   ASP H O   
20740 C  CB  . ASP H  59  ? 3.1028 2.5012 2.5566 0.3598  0.3173  -0.1107 57   ASP H CB  
20741 C  CG  . ASP H  59  ? 3.3748 2.7746 2.8307 0.3659  0.3376  -0.1243 57   ASP H CG  
20742 O  OD1 . ASP H  59  ? 3.2651 2.6255 2.7134 0.3784  0.3534  -0.1512 57   ASP H OD1 
20743 O  OD2 . ASP H  59  ? 3.6169 3.0610 3.0802 0.3560  0.3379  -0.1080 57   ASP H OD2 
20744 N  N   . ARG H  60  ? 2.9418 2.1954 2.3418 0.3853  0.3363  -0.1864 58   ARG H N   
20745 C  CA  . ARG H  60  ? 3.0001 2.2126 2.3377 0.3831  0.3470  -0.2183 58   ARG H CA  
20746 C  C   . ARG H  60  ? 3.2230 2.4441 2.5420 0.3849  0.3718  -0.2368 58   ARG H C   
20747 O  O   . ARG H  60  ? 3.3209 2.5316 2.6602 0.3956  0.3884  -0.2554 58   ARG H O   
20748 C  CB  . ARG H  60  ? 2.8450 2.0078 2.1855 0.3890  0.3422  -0.2370 58   ARG H CB  
20749 C  CG  . ARG H  60  ? 2.7367 1.8914 2.0930 0.3840  0.3150  -0.2152 58   ARG H CG  
20750 C  CD  . ARG H  60  ? 2.9545 2.0583 2.3228 0.3890  0.3068  -0.2324 58   ARG H CD  
20751 N  NE  . ARG H  60  ? 3.1973 2.2990 2.5921 0.3831  0.2775  -0.2043 58   ARG H NE  
20752 C  CZ  . ARG H  60  ? 3.3871 2.4475 2.8065 0.3853  0.2614  -0.2094 58   ARG H CZ  
20753 N  NH1 . ARG H  60  ? 3.4546 2.4713 2.8735 0.3945  0.2741  -0.2476 58   ARG H NH1 
20754 N  NH2 . ARG H  60  ? 3.4085 2.4735 2.8539 0.3772  0.2327  -0.1777 58   ARG H NH2 
20755 N  N   . VAL H  61  ? 2.9762 2.2183 2.2596 0.3741  0.3741  -0.2323 59   VAL H N   
20756 C  CA  . VAL H  61  ? 2.9151 2.1677 2.1780 0.3716  0.3939  -0.2447 59   VAL H CA  
20757 C  C   . VAL H  61  ? 3.1074 2.3232 2.3224 0.3679  0.4049  -0.2730 59   VAL H C   
20758 O  O   . VAL H  61  ? 3.0463 2.2331 2.2216 0.3590  0.3929  -0.2779 59   VAL H O   
20759 C  CB  . VAL H  61  ? 2.6143 1.8927 1.8535 0.3588  0.3885  -0.2328 59   VAL H CB  
20760 C  CG1 . VAL H  61  ? 2.5084 1.8011 1.7347 0.3543  0.4058  -0.2396 59   VAL H CG1 
20761 C  CG2 . VAL H  61  ? 2.4819 1.8000 1.7589 0.3577  0.3762  -0.2072 59   VAL H CG2 
20762 N  N   . ALA H  62  ? 3.3004 2.5220 2.5199 0.3731  0.4280  -0.2906 60   ALA H N   
20763 C  CA  . ALA H  62  ? 3.1772 2.3746 2.3454 0.3650  0.4408  -0.3179 60   ALA H CA  
20764 C  C   . ALA H  62  ? 3.1322 2.3340 2.2462 0.3443  0.4355  -0.3105 60   ALA H C   
20765 O  O   . ALA H  62  ? 2.6541 1.8825 1.7761 0.3396  0.4312  -0.2916 60   ALA H O   
20766 C  CB  . ALA H  62  ? 2.9685 2.1819 2.1576 0.3754  0.4706  -0.3406 60   ALA H CB  
20767 N  N   . GLY H  63  ? 3.0881 2.2623 2.1492 0.3300  0.4326  -0.3242 61   GLY H N   
20768 C  CA  . GLY H  63  ? 2.8584 2.0329 1.8740 0.3081  0.4229  -0.3139 61   GLY H CA  
20769 C  C   . GLY H  63  ? 2.5240 1.6850 1.4842 0.2893  0.4299  -0.3309 61   GLY H C   
20770 O  O   . GLY H  63  ? 2.5240 1.7081 1.4587 0.2738  0.4402  -0.3290 61   GLY H O   
20771 N  N   . PRO H  72  ? 2.9721 1.8245 1.9511 0.1508  0.0400  -0.0793 70   PRO H N   
20772 C  CA  . PRO H  72  ? 3.1696 2.0174 2.1720 0.1357  0.0070  -0.0442 70   PRO H CA  
20773 C  C   . PRO H  72  ? 3.2853 2.1549 2.3409 0.1543  0.0036  -0.0300 70   PRO H C   
20774 O  O   . PRO H  72  ? 2.9962 1.8666 2.0534 0.1689  0.0182  -0.0483 70   PRO H O   
20775 C  CB  . PRO H  72  ? 3.0709 1.9402 2.1078 0.1346  -0.0009 -0.0199 70   PRO H CB  
20776 C  CG  . PRO H  72  ? 3.0371 1.9020 2.0370 0.1307  0.0168  -0.0412 70   PRO H CG  
20777 C  CD  . PRO H  72  ? 2.9525 1.8209 1.9343 0.1515  0.0488  -0.0776 70   PRO H CD  
20778 N  N   . GLU H  73  ? 3.7460 2.6367 2.8495 0.1524  -0.0167 0.0054  71   GLU H N   
20779 C  CA  . GLU H  73  ? 3.7842 2.7051 2.9396 0.1661  -0.0215 0.0246  71   GLU H CA  
20780 C  C   . GLU H  73  ? 3.6338 2.6058 2.8306 0.1982  0.0093  0.0132  71   GLU H C   
20781 O  O   . GLU H  73  ? 3.6695 2.6685 2.8953 0.2089  0.0123  0.0206  71   GLU H O   
20782 C  CB  . GLU H  73  ? 3.7286 2.6656 2.9278 0.1551  -0.0497 0.0663  71   GLU H CB  
20783 C  CG  . GLU H  73  ? 3.8475 2.7401 3.0127 0.1202  -0.0867 0.0856  71   GLU H CG  
20784 C  CD  . GLU H  73  ? 3.9875 2.8419 3.0959 0.0931  -0.0974 0.0789  71   GLU H CD  
20785 O  OE1 . GLU H  73  ? 4.0372 2.9044 3.1496 0.1013  -0.0820 0.0710  71   GLU H OE1 
20786 O  OE2 . GLU H  73  ? 3.9878 2.8013 3.0471 0.0611  -0.1228 0.0823  71   GLU H OE2 
20787 N  N   . ALA H  74  ? 3.3506 2.3381 2.5510 0.2110  0.0301  -0.0030 72   ALA H N   
20788 C  CA  . ALA H  74  ? 3.1578 2.1945 2.3926 0.2382  0.0584  -0.0165 72   ALA H CA  
20789 C  C   . ALA H  74  ? 3.0645 2.0934 2.2667 0.2465  0.0807  -0.0454 72   ALA H C   
20790 O  O   . ALA H  74  ? 3.0047 2.0757 2.2320 0.2648  0.1006  -0.0527 72   ALA H O   
20791 C  CB  . ALA H  74  ? 3.2166 2.2730 2.4782 0.2488  0.0688  -0.0223 72   ALA H CB  
20792 N  N   . ASP H  75  ? 3.2106 2.1912 2.3597 0.2324  0.0779  -0.0617 73   ASP H N   
20793 C  CA  . ASP H  75  ? 3.3188 2.2913 2.4426 0.2411  0.0998  -0.0902 73   ASP H CA  
20794 C  C   . ASP H  75  ? 3.1157 2.0785 2.2469 0.2424  0.0939  -0.0893 73   ASP H C   
20795 O  O   . ASP H  75  ? 3.0513 2.0138 2.1786 0.2529  0.1113  -0.1091 73   ASP H O   
20796 C  CB  . ASP H  75  ? 3.4757 2.4079 2.5417 0.2259  0.1038  -0.1119 73   ASP H CB  
20797 C  CG  . ASP H  75  ? 3.4854 2.4195 2.5334 0.2379  0.1315  -0.1418 73   ASP H CG  
20798 O  OD1 . ASP H  75  ? 3.4447 2.4161 2.5252 0.2579  0.1489  -0.1440 73   ASP H OD1 
20799 O  OD2 . ASP H  75  ? 3.5374 2.4395 2.5392 0.2262  0.1363  -0.1631 73   ASP H OD2 
20800 N  N   . TYR H  76  ? 2.8773 1.8327 2.0257 0.2315  0.0678  -0.0645 74   TYR H N   
20801 C  CA  . TYR H  76  ? 2.8782 1.8202 2.0413 0.2304  0.0560  -0.0598 74   TYR H CA  
20802 C  C   . TYR H  76  ? 2.9157 1.9151 2.1366 0.2441  0.0581  -0.0355 74   TYR H C   
20803 O  O   . TYR H  76  ? 2.9166 1.9147 2.1577 0.2477  0.0548  -0.0334 74   TYR H O   
20804 C  CB  . TYR H  76  ? 2.9523 1.8532 2.1018 0.2068  0.0222  -0.0442 74   TYR H CB  
20805 C  CG  . TYR H  76  ? 3.0796 1.9763 2.2642 0.2035  0.0003  -0.0245 74   TYR H CG  
20806 C  CD1 . TYR H  76  ? 3.1222 1.9773 2.2985 0.2033  -0.0022 -0.0471 74   TYR H CD1 
20807 C  CD2 . TYR H  76  ? 2.9997 1.9354 2.2314 0.2001  -0.0192 0.0175  74   TYR H CD2 
20808 C  CE1 . TYR H  76  ? 3.0449 1.8921 2.2608 0.1989  -0.0269 -0.0266 74   TYR H CE1 
20809 C  CE2 . TYR H  76  ? 2.9869 1.9210 2.2536 0.1938  -0.0430 0.0410  74   TYR H CE2 
20810 C  CZ  . TYR H  76  ? 2.9765 1.8637 2.2362 0.1927  -0.0487 0.0198  74   TYR H CZ  
20811 O  OH  . TYR H  76  ? 2.9545 1.8368 2.2569 0.1853  -0.0767 0.0458  74   TYR H OH  
20812 N  N   . TYR H  77  ? 2.9222 1.9747 2.1726 0.2509  0.0635  -0.0174 75   TYR H N   
20813 C  CA  . TYR H  77  ? 2.9085 2.0270 2.2084 0.2602  0.0676  0.0052  75   TYR H CA  
20814 C  C   . TYR H  77  ? 2.7726 1.9232 2.0747 0.2757  0.0958  -0.0142 75   TYR H C   
20815 O  O   . TYR H  77  ? 2.6207 1.7429 1.8900 0.2811  0.1125  -0.0441 75   TYR H O   
20816 C  CB  . TYR H  77  ? 2.9630 2.1305 2.2949 0.2617  0.0657  0.0264  75   TYR H CB  
20817 C  CG  . TYR H  77  ? 3.0318 2.1786 2.3741 0.2446  0.0340  0.0557  75   TYR H CG  
20818 C  CD1 . TYR H  77  ? 3.1788 2.3540 2.5583 0.2363  0.0137  0.0912  75   TYR H CD1 
20819 C  CD2 . TYR H  77  ? 2.9494 2.0499 2.2649 0.2333  0.0213  0.0519  75   TYR H CD2 
20820 C  CE1 . TYR H  77  ? 3.2341 2.3904 2.6242 0.2187  -0.0176 0.1204  75   TYR H CE1 
20821 C  CE2 . TYR H  77  ? 2.9667 2.0489 2.2912 0.2145  -0.0103 0.0813  75   TYR H CE2 
20822 C  CZ  . TYR H  77  ? 3.0457 2.1546 2.4074 0.2080  -0.0294 0.1145  75   TYR H CZ  
20823 O  OH  . TYR H  77  ? 3.0230 2.1139 2.3947 0.1875  -0.0630 0.1461  75   TYR H OH  
20824 N  N   . ALA H  78  ? 2.8546 2.0699 2.1957 0.2801  0.0998  0.0060  76   ALA H N   
20825 C  CA  . ALA H  78  ? 2.9092 2.1621 2.2559 0.2901  0.1216  -0.0051 76   ALA H CA  
20826 C  C   . ALA H  78  ? 2.9875 2.2763 2.3254 0.3008  0.1474  -0.0264 76   ALA H C   
20827 O  O   . ALA H  78  ? 3.2354 2.5423 2.5824 0.3026  0.1484  -0.0249 76   ALA H O   
20828 C  CB  . ALA H  78  ? 2.9885 2.3031 2.3789 0.2847  0.1126  0.0292  76   ALA H CB  
20829 N  N   . LYS H  79  ? 2.7795 2.0787 2.1057 0.3082  0.1672  -0.0463 77   LYS H N   
20830 C  CA  . LYS H  79  ? 2.7050 2.0332 2.0223 0.3173  0.1904  -0.0701 77   LYS H CA  
20831 C  C   . LYS H  79  ? 2.7908 2.1877 2.1247 0.3183  0.2041  -0.0659 77   LYS H C   
20832 O  O   . LYS H  79  ? 2.8208 2.2165 2.1566 0.3158  0.2031  -0.0595 77   LYS H O   
20833 C  CB  . LYS H  79  ? 2.5599 1.8326 1.8397 0.3210  0.2002  -0.0995 77   LYS H CB  
20834 C  CG  . LYS H  79  ? 2.7020 1.9080 1.9573 0.3137  0.1848  -0.1016 77   LYS H CG  
20835 C  CD  . LYS H  79  ? 2.7754 1.9847 2.0432 0.3117  0.1751  -0.0933 77   LYS H CD  
20836 C  CE  . LYS H  79  ? 2.6907 1.8375 1.9311 0.2990  0.1565  -0.0911 77   LYS H CE  
20837 N  NZ  . LYS H  79  ? 2.7001 1.8520 1.9623 0.2958  0.1434  -0.0767 77   LYS H NZ  
20838 N  N   . GLU H  80  ? 2.8793 2.3379 2.2271 0.3210  0.2167  -0.0704 78   GLU H N   
20839 C  CA  . GLU H  80  ? 2.7430 2.2769 2.1004 0.3174  0.2301  -0.0680 78   GLU H CA  
20840 C  C   . GLU H  80  ? 2.6235 2.1447 1.9554 0.3224  0.2475  -0.0980 78   GLU H C   
20841 O  O   . GLU H  80  ? 2.5283 2.0353 1.8477 0.3308  0.2599  -0.1280 78   GLU H O   
20842 C  CB  . GLU H  80  ? 2.7930 2.3995 2.1707 0.3181  0.2408  -0.0699 78   GLU H CB  
20843 C  CG  . GLU H  80  ? 2.9894 2.6829 2.3697 0.3098  0.2560  -0.0704 78   GLU H CG  
20844 C  CD  . GLU H  80  ? 3.0373 2.8110 2.4377 0.3097  0.2696  -0.0758 78   GLU H CD  
20845 O  OE1 . GLU H  80  ? 3.0317 2.7986 2.4545 0.3154  0.2634  -0.0681 78   GLU H OE1 
20846 O  OE2 . GLU H  80  ? 3.0565 2.9031 2.4509 0.3029  0.2871  -0.0884 78   GLU H OE2 
20847 N  N   . VAL H  81  ? 2.4663 1.9941 1.7971 0.3167  0.2462  -0.0873 79   VAL H N   
20848 C  CA  . VAL H  81  ? 2.4925 2.0075 1.8024 0.3197  0.2599  -0.1099 79   VAL H CA  
20849 C  C   . VAL H  81  ? 2.4429 2.0346 1.7532 0.3124  0.2735  -0.1156 79   VAL H C   
20850 O  O   . VAL H  81  ? 2.5672 2.2200 1.8951 0.2996  0.2680  -0.0882 79   VAL H O   
20851 C  CB  . VAL H  81  ? 2.7645 2.2447 2.0788 0.3184  0.2521  -0.0965 79   VAL H CB  
20852 C  CG1 . VAL H  81  ? 2.9670 2.4438 2.2648 0.3205  0.2667  -0.1159 79   VAL H CG1 
20853 C  CG2 . VAL H  81  ? 2.7362 2.1407 2.0425 0.3240  0.2414  -0.0997 79   VAL H CG2 
20854 N  N   . THR H  82  ? 2.2853 1.8743 1.5766 0.3181  0.2890  -0.1504 80   THR H N   
20855 C  CA  . THR H  82  ? 2.2584 1.9109 1.5420 0.3103  0.3030  -0.1657 80   THR H CA  
20856 C  C   . THR H  82  ? 2.2158 1.8317 1.4772 0.3136  0.3112  -0.1925 80   THR H C   
20857 O  O   . THR H  82  ? 2.3236 1.8724 1.5761 0.3236  0.3094  -0.2055 80   THR H O   
20858 C  CB  . THR H  82  ? 2.2342 1.9323 1.5246 0.3136  0.3147  -0.1878 80   THR H CB  
20859 O  OG1 . THR H  82  ? 2.1929 1.8313 1.4865 0.3295  0.3151  -0.2107 80   THR H OG1 
20860 C  CG2 . THR H  82  ? 2.3536 2.1107 1.6671 0.3055  0.3083  -0.1567 80   THR H CG2 
20861 N  N   . ARG H  83  ? 2.3002 1.9639 1.5520 0.3020  0.3184  -0.1979 81   ARG H N   
20862 C  CA  . ARG H  83  ? 2.2699 1.9057 1.5028 0.3021  0.3243  -0.2201 81   ARG H CA  
20863 C  C   . ARG H  83  ? 2.2631 1.9473 1.4831 0.2947  0.3364  -0.2520 81   ARG H C   
20864 O  O   . ARG H  83  ? 2.2789 2.0313 1.5018 0.2860  0.3420  -0.2532 81   ARG H O   
20865 C  CB  . ARG H  83  ? 2.3231 1.9602 1.5588 0.2934  0.3184  -0.1938 81   ARG H CB  
20866 C  CG  . ARG H  83  ? 2.4541 2.1696 1.6918 0.2730  0.3178  -0.1775 81   ARG H CG  
20867 C  CD  . ARG H  83  ? 2.4921 2.2043 1.7415 0.2659  0.3109  -0.1515 81   ARG H CD  
20868 N  NE  . ARG H  83  ? 2.7659 2.5539 2.0147 0.2421  0.3079  -0.1352 81   ARG H NE  
20869 C  CZ  . ARG H  83  ? 2.8379 2.6406 2.1029 0.2313  0.3002  -0.1084 81   ARG H CZ  
20870 N  NH1 . ARG H  83  ? 2.9495 2.6971 2.2350 0.2452  0.2980  -0.0988 81   ARG H NH1 
20871 N  NH2 . ARG H  83  ? 2.6904 2.5672 1.9527 0.2052  0.2948  -0.0910 81   ARG H NH2 
20872 N  N   . VAL H  84  ? 2.0464 1.6968 1.2522 0.2967  0.3401  -0.2792 82   VAL H N   
20873 C  CA  . VAL H  84  ? 2.0673 1.7526 1.2600 0.2890  0.3498  -0.3155 82   VAL H CA  
20874 C  C   . VAL H  84  ? 2.0741 1.7404 1.2509 0.2794  0.3464  -0.3181 82   VAL H C   
20875 O  O   . VAL H  84  ? 2.0722 1.6756 1.2495 0.2875  0.3412  -0.3163 82   VAL H O   
20876 C  CB  . VAL H  84  ? 2.0846 1.7415 1.2885 0.3047  0.3559  -0.3564 82   VAL H CB  
20877 C  CG1 . VAL H  84  ? 2.0846 1.7922 1.3054 0.3095  0.3645  -0.3618 82   VAL H CG1 
20878 C  CG2 . VAL H  84  ? 2.0799 1.6545 1.2939 0.3192  0.3461  -0.3506 82   VAL H CG2 
20879 N  N   . LEU H  85  ? 2.1959 1.9215 1.3579 0.2594  0.3487  -0.3197 83   LEU H N   
20880 C  CA  . LEU H  85  ? 2.2726 1.9895 1.4208 0.2468  0.3443  -0.3213 83   LEU H CA  
20881 C  C   . LEU H  85  ? 2.1960 1.8780 1.3356 0.2509  0.3471  -0.3687 83   LEU H C   
20882 O  O   . LEU H  85  ? 2.1741 1.8503 1.3209 0.2622  0.3540  -0.4030 83   LEU H O   
20883 C  CB  . LEU H  85  ? 2.4337 2.2296 1.5692 0.2197  0.3424  -0.3044 83   LEU H CB  
20884 C  CG  . LEU H  85  ? 2.2863 2.1204 1.4403 0.2118  0.3344  -0.2514 83   LEU H CG  
20885 C  CD1 . LEU H  85  ? 2.6278 2.5495 1.7696 0.1800  0.3300  -0.2344 83   LEU H CD1 
20886 C  CD2 . LEU H  85  ? 2.3011 2.0846 1.4758 0.2209  0.3262  -0.2203 83   LEU H CD2 
20887 N  N   . MET H  86  ? 2.2708 1.9307 1.4011 0.2413  0.3403  -0.3693 84   MET H N   
20888 C  CA  . MET H  86  ? 2.2693 1.8884 1.3974 0.2433  0.3375  -0.4089 84   MET H CA  
20889 C  C   . MET H  86  ? 2.4691 2.1365 1.5771 0.2239  0.3406  -0.4438 84   MET H C   
20890 O  O   . MET H  86  ? 2.7593 2.4971 1.8505 0.2058  0.3448  -0.4342 84   MET H O   
20891 C  CB  . MET H  86  ? 2.2810 1.8487 1.4111 0.2416  0.3269  -0.3905 84   MET H CB  
20892 C  CG  . MET H  86  ? 2.3246 1.9263 1.4430 0.2205  0.3220  -0.3654 84   MET H CG  
20893 S  SD  . MET H  86  ? 2.3468 1.8926 1.4699 0.2174  0.3109  -0.3553 84   MET H SD  
20894 C  CE  . MET H  86  ? 2.4332 2.0348 1.5491 0.1914  0.3058  -0.3249 84   MET H CE  
20895 N  N   . VAL H  87  ? 2.6773 2.3070 1.7882 0.2254  0.3364  -0.4843 85   VAL H N   
20896 C  CA  . VAL H  87  ? 2.5276 2.1917 1.6183 0.2064  0.3377  -0.5258 85   VAL H CA  
20897 C  C   . VAL H  87  ? 2.5359 2.2028 1.6085 0.1822  0.3238  -0.5027 85   VAL H C   
20898 O  O   . VAL H  87  ? 2.5585 2.1751 1.6435 0.1861  0.3125  -0.4768 85   VAL H O   
20899 C  CB  . VAL H  87  ? 2.4444 2.0616 1.5561 0.2203  0.3372  -0.5831 85   VAL H CB  
20900 C  CG1 . VAL H  87  ? 2.7116 2.3672 1.8010 0.2009  0.3410  -0.6347 85   VAL H CG1 
20901 C  CG2 . VAL H  87  ? 2.3723 1.9843 1.5128 0.2466  0.3497  -0.5978 85   VAL H CG2 
20902 N  N   . GLU H  88  ? 2.7232 2.4550 1.7665 0.1548  0.3246  -0.5098 86   GLU H N   
20903 C  CA  . GLU H  88  ? 2.9163 2.6619 1.9440 0.1280  0.3100  -0.4840 86   GLU H CA  
20904 C  C   . GLU H  88  ? 3.2109 2.9000 2.2409 0.1235  0.2963  -0.5157 86   GLU H C   
20905 O  O   . GLU H  88  ? 3.4214 3.0670 2.4648 0.1385  0.2978  -0.5631 86   GLU H O   
20906 C  CB  . GLU H  88  ? 3.1978 3.0323 2.1918 0.0956  0.3119  -0.4841 86   GLU H CB  
20907 C  CG  . GLU H  88  ? 3.1142 3.0097 2.1085 0.0982  0.3243  -0.4607 86   GLU H CG  
20908 C  CD  . GLU H  88  ? 2.9940 2.9824 1.9511 0.0661  0.3298  -0.4782 86   GLU H CD  
20909 O  OE1 . GLU H  88  ? 2.8683 2.8728 1.7956 0.0407  0.3239  -0.5098 86   GLU H OE1 
20910 O  OE2 . GLU H  88  ? 2.8958 2.9433 1.8520 0.0640  0.3392  -0.4606 86   GLU H OE2 
20911 N  N   . THR H  89  ? 3.0490 2.7406 2.0716 0.1013  0.2808  -0.4872 87   THR H N   
20912 C  CA  . THR H  89  ? 3.0070 2.6516 2.0311 0.0908  0.2639  -0.5130 87   THR H CA  
20913 C  C   . THR H  89  ? 2.9545 2.6307 1.9479 0.0657  0.2608  -0.5657 87   THR H C   
20914 O  O   . THR H  89  ? 2.9819 2.6220 1.9751 0.0522  0.2436  -0.5897 87   THR H O   
20915 C  CB  . THR H  89  ? 2.9956 2.6326 2.0267 0.0756  0.2479  -0.4616 87   THR H CB  
20916 O  OG1 . THR H  89  ? 2.9885 2.6955 2.0066 0.0561  0.2494  -0.4195 87   THR H OG1 
20917 C  CG2 . THR H  89  ? 2.9348 2.5171 1.9978 0.1005  0.2484  -0.4295 87   THR H CG2 
20918 N  N   . HIS H  90  ? 3.0827 2.8267 2.0499 0.0571  0.2763  -0.5848 88   HIS H N   
20919 C  CA  . HIS H  90  ? 3.2748 3.0586 2.2058 0.0306  0.2768  -0.6398 88   HIS H CA  
20920 C  C   . HIS H  90  ? 3.3278 3.0748 2.2730 0.0527  0.2884  -0.7157 88   HIS H C   
20921 O  O   . HIS H  90  ? 3.5117 3.2795 2.4319 0.0348  0.2902  -0.7756 88   HIS H O   
20922 C  CB  . HIS H  90  ? 3.3246 3.2103 2.2190 0.0065  0.2886  -0.6242 88   HIS H CB  
20923 C  CG  . HIS H  90  ? 3.3669 3.2920 2.2614 -0.0120 0.2768  -0.5452 88   HIS H CG  
20924 N  ND1 . HIS H  90  ? 3.2470 3.1534 2.1769 0.0123  0.2794  -0.4896 88   HIS H ND1 
20925 C  CD2 . HIS H  90  ? 3.4020 3.3856 2.2706 -0.0527 0.2616  -0.5132 88   HIS H CD2 
20926 C  CE1 . HIS H  90  ? 3.1514 3.1004 2.0833 -0.0095 0.2674  -0.4290 88   HIS H CE1 
20927 N  NE2 . HIS H  90  ? 3.3615 3.3591 2.2581 -0.0496 0.2554  -0.4385 88   HIS H NE2 
20928 N  N   . ASN H  91  ? 3.1193 2.8124 2.1071 0.0904  0.2952  -0.7147 89   ASN H N   
20929 C  CA  . ASN H  91  ? 3.0470 2.7010 2.0650 0.1160  0.3047  -0.7797 89   ASN H CA  
20930 C  C   . ASN H  91  ? 2.9756 2.5374 2.0461 0.1436  0.2905  -0.7637 89   ASN H C   
20931 O  O   . ASN H  91  ? 2.8845 2.4315 1.9682 0.1568  0.2897  -0.7077 89   ASN H O   
20932 C  CB  . ASN H  91  ? 2.9987 2.7095 2.0158 0.1323  0.3332  -0.7968 89   ASN H CB  
20933 C  CG  . ASN H  91  ? 3.4573 3.2634 2.4236 0.1029  0.3484  -0.8277 89   ASN H CG  
20934 O  OD1 . ASN H  91  ? 3.6612 3.4773 2.5995 0.0773  0.3415  -0.8695 89   ASN H OD1 
20935 N  ND2 . ASN H  91  ? 3.5703 3.4497 2.5230 0.1029  0.3674  -0.8050 89   ASN H ND2 
20936 N  N   . GLU H  92  ? 3.0016 2.5030 2.1028 0.1496  0.2774  -0.8126 90   GLU H N   
20937 C  CA  . GLU H  92  ? 2.9449 2.3605 2.1024 0.1724  0.2603  -0.8029 90   GLU H CA  
20938 C  C   . GLU H  92  ? 2.7276 2.1054 1.8898 0.1653  0.2392  -0.7337 90   GLU H C   
20939 O  O   . GLU H  92  ? 2.7457 2.0548 1.9486 0.1720  0.2177  -0.7284 90   GLU H O   
20940 C  CB  . GLU H  92  ? 2.9897 2.4010 2.1818 0.2063  0.2780  -0.8048 90   GLU H CB  
20941 C  CG  . GLU H  92  ? 3.0579 2.5021 2.2615 0.2199  0.3007  -0.8746 90   GLU H CG  
20942 C  CD  . GLU H  92  ? 3.0259 2.4747 2.2637 0.2510  0.3175  -0.8650 90   GLU H CD  
20943 O  OE1 . GLU H  92  ? 3.1772 2.6058 2.4204 0.2585  0.3109  -0.8037 90   GLU H OE1 
20944 O  OE2 . GLU H  92  ? 2.7416 2.2172 2.0007 0.2669  0.3378  -0.9195 90   GLU H OE2 
20945 N  N   . ILE H  93  ? 2.7962 2.2193 1.9225 0.1513  0.2443  -0.6795 91   ILE H N   
20946 C  CA  . ILE H  93  ? 3.1456 2.5376 2.2810 0.1483  0.2296  -0.6177 91   ILE H CA  
20947 C  C   . ILE H  93  ? 3.1815 2.5585 2.3098 0.1198  0.2054  -0.6096 91   ILE H C   
20948 O  O   . ILE H  93  ? 3.3313 2.6770 2.4745 0.1157  0.1902  -0.5656 91   ILE H O   
20949 C  CB  . ILE H  93  ? 3.2067 2.6464 2.3209 0.1503  0.2452  -0.5624 91   ILE H CB  
20950 C  CG1 . ILE H  93  ? 3.0234 2.4848 2.1420 0.1741  0.2673  -0.5710 91   ILE H CG1 
20951 C  CG2 . ILE H  93  ? 2.9044 2.3103 2.0337 0.1540  0.2361  -0.5069 91   ILE H CG2 
20952 C  CD1 . ILE H  93  ? 2.6863 2.1741 1.7976 0.1809  0.2779  -0.5157 91   ILE H CD1 
20953 N  N   . TYR H  94  ? 3.2063 2.6045 2.3131 0.0987  0.2004  -0.6529 92   TYR H N   
20954 C  CA  . TYR H  94  ? 3.3207 2.7024 2.4218 0.0690  0.1741  -0.6490 92   TYR H CA  
20955 C  C   . TYR H  94  ? 3.5271 2.8471 2.6587 0.0690  0.1542  -0.7069 92   TYR H C   
20956 O  O   . TYR H  94  ? 3.6848 2.9759 2.8221 0.0457  0.1266  -0.7031 92   TYR H O   
20957 C  CB  . TYR H  94  ? 3.5053 2.9586 2.5566 0.0367  0.1770  -0.6482 92   TYR H CB  
20958 C  CG  . TYR H  94  ? 3.7754 3.2624 2.7988 0.0282  0.1884  -0.7190 92   TYR H CG  
20959 C  CD1 . TYR H  94  ? 3.7713 3.3099 2.7792 0.0429  0.2175  -0.7367 92   TYR H CD1 
20960 C  CD2 . TYR H  94  ? 3.8038 3.2760 2.8150 0.0029  0.1701  -0.7685 92   TYR H CD2 
20961 C  CE1 . TYR H  94  ? 3.7977 3.3775 2.7779 0.0334  0.2312  -0.8029 92   TYR H CE1 
20962 C  CE2 . TYR H  94  ? 3.7079 3.2160 2.6897 -0.0063 0.1834  -0.8394 92   TYR H CE2 
20963 C  CZ  . TYR H  94  ? 3.7053 3.2704 2.6708 0.0091  0.2155  -0.8565 92   TYR H CZ  
20964 O  OH  . TYR H  94  ? 3.5856 3.1957 2.5201 -0.0016 0.2318  -0.9286 92   TYR H OH  
20965 N  N   . ASP H  95  ? 3.6444 2.9431 2.8025 0.0949  0.1663  -0.7592 93   ASP H N   
20966 C  CA  . ASP H  95  ? 3.8539 3.0974 3.0487 0.0971  0.1494  -0.8241 93   ASP H CA  
20967 C  C   . ASP H  95  ? 3.7450 2.9066 2.9982 0.1021  0.1168  -0.7988 93   ASP H C   
20968 O  O   . ASP H  95  ? 3.8549 2.9641 3.1434 0.0957  0.0922  -0.8406 93   ASP H O   
20969 C  CB  . ASP H  95  ? 3.8628 3.1142 3.0780 0.1259  0.1745  -0.8874 93   ASP H CB  
20970 C  CG  . ASP H  95  ? 3.6221 2.9625 2.7796 0.1178  0.2066  -0.9135 93   ASP H CG  
20971 O  OD1 . ASP H  95  ? 3.8641 3.2558 2.9676 0.0872  0.2052  -0.8865 93   ASP H OD1 
20972 O  OD2 . ASP H  95  ? 3.0606 2.4239 2.2301 0.1404  0.2320  -0.9581 93   ASP H OD2 
20973 N  N   . LYS H  96  ? 3.3392 2.4901 2.6047 0.1111  0.1148  -0.7322 94   LYS H N   
20974 C  CA  . LYS H  96  ? 3.3619 2.4436 2.6816 0.1124  0.0836  -0.7031 94   LYS H CA  
20975 C  C   . LYS H  96  ? 3.4609 2.5481 2.7653 0.0896  0.0677  -0.6304 94   LYS H C   
20976 O  O   . LYS H  96  ? 3.7157 2.7596 3.0499 0.0713  0.0338  -0.6154 94   LYS H O   
20977 C  CB  . LYS H  96  ? 3.2381 2.2946 2.5983 0.1442  0.0924  -0.6938 94   LYS H CB  
20978 C  CG  . LYS H  96  ? 3.2187 2.2095 2.6365 0.1427  0.0583  -0.6581 94   LYS H CG  
20979 C  CD  . LYS H  96  ? 3.1315 2.1021 2.5878 0.1708  0.0654  -0.6482 94   LYS H CD  
20980 C  CE  . LYS H  96  ? 3.0512 1.9687 2.5562 0.1626  0.0304  -0.5978 94   LYS H CE  
20981 N  NZ  . LYS H  96  ? 3.0813 1.9405 2.6437 0.1487  -0.0096 -0.6203 94   LYS H NZ  
20982 N  N   . PHE H  97  ? 3.3870 2.5274 2.6514 0.0901  0.0906  -0.5851 95   PHE H N   
20983 C  CA  . PHE H  97  ? 3.4319 2.5813 2.6895 0.0740  0.0811  -0.5167 95   PHE H CA  
20984 C  C   . PHE H  97  ? 3.4329 2.6491 2.6442 0.0577  0.0963  -0.4892 95   PHE H C   
20985 O  O   . PHE H  97  ? 3.4204 2.6456 2.6299 0.0348  0.0811  -0.4488 95   PHE H O   
20986 C  CB  . PHE H  97  ? 3.4139 2.5525 2.6858 0.0943  0.0914  -0.4770 95   PHE H CB  
20987 C  CG  . PHE H  97  ? 3.3792 2.5262 2.6494 0.1241  0.1173  -0.5048 95   PHE H CG  
20988 C  CD1 . PHE H  97  ? 3.2752 2.4803 2.5059 0.1316  0.1476  -0.5070 95   PHE H CD1 
20989 C  CD2 . PHE H  97  ? 3.2827 2.3814 2.5966 0.1428  0.1088  -0.5247 95   PHE H CD2 
20990 C  CE1 . PHE H  97  ? 3.2040 2.4200 2.4351 0.1568  0.1696  -0.5290 95   PHE H CE1 
20991 C  CE2 . PHE H  97  ? 3.0812 2.1911 2.3974 0.1694  0.1319  -0.5476 95   PHE H CE2 
20992 C  CZ  . PHE H  97  ? 3.1015 2.2706 2.3745 0.1760  0.1627  -0.5500 95   PHE H CZ  
20993 N  N   . LYS H  98  ? 3.4239 2.6898 2.6034 0.0680  0.1244  -0.5057 96   LYS H N   
20994 C  CA  . LYS H  98  ? 3.3638 2.6968 2.5082 0.0551  0.1391  -0.4728 96   LYS H CA  
20995 C  C   . LYS H  98  ? 3.2351 2.5794 2.3869 0.0640  0.1491  -0.4110 96   LYS H C   
20996 O  O   . LYS H  98  ? 3.1031 2.4194 2.2712 0.0862  0.1570  -0.4029 96   LYS H O   
20997 C  CB  . LYS H  98  ? 3.2687 2.6209 2.3973 0.0196  0.1186  -0.4718 96   LYS H CB  
20998 C  CG  . LYS H  98  ? 3.2702 2.6216 2.3814 0.0070  0.1119  -0.5384 96   LYS H CG  
20999 C  CD  . LYS H  98  ? 3.2269 2.6157 2.3096 -0.0319 0.0956  -0.5316 96   LYS H CD  
21000 C  CE  . LYS H  98  ? 3.2883 2.6339 2.3958 -0.0535 0.0613  -0.5101 96   LYS H CE  
21001 N  NZ  . LYS H  98  ? 3.2968 2.5719 2.4312 -0.0518 0.0391  -0.5658 96   LYS H NZ  
21002 N  N   . GLN H  99  ? 3.3806 2.7685 2.5222 0.0465  0.1497  -0.3689 97   GLN H N   
21003 C  CA  . GLN H  99  ? 3.4343 2.8419 2.5851 0.0554  0.1633  -0.3153 97   GLN H CA  
21004 C  C   . GLN H  99  ? 3.5192 2.9226 2.6867 0.0338  0.1444  -0.2772 97   GLN H C   
21005 O  O   . GLN H  99  ? 3.5065 2.9213 2.6708 0.0070  0.1248  -0.2773 97   GLN H O   
21006 C  CB  . GLN H  99  ? 3.4121 2.8833 2.5490 0.0576  0.1840  -0.2940 97   GLN H CB  
21007 C  CG  . GLN H  99  ? 3.4170 2.9087 2.5701 0.0706  0.2011  -0.2458 97   GLN H CG  
21008 C  CD  . GLN H  99  ? 3.4860 3.0115 2.6540 0.0497  0.1933  -0.2027 97   GLN H CD  
21009 O  OE1 . GLN H  99  ? 3.4609 2.9788 2.6473 0.0515  0.1949  -0.1734 97   GLN H OE1 
21010 N  NE2 . GLN H  99  ? 3.5127 3.0809 2.6733 0.0277  0.1844  -0.1973 97   GLN H NE2 
21011 N  N   . SER H  100 ? 3.4457 2.8364 2.6295 0.0432  0.1499  -0.2441 98   SER H N   
21012 C  CA  . SER H  100 ? 3.4266 2.8230 2.6279 0.0230  0.1354  -0.2029 98   SER H CA  
21013 C  C   . SER H  100 ? 3.3645 2.7846 2.5734 0.0369  0.1591  -0.1636 98   SER H C   
21014 O  O   . SER H  100 ? 3.2732 2.6895 2.4744 0.0617  0.1813  -0.1717 98   SER H O   
21015 C  CB  . SER H  100 ? 3.4125 2.7527 2.6315 0.0092  0.1038  -0.2126 98   SER H CB  
21016 O  OG  . SER H  100 ? 3.3810 2.6981 2.5971 -0.0047 0.0816  -0.2535 98   SER H OG  
21017 N  N   . THR H  101 ? 3.3540 2.8005 2.5789 0.0195  0.1541  -0.1222 99   THR H N   
21018 C  CA  . THR H  101 ? 3.2347 2.7111 2.4685 0.0302  0.1785  -0.0877 99   THR H CA  
21019 C  C   . THR H  101 ? 3.1760 2.6154 2.4050 0.0395  0.1806  -0.0903 99   THR H C   
21020 O  O   . THR H  101 ? 3.2505 2.7123 2.4790 0.0496  0.2040  -0.0705 99   THR H O   
21021 C  CB  . THR H  101 ? 3.3591 2.8760 2.6148 0.0067  0.1712  -0.0439 99   THR H CB  
21022 O  OG1 . THR H  101 ? 3.3977 2.8820 2.6608 -0.0177 0.1392  -0.0358 99   THR H OG1 
21023 C  CG2 . THR H  101 ? 3.4395 2.9941 2.7023 -0.0069 0.1644  -0.0367 99   THR H CG2 
21024 N  N   . HIS H  102 ? 3.3105 2.6956 2.5384 0.0353  0.1562  -0.1148 100  HIS H N   
21025 C  CA  . HIS H  102 ? 3.4318 2.7812 2.6610 0.0382  0.1504  -0.1111 100  HIS H CA  
21026 C  C   . HIS H  102 ? 3.3811 2.7076 2.5954 0.0663  0.1680  -0.1406 100  HIS H C   
21027 O  O   . HIS H  102 ? 3.3230 2.6406 2.5307 0.0726  0.1763  -0.1296 100  HIS H O   
21028 C  CB  . HIS H  102 ? 3.5928 2.8938 2.8432 0.0170  0.1092  -0.1158 100  HIS H CB  
21029 C  CG  . HIS H  102 ? 3.7504 3.0202 3.0113 0.0112  0.0948  -0.0989 100  HIS H CG  
21030 N  ND1 . HIS H  102 ? 3.7133 2.9301 3.0033 -0.0025 0.0562  -0.1052 100  HIS H ND1 
21031 C  CD2 . HIS H  102 ? 3.7912 3.0770 3.0393 0.0145  0.1115  -0.0745 100  HIS H CD2 
21032 C  CE1 . HIS H  102 ? 3.7170 2.9204 3.0136 -0.0086 0.0479  -0.0801 100  HIS H CE1 
21033 N  NE2 . HIS H  102 ? 3.7617 3.0078 3.0283 0.0002  0.0817  -0.0622 100  HIS H NE2 
21034 N  N   . SER H  103 ? 3.3855 2.7077 2.5927 0.0809  0.1739  -0.1758 101  SER H N   
21035 C  CA  . SER H  103 ? 3.3104 2.6133 2.5073 0.1062  0.1883  -0.2025 101  SER H CA  
21036 C  C   . SER H  103 ? 3.0360 2.3659 2.2214 0.1187  0.2039  -0.2266 101  SER H C   
21037 O  O   . SER H  103 ? 2.9448 2.2999 2.1297 0.1054  0.1981  -0.2289 101  SER H O   
21038 C  CB  . SER H  103 ? 3.4253 2.6719 2.6381 0.1070  0.1646  -0.2261 101  SER H CB  
21039 O  OG  . SER H  103 ? 3.5274 2.7551 2.7554 0.0942  0.1408  -0.2501 101  SER H OG  
21040 N  N   . ILE H  104 ? 2.8439 2.1713 2.0200 0.1414  0.2219  -0.2413 102  ILE H N   
21041 C  CA  . ILE H  104 ? 2.7887 2.1436 1.9549 0.1526  0.2356  -0.2615 102  ILE H CA  
21042 C  C   . ILE H  104 ? 2.8226 2.1476 1.9884 0.1699  0.2363  -0.2945 102  ILE H C   
21043 O  O   . ILE H  104 ? 2.7041 2.0039 1.8720 0.1823  0.2404  -0.2886 102  ILE H O   
21044 C  CB  . ILE H  104 ? 2.7817 2.1780 1.9447 0.1630  0.2595  -0.2361 102  ILE H CB  
21045 C  CG1 . ILE H  104 ? 3.0524 2.4905 2.2243 0.1463  0.2589  -0.2084 102  ILE H CG1 
21046 C  CG2 . ILE H  104 ? 2.6683 2.0840 1.8244 0.1777  0.2720  -0.2528 102  ILE H CG2 
21047 C  CD1 . ILE H  104 ? 3.1315 2.6104 2.3146 0.1574  0.2806  -0.1830 102  ILE H CD1 
21048 N  N   . TYR H  105 ? 2.9242 2.2563 2.0877 0.1695  0.2329  -0.3292 103  TYR H N   
21049 C  CA  . TYR H  105 ? 2.7785 2.0869 1.9492 0.1854  0.2337  -0.3649 103  TYR H CA  
21050 C  C   . TYR H  105 ? 2.7481 2.0988 1.9045 0.1970  0.2536  -0.3766 103  TYR H C   
21051 O  O   . TYR H  105 ? 2.9245 2.3213 2.0663 0.1856  0.2584  -0.3772 103  TYR H O   
21052 C  CB  . TYR H  105 ? 2.7264 2.0079 1.9121 0.1768  0.2145  -0.4041 103  TYR H CB  
21053 C  CG  . TYR H  105 ? 2.8468 2.0858 2.0535 0.1619  0.1888  -0.3900 103  TYR H CG  
21054 C  CD1 . TYR H  105 ? 2.9672 2.1575 2.2011 0.1689  0.1752  -0.3850 103  TYR H CD1 
21055 C  CD2 . TYR H  105 ? 3.0722 2.3226 2.2743 0.1380  0.1754  -0.3770 103  TYR H CD2 
21056 C  CE1 . TYR H  105 ? 3.2026 2.3580 2.4591 0.1515  0.1481  -0.3659 103  TYR H CE1 
21057 C  CE2 . TYR H  105 ? 3.3132 2.5278 2.5373 0.1217  0.1493  -0.3595 103  TYR H CE2 
21058 C  CZ  . TYR H  105 ? 3.3691 2.5370 2.6207 0.1281  0.1354  -0.3533 103  TYR H CZ  
21059 O  OH  . TYR H  105 ? 3.4679 2.6044 2.7446 0.1082  0.1061  -0.3301 103  TYR H OH  
21060 N  N   . MET H  106 ? 2.6382 1.9758 1.8006 0.2168  0.2626  -0.3824 104  MET H N   
21061 C  CA  . MET H  106 ? 2.5634 1.9388 1.7175 0.2279  0.2791  -0.3915 104  MET H CA  
21062 C  C   . MET H  106 ? 2.5412 1.8970 1.7120 0.2423  0.2789  -0.4286 104  MET H C   
21063 O  O   . MET H  106 ? 2.5973 1.9056 1.7889 0.2519  0.2699  -0.4287 104  MET H O   
21064 C  CB  . MET H  106 ? 2.5723 1.9553 1.7227 0.2390  0.2909  -0.3570 104  MET H CB  
21065 C  CG  . MET H  106 ? 2.6134 2.0120 1.7586 0.2300  0.2937  -0.3212 104  MET H CG  
21066 S  SD  . MET H  106 ? 2.4439 1.8310 1.5908 0.2459  0.3061  -0.2923 104  MET H SD  
21067 C  CE  . MET H  106 ? 2.5878 1.9136 1.7364 0.2491  0.2953  -0.2979 104  MET H CE  
21068 N  N   . PHE H  107 ? 2.6083 2.0058 1.7725 0.2428  0.2891  -0.4577 105  PHE H N   
21069 C  CA  . PHE H  107 ? 2.5744 1.9625 1.7601 0.2571  0.2924  -0.4993 105  PHE H CA  
21070 C  C   . PHE H  107 ? 2.4944 1.9322 1.6736 0.2670  0.3108  -0.4997 105  PHE H C   
21071 O  O   . PHE H  107 ? 2.7720 2.2643 1.9269 0.2560  0.3195  -0.4821 105  PHE H O   
21072 C  CB  . PHE H  107 ? 2.8295 2.2223 2.0178 0.2471  0.2877  -0.5486 105  PHE H CB  
21073 C  CG  . PHE H  107 ? 2.9910 2.3200 2.2065 0.2442  0.2654  -0.5596 105  PHE H CG  
21074 C  CD1 . PHE H  107 ? 3.1302 2.4420 2.3349 0.2257  0.2500  -0.5305 105  PHE H CD1 
21075 C  CD2 . PHE H  107 ? 3.0151 2.3038 2.2738 0.2591  0.2582  -0.5964 105  PHE H CD2 
21076 C  CE1 . PHE H  107 ? 3.2037 2.4598 2.4364 0.2197  0.2260  -0.5354 105  PHE H CE1 
21077 C  CE2 . PHE H  107 ? 3.0432 2.2721 2.3351 0.2544  0.2328  -0.6021 105  PHE H CE2 
21078 C  CZ  . PHE H  107 ? 3.0844 2.2974 2.3613 0.2333  0.2159  -0.5702 105  PHE H CZ  
21079 N  N   . PHE H  108 ? 2.2665 1.6870 1.4731 0.2863  0.3143  -0.5161 106  PHE H N   
21080 C  CA  . PHE H  108 ? 2.2366 1.7027 1.4446 0.2965  0.3302  -0.5163 106  PHE H CA  
21081 C  C   . PHE H  108 ? 2.2523 1.7230 1.4913 0.3103  0.3376  -0.5665 106  PHE H C   
21082 O  O   . PHE H  108 ? 2.6938 2.1191 1.9613 0.3157  0.3274  -0.5966 106  PHE H O   
21083 C  CB  . PHE H  108 ? 2.6512 2.0928 1.8668 0.3080  0.3275  -0.4753 106  PHE H CB  
21084 C  CG  . PHE H  108 ? 2.9192 2.3609 2.1103 0.2980  0.3245  -0.4312 106  PHE H CG  
21085 C  CD1 . PHE H  108 ? 2.6070 2.0032 1.7940 0.2922  0.3130  -0.4147 106  PHE H CD1 
21086 C  CD2 . PHE H  108 ? 2.9901 2.4796 2.1680 0.2944  0.3329  -0.4054 106  PHE H CD2 
21087 C  CE1 . PHE H  108 ? 2.3376 1.7380 1.5081 0.2855  0.3138  -0.3787 106  PHE H CE1 
21088 C  CE2 . PHE H  108 ? 2.7154 2.2029 1.8820 0.2881  0.3303  -0.3680 106  PHE H CE2 
21089 C  CZ  . PHE H  108 ? 2.4153 1.8590 1.5783 0.2850  0.3228  -0.3572 106  PHE H CZ  
21090 N  N   . GLN H  109 ? 2.2613 1.7889 1.5010 0.3163  0.3549  -0.5747 107  GLN H N   
21091 C  CA  . GLN H  109 ? 2.5311 2.0720 1.8062 0.3324  0.3664  -0.6232 107  GLN H CA  
21092 C  C   . GLN H  109 ? 2.5060 2.0134 1.8231 0.3541  0.3622  -0.6047 107  GLN H C   
21093 O  O   . GLN H  109 ? 2.7361 2.1941 2.0539 0.3551  0.3463  -0.5629 107  GLN H O   
21094 C  CB  . GLN H  109 ? 2.7796 2.4134 2.0324 0.3238  0.3897  -0.6455 107  GLN H CB  
21095 C  CG  . GLN H  109 ? 2.9052 2.5811 2.1156 0.2985  0.3935  -0.6679 107  GLN H CG  
21096 C  CD  . GLN H  109 ? 2.7332 2.5097 1.9193 0.2860  0.4161  -0.6872 107  GLN H CD  
21097 O  OE1 . GLN H  109 ? 2.4968 2.3149 1.6969 0.2957  0.4285  -0.6751 107  GLN H OE1 
21098 N  NE2 . GLN H  109 ? 2.7893 2.6095 1.9376 0.2614  0.4203  -0.7151 107  GLN H NE2 
21099 N  N   . THR H  110 ? 2.3779 1.9162 1.7305 0.3702  0.3768  -0.6364 108  THR H N   
21100 C  CA  . THR H  110 ? 2.3335 1.8549 1.7294 0.3894  0.3740  -0.6178 108  THR H CA  
21101 C  C   . THR H  110 ? 2.3315 1.9314 1.7388 0.3969  0.3976  -0.6318 108  THR H C   
21102 O  O   . THR H  110 ? 2.3191 1.9226 1.7493 0.4068  0.3959  -0.6019 108  THR H O   
21103 C  CB  . THR H  110 ? 2.3473 1.8032 1.8064 0.4070  0.3600  -0.6418 108  THR H CB  
21104 O  OG1 . THR H  110 ? 2.4204 1.8152 1.8701 0.3961  0.3392  -0.6388 108  THR H OG1 
21105 C  CG2 . THR H  110 ? 2.3339 1.7564 1.8296 0.4192  0.3466  -0.6025 108  THR H CG2 
21106 N  N   . SER H  111 ? 2.4981 2.1653 1.8883 0.3899  0.4191  -0.6750 109  SER H N   
21107 C  CA  . SER H  111 ? 2.6659 2.4217 2.0617 0.3926  0.4437  -0.6871 109  SER H CA  
21108 C  C   . SER H  111 ? 2.5014 2.3034 1.8598 0.3763  0.4419  -0.6275 109  SER H C   
21109 O  O   . SER H  111 ? 2.5482 2.4096 1.9219 0.3802  0.4542  -0.6161 109  SER H O   
21110 C  CB  . SER H  111 ? 3.1615 2.9818 2.5377 0.3831  0.4668  -0.7492 109  SER H CB  
21111 O  OG  . SER H  111 ? 3.3920 3.1609 2.8097 0.3991  0.4657  -0.8071 109  SER H OG  
21112 N  N   . GLU H  112 ? 2.3856 2.1614 1.7017 0.3586  0.4258  -0.5884 110  GLU H N   
21113 C  CA  . GLU H  112 ? 2.5189 2.3218 1.8103 0.3451  0.4186  -0.5292 110  GLU H CA  
21114 C  C   . GLU H  112 ? 2.3192 2.0468 1.6250 0.3551  0.3979  -0.4848 110  GLU H C   
21115 O  O   . GLU H  112 ? 2.3055 2.0501 1.6068 0.3502  0.3919  -0.4403 110  GLU H O   
21116 C  CB  . GLU H  112 ? 2.6143 2.4430 1.8568 0.3188  0.4145  -0.5125 110  GLU H CB  
21117 C  CG  . GLU H  112 ? 2.5325 2.2866 1.7622 0.3166  0.3996  -0.5156 110  GLU H CG  
21118 C  CD  . GLU H  112 ? 2.6291 2.4148 1.8174 0.2903  0.3956  -0.4994 110  GLU H CD  
21119 O  OE1 . GLU H  112 ? 2.6706 2.5370 1.8391 0.2717  0.4030  -0.4866 110  GLU H OE1 
21120 O  OE2 . GLU H  112 ? 2.7034 2.4368 1.8815 0.2863  0.3836  -0.4960 110  GLU H OE2 
21121 N  N   . LEU H  113 ? 2.3740 2.0208 1.6961 0.3661  0.3852  -0.4954 111  LEU H N   
21122 C  CA  . LEU H  113 ? 2.3263 1.9054 1.6586 0.3726  0.3661  -0.4572 111  LEU H CA  
21123 C  C   . LEU H  113 ? 2.3693 1.9506 1.7451 0.3883  0.3656  -0.4512 111  LEU H C   
21124 O  O   . LEU H  113 ? 2.4294 2.0030 1.8038 0.3869  0.3560  -0.4106 111  LEU H O   
21125 C  CB  . LEU H  113 ? 2.2490 1.7511 1.5854 0.3746  0.3512  -0.4670 111  LEU H CB  
21126 C  CG  . LEU H  113 ? 2.2317 1.7114 1.5272 0.3586  0.3440  -0.4514 111  LEU H CG  
21127 C  CD1 . LEU H  113 ? 2.2282 1.6908 1.5033 0.3535  0.3356  -0.4036 111  LEU H CD1 
21128 C  CD2 . LEU H  113 ? 2.3776 1.9164 1.6439 0.3442  0.3567  -0.4687 111  LEU H CD2 
21129 N  N   . ARG H  114 ? 2.3739 1.9656 1.7928 0.4034  0.3753  -0.4923 112  ARG H N   
21130 C  CA  . ARG H  114 ? 2.4222 2.0283 1.8926 0.4196  0.3778  -0.4902 112  ARG H CA  
21131 C  C   . ARG H  114 ? 2.3597 2.0611 1.8292 0.4169  0.3987  -0.4896 112  ARG H C   
21132 O  O   . ARG H  114 ? 2.5006 2.2300 2.0165 0.4303  0.4051  -0.4912 112  ARG H O   
21133 C  CB  . ARG H  114 ? 2.4880 2.0659 2.0180 0.4390  0.3794  -0.5356 112  ARG H CB  
21134 C  CG  . ARG H  114 ? 2.3186 1.8013 1.8650 0.4403  0.3517  -0.5228 112  ARG H CG  
21135 C  CD  . ARG H  114 ? 2.2990 1.7500 1.9216 0.4599  0.3468  -0.5586 112  ARG H CD  
21136 N  NE  . ARG H  114 ? 2.3612 1.8242 1.9903 0.4636  0.3606  -0.6177 112  ARG H NE  
21137 C  CZ  . ARG H  114 ? 2.7028 2.2271 2.3595 0.4766  0.3876  -0.6692 112  ARG H CZ  
21138 N  NH1 . ARG H  114 ? 2.9864 2.5695 2.6701 0.4876  0.4041  -0.6645 112  ARG H NH1 
21139 N  NH2 . ARG H  114 ? 2.4852 2.0149 2.1422 0.4773  0.3985  -0.7264 112  ARG H NH2 
21140 N  N   . GLU H  115 ? 2.4138 2.1693 1.8349 0.3979  0.4076  -0.4822 113  GLU H N   
21141 C  CA  . GLU H  115 ? 2.5831 2.4327 1.9995 0.3887  0.4221  -0.4679 113  GLU H CA  
21142 C  C   . GLU H  115 ? 2.5703 2.4166 1.9653 0.3747  0.4041  -0.4045 113  GLU H C   
21143 O  O   . GLU H  115 ? 2.5402 2.4343 1.9533 0.3728  0.4047  -0.3769 113  GLU H O   
21144 C  CB  . GLU H  115 ? 2.8967 2.8237 2.2783 0.3723  0.4427  -0.5005 113  GLU H CB  
21145 C  CG  . GLU H  115 ? 2.9089 2.9501 2.2984 0.3659  0.4664  -0.5092 113  GLU H CG  
21146 C  CD  . GLU H  115 ? 3.0378 3.1303 2.4115 0.3464  0.4564  -0.4462 113  GLU H CD  
21147 O  OE1 . GLU H  115 ? 3.1688 3.2342 2.5096 0.3300  0.4376  -0.4073 113  GLU H OE1 
21148 O  OE2 . GLU H  115 ? 3.0113 3.1733 2.4111 0.3473  0.4670  -0.4354 113  GLU H OE2 
21149 N  N   . ALA H  116 ? 2.6361 2.4264 1.9977 0.3651  0.3876  -0.3818 114  ALA H N   
21150 C  CA  . ALA H  116 ? 2.8028 2.5737 2.1518 0.3554  0.3689  -0.3275 114  ALA H CA  
21151 C  C   . ALA H  116 ? 2.8587 2.5652 2.2335 0.3679  0.3523  -0.3071 114  ALA H C   
21152 O  O   . ALA H  116 ? 2.8613 2.5726 2.2423 0.3628  0.3400  -0.2676 114  ALA H O   
21153 C  CB  . ALA H  116 ? 2.7543 2.4875 2.0665 0.3439  0.3597  -0.3154 114  ALA H CB  
21154 N  N   . VAL H  117 ? 2.7640 2.4094 2.1551 0.3814  0.3486  -0.3310 115  VAL H N   
21155 C  CA  . VAL H  117 ? 2.5545 2.1446 1.9734 0.3904  0.3316  -0.3129 115  VAL H CA  
21156 C  C   . VAL H  117 ? 2.5790 2.1774 2.0495 0.4081  0.3405  -0.3470 115  VAL H C   
21157 O  O   . VAL H  117 ? 2.6191 2.1706 2.1012 0.4153  0.3374  -0.3735 115  VAL H O   
21158 C  CB  . VAL H  117 ? 2.3382 1.8421 1.7321 0.3860  0.3129  -0.3001 115  VAL H CB  
21159 C  CG1 . VAL H  117 ? 2.3316 1.7855 1.7479 0.3889  0.2927  -0.2763 115  VAL H CG1 
21160 C  CG2 . VAL H  117 ? 2.3193 1.8187 1.6695 0.3719  0.3088  -0.2755 115  VAL H CG2 
21161 N  N   . PRO H  118 ? 2.3379 1.9973 1.8463 0.4154  0.3511  -0.3470 116  PRO H N   
21162 C  CA  . PRO H  118 ? 2.3315 2.0065 1.8996 0.4354  0.3632  -0.3844 116  PRO H CA  
21163 C  C   . PRO H  118 ? 2.3347 1.9299 1.9432 0.4460  0.3415  -0.3790 116  PRO H C   
21164 O  O   . PRO H  118 ? 2.3902 1.9555 2.0282 0.4574  0.3431  -0.4151 116  PRO H O   
21165 C  CB  . PRO H  118 ? 2.4592 2.2152 2.0586 0.4380  0.3750  -0.3698 116  PRO H CB  
21166 C  CG  . PRO H  118 ? 2.3867 2.1902 1.9343 0.4166  0.3764  -0.3399 116  PRO H CG  
21167 C  CD  . PRO H  118 ? 2.3714 2.0949 1.8741 0.4050  0.3530  -0.3129 116  PRO H CD  
21168 N  N   . GLU H  119 ? 2.4444 2.0060 2.0571 0.4400  0.3187  -0.3328 117  GLU H N   
21169 C  CA  . GLU H  119 ? 2.6196 2.1132 2.2714 0.4450  0.2947  -0.3203 117  GLU H CA  
21170 C  C   . GLU H  119 ? 2.5404 1.9578 2.1407 0.4288  0.2732  -0.3015 117  GLU H C   
21171 O  O   . GLU H  119 ? 2.3960 1.8057 1.9408 0.4135  0.2679  -0.2754 117  GLU H O   
21172 C  CB  . GLU H  119 ? 2.7930 2.2963 2.4820 0.4449  0.2801  -0.2807 117  GLU H CB  
21173 C  CG  . GLU H  119 ? 2.8856 2.3354 2.6325 0.4504  0.2558  -0.2676 117  GLU H CG  
21174 C  CD  . GLU H  119 ? 2.8664 2.3401 2.6634 0.4523  0.2441  -0.2323 117  GLU H CD  
21175 O  OE1 . GLU H  119 ? 2.8548 2.3865 2.6402 0.4491  0.2550  -0.2177 117  GLU H OE1 
21176 O  OE2 . GLU H  119 ? 2.8553 2.2920 2.7073 0.4551  0.2218  -0.2155 117  GLU H OE2 
21177 N  N   . PRO H  120 ? 2.5006 1.8639 2.1211 0.4312  0.2607  -0.3144 118  PRO H N   
21178 C  CA  . PRO H  120 ? 2.7002 2.0009 2.2697 0.4136  0.2430  -0.2978 118  PRO H CA  
21179 C  C   . PRO H  120 ? 2.7213 1.9880 2.2599 0.3964  0.2209  -0.2516 118  PRO H C   
21180 O  O   . PRO H  120 ? 2.6989 1.9306 2.1811 0.3806  0.2138  -0.2395 118  PRO H O   
21181 C  CB  . PRO H  120 ? 2.5727 1.8293 2.1902 0.4187  0.2285  -0.3126 118  PRO H CB  
21182 C  CG  . PRO H  120 ? 2.4545 1.7537 2.1355 0.4419  0.2478  -0.3548 118  PRO H CG  
21183 C  CD  . PRO H  120 ? 2.4651 1.8248 2.1610 0.4496  0.2618  -0.3451 118  PRO H CD  
21184 N  N   . VAL H  121 ? 2.5977 1.8758 2.1717 0.3983  0.2101  -0.2269 119  VAL H N   
21185 C  CA  . VAL H  121 ? 2.4502 1.6930 1.9941 0.3791  0.1862  -0.1850 119  VAL H CA  
21186 C  C   . VAL H  121 ? 2.4333 1.6950 1.9215 0.3707  0.1947  -0.1743 119  VAL H C   
21187 O  O   . VAL H  121 ? 2.4609 1.6843 1.9045 0.3531  0.1791  -0.1512 119  VAL H O   
21188 C  CB  . VAL H  121 ? 2.5754 1.8243 2.1796 0.3815  0.1683  -0.1586 119  VAL H CB  
21189 C  CG1 . VAL H  121 ? 2.6093 1.8094 2.1815 0.3565  0.1372  -0.1169 119  VAL H CG1 
21190 C  CG2 . VAL H  121 ? 2.6384 1.8832 2.3207 0.3969  0.1645  -0.1748 119  VAL H CG2 
21191 N  N   . LEU H  122 ? 2.4435 1.7649 1.9352 0.3813  0.2184  -0.1911 120  LEU H N   
21192 C  CA  . LEU H  122 ? 2.6665 2.0099 2.1183 0.3727  0.2229  -0.1760 120  LEU H CA  
21193 C  C   . LEU H  122 ? 2.8132 2.1208 2.2068 0.3627  0.2246  -0.1815 120  LEU H C   
21194 O  O   . LEU H  122 ? 2.7212 2.0202 2.0826 0.3528  0.2193  -0.1635 120  LEU H O   
21195 C  CB  . LEU H  122 ? 2.5255 1.9492 1.9961 0.3824  0.2465  -0.1901 120  LEU H CB  
21196 C  CG  . LEU H  122 ? 2.5806 2.0578 2.1125 0.3942  0.2523  -0.1898 120  LEU H CG  
21197 C  CD1 . LEU H  122 ? 2.5701 2.1342 2.1091 0.3998  0.2796  -0.2090 120  LEU H CD1 
21198 C  CD2 . LEU H  122 ? 2.6799 2.1510 2.2263 0.3852  0.2303  -0.1467 120  LEU H CD2 
21199 N  N   . LEU H  123 ? 2.9142 2.2005 2.2993 0.3654  0.2310  -0.2057 121  LEU H N   
21200 C  CA  . LEU H  123 ? 2.7261 1.9879 2.0620 0.3572  0.2358  -0.2121 121  LEU H CA  
21201 C  C   . LEU H  123 ? 2.4966 1.7036 1.7968 0.3418  0.2180  -0.1904 121  LEU H C   
21202 O  O   . LEU H  123 ? 2.4792 1.6496 1.7863 0.3343  0.1999  -0.1792 121  LEU H O   
21203 C  CB  . LEU H  123 ? 2.7702 2.0208 2.1106 0.3611  0.2426  -0.2393 121  LEU H CB  
21204 C  CG  . LEU H  123 ? 2.8652 2.1183 2.1680 0.3569  0.2556  -0.2530 121  LEU H CG  
21205 C  CD1 . LEU H  123 ? 2.8251 2.0292 2.0873 0.3432  0.2462  -0.2393 121  LEU H CD1 
21206 C  CD2 . LEU H  123 ? 3.0140 2.3191 2.3061 0.3585  0.2705  -0.2516 121  LEU H CD2 
21207 N  N   . SER H  124 ? 2.4310 1.6348 1.6956 0.3360  0.2224  -0.1846 122  SER H N   
21208 C  CA  . SER H  124 ? 2.5682 1.7240 1.7944 0.3218  0.2103  -0.1727 122  SER H CA  
21209 C  C   . SER H  124 ? 2.6799 1.8166 1.8696 0.3174  0.2213  -0.1874 122  SER H C   
21210 O  O   . SER H  124 ? 2.7944 1.8951 1.9606 0.3054  0.2134  -0.1869 122  SER H O   
21211 C  CB  . SER H  124 ? 2.3422 1.5031 1.5637 0.3190  0.2048  -0.1563 122  SER H CB  
21212 O  OG  . SER H  124 ? 2.3298 1.4426 1.5134 0.3055  0.1945  -0.1523 122  SER H OG  
21213 N  N   . ARG H  125 ? 2.7845 1.9492 1.9709 0.3245  0.2383  -0.1970 123  ARG H N   
21214 C  CA  . ARG H  125 ? 2.8179 1.9725 1.9776 0.3216  0.2503  -0.2092 123  ARG H CA  
21215 C  C   . ARG H  125 ? 2.6652 1.8623 1.8404 0.3301  0.2656  -0.2217 123  ARG H C   
21216 O  O   . ARG H  125 ? 2.8018 2.0395 1.9952 0.3360  0.2709  -0.2177 123  ARG H O   
21217 C  CB  . ARG H  125 ? 2.9371 2.0755 2.0742 0.3183  0.2535  -0.2059 123  ARG H CB  
21218 C  CG  . ARG H  125 ? 2.9559 2.0900 2.0716 0.3168  0.2685  -0.2182 123  ARG H CG  
21219 C  CD  . ARG H  125 ? 3.0064 2.1194 2.1054 0.3151  0.2725  -0.2203 123  ARG H CD  
21220 N  NE  . ARG H  125 ? 3.1015 2.2145 2.1841 0.3143  0.2892  -0.2329 123  ARG H NE  
21221 C  CZ  . ARG H  125 ? 3.1497 2.2448 2.2173 0.3135  0.2979  -0.2427 123  ARG H CZ  
21222 N  NH1 . ARG H  125 ? 3.1440 2.2137 2.2083 0.3124  0.2891  -0.2433 123  ARG H NH1 
21223 N  NH2 . ARG H  125 ? 3.2592 2.3627 2.3173 0.3137  0.3155  -0.2537 123  ARG H NH2 
21224 N  N   . ALA H  126 ? 2.4126 1.6029 1.5798 0.3276  0.2705  -0.2347 124  ALA H N   
21225 C  CA  . ALA H  126 ? 2.3929 1.6196 1.5703 0.3320  0.2828  -0.2486 124  ALA H CA  
21226 C  C   . ALA H  126 ? 2.1985 1.4141 1.3534 0.3255  0.2901  -0.2520 124  ALA H C   
21227 O  O   . ALA H  126 ? 2.2085 1.3995 1.3554 0.3185  0.2849  -0.2564 124  ALA H O   
21228 C  CB  . ALA H  126 ? 2.5853 1.8194 1.7877 0.3363  0.2795  -0.2645 124  ALA H CB  
21229 N  N   . GLU H  127 ? 2.2239 1.4600 1.3745 0.3268  0.3005  -0.2467 125  GLU H N   
21230 C  CA  . GLU H  127 ? 2.2351 1.4690 1.3717 0.3221  0.3098  -0.2480 125  GLU H CA  
21231 C  C   . GLU H  127 ? 2.2450 1.5208 1.3940 0.3219  0.3172  -0.2523 125  GLU H C   
21232 O  O   . GLU H  127 ? 2.4911 1.8045 1.6558 0.3249  0.3195  -0.2466 125  GLU H O   
21233 C  CB  . GLU H  127 ? 2.4554 1.6797 1.5856 0.3242  0.3161  -0.2399 125  GLU H CB  
21234 C  CG  . GLU H  127 ? 2.4053 1.6505 1.5582 0.3313  0.3141  -0.2286 125  GLU H CG  
21235 C  CD  . GLU H  127 ? 2.6336 1.8589 1.7876 0.3347  0.3175  -0.2247 125  GLU H CD  
21236 O  OE1 . GLU H  127 ? 2.6957 1.9020 1.8325 0.3327  0.3272  -0.2339 125  GLU H OE1 
21237 O  OE2 . GLU H  127 ? 2.8068 2.0370 1.9816 0.3387  0.3103  -0.2134 125  GLU H OE2 
21238 N  N   . LEU H  128 ? 2.0928 1.3647 1.2342 0.3151  0.3188  -0.2595 126  LEU H N   
21239 C  CA  . LEU H  128 ? 2.0897 1.3982 1.2388 0.3109  0.3234  -0.2638 126  LEU H CA  
21240 C  C   . LEU H  128 ? 2.1051 1.4313 1.2566 0.3093  0.3331  -0.2493 126  LEU H C   
21241 O  O   . LEU H  128 ? 2.3233 1.6293 1.4647 0.3068  0.3378  -0.2459 126  LEU H O   
21242 C  CB  . LEU H  128 ? 2.1026 1.3960 1.2481 0.3030  0.3168  -0.2775 126  LEU H CB  
21243 C  CG  . LEU H  128 ? 2.2565 1.5819 1.4054 0.2946  0.3189  -0.2838 126  LEU H CG  
21244 C  CD1 . LEU H  128 ? 2.5969 1.9647 1.7544 0.2962  0.3214  -0.2945 126  LEU H CD1 
21245 C  CD2 . LEU H  128 ? 2.1932 1.4938 1.3421 0.2857  0.3083  -0.2960 126  LEU H CD2 
21246 N  N   . ARG H  129 ? 2.2773 1.6456 1.4457 0.3095  0.3359  -0.2394 127  ARG H N   
21247 C  CA  . ARG H  129 ? 2.3207 1.7092 1.5060 0.3098  0.3428  -0.2218 127  ARG H CA  
21248 C  C   . ARG H  129 ? 2.4533 1.8819 1.6457 0.2984  0.3429  -0.2166 127  ARG H C   
21249 O  O   . ARG H  129 ? 2.6218 2.0804 1.8111 0.2903  0.3375  -0.2225 127  ARG H O   
21250 C  CB  . ARG H  129 ? 2.3016 1.7064 1.5107 0.3164  0.3406  -0.2053 127  ARG H CB  
21251 C  CG  . ARG H  129 ? 2.2765 1.6410 1.4784 0.3254  0.3378  -0.2097 127  ARG H CG  
21252 C  CD  . ARG H  129 ? 2.3038 1.6736 1.5356 0.3319  0.3351  -0.1921 127  ARG H CD  
21253 N  NE  . ARG H  129 ? 2.2887 1.6144 1.5108 0.3385  0.3315  -0.1983 127  ARG H NE  
21254 C  CZ  . ARG H  129 ? 2.4219 1.7359 1.6683 0.3449  0.3274  -0.1888 127  ARG H CZ  
21255 N  NH1 . ARG H  129 ? 2.6590 2.0025 1.9475 0.3469  0.3258  -0.1697 127  ARG H NH1 
21256 N  NH2 . ARG H  129 ? 2.4089 1.6804 1.6408 0.3478  0.3224  -0.1971 127  ARG H NH2 
21257 N  N   . LEU H  130 ? 2.4481 1.8802 1.6502 0.2966  0.3496  -0.2062 128  LEU H N   
21258 C  CA  . LEU H  130 ? 2.5021 1.9712 1.7135 0.2837  0.3480  -0.1966 128  LEU H CA  
21259 C  C   . LEU H  130 ? 2.6912 2.1927 1.9414 0.2860  0.3522  -0.1698 128  LEU H C   
21260 O  O   . LEU H  130 ? 2.9181 2.4162 2.1908 0.2974  0.3540  -0.1604 128  LEU H O   
21261 C  CB  . LEU H  130 ? 2.4375 1.8865 1.6333 0.2766  0.3496  -0.2042 128  LEU H CB  
21262 C  CG  . LEU H  130 ? 2.3580 1.7654 1.5264 0.2750  0.3432  -0.2257 128  LEU H CG  
21263 C  CD1 . LEU H  130 ? 2.3838 1.7821 1.5449 0.2626  0.3399  -0.2247 128  LEU H CD1 
21264 C  CD2 . LEU H  130 ? 2.4377 1.8505 1.5991 0.2725  0.3337  -0.2435 128  LEU H CD2 
21265 N  N   . LEU H  131 ? 2.5367 2.0681 1.8007 0.2749  0.3517  -0.1560 129  LEU H N   
21266 C  CA  . LEU H  131 ? 2.4928 2.0576 1.8047 0.2767  0.3544  -0.1273 129  LEU H CA  
21267 C  C   . LEU H  131 ? 2.7765 2.3491 2.0987 0.2722  0.3620  -0.1203 129  LEU H C   
21268 O  O   . LEU H  131 ? 3.0007 2.5910 2.3081 0.2543  0.3537  -0.1185 129  LEU H O   
21269 C  CB  . LEU H  131 ? 2.5848 2.2026 1.9149 0.2610  0.3398  -0.1041 129  LEU H CB  
21270 C  CG  . LEU H  131 ? 2.6298 2.2863 2.0210 0.2605  0.3368  -0.0668 129  LEU H CG  
21271 C  CD1 . LEU H  131 ? 2.5350 2.1633 1.9658 0.2852  0.3476  -0.0648 129  LEU H CD1 
21272 C  CD2 . LEU H  131 ? 2.9458 2.6554 2.3508 0.2416  0.3185  -0.0405 129  LEU H CD2 
21273 N  N   . ARG H  132 ? 2.9021 2.4646 2.2517 0.2875  0.3777  -0.1173 130  ARG H N   
21274 C  CA  . ARG H  132 ? 2.7989 2.3766 2.1641 0.2845  0.3883  -0.1090 130  ARG H CA  
21275 C  C   . ARG H  132 ? 2.8056 2.4343 2.2291 0.2798  0.3843  -0.0754 130  ARG H C   
21276 O  O   . ARG H  132 ? 3.0142 2.6616 2.4758 0.2839  0.3766  -0.0578 130  ARG H O   
21277 C  CB  . ARG H  132 ? 2.7502 2.3032 2.1198 0.3023  0.4109  -0.1240 130  ARG H CB  
21278 C  CG  . ARG H  132 ? 2.7598 2.2704 2.0725 0.3001  0.4148  -0.1500 130  ARG H CG  
21279 C  CD  . ARG H  132 ? 3.1959 2.6975 2.5125 0.3122  0.4391  -0.1626 130  ARG H CD  
21280 N  NE  . ARG H  132 ? 3.4585 2.9238 2.7201 0.3060  0.4408  -0.1827 130  ARG H NE  
21281 C  CZ  . ARG H  132 ? 3.3677 2.8244 2.6151 0.3105  0.4605  -0.1978 130  ARG H CZ  
21282 N  NH1 . ARG H  132 ? 3.1486 2.6285 2.4356 0.3250  0.4837  -0.2010 130  ARG H NH1 
21283 N  NH2 . ARG H  132 ? 3.3070 2.7346 2.5030 0.2994  0.4569  -0.2101 130  ARG H NH2 
21284 N  N   . LEU H  133 ? 2.5833 2.2367 2.0171 0.2688  0.3866  -0.0624 131  LEU H N   
21285 C  CA  . LEU H  133 ? 2.6449 2.3473 2.1431 0.2661  0.3858  -0.0280 131  LEU H CA  
21286 C  C   . LEU H  133 ? 2.6299 2.3357 2.1607 0.2823  0.4113  -0.0305 131  LEU H C   
21287 O  O   . LEU H  133 ? 2.6238 2.2981 2.1171 0.2895  0.4271  -0.0574 131  LEU H O   
21288 C  CB  . LEU H  133 ? 2.7141 2.4513 2.2017 0.2366  0.3659  -0.0075 131  LEU H CB  
21289 C  CG  . LEU H  133 ? 2.8525 2.6027 2.3164 0.2187  0.3430  -0.0038 131  LEU H CG  
21290 C  CD1 . LEU H  133 ? 3.0419 2.8268 2.4917 0.1870  0.3237  0.0118  131  LEU H CD1 
21291 C  CD2 . LEU H  133 ? 2.7675 2.5434 2.2848 0.2263  0.3376  0.0216  131  LEU H CD2 
21292 N  N   . LYS H  134 ? 2.6140 2.3622 2.2179 0.2872  0.4156  -0.0017 132  LYS H N   
21293 C  CA  . LYS H  134 ? 2.7320 2.4925 2.3743 0.3041  0.4439  -0.0065 132  LYS H CA  
21294 C  C   . LYS H  134 ? 2.9779 2.7440 2.5757 0.2871  0.4491  -0.0104 132  LYS H C   
21295 O  O   . LYS H  134 ? 3.1614 2.9503 2.7493 0.2623  0.4297  0.0120  132  LYS H O   
21296 C  CB  . LYS H  134 ? 2.9033 2.7138 2.6435 0.3117  0.4453  0.0290  132  LYS H CB  
21297 C  CG  . LYS H  134 ? 2.9146 2.7727 2.6738 0.2835  0.4206  0.0718  132  LYS H CG  
21298 C  CD  . LYS H  134 ? 2.9628 2.8722 2.8294 0.2922  0.4225  0.1104  132  LYS H CD  
21299 C  CE  . LYS H  134 ? 2.8275 2.7872 2.7120 0.2598  0.3951  0.1568  132  LYS H CE  
21300 N  NZ  . LYS H  134 ? 2.7708 2.7834 2.7686 0.2674  0.3949  0.1998  132  LYS H NZ  
21301 N  N   . LEU H  135 ? 3.0976 2.8428 2.6660 0.2973  0.4728  -0.0384 133  LEU H N   
21302 C  CA  . LEU H  135 ? 3.2038 2.9542 2.7299 0.2789  0.4759  -0.0394 133  LEU H CA  
21303 C  C   . LEU H  135 ? 3.2225 3.0060 2.7789 0.2898  0.5092  -0.0426 133  LEU H C   
21304 O  O   . LEU H  135 ? 3.2402 3.0418 2.7723 0.2720  0.5123  -0.0352 133  LEU H O   
21305 C  CB  . LEU H  135 ? 3.1509 2.8482 2.5971 0.2706  0.4674  -0.0669 133  LEU H CB  
21306 C  CG  . LEU H  135 ? 3.1018 2.7971 2.5046 0.2432  0.4529  -0.0593 133  LEU H CG  
21307 C  CD1 . LEU H  135 ? 2.8793 2.5990 2.2988 0.2225  0.4272  -0.0317 133  LEU H CD1 
21308 C  CD2 . LEU H  135 ? 3.2191 2.8600 2.5577 0.2368  0.4396  -0.0833 133  LEU H CD2 
21309 N  N   . LYS H  136 ? 3.0468 2.8401 2.6573 0.3176  0.5338  -0.0546 134  LYS H N   
21310 C  CA  . LYS H  136 ? 2.9475 2.7783 2.5967 0.3327  0.5712  -0.0649 134  LYS H CA  
21311 C  C   . LYS H  136 ? 2.9683 2.7836 2.5423 0.3228  0.5874  -0.0925 134  LYS H C   
21312 O  O   . LYS H  136 ? 2.9343 2.6976 2.4449 0.3193  0.5773  -0.1155 134  LYS H O   
21313 C  CB  . LYS H  136 ? 2.9838 2.8786 2.6966 0.3247  0.5726  -0.0261 134  LYS H CB  
21314 C  CG  . LYS H  136 ? 3.0921 3.0084 2.8869 0.3325  0.5559  0.0058  134  LYS H CG  
21315 C  CD  . LYS H  136 ? 3.2340 3.2160 3.0892 0.3202  0.5543  0.0484  134  LYS H CD  
21316 C  CE  . LYS H  136 ? 3.2341 3.2421 3.1735 0.3230  0.5333  0.0870  134  LYS H CE  
21317 N  NZ  . LYS H  136 ? 3.3133 3.3873 3.3136 0.3089  0.5300  0.1318  134  LYS H NZ  
21318 N  N   . VAL H  137 ? 3.1942 3.0586 2.7751 0.3142  0.6089  -0.0852 135  VAL H N   
21319 C  CA  . VAL H  137 ? 3.5573 3.4307 3.0923 0.3106  0.6377  -0.1126 135  VAL H CA  
21320 C  C   . VAL H  137 ? 3.6006 3.4177 3.0442 0.2943  0.6211  -0.1317 135  VAL H C   
21321 O  O   . VAL H  137 ? 3.7251 3.5046 3.1443 0.3089  0.6314  -0.1668 135  VAL H O   
21322 C  CB  . VAL H  137 ? 3.4902 3.4298 3.0351 0.2904  0.6494  -0.0860 135  VAL H CB  
21323 C  CG1 . VAL H  137 ? 3.2564 3.2289 2.7774 0.2923  0.6906  -0.1157 135  VAL H CG1 
21324 C  CG2 . VAL H  137 ? 3.2898 3.2833 2.9287 0.3008  0.6539  -0.0545 135  VAL H CG2 
21325 N  N   . GLU H  138 ? 3.2704 3.0794 2.6678 0.2636  0.5932  -0.1083 136  GLU H N   
21326 C  CA  . GLU H  138 ? 3.0786 2.8445 2.3984 0.2459  0.5797  -0.1224 136  GLU H CA  
21327 C  C   . GLU H  138 ? 2.9085 2.6379 2.2010 0.2243  0.5364  -0.1009 136  GLU H C   
21328 O  O   . GLU H  138 ? 2.9701 2.7224 2.2871 0.2103  0.5193  -0.0711 136  GLU H O   
21329 C  CB  . GLU H  138 ? 3.1024 2.9083 2.3876 0.2251  0.5996  -0.1217 136  GLU H CB  
21330 C  CG  . GLU H  138 ? 2.9213 2.7542 2.2089 0.2429  0.6445  -0.1576 136  GLU H CG  
21331 C  CD  . GLU H  138 ? 2.8793 2.7708 2.1362 0.2180  0.6665  -0.1521 136  GLU H CD  
21332 O  OE1 . GLU H  138 ? 2.8921 2.8485 2.1912 0.2131  0.6809  -0.1287 136  GLU H OE1 
21333 O  OE2 . GLU H  138 ? 2.9037 2.7808 2.0946 0.2006  0.6678  -0.1680 136  GLU H OE2 
21334 N  N   . GLN H  139 ? 2.8003 2.4726 2.0460 0.2224  0.5187  -0.1182 137  GLN H N   
21335 C  CA  . GLN H  139 ? 2.8283 2.4650 2.0428 0.2002  0.4810  -0.1048 137  GLN H CA  
21336 C  C   . GLN H  139 ? 2.8051 2.3937 1.9664 0.1955  0.4724  -0.1241 137  GLN H C   
21337 O  O   . GLN H  139 ? 2.7555 2.3285 1.9048 0.2126  0.4903  -0.1496 137  GLN H O   
21338 C  CB  . GLN H  139 ? 2.8961 2.5144 2.1358 0.2072  0.4581  -0.0995 137  GLN H CB  
21339 C  CG  . GLN H  139 ? 3.0092 2.6077 2.2340 0.1828  0.4220  -0.0842 137  GLN H CG  
21340 C  CD  . GLN H  139 ? 3.1150 2.7537 2.3557 0.1589  0.4155  -0.0535 137  GLN H CD  
21341 O  OE1 . GLN H  139 ? 3.1664 2.7867 2.3912 0.1351  0.3871  -0.0418 137  GLN H OE1 
21342 N  NE2 . GLN H  139 ? 3.1449 2.8389 2.4240 0.1653  0.4399  -0.0395 137  GLN H NE2 
21343 N  N   . HIS H  140 ? 2.8151 2.3794 1.9491 0.1709  0.4425  -0.1104 138  HIS H N   
21344 C  CA  . HIS H  140 ? 2.9290 2.4472 2.0206 0.1629  0.4269  -0.1212 138  HIS H CA  
21345 C  C   . HIS H  140 ? 3.0676 2.5404 2.1622 0.1587  0.3908  -0.1190 138  HIS H C   
21346 O  O   . HIS H  140 ? 3.1646 2.6429 2.2759 0.1435  0.3702  -0.1009 138  HIS H O   
21347 C  CB  . HIS H  140 ? 2.9363 2.4732 1.9956 0.1333  0.4254  -0.1049 138  HIS H CB  
21348 C  CG  . HIS H  140 ? 2.9440 2.4405 1.9615 0.1237  0.4117  -0.1132 138  HIS H CG  
21349 N  ND1 . HIS H  140 ? 3.1418 2.6473 2.1287 0.0908  0.3986  -0.0923 138  HIS H ND1 
21350 C  CD2 . HIS H  140 ? 2.7953 2.2458 1.7994 0.1400  0.4071  -0.1359 138  HIS H CD2 
21351 C  CE1 . HIS H  140 ? 2.9904 2.4558 1.9475 0.0873  0.3855  -0.1015 138  HIS H CE1 
21352 N  NE2 . HIS H  140 ? 2.8360 2.2671 1.8030 0.1177  0.3911  -0.1288 138  HIS H NE2 
21353 N  N   . VAL H  141 ? 3.0529 2.4824 2.1332 0.1717  0.3834  -0.1390 139  VAL H N   
21354 C  CA  . VAL H  141 ? 2.9939 2.3846 2.0821 0.1741  0.3558  -0.1453 139  VAL H CA  
21355 C  C   . VAL H  141 ? 3.0925 2.4403 2.1567 0.1655  0.3365  -0.1488 139  VAL H C   
21356 O  O   . VAL H  141 ? 3.1391 2.4782 2.1787 0.1696  0.3480  -0.1572 139  VAL H O   
21357 C  CB  . VAL H  141 ? 2.9970 2.3853 2.1029 0.1999  0.3648  -0.1631 139  VAL H CB  
21358 C  CG1 . VAL H  141 ? 3.1189 2.4755 2.2296 0.2015  0.3404  -0.1738 139  VAL H CG1 
21359 C  CG2 . VAL H  141 ? 2.9707 2.4038 2.1077 0.2053  0.3794  -0.1530 139  VAL H CG2 
21360 N  N   . GLU H  142 ? 3.0977 2.4186 2.1725 0.1523  0.3056  -0.1423 140  GLU H N   
21361 C  CA  . GLU H  142 ? 2.9877 2.2653 2.0560 0.1465  0.2822  -0.1442 140  GLU H CA  
21362 C  C   . GLU H  142 ? 2.9625 2.2106 2.0538 0.1630  0.2684  -0.1658 140  GLU H C   
21363 O  O   . GLU H  142 ? 3.0010 2.2562 2.1128 0.1641  0.2623  -0.1716 140  GLU H O   
21364 C  CB  . GLU H  142 ? 2.9394 2.2102 2.0116 0.1156  0.2547  -0.1167 140  GLU H CB  
21365 C  CG  . GLU H  142 ? 3.2005 2.5103 2.2470 0.0941  0.2680  -0.0932 140  GLU H CG  
21366 C  CD  . GLU H  142 ? 3.2271 2.5353 2.2809 0.0592  0.2365  -0.0590 140  GLU H CD  
21367 O  OE1 . GLU H  142 ? 3.1494 2.4175 2.2328 0.0543  0.2026  -0.0560 140  GLU H OE1 
21368 O  OE2 . GLU H  142 ? 3.3035 2.6529 2.3374 0.0361  0.2452  -0.0353 140  GLU H OE2 
21369 N  N   . LEU H  143 ? 2.9401 2.1584 2.0274 0.1736  0.2632  -0.1778 141  LEU H N   
21370 C  CA  . LEU H  143 ? 2.8540 2.0517 1.9628 0.1908  0.2550  -0.2009 141  LEU H CA  
21371 C  C   . LEU H  143 ? 2.9895 2.1477 2.1208 0.1825  0.2246  -0.1994 141  LEU H C   
21372 O  O   . LEU H  143 ? 3.1342 2.2763 2.2579 0.1677  0.2116  -0.1798 141  LEU H O   
21373 C  CB  . LEU H  143 ? 2.7532 1.9526 1.8507 0.2123  0.2731  -0.2154 141  LEU H CB  
21374 C  CG  . LEU H  143 ? 2.4612 1.6542 1.5790 0.2301  0.2701  -0.2384 141  LEU H CG  
21375 C  CD1 . LEU H  143 ? 2.3802 1.6006 1.5103 0.2326  0.2749  -0.2494 141  LEU H CD1 
21376 C  CD2 . LEU H  143 ? 2.4387 1.6346 1.5462 0.2469  0.2843  -0.2445 141  LEU H CD2 
21377 N  N   . TYR H  144 ? 2.8115 1.9562 1.9733 0.1908  0.2129  -0.2207 142  TYR H N   
21378 C  CA  . TYR H  144 ? 2.7655 1.8714 1.9638 0.1867  0.1838  -0.2243 142  TYR H CA  
21379 C  C   . TYR H  144 ? 2.4257 1.5221 1.6464 0.2105  0.1875  -0.2576 142  TYR H C   
21380 O  O   . TYR H  144 ? 2.3657 1.4890 1.5728 0.2261  0.2096  -0.2770 142  TYR H O   
21381 C  CB  . TYR H  144 ? 2.8337 1.9295 2.0585 0.1693  0.1609  -0.2202 142  TYR H CB  
21382 C  CG  . TYR H  144 ? 2.7713 1.8785 1.9818 0.1416  0.1519  -0.1816 142  TYR H CG  
21383 C  CD1 . TYR H  144 ? 2.7966 1.8809 2.0216 0.1206  0.1244  -0.1520 142  TYR H CD1 
21384 C  CD2 . TYR H  144 ? 2.8320 1.9786 2.0179 0.1348  0.1704  -0.1717 142  TYR H CD2 
21385 C  CE1 . TYR H  144 ? 2.9716 2.0759 2.1810 0.0916  0.1168  -0.1142 142  TYR H CE1 
21386 C  CE2 . TYR H  144 ? 3.0001 2.1658 2.1743 0.1092  0.1652  -0.1367 142  TYR H CE2 
21387 C  CZ  . TYR H  144 ? 3.1396 2.2861 2.3227 0.0867  0.1390  -0.1083 142  TYR H CZ  
21388 O  OH  . TYR H  144 ? 3.3792 2.5540 2.5483 0.0577  0.1343  -0.0711 142  TYR H OH  
21389 N  N   . GLN H  145 ? 2.7701 1.8315 2.0305 0.2118  0.1643  -0.2616 143  GLN H N   
21390 C  CA  . GLN H  145 ? 2.7423 1.7951 2.0345 0.2339  0.1661  -0.2932 143  GLN H CA  
21391 C  C   . GLN H  145 ? 2.9816 2.0066 2.3273 0.2333  0.1433  -0.3152 143  GLN H C   
21392 O  O   . GLN H  145 ? 3.1807 2.1796 2.5487 0.2142  0.1164  -0.2950 143  GLN H O   
21393 C  CB  . GLN H  145 ? 2.7312 1.7671 2.0326 0.2393  0.1599  -0.2784 143  GLN H CB  
21394 C  CG  . GLN H  145 ? 2.8008 1.8363 2.1370 0.2635  0.1652  -0.3074 143  GLN H CG  
21395 C  CD  . GLN H  145 ? 2.7297 1.7439 2.0861 0.2645  0.1511  -0.2862 143  GLN H CD  
21396 O  OE1 . GLN H  145 ? 2.8653 1.8701 2.1954 0.2465  0.1415  -0.2511 143  GLN H OE1 
21397 N  NE2 . GLN H  145 ? 2.6059 1.6163 2.0095 0.2841  0.1499  -0.3075 143  GLN H NE2 
21398 N  N   . LYS H  146 ? 2.8686 1.9012 2.2368 0.2531  0.1536  -0.3575 144  LYS H N   
21399 C  CA  . LYS H  146 ? 2.8861 1.8911 2.3096 0.2563  0.1349  -0.3895 144  LYS H CA  
21400 C  C   . LYS H  146 ? 2.9459 1.9138 2.4320 0.2655  0.1137  -0.3867 144  LYS H C   
21401 O  O   . LYS H  146 ? 2.8451 1.8241 2.3404 0.2841  0.1268  -0.3955 144  LYS H O   
21402 C  CB  . LYS H  146 ? 2.9759 2.0114 2.3950 0.2717  0.1573  -0.4412 144  LYS H CB  
21403 C  CG  . LYS H  146 ? 3.0774 2.0862 2.5493 0.2749  0.1414  -0.4848 144  LYS H CG  
21404 C  CD  . LYS H  146 ? 3.0998 2.1486 2.5569 0.2869  0.1673  -0.5388 144  LYS H CD  
21405 C  CE  . LYS H  146 ? 2.9831 2.0648 2.4426 0.3100  0.1924  -0.5550 144  LYS H CE  
21406 N  NZ  . LYS H  146 ? 2.8090 1.8560 2.3418 0.3282  0.1795  -0.5696 144  LYS H NZ  
21407 N  N   . TYR H  147 ? 3.0251 1.9507 2.5590 0.2509  0.0785  -0.3702 145  TYR H N   
21408 C  CA  . TYR H  147 ? 2.9748 1.8616 2.5832 0.2566  0.0510  -0.3625 145  TYR H CA  
21409 C  C   . TYR H  147 ? 3.0465 1.9045 2.7270 0.2685  0.0368  -0.4089 145  TYR H C   
21410 O  O   . TYR H  147 ? 3.1027 1.9448 2.7885 0.2539  0.0217  -0.4164 145  TYR H O   
21411 C  CB  . TYR H  147 ? 3.0384 1.8986 2.6580 0.2276  0.0157  -0.3030 145  TYR H CB  
21412 C  CG  . TYR H  147 ? 3.4151 2.2883 3.0026 0.2230  0.0207  -0.2653 145  TYR H CG  
21413 C  CD1 . TYR H  147 ? 3.4703 2.3208 3.1136 0.2272  -0.0005 -0.2481 145  TYR H CD1 
21414 C  CD2 . TYR H  147 ? 3.7638 2.6737 3.2686 0.2174  0.0489  -0.2525 145  TYR H CD2 
21415 C  CE1 . TYR H  147 ? 3.5997 2.4625 3.2089 0.2203  0.0029  -0.2146 145  TYR H CE1 
21416 C  CE2 . TYR H  147 ? 3.8034 2.7236 3.2754 0.2137  0.0550  -0.2253 145  TYR H CE2 
21417 C  CZ  . TYR H  147 ? 3.6896 2.5863 3.2092 0.2132  0.0314  -0.2054 145  TYR H CZ  
21418 O  OH  . TYR H  147 ? 3.5157 2.4234 2.9954 0.2055  0.0361  -0.1778 145  TYR H OH  
21419 N  N   . SER H  148 ? 3.4829 2.3346 3.2215 0.2947  0.0415  -0.4406 146  SER H N   
21420 C  CA  . SER H  148 ? 3.6663 2.4955 3.4764 0.3120  0.0355  -0.4974 146  SER H CA  
21421 C  C   . SER H  148 ? 3.6553 2.5169 3.4068 0.3112  0.0624  -0.5412 146  SER H C   
21422 O  O   . SER H  148 ? 3.4690 2.3821 3.1565 0.3186  0.0982  -0.5515 146  SER H O   
21423 C  CB  . SER H  148 ? 3.4675 2.2369 3.3550 0.2959  -0.0141 -0.4730 146  SER H CB  
21424 O  OG  . SER H  148 ? 3.3582 2.1149 3.2540 0.2790  -0.0388 -0.4051 146  SER H OG  
21425 N  N   . GLN H  149 ? 3.6470 2.4824 3.4152 0.2983  0.0436  -0.5610 147  GLN H N   
21426 C  CA  . GLN H  149 ? 3.5939 2.4621 3.2963 0.2886  0.0638  -0.5885 147  GLN H CA  
21427 C  C   . GLN H  149 ? 3.5600 2.4133 3.2328 0.2559  0.0395  -0.5452 147  GLN H C   
21428 O  O   . GLN H  149 ? 3.7170 2.6090 3.3164 0.2420  0.0573  -0.5323 147  GLN H O   
21429 C  CB  . GLN H  149 ? 3.5186 2.3767 3.2619 0.3014  0.0671  -0.6645 147  GLN H CB  
21430 C  CG  . GLN H  149 ? 3.5493 2.4649 3.2565 0.3200  0.1104  -0.7222 147  GLN H CG  
21431 C  CD  . GLN H  149 ? 3.6186 2.5313 3.3988 0.3524  0.1218  -0.7715 147  GLN H CD  
21432 O  OE1 . GLN H  149 ? 3.7062 2.6042 3.5344 0.3636  0.1219  -0.8372 147  GLN H OE1 
21433 N  NE2 . GLN H  149 ? 3.4831 2.4119 3.2731 0.3674  0.1322  -0.7414 147  GLN H NE2 
21434 N  N   . ASN H  150 ? 3.4643 2.2636 3.2015 0.2426  -0.0032 -0.5196 148  ASN H N   
21435 C  CA  . ASN H  150 ? 3.4992 2.2813 3.2257 0.2093  -0.0331 -0.4779 148  ASN H CA  
21436 C  C   . ASN H  150 ? 3.5201 2.3316 3.1858 0.1895  -0.0283 -0.4084 148  ASN H C   
21437 O  O   . ASN H  150 ? 3.3883 2.2305 2.9942 0.1715  -0.0180 -0.3901 148  ASN H O   
21438 C  CB  . ASN H  150 ? 3.5175 2.2344 3.3421 0.2003  -0.0839 -0.4670 148  ASN H CB  
21439 C  CG  . ASN H  150 ? 3.4747 2.1477 3.3747 0.2143  -0.0989 -0.5425 148  ASN H CG  
21440 O  OD1 . ASN H  150 ? 3.3443 2.0294 3.2106 0.2113  -0.0859 -0.5906 148  ASN H OD1 
21441 N  ND2 . ASN H  150 ? 3.5103 2.1323 3.5146 0.2272  -0.1288 -0.5494 148  ASN H ND2 
21442 N  N   . SER H  151 ? 3.4740 2.2832 3.1500 0.1940  -0.0306 -0.3740 149  SER H N   
21443 C  CA  . SER H  151 ? 3.4165 2.2448 3.0465 0.1705  -0.0340 -0.3092 149  SER H CA  
21444 C  C   . SER H  151 ? 3.2038 2.0836 2.7518 0.1791  0.0088  -0.3034 149  SER H C   
21445 O  O   . SER H  151 ? 3.0584 1.9571 2.5929 0.2051  0.0379  -0.3384 149  SER H O   
21446 C  CB  . SER H  151 ? 3.4303 2.2268 3.1157 0.1622  -0.0673 -0.2681 149  SER H CB  
21447 O  OG  . SER H  151 ? 3.5207 2.2666 3.2947 0.1550  -0.1106 -0.2706 149  SER H OG  
21448 N  N   . TRP H  152 ? 3.0128 1.9175 2.5091 0.1557  0.0118  -0.2585 150  TRP H N   
21449 C  CA  . TRP H  152 ? 2.9136 1.8630 2.3382 0.1597  0.0477  -0.2469 150  TRP H CA  
21450 C  C   . TRP H  152 ? 3.0098 1.9620 2.4152 0.1397  0.0378  -0.1953 150  TRP H C   
21451 O  O   . TRP H  152 ? 3.2984 2.2410 2.7187 0.1111  0.0091  -0.1574 150  TRP H O   
21452 C  CB  . TRP H  152 ? 2.9371 1.9226 2.3161 0.1501  0.0659  -0.2468 150  TRP H CB  
21453 C  CG  . TRP H  152 ? 3.0803 2.0658 2.4726 0.1591  0.0694  -0.2910 150  TRP H CG  
21454 C  CD1 . TRP H  152 ? 3.1927 2.1551 2.6184 0.1442  0.0428  -0.2990 150  TRP H CD1 
21455 C  CD2 . TRP H  152 ? 3.0367 2.0490 2.4069 0.1814  0.0996  -0.3329 150  TRP H CD2 
21456 N  NE1 . TRP H  152 ? 3.0349 2.0081 2.4555 0.1557  0.0563  -0.3470 150  TRP H NE1 
21457 C  CE2 . TRP H  152 ? 2.9903 1.9975 2.3764 0.1776  0.0914  -0.3671 150  TRP H CE2 
21458 C  CE3 . TRP H  152 ? 2.9244 1.9667 2.2635 0.2015  0.1308  -0.3429 150  TRP H CE3 
21459 C  CZ2 . TRP H  152 ? 2.8639 1.9003 2.2307 0.1912  0.1149  -0.4105 150  TRP H CZ2 
21460 C  CZ3 . TRP H  152 ? 2.8737 1.9449 2.1990 0.2155  0.1525  -0.3820 150  TRP H CZ3 
21461 C  CH2 . TRP H  152 ? 2.7988 1.8695 2.1356 0.2094  0.1451  -0.4153 150  TRP H CH2 
21462 N  N   . ARG H  153 ? 2.6707 1.6380 2.0431 0.1516  0.0594  -0.1927 151  ARG H N   
21463 C  CA  . ARG H  153 ? 2.7092 1.6844 2.0513 0.1319  0.0546  -0.1502 151  ARG H CA  
21464 C  C   . ARG H  153 ? 2.7016 1.7173 1.9729 0.1365  0.0930  -0.1508 151  ARG H C   
21465 O  O   . ARG H  153 ? 2.6388 1.6692 1.8932 0.1619  0.1213  -0.1817 151  ARG H O   
21466 C  CB  . ARG H  153 ? 2.6784 1.6273 2.0528 0.1374  0.0378  -0.1424 151  ARG H CB  
21467 C  CG  . ARG H  153 ? 2.7313 1.6899 2.0683 0.1118  0.0303  -0.0980 151  ARG H CG  
21468 C  CD  . ARG H  153 ? 2.9433 1.8783 2.3133 0.1210  0.0160  -0.0941 151  ARG H CD  
21469 N  NE  . ARG H  153 ? 3.2197 2.1615 2.5538 0.1007  0.0099  -0.0599 151  ARG H NE  
21470 C  CZ  . ARG H  153 ? 3.1832 2.1410 2.4672 0.1124  0.0372  -0.0717 151  ARG H CZ  
21471 N  NH1 . ARG H  153 ? 3.2779 2.2487 2.5456 0.1434  0.0712  -0.1116 151  ARG H NH1 
21472 N  NH2 . ARG H  153 ? 2.9709 1.9310 2.2239 0.0908  0.0274  -0.0422 151  ARG H NH2 
21473 N  N   . TYR H  154 ? 2.6915 1.7262 1.9260 0.1104  0.0920  -0.1154 152  TYR H N   
21474 C  CA  . TYR H  154 ? 2.6982 1.7697 1.8715 0.1115  0.1262  -0.1146 152  TYR H CA  
21475 C  C   . TYR H  154 ? 2.6281 1.6947 1.7831 0.1332  0.1440  -0.1328 152  TYR H C   
21476 O  O   . TYR H  154 ? 2.6124 1.6514 1.7937 0.1374  0.1259  -0.1313 152  TYR H O   
21477 C  CB  . TYR H  154 ? 2.9886 2.0791 2.1316 0.0763  0.1173  -0.0745 152  TYR H CB  
21478 C  CG  . TYR H  154 ? 3.2568 2.3868 2.3413 0.0768  0.1538  -0.0783 152  TYR H CG  
21479 C  CD1 . TYR H  154 ? 3.1994 2.3652 2.2708 0.0779  0.1764  -0.0822 152  TYR H CD1 
21480 C  CD2 . TYR H  154 ? 3.4131 2.5445 2.4597 0.0758  0.1650  -0.0786 152  TYR H CD2 
21481 C  CE1 . TYR H  154 ? 3.1656 2.3675 2.1948 0.0814  0.2108  -0.0888 152  TYR H CE1 
21482 C  CE2 . TYR H  154 ? 3.3046 2.4690 2.3033 0.0779  0.1990  -0.0883 152  TYR H CE2 
21483 C  CZ  . TYR H  154 ? 3.1751 2.3749 2.1684 0.0822  0.2227  -0.0943 152  TYR H CZ  
21484 O  OH  . TYR H  154 ? 3.0139 2.2468 1.9695 0.0872  0.2579  -0.1067 152  TYR H OH  
21485 N  N   . LEU H  155 ? 2.6390 1.7334 1.7556 0.1473  0.1783  -0.1487 153  LEU H N   
21486 C  CA  . LEU H  155 ? 2.5728 1.6658 1.6689 0.1654  0.1958  -0.1634 153  LEU H CA  
21487 C  C   . LEU H  155 ? 2.7068 1.8241 1.7513 0.1565  0.2187  -0.1568 153  LEU H C   
21488 O  O   . LEU H  155 ? 2.8482 1.9607 1.8664 0.1361  0.2101  -0.1389 153  LEU H O   
21489 C  CB  . LEU H  155 ? 2.4697 1.5710 1.5814 0.1953  0.2139  -0.1944 153  LEU H CB  
21490 C  CG  . LEU H  155 ? 2.4347 1.5162 1.5949 0.2077  0.1972  -0.2113 153  LEU H CG  
21491 C  CD1 . LEU H  155 ? 2.4290 1.5310 1.5941 0.2324  0.2181  -0.2404 153  LEU H CD1 
21492 C  CD2 . LEU H  155 ? 2.4463 1.4973 1.6299 0.2060  0.1751  -0.2018 153  LEU H CD2 
21493 N  N   . SER H  156 ? 2.6083 1.7539 1.6404 0.1700  0.2472  -0.1716 154  SER H N   
21494 C  CA  . SER H  156 ? 2.5511 1.7210 1.5439 0.1665  0.2729  -0.1728 154  SER H CA  
21495 C  C   . SER H  156 ? 2.5611 1.7682 1.5555 0.1637  0.2905  -0.1700 154  SER H C   
21496 O  O   . SER H  156 ? 2.5755 1.7873 1.5973 0.1624  0.2804  -0.1654 154  SER H O   
21497 C  CB  . SER H  156 ? 2.4732 1.6393 1.4585 0.1908  0.2921  -0.1946 154  SER H CB  
21498 O  OG  . SER H  156 ? 2.3869 1.5659 1.3999 0.2134  0.3032  -0.2086 154  SER H OG  
21499 N  N   . ASN H  157 ? 2.6465 1.8807 1.6132 0.1621  0.3168  -0.1740 155  ASN H N   
21500 C  CA  . ASN H  157 ? 2.6521 1.9283 1.6241 0.1616  0.3383  -0.1712 155  ASN H CA  
21501 C  C   . ASN H  157 ? 2.5881 1.8821 1.5538 0.1824  0.3717  -0.1929 155  ASN H C   
21502 O  O   . ASN H  157 ? 2.5634 1.8382 1.5085 0.1889  0.3774  -0.2078 155  ASN H O   
21503 C  CB  . ASN H  157 ? 2.8983 2.2008 1.8491 0.1295  0.3348  -0.1475 155  ASN H CB  
21504 C  CG  . ASN H  157 ? 3.1881 2.4954 2.0925 0.1142  0.3444  -0.1500 155  ASN H CG  
21505 O  OD1 . ASN H  157 ? 3.1935 2.5303 2.0784 0.1197  0.3765  -0.1663 155  ASN H OD1 
21506 N  ND2 . ASN H  157 ? 3.3896 2.6684 2.2786 0.0944  0.3162  -0.1353 155  ASN H ND2 
21507 N  N   . ARG H  158 ? 2.6878 2.0174 1.6769 0.1924  0.3917  -0.1938 156  ARG H N   
21508 C  CA  . ARG H  158 ? 2.8624 2.2093 1.8608 0.2142  0.4222  -0.2135 156  ARG H CA  
21509 C  C   . ARG H  158 ? 2.9260 2.3229 1.9490 0.2153  0.4439  -0.2060 156  ARG H C   
21510 O  O   . ARG H  158 ? 2.8096 2.2217 1.8586 0.2114  0.4331  -0.1887 156  ARG H O   
21511 C  CB  . ARG H  158 ? 3.0012 2.3271 2.0276 0.2397  0.4181  -0.2248 156  ARG H CB  
21512 C  CG  . ARG H  158 ? 3.1357 2.4674 2.1767 0.2616  0.4426  -0.2442 156  ARG H CG  
21513 C  CD  . ARG H  158 ? 3.2651 2.5689 2.3232 0.2797  0.4317  -0.2514 156  ARG H CD  
21514 N  NE  . ARG H  158 ? 3.2989 2.5641 2.3266 0.2711  0.4107  -0.2530 156  ARG H NE  
21515 C  CZ  . ARG H  158 ? 2.6982 1.9403 1.7358 0.2824  0.3982  -0.2563 156  ARG H CZ  
21516 N  NH1 . ARG H  158 ? 2.4086 1.6626 1.4829 0.3006  0.4030  -0.2570 156  ARG H NH1 
21517 N  NH2 . ARG H  158 ? 2.5423 1.7533 1.5568 0.2738  0.3795  -0.2554 156  ARG H NH2 
21518 N  N   . LEU H  159 ? 3.0785 2.5020 2.0943 0.2196  0.4744  -0.2205 157  LEU H N   
21519 C  CA  . LEU H  159 ? 2.9968 2.4727 2.0454 0.2254  0.5001  -0.2163 157  LEU H CA  
21520 C  C   . LEU H  159 ? 2.9638 2.4427 2.0662 0.2563  0.5112  -0.2256 157  LEU H C   
21521 O  O   . LEU H  159 ? 2.7545 2.1995 1.8612 0.2734  0.5078  -0.2421 157  LEU H O   
21522 C  CB  . LEU H  159 ? 3.0005 2.5096 2.0224 0.2173  0.5311  -0.2320 157  LEU H CB  
21523 C  CG  . LEU H  159 ? 3.2687 2.8437 2.3169 0.2141  0.5580  -0.2227 157  LEU H CG  
21524 C  CD1 . LEU H  159 ? 3.2743 2.8719 2.3157 0.1840  0.5359  -0.1842 157  LEU H CD1 
21525 C  CD2 . LEU H  159 ? 3.2844 2.8931 2.3061 0.2113  0.5949  -0.2502 157  LEU H CD2 
21526 N  N   . LEU H  160 ? 3.0308 2.5524 2.1782 0.2609  0.5212  -0.2101 158  LEU H N   
21527 C  CA  . LEU H  160 ? 2.9347 2.4660 2.1415 0.2846  0.5251  -0.2078 158  LEU H CA  
21528 C  C   . LEU H  160 ? 2.9460 2.5178 2.1982 0.3029  0.5605  -0.2190 158  LEU H C   
21529 O  O   . LEU H  160 ? 3.0799 2.6932 2.3291 0.2934  0.5811  -0.2168 158  LEU H O   
21530 C  CB  . LEU H  160 ? 2.8662 2.4147 2.0979 0.2745  0.5031  -0.1777 158  LEU H CB  
21531 C  CG  . LEU H  160 ? 2.7484 2.2580 1.9597 0.2676  0.4702  -0.1736 158  LEU H CG  
21532 C  CD1 . LEU H  160 ? 2.7306 2.2084 1.8886 0.2474  0.4534  -0.1764 158  LEU H CD1 
21533 C  CD2 . LEU H  160 ? 2.8083 2.3411 2.0492 0.2596  0.4532  -0.1504 158  LEU H CD2 
21534 N  N   . ALA H  161 ? 2.8110 2.3736 2.1119 0.3289  0.5665  -0.2295 159  ALA H N   
21535 C  CA  . ALA H  161 ? 2.7856 2.3770 2.1459 0.3526  0.5977  -0.2447 159  ALA H CA  
21536 C  C   . ALA H  161 ? 2.9497 2.5758 2.3898 0.3633  0.5925  -0.2149 159  ALA H C   
21537 O  O   . ALA H  161 ? 3.0745 2.6885 2.5236 0.3582  0.5633  -0.1913 159  ALA H O   
21538 C  CB  . ALA H  161 ? 2.7336 2.2831 2.0990 0.3736  0.6043  -0.2782 159  ALA H CB  
21539 N  N   . PRO H  162 ? 3.1098 2.7838 2.6115 0.3772  0.6206  -0.2151 160  PRO H N   
21540 C  CA  . PRO H  162 ? 3.1207 2.8332 2.7042 0.3842  0.6132  -0.1804 160  PRO H CA  
21541 C  C   . PRO H  162 ? 3.1079 2.7984 2.7511 0.4041  0.5984  -0.1754 160  PRO H C   
21542 O  O   . PRO H  162 ? 3.1988 2.9025 2.9189 0.4296  0.6171  -0.1852 160  PRO H O   
21543 C  CB  . PRO H  162 ? 3.0975 2.8661 2.7343 0.3967  0.6516  -0.1877 160  PRO H CB  
21544 C  CG  . PRO H  162 ? 3.0776 2.8270 2.6779 0.4077  0.6818  -0.2379 160  PRO H CG  
21545 C  CD  . PRO H  162 ? 3.1969 2.8985 2.6959 0.3844  0.6608  -0.2461 160  PRO H CD  
21546 N  N   . SER H  163 ? 2.8803 2.5404 2.4944 0.3923  0.5647  -0.1595 161  SER H N   
21547 C  CA  . SER H  163 ? 2.8100 2.4584 2.4794 0.4043  0.5453  -0.1449 161  SER H CA  
21548 C  C   . SER H  163 ? 2.8102 2.5077 2.5433 0.3961  0.5292  -0.0985 161  SER H C   
21549 O  O   . SER H  163 ? 2.9428 2.6565 2.6398 0.3711  0.5107  -0.0754 161  SER H O   
21550 C  CB  . SER H  163 ? 2.7917 2.3947 2.4007 0.3935  0.5184  -0.1485 161  SER H CB  
21551 O  OG  . SER H  163 ? 2.8725 2.4755 2.5338 0.3990  0.4963  -0.1260 161  SER H OG  
21552 N  N   . ASP H  164 ? 2.6902 2.4106 2.5213 0.4159  0.5345  -0.0849 162  ASP H N   
21553 C  CA  . ASP H  164 ? 2.6672 2.4367 2.5685 0.4066  0.5155  -0.0353 162  ASP H CA  
21554 C  C   . ASP H  164 ? 2.7770 2.5394 2.6738 0.3905  0.4770  -0.0057 162  ASP H C   
21555 O  O   . ASP H  164 ? 2.9799 2.7844 2.9113 0.3723  0.4551  0.0379  162  ASP H O   
21556 C  CB  . ASP H  164 ? 2.6497 2.4486 2.6697 0.4339  0.5333  -0.0282 162  ASP H CB  
21557 C  CG  . ASP H  164 ? 2.6998 2.5167 2.7284 0.4503  0.5762  -0.0603 162  ASP H CG  
21558 O  OD1 . ASP H  164 ? 2.7227 2.5828 2.7417 0.4355  0.5840  -0.0431 162  ASP H OD1 
21559 O  OD2 . ASP H  164 ? 2.6815 2.4719 2.7248 0.4762  0.6020  -0.1037 162  ASP H OD2 
21560 N  N   . SER H  165 ? 2.7468 2.4624 2.6011 0.3942  0.4682  -0.0272 163  SER H N   
21561 C  CA  . SER H  165 ? 2.7948 2.5067 2.6435 0.3799  0.4350  -0.0028 163  SER H CA  
21562 C  C   . SER H  165 ? 2.7286 2.4137 2.4714 0.3604  0.4248  -0.0205 163  SER H C   
21563 O  O   . SER H  165 ? 2.6480 2.3037 2.3273 0.3624  0.4419  -0.0544 163  SER H O   
21564 C  CB  . SER H  165 ? 2.9288 2.6108 2.8303 0.4015  0.4310  -0.0097 163  SER H CB  
21565 O  OG  . SER H  165 ? 3.0915 2.7198 2.9403 0.4167  0.4501  -0.0587 163  SER H OG  
21566 N  N   . PRO H  166 ? 2.6892 2.3882 2.4135 0.3398  0.3968  0.0027  164  PRO H N   
21567 C  CA  . PRO H  166 ? 2.7448 2.4186 2.3783 0.3248  0.3886  -0.0182 164  PRO H CA  
21568 C  C   . PRO H  166 ? 2.6960 2.3148 2.2958 0.3418  0.3976  -0.0531 164  PRO H C   
21569 O  O   . PRO H  166 ? 2.5187 2.1237 2.1603 0.3562  0.3939  -0.0504 164  PRO H O   
21570 C  CB  . PRO H  166 ? 2.6947 2.4045 2.3326 0.3021  0.3597  0.0139  164  PRO H CB  
21571 C  CG  . PRO H  166 ? 2.6938 2.4341 2.4260 0.3085  0.3497  0.0516  164  PRO H CG  
21572 C  CD  . PRO H  166 ? 2.6701 2.4155 2.4567 0.3263  0.3712  0.0504  164  PRO H CD  
21573 N  N   . GLU H  167 ? 2.9770 2.5641 2.5048 0.3386  0.4068  -0.0837 165  GLU H N   
21574 C  CA  . GLU H  167 ? 2.8884 2.4243 2.3776 0.3507  0.4146  -0.1159 165  GLU H CA  
21575 C  C   . GLU H  167 ? 2.9864 2.5037 2.4129 0.3372  0.3990  -0.1250 165  GLU H C   
21576 O  O   . GLU H  167 ? 3.0502 2.5854 2.4476 0.3195  0.3899  -0.1200 165  GLU H O   
21577 C  CB  . GLU H  167 ? 2.7852 2.3013 2.2495 0.3582  0.4397  -0.1430 165  GLU H CB  
21578 C  CG  . GLU H  167 ? 2.7909 2.2607 2.2342 0.3726  0.4509  -0.1743 165  GLU H CG  
21579 C  CD  . GLU H  167 ? 2.9128 2.3757 2.3310 0.3756  0.4771  -0.1993 165  GLU H CD  
21580 O  OE1 . GLU H  167 ? 2.7828 2.2796 2.2087 0.3686  0.4872  -0.1893 165  GLU H OE1 
21581 O  OE2 . GLU H  167 ? 2.9634 2.3904 2.3519 0.3821  0.4866  -0.2276 165  GLU H OE2 
21582 N  N   . TRP H  168 ? 2.7568 2.2382 2.1665 0.3457  0.3959  -0.1400 166  TRP H N   
21583 C  CA  . TRP H  168 ? 2.3903 1.8552 1.7520 0.3367  0.3825  -0.1487 166  TRP H CA  
21584 C  C   . TRP H  168 ? 2.2968 1.7130 1.6097 0.3410  0.3910  -0.1779 166  TRP H C   
21585 O  O   . TRP H  168 ? 2.6962 2.0838 2.0150 0.3534  0.3996  -0.1907 166  TRP H O   
21586 C  CB  . TRP H  168 ? 2.4533 1.9252 1.8417 0.3391  0.3670  -0.1332 166  TRP H CB  
21587 C  CG  . TRP H  168 ? 2.4714 1.9532 1.8257 0.3267  0.3530  -0.1332 166  TRP H CG  
21588 C  CD1 . TRP H  168 ? 2.7891 2.2378 2.1018 0.3281  0.3512  -0.1538 166  TRP H CD1 
21589 C  CD2 . TRP H  168 ? 2.4202 1.9534 1.7814 0.3101  0.3398  -0.1128 166  TRP H CD2 
21590 N  NE1 . TRP H  168 ? 2.8700 2.3464 2.1680 0.3167  0.3402  -0.1500 166  TRP H NE1 
21591 C  CE2 . TRP H  168 ? 2.6603 2.1900 1.9832 0.3044  0.3339  -0.1269 166  TRP H CE2 
21592 C  CE3 . TRP H  168 ? 2.4899 2.0754 1.8866 0.2975  0.3321  -0.0833 166  TRP H CE3 
21593 C  CZ2 . TRP H  168 ? 2.6610 2.2399 1.9759 0.2875  0.3241  -0.1179 166  TRP H CZ2 
21594 C  CZ3 . TRP H  168 ? 2.6738 2.3075 2.0579 0.2771  0.3192  -0.0708 166  TRP H CZ3 
21595 C  CH2 . TRP H  168 ? 2.6421 2.2733 1.9837 0.2725  0.3170  -0.0907 166  TRP H CH2 
21596 N  N   . LEU H  169 ? 2.2846 1.6916 1.5522 0.3292  0.3868  -0.1881 167  LEU H N   
21597 C  CA  . LEU H  169 ? 2.3018 1.6674 1.5258 0.3282  0.3906  -0.2088 167  LEU H CA  
21598 C  C   . LEU H  169 ? 2.4402 1.7839 1.6393 0.3256  0.3755  -0.2156 167  LEU H C   
21599 O  O   . LEU H  169 ? 2.7741 2.1379 1.9869 0.3250  0.3650  -0.2071 167  LEU H O   
21600 C  CB  . LEU H  169 ? 2.2784 1.6474 1.4795 0.3161  0.3953  -0.2117 167  LEU H CB  
21601 C  CG  . LEU H  169 ? 2.8475 2.2186 2.0529 0.3201  0.4160  -0.2164 167  LEU H CG  
21602 C  CD1 . LEU H  169 ? 2.7899 2.1230 1.9646 0.3236  0.4220  -0.2356 167  LEU H CD1 
21603 C  CD2 . LEU H  169 ? 3.1941 2.5949 2.4542 0.3334  0.4276  -0.2061 167  LEU H CD2 
21604 N  N   . SER H  170 ? 2.2935 1.6003 1.4577 0.3225  0.3744  -0.2293 168  SER H N   
21605 C  CA  . SER H  170 ? 2.2583 1.5426 1.4047 0.3207  0.3601  -0.2347 168  SER H CA  
21606 C  C   . SER H  170 ? 2.2728 1.5238 1.3846 0.3110  0.3566  -0.2434 168  SER H C   
21607 O  O   . SER H  170 ? 2.7207 1.9579 1.8154 0.3080  0.3661  -0.2476 168  SER H O   
21608 C  CB  . SER H  170 ? 2.2504 1.5221 1.4082 0.3302  0.3560  -0.2325 168  SER H CB  
21609 O  OG  . SER H  170 ? 2.4710 1.7136 1.6172 0.3334  0.3640  -0.2415 168  SER H OG  
21610 N  N   . PHE H  171 ? 2.1926 1.4339 1.2974 0.3050  0.3425  -0.2459 169  PHE H N   
21611 C  CA  . PHE H  171 ? 2.2289 1.4399 1.3107 0.2932  0.3326  -0.2476 169  PHE H CA  
21612 C  C   . PHE H  171 ? 2.3942 1.5825 1.4773 0.2953  0.3172  -0.2493 169  PHE H C   
21613 O  O   . PHE H  171 ? 2.5530 1.7532 1.6563 0.3009  0.3108  -0.2538 169  PHE H O   
21614 C  CB  . PHE H  171 ? 2.4402 1.6585 1.5248 0.2823  0.3267  -0.2465 169  PHE H CB  
21615 C  CG  . PHE H  171 ? 2.6549 1.8896 1.7322 0.2743  0.3388  -0.2399 169  PHE H CG  
21616 C  CD1 . PHE H  171 ? 2.5424 1.7640 1.5952 0.2599  0.3388  -0.2341 169  PHE H CD1 
21617 C  CD2 . PHE H  171 ? 2.6687 1.9379 1.7650 0.2789  0.3499  -0.2367 169  PHE H CD2 
21618 C  CE1 . PHE H  171 ? 2.3505 1.5953 1.3981 0.2520  0.3525  -0.2276 169  PHE H CE1 
21619 C  CE2 . PHE H  171 ? 2.8359 2.1248 1.9320 0.2724  0.3620  -0.2289 169  PHE H CE2 
21620 C  CZ  . PHE H  171 ? 2.5830 1.8610 1.6547 0.2597  0.3648  -0.2255 169  PHE H CZ  
21621 N  N   . ASP H  172 ? 2.5219 1.6812 1.5839 0.2891  0.3116  -0.2462 170  ASP H N   
21622 C  CA  . ASP H  172 ? 2.4647 1.6021 1.5308 0.2889  0.2949  -0.2431 170  ASP H CA  
21623 C  C   . ASP H  172 ? 2.3425 1.4690 1.4217 0.2813  0.2786  -0.2410 170  ASP H C   
21624 O  O   . ASP H  172 ? 2.3565 1.4628 1.4210 0.2649  0.2676  -0.2317 170  ASP H O   
21625 C  CB  . ASP H  172 ? 2.4368 1.5465 1.4737 0.2796  0.2907  -0.2387 170  ASP H CB  
21626 C  CG  . ASP H  172 ? 2.3170 1.4093 1.3634 0.2811  0.2739  -0.2321 170  ASP H CG  
21627 O  OD1 . ASP H  172 ? 2.3473 1.4245 1.4005 0.2723  0.2563  -0.2236 170  ASP H OD1 
21628 O  OD2 . ASP H  172 ? 2.2997 1.3948 1.3530 0.2907  0.2764  -0.2327 170  ASP H OD2 
21629 N  N   . VAL H  173 ? 2.5579 1.6996 1.6680 0.2920  0.2759  -0.2497 171  VAL H N   
21630 C  CA  . VAL H  173 ? 2.8504 1.9799 1.9856 0.2890  0.2605  -0.2537 171  VAL H CA  
21631 C  C   . VAL H  173 ? 2.8780 2.0016 2.0406 0.2984  0.2503  -0.2549 171  VAL H C   
21632 O  O   . VAL H  173 ? 2.8240 1.9553 2.0216 0.3070  0.2464  -0.2690 171  VAL H O   
21633 C  CB  . VAL H  173 ? 2.7454 1.8983 1.8970 0.2930  0.2668  -0.2699 171  VAL H CB  
21634 C  CG1 . VAL H  173 ? 2.5314 1.6867 1.6628 0.2801  0.2712  -0.2629 171  VAL H CG1 
21635 C  CG2 . VAL H  173 ? 2.5688 1.7609 1.7260 0.3060  0.2823  -0.2805 171  VAL H CG2 
21636 N  N   . THR H  174 ? 2.7648 1.8763 1.9135 0.2966  0.2465  -0.2418 172  THR H N   
21637 C  CA  . THR H  174 ? 2.3744 1.4845 1.5508 0.3044  0.2365  -0.2380 172  THR H CA  
21638 C  C   . THR H  174 ? 2.3310 1.4197 1.5429 0.3009  0.2165  -0.2347 172  THR H C   
21639 O  O   . THR H  174 ? 2.3140 1.4158 1.5697 0.3145  0.2150  -0.2459 172  THR H O   
21640 C  CB  . THR H  174 ? 2.6011 1.6954 1.7528 0.2979  0.2312  -0.2216 172  THR H CB  
21641 O  OG1 . THR H  174 ? 2.6585 1.7714 1.7918 0.3041  0.2478  -0.2257 172  THR H OG1 
21642 C  CG2 . THR H  174 ? 2.7023 1.7965 1.8855 0.3034  0.2181  -0.2123 172  THR H CG2 
21643 N  N   . GLY H  175 ? 2.5630 1.6221 1.7610 0.2818  0.2006  -0.2188 173  GLY H N   
21644 C  CA  . GLY H  175 ? 2.6834 1.7199 1.9237 0.2757  0.1762  -0.2092 173  GLY H CA  
21645 C  C   . GLY H  175 ? 2.5833 1.6271 1.8682 0.2883  0.1779  -0.2326 173  GLY H C   
21646 O  O   . GLY H  175 ? 2.4778 1.5089 1.8184 0.2939  0.1617  -0.2345 173  GLY H O   
21647 N  N   . VAL H  176 ? 2.6185 1.6828 1.8834 0.2925  0.1967  -0.2518 174  VAL H N   
21648 C  CA  . VAL H  176 ? 2.4816 1.5538 1.7815 0.3020  0.1989  -0.2787 174  VAL H CA  
21649 C  C   . VAL H  176 ? 2.3702 1.4736 1.6990 0.3242  0.2138  -0.3058 174  VAL H C   
21650 O  O   . VAL H  176 ? 2.3706 1.4716 1.7507 0.3352  0.2084  -0.3273 174  VAL H O   
21651 C  CB  . VAL H  176 ? 2.5049 1.5911 1.7706 0.2944  0.2114  -0.2856 174  VAL H CB  
21652 C  CG1 . VAL H  176 ? 2.4394 1.5363 1.7353 0.3025  0.2141  -0.3172 174  VAL H CG1 
21653 C  CG2 . VAL H  176 ? 2.7945 1.8571 2.0376 0.2712  0.1971  -0.2593 174  VAL H CG2 
21654 N  N   . VAL H  177 ? 2.3056 1.4417 1.6051 0.3303  0.2327  -0.3055 175  VAL H N   
21655 C  CA  . VAL H  177 ? 2.2659 1.4443 1.5863 0.3470  0.2486  -0.3275 175  VAL H CA  
21656 C  C   . VAL H  177 ? 2.2745 1.4482 1.6423 0.3576  0.2391  -0.3252 175  VAL H C   
21657 O  O   . VAL H  177 ? 2.2642 1.4651 1.6720 0.3725  0.2480  -0.3520 175  VAL H O   
21658 C  CB  . VAL H  177 ? 2.3895 1.6032 1.6722 0.3467  0.2650  -0.3175 175  VAL H CB  
21659 C  CG1 . VAL H  177 ? 2.2310 1.4985 1.5327 0.3587  0.2803  -0.3353 175  VAL H CG1 
21660 C  CG2 . VAL H  177 ? 2.5807 1.7996 1.8267 0.3369  0.2731  -0.3167 175  VAL H CG2 
21661 N  N   . ARG H  178 ? 2.4441 1.5872 1.8089 0.3492  0.2218  -0.2940 176  ARG H N   
21662 C  CA  . ARG H  178 ? 2.4982 1.6362 1.9133 0.3571  0.2092  -0.2854 176  ARG H CA  
21663 C  C   . ARG H  178 ? 2.5654 1.6856 2.0446 0.3650  0.1973  -0.3035 176  ARG H C   
21664 O  O   . ARG H  178 ? 2.3797 1.5190 1.9163 0.3826  0.2009  -0.3199 176  ARG H O   
21665 C  CB  . ARG H  178 ? 2.5345 1.6394 1.9297 0.3403  0.1882  -0.2463 176  ARG H CB  
21666 C  CG  . ARG H  178 ? 2.4625 1.5574 1.9136 0.3438  0.1687  -0.2293 176  ARG H CG  
21667 C  CD  . ARG H  178 ? 2.5073 1.5755 1.9271 0.3230  0.1484  -0.1904 176  ARG H CD  
21668 N  NE  . ARG H  178 ? 2.6930 1.7822 2.0738 0.3238  0.1609  -0.1847 176  ARG H NE  
21669 C  CZ  . ARG H  178 ? 2.8046 1.8880 2.1222 0.3132  0.1696  -0.1826 176  ARG H CZ  
21670 N  NH1 . ARG H  178 ? 2.9498 2.0125 2.2315 0.3007  0.1702  -0.1857 176  ARG H NH1 
21671 N  NH2 . ARG H  178 ? 2.6402 1.7400 1.9361 0.3151  0.1772  -0.1768 176  ARG H NH2 
21672 N  N   . GLN H  179 ? 2.7974 1.8827 2.2729 0.3524  0.1829  -0.3010 177  GLN H N   
21673 C  CA  . GLN H  179 ? 2.8484 1.9108 2.3913 0.3587  0.1676  -0.3179 177  GLN H CA  
21674 C  C   . GLN H  179 ? 2.5723 1.6656 2.1368 0.3777  0.1901  -0.3690 177  GLN H C   
21675 O  O   . GLN H  179 ? 2.6966 1.7847 2.3314 0.3930  0.1857  -0.3957 177  GLN H O   
21676 C  CB  . GLN H  179 ? 3.0133 2.0345 2.5446 0.3363  0.1442  -0.2979 177  GLN H CB  
21677 C  CG  . GLN H  179 ? 3.1168 2.1107 2.6261 0.3123  0.1198  -0.2486 177  GLN H CG  
21678 C  CD  . GLN H  179 ? 2.9642 1.9297 2.4573 0.2867  0.0992  -0.2275 177  GLN H CD  
21679 O  OE1 . GLN H  179 ? 2.8226 1.7832 2.3294 0.2881  0.0997  -0.2481 177  GLN H OE1 
21680 N  NE2 . GLN H  179 ? 2.9675 1.9176 2.4291 0.2607  0.0805  -0.1858 177  GLN H NE2 
21681 N  N   . TRP H  180 ? 2.4542 1.5815 1.9619 0.3758  0.2137  -0.3838 178  TRP H N   
21682 C  CA  . TRP H  180 ? 2.4355 1.6000 1.9518 0.3882  0.2356  -0.4314 178  TRP H CA  
21683 C  C   . TRP H  180 ? 2.4123 1.6271 1.9556 0.4071  0.2557  -0.4512 178  TRP H C   
21684 O  O   . TRP H  180 ? 2.6778 1.9214 2.2516 0.4204  0.2711  -0.4969 178  TRP H O   
21685 C  CB  . TRP H  180 ? 2.5998 1.7891 2.0484 0.3759  0.2508  -0.4331 178  TRP H CB  
21686 C  CG  . TRP H  180 ? 2.7749 1.9279 2.2070 0.3598  0.2362  -0.4275 178  TRP H CG  
21687 C  CD1 . TRP H  180 ? 3.0135 2.1162 2.4826 0.3534  0.2099  -0.4192 178  TRP H CD1 
21688 C  CD2 . TRP H  180 ? 2.6504 1.8187 2.0299 0.3463  0.2450  -0.4248 178  TRP H CD2 
21689 N  NE1 . TRP H  180 ? 3.0659 2.1534 2.5053 0.3358  0.2025  -0.4119 178  TRP H NE1 
21690 C  CE2 . TRP H  180 ? 2.8842 2.0115 2.2691 0.3322  0.2248  -0.4160 178  TRP H CE2 
21691 C  CE3 . TRP H  180 ? 2.4503 1.6653 1.7844 0.3433  0.2659  -0.4250 178  TRP H CE3 
21692 C  CZ2 . TRP H  180 ? 2.9633 2.0968 2.3087 0.3167  0.2272  -0.4093 178  TRP H CZ2 
21693 C  CZ3 . TRP H  180 ? 2.5198 1.7385 1.8183 0.3286  0.2672  -0.4180 178  TRP H CZ3 
21694 C  CH2 . TRP H  180 ? 2.8675 2.0466 2.1713 0.3162  0.2491  -0.4112 178  TRP H CH2 
21695 N  N   . LEU H  181 ? 2.3345 1.5622 1.8681 0.4072  0.2557  -0.4189 179  LEU H N   
21696 C  CA  . LEU H  181 ? 2.4986 1.7789 2.0609 0.4228  0.2729  -0.4304 179  LEU H CA  
21697 C  C   . LEU H  181 ? 2.8866 2.1517 2.5328 0.4393  0.2621  -0.4380 179  LEU H C   
21698 O  O   . LEU H  181 ? 3.0292 2.3428 2.7164 0.4567  0.2803  -0.4625 179  LEU H O   
21699 C  CB  . LEU H  181 ? 2.4444 1.7439 1.9663 0.4145  0.2740  -0.3901 179  LEU H CB  
21700 C  CG  . LEU H  181 ? 2.4253 1.7781 1.8935 0.4079  0.2947  -0.3908 179  LEU H CG  
21701 C  CD1 . LEU H  181 ? 2.3012 1.6408 1.7228 0.3957  0.2971  -0.3992 179  LEU H CD1 
21702 C  CD2 . LEU H  181 ? 2.5865 1.9428 2.0278 0.3997  0.2882  -0.3479 179  LEU H CD2 
21703 N  N   . SER H  182 ? 3.0454 2.2490 2.7222 0.4331  0.2324  -0.4164 180  SER H N   
21704 C  CA  . SER H  182 ? 3.0846 2.2687 2.8526 0.4472  0.2163  -0.4172 180  SER H CA  
21705 C  C   . SER H  182 ? 2.8218 2.0003 2.6530 0.4643  0.2214  -0.4705 180  SER H C   
21706 O  O   . SER H  182 ? 2.9171 2.1097 2.8309 0.4863  0.2256  -0.4934 180  SER H O   
21707 C  CB  . SER H  182 ? 3.2006 2.3242 2.9775 0.4285  0.1780  -0.3663 180  SER H CB  
21708 O  OG  . SER H  182 ? 3.3243 2.4053 3.0809 0.4130  0.1624  -0.3659 180  SER H OG  
21709 N  N   . ARG H  183 ? 2.6576 1.8166 2.4555 0.4549  0.2213  -0.4921 181  ARG H N   
21710 C  CA  . ARG H  183 ? 2.7390 1.8907 2.5894 0.4688  0.2260  -0.5481 181  ARG H CA  
21711 C  C   . ARG H  183 ? 3.0682 2.2872 2.8860 0.4785  0.2654  -0.6006 181  ARG H C   
21712 O  O   . ARG H  183 ? 2.8695 2.1282 2.6083 0.4662  0.2826  -0.5882 181  ARG H O   
21713 C  CB  . ARG H  183 ? 2.6384 1.7356 2.4715 0.4502  0.2024  -0.5431 181  ARG H CB  
21714 C  CG  . ARG H  183 ? 2.6823 1.7205 2.5381 0.4333  0.1621  -0.4870 181  ARG H CG  
21715 C  CD  . ARG H  183 ? 3.0101 2.0032 2.8526 0.4133  0.1393  -0.4816 181  ARG H CD  
21716 N  NE  . ARG H  183 ? 3.1681 2.1186 3.0102 0.3895  0.1033  -0.4199 181  ARG H NE  
21717 C  CZ  . ARG H  183 ? 3.2350 2.1868 2.9949 0.3651  0.1014  -0.3794 181  ARG H CZ  
21718 N  NH1 . ARG H  183 ? 3.2630 2.2521 2.9434 0.3638  0.1315  -0.3922 181  ARG H NH1 
21719 N  NH2 . ARG H  183 ? 3.1168 2.0360 2.8769 0.3411  0.0694  -0.3264 181  ARG H NH2 
21720 N  N   . GLY H  184 ? 3.5899 2.8229 3.4718 0.4993  0.2787  -0.6599 182  GLY H N   
21721 C  CA  . GLY H  184 ? 3.6064 2.9065 3.4553 0.5045  0.3155  -0.7151 182  GLY H CA  
21722 C  C   . GLY H  184 ? 3.5915 2.8738 3.3941 0.4887  0.3137  -0.7442 182  GLY H C   
21723 O  O   . GLY H  184 ? 3.4159 2.7342 3.2184 0.4945  0.3363  -0.8063 182  GLY H O   
21724 N  N   . GLY H  185 ? 3.6223 2.8511 3.3871 0.4676  0.2865  -0.7012 183  GLY H N   
21725 C  CA  . GLY H  185 ? 3.5027 2.7163 3.2211 0.4494  0.2821  -0.7189 183  GLY H CA  
21726 C  C   . GLY H  185 ? 3.2671 2.5495 2.9033 0.4369  0.3108  -0.7320 183  GLY H C   
21727 O  O   . GLY H  185 ? 2.7553 2.0582 2.3319 0.4236  0.3135  -0.6851 183  GLY H O   
21728 N  N   . GLU H  186 ? 3.4449 2.7624 3.0791 0.4391  0.3302  -0.7951 184  GLU H N   
21729 C  CA  . GLU H  186 ? 3.1612 2.5572 2.7253 0.4257  0.3583  -0.8124 184  GLU H CA  
21730 C  C   . GLU H  186 ? 2.9528 2.3429 2.4436 0.3971  0.3479  -0.7836 184  GLU H C   
21731 O  O   . GLU H  186 ? 2.6950 2.1494 2.1260 0.3813  0.3656  -0.7823 184  GLU H O   
21732 C  CB  . GLU H  186 ? 3.1279 2.5635 2.7166 0.4355  0.3817  -0.8944 184  GLU H CB  
21733 C  CG  . GLU H  186 ? 3.3482 2.8783 2.8694 0.4192  0.4126  -0.9219 184  GLU H CG  
21734 C  CD  . GLU H  186 ? 3.4405 2.9679 2.9055 0.3921  0.4059  -0.9410 184  GLU H CD  
21735 O  OE1 . GLU H  186 ? 3.3482 2.8043 2.8400 0.3913  0.3827  -0.9583 184  GLU H OE1 
21736 O  OE2 . GLU H  186 ? 3.5476 3.1467 2.9450 0.3697  0.4216  -0.9366 184  GLU H OE2 
21737 N  N   . ILE H  187 ? 2.9046 2.2244 2.4014 0.3885  0.3188  -0.7540 185  ILE H N   
21738 C  CA  . ILE H  187 ? 2.6587 1.9730 2.0956 0.3627  0.3088  -0.7259 185  ILE H CA  
21739 C  C   . ILE H  187 ? 2.6462 1.8997 2.0883 0.3571  0.2824  -0.6679 185  ILE H C   
21740 O  O   . ILE H  187 ? 2.6662 1.8613 2.1629 0.3645  0.2603  -0.6658 185  ILE H O   
21741 C  CB  . ILE H  187 ? 2.7295 2.0329 2.1629 0.3502  0.3028  -0.7739 185  ILE H CB  
21742 C  CG1 . ILE H  187 ? 2.6331 1.9314 2.0108 0.3227  0.2900  -0.7374 185  ILE H CG1 
21743 C  CG2 . ILE H  187 ? 2.7824 2.0161 2.2922 0.3635  0.2809  -0.8047 185  ILE H CG2 
21744 C  CD1 . ILE H  187 ? 2.6215 1.9892 1.9351 0.3089  0.3089  -0.7097 185  ILE H CD1 
21745 N  N   . GLU H  188 ? 2.6371 1.9080 2.0251 0.3433  0.2847  -0.6204 186  GLU H N   
21746 C  CA  . GLU H  188 ? 2.5316 1.7576 1.9116 0.3346  0.2650  -0.5675 186  GLU H CA  
21747 C  C   . GLU H  188 ? 2.6052 1.8490 1.9305 0.3134  0.2662  -0.5438 186  GLU H C   
21748 O  O   . GLU H  188 ? 2.8284 2.1147 2.1263 0.3042  0.2781  -0.5656 186  GLU H O   
21749 C  CB  . GLU H  188 ? 2.5638 1.7918 1.9448 0.3446  0.2687  -0.5312 186  GLU H CB  
21750 C  CG  . GLU H  188 ? 2.8512 2.0618 2.2932 0.3646  0.2645  -0.5465 186  GLU H CG  
21751 C  CD  . GLU H  188 ? 3.1160 2.2595 2.6078 0.3632  0.2342  -0.5352 186  GLU H CD  
21752 O  OE1 . GLU H  188 ? 3.2575 2.3700 2.7294 0.3450  0.2167  -0.5098 186  GLU H OE1 
21753 O  OE2 . GLU H  188 ? 3.1127 2.2382 2.6682 0.3793  0.2267  -0.5492 186  GLU H OE2 
21754 N  N   . GLY H  189 ? 2.5552 1.7707 1.8660 0.3042  0.2542  -0.4984 187  GLY H N   
21755 C  CA  . GLY H  189 ? 2.5741 1.8082 1.8423 0.2866  0.2566  -0.4728 187  GLY H CA  
21756 C  C   . GLY H  189 ? 2.5910 1.7895 1.8534 0.2776  0.2430  -0.4298 187  GLY H C   
21757 O  O   . GLY H  189 ? 2.5977 1.7554 1.8864 0.2808  0.2278  -0.4184 187  GLY H O   
21758 N  N   . PHE H  190 ? 2.3777 1.5968 1.6071 0.2646  0.2484  -0.4049 188  PHE H N   
21759 C  CA  . PHE H  190 ? 2.3402 1.5393 1.5578 0.2542  0.2413  -0.3662 188  PHE H CA  
21760 C  C   . PHE H  190 ? 2.6518 1.8541 1.8629 0.2348  0.2322  -0.3574 188  PHE H C   
21761 O  O   . PHE H  190 ? 3.0506 2.2699 2.2623 0.2284  0.2309  -0.3797 188  PHE H O   
21762 C  CB  . PHE H  190 ? 2.3024 1.5265 1.4922 0.2596  0.2599  -0.3409 188  PHE H CB  
21763 C  CG  . PHE H  190 ? 2.2558 1.4731 1.4505 0.2752  0.2651  -0.3415 188  PHE H CG  
21764 C  CD1 . PHE H  190 ? 2.2698 1.4525 1.4667 0.2744  0.2555  -0.3225 188  PHE H CD1 
21765 C  CD2 . PHE H  190 ? 2.2191 1.4692 1.4154 0.2872  0.2782  -0.3580 188  PHE H CD2 
21766 C  CE1 . PHE H  190 ? 2.2364 1.4130 1.4382 0.2863  0.2578  -0.3206 188  PHE H CE1 
21767 C  CE2 . PHE H  190 ? 2.1867 1.4331 1.3904 0.3000  0.2814  -0.3551 188  PHE H CE2 
21768 C  CZ  . PHE H  190 ? 2.1912 1.3987 1.3983 0.3000  0.2707  -0.3367 188  PHE H CZ  
21769 N  N   . ARG H  191 ? 2.6166 1.8066 1.8196 0.2231  0.2261  -0.3237 189  ARG H N   
21770 C  CA  . ARG H  191 ? 2.5598 1.7575 1.7586 0.2031  0.2177  -0.3066 189  ARG H CA  
21771 C  C   . ARG H  191 ? 2.5701 1.7886 1.7458 0.1985  0.2318  -0.2715 189  ARG H C   
21772 O  O   . ARG H  191 ? 2.5617 1.7660 1.7297 0.2020  0.2348  -0.2573 189  ARG H O   
21773 C  CB  . ARG H  191 ? 2.6440 1.7999 1.8715 0.1883  0.1875  -0.3038 189  ARG H CB  
21774 C  CG  . ARG H  191 ? 2.7421 1.9069 1.9665 0.1644  0.1762  -0.2770 189  ARG H CG  
21775 C  CD  . ARG H  191 ? 2.8729 1.9980 2.1253 0.1472  0.1450  -0.2578 189  ARG H CD  
21776 N  NE  . ARG H  191 ? 3.0194 2.1609 2.2668 0.1221  0.1355  -0.2238 189  ARG H NE  
21777 C  CZ  . ARG H  191 ? 3.1656 2.2858 2.4335 0.1001  0.1079  -0.1945 189  ARG H CZ  
21778 N  NH1 . ARG H  191 ? 3.1338 2.2119 2.4315 0.1000  0.0850  -0.1939 189  ARG H NH1 
21779 N  NH2 . ARG H  191 ? 3.2719 2.4165 2.5346 0.0765  0.1017  -0.1619 189  ARG H NH2 
21780 N  N   . LEU H  192 ? 2.5256 1.7796 1.6922 0.1900  0.2409  -0.2590 190  LEU H N   
21781 C  CA  . LEU H  192 ? 2.7221 2.0018 1.8747 0.1879  0.2579  -0.2303 190  LEU H CA  
21782 C  C   . LEU H  192 ? 3.0960 2.3895 2.2546 0.1660  0.2484  -0.2073 190  LEU H C   
21783 O  O   . LEU H  192 ? 3.2622 2.5835 2.4266 0.1588  0.2484  -0.2054 190  LEU H O   
21784 C  CB  . LEU H  192 ? 2.5805 1.8983 1.7275 0.2020  0.2809  -0.2315 190  LEU H CB  
21785 C  CG  . LEU H  192 ? 2.4962 1.8350 1.6369 0.2080  0.3024  -0.2108 190  LEU H CG  
21786 C  CD1 . LEU H  192 ? 2.3928 1.7427 1.5331 0.2278  0.3184  -0.2184 190  LEU H CD1 
21787 C  CD2 . LEU H  192 ? 2.6245 2.0020 1.7763 0.1971  0.3085  -0.1898 190  LEU H CD2 
21788 N  N   . SER H  193 ? 3.0772 2.3547 2.2350 0.1521  0.2378  -0.1869 191  SER H N   
21789 C  CA  . SER H  193 ? 3.0797 2.3789 2.2420 0.1298  0.2318  -0.1577 191  SER H CA  
21790 C  C   . SER H  193 ? 3.0638 2.3961 2.2093 0.1318  0.2582  -0.1373 191  SER H C   
21791 O  O   . SER H  193 ? 3.0104 2.3473 2.1428 0.1514  0.2805  -0.1486 191  SER H O   
21792 C  CB  . SER H  193 ? 3.1613 2.4262 2.3389 0.1079  0.1984  -0.1457 191  SER H CB  
21793 O  OG  . SER H  193 ? 3.2969 2.5374 2.4668 0.1076  0.1937  -0.1387 191  SER H OG  
21794 N  N   . ALA H  194 ? 3.1004 2.4571 2.2475 0.1108  0.2558  -0.1084 192  ALA H N   
21795 C  CA  . ALA H  194 ? 3.1230 2.5188 2.2557 0.1115  0.2842  -0.0934 192  ALA H CA  
21796 C  C   . ALA H  194 ? 3.0913 2.4830 2.2073 0.0885  0.2739  -0.0720 192  ALA H C   
21797 O  O   . ALA H  194 ? 3.0313 2.3839 2.1505 0.0753  0.2435  -0.0677 192  ALA H O   
21798 C  CB  . ALA H  194 ? 3.1667 2.6148 2.3180 0.1073  0.2986  -0.0760 192  ALA H CB  
21799 N  N   . HIS H  195 ? 2.9987 2.4351 2.1000 0.0827  0.2994  -0.0580 193  HIS H N   
21800 C  CA  . HIS H  195 ? 2.8907 2.3380 1.9689 0.0567  0.2939  -0.0357 193  HIS H CA  
21801 C  C   . HIS H  195 ? 3.0067 2.4638 2.1030 0.0228  0.2627  0.0005  193  HIS H C   
21802 O  O   . HIS H  195 ? 3.0648 2.5422 2.1874 0.0183  0.2578  0.0116  193  HIS H O   
21803 C  CB  . HIS H  195 ? 2.8678 2.3685 1.9247 0.0597  0.3343  -0.0367 193  HIS H CB  
21804 C  CG  . HIS H  195 ? 3.1432 2.6650 2.1672 0.0297  0.3323  -0.0159 193  HIS H CG  
21805 N  ND1 . HIS H  195 ? 3.1430 2.6269 2.1409 0.0186  0.3128  -0.0161 193  HIS H ND1 
21806 C  CD2 . HIS H  195 ? 3.3954 2.9784 2.4088 0.0052  0.3464  0.0084  193  HIS H CD2 
21807 C  CE1 . HIS H  195 ? 3.3569 2.8774 2.3262 -0.0136 0.3133  0.0084  193  HIS H CE1 
21808 N  NE2 . HIS H  195 ? 3.4172 2.9998 2.3935 -0.0223 0.3348  0.0224  193  HIS H NE2 
21809 N  N   . CYS H  196 ? 2.8717 2.3153 1.9560 -0.0038 0.2384  0.0226  194  CYS H N   
21810 C  CA  . CYS H  196 ? 2.9714 2.4217 2.0761 -0.0406 0.2028  0.0632  194  CYS H CA  
21811 C  C   . CYS H  196 ? 2.9649 2.4714 2.0407 -0.0711 0.2137  0.0957  194  CYS H C   
21812 O  O   . CYS H  196 ? 2.9479 2.4467 1.9944 -0.0821 0.2107  0.0993  194  CYS H O   
21813 C  CB  . CYS H  196 ? 3.0533 2.4377 2.1817 -0.0492 0.1565  0.0660  194  CYS H CB  
21814 S  SG  . CYS H  196 ? 3.2591 2.5801 2.4080 -0.0093 0.1531  0.0152  194  CYS H SG  
21815 N  N   . SER H  197 ? 3.1167 2.6844 2.2003 -0.0869 0.2262  0.1204  195  SER H N   
21816 C  CA  . SER H  197 ? 3.2841 2.9187 2.3423 -0.1202 0.2376  0.1538  195  SER H CA  
21817 C  C   . SER H  197 ? 3.3060 2.9333 2.3856 -0.1647 0.1854  0.2045  195  SER H C   
21818 O  O   . SER H  197 ? 3.2042 2.8335 2.3227 -0.1765 0.1619  0.2269  195  SER H O   
21819 C  CB  . SER H  197 ? 3.2836 2.9942 2.3480 -0.1148 0.2778  0.1569  195  SER H CB  
21820 O  OG  . SER H  197 ? 3.2660 3.0512 2.3029 -0.1458 0.2957  0.1838  195  SER H OG  
21821 N  N   . CYS H  198 ? 3.4770 3.0948 2.5346 -0.1912 0.1640  0.2249  196  CYS H N   
21822 C  CA  . CYS H  198 ? 3.4897 3.0894 2.5762 -0.2332 0.1070  0.2751  196  CYS H CA  
21823 C  C   . CYS H  198 ? 3.5295 3.1994 2.5801 -0.2802 0.1074  0.3203  196  CYS H C   
21824 O  O   . CYS H  198 ? 3.5238 3.2563 2.5261 -0.2779 0.1551  0.3062  196  CYS H O   
21825 C  CB  . CYS H  198 ? 3.5548 3.0657 2.6655 -0.2223 0.0683  0.2616  196  CYS H CB  
21826 S  SG  . CYS H  198 ? 3.7291 3.2236 2.7950 -0.2257 0.0716  0.2542  196  CYS H SG  
21827 N  N   . ASP H  199 ? 3.5739 3.2338 2.6513 -0.3243 0.0524  0.3743  197  ASP H N   
21828 C  CA  . ASP H  199 ? 3.6575 3.3932 2.7184 -0.3819 0.0376  0.4365  197  ASP H CA  
21829 C  C   . ASP H  199 ? 3.7260 3.5163 2.8160 -0.3974 0.0386  0.4661  197  ASP H C   
21830 O  O   . ASP H  199 ? 3.6640 3.4884 2.7776 -0.4468 -0.0009 0.5290  197  ASP H O   
21831 C  CB  . ASP H  199 ? 3.6128 3.4181 2.5984 -0.3930 0.0833  0.4269  197  ASP H CB  
21832 C  CG  . ASP H  199 ? 3.6019 3.4587 2.5657 -0.4576 0.0509  0.4908  197  ASP H CG  
21833 O  OD1 . ASP H  199 ? 3.5078 3.3238 2.5185 -0.4876 -0.0125 0.5384  197  ASP H OD1 
21834 O  OD2 . ASP H  199 ? 3.7007 3.6402 2.6024 -0.4798 0.0879  0.4932  197  ASP H OD2 
21835 N  N   . SER H  200 ? 3.7368 3.5390 2.8278 -0.3574 0.0821  0.4249  198  SER H N   
21836 C  CA  . SER H  200 ? 3.7751 3.5860 2.9133 -0.3560 0.0720  0.4386  198  SER H CA  
21837 C  C   . SER H  200 ? 3.6289 3.3713 2.7849 -0.3018 0.0859  0.3794  198  SER H C   
21838 O  O   . SER H  200 ? 3.5084 3.2405 2.6325 -0.2635 0.1275  0.3297  198  SER H O   
21839 C  CB  . SER H  200 ? 3.6966 3.6154 2.8212 -0.3680 0.1145  0.4571  198  SER H CB  
21840 O  OG  . SER H  200 ? 3.7880 3.7856 2.8665 -0.4030 0.1327  0.4837  198  SER H OG  
21841 N  N   . ARG H  201 ? 3.6477 3.3457 2.8542 -0.3012 0.0497  0.3854  199  ARG H N   
21842 C  CA  . ARG H  201 ? 3.5546 3.1738 2.7801 -0.2594 0.0462  0.3335  199  ARG H CA  
21843 C  C   . ARG H  201 ? 3.4665 3.1153 2.6902 -0.2271 0.0887  0.3029  199  ARG H C   
21844 O  O   . ARG H  201 ? 3.5720 3.2666 2.8182 -0.2428 0.0872  0.3303  199  ARG H O   
21845 C  CB  . ARG H  201 ? 3.6988 3.2502 2.9791 -0.2760 -0.0160 0.3484  199  ARG H CB  
21846 C  CG  . ARG H  201 ? 3.7309 3.2356 3.0273 -0.2993 -0.0616 0.3714  199  ARG H CG  
21847 C  CD  . ARG H  201 ? 3.8343 3.2442 3.1841 -0.2873 -0.1072 0.3478  199  ARG H CD  
21848 N  NE  . ARG H  201 ? 3.8208 3.1876 3.2053 -0.3133 -0.1584 0.3788  199  ARG H NE  
21849 C  CZ  . ARG H  201 ? 3.7713 3.0538 3.2107 -0.3038 -0.2004 0.3593  199  ARG H CZ  
21850 N  NH1 . ARG H  201 ? 3.6832 2.9180 3.1401 -0.2705 -0.1951 0.3054  199  ARG H NH1 
21851 N  NH2 . ARG H  201 ? 3.7584 3.0071 3.2378 -0.3288 -0.2479 0.3938  199  ARG H NH2 
21852 N  N   . ASP H  202 ? 3.1856 2.8086 2.3876 -0.1839 0.1229  0.2501  200  ASP H N   
21853 C  CA  . ASP H  202 ? 3.1504 2.7903 2.3571 -0.1503 0.1581  0.2190  200  ASP H CA  
21854 C  C   . ASP H  202 ? 3.1621 2.7335 2.3632 -0.1121 0.1615  0.1665  200  ASP H C   
21855 O  O   . ASP H  202 ? 3.2789 2.8079 2.4623 -0.1054 0.1548  0.1503  200  ASP H O   
21856 C  CB  . ASP H  202 ? 3.1090 2.8275 2.2917 -0.1391 0.2141  0.2164  200  ASP H CB  
21857 C  CG  . ASP H  202 ? 3.0958 2.8968 2.2920 -0.1721 0.2185  0.2648  200  ASP H CG  
21858 O  OD1 . ASP H  202 ? 3.2075 3.0103 2.4397 -0.1923 0.1870  0.2945  200  ASP H OD1 
21859 O  OD2 . ASP H  202 ? 3.0202 2.8871 2.1907 -0.1784 0.2543  0.2718  200  ASP H OD2 
21860 N  N   . ASN H  203 ? 3.1137 2.6800 2.3308 -0.0894 0.1717  0.1430  201  ASN H N   
21861 C  CA  . ASN H  203 ? 3.0364 2.5475 2.2503 -0.0567 0.1740  0.0960  201  ASN H CA  
21862 C  C   . ASN H  203 ? 3.0112 2.5475 2.2387 -0.0383 0.1934  0.0822  201  ASN H C   
21863 O  O   . ASN H  203 ? 3.1079 2.6881 2.3561 -0.0549 0.1914  0.1104  201  ASN H O   
21864 C  CB  . ASN H  203 ? 3.0909 2.5310 2.3248 -0.0660 0.1268  0.0866  201  ASN H CB  
21865 C  CG  . ASN H  203 ? 3.1563 2.5945 2.4237 -0.0916 0.0920  0.1079  201  ASN H CG  
21866 O  OD1 . ASN H  203 ? 3.2127 2.7047 2.4888 -0.1137 0.0941  0.1459  201  ASN H OD1 
21867 N  ND2 . ASN H  203 ? 3.1687 2.5470 2.4563 -0.0892 0.0605  0.0817  201  ASN H ND2 
21868 N  N   . THR H  204 ? 3.1122 2.6243 2.3299 -0.0060 0.2109  0.0425  202  THR H N   
21869 C  CA  . THR H  204 ? 3.0501 2.5729 2.2798 0.0120  0.2220  0.0244  202  THR H CA  
21870 C  C   . THR H  204 ? 3.0764 2.5940 2.2905 0.0467  0.2534  -0.0077 202  THR H C   
21871 O  O   . THR H  204 ? 3.2256 2.7444 2.4206 0.0574  0.2741  -0.0130 202  THR H O   
21872 C  CB  . THR H  204 ? 3.0747 2.6628 2.3283 0.0033  0.2357  0.0541  202  THR H CB  
21873 O  OG1 . THR H  204 ? 3.0826 2.7216 2.3344 -0.0011 0.2620  0.0780  202  THR H OG1 
21874 C  CG2 . THR H  204 ? 3.1813 2.7666 2.4570 -0.0267 0.1979  0.0756  202  THR H CG2 
21875 N  N   . LEU H  205 ? 3.0841 2.5983 2.3059 0.0612  0.2551  -0.0274 203  LEU H N   
21876 C  CA  . LEU H  205 ? 2.9878 2.5016 2.2023 0.0913  0.2804  -0.0524 203  LEU H CA  
21877 C  C   . LEU H  205 ? 2.9765 2.5382 2.2162 0.0985  0.2956  -0.0419 203  LEU H C   
21878 O  O   . LEU H  205 ? 3.0405 2.6145 2.2942 0.0825  0.2768  -0.0320 203  LEU H O   
21879 C  CB  . LEU H  205 ? 2.9384 2.4019 2.1391 0.1011  0.2647  -0.0863 203  LEU H CB  
21880 C  CG  . LEU H  205 ? 2.8021 2.2708 1.9993 0.1276  0.2851  -0.1076 203  LEU H CG  
21881 C  CD1 . LEU H  205 ? 2.7404 2.2116 1.9280 0.1466  0.3122  -0.1097 203  LEU H CD1 
21882 C  CD2 . LEU H  205 ? 2.7856 2.2145 1.9714 0.1330  0.2688  -0.1395 203  LEU H CD2 
21883 N  N   . GLN H  206 ? 2.9994 2.5871 2.2485 0.1213  0.3274  -0.0437 204  GLN H N   
21884 C  CA  . GLN H  206 ? 3.0184 2.6537 2.3038 0.1298  0.3417  -0.0291 204  GLN H CA  
21885 C  C   . GLN H  206 ? 3.0704 2.7011 2.3624 0.1559  0.3560  -0.0473 204  GLN H C   
21886 O  O   . GLN H  206 ? 3.0273 2.6977 2.3580 0.1660  0.3698  -0.0327 204  GLN H O   
21887 C  CB  . GLN H  206 ? 3.0901 2.7759 2.4030 0.1314  0.3675  -0.0056 204  GLN H CB  
21888 C  CG  . GLN H  206 ? 3.3124 3.0107 2.6185 0.1040  0.3559  0.0173  204  GLN H CG  
21889 C  CD  . GLN H  206 ? 3.4993 3.2517 2.8253 0.1072  0.3878  0.0341  204  GLN H CD  
21890 O  OE1 . GLN H  206 ? 3.5260 3.2953 2.8654 0.1329  0.4203  0.0199  204  GLN H OE1 
21891 N  NE2 . GLN H  206 ? 3.4808 3.2623 2.8109 0.0806  0.3786  0.0633  204  GLN H NE2 
21892 N  N   . VAL H  207 ? 3.0788 2.6645 2.3405 0.1662  0.3515  -0.0752 205  VAL H N   
21893 C  CA  . VAL H  207 ? 2.9516 2.5335 2.2201 0.1895  0.3641  -0.0894 205  VAL H CA  
21894 C  C   . VAL H  207 ? 3.0782 2.6742 2.3563 0.1838  0.3479  -0.0874 205  VAL H C   
21895 O  O   . VAL H  207 ? 3.1142 2.6945 2.3709 0.1673  0.3257  -0.0974 205  VAL H O   
21896 C  CB  . VAL H  207 ? 2.7104 2.2439 1.9443 0.2012  0.3656  -0.1164 205  VAL H CB  
21897 C  CG1 . VAL H  207 ? 2.6451 2.1750 1.8877 0.2221  0.3740  -0.1280 205  VAL H CG1 
21898 C  CG2 . VAL H  207 ? 2.7104 2.2383 1.9318 0.2036  0.3827  -0.1166 205  VAL H CG2 
21899 N  N   . ASP H  208 ? 3.0184 2.6456 2.3307 0.1963  0.3583  -0.0753 206  ASP H N   
21900 C  CA  . ASP H  208 ? 2.9444 2.5937 2.2656 0.1889  0.3437  -0.0691 206  ASP H CA  
21901 C  C   . ASP H  208 ? 2.7982 2.4265 2.1083 0.2064  0.3478  -0.0880 206  ASP H C   
21902 O  O   . ASP H  208 ? 2.7268 2.3622 2.0668 0.2254  0.3621  -0.0812 206  ASP H O   
21903 C  CB  . ASP H  208 ? 3.0749 2.7787 2.4504 0.1858  0.3462  -0.0333 206  ASP H CB  
21904 C  CG  . ASP H  208 ? 3.3734 3.1053 2.7544 0.1586  0.3300  -0.0120 206  ASP H CG  
21905 O  OD1 . ASP H  208 ? 3.4088 3.1192 2.7496 0.1392  0.3111  -0.0278 206  ASP H OD1 
21906 O  OD2 . ASP H  208 ? 3.5132 3.2881 2.9430 0.1565  0.3353  0.0201  206  ASP H OD2 
21907 N  N   . ILE H  209 ? 2.7997 2.4026 2.0713 0.1999  0.3347  -0.1124 207  ILE H N   
21908 C  CA  . ILE H  209 ? 2.8037 2.3937 2.0635 0.2120  0.3355  -0.1289 207  ILE H CA  
21909 C  C   . ILE H  209 ? 2.8519 2.4822 2.1133 0.1961  0.3216  -0.1216 207  ILE H C   
21910 O  O   . ILE H  209 ? 2.9541 2.6039 2.2062 0.1737  0.3082  -0.1193 207  ILE H O   
21911 C  CB  . ILE H  209 ? 2.5454 2.0859 1.7665 0.2161  0.3318  -0.1614 207  ILE H CB  
21912 C  CG1 . ILE H  209 ? 2.5377 2.0456 1.7507 0.2196  0.3386  -0.1635 207  ILE H CG1 
21913 C  CG2 . ILE H  209 ? 2.4924 2.0204 1.7080 0.2322  0.3363  -0.1739 207  ILE H CG2 
21914 C  CD1 . ILE H  209 ? 2.5380 2.0030 1.7226 0.2141  0.3261  -0.1864 207  ILE H CD1 
21915 N  N   . ASN H  210 ? 2.6250 2.2719 1.8990 0.2044  0.3234  -0.1154 208  ASN H N   
21916 C  CA  . ASN H  210 ? 2.4900 2.1821 1.7596 0.1855  0.3100  -0.1078 208  ASN H CA  
21917 C  C   . ASN H  210 ? 2.7963 2.4767 2.0195 0.1715  0.3016  -0.1432 208  ASN H C   
21918 O  O   . ASN H  210 ? 2.7959 2.4410 1.9962 0.1839  0.3060  -0.1736 208  ASN H O   
21919 C  CB  . ASN H  210 ? 2.4382 2.1443 1.7234 0.1963  0.3118  -0.0985 208  ASN H CB  
21920 C  CG  . ASN H  210 ? 2.5124 2.2835 1.8156 0.1742  0.2978  -0.0682 208  ASN H CG  
21921 O  OD1 . ASN H  210 ? 2.5550 2.3614 1.8769 0.1559  0.2888  -0.0428 208  ASN H OD1 
21922 N  ND2 . ASN H  210 ? 2.7562 2.5480 2.0538 0.1725  0.2940  -0.0674 208  ASN H ND2 
21923 N  N   . GLY H  211 ? 3.1232 2.8326 2.3365 0.1456  0.2886  -0.1401 209  GLY H N   
21924 C  CA  . GLY H  211 ? 3.1225 2.8219 2.2967 0.1306  0.2797  -0.1778 209  GLY H CA  
21925 C  C   . GLY H  211 ? 3.1147 2.8747 2.2741 0.1016  0.2681  -0.1740 209  GLY H C   
21926 O  O   . GLY H  211 ? 3.1433 2.9523 2.3188 0.0954  0.2670  -0.1443 209  GLY H O   
21927 N  N   . PHE H  212 ? 3.3128 3.0694 2.4418 0.0813  0.2573  -0.2044 210  PHE H N   
21928 C  CA  . PHE H  212 ? 3.5314 3.3456 2.6349 0.0488  0.2462  -0.2099 210  PHE H CA  
21929 C  C   . PHE H  212 ? 3.5417 3.3886 2.6537 0.0187  0.2286  -0.1768 210  PHE H C   
21930 O  O   . PHE H  212 ? 3.4548 3.3642 2.5547 -0.0116 0.2176  -0.1610 210  PHE H O   
21931 C  CB  . PHE H  212 ? 3.5849 3.3781 2.6489 0.0434  0.2456  -0.2719 210  PHE H CB  
21932 C  CG  . PHE H  212 ? 3.5931 3.3531 2.6549 0.0732  0.2617  -0.3051 210  PHE H CG  
21933 C  CD1 . PHE H  212 ? 3.4999 3.1916 2.5796 0.1012  0.2670  -0.3131 210  PHE H CD1 
21934 C  CD2 . PHE H  212 ? 3.4035 3.2061 2.4464 0.0707  0.2707  -0.3251 210  PHE H CD2 
21935 C  CE1 . PHE H  212 ? 3.5085 3.1717 2.5897 0.1263  0.2790  -0.3391 210  PHE H CE1 
21936 C  CE2 . PHE H  212 ? 3.2105 2.9865 2.2567 0.0977  0.2849  -0.3523 210  PHE H CE2 
21937 C  CZ  . PHE H  212 ? 3.3742 3.0785 2.4408 0.1257  0.2882  -0.3589 210  PHE H CZ  
21938 N  N   . THR H  213 ? 3.5212 3.3316 2.6536 0.0238  0.2248  -0.1641 211  THR H N   
21939 C  CA  . THR H  213 ? 3.4947 3.3311 2.6397 -0.0039 0.2073  -0.1322 211  THR H CA  
21940 C  C   . THR H  213 ? 3.4670 3.3178 2.5689 -0.0396 0.1885  -0.1634 211  THR H C   
21941 O  O   . THR H  213 ? 3.5010 3.3710 2.6065 -0.0679 0.1698  -0.1418 211  THR H O   
21942 C  CB  . THR H  213 ? 3.4013 3.2994 2.5860 -0.0125 0.2045  -0.0734 211  THR H CB  
21943 O  OG1 . THR H  213 ? 3.5256 3.4788 2.6886 -0.0331 0.1985  -0.0729 211  THR H OG1 
21944 C  CG2 . THR H  213 ? 3.2372 3.1178 2.4674 0.0243  0.2239  -0.0502 211  THR H CG2 
21945 N  N   . THR H  214 ? 3.4899 3.3357 2.5530 -0.0392 0.1939  -0.2146 212  THR H N   
21946 C  CA  . THR H  214 ? 3.6655 3.5171 2.6843 -0.0682 0.1809  -0.2615 212  THR H CA  
21947 C  C   . THR H  214 ? 3.7358 3.6663 2.7328 -0.1119 0.1655  -0.2384 212  THR H C   
21948 O  O   . THR H  214 ? 3.8777 3.8393 2.8296 -0.1343 0.1639  -0.2790 212  THR H O   
21949 C  CB  . THR H  214 ? 3.7547 3.5477 2.7765 -0.0733 0.1653  -0.2802 212  THR H CB  
21950 O  OG1 . THR H  214 ? 3.8063 3.5349 2.8554 -0.0371 0.1763  -0.2838 212  THR H OG1 
21951 C  CG2 . THR H  214 ? 3.6662 3.4439 2.6472 -0.0922 0.1557  -0.3466 212  THR H CG2 
21952 N  N   . GLY H  215 ? 3.6940 3.6616 2.7244 -0.1258 0.1543  -0.1738 213  GLY H N   
21953 C  CA  . GLY H  215 ? 3.7030 3.7415 2.7163 -0.1735 0.1326  -0.1465 213  GLY H CA  
21954 C  C   . GLY H  215 ? 3.7184 3.8367 2.7469 -0.1889 0.1303  -0.0950 213  GLY H C   
21955 O  O   . GLY H  215 ? 3.7693 3.9511 2.7847 -0.2335 0.1086  -0.0664 213  GLY H O   
21956 N  N   . ARG H  216 ? 3.4594 3.5777 2.5167 -0.1568 0.1486  -0.0798 214  ARG H N   
21957 C  CA  . ARG H  216 ? 3.2285 3.4212 2.3081 -0.1725 0.1425  -0.0274 214  ARG H CA  
21958 C  C   . ARG H  216 ? 3.0126 3.2627 2.0314 -0.2032 0.1414  -0.0584 214  ARG H C   
21959 O  O   . ARG H  216 ? 2.9845 3.2106 1.9710 -0.1832 0.1611  -0.1133 214  ARG H O   
21960 C  CB  . ARG H  216 ? 3.0495 3.2198 2.1825 -0.1291 0.1601  -0.0026 214  ARG H CB  
21961 C  CG  . ARG H  216 ? 3.0856 3.2013 2.2739 -0.0964 0.1672  0.0186  214  ARG H CG  
21962 C  CD  . ARG H  216 ? 3.1438 3.2967 2.3770 -0.1199 0.1473  0.0765  214  ARG H CD  
21963 N  NE  . ARG H  216 ? 3.1908 3.2991 2.4776 -0.0876 0.1586  0.0933  214  ARG H NE  
21964 C  CZ  . ARG H  216 ? 3.2561 3.3857 2.5900 -0.0991 0.1469  0.1382  214  ARG H CZ  
21965 N  NH1 . ARG H  216 ? 3.2223 3.4135 2.5571 -0.1434 0.1202  0.1740  214  ARG H NH1 
21966 N  NH2 . ARG H  216 ? 3.2844 3.3784 2.6646 -0.0682 0.1620  0.1480  214  ARG H NH2 
21967 N  N   . ARG H  217 ? 2.8033 3.1343 1.8078 -0.2533 0.1185  -0.0224 215  ARG H N   
21968 C  CA  . ARG H  217 ? 2.7669 3.1659 1.7068 -0.2906 0.1170  -0.0511 215  ARG H CA  
21969 C  C   . ARG H  217 ? 2.7694 3.2594 1.7322 -0.3174 0.1038  0.0161  215  ARG H C   
21970 O  O   . ARG H  217 ? 2.7320 3.2174 1.7656 -0.2940 0.1019  0.0733  215  ARG H O   
21971 C  CB  . ARG H  217 ? 2.7970 3.2175 1.6795 -0.3381 0.0987  -0.0804 215  ARG H CB  
21972 C  CG  . ARG H  217 ? 2.8304 3.1630 1.6919 -0.3172 0.1065  -0.1478 215  ARG H CG  
21973 C  CD  . ARG H  217 ? 2.8534 3.2109 1.6489 -0.3663 0.0898  -0.1907 215  ARG H CD  
21974 N  NE  . ARG H  217 ? 2.8902 3.2978 1.6960 -0.4130 0.0570  -0.1278 215  ARG H NE  
21975 C  CZ  . ARG H  217 ? 2.9476 3.3130 1.7773 -0.4175 0.0387  -0.1109 215  ARG H CZ  
21976 N  NH1 . ARG H  217 ? 2.9693 3.2424 1.8132 -0.3796 0.0492  -0.1512 215  ARG H NH1 
21977 N  NH2 . ARG H  217 ? 3.0326 3.4516 1.8753 -0.4619 0.0080  -0.0494 215  ARG H NH2 
21978 N  N   . GLY H  218 ? 2.9215 3.4959 1.8262 -0.3675 0.0942  0.0084  216  GLY H N   
21979 C  CA  . GLY H  218 ? 2.8223 3.4956 1.7437 -0.4045 0.0756  0.0773  216  GLY H CA  
21980 C  C   . GLY H  218 ? 2.7459 3.4495 1.6682 -0.3887 0.0928  0.0755  216  GLY H C   
21981 O  O   . GLY H  218 ? 2.7295 3.4029 1.6111 -0.3634 0.1210  0.0053  216  GLY H O   
21982 N  N   . ASP H  219 ? 2.6075 3.3723 1.5832 -0.4042 0.0737  0.1559  217  ASP H N   
21983 C  CA  . ASP H  219 ? 2.5583 3.3556 1.5435 -0.3923 0.0850  0.1654  217  ASP H CA  
21984 C  C   . ASP H  219 ? 2.5671 3.2715 1.6133 -0.3250 0.1047  0.1598  217  ASP H C   
21985 O  O   . ASP H  219 ? 2.5416 3.2305 1.5720 -0.2984 0.1274  0.1234  217  ASP H O   
21986 C  CB  . ASP H  219 ? 2.7820 3.6807 1.8068 -0.4383 0.0519  0.2584  217  ASP H CB  
21987 C  CG  . ASP H  219 ? 2.8724 3.8051 1.9176 -0.4275 0.0587  0.2786  217  ASP H CG  
21988 O  OD1 . ASP H  219 ? 3.0010 3.9372 1.9883 -0.4168 0.0865  0.2156  217  ASP H OD1 
21989 O  OD2 . ASP H  219 ? 2.7739 3.7269 1.9004 -0.4279 0.0356  0.3580  217  ASP H OD2 
21990 N  N   . LEU H  220 ? 2.5968 3.2424 1.7122 -0.2981 0.0967  0.1945  218  LEU H N   
21991 C  CA  . LEU H  220 ? 2.6127 3.1736 1.7850 -0.2379 0.1144  0.1905  218  LEU H CA  
21992 C  C   . LEU H  220 ? 2.7881 3.2567 1.9220 -0.1965 0.1441  0.1100  218  LEU H C   
21993 O  O   . LEU H  220 ? 2.8897 3.2890 2.0570 -0.1487 0.1610  0.0979  218  LEU H O   
21994 C  CB  . LEU H  220 ? 2.6750 3.2161 1.9388 -0.2258 0.0971  0.2555  218  LEU H CB  
21995 C  CG  . LEU H  220 ? 2.7372 3.2134 2.0757 -0.1724 0.1087  0.2702  218  LEU H CG  
21996 C  CD1 . LEU H  220 ? 2.6991 3.2027 2.0450 -0.1690 0.1093  0.2826  218  LEU H CD1 
21997 C  CD2 . LEU H  220 ? 2.7978 3.2804 2.2323 -0.1707 0.0883  0.3396  218  LEU H CD2 
21998 N  N   . ALA H  221 ? 2.8937 3.3598 1.9611 -0.2156 0.1484  0.0561  219  ALA H N   
21999 C  CA  . ALA H  221 ? 2.8557 3.2332 1.8959 -0.1791 0.1713  -0.0156 219  ALA H CA  
22000 C  C   . ALA H  221 ? 2.8871 3.2353 1.9150 -0.1443 0.1965  -0.0583 219  ALA H C   
22001 O  O   . ALA H  221 ? 2.8845 3.1491 1.9247 -0.1013 0.2132  -0.0913 219  ALA H O   
22002 C  CB  . ALA H  221 ? 2.7989 3.1858 1.7722 -0.2104 0.1681  -0.0678 219  ALA H CB  
22003 N  N   . THR H  222 ? 2.9715 3.3922 1.9751 -0.1649 0.1987  -0.0560 220  THR H N   
22004 C  CA  . THR H  222 ? 2.8777 3.2795 1.8714 -0.1346 0.2221  -0.0947 220  THR H CA  
22005 C  C   . THR H  222 ? 2.7812 3.1230 1.8375 -0.0905 0.2264  -0.0638 220  THR H C   
22006 O  O   . THR H  222 ? 2.7074 2.9847 1.7635 -0.0518 0.2459  -0.1045 220  THR H O   
22007 C  CB  . THR H  222 ? 2.7852 3.2906 1.7471 -0.1697 0.2218  -0.0867 220  THR H CB  
22008 O  OG1 . THR H  222 ? 2.7517 3.3245 1.7521 -0.2000 0.1955  -0.0033 220  THR H OG1 
22009 C  CG2 . THR H  222 ? 2.7956 3.3531 1.6839 -0.2082 0.2258  -0.1395 220  THR H CG2 
22010 N  N   . ILE H  223 ? 2.7057 3.0657 1.8195 -0.0962 0.2072  0.0070  221  ILE H N   
22011 C  CA  . ILE H  223 ? 2.5857 2.8884 1.7601 -0.0555 0.2110  0.0320  221  ILE H CA  
22012 C  C   . ILE H  223 ? 2.5442 2.7551 1.7372 -0.0205 0.2208  0.0112  221  ILE H C   
22013 O  O   . ILE H  223 ? 2.6488 2.7996 1.8764 0.0171  0.2305  0.0117  221  ILE H O   
22014 C  CB  . ILE H  223 ? 2.6356 2.9868 1.8761 -0.0712 0.1866  0.1123  221  ILE H CB  
22015 C  CG1 . ILE H  223 ? 2.8550 3.3145 2.0733 -0.1198 0.1703  0.1433  221  ILE H CG1 
22016 C  CG2 . ILE H  223 ? 2.6451 2.9470 1.9417 -0.0324 0.1911  0.1300  221  ILE H CG2 
22017 C  CD1 . ILE H  223 ? 2.8906 3.3973 2.1814 -0.1338 0.1438  0.2247  221  ILE H CD1 
22018 N  N   . HIS H  224 ? 2.5670 2.7666 1.7341 -0.0340 0.2183  -0.0094 222  HIS H N   
22019 C  CA  . HIS H  224 ? 2.6317 2.7516 1.8128 -0.0054 0.2269  -0.0282 222  HIS H CA  
22020 C  C   . HIS H  224 ? 2.5714 2.6236 1.7197 0.0249  0.2474  -0.0910 222  HIS H C   
22021 O  O   . HIS H  224 ? 2.5779 2.5656 1.7310 0.0452  0.2536  -0.1098 222  HIS H O   
22022 C  CB  . HIS H  224 ? 2.7861 2.9195 1.9540 -0.0334 0.2135  -0.0244 222  HIS H CB  
22023 C  CG  . HIS H  224 ? 2.8779 2.9685 2.0939 -0.0155 0.2124  0.0011  222  HIS H CG  
22024 N  ND1 . HIS H  224 ? 2.8843 2.9076 2.1287 0.0262  0.2291  -0.0080 222  HIS H ND1 
22025 C  CD2 . HIS H  224 ? 2.8229 2.9344 2.0635 -0.0356 0.1973  0.0357  222  HIS H CD2 
22026 C  CE1 . HIS H  224 ? 2.7967 2.8045 2.0800 0.0318  0.2269  0.0172  222  HIS H CE1 
22027 N  NE2 . HIS H  224 ? 2.8192 2.8791 2.1042 -0.0042 0.2076  0.0452  222  HIS H NE2 
22028 N  N   . GLY H  225 ? 2.5751 2.6447 1.6952 0.0271  0.2570  -0.1200 223  GLY H N   
22029 C  CA  . GLY H  225 ? 2.7166 2.7246 1.8184 0.0574  0.2747  -0.1732 223  GLY H CA  
22030 C  C   . GLY H  225 ? 2.5865 2.5670 1.7202 0.0877  0.2825  -0.1568 223  GLY H C   
22031 O  O   . GLY H  225 ? 2.6387 2.5622 1.7677 0.1155  0.2950  -0.1901 223  GLY H O   
22032 N  N   . MET H  226 ? 2.3232 2.3419 1.4939 0.0812  0.2725  -0.1032 224  MET H N   
22033 C  CA  . MET H  226 ? 2.3099 2.2978 1.5159 0.1085  0.2764  -0.0853 224  MET H CA  
22034 C  C   . MET H  226 ? 2.3154 2.2257 1.5471 0.1382  0.2827  -0.0870 224  MET H C   
22035 O  O   . MET H  226 ? 2.3319 2.2202 1.5598 0.1361  0.2829  -0.0940 224  MET H O   
22036 C  CB  . MET H  226 ? 2.3621 2.4081 1.6104 0.0928  0.2600  -0.0256 224  MET H CB  
22037 C  CG  . MET H  226 ? 2.4397 2.5441 1.6745 0.0787  0.2581  -0.0202 224  MET H CG  
22038 S  SD  . MET H  226 ? 2.3689 2.5262 1.6687 0.0642  0.2338  0.0573  224  MET H SD  
22039 C  CE  . MET H  226 ? 2.4223 2.6357 1.6968 0.0534  0.2370  0.0516  224  MET H CE  
22040 N  N   . ASN H  227 ? 2.3299 2.2011 1.5857 0.1642  0.2879  -0.0816 225  ASN H N   
22041 C  CA  . ASN H  227 ? 2.3834 2.1846 1.6590 0.1920  0.2964  -0.0868 225  ASN H CA  
22042 C  C   . ASN H  227 ? 2.2880 2.0381 1.5275 0.2010  0.3067  -0.1297 225  ASN H C   
22043 O  O   . ASN H  227 ? 2.2560 1.9572 1.5052 0.2172  0.3134  -0.1331 225  ASN H O   
22044 C  CB  . ASN H  227 ? 2.5402 2.3497 1.8640 0.1909  0.2907  -0.0486 225  ASN H CB  
22045 C  CG  . ASN H  227 ? 2.6362 2.4849 2.0124 0.1860  0.2772  -0.0020 225  ASN H CG  
22046 O  OD1 . ASN H  227 ? 2.8363 2.6923 2.2149 0.1886  0.2733  0.0027  225  ASN H OD1 
22047 N  ND2 . ASN H  227 ? 2.5035 2.3789 1.9285 0.1779  0.2678  0.0359  225  ASN H ND2 
22048 N  N   . ARG H  228 ? 2.5470 2.3091 1.7482 0.1899  0.3076  -0.1628 226  ARG H N   
22049 C  CA  . ARG H  228 ? 2.5157 2.2274 1.6922 0.1974  0.3128  -0.2012 226  ARG H CA  
22050 C  C   . ARG H  228 ? 2.4246 2.0781 1.6016 0.2234  0.3207  -0.2182 226  ARG H C   
22051 O  O   . ARG H  228 ? 2.5189 2.1783 1.7053 0.2328  0.3226  -0.2101 226  ARG H O   
22052 C  CB  . ARG H  228 ? 2.4128 2.1507 1.5560 0.1800  0.3112  -0.2370 226  ARG H CB  
22053 C  CG  . ARG H  228 ? 2.3964 2.1631 1.5272 0.1820  0.3173  -0.2575 226  ARG H CG  
22054 C  CD  . ARG H  228 ? 2.5311 2.3229 1.6305 0.1660  0.3191  -0.3019 226  ARG H CD  
22055 N  NE  . ARG H  228 ? 2.8061 2.6383 1.8947 0.1664  0.3287  -0.3247 226  ARG H NE  
22056 C  CZ  . ARG H  228 ? 2.6420 2.5557 1.7150 0.1419  0.3289  -0.3172 226  ARG H CZ  
22057 N  NH1 . ARG H  228 ? 2.5881 2.5487 1.6556 0.1138  0.3172  -0.2851 226  ARG H NH1 
22058 N  NH2 . ARG H  228 ? 2.4163 2.3700 1.4808 0.1434  0.3404  -0.3397 226  ARG H NH2 
22059 N  N   . PRO H  229 ? 2.4298 2.0287 1.5990 0.2326  0.3228  -0.2362 227  PRO H N   
22060 C  CA  . PRO H  229 ? 2.4032 1.9483 1.5701 0.2524  0.3270  -0.2509 227  PRO H CA  
22061 C  C   . PRO H  229 ? 2.3866 1.9389 1.5486 0.2593  0.3287  -0.2695 227  PRO H C   
22062 O  O   . PRO H  229 ? 2.6898 2.2654 1.8405 0.2517  0.3287  -0.2956 227  PRO H O   
22063 C  CB  . PRO H  229 ? 2.7392 2.2428 1.8945 0.2500  0.3233  -0.2715 227  PRO H CB  
22064 C  CG  . PRO H  229 ? 2.7692 2.2932 1.9297 0.2359  0.3207  -0.2518 227  PRO H CG  
22065 C  CD  . PRO H  229 ? 2.6470 2.2340 1.8132 0.2223  0.3188  -0.2355 227  PRO H CD  
22066 N  N   . PHE H  230 ? 2.2424 1.7775 1.4149 0.2732  0.3306  -0.2572 228  PHE H N   
22067 C  CA  . PHE H  230 ? 2.2143 1.7564 1.3879 0.2807  0.3318  -0.2687 228  PHE H CA  
22068 C  C   . PHE H  230 ? 2.1542 1.6381 1.3307 0.2967  0.3305  -0.2703 228  PHE H C   
22069 O  O   . PHE H  230 ? 2.1452 1.5945 1.3225 0.3013  0.3302  -0.2562 228  PHE H O   
22070 C  CB  . PHE H  230 ? 2.4317 2.0280 1.6184 0.2751  0.3305  -0.2425 228  PHE H CB  
22071 C  CG  . PHE H  230 ? 2.4861 2.0606 1.6929 0.2839  0.3269  -0.2120 228  PHE H CG  
22072 C  CD1 . PHE H  230 ? 2.2969 1.8703 1.5187 0.2814  0.3257  -0.1897 228  PHE H CD1 
22073 C  CD2 . PHE H  230 ? 2.5781 2.1333 1.7930 0.2948  0.3243  -0.2071 228  PHE H CD2 
22074 C  CE1 . PHE H  230 ? 2.2956 1.8469 1.5416 0.2914  0.3235  -0.1683 228  PHE H CE1 
22075 C  CE2 . PHE H  230 ? 2.5339 2.0650 1.7676 0.3021  0.3196  -0.1839 228  PHE H CE2 
22076 C  CZ  . PHE H  230 ? 2.3758 1.9037 1.6257 0.3013  0.3200  -0.1671 228  PHE H CZ  
22077 N  N   . LEU H  231 ? 2.0736 1.5519 1.2530 0.3041  0.3302  -0.2878 229  LEU H N   
22078 C  CA  . LEU H  231 ? 2.0624 1.4903 1.2458 0.3159  0.3257  -0.2878 229  LEU H CA  
22079 C  C   . LEU H  231 ? 2.1975 1.6426 1.3924 0.3208  0.3241  -0.2687 229  LEU H C   
22080 O  O   . LEU H  231 ? 2.4786 1.9632 1.6834 0.3213  0.3263  -0.2743 229  LEU H O   
22081 C  CB  . LEU H  231 ? 2.0796 1.4866 1.2697 0.3208  0.3230  -0.3169 229  LEU H CB  
22082 C  CG  . LEU H  231 ? 2.1765 1.5328 1.3752 0.3294  0.3142  -0.3143 229  LEU H CG  
22083 C  CD1 . LEU H  231 ? 2.2812 1.5915 1.4634 0.3250  0.3087  -0.2983 229  LEU H CD1 
22084 C  CD2 . LEU H  231 ? 2.2515 1.5933 1.4709 0.3345  0.3099  -0.3422 229  LEU H CD2 
22085 N  N   . LEU H  232 ? 2.1934 1.6123 1.3886 0.3234  0.3204  -0.2468 230  LEU H N   
22086 C  CA  . LEU H  232 ? 2.2061 1.6317 1.4149 0.3267  0.3146  -0.2267 230  LEU H CA  
22087 C  C   . LEU H  232 ? 2.1848 1.5750 1.3942 0.3336  0.3081  -0.2330 230  LEU H C   
22088 O  O   . LEU H  232 ? 2.1739 1.5135 1.3705 0.3354  0.3047  -0.2403 230  LEU H O   
22089 C  CB  . LEU H  232 ? 2.2862 1.6911 1.4999 0.3276  0.3122  -0.2065 230  LEU H CB  
22090 C  CG  . LEU H  232 ? 2.4045 1.8196 1.6398 0.3285  0.3027  -0.1821 230  LEU H CG  
22091 C  CD1 . LEU H  232 ? 2.4598 1.9455 1.7144 0.3193  0.3006  -0.1649 230  LEU H CD1 
22092 C  CD2 . LEU H  232 ? 2.3405 1.7240 1.5857 0.3322  0.3010  -0.1710 230  LEU H CD2 
22093 N  N   . LEU H  233 ? 2.2419 1.6637 1.4678 0.3352  0.3053  -0.2273 231  LEU H N   
22094 C  CA  . LEU H  233 ? 2.4712 1.8687 1.7062 0.3413  0.2981  -0.2298 231  LEU H CA  
22095 C  C   . LEU H  233 ? 2.5046 1.8991 1.7499 0.3402  0.2868  -0.2025 231  LEU H C   
22096 O  O   . LEU H  233 ? 2.7790 2.2143 2.0360 0.3354  0.2856  -0.1833 231  LEU H O   
22097 C  CB  . LEU H  233 ? 2.6753 2.1151 1.9288 0.3455  0.3053  -0.2495 231  LEU H CB  
22098 C  CG  . LEU H  233 ? 2.3690 1.8149 1.6176 0.3460  0.3150  -0.2815 231  LEU H CG  
22099 C  CD1 . LEU H  233 ? 2.2084 1.7040 1.4789 0.3512  0.3251  -0.3058 231  LEU H CD1 
22100 C  CD2 . LEU H  233 ? 2.1795 1.5595 1.4230 0.3487  0.3070  -0.2911 231  LEU H CD2 
22101 N  N   . MET H  234 ? 2.2683 1.6144 1.5107 0.3418  0.2754  -0.1981 232  MET H N   
22102 C  CA  . MET H  234 ? 2.3094 1.6457 1.5613 0.3391  0.2612  -0.1738 232  MET H CA  
22103 C  C   . MET H  234 ? 2.3168 1.6395 1.5820 0.3411  0.2514  -0.1722 232  MET H C   
22104 O  O   . MET H  234 ? 2.3052 1.5773 1.5566 0.3390  0.2435  -0.1771 232  MET H O   
22105 C  CB  . MET H  234 ? 2.5888 1.8731 1.8202 0.3352  0.2544  -0.1680 232  MET H CB  
22106 C  CG  . MET H  234 ? 2.6718 1.9684 1.9007 0.3356  0.2645  -0.1693 232  MET H CG  
22107 S  SD  . MET H  234 ? 3.0159 2.2520 2.2252 0.3347  0.2624  -0.1733 232  MET H SD  
22108 C  CE  . MET H  234 ? 2.9103 2.1775 2.1349 0.3380  0.2760  -0.1724 232  MET H CE  
22109 N  N   . ALA H  235 ? 2.4422 1.8152 1.7369 0.3434  0.2515  -0.1630 233  ALA H N   
22110 C  CA  . ALA H  235 ? 2.6718 2.0439 1.9916 0.3476  0.2446  -0.1613 233  ALA H CA  
22111 C  C   . ALA H  235 ? 2.8510 2.2464 2.1925 0.3426  0.2311  -0.1302 233  ALA H C   
22112 O  O   . ALA H  235 ? 3.0974 2.5134 2.4375 0.3357  0.2269  -0.1107 233  ALA H O   
22113 C  CB  . ALA H  235 ? 2.7939 2.2124 2.1385 0.3579  0.2616  -0.1873 233  ALA H CB  
22114 N  N   . THR H  236 ? 2.7170 2.1096 2.0856 0.3451  0.2216  -0.1223 234  THR H N   
22115 C  CA  . THR H  236 ? 2.5877 2.0047 1.9828 0.3395  0.2069  -0.0903 234  THR H CA  
22116 C  C   . THR H  236 ? 2.6005 2.1020 2.0360 0.3470  0.2225  -0.0924 234  THR H C   
22117 O  O   . THR H  236 ? 2.6468 2.1636 2.1047 0.3595  0.2362  -0.1179 234  THR H O   
22118 C  CB  . THR H  236 ? 2.5697 1.9345 1.9714 0.3347  0.1848  -0.0759 234  THR H CB  
22119 O  OG1 . THR H  236 ? 2.5629 1.8560 1.9207 0.3242  0.1718  -0.0762 234  THR H OG1 
22120 C  CG2 . THR H  236 ? 2.6491 2.0417 2.0816 0.3275  0.1678  -0.0404 234  THR H CG2 
22121 N  N   . PRO H  237 ? 2.7120 2.2718 2.1602 0.3389  0.2209  -0.0671 235  PRO H N   
22122 C  CA  . PRO H  237 ? 2.7802 2.4337 2.2623 0.3430  0.2391  -0.0699 235  PRO H CA  
22123 C  C   . PRO H  237 ? 2.8347 2.5017 2.3617 0.3535  0.2394  -0.0712 235  PRO H C   
22124 O  O   . PRO H  237 ? 2.8561 2.4713 2.3936 0.3511  0.2171  -0.0510 235  PRO H O   
22125 C  CB  . PRO H  237 ? 2.7407 2.4431 2.2292 0.3263  0.2270  -0.0285 235  PRO H CB  
22126 C  CG  . PRO H  237 ? 2.7860 2.4260 2.2406 0.3178  0.2118  -0.0192 235  PRO H CG  
22127 C  CD  . PRO H  237 ? 2.7678 2.3141 2.2016 0.3246  0.2030  -0.0362 235  PRO H CD  
22128 N  N   . LEU H  238 ? 2.7075 2.4478 2.2634 0.3645  0.2654  -0.0966 236  LEU H N   
22129 C  CA  . LEU H  238 ? 2.5734 2.3389 2.1853 0.3783  0.2707  -0.1024 236  LEU H CA  
22130 C  C   . LEU H  238 ? 2.6567 2.4697 2.3020 0.3687  0.2570  -0.0566 236  LEU H C   
22131 O  O   . LEU H  238 ? 2.6523 2.4611 2.3441 0.3759  0.2483  -0.0447 236  LEU H O   
22132 C  CB  . LEU H  238 ? 2.4865 2.3228 2.1215 0.3935  0.3059  -0.1493 236  LEU H CB  
22133 C  CG  . LEU H  238 ? 2.4113 2.2121 2.0236 0.4038  0.3212  -0.1996 236  LEU H CG  
22134 C  CD1 . LEU H  238 ? 2.3907 2.2112 1.9470 0.3895  0.3295  -0.2053 236  LEU H CD1 
22135 C  CD2 . LEU H  238 ? 2.5628 2.4130 2.2232 0.4242  0.3490  -0.2475 236  LEU H CD2 
22136 N  N   . GLU H  239 ? 2.8657 2.7256 2.4932 0.3510  0.2523  -0.0268 237  GLU H N   
22137 C  CA  . GLU H  239 ? 2.9474 2.8580 2.6083 0.3385  0.2368  0.0212  237  GLU H CA  
22138 C  C   . GLU H  239 ? 2.9718 2.7999 2.6364 0.3312  0.2002  0.0554  237  GLU H C   
22139 O  O   . GLU H  239 ? 3.0447 2.8999 2.7510 0.3266  0.1863  0.0887  237  GLU H O   
22140 C  CB  . GLU H  239 ? 2.9464 2.9168 2.5886 0.3172  0.2332  0.0510  237  GLU H CB  
22141 C  CG  . GLU H  239 ? 2.9191 2.9888 2.5550 0.3166  0.2670  0.0247  237  GLU H CG  
22142 C  CD  . GLU H  239 ? 3.0706 3.1010 2.6615 0.3229  0.2819  -0.0186 237  GLU H CD  
22143 O  OE1 . GLU H  239 ? 3.2310 3.1622 2.7947 0.3259  0.2654  -0.0224 237  GLU H OE1 
22144 O  OE2 . GLU H  239 ? 3.0331 3.1351 2.6147 0.3231  0.3103  -0.0492 237  GLU H OE2 
22145 N  N   . ARG H  240 ? 2.8293 2.5604 2.4503 0.3284  0.1846  0.0471  238  ARG H N   
22146 C  CA  . ARG H  240 ? 2.8305 2.4827 2.4451 0.3176  0.1501  0.0748  238  ARG H CA  
22147 C  C   . ARG H  240 ? 2.8513 2.4718 2.4953 0.3283  0.1464  0.0658  238  ARG H C   
22148 O  O   . ARG H  240 ? 2.9816 2.6148 2.6663 0.3236  0.1290  0.0970  238  ARG H O   
22149 C  CB  . ARG H  240 ? 2.8733 2.4415 2.4300 0.3095  0.1379  0.0657  238  ARG H CB  
22150 C  CG  . ARG H  240 ? 2.8863 2.4845 2.4225 0.3026  0.1443  0.0693  238  ARG H CG  
22151 C  CD  . ARG H  240 ? 2.8556 2.3708 2.3476 0.2949  0.1290  0.0655  238  ARG H CD  
22152 N  NE  . ARG H  240 ? 2.8083 2.3498 2.2872 0.2926  0.1390  0.0622  238  ARG H NE  
22153 C  CZ  . ARG H  240 ? 2.8651 2.4481 2.3635 0.2794  0.1259  0.0967  238  ARG H CZ  
22154 N  NH1 . ARG H  240 ? 2.8868 2.4902 2.4166 0.2673  0.1030  0.1360  238  ARG H NH1 
22155 N  NH2 . ARG H  240 ? 2.9337 2.5397 2.4245 0.2762  0.1331  0.0959  238  ARG H NH2 
22156 N  N   . ALA H  241 ? 2.6637 2.2454 2.2931 0.3415  0.1603  0.0267  239  ALA H N   
22157 C  CA  . ALA H  241 ? 2.6430 2.1923 2.3064 0.3511  0.1546  0.0187  239  ALA H CA  
22158 C  C   . ALA H  241 ? 2.7095 2.2045 2.3753 0.3333  0.1167  0.0588  239  ALA H C   
22159 O  O   . ALA H  241 ? 2.7401 2.1862 2.3572 0.3142  0.0957  0.0762  239  ALA H O   
22160 C  CB  . ALA H  241 ? 2.7250 2.3539 2.4596 0.3710  0.1777  0.0055  239  ALA H CB  
22161 N  N   . GLN H  242 ? 2.7964 2.3014 2.5218 0.3388  0.1075  0.0730  240  GLN H N   
22162 C  CA  . GLN H  242 ? 2.8590 2.3203 2.5930 0.3192  0.0692  0.1151  240  GLN H CA  
22163 C  C   . GLN H  242 ? 2.8375 2.2048 2.5048 0.3000  0.0465  0.1133  240  GLN H C   
22164 O  O   . GLN H  242 ? 2.8220 2.1562 2.4636 0.3068  0.0584  0.0817  240  GLN H O   
22165 C  CB  . GLN H  242 ? 2.8984 2.3941 2.6375 0.3035  0.0530  0.1558  240  GLN H CB  
22166 C  CG  . GLN H  242 ? 2.9745 2.4278 2.7211 0.2799  0.0109  0.2008  240  GLN H CG  
22167 C  CD  . GLN H  242 ? 3.0475 2.4180 2.7157 0.2546  -0.0147 0.2052  240  GLN H CD  
22168 O  OE1 . GLN H  242 ? 2.9359 2.2913 2.5537 0.2554  -0.0017 0.1820  240  GLN H OE1 
22169 N  NE2 . GLN H  242 ? 3.2224 2.5405 2.8817 0.2313  -0.0511 0.2335  240  GLN H NE2 
22170 N  N   . SER H  261 ? 2.4067 2.8071 2.8909 0.4537  -0.1783 0.9526  259  SER H N   
22171 C  CA  . SER H  261 ? 2.2379 2.6907 2.7361 0.4264  -0.1982 0.9848  259  SER H CA  
22172 C  C   . SER H  261 ? 2.2849 2.8369 2.7733 0.3336  -0.2732 1.0723  259  SER H C   
22173 O  O   . SER H  261 ? 2.2998 2.8694 2.7425 0.2808  -0.3143 1.0772  259  SER H O   
22174 C  CB  . SER H  261 ? 2.1245 2.6416 2.7588 0.4908  -0.1288 1.0495  259  SER H CB  
22175 O  OG  . SER H  261 ? 2.2197 2.8496 2.9766 0.5037  -0.1086 1.1683  259  SER H OG  
22176 N  N   . THR H  262 ? 2.4706 3.0867 2.9953 0.3086  -0.2910 1.1411  260  THR H N   
22177 C  CA  . THR H  262 ? 2.5205 3.2340 3.0262 0.2085  -0.3650 1.2287  260  THR H CA  
22178 C  C   . THR H  262 ? 2.6032 3.2074 2.9409 0.1397  -0.4217 1.1530  260  THR H C   
22179 O  O   . THR H  262 ? 2.6473 3.2917 2.9708 0.0867  -0.4573 1.2032  260  THR H O   
22180 C  CB  . THR H  262 ? 2.4985 3.3644 3.1503 0.2177  -0.3504 1.3640  260  THR H CB  
22181 O  OG1 . THR H  262 ? 2.6507 3.4560 3.3084 0.2693  -0.3125 1.3255  260  THR H OG1 
22182 C  CG2 . THR H  262 ? 2.2594 3.2360 3.0769 0.2850  -0.2901 1.4553  260  THR H CG2 
22183 N  N   . GLU H  263 ? 2.5786 3.0365 2.7864 0.1463  -0.4237 1.0301  261  GLU H N   
22184 C  CA  . GLU H  263 ? 2.6860 3.0182 2.7136 0.0824  -0.4716 0.9528  261  GLU H CA  
22185 C  C   . GLU H  263 ? 2.7369 3.0491 2.7266 0.0535  -0.4919 0.9650  261  GLU H C   
22186 O  O   . GLU H  263 ? 2.8142 3.0740 2.6734 -0.0340 -0.5455 0.9585  261  GLU H O   
22187 C  CB  . GLU H  263 ? 2.4820 2.8309 2.4203 -0.0197 -0.5318 0.9811  261  GLU H CB  
22188 C  CG  . GLU H  263 ? 2.4912 2.9653 2.4516 -0.1179 -0.5874 1.1023  261  GLU H CG  
22189 C  CD  . GLU H  263 ? 2.6296 3.1985 2.5820 -0.2067 -0.6346 1.1766  261  GLU H CD  
22190 O  OE1 . GLU H  263 ? 2.8618 3.3463 2.7044 -0.2363 -0.6480 1.1125  261  GLU H OE1 
22191 O  OE2 . GLU H  263 ? 2.5340 3.2765 2.5993 -0.2473 -0.6575 1.3098  261  GLU H OE2 
22192 N  N   . LYS H  264 ? 2.8693 3.2084 2.9607 0.1264  -0.4450 0.9766  262  LYS H N   
22193 C  CA  . LYS H  264 ? 2.9700 3.2666 3.0231 0.1197  -0.4523 0.9644  262  LYS H CA  
22194 C  C   . LYS H  264 ? 2.9169 3.0450 2.8554 0.1640  -0.4323 0.8333  262  LYS H C   
22195 O  O   . LYS H  264 ? 2.9151 2.9444 2.7183 0.1171  -0.4667 0.7886  262  LYS H O   
22196 C  CB  . LYS H  264 ? 2.8623 3.2639 3.0768 0.1802  -0.4052 1.0382  262  LYS H CB  
22197 C  CG  . LYS H  264 ? 2.7124 3.0942 2.9014 0.1659  -0.4161 1.0432  262  LYS H CG  
22198 C  CD  . LYS H  264 ? 2.5772 3.0077 2.9022 0.2533  -0.3476 1.0720  262  LYS H CD  
22199 C  CE  . LYS H  264 ? 2.5447 3.1282 3.0385 0.2856  -0.3110 1.1855  262  LYS H CE  
22200 N  NZ  . LYS H  264 ? 2.5113 3.2510 3.0574 0.2054  -0.3643 1.3177  262  LYS H NZ  
22201 N  N   . ASN H  265 ? 2.8693 2.9635 2.8576 0.2526  -0.3747 0.7750  263  ASN H N   
22202 C  CA  . ASN H  265 ? 2.8593 2.8161 2.7522 0.2973  -0.3545 0.6594  263  ASN H CA  
22203 C  C   . ASN H  265 ? 3.0474 2.9411 2.8603 0.2943  -0.3608 0.5963  263  ASN H C   
22204 O  O   . ASN H  265 ? 3.2738 3.2141 3.0820 0.2446  -0.3890 0.6368  263  ASN H O   
22205 C  CB  . ASN H  265 ? 2.7187 2.6757 2.6999 0.3851  -0.2896 0.6334  263  ASN H CB  
22206 C  CG  . ASN H  265 ? 2.5821 2.5727 2.6145 0.3902  -0.2811 0.6775  263  ASN H CG  
22207 O  OD1 . ASN H  265 ? 2.6788 2.6233 2.6300 0.3497  -0.3176 0.6676  263  ASN H OD1 
22208 N  ND2 . ASN H  265 ? 2.4483 2.5149 2.6118 0.4391  -0.2293 0.7296  263  ASN H ND2 
22209 N  N   . CYS H  266 ? 3.0101 2.8030 2.7587 0.3455  -0.3350 0.5003  264  CYS H N   
22210 C  CA  . CYS H  266 ? 2.9814 2.7130 2.6532 0.3508  -0.3353 0.4371  264  CYS H CA  
22211 C  C   . CYS H  266 ? 2.9213 2.7290 2.6957 0.3846  -0.3043 0.4556  264  CYS H C   
22212 O  O   . CYS H  266 ? 2.7875 2.5910 2.6130 0.4497  -0.2569 0.4179  264  CYS H O   
22213 C  CB  . CYS H  266 ? 2.9802 2.6017 2.5675 0.4003  -0.3141 0.3424  264  CYS H CB  
22214 S  SG  . CYS H  266 ? 3.0210 2.5845 2.5481 0.4411  -0.2923 0.2594  264  CYS H SG  
22215 N  N   . CYS H  267 ? 3.0053 2.8827 2.8061 0.3354  -0.3304 0.5171  265  CYS H N   
22216 C  CA  . CYS H  267 ? 2.9796 2.9295 2.8743 0.3611  -0.3038 0.5441  265  CYS H CA  
22217 C  C   . CYS H  267 ? 2.9790 2.9064 2.7950 0.3188  -0.3332 0.5226  265  CYS H C   
22218 O  O   . CYS H  267 ? 3.0759 2.9624 2.7846 0.2499  -0.3799 0.5228  265  CYS H O   
22219 C  CB  . CYS H  267 ? 3.0500 3.1312 3.0812 0.3501  -0.2996 0.6591  265  CYS H CB  
22220 S  SG  . CYS H  267 ? 3.0672 3.1790 3.2035 0.4082  -0.2508 0.6918  265  CYS H SG  
22221 N  N   . VAL H  268 ? 2.9185 2.8653 2.7796 0.3565  -0.3029 0.5034  266  VAL H N   
22222 C  CA  . VAL H  268 ? 2.9177 2.8436 2.7094 0.3245  -0.3237 0.4775  266  VAL H CA  
22223 C  C   . VAL H  268 ? 2.8897 2.9204 2.7382 0.2644  -0.3552 0.5739  266  VAL H C   
22224 O  O   . VAL H  268 ? 2.7699 2.9001 2.7518 0.2892  -0.3311 0.6448  266  VAL H O   
22225 C  CB  . VAL H  268 ? 2.8706 2.7750 2.6811 0.3868  -0.2798 0.4149  266  VAL H CB  
22226 C  CG1 . VAL H  268 ? 2.7861 2.7547 2.7324 0.4421  -0.2287 0.4504  266  VAL H CG1 
22227 C  CG2 . VAL H  268 ? 2.9484 2.8603 2.7186 0.3536  -0.2983 0.4091  266  VAL H CG2 
22228 N  N   . ARG H  269 ? 3.1014 3.1073 2.8437 0.1839  -0.4058 0.5800  267  ARG H N   
22229 C  CA  . ARG H  269 ? 3.2154 3.3238 2.9912 0.1086  -0.4463 0.6749  267  ARG H CA  
22230 C  C   . ARG H  269 ? 3.3497 3.4657 3.1075 0.0972  -0.4478 0.6591  267  ARG H C   
22231 O  O   . ARG H  269 ? 3.4387 3.4566 3.1072 0.1214  -0.4328 0.5677  267  ARG H O   
22232 C  CB  . ARG H  269 ? 3.2393 3.3150 2.8944 0.0079  -0.5046 0.6982  267  ARG H CB  
22233 C  CG  . ARG H  269 ? 3.1620 3.2239 2.8195 0.0096  -0.5084 0.7124  267  ARG H CG  
22234 C  CD  . ARG H  269 ? 3.2214 3.2410 2.7421 -0.1013 -0.5666 0.7347  267  ARG H CD  
22235 N  NE  . ARG H  269 ? 3.1581 3.3067 2.7156 -0.1928 -0.6135 0.8432  267  ARG H NE  
22236 C  CZ  . ARG H  269 ? 3.1739 3.3108 2.6143 -0.3117 -0.6705 0.8811  267  ARG H CZ  
22237 N  NH1 . ARG H  269 ? 3.3201 3.3055 2.5925 -0.3499 -0.6828 0.8151  267  ARG H NH1 
22238 N  NH2 . ARG H  269 ? 3.0913 3.3671 2.5779 -0.3960 -0.7140 0.9886  267  ARG H NH2 
22239 N  N   . GLN H  270 ? 3.2680 3.5094 3.1155 0.0607  -0.4654 0.7553  268  GLN H N   
22240 C  CA  . GLN H  270 ? 3.1562 3.4225 3.0027 0.0471  -0.4680 0.7546  268  GLN H CA  
22241 C  C   . GLN H  270 ? 3.2914 3.4941 2.9750 -0.0494 -0.5193 0.7290  268  GLN H C   
22242 O  O   . GLN H  270 ? 3.3460 3.5505 2.9583 -0.1345 -0.5658 0.7695  268  GLN H O   
22243 C  CB  . GLN H  270 ? 3.0917 3.5193 3.0953 0.0433  -0.4668 0.8765  268  GLN H CB  
22244 C  CG  . GLN H  270 ? 3.1937 3.6602 3.2127 0.0316  -0.4679 0.8871  268  GLN H CG  
22245 C  CD  . GLN H  270 ? 3.1898 3.8223 3.3635 0.0238  -0.4690 1.0222  268  GLN H CD  
22246 O  OE1 . GLN H  270 ? 3.1868 3.9091 3.4669 0.0373  -0.4616 1.1095  268  GLN H OE1 
22247 N  NE2 . GLN H  270 ? 3.0852 3.7628 3.2744 0.0044  -0.4758 1.0446  268  GLN H NE2 
22248 N  N   . LEU H  271 ? 3.1500 3.2919 2.7674 -0.0399 -0.5084 0.6622  269  LEU H N   
22249 C  CA  . LEU H  271 ? 3.2575 3.3225 2.7097 -0.1268 -0.5461 0.6308  269  LEU H CA  
22250 C  C   . LEU H  271 ? 3.2679 3.3310 2.7166 -0.1076 -0.5295 0.5949  269  LEU H C   
22251 O  O   . LEU H  271 ? 3.3032 3.2985 2.7420 -0.0303 -0.4868 0.5112  269  LEU H O   
22252 C  CB  . LEU H  271 ? 3.2773 3.1778 2.5674 -0.1277 -0.5409 0.5387  269  LEU H CB  
22253 C  CG  . LEU H  271 ? 3.4143 3.1979 2.5090 -0.2087 -0.5643 0.4931  269  LEU H CG  
22254 C  CD1 . LEU H  271 ? 3.5076 3.3519 2.5565 -0.3383 -0.6245 0.5813  269  LEU H CD1 
22255 C  CD2 . LEU H  271 ? 3.5487 3.1614 2.4935 -0.1908 -0.5452 0.4060  269  LEU H CD2 
22256 N  N   . TYR H  272 ? 3.2363 3.3798 2.6917 -0.1818 -0.5648 0.6613  270  TYR H N   
22257 C  CA  . TYR H  272 ? 3.2048 3.3540 2.6535 -0.1760 -0.5547 0.6360  270  TYR H CA  
22258 C  C   . TYR H  272 ? 3.3905 3.4261 2.6424 -0.2572 -0.5808 0.5816  270  TYR H C   
22259 O  O   . TYR H  272 ? 3.5575 3.5955 2.7222 -0.3647 -0.6289 0.6291  270  TYR H O   
22260 C  CB  . TYR H  272 ? 3.0520 3.3647 2.6397 -0.2004 -0.5717 0.7477  270  TYR H CB  
22261 C  CG  . TYR H  272 ? 3.0177 3.3404 2.5857 -0.2139 -0.5709 0.7311  270  TYR H CG  
22262 C  CD1 . TYR H  272 ? 2.9158 3.2201 2.5403 -0.1242 -0.5210 0.6743  270  TYR H CD1 
22263 C  CD2 . TYR H  272 ? 3.0850 3.4366 2.5723 -0.3233 -0.6210 0.7742  270  TYR H CD2 
22264 C  CE1 . TYR H  272 ? 2.9314 3.2472 2.5379 -0.1379 -0.5207 0.6603  270  TYR H CE1 
22265 C  CE2 . TYR H  272 ? 3.0874 3.4491 2.5558 -0.3372 -0.6204 0.7598  270  TYR H CE2 
22266 C  CZ  . TYR H  272 ? 3.0248 3.3695 2.5561 -0.2418 -0.5700 0.7028  270  TYR H CZ  
22267 O  OH  . TYR H  272 ? 3.1292 3.4860 2.6409 -0.2577 -0.5702 0.6896  270  TYR H OH  
22268 N  N   . ILE H  273 ? 3.3351 3.2722 2.5129 -0.2097 -0.5467 0.4858  271  ILE H N   
22269 C  CA  . ILE H  273 ? 3.3949 3.1989 2.3763 -0.2685 -0.5544 0.4219  271  ILE H CA  
22270 C  C   . ILE H  273 ? 3.3092 3.1467 2.2892 -0.2831 -0.5532 0.4168  271  ILE H C   
22271 O  O   . ILE H  273 ? 3.2226 3.0890 2.2873 -0.1998 -0.5164 0.3832  271  ILE H O   
22272 C  CB  . ILE H  273 ? 3.4185 3.0707 2.2996 -0.1989 -0.5106 0.3166  271  ILE H CB  
22273 C  CG1 . ILE H  273 ? 3.4812 3.0876 2.3390 -0.2011 -0.5173 0.3234  271  ILE H CG1 
22274 C  CG2 . ILE H  273 ? 3.5448 3.0559 2.2302 -0.2433 -0.5029 0.2509  271  ILE H CG2 
22275 C  CD1 . ILE H  273 ? 3.6078 3.0602 2.3532 -0.1423 -0.4772 0.2301  271  ILE H CD1 
22276 N  N   . ASP H  274 ? 3.6217 3.4530 2.4971 -0.3952 -0.5940 0.4499  272  ASP H N   
22277 C  CA  . ASP H  274 ? 3.7461 3.5929 2.5888 -0.4261 -0.5971 0.4422  272  ASP H CA  
22278 C  C   . ASP H  274 ? 3.8476 3.5152 2.4761 -0.4527 -0.5773 0.3481  272  ASP H C   
22279 O  O   . ASP H  274 ? 3.9679 3.5123 2.4454 -0.5036 -0.5831 0.3229  272  ASP H O   
22280 C  CB  . ASP H  274 ? 3.8046 3.7755 2.6767 -0.5385 -0.6554 0.5509  272  ASP H CB  
22281 C  CG  . ASP H  274 ? 3.6560 3.6879 2.5544 -0.5532 -0.6580 0.5622  272  ASP H CG  
22282 O  OD1 . ASP H  274 ? 3.6203 3.5513 2.4253 -0.5246 -0.6260 0.4747  272  ASP H OD1 
22283 O  OD2 . ASP H  274 ? 3.5151 3.7011 2.5306 -0.5926 -0.6909 0.6640  272  ASP H OD2 
22284 N  N   . PHE H  275 ? 3.6933 3.3413 2.3055 -0.4162 -0.5489 0.2974  273  PHE H N   
22285 C  CA  . PHE H  275 ? 3.7375 3.2158 2.1540 -0.4266 -0.5181 0.2093  273  PHE H CA  
22286 C  C   . PHE H  275 ? 3.8516 3.2732 2.1011 -0.5657 -0.5543 0.2314  273  PHE H C   
22287 O  O   . PHE H  275 ? 4.0169 3.2698 2.0664 -0.6145 -0.5411 0.1827  273  PHE H O   
22288 C  CB  . PHE H  275 ? 3.7604 3.2459 2.2204 -0.3375 -0.4731 0.1506  273  PHE H CB  
22289 C  CG  . PHE H  275 ? 3.6993 3.2158 2.2851 -0.2107 -0.4332 0.1170  273  PHE H CG  
22290 C  CD1 . PHE H  275 ? 3.8088 3.2046 2.3134 -0.1446 -0.3896 0.0441  273  PHE H CD1 
22291 C  CD2 . PHE H  275 ? 3.5893 3.2518 2.3685 -0.1602 -0.4365 0.1617  273  PHE H CD2 
22292 C  CE1 . PHE H  275 ? 3.7382 3.1717 2.3547 -0.0372 -0.3568 0.0179  273  PHE H CE1 
22293 C  CE2 . PHE H  275 ? 3.5587 3.2416 2.4372 -0.0555 -0.3993 0.1295  273  PHE H CE2 
22294 C  CZ  . PHE H  275 ? 3.6298 3.2050 2.4284 0.0025  -0.3630 0.0585  273  PHE H CZ  
22295 N  N   . ARG H  276 ? 3.8289 3.3839 2.1501 -0.6335 -0.5972 0.3063  274  ARG H N   
22296 C  CA  . ARG H  276 ? 3.9451 3.4607 2.1081 -0.7781 -0.6369 0.3347  274  ARG H CA  
22297 C  C   . ARG H  276 ? 4.1078 3.6167 2.2012 -0.8862 -0.6853 0.3956  274  ARG H C   
22298 O  O   . ARG H  276 ? 4.3038 3.7062 2.1958 -1.0105 -0.7063 0.3910  274  ARG H O   
22299 C  CB  . ARG H  276 ? 3.8173 3.4930 2.0884 -0.8170 -0.6701 0.4045  274  ARG H CB  
22300 C  CG  . ARG H  276 ? 3.6897 3.3625 1.9981 -0.7343 -0.6269 0.3443  274  ARG H CG  
22301 C  CD  . ARG H  276 ? 3.8029 3.3204 1.8925 -0.7915 -0.6063 0.2727  274  ARG H CD  
22302 N  NE  . ARG H  276 ? 3.8140 3.3766 1.8288 -0.9321 -0.6579 0.3339  274  ARG H NE  
22303 C  CZ  . ARG H  276 ? 3.9325 3.4148 1.7716 -1.0677 -0.6922 0.3553  274  ARG H CZ  
22304 N  NH1 . ARG H  276 ? 4.1094 3.4519 1.8267 -1.0771 -0.6774 0.3177  274  ARG H NH1 
22305 N  NH2 . ARG H  276 ? 3.9363 3.4759 1.7146 -1.1993 -0.7415 0.4158  274  ARG H NH2 
22306 N  N   . LYS H  277 ? 4.1174 3.7337 2.3654 -0.8459 -0.7014 0.4530  275  LYS H N   
22307 C  CA  . LYS H  277 ? 4.2539 3.8999 2.4643 -0.9493 -0.7527 0.5270  275  LYS H CA  
22308 C  C   . LYS H  277 ? 4.3558 3.8317 2.4347 -0.9350 -0.7279 0.4626  275  LYS H C   
22309 O  O   . LYS H  277 ? 4.5289 3.9091 2.4301 -1.0547 -0.7557 0.4717  275  LYS H O   
22310 C  CB  . LYS H  277 ? 3.9614 3.8299 2.4172 -0.9174 -0.7829 0.6386  275  LYS H CB  
22311 C  CG  . LYS H  277 ? 3.8482 3.7854 2.2963 -1.0197 -0.8384 0.7320  275  LYS H CG  
22312 C  CD  . LYS H  277 ? 3.8778 3.8487 2.2013 -1.1917 -0.8996 0.7990  275  LYS H CD  
22313 C  CE  . LYS H  277 ? 3.8755 3.9474 2.2094 -1.2987 -0.9599 0.9073  275  LYS H CE  
22314 N  NZ  . LYS H  277 ? 4.1033 4.0171 2.3065 -1.3039 -0.9462 0.8485  275  LYS H NZ  
22315 N  N   . ASP H  278 ? 4.1193 3.5525 2.2742 -0.7962 -0.6758 0.3989  276  ASP H N   
22316 C  CA  . ASP H  278 ? 4.1994 3.4893 2.2573 -0.7690 -0.6512 0.3464  276  ASP H CA  
22317 C  C   . ASP H  278 ? 4.4009 3.4783 2.2855 -0.7175 -0.5880 0.2303  276  ASP H C   
22318 O  O   . ASP H  278 ? 4.6373 3.5745 2.4204 -0.6937 -0.5607 0.1828  276  ASP H O   
22319 C  CB  . ASP H  278 ? 3.9239 3.3161 2.1840 -0.6545 -0.6376 0.3652  276  ASP H CB  
22320 C  CG  . ASP H  278 ? 3.7410 3.3384 2.1765 -0.6935 -0.6894 0.4859  276  ASP H CG  
22321 O  OD1 . ASP H  278 ? 3.7695 3.4061 2.1389 -0.8240 -0.7438 0.5578  276  ASP H OD1 
22322 O  OD2 . ASP H  278 ? 3.6244 3.3441 2.2607 -0.5951 -0.6728 0.5127  276  ASP H OD2 
22323 N  N   . LEU H  279 ? 4.3142 3.3646 2.1619 -0.6980 -0.5613 0.1877  277  LEU H N   
22324 C  CA  . LEU H  279 ? 4.3468 3.2074 2.0422 -0.6383 -0.4940 0.0854  277  LEU H CA  
22325 C  C   . LEU H  279 ? 4.4867 3.2466 1.9996 -0.7271 -0.4881 0.0601  277  LEU H C   
22326 O  O   . LEU H  279 ? 4.6876 3.2396 1.9885 -0.7408 -0.4419 -0.0078 277  LEU H O   
22327 C  CB  . LEU H  279 ? 4.2525 3.1758 2.1029 -0.4834 -0.4462 0.0419  277  LEU H CB  
22328 C  CG  . LEU H  279 ? 4.3127 3.2717 2.2895 -0.3803 -0.4295 0.0361  277  LEU H CG  
22329 C  CD1 . LEU H  279 ? 4.1675 3.1961 2.2832 -0.2469 -0.3863 -0.0028 277  LEU H CD1 
22330 C  CD2 . LEU H  279 ? 4.5064 3.2755 2.3144 -0.3796 -0.3996 -0.0120 277  LEU H CD2 
22331 N  N   . GLY H  280 ? 4.3865 3.2879 1.9773 -0.7863 -0.5305 0.1164  278  GLY H N   
22332 C  CA  . GLY H  280 ? 4.4831 3.3065 1.9141 -0.8716 -0.5271 0.0957  278  GLY H CA  
22333 C  C   . GLY H  280 ? 4.5080 3.2568 1.9138 -0.7688 -0.4584 0.0126  278  GLY H C   
22334 O  O   . GLY H  280 ? 4.7197 3.2955 1.9161 -0.8100 -0.4207 -0.0433 278  GLY H O   
22335 N  N   . TRP H  281 ? 4.3443 3.2166 1.9519 -0.6385 -0.4383 0.0050  279  TRP H N   
22336 C  CA  . TRP H  281 ? 4.3592 3.1901 1.9679 -0.5334 -0.3752 -0.0658 279  TRP H CA  
22337 C  C   . TRP H  281 ? 4.1086 3.1085 1.8640 -0.5256 -0.3974 -0.0328 279  TRP H C   
22338 O  O   . TRP H  281 ? 3.9937 3.1587 1.9579 -0.4691 -0.4178 0.0092  279  TRP H O   
22339 C  CB  . TRP H  281 ? 4.4289 3.2551 2.1334 -0.3920 -0.3299 -0.1056 279  TRP H CB  
22340 C  CG  . TRP H  281 ? 4.5880 3.2255 2.1319 -0.3833 -0.2932 -0.1491 279  TRP H CG  
22341 C  CD1 . TRP H  281 ? 4.7455 3.2113 2.0668 -0.4894 -0.2947 -0.1582 279  TRP H CD1 
22342 C  CD2 . TRP H  281 ? 4.5137 3.1094 2.0993 -0.2651 -0.2475 -0.1875 279  TRP H CD2 
22343 N  NE1 . TRP H  281 ? 4.7820 3.0935 2.0036 -0.4397 -0.2492 -0.2011 279  TRP H NE1 
22344 C  CE2 . TRP H  281 ? 4.6305 3.0249 2.0171 -0.2999 -0.2208 -0.2175 279  TRP H CE2 
22345 C  CE3 . TRP H  281 ? 4.2199 2.9271 1.9849 -0.1387 -0.2262 -0.1974 279  TRP H CE3 
22346 C  CZ2 . TRP H  281 ? 4.5804 2.8888 1.9531 -0.2055 -0.1739 -0.2534 279  TRP H CZ2 
22347 C  CZ3 . TRP H  281 ? 4.2069 2.8372 1.9572 -0.0516 -0.1835 -0.2321 279  TRP H CZ3 
22348 C  CH2 . TRP H  281 ? 4.4015 2.8373 1.9624 -0.0815 -0.1577 -0.2582 279  TRP H CH2 
22349 N  N   . LYS H  282 ? 4.0109 2.9599 1.6491 -0.5838 -0.3896 -0.0521 280  LYS H N   
22350 C  CA  . LYS H  282 ? 3.9766 3.0702 1.7310 -0.5848 -0.4088 -0.0236 280  LYS H CA  
22351 C  C   . LYS H  282 ? 4.1996 3.2852 1.9876 -0.4711 -0.3484 -0.0891 280  LYS H C   
22352 O  O   . LYS H  282 ? 4.3741 3.5500 2.2232 -0.4738 -0.3551 -0.0791 280  LYS H O   
22353 C  CB  . LYS H  282 ? 4.1254 3.1926 1.7420 -0.7299 -0.4455 0.0059  280  LYS H CB  
22354 C  CG  . LYS H  282 ? 3.8756 3.1359 1.6438 -0.7659 -0.4949 0.0775  280  LYS H CG  
22355 C  CD  . LYS H  282 ? 3.9614 3.2090 1.5943 -0.9258 -0.5421 0.1217  280  LYS H CD  
22356 C  CE  . LYS H  282 ? 4.1521 3.2110 1.5485 -0.9654 -0.4958 0.0431  280  LYS H CE  
22357 N  NZ  . LYS H  282 ? 4.3142 3.3541 1.5632 -1.1338 -0.5429 0.0855  280  LYS H NZ  
22358 N  N   . TRP H  283 ? 4.2791 3.2673 2.0314 -0.3725 -0.2903 -0.1505 281  TRP H N   
22359 C  CA  . TRP H  283 ? 4.3433 3.3356 2.1282 -0.2641 -0.2320 -0.2053 281  TRP H CA  
22360 C  C   . TRP H  283 ? 4.2519 3.3993 2.2570 -0.1596 -0.2323 -0.1927 281  TRP H C   
22361 O  O   . TRP H  283 ? 4.2565 3.4315 2.3057 -0.0710 -0.1890 -0.2308 281  TRP H O   
22362 C  CB  . TRP H  283 ? 4.4192 3.2223 2.0369 -0.2116 -0.1608 -0.2732 281  TRP H CB  
22363 C  CG  . TRP H  283 ? 4.4684 3.2173 2.0949 -0.1654 -0.1515 -0.2773 281  TRP H CG  
22364 C  CD1 . TRP H  283 ? 4.6303 3.2856 2.1589 -0.2417 -0.1773 -0.2588 281  TRP H CD1 
22365 C  CD2 . TRP H  283 ? 4.4951 3.2834 2.2306 -0.0378 -0.1150 -0.2991 281  TRP H CD2 
22366 N  NE1 . TRP H  283 ? 4.8541 3.4841 2.4264 -0.1652 -0.1580 -0.2698 281  TRP H NE1 
22367 C  CE2 . TRP H  283 ? 4.6637 3.3752 2.3631 -0.0399 -0.1201 -0.2938 281  TRP H CE2 
22368 C  CE3 . TRP H  283 ? 4.2817 3.1677 2.1382 0.0713  -0.0809 -0.3194 281  TRP H CE3 
22369 C  CZ2 . TRP H  283 ? 4.4475 3.1762 2.2298 0.0655  -0.0918 -0.3085 281  TRP H CZ2 
22370 C  CZ3 . TRP H  283 ? 4.1275 3.0352 2.0636 0.1707  -0.0545 -0.3315 281  TRP H CZ3 
22371 C  CH2 . TRP H  283 ? 4.2101 3.0389 2.1099 0.1685  -0.0598 -0.3262 281  TRP H CH2 
22372 N  N   . ILE H  284 ? 4.2060 3.4544 2.3442 -0.1713 -0.2775 -0.1378 282  ILE H N   
22373 C  CA  . ILE H  284 ? 4.0463 3.4296 2.3818 -0.0844 -0.2765 -0.1227 282  ILE H CA  
22374 C  C   . ILE H  284 ? 4.0096 3.5415 2.4792 -0.1305 -0.3234 -0.0554 282  ILE H C   
22375 O  O   . ILE H  284 ? 4.0478 3.6169 2.5387 -0.2049 -0.3704 0.0075  282  ILE H O   
22376 C  CB  . ILE H  284 ? 3.9310 3.2974 2.3117 -0.0446 -0.2771 -0.1157 282  ILE H CB  
22377 C  CG1 . ILE H  284 ? 3.9510 3.1705 2.2028 0.0101  -0.2251 -0.1791 282  ILE H CG1 
22378 C  CG2 . ILE H  284 ? 3.7641 3.2652 2.3395 0.0311  -0.2765 -0.0964 282  ILE H CG2 
22379 C  CD1 . ILE H  284 ? 3.9554 3.1457 2.2355 0.0463  -0.2245 -0.1751 282  ILE H CD1 
22380 N  N   . HIS H  285 ? 3.9296 3.5501 2.4903 -0.0862 -0.3090 -0.0634 283  HIS H N   
22381 C  CA  . HIS H  285 ? 3.8382 3.5897 2.5199 -0.1231 -0.3445 -0.0006 283  HIS H CA  
22382 C  C   . HIS H  285 ? 3.7475 3.5978 2.6003 -0.0798 -0.3544 0.0469  283  HIS H C   
22383 O  O   . HIS H  285 ? 3.7147 3.6353 2.6383 -0.1305 -0.3928 0.1220  283  HIS H O   
22384 C  CB  . HIS H  285 ? 3.7653 3.5624 2.4679 -0.0958 -0.3224 -0.0286 283  HIS H CB  
22385 C  CG  . HIS H  285 ? 3.8162 3.5288 2.3594 -0.1461 -0.3130 -0.0645 283  HIS H CG  
22386 N  ND1 . HIS H  285 ? 3.8681 3.4388 2.2543 -0.1358 -0.2783 -0.1222 283  HIS H ND1 
22387 C  CD2 . HIS H  285 ? 3.8384 3.5812 2.3494 -0.2063 -0.3288 -0.0502 283  HIS H CD2 
22388 C  CE1 . HIS H  285 ? 4.0080 3.5184 2.2670 -0.1877 -0.2698 -0.1438 283  HIS H CE1 
22389 N  NE2 . HIS H  285 ? 4.0221 3.6389 2.3545 -0.2336 -0.3030 -0.1017 283  HIS H NE2 
22390 N  N   . GLU H  286 ? 3.6853 3.5448 2.6044 0.0121  -0.3175 0.0084  284  GLU H N   
22391 C  CA  . GLU H  286 ? 3.5231 3.4587 2.5904 0.0568  -0.3165 0.0447  284  GLU H CA  
22392 C  C   . GLU H  286 ? 3.4263 3.3074 2.4867 0.1224  -0.2899 0.0038  284  GLU H C   
22393 O  O   . GLU H  286 ? 3.4860 3.3140 2.4819 0.1702  -0.2569 -0.0589 284  GLU H O   
22394 C  CB  . GLU H  286 ? 3.4113 3.4344 2.5873 0.0962  -0.2975 0.0482  284  GLU H CB  
22395 C  CG  . GLU H  286 ? 3.4451 3.5326 2.6470 0.0375  -0.3224 0.0965  284  GLU H CG  
22396 C  CD  . GLU H  286 ? 3.3656 3.5190 2.6526 -0.0086 -0.3573 0.1892  284  GLU H CD  
22397 O  OE1 . GLU H  286 ? 3.1972 3.3652 2.5603 0.0229  -0.3524 0.2167  284  GLU H OE1 
22398 O  OE2 . GLU H  286 ? 3.3908 3.5877 2.6707 -0.0765 -0.3888 0.2392  284  GLU H OE2 
22399 N  N   . PRO H  287 ? 3.2916 3.1917 2.4213 0.1260  -0.3029 0.0444  285  PRO H N   
22400 C  CA  . PRO H  287 ? 3.2457 3.2189 2.4591 0.0748  -0.3383 0.1297  285  PRO H CA  
22401 C  C   . PRO H  287 ? 3.4151 3.3478 2.5302 -0.0150 -0.3802 0.1634  285  PRO H C   
22402 O  O   . PRO H  287 ? 3.5009 3.3284 2.4704 -0.0369 -0.3766 0.1134  285  PRO H O   
22403 C  CB  . PRO H  287 ? 3.1734 3.1709 2.4884 0.1282  -0.3239 0.1480  285  PRO H CB  
22404 C  CG  . PRO H  287 ? 3.2255 3.1300 2.4542 0.1678  -0.3036 0.0808  285  PRO H CG  
22405 C  CD  . PRO H  287 ? 3.2640 3.1242 2.4035 0.1866  -0.2803 0.0138  285  PRO H CD  
22406 N  N   . LYS H  288 ? 3.4596 3.4744 2.6496 -0.0681 -0.4165 0.2516  286  LYS H N   
22407 C  CA  . LYS H  288 ? 3.5014 3.5012 2.6061 -0.1691 -0.4635 0.2986  286  LYS H CA  
22408 C  C   . LYS H  288 ? 3.4393 3.4570 2.5880 -0.1792 -0.4824 0.3493  286  LYS H C   
22409 O  O   . LYS H  288 ? 3.4751 3.5366 2.6116 -0.2648 -0.5275 0.4229  286  LYS H O   
22410 C  CB  . LYS H  288 ? 3.3419 3.4410 2.4878 -0.2400 -0.4984 0.3732  286  LYS H CB  
22411 C  CG  . LYS H  288 ? 3.1666 3.2499 2.2621 -0.2404 -0.4837 0.3268  286  LYS H CG  
22412 C  CD  . LYS H  288 ? 3.0798 3.2778 2.2444 -0.2990 -0.5156 0.4085  286  LYS H CD  
22413 C  CE  . LYS H  288 ? 3.1148 3.3010 2.2388 -0.2929 -0.4982 0.3608  286  LYS H CE  
22414 N  NZ  . LYS H  288 ? 3.0457 3.3468 2.2457 -0.3435 -0.5267 0.4417  286  LYS H NZ  
22415 N  N   . GLY H  289 ? 3.2078 3.1998 2.4072 -0.0980 -0.4501 0.3153  287  GLY H N   
22416 C  CA  . GLY H  289 ? 3.1841 3.1835 2.4185 -0.1012 -0.4633 0.3546  287  GLY H CA  
22417 C  C   . GLY H  289 ? 3.1309 3.1574 2.4888 -0.0023 -0.4232 0.3422  287  GLY H C   
22418 O  O   . GLY H  289 ? 3.0584 3.1396 2.5163 0.0526  -0.3941 0.3423  287  GLY H O   
22419 N  N   . TYR H  290 ? 3.2936 3.2728 2.6342 0.0160  -0.4203 0.3303  288  TYR H N   
22420 C  CA  . TYR H  290 ? 3.2701 3.2675 2.7145 0.0999  -0.3842 0.3206  288  TYR H CA  
22421 C  C   . TYR H  290 ? 3.2582 3.2417 2.7006 0.0831  -0.4018 0.3524  288  TYR H C   
22422 O  O   . TYR H  290 ? 3.3240 3.2710 2.6700 0.0085  -0.4395 0.3706  288  TYR H O   
22423 C  CB  . TYR H  290 ? 3.2670 3.1916 2.6674 0.1728  -0.3419 0.2242  288  TYR H CB  
22424 C  CG  . TYR H  290 ? 3.3950 3.2056 2.6677 0.1778  -0.3394 0.1635  288  TYR H CG  
22425 C  CD1 . TYR H  290 ? 3.5762 3.3018 2.6995 0.1213  -0.3573 0.1380  288  TYR H CD1 
22426 C  CD2 . TYR H  290 ? 3.4316 3.2114 2.7261 0.2391  -0.3144 0.1322  288  TYR H CD2 
22427 C  CE1 . TYR H  290 ? 3.7429 3.3485 2.7423 0.1313  -0.3457 0.0845  288  TYR H CE1 
22428 C  CE2 . TYR H  290 ? 3.5339 3.2088 2.7150 0.2491  -0.3084 0.0818  288  TYR H CE2 
22429 C  CZ  . TYR H  290 ? 3.6650 3.2493 2.6987 0.1982  -0.3216 0.0586  288  TYR H CZ  
22430 O  OH  . TYR H  290 ? 3.7233 3.1885 2.6379 0.2135  -0.3068 0.0107  288  TYR H OH  
22431 N  N   . HIS H  291 ? 3.2116 3.2199 2.7534 0.1485  -0.3726 0.3584  289  HIS H N   
22432 C  CA  . HIS H  291 ? 3.1562 3.1711 2.7247 0.1409  -0.3848 0.3984  289  HIS H CA  
22433 C  C   . HIS H  291 ? 3.2372 3.1446 2.7227 0.1821  -0.3661 0.3182  289  HIS H C   
22434 O  O   . HIS H  291 ? 3.1720 3.0754 2.7165 0.2536  -0.3288 0.2879  289  HIS H O   
22435 C  CB  . HIS H  291 ? 2.9940 3.1054 2.7270 0.1856  -0.3598 0.4657  289  HIS H CB  
22436 C  CG  . HIS H  291 ? 2.9918 3.2185 2.8171 0.1464  -0.3781 0.5659  289  HIS H CG  
22437 N  ND1 . HIS H  291 ? 3.0292 3.3361 2.8989 0.0913  -0.4142 0.6637  289  HIS H ND1 
22438 C  CD2 . HIS H  291 ? 2.9288 3.2113 2.8136 0.1543  -0.3651 0.5899  289  HIS H CD2 
22439 C  CE1 . HIS H  291 ? 2.9908 3.4049 2.9488 0.0696  -0.4222 0.7480  289  HIS H CE1 
22440 N  NE2 . HIS H  291 ? 2.8944 3.2900 2.8615 0.1082  -0.3919 0.7034  289  HIS H NE2 
22441 N  N   . ALA H  292 ? 3.3745 3.1896 2.7157 0.1333  -0.3901 0.2868  290  ALA H N   
22442 C  CA  . ALA H  292 ? 3.5453 3.2519 2.7983 0.1686  -0.3729 0.2202  290  ALA H CA  
22443 C  C   . ALA H  292 ? 3.6683 3.3775 2.9343 0.1423  -0.3943 0.2651  290  ALA H C   
22444 O  O   . ALA H  292 ? 3.9333 3.6042 3.1062 0.0632  -0.4312 0.2911  290  ALA H O   
22445 C  CB  . ALA H  292 ? 3.7867 3.3728 2.8665 0.1371  -0.3754 0.1615  290  ALA H CB  
22446 N  N   . ASN H  293 ? 3.5333 3.2835 2.9059 0.2034  -0.3704 0.2736  291  ASN H N   
22447 C  CA  . ASN H  293 ? 3.5559 3.3237 2.9594 0.1846  -0.3873 0.3216  291  ASN H CA  
22448 C  C   . ASN H  293 ? 3.5099 3.1530 2.7862 0.1867  -0.3874 0.2642  291  ASN H C   
22449 O  O   . ASN H  293 ? 3.5639 3.1062 2.7228 0.1974  -0.3749 0.1959  291  ASN H O   
22450 C  CB  . ASN H  293 ? 3.5177 3.3674 3.0765 0.2490  -0.3551 0.3527  291  ASN H CB  
22451 C  CG  . ASN H  293 ? 3.5344 3.4992 3.2168 0.2458  -0.3503 0.4231  291  ASN H CG  
22452 O  OD1 . ASN H  293 ? 3.6094 3.6159 3.2755 0.1839  -0.3828 0.4673  291  ASN H OD1 
22453 N  ND2 . ASN H  293 ? 3.4430 3.4543 3.2435 0.3105  -0.3067 0.4360  291  ASN H ND2 
22454 N  N   . PHE H  294 ? 3.3615 3.0098 2.6608 0.1792  -0.3980 0.2956  292  PHE H N   
22455 C  CA  . PHE H  294 ? 3.4293 2.9601 2.6149 0.1827  -0.3966 0.2482  292  PHE H CA  
22456 C  C   . PHE H  294 ? 3.4469 3.0184 2.7198 0.2110  -0.3915 0.2785  292  PHE H C   
22457 O  O   . PHE H  294 ? 3.3026 2.9879 2.7092 0.2141  -0.3927 0.3450  292  PHE H O   
22458 C  CB  . PHE H  294 ? 3.4749 2.9193 2.5027 0.0865  -0.4349 0.2566  292  PHE H CB  
22459 C  CG  . PHE H  294 ? 3.4757 3.0069 2.5413 -0.0008 -0.4822 0.3502  292  PHE H CG  
22460 C  CD1 . PHE H  294 ? 3.5285 3.1628 2.6483 -0.0539 -0.5079 0.4131  292  PHE H CD1 
22461 C  CD2 . PHE H  294 ? 3.4838 3.0025 2.5329 -0.0315 -0.5018 0.3810  292  PHE H CD2 
22462 C  CE1 . PHE H  294 ? 3.6377 3.3717 2.8005 -0.1351 -0.5526 0.5109  292  PHE H CE1 
22463 C  CE2 . PHE H  294 ? 3.5034 3.1190 2.5924 -0.1146 -0.5468 0.4757  292  PHE H CE2 
22464 C  CZ  . PHE H  294 ? 3.5869 3.3155 2.7353 -0.1664 -0.5724 0.5437  292  PHE H CZ  
22465 N  N   . CYS H  295 ? 3.4767 2.9510 2.6711 0.2346  -0.3816 0.2317  293  CYS H N   
22466 C  CA  . CYS H  295 ? 3.2537 2.7489 2.5105 0.2606  -0.3760 0.2509  293  CYS H CA  
22467 C  C   . CYS H  295 ? 3.3247 2.7648 2.4856 0.1851  -0.4145 0.2805  293  CYS H C   
22468 O  O   . CYS H  295 ? 3.4648 2.7751 2.4707 0.1593  -0.4196 0.2352  293  CYS H O   
22469 C  CB  . CYS H  295 ? 3.0804 2.5174 2.3282 0.3442  -0.3362 0.1806  293  CYS H CB  
22470 S  SG  . CYS H  295 ? 2.9698 2.4655 2.3105 0.4233  -0.2914 0.1416  293  CYS H SG  
22471 N  N   . LEU H  296 ? 3.1368 2.6718 2.3856 0.1501  -0.4372 0.3586  294  LEU H N   
22472 C  CA  . LEU H  296 ? 3.1397 2.6441 2.3094 0.0692  -0.4777 0.3984  294  LEU H CA  
22473 C  C   . LEU H  296 ? 3.0636 2.6333 2.3386 0.0983  -0.4713 0.4385  294  LEU H C   
22474 O  O   . LEU H  296 ? 3.0586 2.7559 2.4900 0.1293  -0.4574 0.4946  294  LEU H O   
22475 C  CB  . LEU H  296 ? 3.1674 2.7451 2.3263 -0.0331 -0.5249 0.4759  294  LEU H CB  
22476 C  CG  . LEU H  296 ? 3.2136 2.7243 2.2236 -0.1470 -0.5731 0.5021  294  LEU H CG  
22477 C  CD1 . LEU H  296 ? 3.1445 2.7370 2.2246 -0.1762 -0.5964 0.5760  294  LEU H CD1 
22478 C  CD2 . LEU H  296 ? 3.3708 2.6800 2.1892 -0.1436 -0.5569 0.4082  294  LEU H CD2 
22479 N  N   . GLY H  297 ? 3.1692 2.6451 2.3548 0.0898  -0.4767 0.4108  295  GLY H N   
22480 C  CA  . GLY H  297 ? 3.1319 2.6581 2.4008 0.1121  -0.4719 0.4448  295  GLY H CA  
22481 C  C   . GLY H  297 ? 3.2030 2.6038 2.3833 0.1515  -0.4541 0.3758  295  GLY H C   
22482 O  O   . GLY H  297 ? 3.2774 2.5808 2.3845 0.1999  -0.4278 0.2991  295  GLY H O   
22483 N  N   . PRO H  298 ? 3.4043 2.8117 2.5922 0.1319  -0.4676 0.4074  296  PRO H N   
22484 C  CA  . PRO H  298 ? 3.5321 2.8265 2.6423 0.1690  -0.4514 0.3495  296  PRO H CA  
22485 C  C   . PRO H  298 ? 3.5474 2.8883 2.7762 0.2651  -0.4078 0.3250  296  PRO H C   
22486 O  O   . PRO H  298 ? 3.5261 2.9858 2.8997 0.2937  -0.3905 0.3656  296  PRO H O   
22487 C  CB  . PRO H  298 ? 3.5503 2.8430 2.6173 0.0915  -0.4904 0.4040  296  PRO H CB  
22488 C  CG  . PRO H  298 ? 3.4979 2.9630 2.7118 0.0608  -0.5079 0.4995  296  PRO H CG  
22489 C  CD  . PRO H  298 ? 3.4458 2.9661 2.7033 0.0657  -0.5024 0.5050  296  PRO H CD  
22490 N  N   . CYS H  299 ? 3.5598 2.7985 2.7164 0.3131  -0.3866 0.2595  297  CYS H N   
22491 C  CA  . CYS H  299 ? 3.4557 2.7224 2.6959 0.3936  -0.3484 0.2308  297  CYS H CA  
22492 C  C   . CYS H  299 ? 3.4394 2.6188 2.6034 0.4001  -0.3508 0.2082  297  CYS H C   
22493 O  O   . CYS H  299 ? 3.5324 2.6127 2.6058 0.4361  -0.3354 0.1514  297  CYS H O   
22494 C  CB  . CYS H  299 ? 3.3863 2.6388 2.6311 0.4597  -0.3136 0.1704  297  CYS H CB  
22495 S  SG  . CYS H  299 ? 3.2692 2.5970 2.5762 0.4594  -0.3061 0.1787  297  CYS H SG  
22496 N  N   . PRO H  300 ? 3.3284 2.5455 2.5295 0.3680  -0.3679 0.2564  298  PRO H N   
22497 C  CA  . PRO H  300 ? 3.3224 2.4577 2.4535 0.3736  -0.3702 0.2364  298  PRO H CA  
22498 C  C   . PRO H  300 ? 3.1553 2.3434 2.3857 0.4376  -0.3382 0.2264  298  PRO H C   
22499 O  O   . PRO H  300 ? 3.0243 2.3043 2.3713 0.4746  -0.3111 0.2343  298  PRO H O   
22500 C  CB  . PRO H  300 ? 3.5035 2.6489 2.6025 0.2861  -0.4130 0.2992  298  PRO H CB  
22501 C  CG  . PRO H  300 ? 3.4633 2.7534 2.6870 0.2578  -0.4229 0.3685  298  PRO H CG  
22502 C  CD  . PRO H  300 ? 3.3510 2.6841 2.6479 0.3189  -0.3888 0.3384  298  PRO H CD  
22503 N  N   . TYR H  301 ? 3.1149 2.2387 2.2924 0.4475  -0.3387 0.2092  299  TYR H N   
22504 C  CA  . TYR H  301 ? 3.0674 2.2355 2.3261 0.5005  -0.3095 0.1988  299  TYR H CA  
22505 C  C   . TYR H  301 ? 3.0259 2.1485 2.2399 0.4794  -0.3254 0.2119  299  TYR H C   
22506 O  O   . TYR H  301 ? 3.1182 2.1489 2.2162 0.4345  -0.3537 0.2134  299  TYR H O   
22507 C  CB  . TYR H  301 ? 3.1898 2.3308 2.4365 0.5694  -0.2770 0.1369  299  TYR H CB  
22508 C  CG  . TYR H  301 ? 3.3760 2.4067 2.5089 0.5918  -0.2774 0.0975  299  TYR H CG  
22509 C  CD1 . TYR H  301 ? 3.2959 2.2129 2.2974 0.5544  -0.3000 0.0948  299  TYR H CD1 
22510 C  CD2 . TYR H  301 ? 3.4516 2.4887 2.6029 0.6490  -0.2515 0.0662  299  TYR H CD2 
22511 C  CE1 . TYR H  301 ? 3.3593 2.1650 2.2552 0.5828  -0.2910 0.0627  299  TYR H CE1 
22512 C  CE2 . TYR H  301 ? 3.3633 2.3094 2.4207 0.6764  -0.2482 0.0397  299  TYR H CE2 
22513 C  CZ  . TYR H  301 ? 3.3457 2.1727 2.2774 0.6481  -0.2649 0.0382  299  TYR H CZ  
22514 O  OH  . TYR H  301 ? 3.4861 2.2126 2.3226 0.6831  -0.2527 0.0154  299  TYR H OH  
22515 N  N   . ILE H  302 ? 3.0352 2.2154 2.3345 0.5095  -0.3037 0.2199  300  ILE H N   
22516 C  CA  . ILE H  302 ? 3.2241 2.3787 2.5018 0.4954  -0.3139 0.2340  300  ILE H CA  
22517 C  C   . ILE H  302 ? 3.3647 2.5137 2.6022 0.4173  -0.3559 0.2888  300  ILE H C   
22518 O  O   . ILE H  302 ? 3.2703 2.3160 2.3840 0.3813  -0.3819 0.2789  300  ILE H O   
22519 C  CB  . ILE H  302 ? 3.2236 2.2719 2.4002 0.5292  -0.3090 0.1808  300  ILE H CB  
22520 C  CG1 . ILE H  302 ? 3.0408 2.1138 2.2566 0.5975  -0.2726 0.1349  300  ILE H CG1 
22521 C  CG2 . ILE H  302 ? 3.3118 2.3460 2.4831 0.5230  -0.3139 0.1935  300  ILE H CG2 
22522 C  CD1 . ILE H  302 ? 2.8140 1.9849 2.1493 0.6211  -0.2422 0.1444  300  ILE H CD1 
22523 N  N   . TRP H  303 ? 3.5652 2.8254 2.9034 0.3884  -0.3607 0.3512  301  TRP H N   
22524 C  CA  . TRP H  303 ? 3.5213 2.8139 2.8440 0.3079  -0.4024 0.4193  301  TRP H CA  
22525 C  C   . TRP H  303 ? 3.4173 2.7747 2.8113 0.3013  -0.3995 0.4665  301  TRP H C   
22526 O  O   . TRP H  303 ? 3.3523 2.7533 2.8358 0.3595  -0.3587 0.4568  301  TRP H O   
22527 C  CB  . TRP H  303 ? 3.3326 2.7261 2.7300 0.2796  -0.4106 0.4728  301  TRP H CB  
22528 C  CG  . TRP H  303 ? 3.4021 2.7868 2.7174 0.1825  -0.4640 0.5205  301  TRP H CG  
22529 C  CD1 . TRP H  303 ? 3.3897 2.8784 2.7572 0.1162  -0.4945 0.6108  301  TRP H CD1 
22530 C  CD2 . TRP H  303 ? 3.5573 2.8213 2.7150 0.1349  -0.4914 0.4833  301  TRP H CD2 
22531 N  NE1 . TRP H  303 ? 3.5375 2.9816 2.7853 0.0215  -0.5443 0.6318  301  TRP H NE1 
22532 C  CE2 . TRP H  303 ? 3.6314 2.9273 2.7430 0.0310  -0.5406 0.5512  301  TRP H CE2 
22533 C  CE3 . TRP H  303 ? 3.5384 2.6713 2.5870 0.1694  -0.4757 0.4029  301  TRP H CE3 
22534 C  CZ2 . TRP H  303 ? 3.7453 2.9305 2.6916 -0.0453 -0.5732 0.5346  301  TRP H CZ2 
22535 C  CZ3 . TRP H  303 ? 3.6620 2.6838 2.5539 0.1042  -0.5026 0.3878  301  TRP H CZ3 
22536 C  CH2 . TRP H  303 ? 3.7746 2.8153 2.6099 -0.0051 -0.5503 0.4501  301  TRP H CH2 
22537 N  N   . SER H  304 ? 3.4165 2.7768 2.7617 0.2243  -0.4423 0.5184  302  SER H N   
22538 C  CA  . SER H  304 ? 3.3108 2.7337 2.7152 0.2108  -0.4437 0.5684  302  SER H CA  
22539 C  C   . SER H  304 ? 3.1896 2.7660 2.7718 0.2471  -0.4071 0.6289  302  SER H C   
22540 O  O   . SER H  304 ? 3.0567 2.7005 2.7102 0.2611  -0.3931 0.6505  302  SER H O   
22541 C  CB  . SER H  304 ? 3.4241 2.8403 2.7463 0.1090  -0.5002 0.6243  302  SER H CB  
22542 O  OG  . SER H  304 ? 3.4923 2.7424 2.6363 0.0781  -0.5237 0.5667  302  SER H OG  
22543 N  N   . LEU H  305 ? 3.1447 2.7675 2.7939 0.2660  -0.3858 0.6557  303  LEU H N   
22544 C  CA  . LEU H  305 ? 3.0277 2.7761 2.8365 0.3086  -0.3372 0.7127  303  LEU H CA  
22545 C  C   . LEU H  305 ? 2.8143 2.5391 2.6725 0.3925  -0.2745 0.6524  303  LEU H C   
22546 O  O   . LEU H  305 ? 2.7136 2.4565 2.6358 0.4381  -0.2251 0.6495  303  LEU H O   
22547 C  CB  . LEU H  305 ? 3.0183 2.8999 2.9177 0.2720  -0.3507 0.8101  303  LEU H CB  
22548 C  CG  . LEU H  305 ? 2.9658 2.9033 2.8287 0.1745  -0.4150 0.8893  303  LEU H CG  
22549 C  CD1 . LEU H  305 ? 2.7142 2.7797 2.6534 0.1373  -0.4325 0.9769  303  LEU H CD1 
22550 C  CD2 . LEU H  305 ? 2.9938 2.9961 2.9101 0.1637  -0.4106 0.9466  303  LEU H CD2 
22551 N  N   . ASP H  306 ? 2.9359 2.6177 2.7572 0.4076  -0.2751 0.6046  304  ASP H N   
22552 C  CA  . ASP H  306 ? 2.8650 2.5270 2.7226 0.4758  -0.2208 0.5491  304  ASP H CA  
22553 C  C   . ASP H  306 ? 2.8231 2.5807 2.8199 0.5138  -0.1609 0.6034  304  ASP H C   
22554 O  O   . ASP H  306 ? 2.7711 2.6246 2.8471 0.4946  -0.1646 0.6847  304  ASP H O   
22555 C  CB  . ASP H  306 ? 2.8625 2.4351 2.6548 0.5092  -0.2048 0.4721  304  ASP H CB  
22556 N  N   . VAL H  312 ? 3.1773 2.7154 2.9036 0.5186  -0.2277 0.3989  310  VAL H N   
22557 C  CA  . VAL H  312 ? 3.0095 2.6139 2.8452 0.5498  -0.1783 0.4319  310  VAL H CA  
22558 C  C   . VAL H  312 ? 2.7388 2.3122 2.5828 0.6049  -0.1269 0.3688  310  VAL H C   
22559 O  O   . VAL H  312 ? 2.5409 2.0823 2.3463 0.6212  -0.1256 0.3193  310  VAL H O   
22560 C  CB  . VAL H  312 ? 3.0361 2.7455 2.9830 0.5418  -0.1633 0.5132  310  VAL H CB  
22561 C  CG1 . VAL H  312 ? 3.1098 2.8689 3.0496 0.4756  -0.2187 0.5859  310  VAL H CG1 
22562 C  CG2 . VAL H  312 ? 2.9679 2.6837 2.9297 0.5607  -0.1486 0.4926  310  VAL H CG2 
22563 N  N   . LEU H  313 ? 2.8292 2.4127 2.7178 0.6285  -0.0842 0.3724  311  LEU H N   
22564 C  CA  . LEU H  313 ? 2.7718 2.3333 2.6710 0.6689  -0.0286 0.3235  311  LEU H CA  
22565 C  C   . LEU H  313 ? 2.5136 2.1223 2.5031 0.6908  0.0272  0.3577  311  LEU H C   
22566 O  O   . LEU H  313 ? 2.4375 2.0206 2.4277 0.7170  0.0777  0.3185  311  LEU H O   
22567 C  CB  . LEU H  313 ? 2.9219 2.4572 2.8080 0.6776  -0.0053 0.3066  311  LEU H CB  
22568 C  CG  . LEU H  313 ? 2.7415 2.2353 2.5921 0.7015  0.0342  0.2414  311  LEU H CG  
22569 C  CD1 . LEU H  313 ? 2.5175 1.9767 2.2904 0.7048  -0.0002 0.1835  311  LEU H CD1 
22570 C  CD2 . LEU H  313 ? 2.6839 2.1562 2.5169 0.6996  0.0487  0.2337  311  LEU H CD2 
22571 N  N   . ALA H  314 ? 2.4657 2.1426 2.5272 0.6777  0.0201  0.4341  312  ALA H N   
22572 C  CA  . ALA H  314 ? 2.5240 2.2476 2.6753 0.7033  0.0744  0.4768  312  ALA H CA  
22573 C  C   . ALA H  314 ? 2.7021 2.4192 2.8320 0.7031  0.0601  0.4478  312  ALA H C   
22574 O  O   . ALA H  314 ? 2.5443 2.2225 2.6587 0.7284  0.1010  0.3977  312  ALA H O   
22575 C  CB  . ALA H  314 ? 2.3809 2.1987 2.6276 0.6914  0.0721  0.5823  312  ALA H CB  
22576 N  N   . LEU H  315 ? 2.8243 2.5768 2.9443 0.6684  0.0013  0.4782  313  LEU H N   
22577 C  CA  . LEU H  315 ? 2.6647 2.4129 2.7600 0.6632  -0.0170 0.4542  313  LEU H CA  
22578 C  C   . LEU H  315 ? 2.7209 2.3905 2.7016 0.6574  -0.0519 0.3686  313  LEU H C   
22579 O  O   . LEU H  315 ? 2.6707 2.3168 2.5815 0.6237  -0.1079 0.3614  313  LEU H O   
22580 C  CB  . LEU H  315 ? 2.5376 2.3560 2.6637 0.6221  -0.0627 0.5264  313  LEU H CB  
22581 C  CG  . LEU H  315 ? 2.4716 2.3904 2.7251 0.6318  -0.0285 0.6266  313  LEU H CG  
22582 C  CD1 . LEU H  315 ? 2.5444 2.5431 2.8163 0.5779  -0.0860 0.7002  313  LEU H CD1 
22583 C  CD2 . LEU H  315 ? 2.4083 2.3257 2.7217 0.6822  0.0425  0.6203  313  LEU H CD2 
22584 N  N   . TYR H  316 ? 2.7197 2.3458 2.6759 0.6896  -0.0141 0.3061  314  TYR H N   
22585 C  CA  . TYR H  316 ? 2.5951 2.1643 2.4578 0.6935  -0.0381 0.2332  314  TYR H CA  
22586 C  C   . TYR H  316 ? 2.5364 2.1045 2.3903 0.7088  -0.0220 0.1958  314  TYR H C   
22587 O  O   . TYR H  316 ? 2.5530 2.0885 2.3360 0.7128  -0.0445 0.1458  314  TYR H O   
22588 C  CB  . TYR H  316 ? 2.6896 2.2216 2.5195 0.7098  -0.0178 0.1929  314  TYR H CB  
22589 C  CG  . TYR H  316 ? 2.9690 2.4522 2.7081 0.7042  -0.0621 0.1553  314  TYR H CG  
22590 C  CD1 . TYR H  316 ? 3.1679 2.6248 2.8469 0.7213  -0.0679 0.1004  314  TYR H CD1 
22591 C  CD2 . TYR H  316 ? 3.0092 2.4728 2.7218 0.6832  -0.0949 0.1795  314  TYR H CD2 
22592 C  CE1 . TYR H  316 ? 3.1808 2.5901 2.7792 0.7253  -0.0998 0.0735  314  TYR H CE1 
22593 C  CE2 . TYR H  316 ? 3.1550 2.5594 2.7774 0.6817  -0.1285 0.1473  314  TYR H CE2 
22594 C  CZ  . TYR H  316 ? 3.1362 2.5120 2.7035 0.7066  -0.1281 0.0957  314  TYR H CZ  
22595 O  OH  . TYR H  316 ? 2.8797 2.1944 2.3604 0.7141  -0.1530 0.0708  314  TYR H OH  
22596 N  N   . ASN H  317 ? 2.4890 2.0920 2.4129 0.7191  0.0189  0.2228  315  ASN H N   
22597 C  CA  . ASN H  317 ? 2.4455 2.0467 2.3610 0.7304  0.0373  0.1887  315  ASN H CA  
22598 C  C   . ASN H  317 ? 2.4924 2.1133 2.3955 0.7122  -0.0052 0.2011  315  ASN H C   
22599 O  O   . ASN H  317 ? 2.5158 2.1291 2.3890 0.7187  -0.0042 0.1622  315  ASN H O   
22600 C  CB  . ASN H  317 ? 2.6257 2.2400 2.6105 0.7484  0.1050  0.2124  315  ASN H CB  
22601 C  CG  . ASN H  317 ? 2.8911 2.5479 2.9629 0.7500  0.1227  0.2942  315  ASN H CG  
22602 O  OD1 . ASN H  317 ? 2.9855 2.6818 3.0738 0.7279  0.0752  0.3408  315  ASN H OD1 
22603 N  ND2 . ASN H  317 ? 2.9782 2.6262 3.1012 0.7740  0.1944  0.3158  315  ASN H ND2 
22604 N  N   . GLN H  318 ? 2.5473 2.1958 2.4683 0.6844  -0.0421 0.2561  316  GLN H N   
22605 C  CA  . GLN H  318 ? 2.6959 2.3567 2.5900 0.6553  -0.0854 0.2697  316  GLN H CA  
22606 C  C   . GLN H  318 ? 2.9517 2.5661 2.7532 0.6229  -0.1408 0.2570  316  GLN H C   
22607 O  O   . GLN H  318 ? 2.9779 2.5644 2.7137 0.6052  -0.1697 0.2351  316  GLN H O   
22608 C  CB  . GLN H  318 ? 2.5838 2.3213 2.5674 0.6361  -0.0845 0.3546  316  GLN H CB  
22609 C  CG  . GLN H  318 ? 2.4757 2.2479 2.5429 0.6687  -0.0262 0.3729  316  GLN H CG  
22610 C  CD  . GLN H  318 ? 2.4698 2.3230 2.6181 0.6512  -0.0318 0.4582  316  GLN H CD  
22611 O  OE1 . GLN H  318 ? 2.5404 2.4288 2.6742 0.6057  -0.0861 0.4995  316  GLN H OE1 
22612 N  NE2 . GLN H  318 ? 2.4794 2.3601 2.7078 0.6841  0.0262  0.4880  316  GLN H NE2 
22613 N  N   . HIS H  319 ? 3.0738 2.6698 2.8601 0.6139  -0.1522 0.2691  317  HIS H N   
22614 C  CA  . HIS H  319 ? 3.1867 2.7247 2.8750 0.5781  -0.2008 0.2615  317  HIS H CA  
22615 C  C   . HIS H  319 ? 3.1842 2.6404 2.7738 0.6038  -0.2026 0.1865  317  HIS H C   
22616 O  O   . HIS H  319 ? 3.3721 2.7708 2.8705 0.5832  -0.2306 0.1677  317  HIS H O   
22617 C  CB  . HIS H  319 ? 3.0944 2.6374 2.7960 0.5612  -0.2102 0.2978  317  HIS H CB  
22618 C  CG  . HIS H  319 ? 3.2121 2.8445 3.0051 0.5308  -0.2149 0.3851  317  HIS H CG  
22619 N  ND1 . HIS H  319 ? 3.3484 3.0549 3.2186 0.5277  -0.2040 0.4302  317  HIS H ND1 
22620 C  CD2 . HIS H  319 ? 3.2207 2.8894 3.0444 0.5034  -0.2286 0.4427  317  HIS H CD2 
22621 C  CE1 . HIS H  319 ? 3.2562 3.0463 3.2056 0.5027  -0.2094 0.5163  317  HIS H CE1 
22622 N  NE2 . HIS H  319 ? 3.2401 3.0118 3.1635 0.4865  -0.2249 0.5254  317  HIS H NE2 
22623 N  N   . ASN H  320 ? 2.8612 2.3120 2.4645 0.6479  -0.1698 0.1467  318  ASN H N   
22624 C  CA  . ASN H  320 ? 2.7076 2.1015 2.2313 0.6777  -0.1687 0.0872  318  ASN H CA  
22625 C  C   . ASN H  320 ? 2.7512 2.1790 2.3184 0.7163  -0.1283 0.0561  318  ASN H C   
22626 O  O   . ASN H  320 ? 2.8801 2.2979 2.4412 0.7314  -0.1173 0.0424  318  ASN H O   
22627 C  CB  . ASN H  320 ? 2.6102 1.9348 2.0565 0.6706  -0.1915 0.0812  318  ASN H CB  
22628 C  CG  . ASN H  320 ? 2.5820 1.8471 1.9451 0.7065  -0.1880 0.0313  318  ASN H CG  
22629 O  OD1 . ASN H  320 ? 2.5462 1.8176 1.8957 0.7287  -0.1773 0.0042  318  ASN H OD1 
22630 N  ND2 . ASN H  320 ? 2.6195 1.8294 1.9279 0.7140  -0.1956 0.0242  318  ASN H ND2 
22631 N  N   . PRO H  321 ? 2.7987 2.2657 2.4035 0.7268  -0.1057 0.0449  319  PRO H N   
22632 C  CA  . PRO H  321 ? 2.6448 2.1377 2.2721 0.7515  -0.0677 0.0130  319  PRO H CA  
22633 C  C   . PRO H  321 ? 2.5732 2.0537 2.1375 0.7761  -0.0726 -0.0322 319  PRO H C   
22634 O  O   . PRO H  321 ? 2.5766 2.0843 2.1481 0.7881  -0.0475 -0.0558 319  PRO H O   
22635 C  CB  . PRO H  321 ? 2.6426 2.1743 2.3230 0.7475  -0.0442 0.0222  319  PRO H CB  
22636 C  CG  . PRO H  321 ? 2.7236 2.2473 2.3780 0.7323  -0.0788 0.0347  319  PRO H CG  
22637 C  CD  . PRO H  321 ? 2.8434 2.3324 2.4664 0.7100  -0.1141 0.0629  319  PRO H CD  
22638 N  N   . GLY H  322 ? 2.5121 1.9528 2.0115 0.7820  -0.1006 -0.0411 320  GLY H N   
22639 C  CA  . GLY H  322 ? 2.5447 1.9759 1.9882 0.8144  -0.1004 -0.0733 320  GLY H CA  
22640 C  C   . GLY H  322 ? 2.4225 1.8121 1.8213 0.8288  -0.1099 -0.0742 320  GLY H C   
22641 O  O   . GLY H  322 ? 2.3638 1.7606 1.7307 0.8612  -0.1038 -0.0920 320  GLY H O   
22642 N  N   . ALA H  323 ? 2.4735 1.8265 1.8730 0.8046  -0.1246 -0.0496 321  ALA H N   
22643 C  CA  . ALA H  323 ? 2.5572 1.8610 1.9107 0.8121  -0.1359 -0.0468 321  ALA H CA  
22644 C  C   . ALA H  323 ? 2.7091 1.9396 1.9685 0.8367  -0.1462 -0.0607 321  ALA H C   
22645 O  O   . ALA H  323 ? 2.7862 1.9901 2.0066 0.8650  -0.1431 -0.0669 321  ALA H O   
22646 C  CB  . ALA H  323 ? 2.7099 2.0592 2.0942 0.8287  -0.1166 -0.0567 321  ALA H CB  
22647 N  N   . SER H  324 ? 2.8678 2.0602 2.0861 0.8270  -0.1542 -0.0633 322  SER H N   
22648 C  CA  . SER H  324 ? 2.9218 2.0265 2.0387 0.8519  -0.1534 -0.0773 322  SER H CA  
22649 C  C   . SER H  324 ? 2.9808 1.9774 2.0149 0.8225  -0.1730 -0.0634 322  SER H C   
22650 O  O   . SER H  324 ? 2.9636 1.9652 2.0227 0.7743  -0.1940 -0.0389 322  SER H O   
22651 C  CB  . SER H  324 ? 2.8517 1.9474 1.9434 0.8491  -0.1501 -0.0884 322  SER H CB  
22652 O  OG  . SER H  324 ? 2.8792 1.9059 1.8838 0.8913  -0.1330 -0.1058 322  SER H OG  
22653 N  N   . ALA H  325 ? 3.0370 1.9341 1.9687 0.8527  -0.1624 -0.0756 323  ALA H N   
22654 C  CA  . ALA H  325 ? 3.0668 1.8383 1.8952 0.8220  -0.1763 -0.0663 323  ALA H CA  
22655 C  C   . ALA H  325 ? 3.3556 2.0740 2.1319 0.7519  -0.2005 -0.0552 323  ALA H C   
22656 O  O   . ALA H  325 ? 3.3768 2.0367 2.1040 0.6974  -0.2248 -0.0352 323  ALA H O   
22657 C  CB  . ALA H  325 ? 3.1304 1.7911 1.8498 0.8752  -0.1485 -0.0815 323  ALA H CB  
22658 N  N   . ALA H  326 ? 3.5270 2.2721 2.3126 0.7466  -0.1965 -0.0640 324  ALA H N   
22659 C  CA  . ALA H  326 ? 3.4122 2.1188 2.1484 0.6760  -0.2206 -0.0501 324  ALA H CA  
22660 C  C   . ALA H  326 ? 3.0738 1.8975 1.9121 0.6700  -0.2232 -0.0445 324  ALA H C   
22661 O  O   . ALA H  326 ? 3.0534 1.8731 1.8718 0.6971  -0.2047 -0.0677 324  ALA H O   
22662 C  CB  . ALA H  326 ? 3.6199 2.1697 2.1926 0.6693  -0.2069 -0.0716 324  ALA H CB  
22663 N  N   . PRO H  327 ? 3.0825 2.0091 2.0298 0.6375  -0.2418 -0.0114 325  PRO H N   
22664 C  CA  . PRO H  327 ? 3.0327 2.0634 2.0764 0.6337  -0.2393 -0.0019 325  PRO H CA  
22665 C  C   . PRO H  327 ? 3.1352 2.1351 2.1220 0.5760  -0.2608 0.0126  325  PRO H C   
22666 O  O   . PRO H  327 ? 3.3382 2.2945 2.2681 0.5108  -0.2905 0.0425  325  PRO H O   
22667 C  CB  . PRO H  327 ? 3.0653 2.1942 2.2295 0.6192  -0.2451 0.0365  325  PRO H CB  
22668 C  CG  . PRO H  327 ? 2.9498 2.0410 2.0931 0.6340  -0.2440 0.0336  325  PRO H CG  
22669 C  CD  . PRO H  327 ? 3.0355 1.9948 2.0341 0.6164  -0.2565 0.0193  325  PRO H CD  
22670 N  N   . CYS H  328 ? 3.0271 2.0540 2.0257 0.5944  -0.2472 -0.0066 326  CYS H N   
22671 C  CA  . CYS H  328 ? 3.1345 2.1441 2.0861 0.5407  -0.2656 0.0059  326  CYS H CA  
22672 C  C   . CYS H  328 ? 3.1240 2.2607 2.2017 0.5356  -0.2669 0.0314  326  CYS H C   
22673 O  O   . CYS H  328 ? 3.1423 2.3515 2.3102 0.5873  -0.2411 0.0167  326  CYS H O   
22674 C  CB  . CYS H  328 ? 3.2501 2.1644 2.0875 0.5640  -0.2449 -0.0383 326  CYS H CB  
22675 S  SG  . CYS H  328 ? 3.4822 2.2154 2.1444 0.5710  -0.2315 -0.0660 326  CYS H SG  
22676 N  N   . CYS H  329 ? 3.1364 2.2961 2.2115 0.4685  -0.2959 0.0722  327  CYS H N   
22677 C  CA  . CYS H  329 ? 3.1352 2.4095 2.3233 0.4588  -0.2975 0.1066  327  CYS H CA  
22678 C  C   . CYS H  329 ? 3.0445 2.3055 2.1990 0.4781  -0.2825 0.0684  327  CYS H C   
22679 O  O   . CYS H  329 ? 3.1531 2.3861 2.2418 0.4289  -0.3015 0.0763  327  CYS H O   
22680 C  CB  . CYS H  329 ? 3.3086 2.6247 2.5088 0.3778  -0.3369 0.1756  327  CYS H CB  
22681 S  SG  . CYS H  329 ? 3.3475 2.8165 2.7017 0.3635  -0.3392 0.2433  327  CYS H SG  
22682 N  N   . VAL H  330 ? 2.9442 2.2287 2.1406 0.5466  -0.2483 0.0280  328  VAL H N   
22683 C  CA  . VAL H  330 ? 2.9640 2.2383 2.1270 0.5741  -0.2300 -0.0115 328  VAL H CA  
22684 C  C   . VAL H  330 ? 2.8468 2.2288 2.1255 0.5892  -0.2159 -0.0007 328  VAL H C   
22685 O  O   . VAL H  330 ? 2.7738 2.2229 2.1531 0.6019  -0.2052 0.0222  328  VAL H O   
22686 C  CB  . VAL H  330 ? 3.1198 2.3410 2.2289 0.6377  -0.2013 -0.0616 328  VAL H CB  
22687 C  CG1 . VAL H  330 ? 3.3008 2.3942 2.2792 0.6250  -0.2078 -0.0723 328  VAL H CG1 
22688 C  CG2 . VAL H  330 ? 3.0095 2.2965 2.2105 0.6821  -0.1829 -0.0646 328  VAL H CG2 
22689 N  N   . PRO H  331 ? 2.8581 2.2515 2.1203 0.5878  -0.2112 -0.0163 329  PRO H N   
22690 C  CA  . PRO H  331 ? 2.7250 2.2107 2.0880 0.6026  -0.1943 -0.0089 329  PRO H CA  
22691 C  C   . PRO H  331 ? 2.6984 2.2145 2.1000 0.6607  -0.1604 -0.0454 329  PRO H C   
22692 O  O   . PRO H  331 ? 2.6582 2.1377 1.9993 0.6958  -0.1487 -0.0844 329  PRO H O   
22693 C  CB  . PRO H  331 ? 2.8239 2.2997 2.1365 0.5822  -0.2011 -0.0204 329  PRO H CB  
22694 C  CG  . PRO H  331 ? 2.9729 2.3449 2.1546 0.5870  -0.2023 -0.0562 329  PRO H CG  
22695 C  CD  . PRO H  331 ? 3.0258 2.3406 2.1698 0.5669  -0.2189 -0.0389 329  PRO H CD  
22696 N  N   . GLN H  332 ? 2.6700 2.2531 2.1693 0.6684  -0.1415 -0.0282 330  GLN H N   
22697 C  CA  . GLN H  332 ? 2.6869 2.3026 2.2181 0.7076  -0.1093 -0.0591 330  GLN H CA  
22698 C  C   . GLN H  332 ? 2.5174 2.1787 2.0677 0.7137  -0.0920 -0.0772 330  GLN H C   
22699 O  O   . GLN H  332 ? 2.6567 2.3332 2.1819 0.7408  -0.0775 -0.1136 330  GLN H O   
22700 C  CB  . GLN H  332 ? 2.7072 2.3479 2.3140 0.7093  -0.0898 -0.0348 330  GLN H CB  
22701 C  CG  . GLN H  332 ? 2.6890 2.3510 2.3093 0.7373  -0.0573 -0.0676 330  GLN H CG  
22702 C  CD  . GLN H  332 ? 2.4239 2.0903 2.1003 0.7367  -0.0323 -0.0471 330  GLN H CD  
22703 O  OE1 . GLN H  332 ? 2.4753 2.1388 2.1941 0.7220  -0.0366 -0.0033 330  GLN H OE1 
22704 N  NE2 . GLN H  332 ? 2.1607 1.8374 1.8348 0.7500  -0.0046 -0.0753 330  GLN H NE2 
22705 N  N   . ALA H  333 ? 2.2098 1.8998 1.8051 0.6879  -0.0936 -0.0477 331  ALA H N   
22706 C  CA  . ALA H  333 ? 2.1684 1.8988 1.7833 0.6891  -0.0767 -0.0612 331  ALA H CA  
22707 C  C   . ALA H  333 ? 2.4805 2.2064 2.0623 0.6632  -0.1015 -0.0515 331  ALA H C   
22708 O  O   . ALA H  333 ? 2.8064 2.5278 2.4008 0.6299  -0.1242 -0.0090 331  ALA H O   
22709 C  CB  . ALA H  333 ? 2.0865 1.8501 1.7846 0.6842  -0.0463 -0.0335 331  ALA H CB  
22710 N  N   . LEU H  334 ? 2.4990 2.2323 2.0374 0.6747  -0.0973 -0.0872 332  LEU H N   
22711 C  CA  . LEU H  334 ? 2.4745 2.1983 1.9700 0.6502  -0.1162 -0.0849 332  LEU H CA  
22712 C  C   . LEU H  334 ? 2.5147 2.2917 2.0389 0.6521  -0.0992 -0.0971 332  LEU H C   
22713 O  O   . LEU H  334 ? 2.4791 2.2907 2.0283 0.6751  -0.0735 -0.1196 332  LEU H O   
22714 C  CB  . LEU H  334 ? 2.5702 2.2317 1.9616 0.6627  -0.1250 -0.1165 332  LEU H CB  
22715 C  CG  . LEU H  334 ? 2.6911 2.2773 2.0247 0.6479  -0.1450 -0.1047 332  LEU H CG  
22716 C  CD1 . LEU H  334 ? 2.5883 2.1633 1.9338 0.6838  -0.1327 -0.1154 332  LEU H CD1 
22717 C  CD2 . LEU H  334 ? 2.8977 2.4030 2.1122 0.6408  -0.1508 -0.1272 332  LEU H CD2 
22718 N  N   . GLU H  335 ? 2.7988 2.5822 2.3126 0.6208  -0.1152 -0.0808 333  GLU H N   
22719 C  CA  . GLU H  335 ? 2.8600 2.6912 2.3992 0.6162  -0.1025 -0.0872 333  GLU H CA  
22720 C  C   . GLU H  335 ? 3.0375 2.8527 2.5021 0.6049  -0.1160 -0.1080 333  GLU H C   
22721 O  O   . GLU H  335 ? 3.1313 2.9003 2.5408 0.5760  -0.1408 -0.0948 333  GLU H O   
22722 C  CB  . GLU H  335 ? 2.7872 2.6526 2.4060 0.5884  -0.1020 -0.0355 333  GLU H CB  
22723 C  CG  . GLU H  335 ? 2.8081 2.6825 2.5001 0.6039  -0.0757 -0.0131 333  GLU H CG  
22724 C  CD  . GLU H  335 ? 2.8460 2.7521 2.6196 0.5872  -0.0644 0.0451  333  GLU H CD  
22725 O  OE1 . GLU H  335 ? 2.7745 2.7058 2.5525 0.5624  -0.0787 0.0660  333  GLU H OE1 
22726 O  OE2 . GLU H  335 ? 2.9367 2.8416 2.7698 0.6008  -0.0377 0.0733  333  GLU H OE2 
22727 N  N   . PRO H  336 ? 3.0613 2.9117 2.5159 0.6225  -0.0986 -0.1391 334  PRO H N   
22728 C  CA  . PRO H  336 ? 2.9714 2.8062 2.3537 0.6167  -0.1046 -0.1594 334  PRO H CA  
22729 C  C   . PRO H  336 ? 3.0039 2.8510 2.3974 0.5683  -0.1238 -0.1300 334  PRO H C   
22730 O  O   . PRO H  336 ? 3.0027 2.8854 2.4718 0.5468  -0.1275 -0.0921 334  PRO H O   
22731 C  CB  . PRO H  336 ? 2.9449 2.8360 2.3328 0.6502  -0.0789 -0.1924 334  PRO H CB  
22732 C  CG  . PRO H  336 ? 3.0059 2.9465 2.4749 0.6467  -0.0650 -0.1812 334  PRO H CG  
22733 C  CD  . PRO H  336 ? 3.1093 3.0143 2.6104 0.6439  -0.0710 -0.1562 334  PRO H CD  
22734 N  N   . LEU H  337 ? 3.0586 2.8739 2.3728 0.5525  -0.1321 -0.1448 335  LEU H N   
22735 C  CA  . LEU H  337 ? 3.2021 3.0254 2.5096 0.4992  -0.1544 -0.1170 335  LEU H CA  
22736 C  C   . LEU H  337 ? 3.2651 3.1002 2.5236 0.5025  -0.1430 -0.1479 335  LEU H C   
22737 O  O   . LEU H  337 ? 3.3836 3.1643 2.5502 0.5220  -0.1308 -0.1821 335  LEU H O   
22738 C  CB  . LEU H  337 ? 3.2874 3.0421 2.5255 0.4521  -0.1840 -0.0940 335  LEU H CB  
22739 C  CG  . LEU H  337 ? 3.2645 3.0287 2.4792 0.3863  -0.2114 -0.0623 335  LEU H CG  
22740 C  CD1 . LEU H  337 ? 3.1792 3.0332 2.5155 0.3683  -0.2209 -0.0074 335  LEU H CD1 
22741 C  CD2 . LEU H  337 ? 3.3763 3.0653 2.4977 0.3287  -0.2408 -0.0434 335  LEU H CD2 
22742 N  N   . PRO H  338 ? 3.1924 3.0921 2.5052 0.4865  -0.1422 -0.1354 336  PRO H N   
22743 C  CA  . PRO H  338 ? 3.2199 3.1335 2.4844 0.4824  -0.1345 -0.1606 336  PRO H CA  
22744 C  C   . PRO H  338 ? 3.3908 3.2610 2.5852 0.4256  -0.1600 -0.1441 336  PRO H C   
22745 O  O   . PRO H  338 ? 3.4562 3.3290 2.6773 0.3778  -0.1886 -0.0978 336  PRO H O   
22746 C  CB  . PRO H  338 ? 3.1390 3.1340 2.4901 0.4809  -0.1249 -0.1494 336  PRO H CB  
22747 C  CG  . PRO H  338 ? 3.0814 3.0883 2.5139 0.4620  -0.1355 -0.1008 336  PRO H CG  
22748 C  CD  . PRO H  338 ? 3.0945 3.0532 2.5141 0.4786  -0.1400 -0.0992 336  PRO H CD  
22749 N  N   . ILE H  339 ? 3.4823 3.3152 2.5832 0.4292  -0.1474 -0.1786 337  ILE H N   
22750 C  CA  . ILE H  339 ? 3.6159 3.3895 2.6214 0.3709  -0.1658 -0.1720 337  ILE H CA  
22751 C  C   . ILE H  339 ? 3.7235 3.5261 2.7001 0.3675  -0.1524 -0.1930 337  ILE H C   
22752 O  O   . ILE H  339 ? 3.6719 3.5252 2.6785 0.4179  -0.1246 -0.2199 337  ILE H O   
22753 C  CB  . ILE H  339 ? 3.7045 3.3553 2.5808 0.3711  -0.1568 -0.1960 337  ILE H CB  
22754 C  CG1 . ILE H  339 ? 3.6509 3.2724 2.4756 0.4445  -0.1099 -0.2451 337  ILE H CG1 
22755 C  CG2 . ILE H  339 ? 3.7471 3.3704 2.6485 0.3667  -0.1740 -0.1724 337  ILE H CG2 
22756 C  CD1 . ILE H  339 ? 3.7413 3.2243 2.4263 0.4530  -0.0884 -0.2696 337  ILE H CD1 
22757 N  N   . VAL H  340 ? 3.8199 3.5947 2.7343 0.3015  -0.1742 -0.1773 338  VAL H N   
22758 C  CA  . VAL H  340 ? 3.6414 3.4346 2.5155 0.2870  -0.1646 -0.1946 338  VAL H CA  
22759 C  C   . VAL H  340 ? 3.6055 3.2882 2.3264 0.2350  -0.1668 -0.2073 338  VAL H C   
22760 O  O   . VAL H  340 ? 3.6280 3.2803 2.3151 0.1611  -0.2031 -0.1722 338  VAL H O   
22761 C  CB  . VAL H  340 ? 3.4735 3.3640 2.4432 0.2477  -0.1902 -0.1539 338  VAL H CB  
22762 C  CG1 . VAL H  340 ? 3.4836 3.3832 2.3964 0.2212  -0.1850 -0.1699 338  VAL H CG1 
22763 C  CG2 . VAL H  340 ? 3.3947 3.3723 2.4922 0.2972  -0.1767 -0.1487 338  VAL H CG2 
22764 N  N   . TYR H  341 ? 3.6720 3.2943 2.2954 0.2708  -0.1255 -0.2538 339  TYR H N   
22765 C  CA  . TYR H  341 ? 3.8920 3.3863 2.3480 0.2248  -0.1140 -0.2735 339  TYR H CA  
22766 C  C   . TYR H  341 ? 4.0404 3.5343 2.4416 0.2518  -0.0744 -0.3080 339  TYR H C   
22767 O  O   . TYR H  341 ? 3.9236 3.5076 2.4069 0.3187  -0.0507 -0.3206 339  TYR H O   
22768 C  CB  . TYR H  341 ? 4.0380 3.3980 2.3883 0.2487  -0.0883 -0.2962 339  TYR H CB  
22769 C  CG  . TYR H  341 ? 4.0389 3.3868 2.3882 0.3536  -0.0311 -0.3331 339  TYR H CG  
22770 C  CD1 . TYR H  341 ? 3.8263 3.2658 2.3043 0.4199  -0.0300 -0.3263 339  TYR H CD1 
22771 C  CD2 . TYR H  341 ? 4.2044 3.4508 2.4220 0.3858  0.0248  -0.3699 339  TYR H CD2 
22772 C  CE1 . TYR H  341 ? 3.7680 3.2141 2.2504 0.5110  0.0185  -0.3503 339  TYR H CE1 
22773 C  CE2 . TYR H  341 ? 4.1792 3.4304 2.4065 0.4868  0.0792  -0.3914 339  TYR H CE2 
22774 C  CZ  . TYR H  341 ? 3.9478 3.3069 2.3110 0.5469  0.0725  -0.3792 339  TYR H CZ  
22775 O  OH  . TYR H  341 ? 3.9001 3.2808 2.2777 0.6426  0.1230  -0.3915 339  TYR H OH  
22776 N  N   . TYR H  342 ? 4.1172 3.5090 2.3724 0.1941  -0.0666 -0.3213 340  TYR H N   
22777 C  CA  . TYR H  342 ? 4.0723 3.4477 2.2565 0.2123  -0.0254 -0.3527 340  TYR H CA  
22778 C  C   . TYR H  342 ? 4.0819 3.3038 2.1118 0.2589  0.0405  -0.3946 340  TYR H C   
22779 O  O   . TYR H  342 ? 4.0592 3.1567 1.9976 0.2460  0.0472  -0.4001 340  TYR H O   
22780 C  CB  . TYR H  342 ? 4.2133 3.5820 2.3366 0.1123  -0.0568 -0.3375 340  TYR H CB  
22781 C  CG  . TYR H  342 ? 4.1057 3.6349 2.3776 0.0886  -0.1003 -0.3011 340  TYR H CG  
22782 C  CD1 . TYR H  342 ? 4.0216 3.6356 2.3414 0.1245  -0.0793 -0.3157 340  TYR H CD1 
22783 C  CD2 . TYR H  342 ? 4.0885 3.6826 2.4497 0.0307  -0.1586 -0.2479 340  TYR H CD2 
22784 C  CE1 . TYR H  342 ? 3.9151 3.6604 2.3587 0.1010  -0.1147 -0.2833 340  TYR H CE1 
22785 C  CE2 . TYR H  342 ? 3.9811 3.7082 2.4723 0.0145  -0.1895 -0.2111 340  TYR H CE2 
22786 C  CZ  . TYR H  342 ? 3.9153 3.7106 2.4424 0.0484  -0.1672 -0.2315 340  TYR H CZ  
22787 O  OH  . TYR H  342 ? 3.8592 3.7730 2.5053 0.0309  -0.1939 -0.1959 340  TYR H OH  
22788 N  N   . VAL H  343 ? 3.9870 3.2176 1.9874 0.3153  0.0932  -0.4210 341  VAL H N   
22789 C  CA  . VAL H  343 ? 4.1058 3.1918 1.9595 0.3707  0.1697  -0.4561 341  VAL H CA  
22790 C  C   . VAL H  343 ? 4.3093 3.3375 2.0445 0.3432  0.2057  -0.4777 341  VAL H C   
22791 O  O   . VAL H  343 ? 4.3220 3.1999 1.8917 0.2655  0.2112  -0.4911 341  VAL H O   
22792 C  CB  . VAL H  343 ? 3.8171 2.9754 1.7586 0.4956  0.2168  -0.4605 341  VAL H CB  
22793 C  CG1 . VAL H  343 ? 3.9362 2.9416 1.7283 0.5610  0.3035  -0.4876 341  VAL H CG1 
22794 C  CG2 . VAL H  343 ? 3.7393 2.9526 1.7923 0.5186  0.1820  -0.4407 341  VAL H CG2 
22795 N  N   . ARG H  345 ? 3.8513 3.1580 1.7156 0.3983  0.2432  -0.4835 343  ARG H N   
22796 C  CA  . ARG H  345 ? 3.7853 3.2463 1.7638 0.3523  0.1909  -0.4639 343  ARG H CA  
22797 C  C   . ARG H  345 ? 3.6644 3.2921 1.8336 0.3906  0.1530  -0.4385 343  ARG H C   
22798 O  O   . ARG H  345 ? 3.6286 3.3797 1.9017 0.3551  0.1096  -0.4191 343  ARG H O   
22799 C  CB  . ARG H  345 ? 3.7939 3.2961 1.7413 0.3775  0.2352  -0.4784 343  ARG H CB  
22800 C  CG  . ARG H  345 ? 3.7826 3.3563 1.7810 0.4963  0.2981  -0.4824 343  ARG H CG  
22801 C  CD  . ARG H  345 ? 3.8874 3.5081 1.8545 0.5172  0.3423  -0.4912 343  ARG H CD  
22802 N  NE  . ARG H  345 ? 4.0751 3.5212 1.8534 0.4755  0.3837  -0.5178 343  ARG H NE  
22803 C  CZ  . ARG H  345 ? 4.2607 3.5645 1.9045 0.5361  0.4691  -0.5381 343  ARG H CZ  
22804 N  NH1 . ARG H  345 ? 4.2194 3.5489 1.9095 0.6464  0.5196  -0.5291 343  ARG H NH1 
22805 N  NH2 . ARG H  345 ? 4.5456 3.6774 2.0036 0.4853  0.5073  -0.5647 343  ARG H NH2 
22806 N  N   . LYS H  346 ? 3.6599 3.2818 1.8662 0.4606  0.1725  -0.4385 344  LYS H N   
22807 C  CA  . LYS H  346 ? 3.5198 3.2890 1.8893 0.5027  0.1482  -0.4186 344  LYS H CA  
22808 C  C   . LYS H  346 ? 3.6030 3.3488 2.0215 0.4681  0.0994  -0.4008 344  LYS H C   
22809 O  O   . LYS H  346 ? 3.5580 3.2005 1.9174 0.4903  0.1153  -0.4077 344  LYS H O   
22810 C  CB  . LYS H  346 ? 3.4298 3.2381 1.8211 0.6090  0.2049  -0.4238 344  LYS H CB  
22811 C  CG  . LYS H  346 ? 3.5917 3.4259 1.9343 0.6546  0.2628  -0.4341 344  LYS H CG  
22812 C  CD  . LYS H  346 ? 3.6532 3.5554 2.0372 0.7632  0.3177  -0.4244 344  LYS H CD  
22813 C  CE  . LYS H  346 ? 3.7353 3.6436 2.0554 0.8151  0.3862  -0.4287 344  LYS H CE  
22814 N  NZ  . LYS H  346 ? 3.5890 3.6265 1.9636 0.7762  0.3641  -0.4241 344  LYS H NZ  
22815 N  N   . PRO H  347 ? 3.6511 3.4856 2.1741 0.4166  0.0444  -0.3753 345  PRO H N   
22816 C  CA  . PRO H  347 ? 3.5139 3.3405 2.0981 0.3933  0.0039  -0.3520 345  PRO H CA  
22817 C  C   . PRO H  347 ? 3.4892 3.3851 2.1698 0.4651  0.0161  -0.3510 345  PRO H C   
22818 O  O   . PRO H  347 ? 3.4240 3.4372 2.1906 0.4960  0.0227  -0.3493 345  PRO H O   
22819 C  CB  . PRO H  347 ? 3.3830 3.2882 2.0483 0.3244  -0.0462 -0.3199 345  PRO H CB  
22820 C  CG  . PRO H  347 ? 3.3993 3.3980 2.0966 0.3386  -0.0304 -0.3295 345  PRO H CG  
22821 C  CD  . PRO H  347 ? 3.6200 3.5571 2.2030 0.3767  0.0210  -0.3633 345  PRO H CD  
22822 N  N   . LYS H  348 ? 3.6791 3.5014 2.3386 0.4848  0.0180  -0.3510 346  LYS H N   
22823 C  CA  . LYS H  348 ? 3.5832 3.4567 2.3175 0.5510  0.0313  -0.3502 346  LYS H CA  
22824 C  C   . LYS H  348 ? 3.4774 3.3582 2.2873 0.5210  -0.0097 -0.3260 346  LYS H C   
22825 O  O   . LYS H  348 ? 3.5270 3.3154 2.2847 0.4821  -0.0293 -0.3170 346  LYS H O   
22826 C  CB  . LYS H  348 ? 3.6457 3.4278 2.2911 0.6147  0.0790  -0.3696 346  LYS H CB  
22827 C  CG  . LYS H  348 ? 3.6397 3.4184 2.2168 0.6596  0.1319  -0.3874 346  LYS H CG  
22828 C  CD  . LYS H  348 ? 3.6390 3.3330 2.1414 0.7369  0.1883  -0.3981 346  LYS H CD  
22829 C  CE  . LYS H  348 ? 3.6164 3.3133 2.0581 0.7915  0.2500  -0.4081 346  LYS H CE  
22830 N  NZ  . LYS H  348 ? 3.4340 3.3168 1.9891 0.8196  0.2495  -0.3937 346  LYS H NZ  
22831 N  N   . VAL H  349 ? 3.2647 3.2526 2.1905 0.5360  -0.0200 -0.3138 347  VAL H N   
22832 C  CA  . VAL H  349 ? 3.3094 3.3083 2.3135 0.5183  -0.0484 -0.2899 347  VAL H CA  
22833 C  C   . VAL H  349 ? 3.2557 3.2452 2.2719 0.5773  -0.0292 -0.2994 347  VAL H C   
22834 O  O   . VAL H  349 ? 3.1985 3.2650 2.2550 0.6229  -0.0075 -0.3085 347  VAL H O   
22835 C  CB  . VAL H  349 ? 3.3465 3.4450 2.4544 0.4964  -0.0630 -0.2717 347  VAL H CB  
22836 C  CG1 . VAL H  349 ? 3.2565 3.3521 2.4383 0.4815  -0.0832 -0.2435 347  VAL H CG1 
22837 C  CG2 . VAL H  349 ? 3.4577 3.5717 2.5527 0.4436  -0.0788 -0.2608 347  VAL H CG2 
22838 N  N   . GLU H  350 ? 3.2949 3.1959 2.2748 0.5716  -0.0389 -0.2937 348  GLU H N   
22839 C  CA  . GLU H  350 ? 3.2480 3.1264 2.2301 0.6243  -0.0222 -0.3008 348  GLU H CA  
22840 C  C   . GLU H  350 ? 3.2468 3.1167 2.2903 0.6012  -0.0506 -0.2774 348  GLU H C   
22841 O  O   . GLU H  350 ? 3.3287 3.1877 2.3925 0.5453  -0.0811 -0.2521 348  GLU H O   
22842 C  CB  . GLU H  350 ? 3.4315 3.1906 2.2912 0.6496  0.0041  -0.3190 348  GLU H CB  
22843 C  CG  . GLU H  350 ? 3.5263 3.2788 2.3156 0.6812  0.0434  -0.3396 348  GLU H CG  
22844 C  CD  . GLU H  350 ? 3.6369 3.2614 2.3044 0.7227  0.0852  -0.3566 348  GLU H CD  
22845 O  OE1 . GLU H  350 ? 3.6802 3.2928 2.2890 0.7637  0.1294  -0.3702 348  GLU H OE1 
22846 O  OE2 . GLU H  350 ? 3.6681 3.1999 2.2954 0.7159  0.0778  -0.3546 348  GLU H OE2 
22847 N  N   . GLN H  351 ? 3.0949 2.9762 2.1702 0.6458  -0.0389 -0.2809 349  GLN H N   
22848 C  CA  . GLN H  351 ? 3.0141 2.8902 2.1491 0.6325  -0.0589 -0.2602 349  GLN H CA  
22849 C  C   . GLN H  351 ? 3.0103 2.8125 2.0956 0.6676  -0.0487 -0.2685 349  GLN H C   
22850 O  O   . GLN H  351 ? 2.9080 2.7270 1.9805 0.7241  -0.0208 -0.2848 349  GLN H O   
22851 C  CB  . GLN H  351 ? 2.9105 2.8839 2.1458 0.6431  -0.0543 -0.2546 349  GLN H CB  
22852 C  CG  . GLN H  351 ? 2.9387 2.9042 2.2374 0.6280  -0.0681 -0.2310 349  GLN H CG  
22853 C  CD  . GLN H  351 ? 2.8715 2.9106 2.2468 0.6348  -0.0546 -0.2302 349  GLN H CD  
22854 O  OE1 . GLN H  351 ? 2.8235 2.9255 2.2008 0.6518  -0.0379 -0.2484 349  GLN H OE1 
22855 N  NE2 . GLN H  351 ? 2.7892 2.8192 2.2221 0.6182  -0.0592 -0.2065 349  GLN H NE2 
22856 N  N   . LEU H  352 ? 3.1323 2.8585 2.1902 0.6329  -0.0713 -0.2521 350  LEU H N   
22857 C  CA  . LEU H  352 ? 3.2012 2.8439 2.2041 0.6570  -0.0644 -0.2579 350  LEU H CA  
22858 C  C   . LEU H  352 ? 3.1156 2.8048 2.2054 0.6790  -0.0687 -0.2462 350  LEU H C   
22859 O  O   . LEU H  352 ? 3.0617 2.8085 2.2382 0.6525  -0.0856 -0.2239 350  LEU H O   
22860 C  CB  . LEU H  352 ? 3.4033 2.9430 2.3262 0.5982  -0.0890 -0.2438 350  LEU H CB  
22861 C  CG  . LEU H  352 ? 3.6406 3.1079 2.4504 0.5624  -0.0848 -0.2562 350  LEU H CG  
22862 C  CD1 . LEU H  352 ? 3.7530 3.1221 2.4786 0.4905  -0.1137 -0.2374 350  LEU H CD1 
22863 C  CD2 . LEU H  352 ? 3.8068 3.2144 2.5268 0.6232  -0.0365 -0.2920 350  LEU H CD2 
22864 N  N   . SER H  353 ? 3.1855 2.8436 2.2477 0.7284  -0.0492 -0.2591 351  SER H N   
22865 C  CA  . SER H  353 ? 3.0832 2.7801 2.2150 0.7504  -0.0505 -0.2509 351  SER H CA  
22866 C  C   . SER H  353 ? 3.2835 2.8965 2.3877 0.7280  -0.0695 -0.2361 351  SER H C   
22867 O  O   . SER H  353 ? 3.4186 2.9294 2.4237 0.7277  -0.0656 -0.2440 351  SER H O   
22868 C  CB  . SER H  353 ? 2.9243 2.6569 2.0524 0.8167  -0.0200 -0.2661 351  SER H CB  
22869 O  OG  . SER H  353 ? 2.9628 2.6024 1.9920 0.8509  0.0013  -0.2771 351  SER H OG  
22870 N  N   . ASN H  354 ? 3.2779 2.9291 2.4638 0.7078  -0.0863 -0.2135 352  ASN H N   
22871 C  CA  . ASN H  354 ? 3.2471 2.8407 2.4252 0.6867  -0.1053 -0.1931 352  ASN H CA  
22872 C  C   . ASN H  354 ? 3.3327 2.8545 2.4422 0.6283  -0.1311 -0.1751 352  ASN H C   
22873 O  O   . ASN H  354 ? 3.5549 2.9782 2.5536 0.6255  -0.1273 -0.1903 352  ASN H O   
22874 C  CB  . ASN H  354 ? 3.1507 2.6927 2.2817 0.7333  -0.0891 -0.2103 352  ASN H CB  
22875 C  CG  . ASN H  354 ? 3.1071 2.7297 2.3083 0.7790  -0.0701 -0.2188 352  ASN H CG  
22876 O  OD1 . ASN H  354 ? 3.0550 2.7057 2.3194 0.7732  -0.0760 -0.2052 352  ASN H OD1 
22877 N  ND2 . ASN H  354 ? 3.1895 2.8530 2.3770 0.8212  -0.0459 -0.2381 352  ASN H ND2 
22878 N  N   . MET H  355 ? 3.1451 2.7129 2.3142 0.5788  -0.1552 -0.1390 353  MET H N   
22879 C  CA  . MET H  355 ? 3.1565 2.6781 2.2680 0.5111  -0.1860 -0.1111 353  MET H CA  
22880 C  C   . MET H  355 ? 3.0906 2.6584 2.2842 0.4709  -0.2135 -0.0541 353  MET H C   
22881 O  O   . MET H  355 ? 3.1501 2.6700 2.2947 0.4252  -0.2393 -0.0283 353  MET H O   
22882 C  CB  . MET H  355 ? 3.2026 2.7461 2.2928 0.4829  -0.1892 -0.1136 353  MET H CB  
22883 C  CG  . MET H  355 ? 3.2723 2.7638 2.2689 0.5169  -0.1604 -0.1632 353  MET H CG  
22884 S  SD  . MET H  355 ? 3.3123 2.6427 2.1385 0.5068  -0.1522 -0.1868 353  MET H SD  
22885 C  CE  . MET H  355 ? 3.3956 2.6867 2.1592 0.3969  -0.1976 -0.1471 353  MET H CE  
22886 N  N   . ILE H  356 ? 2.9689 2.6275 2.2827 0.4864  -0.2048 -0.0311 354  ILE H N   
22887 C  CA  . ILE H  356 ? 2.9270 2.6406 2.3338 0.4589  -0.2203 0.0317  354  ILE H CA  
22888 C  C   . ILE H  356 ? 3.0571 2.7620 2.5023 0.4915  -0.2087 0.0332  354  ILE H C   
22889 O  O   . ILE H  356 ? 3.1065 2.8265 2.5890 0.5417  -0.1780 0.0028  354  ILE H O   
22890 C  CB  . ILE H  356 ? 2.8123 2.6103 2.3221 0.4646  -0.2057 0.0582  354  ILE H CB  
22891 C  CG1 . ILE H  356 ? 2.9511 2.7660 2.4301 0.4217  -0.2241 0.0699  354  ILE H CG1 
22892 C  CG2 . ILE H  356 ? 2.7303 2.5825 2.3475 0.4579  -0.2051 0.1248  354  ILE H CG2 
22893 C  CD1 . ILE H  356 ? 2.9535 2.7533 2.3791 0.4471  -0.2049 0.0103  354  ILE H CD1 
22894 N  N   . VAL H  357 ? 3.0555 2.7403 2.4890 0.4569  -0.2342 0.0712  355  VAL H N   
22895 C  CA  . VAL H  357 ? 2.8853 2.5616 2.3529 0.4812  -0.2264 0.0784  355  VAL H CA  
22896 C  C   . VAL H  357 ? 2.7239 2.4822 2.3223 0.4865  -0.2141 0.1352  355  VAL H C   
22897 O  O   . VAL H  357 ? 2.7433 2.5517 2.3874 0.4447  -0.2351 0.2005  355  VAL H O   
22898 C  CB  . VAL H  357 ? 3.0917 2.7036 2.4771 0.4389  -0.2581 0.0932  355  VAL H CB  
22899 C  CG1 . VAL H  357 ? 2.9941 2.6134 2.4313 0.4578  -0.2531 0.1129  355  VAL H CG1 
22900 C  CG2 . VAL H  357 ? 3.3662 2.8733 2.6132 0.4467  -0.2548 0.0332  355  VAL H CG2 
22901 N  N   . ARG H  358 ? 2.7854 2.5566 2.4403 0.5366  -0.1770 0.1148  356  ARG H N   
22902 C  CA  . ARG H  358 ? 2.6679 2.4957 2.4364 0.5501  -0.1502 0.1638  356  ARG H CA  
22903 C  C   . ARG H  358 ? 2.6408 2.4637 2.4387 0.5523  -0.1522 0.1957  356  ARG H C   
22904 O  O   . ARG H  358 ? 2.6517 2.5162 2.4985 0.5227  -0.1700 0.2657  356  ARG H O   
22905 C  CB  . ARG H  358 ? 2.5794 2.4122 2.3776 0.5928  -0.1036 0.1235  356  ARG H CB  
22906 C  CG  . ARG H  358 ? 2.6662 2.5335 2.5644 0.6088  -0.0626 0.1686  356  ARG H CG  
22907 C  CD  . ARG H  358 ? 2.7247 2.6452 2.6824 0.5857  -0.0677 0.2321  356  ARG H CD  
22908 N  NE  . ARG H  358 ? 2.7535 2.6800 2.6845 0.5805  -0.0653 0.2010  356  ARG H NE  
22909 C  CZ  . ARG H  358 ? 2.8258 2.7961 2.8031 0.5639  -0.0648 0.2467  356  ARG H CZ  
22910 N  NH1 . ARG H  358 ? 2.7661 2.7859 2.8244 0.5531  -0.0656 0.3316  356  ARG H NH1 
22911 N  NH2 . ARG H  358 ? 2.8580 2.8303 2.8043 0.5586  -0.0631 0.2130  356  ARG H NH2 
22912 N  N   . SER H  359 ? 2.5525 2.3332 2.3223 0.5853  -0.1354 0.1496  357  SER H N   
22913 C  CA  . SER H  359 ? 2.5586 2.3303 2.3524 0.5914  -0.1333 0.1722  357  SER H CA  
22914 C  C   . SER H  359 ? 2.7608 2.4698 2.4573 0.5781  -0.1661 0.1429  357  SER H C   
22915 O  O   . SER H  359 ? 2.8717 2.5352 2.4804 0.5757  -0.1795 0.0982  357  SER H O   
22916 C  CB  . SER H  359 ? 2.5217 2.2893 2.3569 0.6355  -0.0844 0.1467  357  SER H CB  
22917 O  OG  . SER H  359 ? 2.5434 2.3026 2.4030 0.6414  -0.0799 0.1695  357  SER H OG  
22918 N  N   . CYS H  360 ? 2.7931 2.4949 2.5033 0.5714  -0.1741 0.1709  358  CYS H N   
22919 C  CA  . CYS H  360 ? 2.7748 2.4078 2.3928 0.5589  -0.2005 0.1479  358  CYS H CA  
22920 C  C   . CYS H  360 ? 2.6326 2.2549 2.2775 0.5905  -0.1803 0.1397  358  CYS H C   
22921 O  O   . CYS H  360 ? 2.5592 2.2298 2.2932 0.5966  -0.1615 0.1822  358  CYS H O   
22922 C  CB  . CYS H  360 ? 2.9737 2.6036 2.5571 0.4939  -0.2453 0.2003  358  CYS H CB  
22923 S  SG  . CYS H  360 ? 3.0040 2.6468 2.5442 0.4392  -0.2749 0.2187  358  CYS H SG  
22924 N  N   . LYS H  361 ? 2.7450 2.3035 2.3124 0.6126  -0.1808 0.0885  359  LYS H N   
22925 C  CA  . LYS H  361 ? 2.8128 2.3568 2.3921 0.6401  -0.1650 0.0763  359  LYS H CA  
22926 C  C   . LYS H  361 ? 2.9002 2.3696 2.3878 0.6248  -0.1930 0.0681  359  LYS H C   
22927 O  O   . LYS H  361 ? 2.9716 2.3875 2.3735 0.5954  -0.2184 0.0635  359  LYS H O   
22928 C  CB  . LYS H  361 ? 2.7603 2.3088 2.3405 0.6873  -0.1316 0.0239  359  LYS H CB  
22929 C  CG  . LYS H  361 ? 2.9159 2.4236 2.4087 0.7059  -0.1377 -0.0235 359  LYS H CG  
22930 C  CD  . LYS H  361 ? 2.8508 2.3860 2.3514 0.7472  -0.1085 -0.0639 359  LYS H CD  
22931 C  CE  . LYS H  361 ? 2.6854 2.1944 2.1097 0.7723  -0.1104 -0.0994 359  LYS H CE  
22932 N  NZ  . LYS H  361 ? 2.5472 2.1044 1.9830 0.8078  -0.0861 -0.1284 359  LYS H NZ  
22933 N  N   . CYS H  362 ? 2.8556 2.3122 2.3528 0.6423  -0.1849 0.0654  360  CYS H N   
22934 C  CA  . CYS H  362 ? 2.9863 2.3639 2.3939 0.6374  -0.2036 0.0514  360  CYS H CA  
22935 C  C   . CYS H  362 ? 3.0621 2.4212 2.4501 0.6910  -0.1790 0.0045  360  CYS H C   
22936 O  O   . CYS H  362 ? 3.1944 2.5951 2.6453 0.7117  -0.1578 0.0045  360  CYS H O   
22937 C  CB  . CYS H  362 ? 3.0189 2.4028 2.4518 0.6044  -0.2214 0.0984  360  CYS H CB  
22938 S  SG  . CYS H  362 ? 3.1055 2.5457 2.5822 0.5354  -0.2534 0.1757  360  CYS H SG  
22939 N  N   . SER H  363 ? 2.9361 2.2338 2.2347 0.7123  -0.1789 -0.0311 361  SER H N   
22940 C  CA  . SER H  363 ? 2.9543 2.2490 2.2370 0.7646  -0.1569 -0.0651 361  SER H CA  
22941 C  C   . SER H  363 ? 3.2642 2.4602 2.4330 0.7839  -0.1595 -0.0842 361  SER H C   
22942 O  O   . SER H  363 ? 3.4332 2.5478 2.5201 0.7524  -0.1758 -0.0786 361  SER H O   
22943 C  CB  . SER H  363 ? 2.7880 2.1524 2.1139 0.7931  -0.1335 -0.0877 361  SER H CB  
22944 O  OG  . SER H  363 ? 2.7658 2.1121 2.0503 0.7877  -0.1373 -0.0971 361  SER H OG  
22945 O  OXT . SER H  363 ? 3.3150 2.5070 2.4663 0.8305  -0.1421 -0.1027 361  SER H OXT 
23236 MN MN  . MN  JA .   ? 2.5923 1.9275 2.3751 0.0816  -1.0792 0.3436  2001 MN  B MN  
23237 MN MN  . MN  KA .   ? 1.6649 1.2528 1.2734 0.1088  -0.6498 0.4307  2002 MN  B MN  
23238 MN MN  . MN  LA .   ? 2.0948 1.8627 1.5378 0.1216  -0.3500 0.4547  2003 MN  B MN  
23239 C  C1  . NAG MA .   ? 2.2393 2.3394 5.0441 -0.2565 0.8592  -0.5018 2004 NAG B C1  
23240 C  C2  . NAG MA .   ? 2.3062 2.3697 5.3346 -0.2164 0.8556  -0.4798 2004 NAG B C2  
23241 C  C3  . NAG MA .   ? 2.2832 2.2679 5.2541 -0.2188 0.9010  -0.4776 2004 NAG B C3  
23242 C  C4  . NAG MA .   ? 2.4145 2.3482 5.3065 -0.2449 0.9870  -0.5423 2004 NAG B C4  
23243 C  C5  . NAG MA .   ? 2.3216 2.3002 5.0017 -0.2821 0.9732  -0.5609 2004 NAG B C5  
23244 C  C6  . NAG MA .   ? 2.2360 2.1638 4.8495 -0.3077 1.0514  -0.6269 2004 NAG B C6  
23245 C  C7  . NAG MA .   ? 2.1323 2.2762 5.4497 -0.1611 0.7280  -0.4096 2004 NAG B C7  
23246 C  C8  . NAG MA .   ? 2.0644 2.2520 5.4095 -0.1413 0.6281  -0.3482 2004 NAG B C8  
23247 N  N2  . NAG MA .   ? 2.2693 2.3812 5.3546 -0.1945 0.7673  -0.4208 2004 NAG B N2  
23248 O  O3  . NAG MA .   ? 2.3697 2.3101 5.5725 -0.1794 0.9093  -0.4575 2004 NAG B O3  
23249 O  O4  . NAG MA .   ? 2.5245 2.3982 5.3304 -0.2540 1.0235  -0.5395 2004 NAG B O4  
23250 O  O5  . NAG MA .   ? 2.3699 2.4153 5.1255 -0.2766 0.9399  -0.5593 2004 NAG B O5  
23251 O  O6  . NAG MA .   ? 2.2109 2.1801 4.6964 -0.3341 1.0407  -0.6448 2004 NAG B O6  
23252 O  O7  . NAG MA .   ? 1.7625 1.9038 5.2578 -0.1486 0.7663  -0.4472 2004 NAG B O7  
23643 MN MN  . MN  WB .   ? 2.5939 2.0684 3.5873 0.3529  0.1274  0.4798  2001 MN  F MN  
23644 MN MN  . MN  XB .   ? 2.6490 2.3016 3.9279 0.2567  -0.0463 0.4364  2002 MN  F MN  
23645 MN MN  . MN  YB .   ? 2.1415 2.0786 3.9064 0.2159  -0.1391 0.4450  2003 MN  F MN  
23646 C  C1  . NAG ZB .   ? 4.3520 3.0635 2.9517 -0.3400 -0.8069 0.9451  2004 NAG F C1  
23647 C  C2  . NAG ZB .   ? 4.3219 3.1575 2.8606 -0.3025 -0.8770 0.9880  2004 NAG F C2  
23648 C  C3  . NAG ZB .   ? 4.4559 3.2302 2.9465 -0.2455 -0.8895 1.1169  2004 NAG F C3  
23649 C  C4  . NAG ZB .   ? 4.3700 3.0241 2.9763 -0.2000 -0.8756 1.1422  2004 NAG F C4  
23650 C  C5  . NAG ZB .   ? 4.3768 2.9151 3.0443 -0.2460 -0.8057 1.0830  2004 NAG F C5  
23651 C  C6  . NAG ZB .   ? 4.3433 2.7747 3.1303 -0.2035 -0.7929 1.0860  2004 NAG F C6  
23652 C  C7  . NAG ZB .   ? 4.1580 3.2350 2.6035 -0.3628 -0.9254 0.8777  2004 NAG F C7  
23653 C  C8  . NAG ZB .   ? 4.2421 3.4137 2.5684 -0.4099 -0.9239 0.8481  2004 NAG F C8  
23654 N  N2  . NAG ZB .   ? 4.3080 3.2485 2.7394 -0.3481 -0.8830 0.9576  2004 NAG F N2  
23655 O  O3  . NAG ZB .   ? 4.4850 3.3878 2.9317 -0.2028 -0.9628 1.1520  2004 NAG F O3  
23656 O  O4  . NAG ZB .   ? 4.4805 3.0569 3.0443 -0.1505 -0.8754 1.2654  2004 NAG F O4  
23657 O  O5  . NAG ZB .   ? 4.3183 2.9337 3.0202 -0.2934 -0.8028 0.9673  2004 NAG F O5  
23658 O  O6  . NAG ZB .   ? 4.2839 2.6624 3.1440 -0.2436 -0.7477 0.9950  2004 NAG F O6  
23659 O  O7  . NAG ZB .   ? 4.0457 3.1677 2.5986 -0.3394 -0.9602 0.8300  2004 NAG F O7  
# 
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   PHE 1   1   1   PHE PHE A . n 
A 1 2   ASN 2   2   2   ASN ASN A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   ASP 4   4   4   ASP ASP A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   ASP 6   6   6   ASP ASP A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  GLU 10  10  10  GLU GLU A . n 
A 1 11  TYR 11  11  11  TYR TYR A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  SER 17  17  17  SER SER A . n 
A 1 18  TYR 18  18  18  TYR TYR A . n 
A 1 19  PHE 19  19  19  PHE PHE A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  VAL 23  23  23  VAL VAL A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  PHE 25  25  25  PHE PHE A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  MET 34  34  34  MET MET A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  PRO 41  41  41  PRO PRO A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  THR 46  46  46  THR THR A . n 
A 1 47  GLN 47  47  47  GLN GLN A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  CYS 59  59  59  CYS CYS A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  TRP 61  61  61  TRP TRP A . n 
A 1 62  SER 62  62  ?   ?   ?   A . n 
A 1 63  SER 63  63  ?   ?   ?   A . n 
A 1 64  THR 64  64  ?   ?   ?   A . n 
A 1 65  ARG 65  65  65  ARG ARG A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  CYS 67  67  67  CYS CYS A . n 
A 1 68  GLN 68  68  68  GLN GLN A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  PHE 72  72  72  PHE PHE A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  ARG 78  78  78  ARG ARG A . n 
A 1 79  ASP 79  79  79  ASP ASP A . n 
A 1 80  TYR 80  80  80  TYR TYR A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  PHE 88  88  88  PHE PHE A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  TRP 93  93  93  TRP TRP A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 GLN 102 102 102 GLN GLN A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 CYS 108 108 108 CYS CYS A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 PRO 110 110 110 PRO PRO A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 TYR 112 112 112 TYR TYR A . n 
A 1 113 HIS 113 113 113 HIS HIS A . n 
A 1 114 TRP 114 114 114 TRP TRP A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 MET 118 118 118 MET MET A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 GLN 120 120 120 GLN GLN A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 GLY 126 126 126 GLY GLY A . n 
A 1 127 THR 127 127 127 THR THR A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 PHE 129 129 129 PHE PHE A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 THR 136 136 136 THR THR A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 TYR 139 139 139 TYR TYR A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 CYS 142 142 142 CYS CYS A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 GLN 145 145 145 GLN GLN A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 ILE 147 147 147 ILE ILE A . n 
A 1 148 ASP 148 148 148 ASP ASP A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 GLN 152 152 152 GLN GLN A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 PHE 154 154 154 PHE PHE A . n 
A 1 155 CYS 155 155 155 CYS CYS A . n 
A 1 156 GLN 156 156 156 GLN GLN A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 ILE 161 161 161 ILE ILE A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 PHE 163 163 163 PHE PHE A . n 
A 1 164 THR 164 164 164 THR THR A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 TYR 178 178 178 TYR TYR A . n 
A 1 179 TRP 179 179 179 TRP TRP A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 GLN 182 182 182 GLN GLN A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 ILE 184 184 184 ILE ILE A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 GLU 190 190 190 GLU GLU A . n 
A 1 191 ILE 191 191 191 ILE ILE A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 TYR 195 195 195 TYR TYR A . n 
A 1 196 ASP 196 196 196 ASP ASP A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 ASN 198 198 198 ASN ASN A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 TYR 200 200 200 TYR TYR A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 ILE 202 202 202 ILE ILE A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 TYR 204 204 204 TYR TYR A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 GLN 207 207 207 GLN GLN A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 ARG 211 211 211 ARG ARG A . n 
A 1 212 THR 212 212 212 THR THR A . n 
A 1 213 ALA 213 213 213 ALA ALA A . n 
A 1 214 GLN 214 214 214 GLN GLN A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 ASP 219 219 219 ASP ASP A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 TYR 221 221 221 TYR TYR A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 GLY 223 223 223 GLY GLY A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 VAL 228 228 228 VAL VAL A . n 
A 1 229 GLY 229 229 229 GLY GLY A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 PHE 231 231 231 PHE PHE A . n 
A 1 232 ASN 232 232 232 ASN ASN A . n 
A 1 233 GLY 233 233 233 GLY GLY A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 ILE 236 236 236 ILE ILE A . n 
A 1 237 ASP 237 237 237 ASP ASP A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 PHE 239 239 239 PHE PHE A . n 
A 1 240 VAL 240 240 240 VAL VAL A . n 
A 1 241 SER 241 241 241 SER SER A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 PRO 244 244 244 PRO PRO A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 ARG 248 248 248 ARG ARG A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 VAL 253 253 253 VAL VAL A . n 
A 1 254 TYR 254 254 254 TYR TYR A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 ASP 257 257 257 ASP ASP A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 ASN 260 260 260 ASN ASN A . n 
A 1 261 MET 261 261 261 MET MET A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 TYR 265 265 265 TYR TYR A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 PHE 267 267 267 PHE PHE A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 GLY 269 269 269 GLY GLY A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 GLN 271 271 271 GLN GLN A . n 
A 1 272 MET 272 272 272 MET MET A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 ALA 274 274 274 ALA ALA A . n 
A 1 275 TYR 275 275 275 TYR TYR A . n 
A 1 276 PHE 276 276 276 PHE PHE A . n 
A 1 277 GLY 277 277 277 GLY GLY A . n 
A 1 278 PHE 278 278 278 PHE PHE A . n 
A 1 279 SER 279 279 279 SER SER A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 THR 283 283 283 THR THR A . n 
A 1 284 ASP 284 284 284 ASP ASP A . n 
A 1 285 ILE 285 285 285 ILE ILE A . n 
A 1 286 ASN 286 286 286 ASN ASN A . n 
A 1 287 GLY 287 287 287 GLY GLY A . n 
A 1 288 ASP 288 288 288 ASP ASP A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 TYR 290 290 290 TYR TYR A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ASP 292 292 292 ASP ASP A . n 
A 1 293 VAL 293 293 293 VAL VAL A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ILE 295 295 295 ILE ILE A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 MET 301 301 301 MET MET A . n 
A 1 302 ASP 302 302 302 ASP ASP A . n 
A 1 303 ARG 303 303 303 ARG ARG A . n 
A 1 304 GLY 304 304 304 GLY GLY A . n 
A 1 305 SER 305 305 305 SER SER A . n 
A 1 306 ASP 306 306 306 ASP ASP A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 GLN 314 314 314 GLN GLN A . n 
A 1 315 VAL 315 315 315 VAL VAL A . n 
A 1 316 SER 316 316 316 SER SER A . n 
A 1 317 VAL 317 317 317 VAL VAL A . n 
A 1 318 SER 318 318 318 SER SER A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 GLN 320 320 320 GLN GLN A . n 
A 1 321 ARG 321 321 321 ARG ARG A . n 
A 1 322 ALA 322 322 322 ALA ALA A . n 
A 1 323 SER 323 323 323 SER SER A . n 
A 1 324 GLY 324 324 324 GLY GLY A . n 
A 1 325 ASP 325 325 325 ASP ASP A . n 
A 1 326 PHE 326 326 326 PHE PHE A . n 
A 1 327 GLN 327 327 327 GLN GLN A . n 
A 1 328 THR 328 328 328 THR THR A . n 
A 1 329 THR 329 329 329 THR THR A . n 
A 1 330 LYS 330 330 330 LYS LYS A . n 
A 1 331 LEU 331 331 331 LEU LEU A . n 
A 1 332 ASN 332 332 332 ASN ASN A . n 
A 1 333 GLY 333 333 333 GLY GLY A . n 
A 1 334 PHE 334 334 334 PHE PHE A . n 
A 1 335 GLU 335 335 335 GLU GLU A . n 
A 1 336 VAL 336 336 336 VAL VAL A . n 
A 1 337 PHE 337 337 337 PHE PHE A . n 
A 1 338 ALA 338 338 338 ALA ALA A . n 
A 1 339 ARG 339 339 339 ARG ARG A . n 
A 1 340 PHE 340 340 340 PHE PHE A . n 
A 1 341 GLY 341 341 341 GLY GLY A . n 
A 1 342 SER 342 342 342 SER SER A . n 
A 1 343 ALA 343 343 343 ALA ALA A . n 
A 1 344 ILE 344 344 344 ILE ILE A . n 
A 1 345 ALA 345 345 345 ALA ALA A . n 
A 1 346 PRO 346 346 346 PRO PRO A . n 
A 1 347 LEU 347 347 347 LEU LEU A . n 
A 1 348 GLY 348 348 348 GLY GLY A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 LEU 350 350 350 LEU LEU A . n 
A 1 351 ASP 351 351 351 ASP ASP A . n 
A 1 352 GLN 352 352 352 GLN GLN A . n 
A 1 353 ASP 353 353 353 ASP ASP A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 PHE 355 355 355 PHE PHE A . n 
A 1 356 ASN 356 356 356 ASN ASN A . n 
A 1 357 ASP 357 357 357 ASP ASP A . n 
A 1 358 ILE 358 358 358 ILE ILE A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 ILE 360 360 360 ILE ILE A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 ALA 362 362 362 ALA ALA A . n 
A 1 363 PRO 363 363 363 PRO PRO A . n 
A 1 364 TYR 364 364 364 TYR TYR A . n 
A 1 365 GLY 365 365 365 GLY GLY A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 GLU 367 367 367 GLU GLU A . n 
A 1 368 ASP 368 368 368 ASP ASP A . n 
A 1 369 LYS 369 369 369 LYS LYS A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 GLY 371 371 371 GLY GLY A . n 
A 1 372 ILE 372 372 372 ILE ILE A . n 
A 1 373 VAL 373 373 373 VAL VAL A . n 
A 1 374 TYR 374 374 374 TYR TYR A . n 
A 1 375 ILE 375 375 375 ILE ILE A . n 
A 1 376 PHE 376 376 376 PHE PHE A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 GLY 378 378 378 GLY GLY A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 SER 380 380 380 SER SER A . n 
A 1 381 THR 381 381 381 THR THR A . n 
A 1 382 GLY 382 382 382 GLY GLY A . n 
A 1 383 LEU 383 383 383 LEU LEU A . n 
A 1 384 ASN 384 384 384 ASN ASN A . n 
A 1 385 ALA 385 385 385 ALA ALA A . n 
A 1 386 VAL 386 386 386 VAL VAL A . n 
A 1 387 PRO 387 387 387 PRO PRO A . n 
A 1 388 SER 388 388 388 SER SER A . n 
A 1 389 GLN 389 389 389 GLN GLN A . n 
A 1 390 ILE 390 390 390 ILE ILE A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 GLU 392 392 392 GLU GLU A . n 
A 1 393 GLY 393 393 393 GLY GLY A . n 
A 1 394 GLN 394 394 394 GLN GLN A . n 
A 1 395 TRP 395 395 395 TRP TRP A . n 
A 1 396 ALA 396 396 396 ALA ALA A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 ARG 398 398 398 ARG ARG A . n 
A 1 399 SER 399 399 399 SER SER A . n 
A 1 400 GLY 400 400 400 GLY GLY A . n 
A 1 401 CYS 401 401 401 CYS CYS A . n 
A 1 402 PRO 402 402 402 PRO PRO A . n 
A 1 403 PRO 403 403 403 PRO PRO A . n 
A 1 404 SER 404 404 404 SER SER A . n 
A 1 405 PHE 405 405 405 PHE PHE A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 TYR 407 407 407 TYR TYR A . n 
A 1 408 SER 408 408 408 SER SER A . n 
A 1 409 MET 409 409 409 MET MET A . n 
A 1 410 LYS 410 410 410 LYS LYS A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 ALA 412 412 412 ALA ALA A . n 
A 1 413 THR 413 413 413 THR THR A . n 
A 1 414 ASP 414 414 414 ASP ASP A . n 
A 1 415 ILE 415 415 415 ILE ILE A . n 
A 1 416 ASP 416 416 416 ASP ASP A . n 
A 1 417 LYS 417 417 417 LYS LYS A . n 
A 1 418 ASN 418 418 418 ASN ASN A . n 
A 1 419 GLY 419 419 419 GLY GLY A . n 
A 1 420 TYR 420 420 420 TYR TYR A . n 
A 1 421 PRO 421 421 421 PRO PRO A . n 
A 1 422 ASP 422 422 422 ASP ASP A . n 
A 1 423 LEU 423 423 423 LEU LEU A . n 
A 1 424 ILE 424 424 424 ILE ILE A . n 
A 1 425 VAL 425 425 425 VAL VAL A . n 
A 1 426 GLY 426 426 426 GLY GLY A . n 
A 1 427 ALA 427 427 427 ALA ALA A . n 
A 1 428 PHE 428 428 428 PHE PHE A . n 
A 1 429 GLY 429 429 429 GLY GLY A . n 
A 1 430 VAL 430 430 430 VAL VAL A . n 
A 1 431 ASP 431 431 431 ASP ASP A . n 
A 1 432 ARG 432 432 432 ARG ARG A . n 
A 1 433 ALA 433 433 433 ALA ALA A . n 
A 1 434 ILE 434 434 434 ILE ILE A . n 
A 1 435 LEU 435 435 435 LEU LEU A . n 
A 1 436 TYR 436 436 436 TYR TYR A . n 
A 1 437 ARG 437 437 437 ARG ARG A . n 
A 1 438 ALA 438 438 438 ALA ALA A . n 
A 1 439 ARG 439 439 439 ARG ARG A . n 
A 1 440 PRO 440 440 440 PRO PRO A . n 
A 1 441 VAL 441 441 441 VAL VAL A . n 
A 1 442 ILE 442 442 442 ILE ILE A . n 
A 1 443 THR 443 443 443 THR THR A . n 
A 1 444 VAL 444 444 444 VAL VAL A . n 
A 1 445 ASN 445 445 445 ASN ASN A . n 
A 1 446 ALA 446 446 446 ALA ALA A . n 
A 1 447 GLY 447 447 447 GLY GLY A . n 
A 1 448 LEU 448 448 448 LEU LEU A . n 
A 1 449 GLU 449 449 449 GLU GLU A . n 
A 1 450 VAL 450 450 450 VAL VAL A . n 
A 1 451 TYR 451 451 451 TYR TYR A . n 
A 1 452 PRO 452 452 452 PRO PRO A . n 
A 1 453 SER 453 453 453 SER SER A . n 
A 1 454 ILE 454 454 454 ILE ILE A . n 
A 1 455 LEU 455 455 455 LEU LEU A . n 
A 1 456 ASN 456 456 456 ASN ASN A . n 
A 1 457 GLN 457 457 457 GLN GLN A . n 
A 1 458 ASP 458 458 458 ASP ASP A . n 
A 1 459 ASN 459 459 459 ASN ASN A . n 
A 1 460 LYS 460 460 460 LYS LYS A . n 
A 1 461 THR 461 461 461 THR THR A . n 
A 1 462 CYS 462 462 462 CYS CYS A . n 
A 1 463 SER 463 463 463 SER SER A . n 
A 1 464 LEU 464 464 464 LEU LEU A . n 
A 1 465 PRO 465 465 465 PRO PRO A . n 
A 1 466 GLY 466 466 ?   ?   ?   A . n 
A 1 467 THR 467 467 ?   ?   ?   A . n 
A 1 468 ALA 468 468 ?   ?   ?   A . n 
A 1 469 LEU 469 469 ?   ?   ?   A . n 
A 1 470 LYS 470 470 470 LYS LYS A . n 
A 1 471 VAL 471 471 471 VAL VAL A . n 
A 1 472 SER 472 472 472 SER SER A . n 
A 1 473 CYS 473 473 473 CYS CYS A . n 
A 1 474 PHE 474 474 474 PHE PHE A . n 
A 1 475 ASN 475 475 475 ASN ASN A . n 
A 1 476 VAL 476 476 476 VAL VAL A . n 
A 1 477 ARG 477 477 477 ARG ARG A . n 
A 1 478 PHE 478 478 478 PHE PHE A . n 
A 1 479 CYS 479 479 479 CYS CYS A . n 
A 1 480 LEU 480 480 480 LEU LEU A . n 
A 1 481 LYS 481 481 481 LYS LYS A . n 
A 1 482 ALA 482 482 482 ALA ALA A . n 
A 1 483 ASP 483 483 483 ASP ASP A . n 
A 1 484 GLY 484 484 484 GLY GLY A . n 
A 1 485 LYS 485 485 485 LYS LYS A . n 
A 1 486 GLY 486 486 486 GLY GLY A . n 
A 1 487 VAL 487 487 487 VAL VAL A . n 
A 1 488 LEU 488 488 488 LEU LEU A . n 
A 1 489 PRO 489 489 489 PRO PRO A . n 
A 1 490 ARG 490 490 490 ARG ARG A . n 
A 1 491 LYS 491 491 491 LYS LYS A . n 
A 1 492 LEU 492 492 492 LEU LEU A . n 
A 1 493 ASN 493 493 493 ASN ASN A . n 
A 1 494 PHE 494 494 494 PHE PHE A . n 
A 1 495 GLN 495 495 495 GLN GLN A . n 
A 1 496 VAL 496 496 496 VAL VAL A . n 
A 1 497 GLU 497 497 497 GLU GLU A . n 
A 1 498 LEU 498 498 498 LEU LEU A . n 
A 1 499 LEU 499 499 499 LEU LEU A . n 
A 1 500 LEU 500 500 500 LEU LEU A . n 
A 1 501 ASP 501 501 501 ASP ASP A . n 
A 1 502 LYS 502 502 502 LYS LYS A . n 
A 1 503 LEU 503 503 503 LEU LEU A . n 
A 1 504 LYS 504 504 504 LYS LYS A . n 
A 1 505 GLN 505 505 505 GLN GLN A . n 
A 1 506 LYS 506 506 506 LYS LYS A . n 
A 1 507 GLY 507 507 507 GLY GLY A . n 
A 1 508 ALA 508 508 508 ALA ALA A . n 
A 1 509 ILE 509 509 509 ILE ILE A . n 
A 1 510 ARG 510 510 510 ARG ARG A . n 
A 1 511 ARG 511 511 511 ARG ARG A . n 
A 1 512 ALA 512 512 512 ALA ALA A . n 
A 1 513 LEU 513 513 513 LEU LEU A . n 
A 1 514 PHE 514 514 514 PHE PHE A . n 
A 1 515 LEU 515 515 515 LEU LEU A . n 
A 1 516 TYR 516 516 516 TYR TYR A . n 
A 1 517 SER 517 517 517 SER SER A . n 
A 1 518 ARG 518 518 518 ARG ARG A . n 
A 1 519 SER 519 519 519 SER SER A . n 
A 1 520 PRO 520 520 520 PRO PRO A . n 
A 1 521 SER 521 521 521 SER SER A . n 
A 1 522 HIS 522 522 522 HIS HIS A . n 
A 1 523 SER 523 523 523 SER SER A . n 
A 1 524 LYS 524 524 524 LYS LYS A . n 
A 1 525 ASN 525 525 525 ASN ASN A . n 
A 1 526 MET 526 526 526 MET MET A . n 
A 1 527 THR 527 527 527 THR THR A . n 
A 1 528 ILE 528 528 528 ILE ILE A . n 
A 1 529 SER 529 529 529 SER SER A . n 
A 1 530 ARG 530 530 530 ARG ARG A . n 
A 1 531 GLY 531 531 531 GLY GLY A . n 
A 1 532 GLY 532 532 532 GLY GLY A . n 
A 1 533 LEU 533 533 533 LEU LEU A . n 
A 1 534 MET 534 534 534 MET MET A . n 
A 1 535 GLN 535 535 535 GLN GLN A . n 
A 1 536 CYS 536 536 536 CYS CYS A . n 
A 1 537 GLU 537 537 537 GLU GLU A . n 
A 1 538 GLU 538 538 538 GLU GLU A . n 
A 1 539 LEU 539 539 539 LEU LEU A . n 
A 1 540 ILE 540 540 540 ILE ILE A . n 
A 1 541 ALA 541 541 541 ALA ALA A . n 
A 1 542 TYR 542 542 542 TYR TYR A . n 
A 1 543 LEU 543 543 543 LEU LEU A . n 
A 1 544 ARG 544 544 544 ARG ARG A . n 
A 1 545 ASP 545 545 545 ASP ASP A . n 
A 1 546 GLU 546 546 546 GLU GLU A . n 
A 1 547 SER 547 547 547 SER SER A . n 
A 1 548 GLU 548 548 548 GLU GLU A . n 
A 1 549 PHE 549 549 549 PHE PHE A . n 
A 1 550 ARG 550 550 550 ARG ARG A . n 
A 1 551 ASP 551 551 551 ASP ASP A . n 
A 1 552 LYS 552 552 552 LYS LYS A . n 
A 1 553 LEU 553 553 553 LEU LEU A . n 
A 1 554 THR 554 554 554 THR THR A . n 
A 1 555 PRO 555 555 555 PRO PRO A . n 
A 1 556 ILE 556 556 556 ILE ILE A . n 
A 1 557 THR 557 557 557 THR THR A . n 
A 1 558 ILE 558 558 558 ILE ILE A . n 
A 1 559 PHE 559 559 559 PHE PHE A . n 
A 1 560 MET 560 560 560 MET MET A . n 
A 1 561 GLU 561 561 561 GLU GLU A . n 
A 1 562 TYR 562 562 562 TYR TYR A . n 
A 1 563 ARG 563 563 563 ARG ARG A . n 
A 1 564 LEU 564 564 564 LEU LEU A . n 
A 1 565 ASP 565 565 565 ASP ASP A . n 
A 1 566 TYR 566 566 566 TYR TYR A . n 
A 1 567 ARG 567 567 567 ARG ARG A . n 
A 1 568 THR 568 568 568 THR THR A . n 
A 1 569 ALA 569 569 569 ALA ALA A . n 
A 1 570 ALA 570 570 570 ALA ALA A . n 
A 1 571 ASP 571 571 571 ASP ASP A . n 
A 1 572 THR 572 572 572 THR THR A . n 
A 1 573 THR 573 573 573 THR THR A . n 
A 1 574 GLY 574 574 574 GLY GLY A . n 
A 1 575 LEU 575 575 575 LEU LEU A . n 
A 1 576 GLN 576 576 576 GLN GLN A . n 
A 1 577 PRO 577 577 577 PRO PRO A . n 
A 1 578 ILE 578 578 578 ILE ILE A . n 
A 1 579 LEU 579 579 579 LEU LEU A . n 
A 1 580 ASN 580 580 580 ASN ASN A . n 
A 1 581 GLN 581 581 581 GLN GLN A . n 
A 1 582 PHE 582 582 582 PHE PHE A . n 
A 1 583 THR 583 583 583 THR THR A . n 
A 1 584 PRO 584 584 584 PRO PRO A . n 
A 1 585 ALA 585 585 585 ALA ALA A . n 
A 1 586 ASN 586 586 586 ASN ASN A . n 
A 1 587 ILE 587 587 587 ILE ILE A . n 
A 1 588 SER 588 588 588 SER SER A . n 
A 1 589 ARG 589 589 589 ARG ARG A . n 
A 1 590 GLN 590 590 590 GLN GLN A . n 
A 1 591 ALA 591 591 591 ALA ALA A . n 
A 1 592 HIS 592 592 592 HIS HIS A . n 
A 1 593 ILE 593 593 593 ILE ILE A . n 
A 1 594 LEU 594 594 594 LEU LEU A . n 
A 1 595 LEU 595 595 595 LEU LEU A . n 
A 1 596 ASP 596 596 596 ASP ASP A . n 
A 1 597 THR 597 597 ?   ?   ?   A . n 
A 1 598 GLY 598 598 ?   ?   ?   A . n 
A 1 599 GLY 599 599 ?   ?   ?   A . n 
A 1 600 LEU 600 600 ?   ?   ?   A . n 
A 1 601 GLU 601 601 ?   ?   ?   A . n 
B 2 1   THR 1   111 ?   ?   ?   B . n 
B 2 2   GLU 2   112 ?   ?   ?   B . n 
B 2 3   ASP 3   113 113 ASP ASP B . n 
B 2 4   TYR 4   114 114 TYR TYR B . n 
B 2 5   PRO 5   115 115 PRO PRO B . n 
B 2 6   VAL 6   116 116 VAL VAL B . n 
B 2 7   ASP 7   117 117 ASP ASP B . n 
B 2 8   LEU 8   118 118 LEU LEU B . n 
B 2 9   TYR 9   119 119 TYR TYR B . n 
B 2 10  TYR 10  120 120 TYR TYR B . n 
B 2 11  LEU 11  121 121 LEU LEU B . n 
B 2 12  MET 12  122 122 MET MET B . n 
B 2 13  ASP 13  123 123 ASP ASP B . n 
B 2 14  LEU 14  124 124 LEU LEU B . n 
B 2 15  SER 15  125 125 SER SER B . n 
B 2 16  ALA 16  126 126 ALA ALA B . n 
B 2 17  SER 17  127 127 SER SER B . n 
B 2 18  MET 18  128 128 MET MET B . n 
B 2 19  ASP 19  129 129 ASP ASP B . n 
B 2 20  ASP 20  130 130 ASP ASP B . n 
B 2 21  ASP 21  131 131 ASP ASP B . n 
B 2 22  LEU 22  132 132 LEU LEU B . n 
B 2 23  ASN 23  133 133 ASN ASN B . n 
B 2 24  THR 24  134 134 THR THR B . n 
B 2 25  ILE 25  135 135 ILE ILE B . n 
B 2 26  LYS 26  136 136 LYS LYS B . n 
B 2 27  GLU 27  137 137 GLU GLU B . n 
B 2 28  LEU 28  138 138 LEU LEU B . n 
B 2 29  GLY 29  139 139 GLY GLY B . n 
B 2 30  SER 30  140 140 SER SER B . n 
B 2 31  ARG 31  141 141 ARG ARG B . n 
B 2 32  LEU 32  142 142 LEU LEU B . n 
B 2 33  SER 33  143 143 SER SER B . n 
B 2 34  LYS 34  144 144 LYS LYS B . n 
B 2 35  GLU 35  145 145 GLU GLU B . n 
B 2 36  MET 36  146 146 MET MET B . n 
B 2 37  SER 37  147 147 SER SER B . n 
B 2 38  LYS 38  148 148 LYS LYS B . n 
B 2 39  LEU 39  149 149 LEU LEU B . n 
B 2 40  THR 40  150 150 THR THR B . n 
B 2 41  SER 41  151 151 SER SER B . n 
B 2 42  ASN 42  152 152 ASN ASN B . n 
B 2 43  PHE 43  153 153 PHE PHE B . n 
B 2 44  ARG 44  154 154 ARG ARG B . n 
B 2 45  LEU 45  155 155 LEU LEU B . n 
B 2 46  GLY 46  156 156 GLY GLY B . n 
B 2 47  PHE 47  157 157 PHE PHE B . n 
B 2 48  GLY 48  158 158 GLY GLY B . n 
B 2 49  SER 49  159 159 SER SER B . n 
B 2 50  PHE 50  160 160 PHE PHE B . n 
B 2 51  VAL 51  161 161 VAL VAL B . n 
B 2 52  GLU 52  162 162 GLU GLU B . n 
B 2 53  LYS 53  163 163 LYS LYS B . n 
B 2 54  PRO 54  164 164 PRO PRO B . n 
B 2 55  VAL 55  165 165 VAL VAL B . n 
B 2 56  SER 56  166 166 SER SER B . n 
B 2 57  PRO 57  167 167 PRO PRO B . n 
B 2 58  PHE 58  168 168 PHE PHE B . n 
B 2 59  VAL 59  169 169 VAL VAL B . n 
B 2 60  LYS 60  170 170 LYS LYS B . n 
B 2 61  THR 61  171 171 THR THR B . n 
B 2 62  THR 62  172 172 THR THR B . n 
B 2 63  PRO 63  173 173 PRO PRO B . n 
B 2 64  GLU 64  174 174 GLU GLU B . n 
B 2 65  GLU 65  175 175 GLU GLU B . n 
B 2 66  ILE 66  176 176 ILE ILE B . n 
B 2 67  ALA 67  177 177 ALA ALA B . n 
B 2 68  ASN 68  178 178 ASN ASN B . n 
B 2 69  PRO 69  179 179 PRO PRO B . n 
B 2 70  CYS 70  180 180 CYS CYS B . n 
B 2 71  SER 71  181 181 SER SER B . n 
B 2 72  SER 72  182 182 SER SER B . n 
B 2 73  ILE 73  183 183 ILE ILE B . n 
B 2 74  PRO 74  184 184 PRO PRO B . n 
B 2 75  TYR 75  185 185 TYR TYR B . n 
B 2 76  PHE 76  186 186 PHE PHE B . n 
B 2 77  CYS 77  187 187 CYS CYS B . n 
B 2 78  LEU 78  188 188 LEU LEU B . n 
B 2 79  PRO 79  189 189 PRO PRO B . n 
B 2 80  THR 80  190 190 THR THR B . n 
B 2 81  PHE 81  191 191 PHE PHE B . n 
B 2 82  GLY 82  192 192 GLY GLY B . n 
B 2 83  PHE 83  193 193 PHE PHE B . n 
B 2 84  LYS 84  194 194 LYS LYS B . n 
B 2 85  HIS 85  195 195 HIS HIS B . n 
B 2 86  ILE 86  196 196 ILE ILE B . n 
B 2 87  LEU 87  197 197 LEU LEU B . n 
B 2 88  PRO 88  198 198 PRO PRO B . n 
B 2 89  LEU 89  199 199 LEU LEU B . n 
B 2 90  THR 90  200 200 THR THR B . n 
B 2 91  ASN 91  201 201 ASN ASN B . n 
B 2 92  ASP 92  202 202 ASP ASP B . n 
B 2 93  ALA 93  203 203 ALA ALA B . n 
B 2 94  GLU 94  204 204 GLU GLU B . n 
B 2 95  ARG 95  205 205 ARG ARG B . n 
B 2 96  PHE 96  206 206 PHE PHE B . n 
B 2 97  ASN 97  207 207 ASN ASN B . n 
B 2 98  GLU 98  208 208 GLU GLU B . n 
B 2 99  ILE 99  209 209 ILE ILE B . n 
B 2 100 VAL 100 210 210 VAL VAL B . n 
B 2 101 LYS 101 211 211 LYS LYS B . n 
B 2 102 ASN 102 212 212 ASN ASN B . n 
B 2 103 GLN 103 213 213 GLN GLN B . n 
B 2 104 LYS 104 214 214 LYS LYS B . n 
B 2 105 ILE 105 215 215 ILE ILE B . n 
B 2 106 SER 106 216 216 SER SER B . n 
B 2 107 ALA 107 217 217 ALA ALA B . n 
B 2 108 ASN 108 218 218 ASN ASN B . n 
B 2 109 ILE 109 219 219 ILE ILE B . n 
B 2 110 ASP 110 220 220 ASP ASP B . n 
B 2 111 THR 111 221 221 THR THR B . n 
B 2 112 PRO 112 222 222 PRO PRO B . n 
B 2 113 GLU 113 223 223 GLU GLU B . n 
B 2 114 GLY 114 224 224 GLY GLY B . n 
B 2 115 GLY 115 225 225 GLY GLY B . n 
B 2 116 PHE 116 226 226 PHE PHE B . n 
B 2 117 ASP 117 227 227 ASP ASP B . n 
B 2 118 ALA 118 228 228 ALA ALA B . n 
B 2 119 ILE 119 229 229 ILE ILE B . n 
B 2 120 MET 120 230 230 MET MET B . n 
B 2 121 GLN 121 231 231 GLN GLN B . n 
B 2 122 ALA 122 232 232 ALA ALA B . n 
B 2 123 ALA 123 233 233 ALA ALA B . n 
B 2 124 VAL 124 234 234 VAL VAL B . n 
B 2 125 CYS 125 235 235 CYS CYS B . n 
B 2 126 LYS 126 236 236 LYS LYS B . n 
B 2 127 GLU 127 237 237 GLU GLU B . n 
B 2 128 LYS 128 238 238 LYS LYS B . n 
B 2 129 ILE 129 239 239 ILE ILE B . n 
B 2 130 GLY 130 240 240 GLY GLY B . n 
B 2 131 TRP 131 241 241 TRP TRP B . n 
B 2 132 ARG 132 242 242 ARG ARG B . n 
B 2 133 ASN 133 243 243 ASN ASN B . n 
B 2 134 ASP 134 244 244 ASP ASP B . n 
B 2 135 SER 135 245 245 SER SER B . n 
B 2 136 LEU 136 246 246 LEU LEU B . n 
B 2 137 HIS 137 247 247 HIS HIS B . n 
B 2 138 LEU 138 248 248 LEU LEU B . n 
B 2 139 LEU 139 249 249 LEU LEU B . n 
B 2 140 VAL 140 250 250 VAL VAL B . n 
B 2 141 PHE 141 251 251 PHE PHE B . n 
B 2 142 VAL 142 252 252 VAL VAL B . n 
B 2 143 SER 143 253 253 SER SER B . n 
B 2 144 ASP 144 254 254 ASP ASP B . n 
B 2 145 ALA 145 255 255 ALA ALA B . n 
B 2 146 ASP 146 256 256 ASP ASP B . n 
B 2 147 SER 147 257 257 SER SER B . n 
B 2 148 HIS 148 258 258 HIS HIS B . n 
B 2 149 PHE 149 259 259 PHE PHE B . n 
B 2 150 GLY 150 260 260 GLY GLY B . n 
B 2 151 MET 151 261 261 MET MET B . n 
B 2 152 ASP 152 262 262 ASP ASP B . n 
B 2 153 SER 153 263 263 SER SER B . n 
B 2 154 LYS 154 264 264 LYS LYS B . n 
B 2 155 LEU 155 265 265 LEU LEU B . n 
B 2 156 ALA 156 266 266 ALA ALA B . n 
B 2 157 GLY 157 267 267 GLY GLY B . n 
B 2 158 ILE 158 268 268 ILE ILE B . n 
B 2 159 VAL 159 269 269 VAL VAL B . n 
B 2 160 CYS 160 270 270 CYS CYS B . n 
B 2 161 PRO 161 271 271 PRO PRO B . n 
B 2 162 ASN 162 272 272 ASN ASN B . n 
B 2 163 ASP 163 273 273 ASP ASP B . n 
B 2 164 GLY 164 274 274 GLY GLY B . n 
B 2 165 LEU 165 275 275 LEU LEU B . n 
B 2 166 CYS 166 276 276 CYS CYS B . n 
B 2 167 HIS 167 277 277 HIS HIS B . n 
B 2 168 LEU 168 278 278 LEU LEU B . n 
B 2 169 ASP 169 279 279 ASP ASP B . n 
B 2 170 SER 170 280 280 SER SER B . n 
B 2 171 LYS 171 281 281 LYS LYS B . n 
B 2 172 ASN 172 282 282 ASN ASN B . n 
B 2 173 GLU 173 283 283 GLU GLU B . n 
B 2 174 TYR 174 284 284 TYR TYR B . n 
B 2 175 SER 175 285 285 SER SER B . n 
B 2 176 MET 176 286 286 MET MET B . n 
B 2 177 SER 177 287 287 SER SER B . n 
B 2 178 THR 178 288 288 THR THR B . n 
B 2 179 VAL 179 289 289 VAL VAL B . n 
B 2 180 LEU 180 290 290 LEU LEU B . n 
B 2 181 GLU 181 291 291 GLU GLU B . n 
B 2 182 TYR 182 292 292 TYR TYR B . n 
B 2 183 PRO 183 293 293 PRO PRO B . n 
B 2 184 THR 184 294 294 THR THR B . n 
B 2 185 ILE 185 295 295 ILE ILE B . n 
B 2 186 GLY 186 296 296 GLY GLY B . n 
B 2 187 GLN 187 297 297 GLN GLN B . n 
B 2 188 LEU 188 298 298 LEU LEU B . n 
B 2 189 ILE 189 299 299 ILE ILE B . n 
B 2 190 ASP 190 300 300 ASP ASP B . n 
B 2 191 LYS 191 301 301 LYS LYS B . n 
B 2 192 LEU 192 302 302 LEU LEU B . n 
B 2 193 VAL 193 303 303 VAL VAL B . n 
B 2 194 GLN 194 304 304 GLN GLN B . n 
B 2 195 ASN 195 305 305 ASN ASN B . n 
B 2 196 ASN 196 306 306 ASN ASN B . n 
B 2 197 VAL 197 307 307 VAL VAL B . n 
B 2 198 LEU 198 308 308 LEU LEU B . n 
B 2 199 LEU 199 309 309 LEU LEU B . n 
B 2 200 ILE 200 310 310 ILE ILE B . n 
B 2 201 PHE 201 311 311 PHE PHE B . n 
B 2 202 ALA 202 312 312 ALA ALA B . n 
B 2 203 VAL 203 313 313 VAL VAL B . n 
B 2 204 THR 204 314 314 THR THR B . n 
B 2 205 GLN 205 315 315 GLN GLN B . n 
B 2 206 GLU 206 316 316 GLU GLU B . n 
B 2 207 GLN 207 317 317 GLN GLN B . n 
B 2 208 VAL 208 318 318 VAL VAL B . n 
B 2 209 HIS 209 319 319 HIS HIS B . n 
B 2 210 LEU 210 320 320 LEU LEU B . n 
B 2 211 TYR 211 321 321 TYR TYR B . n 
B 2 212 GLU 212 322 322 GLU GLU B . n 
B 2 213 ASN 213 323 323 ASN ASN B . n 
B 2 214 TYR 214 324 324 TYR TYR B . n 
B 2 215 ALA 215 325 325 ALA ALA B . n 
B 2 216 LYS 216 326 326 LYS LYS B . n 
B 2 217 LEU 217 327 327 LEU LEU B . n 
B 2 218 ILE 218 328 328 ILE ILE B . n 
B 2 219 PRO 219 329 329 PRO PRO B . n 
B 2 220 GLY 220 330 330 GLY GLY B . n 
B 2 221 ALA 221 331 331 ALA ALA B . n 
B 2 222 THR 222 332 332 THR THR B . n 
B 2 223 VAL 223 333 333 VAL VAL B . n 
B 2 224 GLY 224 334 334 GLY GLY B . n 
B 2 225 LEU 225 335 335 LEU LEU B . n 
B 2 226 LEU 226 336 336 LEU LEU B . n 
B 2 227 GLN 227 337 337 GLN GLN B . n 
B 2 228 LYS 228 338 338 LYS LYS B . n 
B 2 229 ASP 229 339 339 ASP ASP B . n 
B 2 230 SER 230 340 340 SER SER B . n 
B 2 231 GLY 231 341 341 GLY GLY B . n 
B 2 232 ASN 232 342 342 ASN ASN B . n 
B 2 233 ILE 233 343 343 ILE ILE B . n 
B 2 234 LEU 234 344 344 LEU LEU B . n 
B 2 235 GLN 235 345 345 GLN GLN B . n 
B 2 236 LEU 236 346 346 LEU LEU B . n 
B 2 237 ILE 237 347 347 ILE ILE B . n 
B 2 238 ILE 238 348 348 ILE ILE B . n 
B 2 239 SER 239 349 349 SER SER B . n 
B 2 240 ALA 240 350 350 ALA ALA B . n 
B 2 241 TYR 241 351 351 TYR TYR B . n 
B 2 242 GLU 242 352 352 GLU GLU B . n 
B 2 243 GLU 243 353 353 GLU GLU B . n 
B 2 244 LEU 244 354 354 LEU LEU B . n 
B 2 245 ARG 245 355 ?   ?   ?   B . n 
B 2 246 SER 246 356 ?   ?   ?   B . n 
B 2 247 GLU 247 357 ?   ?   ?   B . n 
B 2 248 VAL 248 358 ?   ?   ?   B . n 
B 2 249 GLU 249 359 ?   ?   ?   B . n 
B 2 250 LEU 250 360 ?   ?   ?   B . n 
B 2 251 GLU 251 361 ?   ?   ?   B . n 
B 2 252 HIS 252 362 ?   ?   ?   B . n 
B 2 253 HIS 253 363 ?   ?   ?   B . n 
B 2 254 HIS 254 364 ?   ?   ?   B . n 
B 2 255 HIS 255 365 ?   ?   ?   B . n 
B 2 256 HIS 256 366 ?   ?   ?   B . n 
B 2 257 HIS 257 367 ?   ?   ?   B . n 
C 3 1   GLY 1   -1  ?   ?   ?   C . n 
C 3 2   PRO 2   0   ?   ?   ?   C . n 
C 3 3   LEU 3   1   ?   ?   ?   C . n 
C 3 4   SER 4   2   ?   ?   ?   C . n 
C 3 5   THR 5   3   ?   ?   ?   C . n 
C 3 6   SER 6   4   ?   ?   ?   C . n 
C 3 7   LYS 7   5   ?   ?   ?   C . n 
C 3 8   THR 8   6   ?   ?   ?   C . n 
C 3 9   ILE 9   7   ?   ?   ?   C . n 
C 3 10  ASP 10  8   8   ASP ASP C . n 
C 3 11  MET 11  9   9   MET MET C . n 
C 3 12  GLU 12  10  10  GLU GLU C . n 
C 3 13  LEU 13  11  11  LEU LEU C . n 
C 3 14  VAL 14  12  12  VAL VAL C . n 
C 3 15  LYS 15  13  13  LYS LYS C . n 
C 3 16  ARG 16  14  14  ARG ARG C . n 
C 3 17  LYS 17  15  15  LYS LYS C . n 
C 3 18  ARG 18  16  16  ARG ARG C . n 
C 3 19  ILE 19  17  17  ILE ILE C . n 
C 3 20  GLU 20  18  18  GLU GLU C . n 
C 3 21  ALA 21  19  19  ALA ALA C . n 
C 3 22  ILE 22  20  20  ILE ILE C . n 
C 3 23  ARG 23  21  21  ARG ARG C . n 
C 3 24  GLY 24  22  22  GLY GLY C . n 
C 3 25  GLN 25  23  23  GLN GLN C . n 
C 3 26  ILE 26  24  24  ILE ILE C . n 
C 3 27  LEU 27  25  25  LEU LEU C . n 
C 3 28  SER 28  26  26  SER SER C . n 
C 3 29  LYS 29  27  27  LYS LYS C . n 
C 3 30  LEU 30  28  28  LEU LEU C . n 
C 3 31  ARG 31  29  29  ARG ARG C . n 
C 3 32  LEU 32  30  30  LEU LEU C . n 
C 3 33  ALA 33  31  31  ALA ALA C . n 
C 3 34  SER 34  32  32  SER SER C . n 
C 3 35  PRO 35  33  33  PRO PRO C . n 
C 3 36  PRO 36  34  34  PRO PRO C . n 
C 3 37  SER 37  35  35  SER SER C . n 
C 3 38  GLN 38  36  36  GLN GLN C . n 
C 3 39  GLY 39  37  37  GLY GLY C . n 
C 3 40  GLU 40  38  38  GLU GLU C . n 
C 3 41  VAL 41  39  39  VAL VAL C . n 
C 3 42  PRO 42  40  40  PRO PRO C . n 
C 3 43  PRO 43  41  41  PRO PRO C . n 
C 3 44  GLY 44  42  42  GLY GLY C . n 
C 3 45  PRO 45  43  43  PRO PRO C . n 
C 3 46  LEU 46  44  44  LEU LEU C . n 
C 3 47  PRO 47  45  45  PRO PRO C . n 
C 3 48  GLU 48  46  46  GLU GLU C . n 
C 3 49  ALA 49  47  47  ALA ALA C . n 
C 3 50  VAL 50  48  48  VAL VAL C . n 
C 3 51  LEU 51  49  49  LEU LEU C . n 
C 3 52  ALA 52  50  50  ALA ALA C . n 
C 3 53  LEU 53  51  51  LEU LEU C . n 
C 3 54  TYR 54  52  52  TYR TYR C . n 
C 3 55  ASN 55  53  53  ASN ASN C . n 
C 3 56  SER 56  54  54  SER SER C . n 
C 3 57  THR 57  55  55  THR THR C . n 
C 3 58  ARG 58  56  56  ARG ARG C . n 
C 3 59  ASP 59  57  57  ASP ASP C . n 
C 3 60  ARG 60  58  58  ARG ARG C . n 
C 3 61  VAL 61  59  59  VAL VAL C . n 
C 3 62  ALA 62  60  60  ALA ALA C . n 
C 3 63  GLY 63  61  ?   ?   ?   C . n 
C 3 64  GLU 64  62  ?   ?   ?   C . n 
C 3 65  SER 65  63  ?   ?   ?   C . n 
C 3 66  ALA 66  64  ?   ?   ?   C . n 
C 3 67  GLU 67  65  ?   ?   ?   C . n 
C 3 68  PRO 68  66  ?   ?   ?   C . n 
C 3 69  GLU 69  67  ?   ?   ?   C . n 
C 3 70  PRO 70  68  ?   ?   ?   C . n 
C 3 71  GLU 71  69  ?   ?   ?   C . n 
C 3 72  PRO 72  70  ?   ?   ?   C . n 
C 3 73  GLU 73  71  ?   ?   ?   C . n 
C 3 74  ALA 74  72  72  ALA ALA C . n 
C 3 75  ASP 75  73  73  ASP ASP C . n 
C 3 76  TYR 76  74  74  TYR TYR C . n 
C 3 77  TYR 77  75  75  TYR TYR C . n 
C 3 78  ALA 78  76  76  ALA ALA C . n 
C 3 79  LYS 79  77  77  LYS LYS C . n 
C 3 80  GLU 80  78  78  GLU GLU C . n 
C 3 81  VAL 81  79  79  VAL VAL C . n 
C 3 82  THR 82  80  80  THR THR C . n 
C 3 83  ARG 83  81  81  ARG ARG C . n 
C 3 84  VAL 84  82  82  VAL VAL C . n 
C 3 85  LEU 85  83  83  LEU LEU C . n 
C 3 86  MET 86  84  84  MET MET C . n 
C 3 87  VAL 87  85  85  VAL VAL C . n 
C 3 88  GLU 88  86  86  GLU GLU C . n 
C 3 89  THR 89  87  87  THR THR C . n 
C 3 90  HIS 90  88  88  HIS HIS C . n 
C 3 91  ASN 91  89  89  ASN ASN C . n 
C 3 92  GLU 92  90  90  GLU GLU C . n 
C 3 93  ILE 93  91  91  ILE ILE C . n 
C 3 94  TYR 94  92  92  TYR TYR C . n 
C 3 95  ASP 95  93  93  ASP ASP C . n 
C 3 96  LYS 96  94  94  LYS LYS C . n 
C 3 97  PHE 97  95  95  PHE PHE C . n 
C 3 98  LYS 98  96  96  LYS LYS C . n 
C 3 99  GLN 99  97  97  GLN GLN C . n 
C 3 100 SER 100 98  98  SER SER C . n 
C 3 101 THR 101 99  99  THR THR C . n 
C 3 102 HIS 102 100 100 HIS HIS C . n 
C 3 103 SER 103 101 101 SER SER C . n 
C 3 104 ILE 104 102 102 ILE ILE C . n 
C 3 105 TYR 105 103 103 TYR TYR C . n 
C 3 106 MET 106 104 104 MET MET C . n 
C 3 107 PHE 107 105 105 PHE PHE C . n 
C 3 108 PHE 108 106 106 PHE PHE C . n 
C 3 109 GLN 109 107 107 GLN GLN C . n 
C 3 110 THR 110 108 108 THR THR C . n 
C 3 111 SER 111 109 109 SER SER C . n 
C 3 112 GLU 112 110 110 GLU GLU C . n 
C 3 113 LEU 113 111 111 LEU LEU C . n 
C 3 114 ARG 114 112 112 ARG ARG C . n 
C 3 115 GLU 115 113 113 GLU GLU C . n 
C 3 116 ALA 116 114 114 ALA ALA C . n 
C 3 117 VAL 117 115 115 VAL VAL C . n 
C 3 118 PRO 118 116 116 PRO PRO C . n 
C 3 119 GLU 119 117 117 GLU GLU C . n 
C 3 120 PRO 120 118 118 PRO PRO C . n 
C 3 121 VAL 121 119 119 VAL VAL C . n 
C 3 122 LEU 122 120 120 LEU LEU C . n 
C 3 123 LEU 123 121 121 LEU LEU C . n 
C 3 124 SER 124 122 122 SER SER C . n 
C 3 125 ARG 125 123 123 ARG ARG C . n 
C 3 126 ALA 126 124 124 ALA ALA C . n 
C 3 127 GLU 127 125 125 GLU GLU C . n 
C 3 128 LEU 128 126 126 LEU LEU C . n 
C 3 129 ARG 129 127 127 ARG ARG C . n 
C 3 130 LEU 130 128 128 LEU LEU C . n 
C 3 131 LEU 131 129 129 LEU LEU C . n 
C 3 132 ARG 132 130 130 ARG ARG C . n 
C 3 133 LEU 133 131 131 LEU LEU C . n 
C 3 134 LYS 134 132 132 LYS LYS C . n 
C 3 135 LEU 135 133 133 LEU LEU C . n 
C 3 136 LYS 136 134 134 LYS LYS C . n 
C 3 137 VAL 137 135 135 VAL VAL C . n 
C 3 138 GLU 138 136 136 GLU GLU C . n 
C 3 139 GLN 139 137 137 GLN GLN C . n 
C 3 140 HIS 140 138 138 HIS HIS C . n 
C 3 141 VAL 141 139 139 VAL VAL C . n 
C 3 142 GLU 142 140 140 GLU GLU C . n 
C 3 143 LEU 143 141 141 LEU LEU C . n 
C 3 144 TYR 144 142 142 TYR TYR C . n 
C 3 145 GLN 145 143 143 GLN GLN C . n 
C 3 146 LYS 146 144 144 LYS LYS C . n 
C 3 147 TYR 147 145 145 TYR TYR C . n 
C 3 148 SER 148 146 146 SER SER C . n 
C 3 149 GLN 149 147 147 GLN GLN C . n 
C 3 150 ASN 150 148 148 ASN ASN C . n 
C 3 151 SER 151 149 149 SER SER C . n 
C 3 152 TRP 152 150 150 TRP TRP C . n 
C 3 153 ARG 153 151 151 ARG ARG C . n 
C 3 154 TYR 154 152 152 TYR TYR C . n 
C 3 155 LEU 155 153 153 LEU LEU C . n 
C 3 156 SER 156 154 154 SER SER C . n 
C 3 157 ASN 157 155 155 ASN ASN C . n 
C 3 158 ARG 158 156 156 ARG ARG C . n 
C 3 159 LEU 159 157 157 LEU LEU C . n 
C 3 160 LEU 160 158 158 LEU LEU C . n 
C 3 161 ALA 161 159 159 ALA ALA C . n 
C 3 162 PRO 162 160 160 PRO PRO C . n 
C 3 163 SER 163 161 161 SER SER C . n 
C 3 164 ASP 164 162 162 ASP ASP C . n 
C 3 165 SER 165 163 163 SER SER C . n 
C 3 166 PRO 166 164 164 PRO PRO C . n 
C 3 167 GLU 167 165 165 GLU GLU C . n 
C 3 168 TRP 168 166 166 TRP TRP C . n 
C 3 169 LEU 169 167 167 LEU LEU C . n 
C 3 170 SER 170 168 168 SER SER C . n 
C 3 171 PHE 171 169 169 PHE PHE C . n 
C 3 172 ASP 172 170 170 ASP ASP C . n 
C 3 173 VAL 173 171 171 VAL VAL C . n 
C 3 174 THR 174 172 172 THR THR C . n 
C 3 175 GLY 175 173 173 GLY GLY C . n 
C 3 176 VAL 176 174 174 VAL VAL C . n 
C 3 177 VAL 177 175 175 VAL VAL C . n 
C 3 178 ARG 178 176 176 ARG ARG C . n 
C 3 179 GLN 179 177 177 GLN GLN C . n 
C 3 180 TRP 180 178 178 TRP TRP C . n 
C 3 181 LEU 181 179 179 LEU LEU C . n 
C 3 182 SER 182 180 180 SER SER C . n 
C 3 183 ARG 183 181 181 ARG ARG C . n 
C 3 184 GLY 184 182 182 GLY GLY C . n 
C 3 185 GLY 185 183 183 GLY GLY C . n 
C 3 186 GLU 186 184 184 GLU GLU C . n 
C 3 187 ILE 187 185 185 ILE ILE C . n 
C 3 188 GLU 188 186 186 GLU GLU C . n 
C 3 189 GLY 189 187 187 GLY GLY C . n 
C 3 190 PHE 190 188 188 PHE PHE C . n 
C 3 191 ARG 191 189 189 ARG ARG C . n 
C 3 192 LEU 192 190 190 LEU LEU C . n 
C 3 193 SER 193 191 191 SER SER C . n 
C 3 194 ALA 194 192 192 ALA ALA C . n 
C 3 195 HIS 195 193 193 HIS HIS C . n 
C 3 196 CYS 196 194 194 CYS CYS C . n 
C 3 197 SER 197 195 195 SER SER C . n 
C 3 198 CYS 198 196 196 CYS CYS C . n 
C 3 199 ASP 199 197 ?   ?   ?   C . n 
C 3 200 SER 200 198 ?   ?   ?   C . n 
C 3 201 ARG 201 199 ?   ?   ?   C . n 
C 3 202 ASP 202 200 ?   ?   ?   C . n 
C 3 203 ASN 203 201 ?   ?   ?   C . n 
C 3 204 THR 204 202 ?   ?   ?   C . n 
C 3 205 LEU 205 203 ?   ?   ?   C . n 
C 3 206 GLN 206 204 ?   ?   ?   C . n 
C 3 207 VAL 207 205 ?   ?   ?   C . n 
C 3 208 ASP 208 206 ?   ?   ?   C . n 
C 3 209 ILE 209 207 207 ILE ILE C . n 
C 3 210 ASN 210 208 208 ASN ASN C . n 
C 3 211 GLY 211 209 209 GLY GLY C . n 
C 3 212 PHE 212 210 210 PHE PHE C . n 
C 3 213 THR 213 211 211 THR THR C . n 
C 3 214 THR 214 212 212 THR THR C . n 
C 3 215 GLY 215 213 213 GLY GLY C . n 
C 3 216 ARG 216 214 214 ARG ARG C . n 
C 3 217 ARG 217 215 215 ARG ARG C . n 
C 3 218 GLY 218 216 216 GLY GLY C . n 
C 3 219 ASP 219 217 217 ASP ASP C . n 
C 3 220 LEU 220 218 218 LEU LEU C . n 
C 3 221 ALA 221 219 219 ALA ALA C . n 
C 3 222 THR 222 220 220 THR THR C . n 
C 3 223 ILE 223 221 221 ILE ILE C . n 
C 3 224 HIS 224 222 222 HIS HIS C . n 
C 3 225 GLY 225 223 223 GLY GLY C . n 
C 3 226 MET 226 224 224 MET MET C . n 
C 3 227 ASN 227 225 225 ASN ASN C . n 
C 3 228 ARG 228 226 226 ARG ARG C . n 
C 3 229 PRO 229 227 227 PRO PRO C . n 
C 3 230 PHE 230 228 228 PHE PHE C . n 
C 3 231 LEU 231 229 229 LEU LEU C . n 
C 3 232 LEU 232 230 230 LEU LEU C . n 
C 3 233 LEU 233 231 231 LEU LEU C . n 
C 3 234 MET 234 232 232 MET MET C . n 
C 3 235 ALA 235 233 233 ALA ALA C . n 
C 3 236 THR 236 234 234 THR THR C . n 
C 3 237 PRO 237 235 235 PRO PRO C . n 
C 3 238 LEU 238 236 236 LEU LEU C . n 
C 3 239 GLU 239 237 237 GLU GLU C . n 
C 3 240 ARG 240 238 238 ARG ARG C . n 
C 3 241 ALA 241 239 239 ALA ALA C . n 
C 3 242 GLN 242 240 240 GLN GLN C . n 
C 3 243 HIS 243 241 ?   ?   ?   C . n 
C 3 244 LEU 244 242 ?   ?   ?   C . n 
C 3 245 GLN 245 243 ?   ?   ?   C . n 
C 3 246 SER 246 244 ?   ?   ?   C . n 
C 3 247 SER 247 245 ?   ?   ?   C . n 
C 3 248 ARG 248 246 ?   ?   ?   C . n 
C 3 249 HIS 249 247 ?   ?   ?   C . n 
C 3 250 ARG 250 248 ?   ?   ?   C . n 
C 3 251 ARG 251 249 ?   ?   ?   C . n 
C 3 252 ALA 252 250 250 ALA ALA C . n 
C 3 253 LEU 253 251 251 LEU LEU C . n 
C 3 254 ASP 254 252 252 ASP ASP C . n 
C 3 255 THR 255 253 253 THR THR C . n 
C 3 256 ASN 256 254 254 ASN ASN C . n 
C 3 257 TYR 257 255 255 TYR TYR C . n 
C 3 258 CYS 258 256 256 CYS CYS C . n 
C 3 259 PHE 259 257 257 PHE PHE C . n 
C 3 260 SER 260 258 258 SER SER C . n 
C 3 261 SER 261 259 259 SER SER C . n 
C 3 262 THR 262 260 260 THR THR C . n 
C 3 263 GLU 263 261 261 GLU GLU C . n 
C 3 264 LYS 264 262 262 LYS LYS C . n 
C 3 265 ASN 265 263 263 ASN ASN C . n 
C 3 266 CYS 266 264 264 CYS CYS C . n 
C 3 267 CYS 267 265 265 CYS CYS C . n 
C 3 268 VAL 268 266 266 VAL VAL C . n 
C 3 269 ARG 269 267 267 ARG ARG C . n 
C 3 270 GLN 270 268 268 GLN GLN C . n 
C 3 271 LEU 271 269 269 LEU LEU C . n 
C 3 272 TYR 272 270 270 TYR TYR C . n 
C 3 273 ILE 273 271 271 ILE ILE C . n 
C 3 274 ASP 274 272 272 ASP ASP C . n 
C 3 275 PHE 275 273 273 PHE PHE C . n 
C 3 276 ARG 276 274 274 ARG ARG C . n 
C 3 277 LYS 277 275 275 LYS LYS C . n 
C 3 278 ASP 278 276 276 ASP ASP C . n 
C 3 279 LEU 279 277 277 LEU LEU C . n 
C 3 280 GLY 280 278 278 GLY GLY C . n 
C 3 281 TRP 281 279 279 TRP TRP C . n 
C 3 282 LYS 282 280 280 LYS LYS C . n 
C 3 283 TRP 283 281 281 TRP TRP C . n 
C 3 284 ILE 284 282 282 ILE ILE C . n 
C 3 285 HIS 285 283 283 HIS HIS C . n 
C 3 286 GLU 286 284 284 GLU GLU C . n 
C 3 287 PRO 287 285 285 PRO PRO C . n 
C 3 288 LYS 288 286 286 LYS LYS C . n 
C 3 289 GLY 289 287 287 GLY GLY C . n 
C 3 290 TYR 290 288 288 TYR TYR C . n 
C 3 291 HIS 291 289 289 HIS HIS C . n 
C 3 292 ALA 292 290 290 ALA ALA C . n 
C 3 293 ASN 293 291 291 ASN ASN C . n 
C 3 294 PHE 294 292 292 PHE PHE C . n 
C 3 295 CYS 295 293 293 CYS CYS C . n 
C 3 296 LEU 296 294 294 LEU LEU C . n 
C 3 297 GLY 297 295 295 GLY GLY C . n 
C 3 298 PRO 298 296 296 PRO PRO C . n 
C 3 299 CYS 299 297 297 CYS CYS C . n 
C 3 300 PRO 300 298 298 PRO PRO C . n 
C 3 301 TYR 301 299 299 TYR TYR C . n 
C 3 302 ILE 302 300 ?   ?   ?   C . n 
C 3 303 TRP 303 301 ?   ?   ?   C . n 
C 3 304 SER 304 302 ?   ?   ?   C . n 
C 3 305 LEU 305 303 ?   ?   ?   C . n 
C 3 306 ASP 306 304 ?   ?   ?   C . n 
C 3 307 THR 307 305 ?   ?   ?   C . n 
C 3 308 GLN 308 306 ?   ?   ?   C . n 
C 3 309 TYR 309 307 ?   ?   ?   C . n 
C 3 310 SER 310 308 ?   ?   ?   C . n 
C 3 311 LYS 311 309 ?   ?   ?   C . n 
C 3 312 VAL 312 310 ?   ?   ?   C . n 
C 3 313 LEU 313 311 ?   ?   ?   C . n 
C 3 314 ALA 314 312 ?   ?   ?   C . n 
C 3 315 LEU 315 313 ?   ?   ?   C . n 
C 3 316 TYR 316 314 ?   ?   ?   C . n 
C 3 317 ASN 317 315 ?   ?   ?   C . n 
C 3 318 GLN 318 316 ?   ?   ?   C . n 
C 3 319 HIS 319 317 ?   ?   ?   C . n 
C 3 320 ASN 320 318 ?   ?   ?   C . n 
C 3 321 PRO 321 319 319 PRO ALA C . n 
C 3 322 GLY 322 320 320 GLY GLY C . n 
C 3 323 ALA 323 321 321 ALA ALA C . n 
C 3 324 SER 324 322 322 SER SER C . n 
C 3 325 ALA 325 323 323 ALA ALA C . n 
C 3 326 ALA 326 324 324 ALA ALA C . n 
C 3 327 PRO 327 325 325 PRO PRO C . n 
C 3 328 CYS 328 326 326 CYS CYS C . n 
C 3 329 CYS 329 327 327 CYS CYS C . n 
C 3 330 VAL 330 328 328 VAL VAL C . n 
C 3 331 PRO 331 329 329 PRO PRO C . n 
C 3 332 GLN 332 330 330 GLN GLN C . n 
C 3 333 ALA 333 331 331 ALA ALA C . n 
C 3 334 LEU 334 332 332 LEU LEU C . n 
C 3 335 GLU 335 333 333 GLU GLU C . n 
C 3 336 PRO 336 334 334 PRO PRO C . n 
C 3 337 LEU 337 335 335 LEU LEU C . n 
C 3 338 PRO 338 336 336 PRO PRO C . n 
C 3 339 ILE 339 337 337 ILE ILE C . n 
C 3 340 VAL 340 338 338 VAL VAL C . n 
C 3 341 TYR 341 339 339 TYR TYR C . n 
C 3 342 TYR 342 340 340 TYR TYR C . n 
C 3 343 VAL 343 341 341 VAL VAL C . n 
C 3 344 GLY 344 342 342 GLY GLY C . n 
C 3 345 ARG 345 343 343 ARG ARG C . n 
C 3 346 LYS 346 344 344 LYS LYS C . n 
C 3 347 PRO 347 345 345 PRO PRO C . n 
C 3 348 LYS 348 346 346 LYS LYS C . n 
C 3 349 VAL 349 347 347 VAL VAL C . n 
C 3 350 GLU 350 348 348 GLU GLU C . n 
C 3 351 GLN 351 349 349 GLN GLN C . n 
C 3 352 LEU 352 350 350 LEU LEU C . n 
C 3 353 SER 353 351 351 SER SER C . n 
C 3 354 ASN 354 352 352 ASN ASN C . n 
C 3 355 MET 355 353 353 MET MET C . n 
C 3 356 ILE 356 354 354 ILE ILE C . n 
C 3 357 VAL 357 355 355 VAL VAL C . n 
C 3 358 ARG 358 356 356 ARG ARG C . n 
C 3 359 SER 359 357 357 SER SER C . n 
C 3 360 CYS 360 358 358 CYS CYS C . n 
C 3 361 LYS 361 359 359 LYS LYS C . n 
C 3 362 CYS 362 360 360 CYS CYS C . n 
C 3 363 SER 363 361 361 SER SER C . n 
D 3 1   GLY 1   -1  ?   ?   ?   D . n 
D 3 2   PRO 2   0   ?   ?   ?   D . n 
D 3 3   LEU 3   1   ?   ?   ?   D . n 
D 3 4   SER 4   2   ?   ?   ?   D . n 
D 3 5   THR 5   3   ?   ?   ?   D . n 
D 3 6   SER 6   4   ?   ?   ?   D . n 
D 3 7   LYS 7   5   ?   ?   ?   D . n 
D 3 8   THR 8   6   ?   ?   ?   D . n 
D 3 9   ILE 9   7   7   ILE ILE D . n 
D 3 10  ASP 10  8   8   ASP ASP D . n 
D 3 11  MET 11  9   9   MET MET D . n 
D 3 12  GLU 12  10  10  GLU GLU D . n 
D 3 13  LEU 13  11  11  LEU LEU D . n 
D 3 14  VAL 14  12  12  VAL VAL D . n 
D 3 15  LYS 15  13  13  LYS LYS D . n 
D 3 16  ARG 16  14  14  ARG ARG D . n 
D 3 17  LYS 17  15  15  LYS LYS D . n 
D 3 18  ARG 18  16  16  ARG ARG D . n 
D 3 19  ILE 19  17  17  ILE ILE D . n 
D 3 20  GLU 20  18  18  GLU GLU D . n 
D 3 21  ALA 21  19  19  ALA ALA D . n 
D 3 22  ILE 22  20  20  ILE ILE D . n 
D 3 23  ARG 23  21  21  ARG ARG D . n 
D 3 24  GLY 24  22  22  GLY GLY D . n 
D 3 25  GLN 25  23  23  GLN GLN D . n 
D 3 26  ILE 26  24  24  ILE ILE D . n 
D 3 27  LEU 27  25  25  LEU LEU D . n 
D 3 28  SER 28  26  26  SER SER D . n 
D 3 29  LYS 29  27  27  LYS LYS D . n 
D 3 30  LEU 30  28  28  LEU LEU D . n 
D 3 31  ARG 31  29  29  ARG ARG D . n 
D 3 32  LEU 32  30  30  LEU LEU D . n 
D 3 33  ALA 33  31  31  ALA ALA D . n 
D 3 34  SER 34  32  32  SER SER D . n 
D 3 35  PRO 35  33  33  PRO PRO D . n 
D 3 36  PRO 36  34  34  PRO PRO D . n 
D 3 37  SER 37  35  35  SER SER D . n 
D 3 38  GLN 38  36  36  GLN GLN D . n 
D 3 39  GLY 39  37  37  GLY GLY D . n 
D 3 40  GLU 40  38  38  GLU GLU D . n 
D 3 41  VAL 41  39  39  VAL VAL D . n 
D 3 42  PRO 42  40  40  PRO PRO D . n 
D 3 43  PRO 43  41  41  PRO PRO D . n 
D 3 44  GLY 44  42  42  GLY GLY D . n 
D 3 45  PRO 45  43  43  PRO PRO D . n 
D 3 46  LEU 46  44  44  LEU LEU D . n 
D 3 47  PRO 47  45  45  PRO PRO D . n 
D 3 48  GLU 48  46  46  GLU GLU D . n 
D 3 49  ALA 49  47  47  ALA ALA D . n 
D 3 50  VAL 50  48  48  VAL VAL D . n 
D 3 51  LEU 51  49  49  LEU LEU D . n 
D 3 52  ALA 52  50  50  ALA ALA D . n 
D 3 53  LEU 53  51  51  LEU LEU D . n 
D 3 54  TYR 54  52  52  TYR TYR D . n 
D 3 55  ASN 55  53  53  ASN ASN D . n 
D 3 56  SER 56  54  54  SER SER D . n 
D 3 57  THR 57  55  55  THR THR D . n 
D 3 58  ARG 58  56  56  ARG ARG D . n 
D 3 59  ASP 59  57  57  ASP ASP D . n 
D 3 60  ARG 60  58  58  ARG ARG D . n 
D 3 61  VAL 61  59  59  VAL VAL D . n 
D 3 62  ALA 62  60  60  ALA ALA D . n 
D 3 63  GLY 63  61  61  GLY GLY D . n 
D 3 64  GLU 64  62  62  GLU GLU D . n 
D 3 65  SER 65  63  ?   ?   ?   D . n 
D 3 66  ALA 66  64  ?   ?   ?   D . n 
D 3 67  GLU 67  65  ?   ?   ?   D . n 
D 3 68  PRO 68  66  ?   ?   ?   D . n 
D 3 69  GLU 69  67  ?   ?   ?   D . n 
D 3 70  PRO 70  68  ?   ?   ?   D . n 
D 3 71  GLU 71  69  ?   ?   ?   D . n 
D 3 72  PRO 72  70  70  PRO PRO D . n 
D 3 73  GLU 73  71  71  GLU GLU D . n 
D 3 74  ALA 74  72  72  ALA ALA D . n 
D 3 75  ASP 75  73  73  ASP ASP D . n 
D 3 76  TYR 76  74  74  TYR TYR D . n 
D 3 77  TYR 77  75  75  TYR TYR D . n 
D 3 78  ALA 78  76  76  ALA ALA D . n 
D 3 79  LYS 79  77  77  LYS LYS D . n 
D 3 80  GLU 80  78  78  GLU GLU D . n 
D 3 81  VAL 81  79  79  VAL VAL D . n 
D 3 82  THR 82  80  80  THR THR D . n 
D 3 83  ARG 83  81  81  ARG ARG D . n 
D 3 84  VAL 84  82  82  VAL VAL D . n 
D 3 85  LEU 85  83  83  LEU LEU D . n 
D 3 86  MET 86  84  84  MET MET D . n 
D 3 87  VAL 87  85  85  VAL VAL D . n 
D 3 88  GLU 88  86  86  GLU GLU D . n 
D 3 89  THR 89  87  87  THR THR D . n 
D 3 90  HIS 90  88  88  HIS HIS D . n 
D 3 91  ASN 91  89  89  ASN ASN D . n 
D 3 92  GLU 92  90  90  GLU GLU D . n 
D 3 93  ILE 93  91  91  ILE ILE D . n 
D 3 94  TYR 94  92  92  TYR TYR D . n 
D 3 95  ASP 95  93  93  ASP ASP D . n 
D 3 96  LYS 96  94  94  LYS LYS D . n 
D 3 97  PHE 97  95  95  PHE PHE D . n 
D 3 98  LYS 98  96  96  LYS LYS D . n 
D 3 99  GLN 99  97  97  GLN GLN D . n 
D 3 100 SER 100 98  98  SER SER D . n 
D 3 101 THR 101 99  99  THR THR D . n 
D 3 102 HIS 102 100 100 HIS HIS D . n 
D 3 103 SER 103 101 101 SER SER D . n 
D 3 104 ILE 104 102 102 ILE ILE D . n 
D 3 105 TYR 105 103 103 TYR TYR D . n 
D 3 106 MET 106 104 104 MET MET D . n 
D 3 107 PHE 107 105 105 PHE PHE D . n 
D 3 108 PHE 108 106 106 PHE PHE D . n 
D 3 109 GLN 109 107 107 GLN GLN D . n 
D 3 110 THR 110 108 108 THR THR D . n 
D 3 111 SER 111 109 109 SER SER D . n 
D 3 112 GLU 112 110 110 GLU GLU D . n 
D 3 113 LEU 113 111 111 LEU LEU D . n 
D 3 114 ARG 114 112 112 ARG ARG D . n 
D 3 115 GLU 115 113 113 GLU GLU D . n 
D 3 116 ALA 116 114 114 ALA ALA D . n 
D 3 117 VAL 117 115 115 VAL VAL D . n 
D 3 118 PRO 118 116 116 PRO PRO D . n 
D 3 119 GLU 119 117 117 GLU GLU D . n 
D 3 120 PRO 120 118 118 PRO PRO D . n 
D 3 121 VAL 121 119 119 VAL VAL D . n 
D 3 122 LEU 122 120 120 LEU LEU D . n 
D 3 123 LEU 123 121 121 LEU LEU D . n 
D 3 124 SER 124 122 122 SER SER D . n 
D 3 125 ARG 125 123 123 ARG ARG D . n 
D 3 126 ALA 126 124 124 ALA ALA D . n 
D 3 127 GLU 127 125 125 GLU GLU D . n 
D 3 128 LEU 128 126 126 LEU LEU D . n 
D 3 129 ARG 129 127 127 ARG ARG D . n 
D 3 130 LEU 130 128 128 LEU LEU D . n 
D 3 131 LEU 131 129 129 LEU LEU D . n 
D 3 132 ARG 132 130 130 ARG ARG D . n 
D 3 133 LEU 133 131 131 LEU LEU D . n 
D 3 134 LYS 134 132 132 LYS LYS D . n 
D 3 135 LEU 135 133 133 LEU LEU D . n 
D 3 136 LYS 136 134 134 LYS LYS D . n 
D 3 137 VAL 137 135 135 VAL VAL D . n 
D 3 138 GLU 138 136 136 GLU GLU D . n 
D 3 139 GLN 139 137 137 GLN GLN D . n 
D 3 140 HIS 140 138 138 HIS HIS D . n 
D 3 141 VAL 141 139 139 VAL VAL D . n 
D 3 142 GLU 142 140 140 GLU GLU D . n 
D 3 143 LEU 143 141 141 LEU LEU D . n 
D 3 144 TYR 144 142 142 TYR TYR D . n 
D 3 145 GLN 145 143 143 GLN GLN D . n 
D 3 146 LYS 146 144 144 LYS LYS D . n 
D 3 147 TYR 147 145 145 TYR TYR D . n 
D 3 148 SER 148 146 146 SER SER D . n 
D 3 149 GLN 149 147 147 GLN GLN D . n 
D 3 150 ASN 150 148 148 ASN ASN D . n 
D 3 151 SER 151 149 149 SER SER D . n 
D 3 152 TRP 152 150 150 TRP TRP D . n 
D 3 153 ARG 153 151 151 ARG ARG D . n 
D 3 154 TYR 154 152 152 TYR TYR D . n 
D 3 155 LEU 155 153 153 LEU LEU D . n 
D 3 156 SER 156 154 154 SER SER D . n 
D 3 157 ASN 157 155 155 ASN ASN D . n 
D 3 158 ARG 158 156 156 ARG ARG D . n 
D 3 159 LEU 159 157 157 LEU LEU D . n 
D 3 160 LEU 160 158 158 LEU LEU D . n 
D 3 161 ALA 161 159 159 ALA ALA D . n 
D 3 162 PRO 162 160 160 PRO PRO D . n 
D 3 163 SER 163 161 161 SER SER D . n 
D 3 164 ASP 164 162 162 ASP ASP D . n 
D 3 165 SER 165 163 163 SER SER D . n 
D 3 166 PRO 166 164 164 PRO PRO D . n 
D 3 167 GLU 167 165 165 GLU GLU D . n 
D 3 168 TRP 168 166 166 TRP TRP D . n 
D 3 169 LEU 169 167 167 LEU LEU D . n 
D 3 170 SER 170 168 168 SER SER D . n 
D 3 171 PHE 171 169 169 PHE PHE D . n 
D 3 172 ASP 172 170 170 ASP ASP D . n 
D 3 173 VAL 173 171 171 VAL VAL D . n 
D 3 174 THR 174 172 172 THR THR D . n 
D 3 175 GLY 175 173 173 GLY GLY D . n 
D 3 176 VAL 176 174 174 VAL VAL D . n 
D 3 177 VAL 177 175 175 VAL VAL D . n 
D 3 178 ARG 178 176 176 ARG ARG D . n 
D 3 179 GLN 179 177 177 GLN GLN D . n 
D 3 180 TRP 180 178 178 TRP TRP D . n 
D 3 181 LEU 181 179 179 LEU LEU D . n 
D 3 182 SER 182 180 180 SER SER D . n 
D 3 183 ARG 183 181 181 ARG ARG D . n 
D 3 184 GLY 184 182 182 GLY GLY D . n 
D 3 185 GLY 185 183 183 GLY GLY D . n 
D 3 186 GLU 186 184 184 GLU GLU D . n 
D 3 187 ILE 187 185 185 ILE ILE D . n 
D 3 188 GLU 188 186 186 GLU GLU D . n 
D 3 189 GLY 189 187 187 GLY GLY D . n 
D 3 190 PHE 190 188 188 PHE PHE D . n 
D 3 191 ARG 191 189 189 ARG ARG D . n 
D 3 192 LEU 192 190 190 LEU LEU D . n 
D 3 193 SER 193 191 191 SER SER D . n 
D 3 194 ALA 194 192 192 ALA ALA D . n 
D 3 195 HIS 195 193 193 HIS HIS D . n 
D 3 196 CYS 196 194 194 CYS CYS D . n 
D 3 197 SER 197 195 195 SER SER D . n 
D 3 198 CYS 198 196 196 CYS CYS D . n 
D 3 199 ASP 199 197 197 ASP ASP D . n 
D 3 200 SER 200 198 ?   ?   ?   D . n 
D 3 201 ARG 201 199 ?   ?   ?   D . n 
D 3 202 ASP 202 200 ?   ?   ?   D . n 
D 3 203 ASN 203 201 ?   ?   ?   D . n 
D 3 204 THR 204 202 202 THR THR D . n 
D 3 205 LEU 205 203 203 LEU LEU D . n 
D 3 206 GLN 206 204 204 GLN GLN D . n 
D 3 207 VAL 207 205 205 VAL VAL D . n 
D 3 208 ASP 208 206 206 ASP ASP D . n 
D 3 209 ILE 209 207 207 ILE ILE D . n 
D 3 210 ASN 210 208 208 ASN ASN D . n 
D 3 211 GLY 211 209 209 GLY GLY D . n 
D 3 212 PHE 212 210 210 PHE PHE D . n 
D 3 213 THR 213 211 211 THR THR D . n 
D 3 214 THR 214 212 212 THR THR D . n 
D 3 215 GLY 215 213 213 GLY GLY D . n 
D 3 216 ARG 216 214 214 ARG ARG D . n 
D 3 217 ARG 217 215 215 ARG ARG D . n 
D 3 218 GLY 218 216 216 GLY GLY D . n 
D 3 219 ASP 219 217 217 ASP ASP D . n 
D 3 220 LEU 220 218 218 LEU LEU D . n 
D 3 221 ALA 221 219 219 ALA ALA D . n 
D 3 222 THR 222 220 220 THR THR D . n 
D 3 223 ILE 223 221 221 ILE ILE D . n 
D 3 224 HIS 224 222 222 HIS HIS D . n 
D 3 225 GLY 225 223 223 GLY GLY D . n 
D 3 226 MET 226 224 224 MET MET D . n 
D 3 227 ASN 227 225 225 ASN ASN D . n 
D 3 228 ARG 228 226 226 ARG ARG D . n 
D 3 229 PRO 229 227 227 PRO PRO D . n 
D 3 230 PHE 230 228 228 PHE PHE D . n 
D 3 231 LEU 231 229 229 LEU LEU D . n 
D 3 232 LEU 232 230 230 LEU LEU D . n 
D 3 233 LEU 233 231 231 LEU LEU D . n 
D 3 234 MET 234 232 232 MET MET D . n 
D 3 235 ALA 235 233 233 ALA ALA D . n 
D 3 236 THR 236 234 234 THR THR D . n 
D 3 237 PRO 237 235 235 PRO PRO D . n 
D 3 238 LEU 238 236 236 LEU LEU D . n 
D 3 239 GLU 239 237 237 GLU GLU D . n 
D 3 240 ARG 240 238 238 ARG ARG D . n 
D 3 241 ALA 241 239 239 ALA ALA D . n 
D 3 242 GLN 242 240 240 GLN GLN D . n 
D 3 243 HIS 243 241 ?   ?   ?   D . n 
D 3 244 LEU 244 242 ?   ?   ?   D . n 
D 3 245 GLN 245 243 ?   ?   ?   D . n 
D 3 246 SER 246 244 ?   ?   ?   D . n 
D 3 247 SER 247 245 ?   ?   ?   D . n 
D 3 248 ARG 248 246 ?   ?   ?   D . n 
D 3 249 HIS 249 247 ?   ?   ?   D . n 
D 3 250 ARG 250 248 ?   ?   ?   D . n 
D 3 251 ARG 251 249 ?   ?   ?   D . n 
D 3 252 ALA 252 250 ?   ?   ?   D . n 
D 3 253 LEU 253 251 ?   ?   ?   D . n 
D 3 254 ASP 254 252 ?   ?   ?   D . n 
D 3 255 THR 255 253 ?   ?   ?   D . n 
D 3 256 ASN 256 254 ?   ?   ?   D . n 
D 3 257 TYR 257 255 ?   ?   ?   D . n 
D 3 258 CYS 258 256 256 CYS CYS D . n 
D 3 259 PHE 259 257 257 PHE PHE D . n 
D 3 260 SER 260 258 258 SER SER D . n 
D 3 261 SER 261 259 259 SER SER D . n 
D 3 262 THR 262 260 260 THR THR D . n 
D 3 263 GLU 263 261 261 GLU GLU D . n 
D 3 264 LYS 264 262 262 LYS LYS D . n 
D 3 265 ASN 265 263 263 ASN ASN D . n 
D 3 266 CYS 266 264 264 CYS CYS D . n 
D 3 267 CYS 267 265 265 CYS CYS D . n 
D 3 268 VAL 268 266 266 VAL VAL D . n 
D 3 269 ARG 269 267 267 ARG ARG D . n 
D 3 270 GLN 270 268 268 GLN GLN D . n 
D 3 271 LEU 271 269 269 LEU LEU D . n 
D 3 272 TYR 272 270 270 TYR TYR D . n 
D 3 273 ILE 273 271 271 ILE ILE D . n 
D 3 274 ASP 274 272 272 ASP ASP D . n 
D 3 275 PHE 275 273 273 PHE PHE D . n 
D 3 276 ARG 276 274 274 ARG ARG D . n 
D 3 277 LYS 277 275 275 LYS LYS D . n 
D 3 278 ASP 278 276 276 ASP ASP D . n 
D 3 279 LEU 279 277 277 LEU LEU D . n 
D 3 280 GLY 280 278 278 GLY GLY D . n 
D 3 281 TRP 281 279 279 TRP TRP D . n 
D 3 282 LYS 282 280 280 LYS LYS D . n 
D 3 283 TRP 283 281 281 TRP TRP D . n 
D 3 284 ILE 284 282 282 ILE ILE D . n 
D 3 285 HIS 285 283 283 HIS HIS D . n 
D 3 286 GLU 286 284 284 GLU GLU D . n 
D 3 287 PRO 287 285 285 PRO PRO D . n 
D 3 288 LYS 288 286 286 LYS LYS D . n 
D 3 289 GLY 289 287 287 GLY GLY D . n 
D 3 290 TYR 290 288 288 TYR TYR D . n 
D 3 291 HIS 291 289 289 HIS HIS D . n 
D 3 292 ALA 292 290 290 ALA ALA D . n 
D 3 293 ASN 293 291 291 ASN ASN D . n 
D 3 294 PHE 294 292 292 PHE PHE D . n 
D 3 295 CYS 295 293 293 CYS CYS D . n 
D 3 296 LEU 296 294 294 LEU LEU D . n 
D 3 297 GLY 297 295 295 GLY GLY D . n 
D 3 298 PRO 298 296 296 PRO PRO D . n 
D 3 299 CYS 299 297 297 CYS CYS D . n 
D 3 300 PRO 300 298 298 PRO PRO D . n 
D 3 301 TYR 301 299 299 TYR TYR D . n 
D 3 302 ILE 302 300 300 ILE ILE D . n 
D 3 303 TRP 303 301 301 TRP TRP D . n 
D 3 304 SER 304 302 302 SER SER D . n 
D 3 305 LEU 305 303 303 LEU LEU D . n 
D 3 306 ASP 306 304 ?   ?   ?   D . n 
D 3 307 THR 307 305 ?   ?   ?   D . n 
D 3 308 GLN 308 306 ?   ?   ?   D . n 
D 3 309 TYR 309 307 ?   ?   ?   D . n 
D 3 310 SER 310 308 ?   ?   ?   D . n 
D 3 311 LYS 311 309 ?   ?   ?   D . n 
D 3 312 VAL 312 310 310 VAL VAL D . n 
D 3 313 LEU 313 311 311 LEU LEU D . n 
D 3 314 ALA 314 312 312 ALA ALA D . n 
D 3 315 LEU 315 313 313 LEU LEU D . n 
D 3 316 TYR 316 314 314 TYR TYR D . n 
D 3 317 ASN 317 315 315 ASN ASN D . n 
D 3 318 GLN 318 316 316 GLN GLN D . n 
D 3 319 HIS 319 317 317 HIS HIS D . n 
D 3 320 ASN 320 318 318 ASN ASN D . n 
D 3 321 PRO 321 319 319 PRO PRO D . n 
D 3 322 GLY 322 320 320 GLY GLY D . n 
D 3 323 ALA 323 321 321 ALA ALA D . n 
D 3 324 SER 324 322 322 SER SER D . n 
D 3 325 ALA 325 323 323 ALA ALA D . n 
D 3 326 ALA 326 324 324 ALA ALA D . n 
D 3 327 PRO 327 325 325 PRO PRO D . n 
D 3 328 CYS 328 326 326 CYS CYS D . n 
D 3 329 CYS 329 327 327 CYS CYS D . n 
D 3 330 VAL 330 328 328 VAL VAL D . n 
D 3 331 PRO 331 329 329 PRO PRO D . n 
D 3 332 GLN 332 330 330 GLN GLN D . n 
D 3 333 ALA 333 331 331 ALA ALA D . n 
D 3 334 LEU 334 332 332 LEU LEU D . n 
D 3 335 GLU 335 333 333 GLU GLU D . n 
D 3 336 PRO 336 334 334 PRO PRO D . n 
D 3 337 LEU 337 335 335 LEU LEU D . n 
D 3 338 PRO 338 336 336 PRO PRO D . n 
D 3 339 ILE 339 337 337 ILE ILE D . n 
D 3 340 VAL 340 338 338 VAL VAL D . n 
D 3 341 TYR 341 339 339 TYR TYR D . n 
D 3 342 TYR 342 340 340 TYR TYR D . n 
D 3 343 VAL 343 341 341 VAL VAL D . n 
D 3 344 GLY 344 342 ?   ?   ?   D . n 
D 3 345 ARG 345 343 343 ARG ARG D . n 
D 3 346 LYS 346 344 344 LYS LYS D . n 
D 3 347 PRO 347 345 345 PRO PRO D . n 
D 3 348 LYS 348 346 346 LYS LYS D . n 
D 3 349 VAL 349 347 347 VAL VAL D . n 
D 3 350 GLU 350 348 348 GLU GLU D . n 
D 3 351 GLN 351 349 349 GLN GLN D . n 
D 3 352 LEU 352 350 350 LEU LEU D . n 
D 3 353 SER 353 351 351 SER SER D . n 
D 3 354 ASN 354 352 352 ASN ASN D . n 
D 3 355 MET 355 353 353 MET MET D . n 
D 3 356 ILE 356 354 354 ILE ILE D . n 
D 3 357 VAL 357 355 355 VAL VAL D . n 
D 3 358 ARG 358 356 356 ARG ARG D . n 
D 3 359 SER 359 357 357 SER SER D . n 
D 3 360 CYS 360 358 358 CYS CYS D . n 
D 3 361 LYS 361 359 359 LYS LYS D . n 
D 3 362 CYS 362 360 360 CYS CYS D . n 
D 3 363 SER 363 361 361 SER SER D . n 
E 1 1   PHE 1   1   1   PHE PHE E . n 
E 1 2   ASN 2   2   2   ASN ASN E . n 
E 1 3   LEU 3   3   3   LEU LEU E . n 
E 1 4   ASP 4   4   4   ASP ASP E . n 
E 1 5   VAL 5   5   5   VAL VAL E . n 
E 1 6   ASP 6   6   6   ASP ASP E . n 
E 1 7   SER 7   7   7   SER SER E . n 
E 1 8   PRO 8   8   8   PRO PRO E . n 
E 1 9   ALA 9   9   9   ALA ALA E . n 
E 1 10  GLU 10  10  10  GLU GLU E . n 
E 1 11  TYR 11  11  11  TYR TYR E . n 
E 1 12  SER 12  12  12  SER SER E . n 
E 1 13  GLY 13  13  13  GLY GLY E . n 
E 1 14  PRO 14  14  14  PRO PRO E . n 
E 1 15  GLU 15  15  15  GLU GLU E . n 
E 1 16  GLY 16  16  16  GLY GLY E . n 
E 1 17  SER 17  17  17  SER SER E . n 
E 1 18  TYR 18  18  18  TYR TYR E . n 
E 1 19  PHE 19  19  19  PHE PHE E . n 
E 1 20  GLY 20  20  20  GLY GLY E . n 
E 1 21  PHE 21  21  21  PHE PHE E . n 
E 1 22  ALA 22  22  22  ALA ALA E . n 
E 1 23  VAL 23  23  23  VAL VAL E . n 
E 1 24  ASP 24  24  24  ASP ASP E . n 
E 1 25  PHE 25  25  25  PHE PHE E . n 
E 1 26  PHE 26  26  26  PHE PHE E . n 
E 1 27  VAL 27  27  27  VAL VAL E . n 
E 1 28  PRO 28  28  28  PRO PRO E . n 
E 1 29  SER 29  29  29  SER SER E . n 
E 1 30  ALA 30  30  30  ALA ALA E . n 
E 1 31  SER 31  31  31  SER SER E . n 
E 1 32  SER 32  32  32  SER SER E . n 
E 1 33  ARG 33  33  33  ARG ARG E . n 
E 1 34  MET 34  34  34  MET MET E . n 
E 1 35  PHE 35  35  35  PHE PHE E . n 
E 1 36  LEU 36  36  36  LEU LEU E . n 
E 1 37  LEU 37  37  37  LEU LEU E . n 
E 1 38  VAL 38  38  38  VAL VAL E . n 
E 1 39  GLY 39  39  39  GLY GLY E . n 
E 1 40  ALA 40  40  40  ALA ALA E . n 
E 1 41  PRO 41  41  41  PRO PRO E . n 
E 1 42  LYS 42  42  42  LYS LYS E . n 
E 1 43  ALA 43  43  43  ALA ALA E . n 
E 1 44  ASN 44  44  44  ASN ASN E . n 
E 1 45  THR 45  45  45  THR THR E . n 
E 1 46  THR 46  46  46  THR THR E . n 
E 1 47  GLN 47  47  47  GLN GLN E . n 
E 1 48  PRO 48  48  48  PRO PRO E . n 
E 1 49  GLY 49  49  49  GLY GLY E . n 
E 1 50  ILE 50  50  50  ILE ILE E . n 
E 1 51  VAL 51  51  51  VAL VAL E . n 
E 1 52  GLU 52  52  52  GLU GLU E . n 
E 1 53  GLY 53  53  53  GLY GLY E . n 
E 1 54  GLY 54  54  54  GLY GLY E . n 
E 1 55  GLN 55  55  55  GLN GLN E . n 
E 1 56  VAL 56  56  56  VAL VAL E . n 
E 1 57  LEU 57  57  57  LEU LEU E . n 
E 1 58  LYS 58  58  58  LYS LYS E . n 
E 1 59  CYS 59  59  59  CYS CYS E . n 
E 1 60  ASP 60  60  60  ASP ASP E . n 
E 1 61  TRP 61  61  61  TRP TRP E . n 
E 1 62  SER 62  62  62  SER SER E . n 
E 1 63  SER 63  63  63  SER SER E . n 
E 1 64  THR 64  64  64  THR THR E . n 
E 1 65  ARG 65  65  65  ARG ARG E . n 
E 1 66  ARG 66  66  66  ARG ARG E . n 
E 1 67  CYS 67  67  67  CYS CYS E . n 
E 1 68  GLN 68  68  68  GLN GLN E . n 
E 1 69  PRO 69  69  69  PRO PRO E . n 
E 1 70  ILE 70  70  70  ILE ILE E . n 
E 1 71  GLU 71  71  71  GLU GLU E . n 
E 1 72  PHE 72  72  72  PHE PHE E . n 
E 1 73  ASP 73  73  73  ASP ASP E . n 
E 1 74  ALA 74  74  74  ALA ALA E . n 
E 1 75  THR 75  75  75  THR THR E . n 
E 1 76  GLY 76  76  76  GLY GLY E . n 
E 1 77  ASN 77  77  77  ASN ASN E . n 
E 1 78  ARG 78  78  78  ARG ARG E . n 
E 1 79  ASP 79  79  79  ASP ASP E . n 
E 1 80  TYR 80  80  80  TYR TYR E . n 
E 1 81  ALA 81  81  81  ALA ALA E . n 
E 1 82  LYS 82  82  82  LYS LYS E . n 
E 1 83  ASP 83  83  83  ASP ASP E . n 
E 1 84  ASP 84  84  84  ASP ASP E . n 
E 1 85  PRO 85  85  85  PRO PRO E . n 
E 1 86  LEU 86  86  86  LEU LEU E . n 
E 1 87  GLU 87  87  87  GLU GLU E . n 
E 1 88  PHE 88  88  88  PHE PHE E . n 
E 1 89  LYS 89  89  89  LYS LYS E . n 
E 1 90  SER 90  90  90  SER SER E . n 
E 1 91  HIS 91  91  91  HIS HIS E . n 
E 1 92  GLN 92  92  92  GLN GLN E . n 
E 1 93  TRP 93  93  93  TRP TRP E . n 
E 1 94  PHE 94  94  94  PHE PHE E . n 
E 1 95  GLY 95  95  95  GLY GLY E . n 
E 1 96  ALA 96  96  96  ALA ALA E . n 
E 1 97  SER 97  97  97  SER SER E . n 
E 1 98  VAL 98  98  98  VAL VAL E . n 
E 1 99  ARG 99  99  99  ARG ARG E . n 
E 1 100 SER 100 100 100 SER SER E . n 
E 1 101 LYS 101 101 101 LYS LYS E . n 
E 1 102 GLN 102 102 102 GLN GLN E . n 
E 1 103 ASP 103 103 103 ASP ASP E . n 
E 1 104 LYS 104 104 104 LYS LYS E . n 
E 1 105 ILE 105 105 105 ILE ILE E . n 
E 1 106 LEU 106 106 106 LEU LEU E . n 
E 1 107 ALA 107 107 107 ALA ALA E . n 
E 1 108 CYS 108 108 108 CYS CYS E . n 
E 1 109 ALA 109 109 109 ALA ALA E . n 
E 1 110 PRO 110 110 110 PRO PRO E . n 
E 1 111 LEU 111 111 111 LEU LEU E . n 
E 1 112 TYR 112 112 112 TYR TYR E . n 
E 1 113 HIS 113 113 113 HIS HIS E . n 
E 1 114 TRP 114 114 114 TRP TRP E . n 
E 1 115 ARG 115 115 115 ARG ARG E . n 
E 1 116 THR 116 116 116 THR THR E . n 
E 1 117 GLU 117 117 117 GLU GLU E . n 
E 1 118 MET 118 118 118 MET MET E . n 
E 1 119 LYS 119 119 119 LYS LYS E . n 
E 1 120 GLN 120 120 120 GLN GLN E . n 
E 1 121 GLU 121 121 121 GLU GLU E . n 
E 1 122 ARG 122 122 122 ARG ARG E . n 
E 1 123 GLU 123 123 123 GLU GLU E . n 
E 1 124 PRO 124 124 124 PRO PRO E . n 
E 1 125 VAL 125 125 125 VAL VAL E . n 
E 1 126 GLY 126 126 126 GLY GLY E . n 
E 1 127 THR 127 127 127 THR THR E . n 
E 1 128 CYS 128 128 128 CYS CYS E . n 
E 1 129 PHE 129 129 129 PHE PHE E . n 
E 1 130 LEU 130 130 130 LEU LEU E . n 
E 1 131 GLN 131 131 131 GLN GLN E . n 
E 1 132 ASP 132 132 132 ASP ASP E . n 
E 1 133 GLY 133 133 133 GLY GLY E . n 
E 1 134 THR 134 134 134 THR THR E . n 
E 1 135 LYS 135 135 135 LYS LYS E . n 
E 1 136 THR 136 136 136 THR THR E . n 
E 1 137 VAL 137 137 137 VAL VAL E . n 
E 1 138 GLU 138 138 138 GLU GLU E . n 
E 1 139 TYR 139 139 139 TYR TYR E . n 
E 1 140 ALA 140 140 140 ALA ALA E . n 
E 1 141 PRO 141 141 141 PRO PRO E . n 
E 1 142 CYS 142 142 142 CYS CYS E . n 
E 1 143 ARG 143 143 143 ARG ARG E . n 
E 1 144 SER 144 144 144 SER SER E . n 
E 1 145 GLN 145 145 145 GLN GLN E . n 
E 1 146 ASP 146 146 146 ASP ASP E . n 
E 1 147 ILE 147 147 147 ILE ILE E . n 
E 1 148 ASP 148 148 148 ASP ASP E . n 
E 1 149 ALA 149 149 149 ALA ALA E . n 
E 1 150 ASP 150 150 150 ASP ASP E . n 
E 1 151 GLY 151 151 151 GLY GLY E . n 
E 1 152 GLN 152 152 152 GLN GLN E . n 
E 1 153 GLY 153 153 153 GLY GLY E . n 
E 1 154 PHE 154 154 154 PHE PHE E . n 
E 1 155 CYS 155 155 155 CYS CYS E . n 
E 1 156 GLN 156 156 156 GLN GLN E . n 
E 1 157 GLY 157 157 157 GLY GLY E . n 
E 1 158 GLY 158 158 158 GLY GLY E . n 
E 1 159 PHE 159 159 159 PHE PHE E . n 
E 1 160 SER 160 160 160 SER SER E . n 
E 1 161 ILE 161 161 161 ILE ILE E . n 
E 1 162 ASP 162 162 162 ASP ASP E . n 
E 1 163 PHE 163 163 163 PHE PHE E . n 
E 1 164 THR 164 164 164 THR THR E . n 
E 1 165 LYS 165 165 165 LYS LYS E . n 
E 1 166 ALA 166 166 166 ALA ALA E . n 
E 1 167 ASP 167 167 167 ASP ASP E . n 
E 1 168 ARG 168 168 168 ARG ARG E . n 
E 1 169 VAL 169 169 169 VAL VAL E . n 
E 1 170 LEU 170 170 170 LEU LEU E . n 
E 1 171 LEU 171 171 171 LEU LEU E . n 
E 1 172 GLY 172 172 172 GLY GLY E . n 
E 1 173 GLY 173 173 173 GLY GLY E . n 
E 1 174 PRO 174 174 174 PRO PRO E . n 
E 1 175 GLY 175 175 175 GLY GLY E . n 
E 1 176 SER 176 176 176 SER SER E . n 
E 1 177 PHE 177 177 177 PHE PHE E . n 
E 1 178 TYR 178 178 178 TYR TYR E . n 
E 1 179 TRP 179 179 179 TRP TRP E . n 
E 1 180 GLN 180 180 180 GLN GLN E . n 
E 1 181 GLY 181 181 181 GLY GLY E . n 
E 1 182 GLN 182 182 182 GLN GLN E . n 
E 1 183 LEU 183 183 183 LEU LEU E . n 
E 1 184 ILE 184 184 184 ILE ILE E . n 
E 1 185 SER 185 185 185 SER SER E . n 
E 1 186 ASP 186 186 186 ASP ASP E . n 
E 1 187 GLN 187 187 187 GLN GLN E . n 
E 1 188 VAL 188 188 188 VAL VAL E . n 
E 1 189 ALA 189 189 189 ALA ALA E . n 
E 1 190 GLU 190 190 190 GLU GLU E . n 
E 1 191 ILE 191 191 191 ILE ILE E . n 
E 1 192 VAL 192 192 192 VAL VAL E . n 
E 1 193 SER 193 193 193 SER SER E . n 
E 1 194 LYS 194 194 194 LYS LYS E . n 
E 1 195 TYR 195 195 195 TYR TYR E . n 
E 1 196 ASP 196 196 196 ASP ASP E . n 
E 1 197 PRO 197 197 197 PRO PRO E . n 
E 1 198 ASN 198 198 198 ASN ASN E . n 
E 1 199 VAL 199 199 199 VAL VAL E . n 
E 1 200 TYR 200 200 200 TYR TYR E . n 
E 1 201 SER 201 201 201 SER SER E . n 
E 1 202 ILE 202 202 202 ILE ILE E . n 
E 1 203 LYS 203 203 203 LYS LYS E . n 
E 1 204 TYR 204 204 204 TYR TYR E . n 
E 1 205 ASN 205 205 205 ASN ASN E . n 
E 1 206 ASN 206 206 206 ASN ASN E . n 
E 1 207 GLN 207 207 207 GLN GLN E . n 
E 1 208 LEU 208 208 208 LEU LEU E . n 
E 1 209 ALA 209 209 209 ALA ALA E . n 
E 1 210 THR 210 210 210 THR THR E . n 
E 1 211 ARG 211 211 211 ARG ARG E . n 
E 1 212 THR 212 212 212 THR THR E . n 
E 1 213 ALA 213 213 213 ALA ALA E . n 
E 1 214 GLN 214 214 214 GLN GLN E . n 
E 1 215 ALA 215 215 215 ALA ALA E . n 
E 1 216 ILE 216 216 216 ILE ILE E . n 
E 1 217 PHE 217 217 217 PHE PHE E . n 
E 1 218 ASP 218 218 218 ASP ASP E . n 
E 1 219 ASP 219 219 219 ASP ASP E . n 
E 1 220 SER 220 220 220 SER SER E . n 
E 1 221 TYR 221 221 221 TYR TYR E . n 
E 1 222 LEU 222 222 222 LEU LEU E . n 
E 1 223 GLY 223 223 223 GLY GLY E . n 
E 1 224 TYR 224 224 224 TYR TYR E . n 
E 1 225 SER 225 225 225 SER SER E . n 
E 1 226 VAL 226 226 226 VAL VAL E . n 
E 1 227 ALA 227 227 227 ALA ALA E . n 
E 1 228 VAL 228 228 228 VAL VAL E . n 
E 1 229 GLY 229 229 229 GLY GLY E . n 
E 1 230 ASP 230 230 230 ASP ASP E . n 
E 1 231 PHE 231 231 231 PHE PHE E . n 
E 1 232 ASN 232 232 232 ASN ASN E . n 
E 1 233 GLY 233 233 233 GLY GLY E . n 
E 1 234 ASP 234 234 234 ASP ASP E . n 
E 1 235 GLY 235 235 235 GLY GLY E . n 
E 1 236 ILE 236 236 236 ILE ILE E . n 
E 1 237 ASP 237 237 237 ASP ASP E . n 
E 1 238 ASP 238 238 238 ASP ASP E . n 
E 1 239 PHE 239 239 239 PHE PHE E . n 
E 1 240 VAL 240 240 240 VAL VAL E . n 
E 1 241 SER 241 241 241 SER SER E . n 
E 1 242 GLY 242 242 242 GLY GLY E . n 
E 1 243 VAL 243 243 243 VAL VAL E . n 
E 1 244 PRO 244 244 244 PRO PRO E . n 
E 1 245 ARG 245 245 245 ARG ARG E . n 
E 1 246 ALA 246 246 246 ALA ALA E . n 
E 1 247 ALA 247 247 247 ALA ALA E . n 
E 1 248 ARG 248 248 248 ARG ARG E . n 
E 1 249 THR 249 249 249 THR THR E . n 
E 1 250 LEU 250 250 250 LEU LEU E . n 
E 1 251 GLY 251 251 251 GLY GLY E . n 
E 1 252 MET 252 252 252 MET MET E . n 
E 1 253 VAL 253 253 253 VAL VAL E . n 
E 1 254 TYR 254 254 254 TYR TYR E . n 
E 1 255 ILE 255 255 255 ILE ILE E . n 
E 1 256 TYR 256 256 256 TYR TYR E . n 
E 1 257 ASP 257 257 257 ASP ASP E . n 
E 1 258 GLY 258 258 258 GLY GLY E . n 
E 1 259 LYS 259 259 259 LYS LYS E . n 
E 1 260 ASN 260 260 260 ASN ASN E . n 
E 1 261 MET 261 261 261 MET MET E . n 
E 1 262 SER 262 262 262 SER SER E . n 
E 1 263 SER 263 263 263 SER SER E . n 
E 1 264 LEU 264 264 264 LEU LEU E . n 
E 1 265 TYR 265 265 265 TYR TYR E . n 
E 1 266 ASN 266 266 266 ASN ASN E . n 
E 1 267 PHE 267 267 267 PHE PHE E . n 
E 1 268 THR 268 268 268 THR THR E . n 
E 1 269 GLY 269 269 269 GLY GLY E . n 
E 1 270 GLU 270 270 270 GLU GLU E . n 
E 1 271 GLN 271 271 271 GLN GLN E . n 
E 1 272 MET 272 272 272 MET MET E . n 
E 1 273 ALA 273 273 273 ALA ALA E . n 
E 1 274 ALA 274 274 274 ALA ALA E . n 
E 1 275 TYR 275 275 275 TYR TYR E . n 
E 1 276 PHE 276 276 276 PHE PHE E . n 
E 1 277 GLY 277 277 277 GLY GLY E . n 
E 1 278 PHE 278 278 278 PHE PHE E . n 
E 1 279 SER 279 279 279 SER SER E . n 
E 1 280 VAL 280 280 280 VAL VAL E . n 
E 1 281 ALA 281 281 281 ALA ALA E . n 
E 1 282 ALA 282 282 282 ALA ALA E . n 
E 1 283 THR 283 283 283 THR THR E . n 
E 1 284 ASP 284 284 284 ASP ASP E . n 
E 1 285 ILE 285 285 285 ILE ILE E . n 
E 1 286 ASN 286 286 286 ASN ASN E . n 
E 1 287 GLY 287 287 287 GLY GLY E . n 
E 1 288 ASP 288 288 288 ASP ASP E . n 
E 1 289 ASP 289 289 289 ASP ASP E . n 
E 1 290 TYR 290 290 290 TYR TYR E . n 
E 1 291 ALA 291 291 291 ALA ALA E . n 
E 1 292 ASP 292 292 292 ASP ASP E . n 
E 1 293 VAL 293 293 293 VAL VAL E . n 
E 1 294 PHE 294 294 294 PHE PHE E . n 
E 1 295 ILE 295 295 295 ILE ILE E . n 
E 1 296 GLY 296 296 296 GLY GLY E . n 
E 1 297 ALA 297 297 297 ALA ALA E . n 
E 1 298 PRO 298 298 298 PRO PRO E . n 
E 1 299 LEU 299 299 299 LEU LEU E . n 
E 1 300 PHE 300 300 300 PHE PHE E . n 
E 1 301 MET 301 301 301 MET MET E . n 
E 1 302 ASP 302 302 302 ASP ASP E . n 
E 1 303 ARG 303 303 303 ARG ARG E . n 
E 1 304 GLY 304 304 304 GLY GLY E . n 
E 1 305 SER 305 305 305 SER SER E . n 
E 1 306 ASP 306 306 306 ASP ASP E . n 
E 1 307 GLY 307 307 307 GLY GLY E . n 
E 1 308 LYS 308 308 308 LYS LYS E . n 
E 1 309 LEU 309 309 309 LEU LEU E . n 
E 1 310 GLN 310 310 310 GLN GLN E . n 
E 1 311 GLU 311 311 311 GLU GLU E . n 
E 1 312 VAL 312 312 312 VAL VAL E . n 
E 1 313 GLY 313 313 313 GLY GLY E . n 
E 1 314 GLN 314 314 314 GLN GLN E . n 
E 1 315 VAL 315 315 315 VAL VAL E . n 
E 1 316 SER 316 316 316 SER SER E . n 
E 1 317 VAL 317 317 317 VAL VAL E . n 
E 1 318 SER 318 318 318 SER SER E . n 
E 1 319 LEU 319 319 319 LEU LEU E . n 
E 1 320 GLN 320 320 320 GLN GLN E . n 
E 1 321 ARG 321 321 321 ARG ARG E . n 
E 1 322 ALA 322 322 322 ALA ALA E . n 
E 1 323 SER 323 323 323 SER SER E . n 
E 1 324 GLY 324 324 324 GLY GLY E . n 
E 1 325 ASP 325 325 325 ASP ASP E . n 
E 1 326 PHE 326 326 326 PHE PHE E . n 
E 1 327 GLN 327 327 327 GLN GLN E . n 
E 1 328 THR 328 328 328 THR THR E . n 
E 1 329 THR 329 329 329 THR THR E . n 
E 1 330 LYS 330 330 330 LYS LYS E . n 
E 1 331 LEU 331 331 331 LEU LEU E . n 
E 1 332 ASN 332 332 332 ASN ASN E . n 
E 1 333 GLY 333 333 333 GLY GLY E . n 
E 1 334 PHE 334 334 334 PHE PHE E . n 
E 1 335 GLU 335 335 335 GLU GLU E . n 
E 1 336 VAL 336 336 336 VAL VAL E . n 
E 1 337 PHE 337 337 337 PHE PHE E . n 
E 1 338 ALA 338 338 338 ALA ALA E . n 
E 1 339 ARG 339 339 339 ARG ARG E . n 
E 1 340 PHE 340 340 340 PHE PHE E . n 
E 1 341 GLY 341 341 341 GLY GLY E . n 
E 1 342 SER 342 342 342 SER SER E . n 
E 1 343 ALA 343 343 343 ALA ALA E . n 
E 1 344 ILE 344 344 344 ILE ILE E . n 
E 1 345 ALA 345 345 345 ALA ALA E . n 
E 1 346 PRO 346 346 346 PRO PRO E . n 
E 1 347 LEU 347 347 347 LEU LEU E . n 
E 1 348 GLY 348 348 348 GLY GLY E . n 
E 1 349 ASP 349 349 349 ASP ASP E . n 
E 1 350 LEU 350 350 350 LEU LEU E . n 
E 1 351 ASP 351 351 351 ASP ASP E . n 
E 1 352 GLN 352 352 352 GLN GLN E . n 
E 1 353 ASP 353 353 353 ASP ASP E . n 
E 1 354 GLY 354 354 354 GLY GLY E . n 
E 1 355 PHE 355 355 355 PHE PHE E . n 
E 1 356 ASN 356 356 356 ASN ASN E . n 
E 1 357 ASP 357 357 357 ASP ASP E . n 
E 1 358 ILE 358 358 358 ILE ILE E . n 
E 1 359 ALA 359 359 359 ALA ALA E . n 
E 1 360 ILE 360 360 360 ILE ILE E . n 
E 1 361 ALA 361 361 361 ALA ALA E . n 
E 1 362 ALA 362 362 362 ALA ALA E . n 
E 1 363 PRO 363 363 363 PRO PRO E . n 
E 1 364 TYR 364 364 364 TYR TYR E . n 
E 1 365 GLY 365 365 365 GLY GLY E . n 
E 1 366 GLY 366 366 366 GLY GLY E . n 
E 1 367 GLU 367 367 367 GLU GLU E . n 
E 1 368 ASP 368 368 368 ASP ASP E . n 
E 1 369 LYS 369 369 369 LYS LYS E . n 
E 1 370 LYS 370 370 370 LYS LYS E . n 
E 1 371 GLY 371 371 371 GLY GLY E . n 
E 1 372 ILE 372 372 372 ILE ILE E . n 
E 1 373 VAL 373 373 373 VAL VAL E . n 
E 1 374 TYR 374 374 374 TYR TYR E . n 
E 1 375 ILE 375 375 375 ILE ILE E . n 
E 1 376 PHE 376 376 376 PHE PHE E . n 
E 1 377 ASN 377 377 377 ASN ASN E . n 
E 1 378 GLY 378 378 378 GLY GLY E . n 
E 1 379 ARG 379 379 379 ARG ARG E . n 
E 1 380 SER 380 380 380 SER SER E . n 
E 1 381 THR 381 381 381 THR THR E . n 
E 1 382 GLY 382 382 382 GLY GLY E . n 
E 1 383 LEU 383 383 383 LEU LEU E . n 
E 1 384 ASN 384 384 384 ASN ASN E . n 
E 1 385 ALA 385 385 385 ALA ALA E . n 
E 1 386 VAL 386 386 386 VAL VAL E . n 
E 1 387 PRO 387 387 387 PRO PRO E . n 
E 1 388 SER 388 388 388 SER SER E . n 
E 1 389 GLN 389 389 389 GLN GLN E . n 
E 1 390 ILE 390 390 390 ILE ILE E . n 
E 1 391 LEU 391 391 391 LEU LEU E . n 
E 1 392 GLU 392 392 392 GLU GLU E . n 
E 1 393 GLY 393 393 393 GLY GLY E . n 
E 1 394 GLN 394 394 394 GLN GLN E . n 
E 1 395 TRP 395 395 395 TRP TRP E . n 
E 1 396 ALA 396 396 396 ALA ALA E . n 
E 1 397 ALA 397 397 397 ALA ALA E . n 
E 1 398 ARG 398 398 398 ARG ARG E . n 
E 1 399 SER 399 399 399 SER SER E . n 
E 1 400 GLY 400 400 400 GLY GLY E . n 
E 1 401 CYS 401 401 401 CYS CYS E . n 
E 1 402 PRO 402 402 402 PRO PRO E . n 
E 1 403 PRO 403 403 403 PRO PRO E . n 
E 1 404 SER 404 404 404 SER SER E . n 
E 1 405 PHE 405 405 405 PHE PHE E . n 
E 1 406 GLY 406 406 406 GLY GLY E . n 
E 1 407 TYR 407 407 407 TYR TYR E . n 
E 1 408 SER 408 408 408 SER SER E . n 
E 1 409 MET 409 409 409 MET MET E . n 
E 1 410 LYS 410 410 410 LYS LYS E . n 
E 1 411 GLY 411 411 411 GLY GLY E . n 
E 1 412 ALA 412 412 412 ALA ALA E . n 
E 1 413 THR 413 413 413 THR THR E . n 
E 1 414 ASP 414 414 414 ASP ASP E . n 
E 1 415 ILE 415 415 415 ILE ILE E . n 
E 1 416 ASP 416 416 416 ASP ASP E . n 
E 1 417 LYS 417 417 417 LYS LYS E . n 
E 1 418 ASN 418 418 418 ASN ASN E . n 
E 1 419 GLY 419 419 419 GLY GLY E . n 
E 1 420 TYR 420 420 420 TYR TYR E . n 
E 1 421 PRO 421 421 421 PRO PRO E . n 
E 1 422 ASP 422 422 422 ASP ASP E . n 
E 1 423 LEU 423 423 423 LEU LEU E . n 
E 1 424 ILE 424 424 424 ILE ILE E . n 
E 1 425 VAL 425 425 425 VAL VAL E . n 
E 1 426 GLY 426 426 426 GLY GLY E . n 
E 1 427 ALA 427 427 427 ALA ALA E . n 
E 1 428 PHE 428 428 428 PHE PHE E . n 
E 1 429 GLY 429 429 429 GLY GLY E . n 
E 1 430 VAL 430 430 430 VAL VAL E . n 
E 1 431 ASP 431 431 431 ASP ASP E . n 
E 1 432 ARG 432 432 432 ARG ARG E . n 
E 1 433 ALA 433 433 433 ALA ALA E . n 
E 1 434 ILE 434 434 434 ILE ILE E . n 
E 1 435 LEU 435 435 435 LEU LEU E . n 
E 1 436 TYR 436 436 436 TYR TYR E . n 
E 1 437 ARG 437 437 437 ARG ARG E . n 
E 1 438 ALA 438 438 438 ALA ALA E . n 
E 1 439 ARG 439 439 439 ARG ARG E . n 
E 1 440 PRO 440 440 440 PRO PRO E . n 
E 1 441 VAL 441 441 441 VAL VAL E . n 
E 1 442 ILE 442 442 442 ILE ILE E . n 
E 1 443 THR 443 443 443 THR THR E . n 
E 1 444 VAL 444 444 444 VAL VAL E . n 
E 1 445 ASN 445 445 445 ASN ASN E . n 
E 1 446 ALA 446 446 446 ALA ALA E . n 
E 1 447 GLY 447 447 447 GLY GLY E . n 
E 1 448 LEU 448 448 448 LEU LEU E . n 
E 1 449 GLU 449 449 449 GLU GLU E . n 
E 1 450 VAL 450 450 450 VAL VAL E . n 
E 1 451 TYR 451 451 451 TYR TYR E . n 
E 1 452 PRO 452 452 452 PRO PRO E . n 
E 1 453 SER 453 453 453 SER SER E . n 
E 1 454 ILE 454 454 454 ILE ILE E . n 
E 1 455 LEU 455 455 455 LEU LEU E . n 
E 1 456 ASN 456 456 456 ASN ASN E . n 
E 1 457 GLN 457 457 457 GLN GLN E . n 
E 1 458 ASP 458 458 458 ASP ASP E . n 
E 1 459 ASN 459 459 459 ASN ASN E . n 
E 1 460 LYS 460 460 460 LYS LYS E . n 
E 1 461 THR 461 461 461 THR THR E . n 
E 1 462 CYS 462 462 462 CYS CYS E . n 
E 1 463 SER 463 463 463 SER SER E . n 
E 1 464 LEU 464 464 464 LEU LEU E . n 
E 1 465 PRO 465 465 465 PRO PRO E . n 
E 1 466 GLY 466 466 ?   ?   ?   E . n 
E 1 467 THR 467 467 ?   ?   ?   E . n 
E 1 468 ALA 468 468 ?   ?   ?   E . n 
E 1 469 LEU 469 469 ?   ?   ?   E . n 
E 1 470 LYS 470 470 470 LYS LYS E . n 
E 1 471 VAL 471 471 471 VAL VAL E . n 
E 1 472 SER 472 472 472 SER SER E . n 
E 1 473 CYS 473 473 473 CYS CYS E . n 
E 1 474 PHE 474 474 474 PHE PHE E . n 
E 1 475 ASN 475 475 475 ASN ASN E . n 
E 1 476 VAL 476 476 476 VAL VAL E . n 
E 1 477 ARG 477 477 477 ARG ARG E . n 
E 1 478 PHE 478 478 478 PHE PHE E . n 
E 1 479 CYS 479 479 479 CYS CYS E . n 
E 1 480 LEU 480 480 480 LEU LEU E . n 
E 1 481 LYS 481 481 481 LYS LYS E . n 
E 1 482 ALA 482 482 482 ALA ALA E . n 
E 1 483 ASP 483 483 483 ASP ASP E . n 
E 1 484 GLY 484 484 484 GLY GLY E . n 
E 1 485 LYS 485 485 485 LYS LYS E . n 
E 1 486 GLY 486 486 486 GLY GLY E . n 
E 1 487 VAL 487 487 487 VAL VAL E . n 
E 1 488 LEU 488 488 488 LEU LEU E . n 
E 1 489 PRO 489 489 489 PRO PRO E . n 
E 1 490 ARG 490 490 490 ARG ARG E . n 
E 1 491 LYS 491 491 491 LYS LYS E . n 
E 1 492 LEU 492 492 492 LEU LEU E . n 
E 1 493 ASN 493 493 493 ASN ASN E . n 
E 1 494 PHE 494 494 494 PHE PHE E . n 
E 1 495 GLN 495 495 495 GLN GLN E . n 
E 1 496 VAL 496 496 496 VAL VAL E . n 
E 1 497 GLU 497 497 497 GLU GLU E . n 
E 1 498 LEU 498 498 498 LEU LEU E . n 
E 1 499 LEU 499 499 499 LEU LEU E . n 
E 1 500 LEU 500 500 500 LEU LEU E . n 
E 1 501 ASP 501 501 501 ASP ASP E . n 
E 1 502 LYS 502 502 502 LYS LYS E . n 
E 1 503 LEU 503 503 503 LEU LEU E . n 
E 1 504 LYS 504 504 504 LYS LYS E . n 
E 1 505 GLN 505 505 505 GLN GLN E . n 
E 1 506 LYS 506 506 506 LYS LYS E . n 
E 1 507 GLY 507 507 507 GLY GLY E . n 
E 1 508 ALA 508 508 508 ALA ALA E . n 
E 1 509 ILE 509 509 509 ILE ILE E . n 
E 1 510 ARG 510 510 510 ARG ARG E . n 
E 1 511 ARG 511 511 511 ARG ARG E . n 
E 1 512 ALA 512 512 512 ALA ALA E . n 
E 1 513 LEU 513 513 513 LEU LEU E . n 
E 1 514 PHE 514 514 514 PHE PHE E . n 
E 1 515 LEU 515 515 515 LEU LEU E . n 
E 1 516 TYR 516 516 516 TYR TYR E . n 
E 1 517 SER 517 517 517 SER SER E . n 
E 1 518 ARG 518 518 518 ARG ARG E . n 
E 1 519 SER 519 519 519 SER SER E . n 
E 1 520 PRO 520 520 520 PRO PRO E . n 
E 1 521 SER 521 521 521 SER SER E . n 
E 1 522 HIS 522 522 522 HIS HIS E . n 
E 1 523 SER 523 523 523 SER SER E . n 
E 1 524 LYS 524 524 524 LYS LYS E . n 
E 1 525 ASN 525 525 525 ASN ASN E . n 
E 1 526 MET 526 526 526 MET MET E . n 
E 1 527 THR 527 527 527 THR THR E . n 
E 1 528 ILE 528 528 528 ILE ILE E . n 
E 1 529 SER 529 529 529 SER SER E . n 
E 1 530 ARG 530 530 530 ARG ARG E . n 
E 1 531 GLY 531 531 531 GLY GLY E . n 
E 1 532 GLY 532 532 532 GLY GLY E . n 
E 1 533 LEU 533 533 533 LEU LEU E . n 
E 1 534 MET 534 534 534 MET MET E . n 
E 1 535 GLN 535 535 535 GLN GLN E . n 
E 1 536 CYS 536 536 536 CYS CYS E . n 
E 1 537 GLU 537 537 537 GLU GLU E . n 
E 1 538 GLU 538 538 538 GLU GLU E . n 
E 1 539 LEU 539 539 539 LEU LEU E . n 
E 1 540 ILE 540 540 540 ILE ILE E . n 
E 1 541 ALA 541 541 541 ALA ALA E . n 
E 1 542 TYR 542 542 542 TYR TYR E . n 
E 1 543 LEU 543 543 543 LEU LEU E . n 
E 1 544 ARG 544 544 544 ARG ARG E . n 
E 1 545 ASP 545 545 545 ASP ASP E . n 
E 1 546 GLU 546 546 546 GLU GLU E . n 
E 1 547 SER 547 547 547 SER SER E . n 
E 1 548 GLU 548 548 548 GLU GLU E . n 
E 1 549 PHE 549 549 549 PHE PHE E . n 
E 1 550 ARG 550 550 550 ARG ARG E . n 
E 1 551 ASP 551 551 551 ASP ASP E . n 
E 1 552 LYS 552 552 552 LYS LYS E . n 
E 1 553 LEU 553 553 553 LEU LEU E . n 
E 1 554 THR 554 554 554 THR THR E . n 
E 1 555 PRO 555 555 555 PRO PRO E . n 
E 1 556 ILE 556 556 556 ILE ILE E . n 
E 1 557 THR 557 557 557 THR THR E . n 
E 1 558 ILE 558 558 558 ILE ILE E . n 
E 1 559 PHE 559 559 559 PHE PHE E . n 
E 1 560 MET 560 560 560 MET MET E . n 
E 1 561 GLU 561 561 561 GLU GLU E . n 
E 1 562 TYR 562 562 562 TYR TYR E . n 
E 1 563 ARG 563 563 563 ARG ARG E . n 
E 1 564 LEU 564 564 564 LEU LEU E . n 
E 1 565 ASP 565 565 565 ASP ASP E . n 
E 1 566 TYR 566 566 566 TYR TYR E . n 
E 1 567 ARG 567 567 567 ARG ARG E . n 
E 1 568 THR 568 568 568 THR THR E . n 
E 1 569 ALA 569 569 569 ALA ALA E . n 
E 1 570 ALA 570 570 570 ALA ALA E . n 
E 1 571 ASP 571 571 571 ASP ASP E . n 
E 1 572 THR 572 572 572 THR THR E . n 
E 1 573 THR 573 573 573 THR THR E . n 
E 1 574 GLY 574 574 574 GLY GLY E . n 
E 1 575 LEU 575 575 575 LEU LEU E . n 
E 1 576 GLN 576 576 576 GLN GLN E . n 
E 1 577 PRO 577 577 577 PRO PRO E . n 
E 1 578 ILE 578 578 578 ILE ILE E . n 
E 1 579 LEU 579 579 579 LEU LEU E . n 
E 1 580 ASN 580 580 580 ASN ASN E . n 
E 1 581 GLN 581 581 581 GLN GLN E . n 
E 1 582 PHE 582 582 582 PHE PHE E . n 
E 1 583 THR 583 583 583 THR THR E . n 
E 1 584 PRO 584 584 584 PRO PRO E . n 
E 1 585 ALA 585 585 585 ALA ALA E . n 
E 1 586 ASN 586 586 586 ASN ASN E . n 
E 1 587 ILE 587 587 587 ILE ILE E . n 
E 1 588 SER 588 588 588 SER SER E . n 
E 1 589 ARG 589 589 589 ARG ARG E . n 
E 1 590 GLN 590 590 590 GLN GLN E . n 
E 1 591 ALA 591 591 591 ALA ALA E . n 
E 1 592 HIS 592 592 ?   ?   ?   E . n 
E 1 593 ILE 593 593 ?   ?   ?   E . n 
E 1 594 LEU 594 594 ?   ?   ?   E . n 
E 1 595 LEU 595 595 ?   ?   ?   E . n 
E 1 596 ASP 596 596 ?   ?   ?   E . n 
E 1 597 THR 597 597 ?   ?   ?   E . n 
E 1 598 GLY 598 598 ?   ?   ?   E . n 
E 1 599 GLY 599 599 ?   ?   ?   E . n 
E 1 600 LEU 600 600 ?   ?   ?   E . n 
E 1 601 GLU 601 601 ?   ?   ?   E . n 
F 2 1   THR 1   111 ?   ?   ?   F . n 
F 2 2   GLU 2   112 ?   ?   ?   F . n 
F 2 3   ASP 3   113 113 ASP ASP F . n 
F 2 4   TYR 4   114 114 TYR TYR F . n 
F 2 5   PRO 5   115 115 PRO PRO F . n 
F 2 6   VAL 6   116 116 VAL VAL F . n 
F 2 7   ASP 7   117 117 ASP ASP F . n 
F 2 8   LEU 8   118 118 LEU LEU F . n 
F 2 9   TYR 9   119 119 TYR TYR F . n 
F 2 10  TYR 10  120 120 TYR TYR F . n 
F 2 11  LEU 11  121 121 LEU LEU F . n 
F 2 12  MET 12  122 122 MET MET F . n 
F 2 13  ASP 13  123 123 ASP ASP F . n 
F 2 14  LEU 14  124 124 LEU LEU F . n 
F 2 15  SER 15  125 125 SER SER F . n 
F 2 16  ALA 16  126 126 ALA ALA F . n 
F 2 17  SER 17  127 127 SER SER F . n 
F 2 18  MET 18  128 128 MET MET F . n 
F 2 19  ASP 19  129 129 ASP ASP F . n 
F 2 20  ASP 20  130 130 ASP ASP F . n 
F 2 21  ASP 21  131 131 ASP ASP F . n 
F 2 22  LEU 22  132 132 LEU LEU F . n 
F 2 23  ASN 23  133 133 ASN ASN F . n 
F 2 24  THR 24  134 134 THR THR F . n 
F 2 25  ILE 25  135 135 ILE ILE F . n 
F 2 26  LYS 26  136 136 LYS LYS F . n 
F 2 27  GLU 27  137 137 GLU GLU F . n 
F 2 28  LEU 28  138 138 LEU LEU F . n 
F 2 29  GLY 29  139 139 GLY GLY F . n 
F 2 30  SER 30  140 140 SER SER F . n 
F 2 31  ARG 31  141 141 ARG ARG F . n 
F 2 32  LEU 32  142 142 LEU LEU F . n 
F 2 33  SER 33  143 143 SER SER F . n 
F 2 34  LYS 34  144 144 LYS LYS F . n 
F 2 35  GLU 35  145 145 GLU GLU F . n 
F 2 36  MET 36  146 146 MET MET F . n 
F 2 37  SER 37  147 147 SER SER F . n 
F 2 38  LYS 38  148 148 LYS LYS F . n 
F 2 39  LEU 39  149 149 LEU LEU F . n 
F 2 40  THR 40  150 150 THR THR F . n 
F 2 41  SER 41  151 151 SER SER F . n 
F 2 42  ASN 42  152 152 ASN ASN F . n 
F 2 43  PHE 43  153 153 PHE PHE F . n 
F 2 44  ARG 44  154 154 ARG ARG F . n 
F 2 45  LEU 45  155 155 LEU LEU F . n 
F 2 46  GLY 46  156 156 GLY GLY F . n 
F 2 47  PHE 47  157 157 PHE PHE F . n 
F 2 48  GLY 48  158 158 GLY GLY F . n 
F 2 49  SER 49  159 159 SER SER F . n 
F 2 50  PHE 50  160 160 PHE PHE F . n 
F 2 51  VAL 51  161 161 VAL VAL F . n 
F 2 52  GLU 52  162 162 GLU GLU F . n 
F 2 53  LYS 53  163 163 LYS LYS F . n 
F 2 54  PRO 54  164 164 PRO PRO F . n 
F 2 55  VAL 55  165 165 VAL VAL F . n 
F 2 56  SER 56  166 166 SER SER F . n 
F 2 57  PRO 57  167 167 PRO PRO F . n 
F 2 58  PHE 58  168 168 PHE PHE F . n 
F 2 59  VAL 59  169 169 VAL VAL F . n 
F 2 60  LYS 60  170 170 LYS LYS F . n 
F 2 61  THR 61  171 171 THR THR F . n 
F 2 62  THR 62  172 172 THR THR F . n 
F 2 63  PRO 63  173 173 PRO PRO F . n 
F 2 64  GLU 64  174 174 GLU GLU F . n 
F 2 65  GLU 65  175 175 GLU GLU F . n 
F 2 66  ILE 66  176 176 ILE ILE F . n 
F 2 67  ALA 67  177 177 ALA ALA F . n 
F 2 68  ASN 68  178 178 ASN ASN F . n 
F 2 69  PRO 69  179 179 PRO PRO F . n 
F 2 70  CYS 70  180 180 CYS CYS F . n 
F 2 71  SER 71  181 181 SER SER F . n 
F 2 72  SER 72  182 182 SER SER F . n 
F 2 73  ILE 73  183 183 ILE ILE F . n 
F 2 74  PRO 74  184 184 PRO PRO F . n 
F 2 75  TYR 75  185 185 TYR TYR F . n 
F 2 76  PHE 76  186 186 PHE PHE F . n 
F 2 77  CYS 77  187 187 CYS CYS F . n 
F 2 78  LEU 78  188 188 LEU LEU F . n 
F 2 79  PRO 79  189 189 PRO PRO F . n 
F 2 80  THR 80  190 190 THR THR F . n 
F 2 81  PHE 81  191 191 PHE PHE F . n 
F 2 82  GLY 82  192 192 GLY GLY F . n 
F 2 83  PHE 83  193 193 PHE PHE F . n 
F 2 84  LYS 84  194 194 LYS LYS F . n 
F 2 85  HIS 85  195 195 HIS HIS F . n 
F 2 86  ILE 86  196 196 ILE ILE F . n 
F 2 87  LEU 87  197 197 LEU LEU F . n 
F 2 88  PRO 88  198 198 PRO PRO F . n 
F 2 89  LEU 89  199 199 LEU LEU F . n 
F 2 90  THR 90  200 200 THR THR F . n 
F 2 91  ASN 91  201 201 ASN ASN F . n 
F 2 92  ASP 92  202 202 ASP ASP F . n 
F 2 93  ALA 93  203 203 ALA ALA F . n 
F 2 94  GLU 94  204 204 GLU GLU F . n 
F 2 95  ARG 95  205 205 ARG ARG F . n 
F 2 96  PHE 96  206 206 PHE PHE F . n 
F 2 97  ASN 97  207 207 ASN ASN F . n 
F 2 98  GLU 98  208 208 GLU GLU F . n 
F 2 99  ILE 99  209 209 ILE ILE F . n 
F 2 100 VAL 100 210 210 VAL VAL F . n 
F 2 101 LYS 101 211 211 LYS LYS F . n 
F 2 102 ASN 102 212 212 ASN ASN F . n 
F 2 103 GLN 103 213 213 GLN GLN F . n 
F 2 104 LYS 104 214 214 LYS LYS F . n 
F 2 105 ILE 105 215 215 ILE ILE F . n 
F 2 106 SER 106 216 216 SER SER F . n 
F 2 107 ALA 107 217 217 ALA ALA F . n 
F 2 108 ASN 108 218 218 ASN ASN F . n 
F 2 109 ILE 109 219 219 ILE ILE F . n 
F 2 110 ASP 110 220 220 ASP ASP F . n 
F 2 111 THR 111 221 221 THR THR F . n 
F 2 112 PRO 112 222 222 PRO PRO F . n 
F 2 113 GLU 113 223 223 GLU GLU F . n 
F 2 114 GLY 114 224 224 GLY GLY F . n 
F 2 115 GLY 115 225 225 GLY GLY F . n 
F 2 116 PHE 116 226 226 PHE PHE F . n 
F 2 117 ASP 117 227 227 ASP ASP F . n 
F 2 118 ALA 118 228 228 ALA ALA F . n 
F 2 119 ILE 119 229 229 ILE ILE F . n 
F 2 120 MET 120 230 230 MET MET F . n 
F 2 121 GLN 121 231 231 GLN GLN F . n 
F 2 122 ALA 122 232 232 ALA ALA F . n 
F 2 123 ALA 123 233 233 ALA ALA F . n 
F 2 124 VAL 124 234 234 VAL VAL F . n 
F 2 125 CYS 125 235 235 CYS CYS F . n 
F 2 126 LYS 126 236 236 LYS LYS F . n 
F 2 127 GLU 127 237 237 GLU GLU F . n 
F 2 128 LYS 128 238 238 LYS LYS F . n 
F 2 129 ILE 129 239 239 ILE ILE F . n 
F 2 130 GLY 130 240 240 GLY GLY F . n 
F 2 131 TRP 131 241 241 TRP TRP F . n 
F 2 132 ARG 132 242 242 ARG ARG F . n 
F 2 133 ASN 133 243 243 ASN ASN F . n 
F 2 134 ASP 134 244 244 ASP ASP F . n 
F 2 135 SER 135 245 245 SER SER F . n 
F 2 136 LEU 136 246 246 LEU LEU F . n 
F 2 137 HIS 137 247 247 HIS HIS F . n 
F 2 138 LEU 138 248 248 LEU LEU F . n 
F 2 139 LEU 139 249 249 LEU LEU F . n 
F 2 140 VAL 140 250 250 VAL VAL F . n 
F 2 141 PHE 141 251 251 PHE PHE F . n 
F 2 142 VAL 142 252 252 VAL VAL F . n 
F 2 143 SER 143 253 253 SER SER F . n 
F 2 144 ASP 144 254 254 ASP ASP F . n 
F 2 145 ALA 145 255 255 ALA ALA F . n 
F 2 146 ASP 146 256 256 ASP ASP F . n 
F 2 147 SER 147 257 257 SER SER F . n 
F 2 148 HIS 148 258 258 HIS HIS F . n 
F 2 149 PHE 149 259 259 PHE PHE F . n 
F 2 150 GLY 150 260 260 GLY GLY F . n 
F 2 151 MET 151 261 261 MET MET F . n 
F 2 152 ASP 152 262 262 ASP ASP F . n 
F 2 153 SER 153 263 263 SER SER F . n 
F 2 154 LYS 154 264 264 LYS LYS F . n 
F 2 155 LEU 155 265 265 LEU LEU F . n 
F 2 156 ALA 156 266 266 ALA ALA F . n 
F 2 157 GLY 157 267 267 GLY GLY F . n 
F 2 158 ILE 158 268 268 ILE ILE F . n 
F 2 159 VAL 159 269 269 VAL VAL F . n 
F 2 160 CYS 160 270 270 CYS CYS F . n 
F 2 161 PRO 161 271 271 PRO PRO F . n 
F 2 162 ASN 162 272 272 ASN ASN F . n 
F 2 163 ASP 163 273 273 ASP ASP F . n 
F 2 164 GLY 164 274 274 GLY GLY F . n 
F 2 165 LEU 165 275 275 LEU LEU F . n 
F 2 166 CYS 166 276 276 CYS CYS F . n 
F 2 167 HIS 167 277 277 HIS HIS F . n 
F 2 168 LEU 168 278 278 LEU LEU F . n 
F 2 169 ASP 169 279 279 ASP ASP F . n 
F 2 170 SER 170 280 280 SER SER F . n 
F 2 171 LYS 171 281 281 LYS LYS F . n 
F 2 172 ASN 172 282 282 ASN ASN F . n 
F 2 173 GLU 173 283 283 GLU GLU F . n 
F 2 174 TYR 174 284 284 TYR TYR F . n 
F 2 175 SER 175 285 285 SER SER F . n 
F 2 176 MET 176 286 286 MET MET F . n 
F 2 177 SER 177 287 287 SER SER F . n 
F 2 178 THR 178 288 288 THR THR F . n 
F 2 179 VAL 179 289 289 VAL VAL F . n 
F 2 180 LEU 180 290 290 LEU LEU F . n 
F 2 181 GLU 181 291 291 GLU GLU F . n 
F 2 182 TYR 182 292 292 TYR TYR F . n 
F 2 183 PRO 183 293 293 PRO PRO F . n 
F 2 184 THR 184 294 294 THR THR F . n 
F 2 185 ILE 185 295 295 ILE ILE F . n 
F 2 186 GLY 186 296 296 GLY GLY F . n 
F 2 187 GLN 187 297 297 GLN GLN F . n 
F 2 188 LEU 188 298 298 LEU LEU F . n 
F 2 189 ILE 189 299 299 ILE ILE F . n 
F 2 190 ASP 190 300 300 ASP ASP F . n 
F 2 191 LYS 191 301 301 LYS LYS F . n 
F 2 192 LEU 192 302 302 LEU LEU F . n 
F 2 193 VAL 193 303 303 VAL VAL F . n 
F 2 194 GLN 194 304 304 GLN GLN F . n 
F 2 195 ASN 195 305 305 ASN ASN F . n 
F 2 196 ASN 196 306 306 ASN ASN F . n 
F 2 197 VAL 197 307 307 VAL VAL F . n 
F 2 198 LEU 198 308 308 LEU LEU F . n 
F 2 199 LEU 199 309 309 LEU LEU F . n 
F 2 200 ILE 200 310 310 ILE ILE F . n 
F 2 201 PHE 201 311 311 PHE PHE F . n 
F 2 202 ALA 202 312 312 ALA ALA F . n 
F 2 203 VAL 203 313 313 VAL VAL F . n 
F 2 204 THR 204 314 314 THR THR F . n 
F 2 205 GLN 205 315 315 GLN GLN F . n 
F 2 206 GLU 206 316 316 GLU GLU F . n 
F 2 207 GLN 207 317 317 GLN GLN F . n 
F 2 208 VAL 208 318 318 VAL VAL F . n 
F 2 209 HIS 209 319 319 HIS HIS F . n 
F 2 210 LEU 210 320 320 LEU LEU F . n 
F 2 211 TYR 211 321 321 TYR TYR F . n 
F 2 212 GLU 212 322 322 GLU GLU F . n 
F 2 213 ASN 213 323 323 ASN ASN F . n 
F 2 214 TYR 214 324 324 TYR TYR F . n 
F 2 215 ALA 215 325 325 ALA ALA F . n 
F 2 216 LYS 216 326 326 LYS LYS F . n 
F 2 217 LEU 217 327 327 LEU LEU F . n 
F 2 218 ILE 218 328 328 ILE ILE F . n 
F 2 219 PRO 219 329 329 PRO PRO F . n 
F 2 220 GLY 220 330 330 GLY GLY F . n 
F 2 221 ALA 221 331 331 ALA ALA F . n 
F 2 222 THR 222 332 332 THR THR F . n 
F 2 223 VAL 223 333 333 VAL VAL F . n 
F 2 224 GLY 224 334 334 GLY GLY F . n 
F 2 225 LEU 225 335 335 LEU LEU F . n 
F 2 226 LEU 226 336 336 LEU LEU F . n 
F 2 227 GLN 227 337 337 GLN GLN F . n 
F 2 228 LYS 228 338 338 LYS LYS F . n 
F 2 229 ASP 229 339 339 ASP ASP F . n 
F 2 230 SER 230 340 340 SER SER F . n 
F 2 231 GLY 231 341 341 GLY GLY F . n 
F 2 232 ASN 232 342 342 ASN ASN F . n 
F 2 233 ILE 233 343 343 ILE ILE F . n 
F 2 234 LEU 234 344 344 LEU LEU F . n 
F 2 235 GLN 235 345 345 GLN GLN F . n 
F 2 236 LEU 236 346 346 LEU LEU F . n 
F 2 237 ILE 237 347 347 ILE ILE F . n 
F 2 238 ILE 238 348 348 ILE ILE F . n 
F 2 239 SER 239 349 349 SER SER F . n 
F 2 240 ALA 240 350 350 ALA ALA F . n 
F 2 241 TYR 241 351 351 TYR TYR F . n 
F 2 242 GLU 242 352 352 GLU GLU F . n 
F 2 243 GLU 243 353 353 GLU GLU F . n 
F 2 244 LEU 244 354 354 LEU LEU F . n 
F 2 245 ARG 245 355 ?   ?   ?   F . n 
F 2 246 SER 246 356 ?   ?   ?   F . n 
F 2 247 GLU 247 357 ?   ?   ?   F . n 
F 2 248 VAL 248 358 ?   ?   ?   F . n 
F 2 249 GLU 249 359 ?   ?   ?   F . n 
F 2 250 LEU 250 360 ?   ?   ?   F . n 
F 2 251 GLU 251 361 ?   ?   ?   F . n 
F 2 252 HIS 252 362 ?   ?   ?   F . n 
F 2 253 HIS 253 363 ?   ?   ?   F . n 
F 2 254 HIS 254 364 ?   ?   ?   F . n 
F 2 255 HIS 255 365 ?   ?   ?   F . n 
F 2 256 HIS 256 366 ?   ?   ?   F . n 
F 2 257 HIS 257 367 ?   ?   ?   F . n 
G 3 1   GLY 1   -1  ?   ?   ?   G . n 
G 3 2   PRO 2   0   ?   ?   ?   G . n 
G 3 3   LEU 3   1   ?   ?   ?   G . n 
G 3 4   SER 4   2   ?   ?   ?   G . n 
G 3 5   THR 5   3   ?   ?   ?   G . n 
G 3 6   SER 6   4   ?   ?   ?   G . n 
G 3 7   LYS 7   5   ?   ?   ?   G . n 
G 3 8   THR 8   6   ?   ?   ?   G . n 
G 3 9   ILE 9   7   ?   ?   ?   G . n 
G 3 10  ASP 10  8   ?   ?   ?   G . n 
G 3 11  MET 11  9   ?   ?   ?   G . n 
G 3 12  GLU 12  10  10  GLU GLU G . n 
G 3 13  LEU 13  11  11  LEU LEU G . n 
G 3 14  VAL 14  12  12  VAL VAL G . n 
G 3 15  LYS 15  13  13  LYS LYS G . n 
G 3 16  ARG 16  14  14  ARG ARG G . n 
G 3 17  LYS 17  15  15  LYS LYS G . n 
G 3 18  ARG 18  16  16  ARG ARG G . n 
G 3 19  ILE 19  17  17  ILE ILE G . n 
G 3 20  GLU 20  18  18  GLU GLU G . n 
G 3 21  ALA 21  19  19  ALA ALA G . n 
G 3 22  ILE 22  20  20  ILE ILE G . n 
G 3 23  ARG 23  21  21  ARG ARG G . n 
G 3 24  GLY 24  22  22  GLY GLY G . n 
G 3 25  GLN 25  23  23  GLN GLN G . n 
G 3 26  ILE 26  24  24  ILE ILE G . n 
G 3 27  LEU 27  25  25  LEU LEU G . n 
G 3 28  SER 28  26  26  SER SER G . n 
G 3 29  LYS 29  27  27  LYS LYS G . n 
G 3 30  LEU 30  28  28  LEU LEU G . n 
G 3 31  ARG 31  29  29  ARG ARG G . n 
G 3 32  LEU 32  30  30  LEU LEU G . n 
G 3 33  ALA 33  31  31  ALA ALA G . n 
G 3 34  SER 34  32  32  SER SER G . n 
G 3 35  PRO 35  33  33  PRO PRO G . n 
G 3 36  PRO 36  34  34  PRO PRO G . n 
G 3 37  SER 37  35  35  SER SER G . n 
G 3 38  GLN 38  36  ?   ?   ?   G . n 
G 3 39  GLY 39  37  ?   ?   ?   G . n 
G 3 40  GLU 40  38  38  GLU GLU G . n 
G 3 41  VAL 41  39  39  VAL VAL G . n 
G 3 42  PRO 42  40  40  PRO PRO G . n 
G 3 43  PRO 43  41  41  PRO PRO G . n 
G 3 44  GLY 44  42  42  GLY GLY G . n 
G 3 45  PRO 45  43  43  PRO PRO G . n 
G 3 46  LEU 46  44  44  LEU LEU G . n 
G 3 47  PRO 47  45  45  PRO PRO G . n 
G 3 48  GLU 48  46  46  GLU GLU G . n 
G 3 49  ALA 49  47  47  ALA ALA G . n 
G 3 50  VAL 50  48  48  VAL VAL G . n 
G 3 51  LEU 51  49  49  LEU LEU G . n 
G 3 52  ALA 52  50  50  ALA ALA G . n 
G 3 53  LEU 53  51  51  LEU LEU G . n 
G 3 54  TYR 54  52  52  TYR TYR G . n 
G 3 55  ASN 55  53  53  ASN ASN G . n 
G 3 56  SER 56  54  54  SER SER G . n 
G 3 57  THR 57  55  55  THR THR G . n 
G 3 58  ARG 58  56  56  ARG ARG G . n 
G 3 59  ASP 59  57  57  ASP ASP G . n 
G 3 60  ARG 60  58  58  ARG ARG G . n 
G 3 61  VAL 61  59  59  VAL VAL G . n 
G 3 62  ALA 62  60  60  ALA ALA G . n 
G 3 63  GLY 63  61  ?   ?   ?   G . n 
G 3 64  GLU 64  62  ?   ?   ?   G . n 
G 3 65  SER 65  63  ?   ?   ?   G . n 
G 3 66  ALA 66  64  ?   ?   ?   G . n 
G 3 67  GLU 67  65  ?   ?   ?   G . n 
G 3 68  PRO 68  66  ?   ?   ?   G . n 
G 3 69  GLU 69  67  ?   ?   ?   G . n 
G 3 70  PRO 70  68  ?   ?   ?   G . n 
G 3 71  GLU 71  69  ?   ?   ?   G . n 
G 3 72  PRO 72  70  ?   ?   ?   G . n 
G 3 73  GLU 73  71  ?   ?   ?   G . n 
G 3 74  ALA 74  72  72  ALA ALA G . n 
G 3 75  ASP 75  73  73  ASP ASP G . n 
G 3 76  TYR 76  74  74  TYR TYR G . n 
G 3 77  TYR 77  75  75  TYR TYR G . n 
G 3 78  ALA 78  76  76  ALA ALA G . n 
G 3 79  LYS 79  77  77  LYS LYS G . n 
G 3 80  GLU 80  78  78  GLU GLU G . n 
G 3 81  VAL 81  79  79  VAL VAL G . n 
G 3 82  THR 82  80  80  THR THR G . n 
G 3 83  ARG 83  81  81  ARG ARG G . n 
G 3 84  VAL 84  82  82  VAL VAL G . n 
G 3 85  LEU 85  83  83  LEU LEU G . n 
G 3 86  MET 86  84  84  MET MET G . n 
G 3 87  VAL 87  85  85  VAL VAL G . n 
G 3 88  GLU 88  86  86  GLU GLU G . n 
G 3 89  THR 89  87  87  THR THR G . n 
G 3 90  HIS 90  88  88  HIS HIS G . n 
G 3 91  ASN 91  89  89  ASN ASN G . n 
G 3 92  GLU 92  90  90  GLU GLU G . n 
G 3 93  ILE 93  91  91  ILE ILE G . n 
G 3 94  TYR 94  92  92  TYR TYR G . n 
G 3 95  ASP 95  93  93  ASP ASP G . n 
G 3 96  LYS 96  94  94  LYS LYS G . n 
G 3 97  PHE 97  95  95  PHE PHE G . n 
G 3 98  LYS 98  96  96  LYS LYS G . n 
G 3 99  GLN 99  97  97  GLN GLN G . n 
G 3 100 SER 100 98  98  SER SER G . n 
G 3 101 THR 101 99  99  THR THR G . n 
G 3 102 HIS 102 100 100 HIS HIS G . n 
G 3 103 SER 103 101 101 SER SER G . n 
G 3 104 ILE 104 102 102 ILE ILE G . n 
G 3 105 TYR 105 103 103 TYR TYR G . n 
G 3 106 MET 106 104 104 MET MET G . n 
G 3 107 PHE 107 105 105 PHE PHE G . n 
G 3 108 PHE 108 106 106 PHE PHE G . n 
G 3 109 GLN 109 107 107 GLN GLN G . n 
G 3 110 THR 110 108 108 THR THR G . n 
G 3 111 SER 111 109 109 SER SER G . n 
G 3 112 GLU 112 110 110 GLU GLU G . n 
G 3 113 LEU 113 111 111 LEU LEU G . n 
G 3 114 ARG 114 112 112 ARG ARG G . n 
G 3 115 GLU 115 113 113 GLU GLU G . n 
G 3 116 ALA 116 114 114 ALA ALA G . n 
G 3 117 VAL 117 115 115 VAL VAL G . n 
G 3 118 PRO 118 116 116 PRO PRO G . n 
G 3 119 GLU 119 117 117 GLU GLU G . n 
G 3 120 PRO 120 118 118 PRO PRO G . n 
G 3 121 VAL 121 119 119 VAL VAL G . n 
G 3 122 LEU 122 120 120 LEU LEU G . n 
G 3 123 LEU 123 121 121 LEU LEU G . n 
G 3 124 SER 124 122 122 SER SER G . n 
G 3 125 ARG 125 123 123 ARG ARG G . n 
G 3 126 ALA 126 124 124 ALA ALA G . n 
G 3 127 GLU 127 125 125 GLU GLU G . n 
G 3 128 LEU 128 126 126 LEU LEU G . n 
G 3 129 ARG 129 127 127 ARG ARG G . n 
G 3 130 LEU 130 128 128 LEU LEU G . n 
G 3 131 LEU 131 129 129 LEU LEU G . n 
G 3 132 ARG 132 130 130 ARG ARG G . n 
G 3 133 LEU 133 131 131 LEU LEU G . n 
G 3 134 LYS 134 132 132 LYS LYS G . n 
G 3 135 LEU 135 133 133 LEU LEU G . n 
G 3 136 LYS 136 134 134 LYS LYS G . n 
G 3 137 VAL 137 135 135 VAL VAL G . n 
G 3 138 GLU 138 136 136 GLU GLU G . n 
G 3 139 GLN 139 137 137 GLN GLN G . n 
G 3 140 HIS 140 138 138 HIS HIS G . n 
G 3 141 VAL 141 139 139 VAL VAL G . n 
G 3 142 GLU 142 140 140 GLU GLU G . n 
G 3 143 LEU 143 141 141 LEU LEU G . n 
G 3 144 TYR 144 142 142 TYR TYR G . n 
G 3 145 GLN 145 143 143 GLN GLN G . n 
G 3 146 LYS 146 144 144 LYS LYS G . n 
G 3 147 TYR 147 145 145 TYR TYR G . n 
G 3 148 SER 148 146 146 SER SER G . n 
G 3 149 GLN 149 147 147 GLN GLN G . n 
G 3 150 ASN 150 148 148 ASN ASN G . n 
G 3 151 SER 151 149 149 SER SER G . n 
G 3 152 TRP 152 150 150 TRP TRP G . n 
G 3 153 ARG 153 151 151 ARG ARG G . n 
G 3 154 TYR 154 152 152 TYR TYR G . n 
G 3 155 LEU 155 153 153 LEU LEU G . n 
G 3 156 SER 156 154 154 SER SER G . n 
G 3 157 ASN 157 155 155 ASN ASN G . n 
G 3 158 ARG 158 156 156 ARG ARG G . n 
G 3 159 LEU 159 157 157 LEU LEU G . n 
G 3 160 LEU 160 158 158 LEU LEU G . n 
G 3 161 ALA 161 159 159 ALA ALA G . n 
G 3 162 PRO 162 160 160 PRO PRO G . n 
G 3 163 SER 163 161 161 SER SER G . n 
G 3 164 ASP 164 162 162 ASP ASP G . n 
G 3 165 SER 165 163 163 SER SER G . n 
G 3 166 PRO 166 164 164 PRO PRO G . n 
G 3 167 GLU 167 165 165 GLU GLU G . n 
G 3 168 TRP 168 166 166 TRP TRP G . n 
G 3 169 LEU 169 167 167 LEU LEU G . n 
G 3 170 SER 170 168 168 SER SER G . n 
G 3 171 PHE 171 169 169 PHE PHE G . n 
G 3 172 ASP 172 170 170 ASP ASP G . n 
G 3 173 VAL 173 171 171 VAL VAL G . n 
G 3 174 THR 174 172 172 THR THR G . n 
G 3 175 GLY 175 173 173 GLY GLY G . n 
G 3 176 VAL 176 174 174 VAL VAL G . n 
G 3 177 VAL 177 175 175 VAL VAL G . n 
G 3 178 ARG 178 176 176 ARG ARG G . n 
G 3 179 GLN 179 177 177 GLN GLN G . n 
G 3 180 TRP 180 178 178 TRP TRP G . n 
G 3 181 LEU 181 179 179 LEU LEU G . n 
G 3 182 SER 182 180 180 SER SER G . n 
G 3 183 ARG 183 181 181 ARG ARG G . n 
G 3 184 GLY 184 182 182 GLY GLY G . n 
G 3 185 GLY 185 183 183 GLY GLY G . n 
G 3 186 GLU 186 184 184 GLU GLU G . n 
G 3 187 ILE 187 185 185 ILE ILE G . n 
G 3 188 GLU 188 186 186 GLU GLU G . n 
G 3 189 GLY 189 187 187 GLY GLY G . n 
G 3 190 PHE 190 188 188 PHE PHE G . n 
G 3 191 ARG 191 189 189 ARG ARG G . n 
G 3 192 LEU 192 190 190 LEU LEU G . n 
G 3 193 SER 193 191 191 SER SER G . n 
G 3 194 ALA 194 192 192 ALA ALA G . n 
G 3 195 HIS 195 193 193 HIS HIS G . n 
G 3 196 CYS 196 194 194 CYS CYS G . n 
G 3 197 SER 197 195 195 SER SER G . n 
G 3 198 CYS 198 196 196 CYS CYS G . n 
G 3 199 ASP 199 197 ?   ?   ?   G . n 
G 3 200 SER 200 198 ?   ?   ?   G . n 
G 3 201 ARG 201 199 ?   ?   ?   G . n 
G 3 202 ASP 202 200 ?   ?   ?   G . n 
G 3 203 ASN 203 201 ?   ?   ?   G . n 
G 3 204 THR 204 202 ?   ?   ?   G . n 
G 3 205 LEU 205 203 ?   ?   ?   G . n 
G 3 206 GLN 206 204 ?   ?   ?   G . n 
G 3 207 VAL 207 205 ?   ?   ?   G . n 
G 3 208 ASP 208 206 206 ASP ASP G . n 
G 3 209 ILE 209 207 207 ILE ILE G . n 
G 3 210 ASN 210 208 208 ASN ASN G . n 
G 3 211 GLY 211 209 209 GLY GLY G . n 
G 3 212 PHE 212 210 210 PHE PHE G . n 
G 3 213 THR 213 211 211 THR THR G . n 
G 3 214 THR 214 212 212 THR THR G . n 
G 3 215 GLY 215 213 213 GLY GLY G . n 
G 3 216 ARG 216 214 214 ARG ARG G . n 
G 3 217 ARG 217 215 215 ARG ARG G . n 
G 3 218 GLY 218 216 216 GLY GLY G . n 
G 3 219 ASP 219 217 217 ASP ASP G . n 
G 3 220 LEU 220 218 218 LEU LEU G . n 
G 3 221 ALA 221 219 219 ALA ALA G . n 
G 3 222 THR 222 220 220 THR THR G . n 
G 3 223 ILE 223 221 221 ILE ILE G . n 
G 3 224 HIS 224 222 222 HIS HIS G . n 
G 3 225 GLY 225 223 223 GLY GLY G . n 
G 3 226 MET 226 224 224 MET MET G . n 
G 3 227 ASN 227 225 225 ASN ASN G . n 
G 3 228 ARG 228 226 226 ARG ARG G . n 
G 3 229 PRO 229 227 227 PRO PRO G . n 
G 3 230 PHE 230 228 228 PHE PHE G . n 
G 3 231 LEU 231 229 229 LEU LEU G . n 
G 3 232 LEU 232 230 230 LEU LEU G . n 
G 3 233 LEU 233 231 231 LEU LEU G . n 
G 3 234 MET 234 232 232 MET MET G . n 
G 3 235 ALA 235 233 233 ALA ALA G . n 
G 3 236 THR 236 234 234 THR THR G . n 
G 3 237 PRO 237 235 235 PRO PRO G . n 
G 3 238 LEU 238 236 236 LEU LEU G . n 
G 3 239 GLU 239 237 237 GLU GLU G . n 
G 3 240 ARG 240 238 238 ARG ARG G . n 
G 3 241 ALA 241 239 239 ALA ALA G . n 
G 3 242 GLN 242 240 240 GLN GLN G . n 
G 3 243 HIS 243 241 ?   ?   ?   G . n 
G 3 244 LEU 244 242 ?   ?   ?   G . n 
G 3 245 GLN 245 243 ?   ?   ?   G . n 
G 3 246 SER 246 244 ?   ?   ?   G . n 
G 3 247 SER 247 245 ?   ?   ?   G . n 
G 3 248 ARG 248 246 ?   ?   ?   G . n 
G 3 249 HIS 249 247 ?   ?   ?   G . n 
G 3 250 ARG 250 248 ?   ?   ?   G . n 
G 3 251 ARG 251 249 ?   ?   ?   G . n 
G 3 252 ALA 252 250 250 ALA ALA G . n 
G 3 253 LEU 253 251 251 LEU LEU G . n 
G 3 254 ASP 254 252 252 ASP ASP G . n 
G 3 255 THR 255 253 253 THR THR G . n 
G 3 256 ASN 256 254 254 ASN ASN G . n 
G 3 257 TYR 257 255 255 TYR TYR G . n 
G 3 258 CYS 258 256 256 CYS CYS G . n 
G 3 259 PHE 259 257 257 PHE PHE G . n 
G 3 260 SER 260 258 258 SER SER G . n 
G 3 261 SER 261 259 259 SER SER G . n 
G 3 262 THR 262 260 260 THR THR G . n 
G 3 263 GLU 263 261 261 GLU GLU G . n 
G 3 264 LYS 264 262 262 LYS LYS G . n 
G 3 265 ASN 265 263 263 ASN ASN G . n 
G 3 266 CYS 266 264 264 CYS CYS G . n 
G 3 267 CYS 267 265 265 CYS CYS G . n 
G 3 268 VAL 268 266 266 VAL VAL G . n 
G 3 269 ARG 269 267 267 ARG ARG G . n 
G 3 270 GLN 270 268 268 GLN GLN G . n 
G 3 271 LEU 271 269 269 LEU LEU G . n 
G 3 272 TYR 272 270 270 TYR TYR G . n 
G 3 273 ILE 273 271 271 ILE ILE G . n 
G 3 274 ASP 274 272 272 ASP ASP G . n 
G 3 275 PHE 275 273 273 PHE PHE G . n 
G 3 276 ARG 276 274 274 ARG ARG G . n 
G 3 277 LYS 277 275 275 LYS LYS G . n 
G 3 278 ASP 278 276 276 ASP ASP G . n 
G 3 279 LEU 279 277 277 LEU LEU G . n 
G 3 280 GLY 280 278 278 GLY GLY G . n 
G 3 281 TRP 281 279 279 TRP TRP G . n 
G 3 282 LYS 282 280 280 LYS LYS G . n 
G 3 283 TRP 283 281 281 TRP TRP G . n 
G 3 284 ILE 284 282 282 ILE ILE G . n 
G 3 285 HIS 285 283 283 HIS HIS G . n 
G 3 286 GLU 286 284 284 GLU GLU G . n 
G 3 287 PRO 287 285 285 PRO PRO G . n 
G 3 288 LYS 288 286 286 LYS LYS G . n 
G 3 289 GLY 289 287 287 GLY GLY G . n 
G 3 290 TYR 290 288 288 TYR TYR G . n 
G 3 291 HIS 291 289 289 HIS HIS G . n 
G 3 292 ALA 292 290 290 ALA ALA G . n 
G 3 293 ASN 293 291 291 ASN ASN G . n 
G 3 294 PHE 294 292 292 PHE PHE G . n 
G 3 295 CYS 295 293 293 CYS CYS G . n 
G 3 296 LEU 296 294 294 LEU LEU G . n 
G 3 297 GLY 297 295 295 GLY GLY G . n 
G 3 298 PRO 298 296 296 PRO PRO G . n 
G 3 299 CYS 299 297 297 CYS CYS G . n 
G 3 300 PRO 300 298 298 PRO PRO G . n 
G 3 301 TYR 301 299 299 TYR TYR G . n 
G 3 302 ILE 302 300 ?   ?   ?   G . n 
G 3 303 TRP 303 301 ?   ?   ?   G . n 
G 3 304 SER 304 302 ?   ?   ?   G . n 
G 3 305 LEU 305 303 ?   ?   ?   G . n 
G 3 306 ASP 306 304 ?   ?   ?   G . n 
G 3 307 THR 307 305 ?   ?   ?   G . n 
G 3 308 GLN 308 306 ?   ?   ?   G . n 
G 3 309 TYR 309 307 ?   ?   ?   G . n 
G 3 310 SER 310 308 ?   ?   ?   G . n 
G 3 311 LYS 311 309 ?   ?   ?   G . n 
G 3 312 VAL 312 310 ?   ?   ?   G . n 
G 3 313 LEU 313 311 ?   ?   ?   G . n 
G 3 314 ALA 314 312 ?   ?   ?   G . n 
G 3 315 LEU 315 313 ?   ?   ?   G . n 
G 3 316 TYR 316 314 ?   ?   ?   G . n 
G 3 317 ASN 317 315 ?   ?   ?   G . n 
G 3 318 GLN 318 316 ?   ?   ?   G . n 
G 3 319 HIS 319 317 ?   ?   ?   G . n 
G 3 320 ASN 320 318 ?   ?   ?   G . n 
G 3 321 PRO 321 319 ?   ?   ?   G . n 
G 3 322 GLY 322 320 ?   ?   ?   G . n 
G 3 323 ALA 323 321 ?   ?   ?   G . n 
G 3 324 SER 324 322 ?   ?   ?   G . n 
G 3 325 ALA 325 323 ?   ?   ?   G . n 
G 3 326 ALA 326 324 324 ALA ALA G . n 
G 3 327 PRO 327 325 325 PRO PRO G . n 
G 3 328 CYS 328 326 326 CYS CYS G . n 
G 3 329 CYS 329 327 327 CYS CYS G . n 
G 3 330 VAL 330 328 328 VAL VAL G . n 
G 3 331 PRO 331 329 329 PRO PRO G . n 
G 3 332 GLN 332 330 330 GLN GLN G . n 
G 3 333 ALA 333 331 331 ALA ALA G . n 
G 3 334 LEU 334 332 332 LEU LEU G . n 
G 3 335 GLU 335 333 333 GLU GLU G . n 
G 3 336 PRO 336 334 334 PRO PRO G . n 
G 3 337 LEU 337 335 335 LEU LEU G . n 
G 3 338 PRO 338 336 336 PRO PRO G . n 
G 3 339 ILE 339 337 337 ILE ILE G . n 
G 3 340 VAL 340 338 338 VAL VAL G . n 
G 3 341 TYR 341 339 339 TYR TYR G . n 
G 3 342 TYR 342 340 340 TYR TYR G . n 
G 3 343 VAL 343 341 341 VAL VAL G . n 
G 3 344 GLY 344 342 342 GLY GLY G . n 
G 3 345 ARG 345 343 343 ARG ARG G . n 
G 3 346 LYS 346 344 344 LYS LYS G . n 
G 3 347 PRO 347 345 345 PRO PRO G . n 
G 3 348 LYS 348 346 346 LYS LYS G . n 
G 3 349 VAL 349 347 347 VAL VAL G . n 
G 3 350 GLU 350 348 348 GLU GLU G . n 
G 3 351 GLN 351 349 349 GLN GLN G . n 
G 3 352 LEU 352 350 350 LEU LEU G . n 
G 3 353 SER 353 351 351 SER SER G . n 
G 3 354 ASN 354 352 352 ASN ASN G . n 
G 3 355 MET 355 353 353 MET MET G . n 
G 3 356 ILE 356 354 354 ILE ILE G . n 
G 3 357 VAL 357 355 355 VAL VAL G . n 
G 3 358 ARG 358 356 356 ARG ARG G . n 
G 3 359 SER 359 357 357 SER SER G . n 
G 3 360 CYS 360 358 358 CYS CYS G . n 
G 3 361 LYS 361 359 359 LYS LYS G . n 
G 3 362 CYS 362 360 360 CYS CYS G . n 
G 3 363 SER 363 361 361 SER SER G . n 
H 3 1   GLY 1   -1  ?   ?   ?   H . n 
H 3 2   PRO 2   0   ?   ?   ?   H . n 
H 3 3   LEU 3   1   ?   ?   ?   H . n 
H 3 4   SER 4   2   ?   ?   ?   H . n 
H 3 5   THR 5   3   ?   ?   ?   H . n 
H 3 6   SER 6   4   ?   ?   ?   H . n 
H 3 7   LYS 7   5   5   LYS LYS H . n 
H 3 8   THR 8   6   6   THR THR H . n 
H 3 9   ILE 9   7   7   ILE ILE H . n 
H 3 10  ASP 10  8   8   ASP ASP H . n 
H 3 11  MET 11  9   9   MET MET H . n 
H 3 12  GLU 12  10  10  GLU GLU H . n 
H 3 13  LEU 13  11  11  LEU LEU H . n 
H 3 14  VAL 14  12  12  VAL VAL H . n 
H 3 15  LYS 15  13  13  LYS LYS H . n 
H 3 16  ARG 16  14  14  ARG ARG H . n 
H 3 17  LYS 17  15  15  LYS LYS H . n 
H 3 18  ARG 18  16  16  ARG ARG H . n 
H 3 19  ILE 19  17  17  ILE ILE H . n 
H 3 20  GLU 20  18  18  GLU GLU H . n 
H 3 21  ALA 21  19  19  ALA ALA H . n 
H 3 22  ILE 22  20  20  ILE ILE H . n 
H 3 23  ARG 23  21  21  ARG ARG H . n 
H 3 24  GLY 24  22  22  GLY GLY H . n 
H 3 25  GLN 25  23  23  GLN GLN H . n 
H 3 26  ILE 26  24  24  ILE ILE H . n 
H 3 27  LEU 27  25  25  LEU LEU H . n 
H 3 28  SER 28  26  26  SER SER H . n 
H 3 29  LYS 29  27  27  LYS LYS H . n 
H 3 30  LEU 30  28  28  LEU LEU H . n 
H 3 31  ARG 31  29  29  ARG ARG H . n 
H 3 32  LEU 32  30  30  LEU LEU H . n 
H 3 33  ALA 33  31  31  ALA ALA H . n 
H 3 34  SER 34  32  32  SER SER H . n 
H 3 35  PRO 35  33  33  PRO PRO H . n 
H 3 36  PRO 36  34  34  PRO PRO H . n 
H 3 37  SER 37  35  35  SER SER H . n 
H 3 38  GLN 38  36  36  GLN GLN H . n 
H 3 39  GLY 39  37  37  GLY GLY H . n 
H 3 40  GLU 40  38  38  GLU GLU H . n 
H 3 41  VAL 41  39  39  VAL VAL H . n 
H 3 42  PRO 42  40  40  PRO PRO H . n 
H 3 43  PRO 43  41  41  PRO PRO H . n 
H 3 44  GLY 44  42  42  GLY GLY H . n 
H 3 45  PRO 45  43  43  PRO PRO H . n 
H 3 46  LEU 46  44  44  LEU LEU H . n 
H 3 47  PRO 47  45  45  PRO PRO H . n 
H 3 48  GLU 48  46  46  GLU GLU H . n 
H 3 49  ALA 49  47  47  ALA ALA H . n 
H 3 50  VAL 50  48  48  VAL VAL H . n 
H 3 51  LEU 51  49  49  LEU LEU H . n 
H 3 52  ALA 52  50  50  ALA ALA H . n 
H 3 53  LEU 53  51  51  LEU LEU H . n 
H 3 54  TYR 54  52  52  TYR TYR H . n 
H 3 55  ASN 55  53  53  ASN ASN H . n 
H 3 56  SER 56  54  54  SER SER H . n 
H 3 57  THR 57  55  55  THR THR H . n 
H 3 58  ARG 58  56  56  ARG ARG H . n 
H 3 59  ASP 59  57  57  ASP ASP H . n 
H 3 60  ARG 60  58  58  ARG ARG H . n 
H 3 61  VAL 61  59  59  VAL VAL H . n 
H 3 62  ALA 62  60  60  ALA ALA H . n 
H 3 63  GLY 63  61  61  GLY GLY H . n 
H 3 64  GLU 64  62  ?   ?   ?   H . n 
H 3 65  SER 65  63  ?   ?   ?   H . n 
H 3 66  ALA 66  64  ?   ?   ?   H . n 
H 3 67  GLU 67  65  ?   ?   ?   H . n 
H 3 68  PRO 68  66  ?   ?   ?   H . n 
H 3 69  GLU 69  67  ?   ?   ?   H . n 
H 3 70  PRO 70  68  ?   ?   ?   H . n 
H 3 71  GLU 71  69  ?   ?   ?   H . n 
H 3 72  PRO 72  70  70  PRO PRO H . n 
H 3 73  GLU 73  71  71  GLU GLU H . n 
H 3 74  ALA 74  72  72  ALA ALA H . n 
H 3 75  ASP 75  73  73  ASP ASP H . n 
H 3 76  TYR 76  74  74  TYR TYR H . n 
H 3 77  TYR 77  75  75  TYR TYR H . n 
H 3 78  ALA 78  76  76  ALA ALA H . n 
H 3 79  LYS 79  77  77  LYS LYS H . n 
H 3 80  GLU 80  78  78  GLU GLU H . n 
H 3 81  VAL 81  79  79  VAL VAL H . n 
H 3 82  THR 82  80  80  THR THR H . n 
H 3 83  ARG 83  81  81  ARG ARG H . n 
H 3 84  VAL 84  82  82  VAL VAL H . n 
H 3 85  LEU 85  83  83  LEU LEU H . n 
H 3 86  MET 86  84  84  MET MET H . n 
H 3 87  VAL 87  85  85  VAL VAL H . n 
H 3 88  GLU 88  86  86  GLU GLU H . n 
H 3 89  THR 89  87  87  THR THR H . n 
H 3 90  HIS 90  88  88  HIS HIS H . n 
H 3 91  ASN 91  89  89  ASN ASN H . n 
H 3 92  GLU 92  90  90  GLU GLU H . n 
H 3 93  ILE 93  91  91  ILE ILE H . n 
H 3 94  TYR 94  92  92  TYR TYR H . n 
H 3 95  ASP 95  93  93  ASP ASP H . n 
H 3 96  LYS 96  94  94  LYS LYS H . n 
H 3 97  PHE 97  95  95  PHE PHE H . n 
H 3 98  LYS 98  96  96  LYS LYS H . n 
H 3 99  GLN 99  97  97  GLN GLN H . n 
H 3 100 SER 100 98  98  SER SER H . n 
H 3 101 THR 101 99  99  THR THR H . n 
H 3 102 HIS 102 100 100 HIS HIS H . n 
H 3 103 SER 103 101 101 SER SER H . n 
H 3 104 ILE 104 102 102 ILE ILE H . n 
H 3 105 TYR 105 103 103 TYR TYR H . n 
H 3 106 MET 106 104 104 MET MET H . n 
H 3 107 PHE 107 105 105 PHE PHE H . n 
H 3 108 PHE 108 106 106 PHE PHE H . n 
H 3 109 GLN 109 107 107 GLN GLN H . n 
H 3 110 THR 110 108 108 THR THR H . n 
H 3 111 SER 111 109 109 SER SER H . n 
H 3 112 GLU 112 110 110 GLU GLU H . n 
H 3 113 LEU 113 111 111 LEU LEU H . n 
H 3 114 ARG 114 112 112 ARG ARG H . n 
H 3 115 GLU 115 113 113 GLU GLU H . n 
H 3 116 ALA 116 114 114 ALA ALA H . n 
H 3 117 VAL 117 115 115 VAL VAL H . n 
H 3 118 PRO 118 116 116 PRO PRO H . n 
H 3 119 GLU 119 117 117 GLU GLU H . n 
H 3 120 PRO 120 118 118 PRO PRO H . n 
H 3 121 VAL 121 119 119 VAL VAL H . n 
H 3 122 LEU 122 120 120 LEU LEU H . n 
H 3 123 LEU 123 121 121 LEU LEU H . n 
H 3 124 SER 124 122 122 SER SER H . n 
H 3 125 ARG 125 123 123 ARG ARG H . n 
H 3 126 ALA 126 124 124 ALA ALA H . n 
H 3 127 GLU 127 125 125 GLU GLU H . n 
H 3 128 LEU 128 126 126 LEU LEU H . n 
H 3 129 ARG 129 127 127 ARG ARG H . n 
H 3 130 LEU 130 128 128 LEU LEU H . n 
H 3 131 LEU 131 129 129 LEU LEU H . n 
H 3 132 ARG 132 130 130 ARG ARG H . n 
H 3 133 LEU 133 131 131 LEU LEU H . n 
H 3 134 LYS 134 132 132 LYS LYS H . n 
H 3 135 LEU 135 133 133 LEU LEU H . n 
H 3 136 LYS 136 134 134 LYS LYS H . n 
H 3 137 VAL 137 135 135 VAL VAL H . n 
H 3 138 GLU 138 136 136 GLU GLU H . n 
H 3 139 GLN 139 137 137 GLN GLN H . n 
H 3 140 HIS 140 138 138 HIS HIS H . n 
H 3 141 VAL 141 139 139 VAL VAL H . n 
H 3 142 GLU 142 140 140 GLU GLU H . n 
H 3 143 LEU 143 141 141 LEU LEU H . n 
H 3 144 TYR 144 142 142 TYR TYR H . n 
H 3 145 GLN 145 143 143 GLN GLN H . n 
H 3 146 LYS 146 144 144 LYS LYS H . n 
H 3 147 TYR 147 145 145 TYR TYR H . n 
H 3 148 SER 148 146 146 SER SER H . n 
H 3 149 GLN 149 147 147 GLN GLN H . n 
H 3 150 ASN 150 148 148 ASN ASN H . n 
H 3 151 SER 151 149 149 SER SER H . n 
H 3 152 TRP 152 150 150 TRP TRP H . n 
H 3 153 ARG 153 151 151 ARG ARG H . n 
H 3 154 TYR 154 152 152 TYR TYR H . n 
H 3 155 LEU 155 153 153 LEU LEU H . n 
H 3 156 SER 156 154 154 SER SER H . n 
H 3 157 ASN 157 155 155 ASN ASN H . n 
H 3 158 ARG 158 156 156 ARG ARG H . n 
H 3 159 LEU 159 157 157 LEU LEU H . n 
H 3 160 LEU 160 158 158 LEU LEU H . n 
H 3 161 ALA 161 159 159 ALA ALA H . n 
H 3 162 PRO 162 160 160 PRO PRO H . n 
H 3 163 SER 163 161 161 SER SER H . n 
H 3 164 ASP 164 162 162 ASP ASP H . n 
H 3 165 SER 165 163 163 SER SER H . n 
H 3 166 PRO 166 164 164 PRO PRO H . n 
H 3 167 GLU 167 165 165 GLU GLU H . n 
H 3 168 TRP 168 166 166 TRP TRP H . n 
H 3 169 LEU 169 167 167 LEU LEU H . n 
H 3 170 SER 170 168 168 SER SER H . n 
H 3 171 PHE 171 169 169 PHE PHE H . n 
H 3 172 ASP 172 170 170 ASP ASP H . n 
H 3 173 VAL 173 171 171 VAL VAL H . n 
H 3 174 THR 174 172 172 THR THR H . n 
H 3 175 GLY 175 173 173 GLY GLY H . n 
H 3 176 VAL 176 174 174 VAL VAL H . n 
H 3 177 VAL 177 175 175 VAL VAL H . n 
H 3 178 ARG 178 176 176 ARG ARG H . n 
H 3 179 GLN 179 177 177 GLN GLN H . n 
H 3 180 TRP 180 178 178 TRP TRP H . n 
H 3 181 LEU 181 179 179 LEU LEU H . n 
H 3 182 SER 182 180 180 SER SER H . n 
H 3 183 ARG 183 181 181 ARG ARG H . n 
H 3 184 GLY 184 182 182 GLY GLY H . n 
H 3 185 GLY 185 183 183 GLY GLY H . n 
H 3 186 GLU 186 184 184 GLU GLU H . n 
H 3 187 ILE 187 185 185 ILE ILE H . n 
H 3 188 GLU 188 186 186 GLU GLU H . n 
H 3 189 GLY 189 187 187 GLY GLY H . n 
H 3 190 PHE 190 188 188 PHE PHE H . n 
H 3 191 ARG 191 189 189 ARG ARG H . n 
H 3 192 LEU 192 190 190 LEU LEU H . n 
H 3 193 SER 193 191 191 SER SER H . n 
H 3 194 ALA 194 192 192 ALA ALA H . n 
H 3 195 HIS 195 193 193 HIS HIS H . n 
H 3 196 CYS 196 194 194 CYS CYS H . n 
H 3 197 SER 197 195 195 SER SER H . n 
H 3 198 CYS 198 196 196 CYS CYS H . n 
H 3 199 ASP 199 197 197 ASP ASP H . n 
H 3 200 SER 200 198 198 SER SER H . n 
H 3 201 ARG 201 199 199 ARG ARG H . n 
H 3 202 ASP 202 200 200 ASP ASP H . n 
H 3 203 ASN 203 201 201 ASN ASN H . n 
H 3 204 THR 204 202 202 THR THR H . n 
H 3 205 LEU 205 203 203 LEU LEU H . n 
H 3 206 GLN 206 204 204 GLN GLN H . n 
H 3 207 VAL 207 205 205 VAL VAL H . n 
H 3 208 ASP 208 206 206 ASP ASP H . n 
H 3 209 ILE 209 207 207 ILE ILE H . n 
H 3 210 ASN 210 208 208 ASN ASN H . n 
H 3 211 GLY 211 209 209 GLY GLY H . n 
H 3 212 PHE 212 210 210 PHE PHE H . n 
H 3 213 THR 213 211 211 THR THR H . n 
H 3 214 THR 214 212 212 THR THR H . n 
H 3 215 GLY 215 213 213 GLY GLY H . n 
H 3 216 ARG 216 214 214 ARG ARG H . n 
H 3 217 ARG 217 215 215 ARG ARG H . n 
H 3 218 GLY 218 216 216 GLY GLY H . n 
H 3 219 ASP 219 217 217 ASP ASP H . n 
H 3 220 LEU 220 218 218 LEU LEU H . n 
H 3 221 ALA 221 219 219 ALA ALA H . n 
H 3 222 THR 222 220 220 THR THR H . n 
H 3 223 ILE 223 221 221 ILE ILE H . n 
H 3 224 HIS 224 222 222 HIS HIS H . n 
H 3 225 GLY 225 223 223 GLY GLY H . n 
H 3 226 MET 226 224 224 MET MET H . n 
H 3 227 ASN 227 225 225 ASN ASN H . n 
H 3 228 ARG 228 226 226 ARG ARG H . n 
H 3 229 PRO 229 227 227 PRO PRO H . n 
H 3 230 PHE 230 228 228 PHE PHE H . n 
H 3 231 LEU 231 229 229 LEU LEU H . n 
H 3 232 LEU 232 230 230 LEU LEU H . n 
H 3 233 LEU 233 231 231 LEU LEU H . n 
H 3 234 MET 234 232 232 MET MET H . n 
H 3 235 ALA 235 233 233 ALA ALA H . n 
H 3 236 THR 236 234 234 THR THR H . n 
H 3 237 PRO 237 235 235 PRO PRO H . n 
H 3 238 LEU 238 236 236 LEU LEU H . n 
H 3 239 GLU 239 237 237 GLU GLU H . n 
H 3 240 ARG 240 238 238 ARG ARG H . n 
H 3 241 ALA 241 239 239 ALA ALA H . n 
H 3 242 GLN 242 240 240 GLN GLN H . n 
H 3 243 HIS 243 241 ?   ?   ?   H . n 
H 3 244 LEU 244 242 ?   ?   ?   H . n 
H 3 245 GLN 245 243 ?   ?   ?   H . n 
H 3 246 SER 246 244 ?   ?   ?   H . n 
H 3 247 SER 247 245 ?   ?   ?   H . n 
H 3 248 ARG 248 246 ?   ?   ?   H . n 
H 3 249 HIS 249 247 ?   ?   ?   H . n 
H 3 250 ARG 250 248 ?   ?   ?   H . n 
H 3 251 ARG 251 249 ?   ?   ?   H . n 
H 3 252 ALA 252 250 ?   ?   ?   H . n 
H 3 253 LEU 253 251 ?   ?   ?   H . n 
H 3 254 ASP 254 252 ?   ?   ?   H . n 
H 3 255 THR 255 253 ?   ?   ?   H . n 
H 3 256 ASN 256 254 ?   ?   ?   H . n 
H 3 257 TYR 257 255 ?   ?   ?   H . n 
H 3 258 CYS 258 256 ?   ?   ?   H . n 
H 3 259 PHE 259 257 ?   ?   ?   H . n 
H 3 260 SER 260 258 ?   ?   ?   H . n 
H 3 261 SER 261 259 259 SER SER H . n 
H 3 262 THR 262 260 260 THR THR H . n 
H 3 263 GLU 263 261 261 GLU GLU H . n 
H 3 264 LYS 264 262 262 LYS LYS H . n 
H 3 265 ASN 265 263 263 ASN ASN H . n 
H 3 266 CYS 266 264 264 CYS CYS H . n 
H 3 267 CYS 267 265 265 CYS CYS H . n 
H 3 268 VAL 268 266 266 VAL VAL H . n 
H 3 269 ARG 269 267 267 ARG ARG H . n 
H 3 270 GLN 270 268 268 GLN GLN H . n 
H 3 271 LEU 271 269 269 LEU LEU H . n 
H 3 272 TYR 272 270 270 TYR TYR H . n 
H 3 273 ILE 273 271 271 ILE ILE H . n 
H 3 274 ASP 274 272 272 ASP ASP H . n 
H 3 275 PHE 275 273 273 PHE PHE H . n 
H 3 276 ARG 276 274 274 ARG ARG H . n 
H 3 277 LYS 277 275 275 LYS LYS H . n 
H 3 278 ASP 278 276 276 ASP ASP H . n 
H 3 279 LEU 279 277 277 LEU LEU H . n 
H 3 280 GLY 280 278 278 GLY GLY H . n 
H 3 281 TRP 281 279 279 TRP TRP H . n 
H 3 282 LYS 282 280 280 LYS LYS H . n 
H 3 283 TRP 283 281 281 TRP TRP H . n 
H 3 284 ILE 284 282 282 ILE ILE H . n 
H 3 285 HIS 285 283 283 HIS HIS H . n 
H 3 286 GLU 286 284 284 GLU GLU H . n 
H 3 287 PRO 287 285 285 PRO PRO H . n 
H 3 288 LYS 288 286 286 LYS LYS H . n 
H 3 289 GLY 289 287 287 GLY GLY H . n 
H 3 290 TYR 290 288 288 TYR TYR H . n 
H 3 291 HIS 291 289 289 HIS HIS H . n 
H 3 292 ALA 292 290 290 ALA ALA H . n 
H 3 293 ASN 293 291 291 ASN ASN H . n 
H 3 294 PHE 294 292 292 PHE PHE H . n 
H 3 295 CYS 295 293 293 CYS CYS H . n 
H 3 296 LEU 296 294 294 LEU LEU H . n 
H 3 297 GLY 297 295 295 GLY GLY H . n 
H 3 298 PRO 298 296 296 PRO PRO H . n 
H 3 299 CYS 299 297 297 CYS CYS H . n 
H 3 300 PRO 300 298 298 PRO PRO H . n 
H 3 301 TYR 301 299 299 TYR TYR H . n 
H 3 302 ILE 302 300 300 ILE ILE H . n 
H 3 303 TRP 303 301 301 TRP TRP H . n 
H 3 304 SER 304 302 302 SER SER H . n 
H 3 305 LEU 305 303 303 LEU LEU H . n 
H 3 306 ASP 306 304 304 ASP ALA H . n 
H 3 307 THR 307 305 ?   ?   ?   H . n 
H 3 308 GLN 308 306 ?   ?   ?   H . n 
H 3 309 TYR 309 307 ?   ?   ?   H . n 
H 3 310 SER 310 308 ?   ?   ?   H . n 
H 3 311 LYS 311 309 ?   ?   ?   H . n 
H 3 312 VAL 312 310 310 VAL VAL H . n 
H 3 313 LEU 313 311 311 LEU LEU H . n 
H 3 314 ALA 314 312 312 ALA ALA H . n 
H 3 315 LEU 315 313 313 LEU LEU H . n 
H 3 316 TYR 316 314 314 TYR TYR H . n 
H 3 317 ASN 317 315 315 ASN ASN H . n 
H 3 318 GLN 318 316 316 GLN GLN H . n 
H 3 319 HIS 319 317 317 HIS HIS H . n 
H 3 320 ASN 320 318 318 ASN ASN H . n 
H 3 321 PRO 321 319 319 PRO PRO H . n 
H 3 322 GLY 322 320 320 GLY GLY H . n 
H 3 323 ALA 323 321 321 ALA ALA H . n 
H 3 324 SER 324 322 322 SER SER H . n 
H 3 325 ALA 325 323 323 ALA ALA H . n 
H 3 326 ALA 326 324 324 ALA ALA H . n 
H 3 327 PRO 327 325 325 PRO PRO H . n 
H 3 328 CYS 328 326 326 CYS CYS H . n 
H 3 329 CYS 329 327 327 CYS CYS H . n 
H 3 330 VAL 330 328 328 VAL VAL H . n 
H 3 331 PRO 331 329 329 PRO PRO H . n 
H 3 332 GLN 332 330 330 GLN GLN H . n 
H 3 333 ALA 333 331 331 ALA ALA H . n 
H 3 334 LEU 334 332 332 LEU LEU H . n 
H 3 335 GLU 335 333 333 GLU GLU H . n 
H 3 336 PRO 336 334 334 PRO PRO H . n 
H 3 337 LEU 337 335 335 LEU LEU H . n 
H 3 338 PRO 338 336 336 PRO PRO H . n 
H 3 339 ILE 339 337 337 ILE ILE H . n 
H 3 340 VAL 340 338 338 VAL VAL H . n 
H 3 341 TYR 341 339 339 TYR TYR H . n 
H 3 342 TYR 342 340 340 TYR TYR H . n 
H 3 343 VAL 343 341 341 VAL VAL H . n 
H 3 344 GLY 344 342 ?   ?   ?   H . n 
H 3 345 ARG 345 343 343 ARG ARG H . n 
H 3 346 LYS 346 344 344 LYS LYS H . n 
H 3 347 PRO 347 345 345 PRO PRO H . n 
H 3 348 LYS 348 346 346 LYS LYS H . n 
H 3 349 VAL 349 347 347 VAL VAL H . n 
H 3 350 GLU 350 348 348 GLU GLU H . n 
H 3 351 GLN 351 349 349 GLN GLN H . n 
H 3 352 LEU 352 350 350 LEU LEU H . n 
H 3 353 SER 353 351 351 SER SER H . n 
H 3 354 ASN 354 352 352 ASN ASN H . n 
H 3 355 MET 355 353 353 MET MET H . n 
H 3 356 ILE 356 354 354 ILE ILE H . n 
H 3 357 VAL 357 355 355 VAL VAL H . n 
H 3 358 ARG 358 356 356 ARG ARG H . n 
H 3 359 SER 359 357 357 SER SER H . n 
H 3 360 CYS 360 358 358 CYS CYS H . n 
H 3 361 LYS 361 359 359 LYS LYS H . n 
H 3 362 CYS 362 360 360 CYS CYS H . n 
H 3 363 SER 363 361 361 SER SER H . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
I  4 CA  1 2001 2001 CA  CA  A . 
J  4 CA  1 2002 2002 CA  CA  A . 
K  4 CA  1 2003 2003 CA  CA  A . 
L  4 CA  1 2004 2004 CA  CA  A . 
M  5 NAG 1 2005 3044 NAG NAG A . 
N  5 NAG 2 2006 3045 NAG NAG A . 
O  6 BMA 3 2007 3046 BMA BMA A . 
P  5 NAG 1 2008 3260 NAG NAG A . 
Q  5 NAG 2 2009 3261 NAG NAG A . 
R  6 BMA 3 2010 3262 BMA BMA A . 
S  7 MAN 4 2011 3263 MAN MAN A . 
T  7 MAN 5 2012 3264 MAN MAN A . 
U  7 MAN 6 2013 3265 MAN MAN A . 
V  5 NAG 1 2014 3266 NAG NAG A . 
W  5 NAG 2 2015 3267 NAG NAG A . 
X  6 BMA 3 2016 3268 BMA BMA A . 
Y  7 MAN 4 2017 3269 MAN MAN A . 
Z  7 MAN 5 2018 3270 MAN MAN A . 
AA 7 MAN 6 2019 3271 MAN MAN A . 
BA 7 MAN 7 2020 3272 MAN MAN A . 
CA 5 NAG 1 2021 3458 NAG NAG A . 
DA 5 NAG 2 2022 3459 NAG NAG A . 
EA 6 BMA 3 2023 3460 BMA BMA A . 
FA 7 MAN 4 2024 3461 MAN MAN A . 
GA 5 NAG 1 2025 3525 NAG NAG A . 
HA 5 NAG 1 2026 3585 NAG NAG A . 
IA 5 NAG 2 2027 3586 NAG NAG A . 
JA 8 MN  1 2001 2001 MN  MN  B . 
KA 8 MN  1 2002 2002 MN  MN  B . 
LA 8 MN  1 2003 2003 MN  MN  B . 
MA 5 NAG 1 2004 3243 NAG NAG B . 
NA 5 NAG 1 401  3053 NAG NAG C . 
OA 5 NAG 2 402  3054 NAG NAG C . 
PA 6 BMA 3 403  3055 BMA BMA C . 
QA 7 MAN 4 404  3056 MAN MAN C . 
RA 5 NAG 1 401  3053 NAG NAG D . 
SA 5 NAG 2 402  3054 NAG NAG D . 
TA 6 BMA 3 403  3055 BMA BMA D . 
UA 7 MAN 4 404  3056 MAN MAN D . 
VA 4 CA  1 2001 2001 CA  CA  E . 
WA 4 CA  1 2002 2002 CA  CA  E . 
XA 4 CA  1 2003 2003 CA  CA  E . 
YA 4 CA  1 2004 2004 CA  CA  E . 
ZA 5 NAG 1 2005 3044 NAG NAG E . 
AB 5 NAG 2 2006 3045 NAG NAG E . 
BB 6 BMA 3 2007 3046 BMA BMA E . 
CB 5 NAG 1 2008 3260 NAG NAG E . 
DB 5 NAG 2 2009 3261 NAG NAG E . 
EB 6 BMA 3 2010 3262 BMA BMA E . 
FB 7 MAN 4 2011 3263 MAN MAN E . 
GB 7 MAN 5 2012 3264 MAN MAN E . 
HB 7 MAN 6 2013 3265 MAN MAN E . 
IB 5 NAG 1 2014 3266 NAG NAG E . 
JB 5 NAG 2 2015 3267 NAG NAG E . 
KB 6 BMA 3 2016 3268 BMA BMA E . 
LB 7 MAN 4 2017 3269 MAN MAN E . 
MB 7 MAN 5 2018 3270 MAN MAN E . 
NB 7 MAN 6 2019 3271 MAN MAN E . 
OB 7 MAN 7 2020 3272 MAN MAN E . 
PB 5 NAG 1 2021 3458 NAG NAG E . 
QB 5 NAG 2 2022 3459 NAG NAG E . 
RB 6 BMA 3 2023 3460 BMA BMA E . 
SB 7 MAN 4 2024 3461 MAN MAN E . 
TB 5 NAG 1 2025 3525 NAG NAG E . 
UB 5 NAG 1 2026 3585 NAG NAG E . 
VB 5 NAG 2 2027 3586 NAG NAG E . 
WB 8 MN  1 2001 2001 MN  MN  F . 
XB 8 MN  1 2002 2002 MN  MN  F . 
YB 8 MN  1 2003 2003 MN  MN  F . 
ZB 5 NAG 1 2004 3243 NAG NAG F . 
AC 5 NAG 1 401  3053 NAG NAG G . 
BC 5 NAG 2 402  3054 NAG NAG G . 
CC 6 BMA 3 403  3055 BMA BMA G . 
DC 7 MAN 4 404  3056 MAN MAN G . 
EC 5 NAG 1 401  3053 NAG NAG H . 
FC 5 NAG 2 402  3054 NAG NAG H . 
GC 6 BMA 3 403  3055 BMA BMA H . 
HC 7 MAN 4 404  3056 MAN MAN H . 
IC 7 MAN 5 405  3057 MAN MAN H . 
JC 7 MAN 6 406  3058 MAN MAN H . 
KC 9 HOH 1 2101 4    HOH HOH B . 
KC 9 HOH 2 2102 2    HOH HOH B . 
KC 9 HOH 3 2103 1    HOH HOH B . 
LC 9 HOH 1 2101 3    HOH HOH F . 
LC 9 HOH 2 2102 5    HOH HOH F . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   octameric 
_pdbx_struct_assembly.oligomeric_count     8 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      
;A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA,XA,YA,ZA,AB,BB,CB,DB,EB,FB,GB,HB,IB,JB,KB,LB,MB,NB,OB,PB,QB,RB,SB,TB,UB,VB,WB,XB,YB,ZB,AC,BC,CC,DC,EC,FC,GC,HC,IC,JC,KC,LC
;
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 34200  ? 
1 MORE         75     ? 
1 'SSA (A^2)'  138500 ? 
# 
_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]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   OD1 ? A  ASP 230 ? A ASP 230  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 OD1 ? A  ASN 232 ? A ASN 232  ? 1_555 75.0  ? 
2   OD1 ? A  ASP 230 ? A ASP 230  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 OD1 ? A  ASP 234 ? A ASP 234  ? 1_555 70.0  ? 
3   OD1 ? A  ASN 232 ? A ASN 232  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 OD1 ? A  ASP 234 ? A ASP 234  ? 1_555 84.1  ? 
4   OD1 ? A  ASP 230 ? A ASP 230  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 O   ? A  ILE 236 ? A ILE 236  ? 1_555 87.0  ? 
5   OD1 ? A  ASN 232 ? A ASN 232  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 O   ? A  ILE 236 ? A ILE 236  ? 1_555 159.7 ? 
6   OD1 ? A  ASP 234 ? A ASP 234  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 O   ? A  ILE 236 ? A ILE 236  ? 1_555 98.7  ? 
7   OD1 ? A  ASP 230 ? A ASP 230  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 OD1 ? A  ASP 238 ? A ASP 238  ? 1_555 134.7 ? 
8   OD1 ? A  ASN 232 ? A ASN 232  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 OD1 ? A  ASP 238 ? A ASP 238  ? 1_555 99.0  ? 
9   OD1 ? A  ASP 234 ? A ASP 234  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 OD1 ? A  ASP 238 ? A ASP 238  ? 1_555 155.2 ? 
10  O   ? A  ILE 236 ? A ILE 236  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 OD1 ? A  ASP 238 ? A ASP 238  ? 1_555 86.8  ? 
11  OD1 ? A  ASP 230 ? A ASP 230  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 OD2 ? A  ASP 238 ? A ASP 238  ? 1_555 84.1  ? 
12  OD1 ? A  ASN 232 ? A ASN 232  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 OD2 ? A  ASP 238 ? A ASP 238  ? 1_555 64.3  ? 
13  OD1 ? A  ASP 234 ? A ASP 234  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 OD2 ? A  ASP 238 ? A ASP 238  ? 1_555 143.7 ? 
14  O   ? A  ILE 236 ? A ILE 236  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 OD2 ? A  ASP 238 ? A ASP 238  ? 1_555 105.1 ? 
15  OD1 ? A  ASP 238 ? A ASP 238  ? 1_555 CA ? L  CA . ? A CA 2004 ? 1_555 OD2 ? A  ASP 238 ? A ASP 238  ? 1_555 54.7  ? 
16  OD1 ? A  ASP 284 ? A ASP 284  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 OD1 ? A  ASN 286 ? A ASN 286  ? 1_555 79.3  ? 
17  OD1 ? A  ASP 284 ? A ASP 284  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 OD1 ? A  ASP 288 ? A ASP 288  ? 1_555 60.6  ? 
18  OD1 ? A  ASN 286 ? A ASN 286  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 OD1 ? A  ASP 288 ? A ASP 288  ? 1_555 61.9  ? 
19  OD1 ? A  ASP 284 ? A ASP 284  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 O   ? A  TYR 290 ? A TYR 290  ? 1_555 84.1  ? 
20  OD1 ? A  ASN 286 ? A ASN 286  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 O   ? A  TYR 290 ? A TYR 290  ? 1_555 163.4 ? 
21  OD1 ? A  ASP 288 ? A ASP 288  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 O   ? A  TYR 290 ? A TYR 290  ? 1_555 109.8 ? 
22  OD1 ? A  ASP 284 ? A ASP 284  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 OD1 ? A  ASP 292 ? A ASP 292  ? 1_555 142.8 ? 
23  OD1 ? A  ASN 286 ? A ASN 286  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 OD1 ? A  ASP 292 ? A ASP 292  ? 1_555 113.8 ? 
24  OD1 ? A  ASP 288 ? A ASP 288  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 OD1 ? A  ASP 292 ? A ASP 292  ? 1_555 156.6 ? 
25  O   ? A  TYR 290 ? A TYR 290  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 OD1 ? A  ASP 292 ? A ASP 292  ? 1_555 79.6  ? 
26  OD1 ? A  ASP 284 ? A ASP 284  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 OD2 ? A  ASP 292 ? A ASP 292  ? 1_555 97.2  ? 
27  OD1 ? A  ASN 286 ? A ASN 286  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 OD2 ? A  ASP 292 ? A ASP 292  ? 1_555 77.8  ? 
28  OD1 ? A  ASP 288 ? A ASP 288  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 OD2 ? A  ASP 292 ? A ASP 292  ? 1_555 136.2 ? 
29  O   ? A  TYR 290 ? A TYR 290  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 OD2 ? A  ASP 292 ? A ASP 292  ? 1_555 104.1 ? 
30  OD1 ? A  ASP 292 ? A ASP 292  ? 1_555 CA ? I  CA . ? A CA 2001 ? 1_555 OD2 ? A  ASP 292 ? A ASP 292  ? 1_555 55.7  ? 
31  OD1 ? A  ASP 349 ? A ASP 349  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP 351 ? A ASP 351  ? 1_555 87.5  ? 
32  OD1 ? A  ASP 349 ? A ASP 349  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP 353 ? A ASP 353  ? 1_555 71.1  ? 
33  OD1 ? A  ASP 351 ? A ASP 351  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP 353 ? A ASP 353  ? 1_555 118.2 ? 
34  OD1 ? A  ASP 349 ? A ASP 349  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP 353 ? A ASP 353  ? 1_555 114.1 ? 
35  OD1 ? A  ASP 351 ? A ASP 351  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP 353 ? A ASP 353  ? 1_555 88.3  ? 
36  OD1 ? A  ASP 353 ? A ASP 353  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP 353 ? A ASP 353  ? 1_555 54.2  ? 
37  OD1 ? A  ASP 349 ? A ASP 349  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 O   ? A  PHE 355 ? A PHE 355  ? 1_555 68.1  ? 
38  OD1 ? A  ASP 351 ? A ASP 351  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 O   ? A  PHE 355 ? A PHE 355  ? 1_555 148.7 ? 
39  OD1 ? A  ASP 353 ? A ASP 353  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 O   ? A  PHE 355 ? A PHE 355  ? 1_555 73.4  ? 
40  OD2 ? A  ASP 353 ? A ASP 353  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 O   ? A  PHE 355 ? A PHE 355  ? 1_555 119.0 ? 
41  OD1 ? A  ASP 349 ? A ASP 349  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP 357 ? A ASP 357  ? 1_555 125.6 ? 
42  OD1 ? A  ASP 351 ? A ASP 351  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP 357 ? A ASP 357  ? 1_555 99.7  ? 
43  OD1 ? A  ASP 353 ? A ASP 353  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP 357 ? A ASP 357  ? 1_555 140.2 ? 
44  OD2 ? A  ASP 353 ? A ASP 353  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP 357 ? A ASP 357  ? 1_555 120.0 ? 
45  O   ? A  PHE 355 ? A PHE 355  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP 357 ? A ASP 357  ? 1_555 80.6  ? 
46  OD1 ? A  ASP 349 ? A ASP 349  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP 357 ? A ASP 357  ? 1_555 88.4  ? 
47  OD1 ? A  ASP 351 ? A ASP 351  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP 357 ? A ASP 357  ? 1_555 58.1  ? 
48  OD1 ? A  ASP 353 ? A ASP 353  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP 357 ? A ASP 357  ? 1_555 159.5 ? 
49  OD2 ? A  ASP 353 ? A ASP 353  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP 357 ? A ASP 357  ? 1_555 139.5 ? 
50  O   ? A  PHE 355 ? A PHE 355  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP 357 ? A ASP 357  ? 1_555 100.3 ? 
51  OD1 ? A  ASP 357 ? A ASP 357  ? 1_555 CA ? J  CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP 357 ? A ASP 357  ? 1_555 54.0  ? 
52  OD1 ? A  ASP 414 ? A ASP 414  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 OD1 ? A  ASP 416 ? A ASP 416  ? 1_555 65.2  ? 
53  OD1 ? A  ASP 414 ? A ASP 414  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 OD1 ? A  ASN 418 ? A ASN 418  ? 1_555 52.6  ? 
54  OD1 ? A  ASP 416 ? A ASP 416  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 OD1 ? A  ASN 418 ? A ASN 418  ? 1_555 77.9  ? 
55  OD1 ? A  ASP 414 ? A ASP 414  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 O   ? A  TYR 420 ? A TYR 420  ? 1_555 54.0  ? 
56  OD1 ? A  ASP 416 ? A ASP 416  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 O   ? A  TYR 420 ? A TYR 420  ? 1_555 119.0 ? 
57  OD1 ? A  ASN 418 ? A ASN 418  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 O   ? A  TYR 420 ? A TYR 420  ? 1_555 69.0  ? 
58  OD1 ? A  ASP 414 ? A ASP 414  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 OD1 ? A  ASP 422 ? A ASP 422  ? 1_555 70.0  ? 
59  OD1 ? A  ASP 416 ? A ASP 416  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 OD1 ? A  ASP 422 ? A ASP 422  ? 1_555 80.8  ? 
60  OD1 ? A  ASN 418 ? A ASN 418  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 OD1 ? A  ASP 422 ? A ASP 422  ? 1_555 122.6 ? 
61  O   ? A  TYR 420 ? A TYR 420  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 OD1 ? A  ASP 422 ? A ASP 422  ? 1_555 76.5  ? 
62  OD1 ? A  ASP 414 ? A ASP 414  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 OD2 ? A  ASP 422 ? A ASP 422  ? 1_555 124.3 ? 
63  OD1 ? A  ASP 416 ? A ASP 416  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 OD2 ? A  ASP 422 ? A ASP 422  ? 1_555 96.4  ? 
64  OD1 ? A  ASN 418 ? A ASN 418  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 OD2 ? A  ASP 422 ? A ASP 422  ? 1_555 174.3 ? 
65  O   ? A  TYR 420 ? A TYR 420  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 OD2 ? A  ASP 422 ? A ASP 422  ? 1_555 113.6 ? 
66  OD1 ? A  ASP 422 ? A ASP 422  ? 1_555 CA ? K  CA . ? A CA 2003 ? 1_555 OD2 ? A  ASP 422 ? A ASP 422  ? 1_555 54.8  ? 
67  OG  ? B  SER 15  ? B SER 125  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 OG  ? B  SER 17  ? B SER 127  ? 1_555 105.5 ? 
68  OG  ? B  SER 15  ? B SER 125  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 OE2 ? B  GLU 113 ? B GLU 223  ? 1_555 90.4  ? 
69  OG  ? B  SER 17  ? B SER 127  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 OE2 ? B  GLU 113 ? B GLU 223  ? 1_555 163.1 ? 
70  OG  ? B  SER 15  ? B SER 125  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 OD1 ? D  ASP 219 ? D ASP 217  ? 1_555 118.8 ? 
71  OG  ? B  SER 17  ? B SER 127  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 OD1 ? D  ASP 219 ? D ASP 217  ? 1_555 81.1  ? 
72  OE2 ? B  GLU 113 ? B GLU 223  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 OD1 ? D  ASP 219 ? D ASP 217  ? 1_555 96.3  ? 
73  OG  ? B  SER 15  ? B SER 125  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 O   ? KC HOH .   ? B HOH 2102 ? 1_555 77.8  ? 
74  OG  ? B  SER 17  ? B SER 127  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 O   ? KC HOH .   ? B HOH 2102 ? 1_555 65.5  ? 
75  OE2 ? B  GLU 113 ? B GLU 223  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 O   ? KC HOH .   ? B HOH 2102 ? 1_555 113.9 ? 
76  OD1 ? D  ASP 219 ? D ASP 217  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 O   ? KC HOH .   ? B HOH 2102 ? 1_555 146.1 ? 
77  OG  ? B  SER 15  ? B SER 125  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 O   ? KC HOH .   ? B HOH 2101 ? 1_555 159.4 ? 
78  OG  ? B  SER 17  ? B SER 127  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 O   ? KC HOH .   ? B HOH 2101 ? 1_555 84.3  ? 
79  OE2 ? B  GLU 113 ? B GLU 223  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 O   ? KC HOH .   ? B HOH 2101 ? 1_555 78.9  ? 
80  OD1 ? D  ASP 219 ? D ASP 217  ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 O   ? KC HOH .   ? B HOH 2101 ? 1_555 80.2  ? 
81  O   ? KC HOH .   ? B HOH 2102 ? 1_555 MN ? KA MN . ? B MN 2002 ? 1_555 O   ? KC HOH .   ? B HOH 2101 ? 1_555 90.5  ? 
82  O   ? B  SER 17  ? B SER 127  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD1 ? B  ASP 20  ? B ASP 130  ? 1_555 71.0  ? 
83  O   ? B  SER 17  ? B SER 127  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD2 ? B  ASP 20  ? B ASP 130  ? 1_555 123.8 ? 
84  OD1 ? B  ASP 20  ? B ASP 130  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD2 ? B  ASP 20  ? B ASP 130  ? 1_555 60.0  ? 
85  O   ? B  SER 17  ? B SER 127  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD1 ? B  ASP 21  ? B ASP 131  ? 1_555 129.2 ? 
86  OD1 ? B  ASP 20  ? B ASP 130  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD1 ? B  ASP 21  ? B ASP 131  ? 1_555 87.3  ? 
87  OD2 ? B  ASP 20  ? B ASP 130  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD1 ? B  ASP 21  ? B ASP 131  ? 1_555 76.0  ? 
88  O   ? B  SER 17  ? B SER 127  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD2 ? B  ASP 21  ? B ASP 131  ? 1_555 80.9  ? 
89  OD1 ? B  ASP 20  ? B ASP 130  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD2 ? B  ASP 21  ? B ASP 131  ? 1_555 101.7 ? 
90  OD2 ? B  ASP 20  ? B ASP 130  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD2 ? B  ASP 21  ? B ASP 131  ? 1_555 132.6 ? 
91  OD1 ? B  ASP 21  ? B ASP 131  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD2 ? B  ASP 21  ? B ASP 131  ? 1_555 58.7  ? 
92  O   ? B  SER 17  ? B SER 127  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD2 ? B  ASP 144 ? B ASP 254  ? 1_555 55.7  ? 
93  OD1 ? B  ASP 20  ? B ASP 130  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD2 ? B  ASP 144 ? B ASP 254  ? 1_555 126.6 ? 
94  OD2 ? B  ASP 20  ? B ASP 130  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD2 ? B  ASP 144 ? B ASP 254  ? 1_555 152.5 ? 
95  OD1 ? B  ASP 21  ? B ASP 131  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD2 ? B  ASP 144 ? B ASP 254  ? 1_555 127.8 ? 
96  OD2 ? B  ASP 21  ? B ASP 131  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 OD2 ? B  ASP 144 ? B ASP 254  ? 1_555 74.7  ? 
97  O   ? B  SER 17  ? B SER 127  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 O   ? KC HOH .   ? B HOH 2103 ? 1_555 120.6 ? 
98  OD1 ? B  ASP 20  ? B ASP 130  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 O   ? KC HOH .   ? B HOH 2103 ? 1_555 139.9 ? 
99  OD2 ? B  ASP 20  ? B ASP 130  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 O   ? KC HOH .   ? B HOH 2103 ? 1_555 86.1  ? 
100 OD1 ? B  ASP 21  ? B ASP 131  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 O   ? KC HOH .   ? B HOH 2103 ? 1_555 105.8 ? 
101 OD2 ? B  ASP 21  ? B ASP 131  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 O   ? KC HOH .   ? B HOH 2103 ? 1_555 117.6 ? 
102 OD2 ? B  ASP 144 ? B ASP 254  ? 1_555 MN ? JA MN . ? B MN 2001 ? 1_555 O   ? KC HOH .   ? B HOH 2103 ? 1_555 74.6  ? 
103 OE2 ? B  GLU 52  ? B GLU 162  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 OD1 ? B  ASN 108 ? B ASN 218  ? 1_555 119.9 ? 
104 OE2 ? B  GLU 52  ? B GLU 162  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 O   ? B  ASP 110 ? B ASP 220  ? 1_555 156.1 ? 
105 OD1 ? B  ASN 108 ? B ASN 218  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 O   ? B  ASP 110 ? B ASP 220  ? 1_555 81.5  ? 
106 OE2 ? B  GLU 52  ? B GLU 162  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 OD1 ? B  ASP 110 ? B ASP 220  ? 1_555 96.9  ? 
107 OD1 ? B  ASN 108 ? B ASN 218  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 OD1 ? B  ASP 110 ? B ASP 220  ? 1_555 94.2  ? 
108 O   ? B  ASP 110 ? B ASP 220  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 OD1 ? B  ASP 110 ? B ASP 220  ? 1_555 69.3  ? 
109 OE2 ? B  GLU 52  ? B GLU 162  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 O   ? B  PRO 112 ? B PRO 222  ? 1_555 78.8  ? 
110 OD1 ? B  ASN 108 ? B ASN 218  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 O   ? B  PRO 112 ? B PRO 222  ? 1_555 160.9 ? 
111 O   ? B  ASP 110 ? B ASP 220  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 O   ? B  PRO 112 ? B PRO 222  ? 1_555 80.9  ? 
112 OD1 ? B  ASP 110 ? B ASP 220  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 O   ? B  PRO 112 ? B PRO 222  ? 1_555 86.6  ? 
113 OE2 ? B  GLU 52  ? B GLU 162  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 OE1 ? B  GLU 113 ? B GLU 223  ? 1_555 81.5  ? 
114 OD1 ? B  ASN 108 ? B ASN 218  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 OE1 ? B  GLU 113 ? B GLU 223  ? 1_555 88.0  ? 
115 O   ? B  ASP 110 ? B ASP 220  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 OE1 ? B  GLU 113 ? B GLU 223  ? 1_555 111.7 ? 
116 OD1 ? B  ASP 110 ? B ASP 220  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 OE1 ? B  GLU 113 ? B GLU 223  ? 1_555 177.8 ? 
117 O   ? B  PRO 112 ? B PRO 222  ? 1_555 MN ? LA MN . ? B MN 2003 ? 1_555 OE1 ? B  GLU 113 ? B GLU 223  ? 1_555 91.7  ? 
118 OD1 ? E  ASN 232 ? E ASN 232  ? 1_555 CA ? YA CA . ? E CA 2004 ? 1_555 OD1 ? E  ASP 234 ? E ASP 234  ? 1_555 80.4  ? 
119 OD1 ? E  ASN 232 ? E ASN 232  ? 1_555 CA ? YA CA . ? E CA 2004 ? 1_555 O   ? E  ILE 236 ? E ILE 236  ? 1_555 134.7 ? 
120 OD1 ? E  ASP 234 ? E ASP 234  ? 1_555 CA ? YA CA . ? E CA 2004 ? 1_555 O   ? E  ILE 236 ? E ILE 236  ? 1_555 92.3  ? 
121 OD1 ? E  ASN 232 ? E ASN 232  ? 1_555 CA ? YA CA . ? E CA 2004 ? 1_555 OD1 ? E  ASP 238 ? E ASP 238  ? 1_555 105.8 ? 
122 OD1 ? E  ASP 234 ? E ASP 234  ? 1_555 CA ? YA CA . ? E CA 2004 ? 1_555 OD1 ? E  ASP 238 ? E ASP 238  ? 1_555 173.6 ? 
123 O   ? E  ILE 236 ? E ILE 236  ? 1_555 CA ? YA CA . ? E CA 2004 ? 1_555 OD1 ? E  ASP 238 ? E ASP 238  ? 1_555 84.4  ? 
124 OD1 ? E  ASN 232 ? E ASN 232  ? 1_555 CA ? YA CA . ? E CA 2004 ? 1_555 OD2 ? E  ASP 238 ? E ASP 238  ? 1_555 61.4  ? 
125 OD1 ? E  ASP 234 ? E ASP 234  ? 1_555 CA ? YA CA . ? E CA 2004 ? 1_555 OD2 ? E  ASP 238 ? E ASP 238  ? 1_555 131.3 ? 
126 O   ? E  ILE 236 ? E ILE 236  ? 1_555 CA ? YA CA . ? E CA 2004 ? 1_555 OD2 ? E  ASP 238 ? E ASP 238  ? 1_555 94.1  ? 
127 OD1 ? E  ASP 238 ? E ASP 238  ? 1_555 CA ? YA CA . ? E CA 2004 ? 1_555 OD2 ? E  ASP 238 ? E ASP 238  ? 1_555 54.7  ? 
128 OD1 ? E  ASP 284 ? E ASP 284  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD1 ? E  ASN 286 ? E ASN 286  ? 1_555 81.8  ? 
129 OD1 ? E  ASP 284 ? E ASP 284  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD1 ? E  ASP 288 ? E ASP 288  ? 1_555 58.8  ? 
130 OD1 ? E  ASN 286 ? E ASN 286  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD1 ? E  ASP 288 ? E ASP 288  ? 1_555 66.3  ? 
131 OD1 ? E  ASP 284 ? E ASP 284  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD2 ? E  ASP 288 ? E ASP 288  ? 1_555 100.6 ? 
132 OD1 ? E  ASN 286 ? E ASN 286  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD2 ? E  ASP 288 ? E ASP 288  ? 1_555 82.0  ? 
133 OD1 ? E  ASP 288 ? E ASP 288  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD2 ? E  ASP 288 ? E ASP 288  ? 1_555 43.6  ? 
134 OD1 ? E  ASP 284 ? E ASP 284  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 O   ? E  TYR 290 ? E TYR 290  ? 1_555 79.1  ? 
135 OD1 ? E  ASN 286 ? E ASN 286  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 O   ? E  TYR 290 ? E TYR 290  ? 1_555 160.9 ? 
136 OD1 ? E  ASP 288 ? E ASP 288  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 O   ? E  TYR 290 ? E TYR 290  ? 1_555 104.2 ? 
137 OD2 ? E  ASP 288 ? E ASP 288  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 O   ? E  TYR 290 ? E TYR 290  ? 1_555 102.7 ? 
138 OD1 ? E  ASP 284 ? E ASP 284  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD1 ? E  ASP 292 ? E ASP 292  ? 1_555 142.3 ? 
139 OD1 ? E  ASN 286 ? E ASN 286  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD1 ? E  ASP 292 ? E ASP 292  ? 1_555 113.7 ? 
140 OD1 ? E  ASP 288 ? E ASP 288  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD1 ? E  ASP 292 ? E ASP 292  ? 1_555 158.5 ? 
141 OD2 ? E  ASP 288 ? E ASP 288  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD1 ? E  ASP 292 ? E ASP 292  ? 1_555 115.1 ? 
142 O   ? E  TYR 290 ? E TYR 290  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD1 ? E  ASP 292 ? E ASP 292  ? 1_555 81.4  ? 
143 OD1 ? E  ASP 284 ? E ASP 284  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD2 ? E  ASP 292 ? E ASP 292  ? 1_555 99.2  ? 
144 OD1 ? E  ASN 286 ? E ASN 286  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD2 ? E  ASP 292 ? E ASP 292  ? 1_555 76.7  ? 
145 OD1 ? E  ASP 288 ? E ASP 288  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD2 ? E  ASP 292 ? E ASP 292  ? 1_555 138.6 ? 
146 OD2 ? E  ASP 288 ? E ASP 288  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD2 ? E  ASP 292 ? E ASP 292  ? 1_555 148.4 ? 
147 O   ? E  TYR 290 ? E TYR 290  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD2 ? E  ASP 292 ? E ASP 292  ? 1_555 105.0 ? 
148 OD1 ? E  ASP 292 ? E ASP 292  ? 1_555 CA ? VA CA . ? E CA 2001 ? 1_555 OD2 ? E  ASP 292 ? E ASP 292  ? 1_555 55.7  ? 
149 OD1 ? E  ASP 349 ? E ASP 349  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD1 ? E  ASP 351 ? E ASP 351  ? 1_555 90.3  ? 
150 OD1 ? E  ASP 349 ? E ASP 349  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD1 ? E  ASP 353 ? E ASP 353  ? 1_555 71.4  ? 
151 OD1 ? E  ASP 351 ? E ASP 351  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD1 ? E  ASP 353 ? E ASP 353  ? 1_555 119.4 ? 
152 OD1 ? E  ASP 349 ? E ASP 349  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD2 ? E  ASP 353 ? E ASP 353  ? 1_555 115.1 ? 
153 OD1 ? E  ASP 351 ? E ASP 351  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD2 ? E  ASP 353 ? E ASP 353  ? 1_555 89.3  ? 
154 OD1 ? E  ASP 353 ? E ASP 353  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD2 ? E  ASP 353 ? E ASP 353  ? 1_555 53.5  ? 
155 OD1 ? E  ASP 349 ? E ASP 349  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 O   ? E  PHE 355 ? E PHE 355  ? 1_555 68.0  ? 
156 OD1 ? E  ASP 351 ? E ASP 351  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 O   ? E  PHE 355 ? E PHE 355  ? 1_555 151.6 ? 
157 OD1 ? E  ASP 353 ? E ASP 353  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 O   ? E  PHE 355 ? E PHE 355  ? 1_555 72.1  ? 
158 OD2 ? E  ASP 353 ? E ASP 353  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 O   ? E  PHE 355 ? E PHE 355  ? 1_555 116.0 ? 
159 OD1 ? E  ASP 349 ? E ASP 349  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD1 ? E  ASP 357 ? E ASP 357  ? 1_555 126.8 ? 
160 OD1 ? E  ASP 351 ? E ASP 351  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD1 ? E  ASP 357 ? E ASP 357  ? 1_555 100.0 ? 
161 OD1 ? E  ASP 353 ? E ASP 353  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD1 ? E  ASP 357 ? E ASP 357  ? 1_555 137.5 ? 
162 OD2 ? E  ASP 353 ? E ASP 353  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD1 ? E  ASP 357 ? E ASP 357  ? 1_555 117.1 ? 
163 O   ? E  PHE 355 ? E PHE 355  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD1 ? E  ASP 357 ? E ASP 357  ? 1_555 80.5  ? 
164 OD1 ? E  ASP 349 ? E ASP 349  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD2 ? E  ASP 357 ? E ASP 357  ? 1_555 89.7  ? 
165 OD1 ? E  ASP 351 ? E ASP 351  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD2 ? E  ASP 357 ? E ASP 357  ? 1_555 59.2  ? 
166 OD1 ? E  ASP 353 ? E ASP 353  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD2 ? E  ASP 357 ? E ASP 357  ? 1_555 161.1 ? 
167 OD2 ? E  ASP 353 ? E ASP 353  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD2 ? E  ASP 357 ? E ASP 357  ? 1_555 140.8 ? 
168 O   ? E  PHE 355 ? E PHE 355  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD2 ? E  ASP 357 ? E ASP 357  ? 1_555 101.0 ? 
169 OD1 ? E  ASP 357 ? E ASP 357  ? 1_555 CA ? WA CA . ? E CA 2002 ? 1_555 OD2 ? E  ASP 357 ? E ASP 357  ? 1_555 54.8  ? 
170 OD1 ? E  ASP 414 ? E ASP 414  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 OD1 ? E  ASP 416 ? E ASP 416  ? 1_555 74.8  ? 
171 OD1 ? E  ASP 414 ? E ASP 414  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 OD1 ? E  ASN 418 ? E ASN 418  ? 1_555 75.5  ? 
172 OD1 ? E  ASP 416 ? E ASP 416  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 OD1 ? E  ASN 418 ? E ASN 418  ? 1_555 83.3  ? 
173 OD1 ? E  ASP 414 ? E ASP 414  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 O   ? E  TYR 420 ? E TYR 420  ? 1_555 65.1  ? 
174 OD1 ? E  ASP 416 ? E ASP 416  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 O   ? E  TYR 420 ? E TYR 420  ? 1_555 139.6 ? 
175 OD1 ? E  ASN 418 ? E ASN 418  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 O   ? E  TYR 420 ? E TYR 420  ? 1_555 82.0  ? 
176 OD1 ? E  ASP 414 ? E ASP 414  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 OD1 ? E  ASP 422 ? E ASP 422  ? 1_555 83.6  ? 
177 OD1 ? E  ASP 416 ? E ASP 416  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 OD1 ? E  ASP 422 ? E ASP 422  ? 1_555 95.9  ? 
178 OD1 ? E  ASN 418 ? E ASN 418  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 OD1 ? E  ASP 422 ? E ASP 422  ? 1_555 158.6 ? 
179 O   ? E  TYR 420 ? E TYR 420  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 OD1 ? E  ASP 422 ? E ASP 422  ? 1_555 84.9  ? 
180 OD1 ? E  ASP 414 ? E ASP 414  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 OD2 ? E  ASP 422 ? E ASP 422  ? 1_555 137.3 ? 
181 OD1 ? E  ASP 416 ? E ASP 416  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 OD2 ? E  ASP 422 ? E ASP 422  ? 1_555 98.9  ? 
182 OD1 ? E  ASN 418 ? E ASN 418  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 OD2 ? E  ASP 422 ? E ASP 422  ? 1_555 146.7 ? 
183 O   ? E  TYR 420 ? E TYR 420  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 OD2 ? E  ASP 422 ? E ASP 422  ? 1_555 113.7 ? 
184 OD1 ? E  ASP 422 ? E ASP 422  ? 1_555 CA ? XA CA . ? E CA 2003 ? 1_555 OD2 ? E  ASP 422 ? E ASP 422  ? 1_555 54.6  ? 
185 OG  ? F  SER 15  ? F SER 125  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 OG  ? F  SER 17  ? F SER 127  ? 1_555 98.6  ? 
186 OG  ? F  SER 15  ? F SER 125  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 OE2 ? F  GLU 113 ? F GLU 223  ? 1_555 101.9 ? 
187 OG  ? F  SER 17  ? F SER 127  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 OE2 ? F  GLU 113 ? F GLU 223  ? 1_555 159.2 ? 
188 OG  ? F  SER 15  ? F SER 125  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 OD1 ? H  ASP 219 ? H ASP 217  ? 1_555 115.6 ? 
189 OG  ? F  SER 17  ? F SER 127  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 OD1 ? H  ASP 219 ? H ASP 217  ? 1_555 75.2  ? 
190 OE2 ? F  GLU 113 ? F GLU 223  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 OD1 ? H  ASP 219 ? H ASP 217  ? 1_555 92.6  ? 
191 OG  ? F  SER 15  ? F SER 125  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 O   ? LC HOH .   ? F HOH 2101 ? 1_555 166.4 ? 
192 OG  ? F  SER 17  ? F SER 127  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 O   ? LC HOH .   ? F HOH 2101 ? 1_555 83.4  ? 
193 OE2 ? F  GLU 113 ? F GLU 223  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 O   ? LC HOH .   ? F HOH 2101 ? 1_555 77.5  ? 
194 OD1 ? H  ASP 219 ? H ASP 217  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 O   ? LC HOH .   ? F HOH 2101 ? 1_555 78.0  ? 
195 OG  ? F  SER 15  ? F SER 125  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 O   ? LC HOH .   ? F HOH 2102 ? 1_555 76.9  ? 
196 OG  ? F  SER 17  ? F SER 127  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 O   ? LC HOH .   ? F HOH 2102 ? 1_555 81.3  ? 
197 OE2 ? F  GLU 113 ? F GLU 223  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 O   ? LC HOH .   ? F HOH 2102 ? 1_555 106.7 ? 
198 OD1 ? H  ASP 219 ? H ASP 217  ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 O   ? LC HOH .   ? F HOH 2102 ? 1_555 154.7 ? 
199 O   ? LC HOH .   ? F HOH 2101 ? 1_555 MN ? XB MN . ? F MN 2002 ? 1_555 O   ? LC HOH .   ? F HOH 2102 ? 1_555 90.2  ? 
200 O   ? F  SER 17  ? F SER 127  ? 1_555 MN ? WB MN . ? F MN 2001 ? 1_555 OD1 ? F  ASP 20  ? F ASP 130  ? 1_555 76.7  ? 
201 O   ? F  SER 17  ? F SER 127  ? 1_555 MN ? WB MN . ? F MN 2001 ? 1_555 OD2 ? F  ASP 20  ? F ASP 130  ? 1_555 133.0 ? 
202 OD1 ? F  ASP 20  ? F ASP 130  ? 1_555 MN ? WB MN . ? F MN 2001 ? 1_555 OD2 ? F  ASP 20  ? F ASP 130  ? 1_555 60.6  ? 
203 O   ? F  SER 17  ? F SER 127  ? 1_555 MN ? WB MN . ? F MN 2001 ? 1_555 OD2 ? F  ASP 21  ? F ASP 131  ? 1_555 96.5  ? 
204 OD1 ? F  ASP 20  ? F ASP 130  ? 1_555 MN ? WB MN . ? F MN 2001 ? 1_555 OD2 ? F  ASP 21  ? F ASP 131  ? 1_555 91.9  ? 
205 OD2 ? F  ASP 20  ? F ASP 130  ? 1_555 MN ? WB MN . ? F MN 2001 ? 1_555 OD2 ? F  ASP 21  ? F ASP 131  ? 1_555 103.3 ? 
206 O   ? F  SER 17  ? F SER 127  ? 1_555 MN ? WB MN . ? F MN 2001 ? 1_555 OD2 ? F  ASP 144 ? F ASP 254  ? 1_555 55.4  ? 
207 OD1 ? F  ASP 20  ? F ASP 130  ? 1_555 MN ? WB MN . ? F MN 2001 ? 1_555 OD2 ? F  ASP 144 ? F ASP 254  ? 1_555 130.9 ? 
208 OD2 ? F  ASP 20  ? F ASP 130  ? 1_555 MN ? WB MN . ? F MN 2001 ? 1_555 OD2 ? F  ASP 144 ? F ASP 254  ? 1_555 167.0 ? 
209 OD2 ? F  ASP 21  ? F ASP 131  ? 1_555 MN ? WB MN . ? F MN 2001 ? 1_555 OD2 ? F  ASP 144 ? F ASP 254  ? 1_555 83.7  ? 
210 OE2 ? F  GLU 52  ? F GLU 162  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 OD1 ? F  ASN 108 ? F ASN 218  ? 1_555 133.4 ? 
211 OE2 ? F  GLU 52  ? F GLU 162  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 O   ? F  ASP 110 ? F ASP 220  ? 1_555 141.1 ? 
212 OD1 ? F  ASN 108 ? F ASN 218  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 O   ? F  ASP 110 ? F ASP 220  ? 1_555 82.2  ? 
213 OE2 ? F  GLU 52  ? F GLU 162  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 OD1 ? F  ASP 110 ? F ASP 220  ? 1_555 91.7  ? 
214 OD1 ? F  ASN 108 ? F ASN 218  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 OD1 ? F  ASP 110 ? F ASP 220  ? 1_555 92.2  ? 
215 O   ? F  ASP 110 ? F ASP 220  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 OD1 ? F  ASP 110 ? F ASP 220  ? 1_555 68.2  ? 
216 OE2 ? F  GLU 52  ? F GLU 162  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 O   ? F  PRO 112 ? F PRO 222  ? 1_555 73.8  ? 
217 OD1 ? F  ASN 108 ? F ASN 218  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 O   ? F  PRO 112 ? F PRO 222  ? 1_555 151.6 ? 
218 O   ? F  ASP 110 ? F ASP 220  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 O   ? F  PRO 112 ? F PRO 222  ? 1_555 75.2  ? 
219 OD1 ? F  ASP 110 ? F ASP 220  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 O   ? F  PRO 112 ? F PRO 222  ? 1_555 95.1  ? 
220 OE2 ? F  GLU 52  ? F GLU 162  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 OE1 ? F  GLU 113 ? F GLU 223  ? 1_555 93.5  ? 
221 OD1 ? F  ASN 108 ? F ASN 218  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 OE1 ? F  GLU 113 ? F GLU 223  ? 1_555 86.3  ? 
222 O   ? F  ASP 110 ? F ASP 220  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 OE1 ? F  GLU 113 ? F GLU 223  ? 1_555 105.9 ? 
223 OD1 ? F  ASP 110 ? F ASP 220  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 OE1 ? F  GLU 113 ? F GLU 223  ? 1_555 174.1 ? 
224 O   ? F  PRO 112 ? F PRO 222  ? 1_555 MN ? YB MN . ? F MN 2003 ? 1_555 OE1 ? F  GLU 113 ? F GLU 223  ? 1_555 83.6  ? 
# 
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 
1 'Structure model' 1 0 2017-01-25 
2 'Structure model' 1 1 2017-02-08 
3 'Structure model' 1 2 2017-02-15 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1  ? refined 5.8910   -12.7734 28.0881  0.8414 2.4760 2.6028 0.8803  -0.1377 0.2441  3.2078 3.4324 4.6346 
1.2307  0.6388  -1.1418 -0.0145 -0.3381 0.3291  -0.2248 0.5827  -0.8717 -0.4781 0.4523  1.8850  
'X-RAY DIFFRACTION' 2  ? refined 20.9843  -13.4214 78.5475  2.0681 3.0336 2.3462 -0.0538 -0.5893 -0.4682 0.6045 0.5340 6.0572 
-0.1443 1.9301  -0.1667 0.0497  -0.3804 0.4349  -0.0096 0.7353  -0.3132 0.8469  -0.1247 1.6132  
'X-RAY DIFFRACTION' 3  ? refined -25.9120 -1.1217  23.2451  0.8671 1.0341 2.3380 -0.1914 -0.5852 0.4161  2.5677 8.5937 8.1864 
-1.6587 -0.5297 1.5108  1.7993  -1.5029 -0.5062 0.2000  2.4533  4.3965  -2.4543 -0.5156 -0.9771 
'X-RAY DIFFRACTION' 4  ? refined -21.6655 -17.3987 -46.1630 2.2982 1.7862 1.4506 0.0296  -0.1130 -0.4293 5.9439 5.1988 3.5953 
-3.3955 0.4233  -3.0722 0.8211  -0.6225 -0.2489 0.8581  -0.7611 0.3315  -2.0155 1.1867  0.3923  
'X-RAY DIFFRACTION' 5  ? refined -44.7678 5.3811   -48.5697 2.4977 2.1728 1.9290 0.5953  -0.3390 -0.0940 1.7844 1.0707 9.6669 
0.8997  -2.8815 0.3054  0.1712  0.3919  -0.5081 0.8989  0.7853  0.2133  -1.1574 0.3524  -1.4933 
'X-RAY DIFFRACTION' 6  ? refined -29.3088 -14.6847 -11.8844 1.7338 1.5444 1.6575 0.3236  -0.5648 -0.2047 6.8323 3.2143 5.6067 
-0.5789 -2.8268 0.3148  -0.1846 -0.2044 0.3870  0.7337  -1.7487 0.0399  0.2339  0.2978  0.9398  
'X-RAY DIFFRACTION' 7  ? refined -40.8198 13.0102  -19.7696 1.9509 2.2985 1.5946 1.1581  -0.4721 -0.3948 3.5455 7.7608 8.2637 
2.8342  -5.0254 -3.4333 0.7824  -0.1117 -0.4942 -0.2465 0.8045  0.3787  -0.4917 0.0178  0.8212  
'X-RAY DIFFRACTION' 8  ? refined -6.3688  -58.3939 -26.8710 1.8395 1.5728 1.7493 0.7612  -0.1440 -0.2472 4.1412 0.5575 7.1412 
1.0825  -0.7298 0.6041  -0.0054 -0.4897 0.3837  0.4292  0.7251  0.8695  -0.1320 -0.9027 -1.8092 
'X-RAY DIFFRACTION' 9  ? refined -21.4691 -58.9580 -76.9923 2.1084 2.8865 2.3933 0.3535  -0.3468 -0.1242 4.1476 2.8021 2.6210 
-1.2375 0.7617  -1.7180 -0.2957 0.2909  -0.1130 1.2376  0.2808  0.3882  -0.4511 0.5943  -0.4650 
'X-RAY DIFFRACTION' 10 ? refined 25.6069  -46.8526 -21.9897 2.1365 1.5235 2.5578 -0.0354 -0.5744 0.1707  9.8717 5.3750 4.4994 
-2.0624 -2.1876 1.2858  -1.0749 1.0876  0.1668  0.8798  -0.6311 1.8643  -0.5052 -0.8674 -1.1127 
'X-RAY DIFFRACTION' 11 ? refined 21.3391  -63.1367 47.3858  1.9973 1.8232 1.5127 0.0713  0.2315  0.4401  7.4879 5.9341 6.0615 
0.2011  -0.0267 -0.4152 0.1442  0.3525  -0.3608 -1.6511 -1.4507 0.5534  1.5661  0.8760  -0.5787 
'X-RAY DIFFRACTION' 12 ? refined 44.0283  -40.1995 49.8581  2.6471 2.0124 1.6039 0.2881  -0.3056 0.0269  2.9248 3.8854 9.1462 
3.2482  -3.5196 -5.1321 0.8315  -1.7243 0.7194  -1.1154 -0.2950 -0.7349 1.5704  -2.6168 0.8201  
'X-RAY DIFFRACTION' 13 ? refined 28.6073  -60.7975 13.4684  2.0972 1.4558 1.2504 0.2903  0.3202  -0.2916 6.8879 3.1124 2.3240 
2.4917  1.7828  -1.4030 0.0651  0.2079  -0.2818 0.8059  -0.3775 -0.0984 0.1025  0.3970  -0.2333 
'X-RAY DIFFRACTION' 14 ? refined 40.5503  -32.4157 20.6862  1.7412 0.6167 2.4580 0.6372  -0.2767 -0.4927 4.7678 1.7955 6.4019 
1.9619  0.5453  -2.2592 -1.0273 0.0159  1.1429  0.1765  -1.1534 0.1432  0.5810  0.5404  0.7728  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1  1  A 1    A 438  '( CHAIN A AND RESID 1:438 )'                            ? ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  A 439  A 594  '( CHAIN A AND RESID 439:594 )'                          ? ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  B 113  B 354  '( CHAIN B AND  ( RESID 113:354 OR RESID 2001:2004 )  )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 4  3  B 2001 B 2004 '( CHAIN B AND  ( RESID 113:354 OR RESID 2001:2004 )  )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 5  4  C 42   C 240  '( CHAIN C AND RESID 42:240 )'                           ? ? ? ? ? 
'X-RAY DIFFRACTION' 6  5  C 8    C 41   '( CHAIN C AND  ( RESID 8:41 OR RESID 250:361 )  )'      ? ? ? ? ? 
'X-RAY DIFFRACTION' 7  5  C 250  C 361  '( CHAIN C AND  ( RESID 8:41 OR RESID 250:361 )  )'      ? ? ? ? ? 
'X-RAY DIFFRACTION' 8  6  D 42   D 240  '( CHAIN D AND RESID 42:240 )'                           ? ? ? ? ? 
'X-RAY DIFFRACTION' 9  7  D 7    D 41   '( CHAIN D AND  ( RESID 7:41 OR RESID 256:361 )  )'      ? ? ? ? ? 
'X-RAY DIFFRACTION' 10 7  D 256  D 361  '( CHAIN D AND  ( RESID 7:41 OR RESID 256:361 )  )'      ? ? ? ? ? 
'X-RAY DIFFRACTION' 11 8  E 1    E 438  '( CHAIN E AND RESID 1:438 )'                            ? ? ? ? ? 
'X-RAY DIFFRACTION' 12 9  E 439  E 591  '( CHAIN E AND RESID 439:591 )'                          ? ? ? ? ? 
'X-RAY DIFFRACTION' 13 10 F 113  F 354  '( CHAIN F AND  ( RESID 113:354 OR RESID 2001:2004 )  )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 14 10 F 2001 F 2004 '( CHAIN F AND  ( RESID 113:354 OR RESID 2001:2004 )  )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 15 11 G 42   G 240  '( CHAIN G AND RESID 42:240 )'                           ? ? ? ? ? 
'X-RAY DIFFRACTION' 16 12 G 10   G 41   '( CHAIN G AND  ( RESID 10:41 OR RESID 250:361 )  )'     ? ? ? ? ? 
'X-RAY DIFFRACTION' 17 12 G 250  G 361  '( CHAIN G AND  ( RESID 10:41 OR RESID 250:361 )  )'     ? ? ? ? ? 
'X-RAY DIFFRACTION' 18 13 H 42   H 240  '( CHAIN H AND RESID 42:240 )'                           ? ? ? ? ? 
'X-RAY DIFFRACTION' 19 14 H 5    H 41   '( CHAIN H AND  ( RESID 5:41 OR RESID 259:361 )  )'      ? ? ? ? ? 
'X-RAY DIFFRACTION' 20 14 H 259  H 361  '( CHAIN H AND  ( RESID 5:41 OR RESID 259:361 )  )'      ? ? ? ? ? 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.10_2155: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                  4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   F SER 127 ? ? OD2 F ASP 254  ? ? 2.02 
2 1 O   B SER 127 ? ? OD2 B ASP 254  ? ? 2.09 
3 1 OD1 A ASP 414 ? ? OD1 A ASN 418  ? ? 2.18 
4 1 OG  C SER 122 ? ? O   C MET 232  ? ? 2.18 
5 1 CG  E ASN 586 ? ? C1  E NAG 2026 ? ? 2.19 
6 1 CG  A ASN 586 ? ? C1  A NAG 2026 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG C GLU 38  ? ? CD  C GLU 38  ? ? 1.636 1.515 0.121 0.015 N 
2 1 CB D GLU 38  ? ? CG  D GLU 38  ? ? 1.649 1.517 0.132 0.019 N 
3 1 CG D GLU 38  ? ? CD  D GLU 38  ? ? 1.640 1.515 0.125 0.015 N 
4 1 CD D GLU 38  ? ? OE1 D GLU 38  ? ? 1.319 1.252 0.067 0.011 N 
5 1 CG G GLU 38  ? ? CD  G GLU 38  ? ? 1.630 1.515 0.115 0.015 N 
6 1 CB H GLU 38  ? ? CG  H GLU 38  ? ? 1.667 1.517 0.150 0.019 N 
7 1 CG H GLU 38  ? ? CD  H GLU 38  ? ? 1.648 1.515 0.133 0.015 N 
8 1 CB H ASN 148 ? ? CG  H ASN 148 ? ? 1.687 1.506 0.181 0.023 N 
9 1 CD H GLU 261 ? ? OE1 H GLU 261 ? ? 1.320 1.252 0.068 0.011 N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              595 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              595 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              595 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                132.66 
_pdbx_validate_rmsd_angle.angle_target_value         115.30 
_pdbx_validate_rmsd_angle.angle_deviation            17.36 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.30 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1   1 PRO A 28  ? ? -78.65  -162.02 
2   1 ALA A 30  ? ? 55.55   -155.54 
3   1 SER A 32  ? ? -103.49 -166.44 
4   1 GLN A 102 ? ? 60.49   -120.64 
5   1 ASP A 132 ? ? -104.99 59.36   
6   1 SER A 144 ? ? -124.64 -169.36 
7   1 ASP A 148 ? ? 66.56   171.21  
8   1 ALA A 213 ? ? -118.06 -167.18 
9   1 PHE A 231 ? ? -134.21 -33.74  
10  1 MET A 261 ? ? 59.07   70.31   
11  1 PHE A 276 ? ? -56.28  109.75  
12  1 ARG A 398 ? ? -58.52  -71.06  
13  1 SER A 399 ? ? -173.49 130.81  
14  1 ASP A 458 ? ? -152.81 86.36   
15  1 THR A 461 ? ? -138.71 -58.19  
16  1 SER A 472 ? ? -54.30  102.57  
17  1 LYS A 506 ? ? -59.56  102.99  
18  1 ALA A 508 ? ? -75.70  -158.72 
19  1 LEU A 513 ? ? -172.96 142.27  
20  1 TYR A 566 ? ? 53.28   -48.04  
21  1 LYS B 144 ? ? -135.30 -50.83  
22  1 VAL B 161 ? ? -136.05 -74.83  
23  1 ASP B 202 ? ? -54.99  103.83  
24  1 SER B 216 ? ? -111.74 -159.82 
25  1 ASN B 218 ? ? -162.54 -158.62 
26  1 CYS B 235 ? ? -66.24  86.81   
27  1 PHE B 259 ? ? -119.92 -161.96 
28  1 MET B 261 ? ? 66.11   -4.15   
29  1 ASP B 279 ? ? -78.03  -165.35 
30  1 MET B 286 ? ? -97.14  43.36   
31  1 ASN B 306 ? ? 55.60   77.80   
32  1 GLU B 353 ? ? 56.25   -114.45 
33  1 SER C 35  ? ? -161.38 98.93   
34  1 VAL C 59  ? ? -134.84 -83.18  
35  1 PHE C 95  ? ? -123.30 -110.34 
36  1 LYS C 96  ? ? 82.60   -53.44  
37  1 LEU C 128 ? ? -121.10 -160.57 
38  1 VAL C 135 ? ? 65.21   177.11  
39  1 SER C 146 ? ? 56.37   19.01   
40  1 GLN C 147 ? ? 58.35   13.01   
41  1 ASN C 148 ? ? -144.54 -41.38  
42  1 LEU C 153 ? ? -127.62 -89.13  
43  1 PRO C 160 ? ? -69.07  83.30   
44  1 SER C 191 ? ? -102.38 -159.37 
45  1 ALA C 192 ? ? -120.45 -168.63 
46  1 ASN C 208 ? ? -104.26 -157.27 
47  1 ARG C 215 ? ? 66.96   -13.80  
48  1 HIS C 222 ? ? 39.12   39.84   
49  1 PRO C 227 ? ? -38.97  130.54  
50  1 ASP C 252 ? ? -103.00 -137.76 
51  1 CYS C 264 ? ? -65.03  90.16   
52  1 LEU C 277 ? ? -135.45 -30.68  
53  1 ASN C 291 ? ? 62.03   -176.18 
54  1 ALA C 321 ? ? 65.90   -65.31  
55  1 ASN C 352 ? ? 57.52   87.65   
56  1 ARG C 356 ? ? -93.80  -68.91  
57  1 ASP D 8   ? ? 81.69   -59.71  
58  1 MET D 9   ? ? 84.49   172.26  
59  1 ARG D 58  ? ? -62.56  92.26   
60  1 ASN D 89  ? ? -133.47 -53.09  
61  1 PHE D 95  ? ? -131.11 -36.28  
62  1 LYS D 96  ? ? 65.44   -147.25 
63  1 THR D 108 ? ? -143.57 -20.60  
64  1 LEU D 128 ? ? -120.44 -164.28 
65  1 LYS D 134 ? ? 57.91   -139.84 
66  1 VAL D 135 ? ? -53.03  -77.20  
67  1 SER D 146 ? ? 57.19   19.12   
68  1 ASN D 148 ? ? -154.76 -39.30  
69  1 LEU D 153 ? ? -127.46 -86.02  
70  1 PRO D 160 ? ? -68.91  79.97   
71  1 ASP D 170 ? ? -69.67  97.11   
72  1 SER D 191 ? ? -103.82 -164.50 
73  1 THR D 211 ? ? 60.15   -5.37   
74  1 THR D 212 ? ? 69.18   -36.89  
75  1 ARG D 215 ? ? -121.89 -160.67 
76  1 ASN D 225 ? ? 56.71   13.68   
77  1 ALA D 239 ? ? 47.76   -144.44 
78  1 ASN D 263 ? ? -78.94  -169.15 
79  1 CYS D 264 ? ? -64.69  73.84   
80  1 LEU D 277 ? ? -132.90 -34.60  
81  1 ASN D 318 ? ? -155.51 76.72   
82  1 ASN D 352 ? ? 60.69   89.11   
83  1 MET D 353 ? ? -134.62 -47.86  
84  1 ARG D 356 ? ? -95.02  -69.49  
85  1 PRO E 28  ? ? -79.37  -161.40 
86  1 ALA E 30  ? ? 55.72   -154.92 
87  1 SER E 32  ? ? -103.35 -164.86 
88  1 THR E 64  ? ? 75.56   -23.11  
89  1 GLN E 102 ? ? 60.74   -120.58 
90  1 ASP E 132 ? ? -105.14 58.08   
91  1 SER E 144 ? ? -124.94 -168.58 
92  1 ASP E 148 ? ? 66.39   171.80  
93  1 ALA E 213 ? ? -117.44 -166.48 
94  1 PHE E 231 ? ? -135.04 -34.15  
95  1 ASP E 458 ? ? -151.89 85.44   
96  1 THR E 461 ? ? -138.21 -58.86  
97  1 SER E 472 ? ? -53.81  102.87  
98  1 LYS E 506 ? ? -59.58  102.87  
99  1 ALA E 508 ? ? -76.12  -159.29 
100 1 LEU E 513 ? ? -173.37 142.35  
101 1 LYS F 144 ? ? -135.29 -51.04  
102 1 VAL F 161 ? ? -134.80 -75.24  
103 1 ASP F 202 ? ? -56.61  102.24  
104 1 SER F 216 ? ? -112.33 -160.50 
105 1 ASN F 218 ? ? -162.46 -158.87 
106 1 CYS F 235 ? ? -65.40  87.13   
107 1 PHE F 259 ? ? -120.18 -160.58 
108 1 MET F 261 ? ? 66.25   -2.45   
109 1 ASP F 279 ? ? -77.25  -165.61 
110 1 MET F 286 ? ? -97.55  44.21   
111 1 ASN F 306 ? ? 54.68   76.86   
112 1 GLU F 353 ? ? 56.26   -114.76 
113 1 VAL G 39  ? ? 63.20   143.63  
114 1 VAL G 59  ? ? -108.06 -75.59  
115 1 HIS G 88  ? ? -91.04  -158.23 
116 1 PHE G 95  ? ? -124.97 -109.39 
117 1 LYS G 96  ? ? 83.33   -43.58  
118 1 SER G 98  ? ? -64.49  94.19   
119 1 LEU G 128 ? ? -120.71 -159.40 
120 1 VAL G 135 ? ? 53.87   -163.59 
121 1 SER G 146 ? ? 59.55   17.37   
122 1 GLN G 147 ? ? 57.88   14.90   
123 1 ASN G 148 ? ? -145.69 -38.97  
124 1 LEU G 153 ? ? -127.78 -87.83  
125 1 SER G 191 ? ? -103.23 -163.20 
126 1 ALA G 192 ? ? -117.98 -166.87 
127 1 ARG G 215 ? ? 67.82   -10.46  
128 1 HIS G 222 ? ? 48.98   10.76   
129 1 ASP G 252 ? ? -103.59 -138.71 
130 1 CYS G 264 ? ? -64.89  90.60   
131 1 LEU G 277 ? ? -135.41 -31.20  
132 1 ASN G 291 ? ? 61.59   -175.80 
133 1 ASN G 352 ? ? 58.02   87.43   
134 1 ARG G 356 ? ? -92.26  -68.52  
135 1 ILE H 7   ? ? 68.91   -51.74  
136 1 ASP H 8   ? ? 73.16   153.89  
137 1 GLU H 90  ? ? 57.70   -22.64  
138 1 PHE H 95  ? ? -131.50 -36.42  
139 1 LYS H 96  ? ? 65.97   -147.00 
140 1 THR H 108 ? ? -141.95 -21.06  
141 1 LEU H 128 ? ? -121.34 -163.51 
142 1 LYS H 134 ? ? 57.74   -138.41 
143 1 VAL H 135 ? ? -42.46  -79.00  
144 1 SER H 146 ? ? 55.21   -120.77 
145 1 LEU H 153 ? ? -127.61 -86.08  
146 1 PRO H 160 ? ? -69.20  79.53   
147 1 ASP H 170 ? ? -69.98  97.90   
148 1 SER H 191 ? ? -104.64 -166.54 
149 1 ALA H 192 ? ? -119.39 -168.30 
150 1 ASP H 197 ? ? 79.77   -37.42  
151 1 THR H 202 ? ? 154.97  160.52  
152 1 THR H 211 ? ? 60.51   -5.60   
153 1 THR H 212 ? ? 69.25   -37.27  
154 1 ARG H 215 ? ? -121.28 -161.27 
155 1 ASN H 225 ? ? 56.51   13.01   
156 1 ALA H 239 ? ? 47.46   -144.04 
157 1 THR H 260 ? ? -96.45  46.57   
158 1 GLU H 261 ? ? 39.20   37.30   
159 1 LEU H 277 ? ? -133.06 -34.92  
160 1 LEU H 303 ? ? 73.34   -48.92  
161 1 ALA H 312 ? ? -79.24  -72.68  
162 1 ASN H 318 ? ? -159.31 75.93   
163 1 ASN H 352 ? ? 60.01   87.76   
164 1 MET H 353 ? ? -133.71 -47.13  
165 1 ARG H 356 ? ? -94.03  -70.93  
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 C PRO 319 ? CG  ? C PRO 321 CG  
2 1 Y 1 C PRO 319 ? CD  ? C PRO 321 CD  
3 1 Y 1 H ASP 304 ? CG  ? H ASP 306 CG  
4 1 Y 1 H ASP 304 ? OD1 ? H ASP 306 OD1 
5 1 Y 1 H ASP 304 ? OD2 ? H ASP 306 OD2 
# 
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 SER 62  ? A SER 62  
2   1 Y 1 A SER 63  ? A SER 63  
3   1 Y 1 A THR 64  ? A THR 64  
4   1 Y 1 A GLY 466 ? A GLY 466 
5   1 Y 1 A THR 467 ? A THR 467 
6   1 Y 1 A ALA 468 ? A ALA 468 
7   1 Y 1 A LEU 469 ? A LEU 469 
8   1 Y 1 A THR 597 ? A THR 597 
9   1 Y 1 A GLY 598 ? A GLY 598 
10  1 Y 1 A GLY 599 ? A GLY 599 
11  1 Y 1 A LEU 600 ? A LEU 600 
12  1 Y 1 A GLU 601 ? A GLU 601 
13  1 Y 1 B THR 111 ? B THR 1   
14  1 Y 1 B GLU 112 ? B GLU 2   
15  1 Y 1 B ARG 355 ? B ARG 245 
16  1 Y 1 B SER 356 ? B SER 246 
17  1 Y 1 B GLU 357 ? B GLU 247 
18  1 Y 1 B VAL 358 ? B VAL 248 
19  1 Y 1 B GLU 359 ? B GLU 249 
20  1 Y 1 B LEU 360 ? B LEU 250 
21  1 Y 1 B GLU 361 ? B GLU 251 
22  1 Y 1 B HIS 362 ? B HIS 252 
23  1 Y 1 B HIS 363 ? B HIS 253 
24  1 Y 1 B HIS 364 ? B HIS 254 
25  1 Y 1 B HIS 365 ? B HIS 255 
26  1 Y 1 B HIS 366 ? B HIS 256 
27  1 Y 1 B HIS 367 ? B HIS 257 
28  1 Y 1 C GLY -1  ? C GLY 1   
29  1 Y 1 C PRO 0   ? C PRO 2   
30  1 Y 1 C LEU 1   ? C LEU 3   
31  1 Y 1 C SER 2   ? C SER 4   
32  1 Y 1 C THR 3   ? C THR 5   
33  1 Y 1 C SER 4   ? C SER 6   
34  1 Y 1 C LYS 5   ? C LYS 7   
35  1 Y 1 C THR 6   ? C THR 8   
36  1 Y 1 C ILE 7   ? C ILE 9   
37  1 Y 1 C GLY 61  ? C GLY 63  
38  1 Y 1 C GLU 62  ? C GLU 64  
39  1 Y 1 C SER 63  ? C SER 65  
40  1 Y 1 C ALA 64  ? C ALA 66  
41  1 Y 1 C GLU 65  ? C GLU 67  
42  1 Y 1 C PRO 66  ? C PRO 68  
43  1 Y 1 C GLU 67  ? C GLU 69  
44  1 Y 1 C PRO 68  ? C PRO 70  
45  1 Y 1 C GLU 69  ? C GLU 71  
46  1 Y 1 C PRO 70  ? C PRO 72  
47  1 Y 1 C GLU 71  ? C GLU 73  
48  1 Y 1 C ASP 197 ? C ASP 199 
49  1 Y 1 C SER 198 ? C SER 200 
50  1 Y 1 C ARG 199 ? C ARG 201 
51  1 Y 1 C ASP 200 ? C ASP 202 
52  1 Y 1 C ASN 201 ? C ASN 203 
53  1 Y 1 C THR 202 ? C THR 204 
54  1 Y 1 C LEU 203 ? C LEU 205 
55  1 Y 1 C GLN 204 ? C GLN 206 
56  1 Y 1 C VAL 205 ? C VAL 207 
57  1 Y 1 C ASP 206 ? C ASP 208 
58  1 Y 1 C HIS 241 ? C HIS 243 
59  1 Y 1 C LEU 242 ? C LEU 244 
60  1 Y 1 C GLN 243 ? C GLN 245 
61  1 Y 1 C SER 244 ? C SER 246 
62  1 Y 1 C SER 245 ? C SER 247 
63  1 Y 1 C ARG 246 ? C ARG 248 
64  1 Y 1 C HIS 247 ? C HIS 249 
65  1 Y 1 C ARG 248 ? C ARG 250 
66  1 Y 1 C ARG 249 ? C ARG 251 
67  1 Y 1 C ILE 300 ? C ILE 302 
68  1 Y 1 C TRP 301 ? C TRP 303 
69  1 Y 1 C SER 302 ? C SER 304 
70  1 Y 1 C LEU 303 ? C LEU 305 
71  1 Y 1 C ASP 304 ? C ASP 306 
72  1 Y 1 C THR 305 ? C THR 307 
73  1 Y 1 C GLN 306 ? C GLN 308 
74  1 Y 1 C TYR 307 ? C TYR 309 
75  1 Y 1 C SER 308 ? C SER 310 
76  1 Y 1 C LYS 309 ? C LYS 311 
77  1 Y 1 C VAL 310 ? C VAL 312 
78  1 Y 1 C LEU 311 ? C LEU 313 
79  1 Y 1 C ALA 312 ? C ALA 314 
80  1 Y 1 C LEU 313 ? C LEU 315 
81  1 Y 1 C TYR 314 ? C TYR 316 
82  1 Y 1 C ASN 315 ? C ASN 317 
83  1 Y 1 C GLN 316 ? C GLN 318 
84  1 Y 1 C HIS 317 ? C HIS 319 
85  1 Y 1 C ASN 318 ? C ASN 320 
86  1 Y 1 D GLY -1  ? D GLY 1   
87  1 Y 1 D PRO 0   ? D PRO 2   
88  1 Y 1 D LEU 1   ? D LEU 3   
89  1 Y 1 D SER 2   ? D SER 4   
90  1 Y 1 D THR 3   ? D THR 5   
91  1 Y 1 D SER 4   ? D SER 6   
92  1 Y 1 D LYS 5   ? D LYS 7   
93  1 Y 1 D THR 6   ? D THR 8   
94  1 Y 1 D SER 63  ? D SER 65  
95  1 Y 1 D ALA 64  ? D ALA 66  
96  1 Y 1 D GLU 65  ? D GLU 67  
97  1 Y 1 D PRO 66  ? D PRO 68  
98  1 Y 1 D GLU 67  ? D GLU 69  
99  1 Y 1 D PRO 68  ? D PRO 70  
100 1 Y 1 D GLU 69  ? D GLU 71  
101 1 Y 1 D SER 198 ? D SER 200 
102 1 Y 1 D ARG 199 ? D ARG 201 
103 1 Y 1 D ASP 200 ? D ASP 202 
104 1 Y 1 D ASN 201 ? D ASN 203 
105 1 Y 1 D HIS 241 ? D HIS 243 
106 1 Y 1 D LEU 242 ? D LEU 244 
107 1 Y 1 D GLN 243 ? D GLN 245 
108 1 Y 1 D SER 244 ? D SER 246 
109 1 Y 1 D SER 245 ? D SER 247 
110 1 Y 1 D ARG 246 ? D ARG 248 
111 1 Y 1 D HIS 247 ? D HIS 249 
112 1 Y 1 D ARG 248 ? D ARG 250 
113 1 Y 1 D ARG 249 ? D ARG 251 
114 1 Y 1 D ALA 250 ? D ALA 252 
115 1 Y 1 D LEU 251 ? D LEU 253 
116 1 Y 1 D ASP 252 ? D ASP 254 
117 1 Y 1 D THR 253 ? D THR 255 
118 1 Y 1 D ASN 254 ? D ASN 256 
119 1 Y 1 D TYR 255 ? D TYR 257 
120 1 Y 1 D ASP 304 ? D ASP 306 
121 1 Y 1 D THR 305 ? D THR 307 
122 1 Y 1 D GLN 306 ? D GLN 308 
123 1 Y 1 D TYR 307 ? D TYR 309 
124 1 Y 1 D SER 308 ? D SER 310 
125 1 Y 1 D LYS 309 ? D LYS 311 
126 1 Y 1 D GLY 342 ? D GLY 344 
127 1 Y 1 E GLY 466 ? E GLY 466 
128 1 Y 1 E THR 467 ? E THR 467 
129 1 Y 1 E ALA 468 ? E ALA 468 
130 1 Y 1 E LEU 469 ? E LEU 469 
131 1 Y 1 E HIS 592 ? E HIS 592 
132 1 Y 1 E ILE 593 ? E ILE 593 
133 1 Y 1 E LEU 594 ? E LEU 594 
134 1 Y 1 E LEU 595 ? E LEU 595 
135 1 Y 1 E ASP 596 ? E ASP 596 
136 1 Y 1 E THR 597 ? E THR 597 
137 1 Y 1 E GLY 598 ? E GLY 598 
138 1 Y 1 E GLY 599 ? E GLY 599 
139 1 Y 1 E LEU 600 ? E LEU 600 
140 1 Y 1 E GLU 601 ? E GLU 601 
141 1 Y 1 F THR 111 ? F THR 1   
142 1 Y 1 F GLU 112 ? F GLU 2   
143 1 Y 1 F ARG 355 ? F ARG 245 
144 1 Y 1 F SER 356 ? F SER 246 
145 1 Y 1 F GLU 357 ? F GLU 247 
146 1 Y 1 F VAL 358 ? F VAL 248 
147 1 Y 1 F GLU 359 ? F GLU 249 
148 1 Y 1 F LEU 360 ? F LEU 250 
149 1 Y 1 F GLU 361 ? F GLU 251 
150 1 Y 1 F HIS 362 ? F HIS 252 
151 1 Y 1 F HIS 363 ? F HIS 253 
152 1 Y 1 F HIS 364 ? F HIS 254 
153 1 Y 1 F HIS 365 ? F HIS 255 
154 1 Y 1 F HIS 366 ? F HIS 256 
155 1 Y 1 F HIS 367 ? F HIS 257 
156 1 Y 1 G GLY -1  ? G GLY 1   
157 1 Y 1 G PRO 0   ? G PRO 2   
158 1 Y 1 G LEU 1   ? G LEU 3   
159 1 Y 1 G SER 2   ? G SER 4   
160 1 Y 1 G THR 3   ? G THR 5   
161 1 Y 1 G SER 4   ? G SER 6   
162 1 Y 1 G LYS 5   ? G LYS 7   
163 1 Y 1 G THR 6   ? G THR 8   
164 1 Y 1 G ILE 7   ? G ILE 9   
165 1 Y 1 G ASP 8   ? G ASP 10  
166 1 Y 1 G MET 9   ? G MET 11  
167 1 Y 1 G GLN 36  ? G GLN 38  
168 1 Y 1 G GLY 37  ? G GLY 39  
169 1 Y 1 G GLY 61  ? G GLY 63  
170 1 Y 1 G GLU 62  ? G GLU 64  
171 1 Y 1 G SER 63  ? G SER 65  
172 1 Y 1 G ALA 64  ? G ALA 66  
173 1 Y 1 G GLU 65  ? G GLU 67  
174 1 Y 1 G PRO 66  ? G PRO 68  
175 1 Y 1 G GLU 67  ? G GLU 69  
176 1 Y 1 G PRO 68  ? G PRO 70  
177 1 Y 1 G GLU 69  ? G GLU 71  
178 1 Y 1 G PRO 70  ? G PRO 72  
179 1 Y 1 G GLU 71  ? G GLU 73  
180 1 Y 1 G ASP 197 ? G ASP 199 
181 1 Y 1 G SER 198 ? G SER 200 
182 1 Y 1 G ARG 199 ? G ARG 201 
183 1 Y 1 G ASP 200 ? G ASP 202 
184 1 Y 1 G ASN 201 ? G ASN 203 
185 1 Y 1 G THR 202 ? G THR 204 
186 1 Y 1 G LEU 203 ? G LEU 205 
187 1 Y 1 G GLN 204 ? G GLN 206 
188 1 Y 1 G VAL 205 ? G VAL 207 
189 1 Y 1 G HIS 241 ? G HIS 243 
190 1 Y 1 G LEU 242 ? G LEU 244 
191 1 Y 1 G GLN 243 ? G GLN 245 
192 1 Y 1 G SER 244 ? G SER 246 
193 1 Y 1 G SER 245 ? G SER 247 
194 1 Y 1 G ARG 246 ? G ARG 248 
195 1 Y 1 G HIS 247 ? G HIS 249 
196 1 Y 1 G ARG 248 ? G ARG 250 
197 1 Y 1 G ARG 249 ? G ARG 251 
198 1 Y 1 G ILE 300 ? G ILE 302 
199 1 Y 1 G TRP 301 ? G TRP 303 
200 1 Y 1 G SER 302 ? G SER 304 
201 1 Y 1 G LEU 303 ? G LEU 305 
202 1 Y 1 G ASP 304 ? G ASP 306 
203 1 Y 1 G THR 305 ? G THR 307 
204 1 Y 1 G GLN 306 ? G GLN 308 
205 1 Y 1 G TYR 307 ? G TYR 309 
206 1 Y 1 G SER 308 ? G SER 310 
207 1 Y 1 G LYS 309 ? G LYS 311 
208 1 Y 1 G VAL 310 ? G VAL 312 
209 1 Y 1 G LEU 311 ? G LEU 313 
210 1 Y 1 G ALA 312 ? G ALA 314 
211 1 Y 1 G LEU 313 ? G LEU 315 
212 1 Y 1 G TYR 314 ? G TYR 316 
213 1 Y 1 G ASN 315 ? G ASN 317 
214 1 Y 1 G GLN 316 ? G GLN 318 
215 1 Y 1 G HIS 317 ? G HIS 319 
216 1 Y 1 G ASN 318 ? G ASN 320 
217 1 Y 1 G PRO 319 ? G PRO 321 
218 1 Y 1 G GLY 320 ? G GLY 322 
219 1 Y 1 G ALA 321 ? G ALA 323 
220 1 Y 1 G SER 322 ? G SER 324 
221 1 Y 1 G ALA 323 ? G ALA 325 
222 1 Y 1 H GLY -1  ? H GLY 1   
223 1 Y 1 H PRO 0   ? H PRO 2   
224 1 Y 1 H LEU 1   ? H LEU 3   
225 1 Y 1 H SER 2   ? H SER 4   
226 1 Y 1 H THR 3   ? H THR 5   
227 1 Y 1 H SER 4   ? H SER 6   
228 1 Y 1 H GLU 62  ? H GLU 64  
229 1 Y 1 H SER 63  ? H SER 65  
230 1 Y 1 H ALA 64  ? H ALA 66  
231 1 Y 1 H GLU 65  ? H GLU 67  
232 1 Y 1 H PRO 66  ? H PRO 68  
233 1 Y 1 H GLU 67  ? H GLU 69  
234 1 Y 1 H PRO 68  ? H PRO 70  
235 1 Y 1 H GLU 69  ? H GLU 71  
236 1 Y 1 H HIS 241 ? H HIS 243 
237 1 Y 1 H LEU 242 ? H LEU 244 
238 1 Y 1 H GLN 243 ? H GLN 245 
239 1 Y 1 H SER 244 ? H SER 246 
240 1 Y 1 H SER 245 ? H SER 247 
241 1 Y 1 H ARG 246 ? H ARG 248 
242 1 Y 1 H HIS 247 ? H HIS 249 
243 1 Y 1 H ARG 248 ? H ARG 250 
244 1 Y 1 H ARG 249 ? H ARG 251 
245 1 Y 1 H ALA 250 ? H ALA 252 
246 1 Y 1 H LEU 251 ? H LEU 253 
247 1 Y 1 H ASP 252 ? H ASP 254 
248 1 Y 1 H THR 253 ? H THR 255 
249 1 Y 1 H ASN 254 ? H ASN 256 
250 1 Y 1 H TYR 255 ? H TYR 257 
251 1 Y 1 H CYS 256 ? H CYS 258 
252 1 Y 1 H PHE 257 ? H PHE 259 
253 1 Y 1 H SER 258 ? H SER 260 
254 1 Y 1 H THR 305 ? H THR 307 
255 1 Y 1 H GLN 306 ? H GLN 308 
256 1 Y 1 H TYR 307 ? H TYR 309 
257 1 Y 1 H SER 308 ? H SER 310 
258 1 Y 1 H LYS 309 ? H LYS 311 
259 1 Y 1 H GLY 342 ? H GLY 344 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'CALCIUM ION'          CA  
5 N-ACETYL-D-GLUCOSAMINE NAG 
6 BETA-D-MANNOSE         BMA 
7 ALPHA-D-MANNOSE        MAN 
8 'MANGANESE (II) ION'   MN  
9 water                  HOH 
# 
