data_9DOL
# 
_entry.id   9DOL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DOL         pdb_00009dol 10.2210/pdb9dol/pdb 
WWPDB D_1000288541 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-28 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DOL 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              shenping.liu@pfizer.com 
_pdbx_contact_author.name_first         Shenping 
_pdbx_contact_author.name_last          Liu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9400-3007 
# 
_audit_author.name               'Liu, S.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0001-9400-3007 
# 
_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            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                4579 
_citation.page_last                 4579 
_citation.title                     
'Inhibiting peptidylarginine deiminases (PAD1-4) by targeting a Ca 2+ dependent allosteric binding site.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-59919-4 
_citation.pdbx_database_id_PubMed   40379660 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dakin, L.A.'        1  ?                   
primary 'Xing, L.'           2  0000-0002-9056-7996 
primary 'Hall, J.'           3  0000-0002-0316-847X 
primary 'Ding, W.'           4  ?                   
primary 'Vajdos, F.F.'       5  ?                   
primary 'Pelker, J.W.'       6  ?                   
primary 'Ramsey, S.'         7  ?                   
primary 'Balbo, P.'          8  ?                   
primary 'Sahasrabudhe, P.V.' 9  0000-0002-8442-637X 
primary 'Banker, M.E.'       10 ?                   
primary 'Choi, W.Y.'         11 ?                   
primary 'Wright, S.W.'       12 0000-0002-9785-5077 
primary 'Chang, J.S.'        13 0000-0002-8043-8621 
primary 'Curto, J.M.'        14 0000-0001-9033-5952 
primary 'Davoren, J.E.'      15 ?                   
primary 'Drozda, S.E.'       16 ?                   
primary 'Fennell, K.F.'      17 0000-0002-1687-5237 
primary 'Futatsugi, K.'      18 ?                   
primary 'Kortum, S.'         19 ?                   
primary 'Lee, K.L.'          20 ?                   
primary 'Liu, S.'            21 0000-0001-9400-3007 
primary 'Lovering, F.'       22 ?                   
primary 'Nicki, J.A.'        23 0000-0002-5440-2991 
primary 'Trujillo, J.I.'     24 ?                   
primary 'Vincent, F.'        25 0000-0002-8782-0225 
primary 'Schnute, M.E.'      26 0000-0003-3075-4578 
# 
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 'Protein-arginine deiminase type-2' 78673.008 1   3.5.3.15 ? ? ? 
2 non-polymer nat 'CALCIUM ION' 40.078    4   ?        ? ? ? 
3 non-polymer syn 
'(2S)-2-amino-2-{1-[(5M)-5-(3,5-dichloropyridin-2-yl)isoquinolin-1-yl]piperidin-4-yl}-1-(pyrrolidin-1-yl)ethan-1-one' 484.421   1 
?        ? ? ? 
4 water       nat water 18.015    378 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'PAD-H19,Peptidylarginine deiminase II,Protein-arginine deiminase type II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGHHHHHHHHHHSSGHIEGRHMLRERTVRLQYGSRVEAVYVLGTYLWTDVYSAAPAGAQTFSLKHSEHVWVEVVRDGEAE
EVATNGKQRWLLSPSTTLRVTMSQASTEASSDKVTVNYYDEEGSIPIDQAGLFLTAIEISLDVDADRDGVVEKNNPKKAS
WTWGPEGQGAILLVNCDRETPWLPKEDCRDEKVYSKEDLKDMSQMILRTKGPDRLPAGYEIVLYISMSDSDKVGVFYVEN
PFFGQRYIHILGRRKLYHVVKYTGGSAELLFFVEGLCFPDEGFSGLVSIHVSLLEYMAQDIPLTPIFTDTVIFRIAPWIM
TPNILPPVSVFVCCMKDNYLFLKEVKNLVEKTNCELKVCFQYLNRGDRWIQDEIEFGYIEAPHKGFPVVLDSPRDGNLKD
FPVKELLGPDFGYVTREPLFESVTSLDSFGNLEVSPPVTVNGKTYPLGRILIGSSFPLSGGRRMTKVVRDFLKAQQVQAP
VELYSDWLTVGHVDEFMSFVPIPGTKKFLLLMASTSACYKLFREKQKDGHGEAIMFKGLGGMSSKRITINKILSNESLVQ
ENLYFQRCLDWNRDILKKELGLTEQDIIDLPALFKMDEDHRARAFFPNMVNMIVLDKDLGIPKPFGPQVEEECCLEMHVR
GLLEPLGLECTFIDDISAYHKFLGEVHCGTNVRRKPFTFKWWHMVPSRRS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGHHHHHHHHHHSSGHIEGRHMLRERTVRLQYGSRVEAVYVLGTYLWTDVYSAAPAGAQTFSLKHSEHVWVEVVRDGEAE
EVATNGKQRWLLSPSTTLRVTMSQASTEASSDKVTVNYYDEEGSIPIDQAGLFLTAIEISLDVDADRDGVVEKNNPKKAS
WTWGPEGQGAILLVNCDRETPWLPKEDCRDEKVYSKEDLKDMSQMILRTKGPDRLPAGYEIVLYISMSDSDKVGVFYVEN
PFFGQRYIHILGRRKLYHVVKYTGGSAELLFFVEGLCFPDEGFSGLVSIHVSLLEYMAQDIPLTPIFTDTVIFRIAPWIM
TPNILPPVSVFVCCMKDNYLFLKEVKNLVEKTNCELKVCFQYLNRGDRWIQDEIEFGYIEAPHKGFPVVLDSPRDGNLKD
FPVKELLGPDFGYVTREPLFESVTSLDSFGNLEVSPPVTVNGKTYPLGRILIGSSFPLSGGRRMTKVVRDFLKAQQVQAP
VELYSDWLTVGHVDEFMSFVPIPGTKKFLLLMASTSACYKLFREKQKDGHGEAIMFKGLGGMSSKRITINKILSNESLVQ
ENLYFQRCLDWNRDILKKELGLTEQDIIDLPALFKMDEDHRARAFFPNMVNMIVLDKDLGIPKPFGPQVEEECCLEMHVR
GLLEPLGLECTFIDDISAYHKFLGEVHCGTNVRRKPFTFKWWHMVPSRRS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CALCIUM ION'                                                                                                         CA    
3 '(2S)-2-amino-2-{1-[(5M)-5-(3,5-dichloropyridin-2-yl)isoquinolin-1-yl]piperidin-4-yl}-1-(pyrrolidin-1-yl)ethan-1-one' A1A8O 
4 water                                                                                                                 HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  HIS n 
1 12  HIS n 
1 13  SER n 
1 14  SER n 
1 15  GLY n 
1 16  HIS n 
1 17  ILE n 
1 18  GLU n 
1 19  GLY n 
1 20  ARG n 
1 21  HIS n 
1 22  MET n 
1 23  LEU n 
1 24  ARG n 
1 25  GLU n 
1 26  ARG n 
1 27  THR n 
1 28  VAL n 
1 29  ARG n 
1 30  LEU n 
1 31  GLN n 
1 32  TYR n 
1 33  GLY n 
1 34  SER n 
1 35  ARG n 
1 36  VAL n 
1 37  GLU n 
1 38  ALA n 
1 39  VAL n 
1 40  TYR n 
1 41  VAL n 
1 42  LEU n 
1 43  GLY n 
1 44  THR n 
1 45  TYR n 
1 46  LEU n 
1 47  TRP n 
1 48  THR n 
1 49  ASP n 
1 50  VAL n 
1 51  TYR n 
1 52  SER n 
1 53  ALA n 
1 54  ALA n 
1 55  PRO n 
1 56  ALA n 
1 57  GLY n 
1 58  ALA n 
1 59  GLN n 
1 60  THR n 
1 61  PHE n 
1 62  SER n 
1 63  LEU n 
1 64  LYS n 
1 65  HIS n 
1 66  SER n 
1 67  GLU n 
1 68  HIS n 
1 69  VAL n 
1 70  TRP n 
1 71  VAL n 
1 72  GLU n 
1 73  VAL n 
1 74  VAL n 
1 75  ARG n 
1 76  ASP n 
1 77  GLY n 
1 78  GLU n 
1 79  ALA n 
1 80  GLU n 
1 81  GLU n 
1 82  VAL n 
1 83  ALA n 
1 84  THR n 
1 85  ASN n 
1 86  GLY n 
1 87  LYS n 
1 88  GLN n 
1 89  ARG n 
1 90  TRP n 
1 91  LEU n 
1 92  LEU n 
1 93  SER n 
1 94  PRO n 
1 95  SER n 
1 96  THR n 
1 97  THR n 
1 98  LEU n 
1 99  ARG n 
1 100 VAL n 
1 101 THR n 
1 102 MET n 
1 103 SER n 
1 104 GLN n 
1 105 ALA n 
1 106 SER n 
1 107 THR n 
1 108 GLU n 
1 109 ALA n 
1 110 SER n 
1 111 SER n 
1 112 ASP n 
1 113 LYS n 
1 114 VAL n 
1 115 THR n 
1 116 VAL n 
1 117 ASN n 
1 118 TYR n 
1 119 TYR n 
1 120 ASP n 
1 121 GLU n 
1 122 GLU n 
1 123 GLY n 
1 124 SER n 
1 125 ILE n 
1 126 PRO n 
1 127 ILE n 
1 128 ASP n 
1 129 GLN n 
1 130 ALA n 
1 131 GLY n 
1 132 LEU n 
1 133 PHE n 
1 134 LEU n 
1 135 THR n 
1 136 ALA n 
1 137 ILE n 
1 138 GLU n 
1 139 ILE n 
1 140 SER n 
1 141 LEU n 
1 142 ASP n 
1 143 VAL n 
1 144 ASP n 
1 145 ALA n 
1 146 ASP n 
1 147 ARG n 
1 148 ASP n 
1 149 GLY n 
1 150 VAL n 
1 151 VAL n 
1 152 GLU n 
1 153 LYS n 
1 154 ASN n 
1 155 ASN n 
1 156 PRO n 
1 157 LYS n 
1 158 LYS n 
1 159 ALA n 
1 160 SER n 
1 161 TRP n 
1 162 THR n 
1 163 TRP n 
1 164 GLY n 
1 165 PRO n 
1 166 GLU n 
1 167 GLY n 
1 168 GLN n 
1 169 GLY n 
1 170 ALA n 
1 171 ILE n 
1 172 LEU n 
1 173 LEU n 
1 174 VAL n 
1 175 ASN n 
1 176 CYS n 
1 177 ASP n 
1 178 ARG n 
1 179 GLU n 
1 180 THR n 
1 181 PRO n 
1 182 TRP n 
1 183 LEU n 
1 184 PRO n 
1 185 LYS n 
1 186 GLU n 
1 187 ASP n 
1 188 CYS n 
1 189 ARG n 
1 190 ASP n 
1 191 GLU n 
1 192 LYS n 
1 193 VAL n 
1 194 TYR n 
1 195 SER n 
1 196 LYS n 
1 197 GLU n 
1 198 ASP n 
1 199 LEU n 
1 200 LYS n 
1 201 ASP n 
1 202 MET n 
1 203 SER n 
1 204 GLN n 
1 205 MET n 
1 206 ILE n 
1 207 LEU n 
1 208 ARG n 
1 209 THR n 
1 210 LYS n 
1 211 GLY n 
1 212 PRO n 
1 213 ASP n 
1 214 ARG n 
1 215 LEU n 
1 216 PRO n 
1 217 ALA n 
1 218 GLY n 
1 219 TYR n 
1 220 GLU n 
1 221 ILE n 
1 222 VAL n 
1 223 LEU n 
1 224 TYR n 
1 225 ILE n 
1 226 SER n 
1 227 MET n 
1 228 SER n 
1 229 ASP n 
1 230 SER n 
1 231 ASP n 
1 232 LYS n 
1 233 VAL n 
1 234 GLY n 
1 235 VAL n 
1 236 PHE n 
1 237 TYR n 
1 238 VAL n 
1 239 GLU n 
1 240 ASN n 
1 241 PRO n 
1 242 PHE n 
1 243 PHE n 
1 244 GLY n 
1 245 GLN n 
1 246 ARG n 
1 247 TYR n 
1 248 ILE n 
1 249 HIS n 
1 250 ILE n 
1 251 LEU n 
1 252 GLY n 
1 253 ARG n 
1 254 ARG n 
1 255 LYS n 
1 256 LEU n 
1 257 TYR n 
1 258 HIS n 
1 259 VAL n 
1 260 VAL n 
1 261 LYS n 
1 262 TYR n 
1 263 THR n 
1 264 GLY n 
1 265 GLY n 
1 266 SER n 
1 267 ALA n 
1 268 GLU n 
1 269 LEU n 
1 270 LEU n 
1 271 PHE n 
1 272 PHE n 
1 273 VAL n 
1 274 GLU n 
1 275 GLY n 
1 276 LEU n 
1 277 CYS n 
1 278 PHE n 
1 279 PRO n 
1 280 ASP n 
1 281 GLU n 
1 282 GLY n 
1 283 PHE n 
1 284 SER n 
1 285 GLY n 
1 286 LEU n 
1 287 VAL n 
1 288 SER n 
1 289 ILE n 
1 290 HIS n 
1 291 VAL n 
1 292 SER n 
1 293 LEU n 
1 294 LEU n 
1 295 GLU n 
1 296 TYR n 
1 297 MET n 
1 298 ALA n 
1 299 GLN n 
1 300 ASP n 
1 301 ILE n 
1 302 PRO n 
1 303 LEU n 
1 304 THR n 
1 305 PRO n 
1 306 ILE n 
1 307 PHE n 
1 308 THR n 
1 309 ASP n 
1 310 THR n 
1 311 VAL n 
1 312 ILE n 
1 313 PHE n 
1 314 ARG n 
1 315 ILE n 
1 316 ALA n 
1 317 PRO n 
1 318 TRP n 
1 319 ILE n 
1 320 MET n 
1 321 THR n 
1 322 PRO n 
1 323 ASN n 
1 324 ILE n 
1 325 LEU n 
1 326 PRO n 
1 327 PRO n 
1 328 VAL n 
1 329 SER n 
1 330 VAL n 
1 331 PHE n 
1 332 VAL n 
1 333 CYS n 
1 334 CYS n 
1 335 MET n 
1 336 LYS n 
1 337 ASP n 
1 338 ASN n 
1 339 TYR n 
1 340 LEU n 
1 341 PHE n 
1 342 LEU n 
1 343 LYS n 
1 344 GLU n 
1 345 VAL n 
1 346 LYS n 
1 347 ASN n 
1 348 LEU n 
1 349 VAL n 
1 350 GLU n 
1 351 LYS n 
1 352 THR n 
1 353 ASN n 
1 354 CYS n 
1 355 GLU n 
1 356 LEU n 
1 357 LYS n 
1 358 VAL n 
1 359 CYS n 
1 360 PHE n 
1 361 GLN n 
1 362 TYR n 
1 363 LEU n 
1 364 ASN n 
1 365 ARG n 
1 366 GLY n 
1 367 ASP n 
1 368 ARG n 
1 369 TRP n 
1 370 ILE n 
1 371 GLN n 
1 372 ASP n 
1 373 GLU n 
1 374 ILE n 
1 375 GLU n 
1 376 PHE n 
1 377 GLY n 
1 378 TYR n 
1 379 ILE n 
1 380 GLU n 
1 381 ALA n 
1 382 PRO n 
1 383 HIS n 
1 384 LYS n 
1 385 GLY n 
1 386 PHE n 
1 387 PRO n 
1 388 VAL n 
1 389 VAL n 
1 390 LEU n 
1 391 ASP n 
1 392 SER n 
1 393 PRO n 
1 394 ARG n 
1 395 ASP n 
1 396 GLY n 
1 397 ASN n 
1 398 LEU n 
1 399 LYS n 
1 400 ASP n 
1 401 PHE n 
1 402 PRO n 
1 403 VAL n 
1 404 LYS n 
1 405 GLU n 
1 406 LEU n 
1 407 LEU n 
1 408 GLY n 
1 409 PRO n 
1 410 ASP n 
1 411 PHE n 
1 412 GLY n 
1 413 TYR n 
1 414 VAL n 
1 415 THR n 
1 416 ARG n 
1 417 GLU n 
1 418 PRO n 
1 419 LEU n 
1 420 PHE n 
1 421 GLU n 
1 422 SER n 
1 423 VAL n 
1 424 THR n 
1 425 SER n 
1 426 LEU n 
1 427 ASP n 
1 428 SER n 
1 429 PHE n 
1 430 GLY n 
1 431 ASN n 
1 432 LEU n 
1 433 GLU n 
1 434 VAL n 
1 435 SER n 
1 436 PRO n 
1 437 PRO n 
1 438 VAL n 
1 439 THR n 
1 440 VAL n 
1 441 ASN n 
1 442 GLY n 
1 443 LYS n 
1 444 THR n 
1 445 TYR n 
1 446 PRO n 
1 447 LEU n 
1 448 GLY n 
1 449 ARG n 
1 450 ILE n 
1 451 LEU n 
1 452 ILE n 
1 453 GLY n 
1 454 SER n 
1 455 SER n 
1 456 PHE n 
1 457 PRO n 
1 458 LEU n 
1 459 SER n 
1 460 GLY n 
1 461 GLY n 
1 462 ARG n 
1 463 ARG n 
1 464 MET n 
1 465 THR n 
1 466 LYS n 
1 467 VAL n 
1 468 VAL n 
1 469 ARG n 
1 470 ASP n 
1 471 PHE n 
1 472 LEU n 
1 473 LYS n 
1 474 ALA n 
1 475 GLN n 
1 476 GLN n 
1 477 VAL n 
1 478 GLN n 
1 479 ALA n 
1 480 PRO n 
1 481 VAL n 
1 482 GLU n 
1 483 LEU n 
1 484 TYR n 
1 485 SER n 
1 486 ASP n 
1 487 TRP n 
1 488 LEU n 
1 489 THR n 
1 490 VAL n 
1 491 GLY n 
1 492 HIS n 
1 493 VAL n 
1 494 ASP n 
1 495 GLU n 
1 496 PHE n 
1 497 MET n 
1 498 SER n 
1 499 PHE n 
1 500 VAL n 
1 501 PRO n 
1 502 ILE n 
1 503 PRO n 
1 504 GLY n 
1 505 THR n 
1 506 LYS n 
1 507 LYS n 
1 508 PHE n 
1 509 LEU n 
1 510 LEU n 
1 511 LEU n 
1 512 MET n 
1 513 ALA n 
1 514 SER n 
1 515 THR n 
1 516 SER n 
1 517 ALA n 
1 518 CYS n 
1 519 TYR n 
1 520 LYS n 
1 521 LEU n 
1 522 PHE n 
1 523 ARG n 
1 524 GLU n 
1 525 LYS n 
1 526 GLN n 
1 527 LYS n 
1 528 ASP n 
1 529 GLY n 
1 530 HIS n 
1 531 GLY n 
1 532 GLU n 
1 533 ALA n 
1 534 ILE n 
1 535 MET n 
1 536 PHE n 
1 537 LYS n 
1 538 GLY n 
1 539 LEU n 
1 540 GLY n 
1 541 GLY n 
1 542 MET n 
1 543 SER n 
1 544 SER n 
1 545 LYS n 
1 546 ARG n 
1 547 ILE n 
1 548 THR n 
1 549 ILE n 
1 550 ASN n 
1 551 LYS n 
1 552 ILE n 
1 553 LEU n 
1 554 SER n 
1 555 ASN n 
1 556 GLU n 
1 557 SER n 
1 558 LEU n 
1 559 VAL n 
1 560 GLN n 
1 561 GLU n 
1 562 ASN n 
1 563 LEU n 
1 564 TYR n 
1 565 PHE n 
1 566 GLN n 
1 567 ARG n 
1 568 CYS n 
1 569 LEU n 
1 570 ASP n 
1 571 TRP n 
1 572 ASN n 
1 573 ARG n 
1 574 ASP n 
1 575 ILE n 
1 576 LEU n 
1 577 LYS n 
1 578 LYS n 
1 579 GLU n 
1 580 LEU n 
1 581 GLY n 
1 582 LEU n 
1 583 THR n 
1 584 GLU n 
1 585 GLN n 
1 586 ASP n 
1 587 ILE n 
1 588 ILE n 
1 589 ASP n 
1 590 LEU n 
1 591 PRO n 
1 592 ALA n 
1 593 LEU n 
1 594 PHE n 
1 595 LYS n 
1 596 MET n 
1 597 ASP n 
1 598 GLU n 
1 599 ASP n 
1 600 HIS n 
1 601 ARG n 
1 602 ALA n 
1 603 ARG n 
1 604 ALA n 
1 605 PHE n 
1 606 PHE n 
1 607 PRO n 
1 608 ASN n 
1 609 MET n 
1 610 VAL n 
1 611 ASN n 
1 612 MET n 
1 613 ILE n 
1 614 VAL n 
1 615 LEU n 
1 616 ASP n 
1 617 LYS n 
1 618 ASP n 
1 619 LEU n 
1 620 GLY n 
1 621 ILE n 
1 622 PRO n 
1 623 LYS n 
1 624 PRO n 
1 625 PHE n 
1 626 GLY n 
1 627 PRO n 
1 628 GLN n 
1 629 VAL n 
1 630 GLU n 
1 631 GLU n 
1 632 GLU n 
1 633 CYS n 
1 634 CYS n 
1 635 LEU n 
1 636 GLU n 
1 637 MET n 
1 638 HIS n 
1 639 VAL n 
1 640 ARG n 
1 641 GLY n 
1 642 LEU n 
1 643 LEU n 
1 644 GLU n 
1 645 PRO n 
1 646 LEU n 
1 647 GLY n 
1 648 LEU n 
1 649 GLU n 
1 650 CYS n 
1 651 THR n 
1 652 PHE n 
1 653 ILE n 
1 654 ASP n 
1 655 ASP n 
1 656 ILE n 
1 657 SER n 
1 658 ALA n 
1 659 TYR n 
1 660 HIS n 
1 661 LYS n 
1 662 PHE n 
1 663 LEU n 
1 664 GLY n 
1 665 GLU n 
1 666 VAL n 
1 667 HIS n 
1 668 CYS n 
1 669 GLY n 
1 670 THR n 
1 671 ASN n 
1 672 VAL n 
1 673 ARG n 
1 674 ARG n 
1 675 LYS n 
1 676 PRO n 
1 677 PHE n 
1 678 THR n 
1 679 PHE n 
1 680 LYS n 
1 681 TRP n 
1 682 TRP n 
1 683 HIS n 
1 684 MET n 
1 685 VAL n 
1 686 PRO n 
1 687 SER n 
1 688 ARG n 
1 689 ARG n 
1 690 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   690 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PADI2, KIAA0994, PAD2, PDI2' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Insect expression vector pBlueBacmsGCA1C239A-C244A' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     1944737 
_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                   ? 
# 
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 
A1A8O non-polymer         . 
'(2S)-2-amino-2-{1-[(5M)-5-(3,5-dichloropyridin-2-yl)isoquinolin-1-yl]piperidin-4-yl}-1-(pyrrolidin-1-yl)ethan-1-one' ? 
'C25 H27 Cl2 N5 O' 484.421 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'       133.103 
CA    non-polymer         . 'CALCIUM ION' ? 'Ca 2'             40.078  
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'       75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'   156.162 
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 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -20 ?   ?   ?   A . n 
A 1 2   GLY 2   -19 ?   ?   ?   A . n 
A 1 3   HIS 3   -18 ?   ?   ?   A . n 
A 1 4   HIS 4   -17 ?   ?   ?   A . n 
A 1 5   HIS 5   -16 ?   ?   ?   A . n 
A 1 6   HIS 6   -15 ?   ?   ?   A . n 
A 1 7   HIS 7   -14 ?   ?   ?   A . n 
A 1 8   HIS 8   -13 ?   ?   ?   A . n 
A 1 9   HIS 9   -12 ?   ?   ?   A . n 
A 1 10  HIS 10  -11 ?   ?   ?   A . n 
A 1 11  HIS 11  -10 ?   ?   ?   A . n 
A 1 12  HIS 12  -9  ?   ?   ?   A . n 
A 1 13  SER 13  -8  ?   ?   ?   A . n 
A 1 14  SER 14  -7  ?   ?   ?   A . n 
A 1 15  GLY 15  -6  ?   ?   ?   A . n 
A 1 16  HIS 16  -5  ?   ?   ?   A . n 
A 1 17  ILE 17  -4  ?   ?   ?   A . n 
A 1 18  GLU 18  -3  ?   ?   ?   A . n 
A 1 19  GLY 19  -2  ?   ?   ?   A . n 
A 1 20  ARG 20  -1  ?   ?   ?   A . n 
A 1 21  HIS 21  0   ?   ?   ?   A . n 
A 1 22  MET 22  1   1   MET MET A . n 
A 1 23  LEU 23  2   2   LEU LEU A . n 
A 1 24  ARG 24  3   3   ARG ARG A . n 
A 1 25  GLU 25  4   4   GLU GLU A . n 
A 1 26  ARG 26  5   5   ARG ARG A . n 
A 1 27  THR 27  6   6   THR THR A . n 
A 1 28  VAL 28  7   7   VAL VAL A . n 
A 1 29  ARG 29  8   8   ARG ARG A . n 
A 1 30  LEU 30  9   9   LEU LEU A . n 
A 1 31  GLN 31  10  10  GLN GLN A . n 
A 1 32  TYR 32  11  11  TYR TYR A . n 
A 1 33  GLY 33  12  12  GLY GLY A . n 
A 1 34  SER 34  13  13  SER SER A . n 
A 1 35  ARG 35  14  14  ARG ARG A . n 
A 1 36  VAL 36  15  15  VAL VAL A . n 
A 1 37  GLU 37  16  16  GLU GLU A . n 
A 1 38  ALA 38  17  17  ALA ALA A . n 
A 1 39  VAL 39  18  18  VAL VAL A . n 
A 1 40  TYR 40  19  19  TYR TYR A . n 
A 1 41  VAL 41  20  20  VAL VAL A . n 
A 1 42  LEU 42  21  21  LEU LEU A . n 
A 1 43  GLY 43  22  22  GLY GLY A . n 
A 1 44  THR 44  23  23  THR THR A . n 
A 1 45  TYR 45  24  24  TYR TYR A . n 
A 1 46  LEU 46  25  25  LEU LEU A . n 
A 1 47  TRP 47  26  26  TRP TRP A . n 
A 1 48  THR 48  27  27  THR THR A . n 
A 1 49  ASP 49  28  28  ASP ASP A . n 
A 1 50  VAL 50  29  29  VAL VAL A . n 
A 1 51  TYR 51  30  30  TYR TYR A . n 
A 1 52  SER 52  31  31  SER SER A . n 
A 1 53  ALA 53  32  32  ALA ALA A . n 
A 1 54  ALA 54  33  33  ALA ALA A . n 
A 1 55  PRO 55  34  34  PRO PRO A . n 
A 1 56  ALA 56  35  35  ALA ALA A . n 
A 1 57  GLY 57  36  36  GLY GLY A . n 
A 1 58  ALA 58  37  37  ALA ALA A . n 
A 1 59  GLN 59  38  38  GLN GLN A . n 
A 1 60  THR 60  39  39  THR THR A . n 
A 1 61  PHE 61  40  40  PHE PHE A . n 
A 1 62  SER 62  41  41  SER SER A . n 
A 1 63  LEU 63  42  42  LEU LEU A . n 
A 1 64  LYS 64  43  43  LYS LYS A . n 
A 1 65  HIS 65  44  44  HIS HIS A . n 
A 1 66  SER 66  45  45  SER SER A . n 
A 1 67  GLU 67  46  46  GLU GLU A . n 
A 1 68  HIS 68  47  47  HIS HIS A . n 
A 1 69  VAL 69  48  48  VAL VAL A . n 
A 1 70  TRP 70  49  49  TRP TRP A . n 
A 1 71  VAL 71  50  50  VAL VAL A . n 
A 1 72  GLU 72  51  51  GLU GLU A . n 
A 1 73  VAL 73  52  52  VAL VAL A . n 
A 1 74  VAL 74  53  53  VAL VAL A . n 
A 1 75  ARG 75  54  54  ARG ARG A . n 
A 1 76  ASP 76  55  55  ASP ASP A . n 
A 1 77  GLY 77  56  56  GLY GLY A . n 
A 1 78  GLU 78  57  57  GLU GLU A . n 
A 1 79  ALA 79  58  58  ALA ALA A . n 
A 1 80  GLU 80  59  59  GLU GLU A . n 
A 1 81  GLU 81  60  60  GLU GLU A . n 
A 1 82  VAL 82  61  61  VAL VAL A . n 
A 1 83  ALA 83  62  62  ALA ALA A . n 
A 1 84  THR 84  63  63  THR THR A . n 
A 1 85  ASN 85  64  64  ASN ASN A . n 
A 1 86  GLY 86  65  65  GLY GLY A . n 
A 1 87  LYS 87  66  66  LYS LYS A . n 
A 1 88  GLN 88  67  67  GLN GLN A . n 
A 1 89  ARG 89  68  68  ARG ARG A . n 
A 1 90  TRP 90  69  69  TRP TRP A . n 
A 1 91  LEU 91  70  70  LEU LEU A . n 
A 1 92  LEU 92  71  71  LEU LEU A . n 
A 1 93  SER 93  72  72  SER SER A . n 
A 1 94  PRO 94  73  73  PRO PRO A . n 
A 1 95  SER 95  74  74  SER SER A . n 
A 1 96  THR 96  75  75  THR THR A . n 
A 1 97  THR 97  76  76  THR THR A . n 
A 1 98  LEU 98  77  77  LEU LEU A . n 
A 1 99  ARG 99  78  78  ARG ARG A . n 
A 1 100 VAL 100 79  79  VAL VAL A . n 
A 1 101 THR 101 80  80  THR THR A . n 
A 1 102 MET 102 81  81  MET MET A . n 
A 1 103 SER 103 82  82  SER SER A . n 
A 1 104 GLN 104 83  83  GLN GLN A . n 
A 1 105 ALA 105 84  84  ALA ALA A . n 
A 1 106 SER 106 85  85  SER SER A . n 
A 1 107 THR 107 86  86  THR THR A . n 
A 1 108 GLU 108 87  87  GLU GLU A . n 
A 1 109 ALA 109 88  88  ALA ALA A . n 
A 1 110 SER 110 89  89  SER SER A . n 
A 1 111 SER 111 90  90  SER SER A . n 
A 1 112 ASP 112 91  91  ASP ASP A . n 
A 1 113 LYS 113 92  92  LYS LYS A . n 
A 1 114 VAL 114 93  93  VAL VAL A . n 
A 1 115 THR 115 94  94  THR THR A . n 
A 1 116 VAL 116 95  95  VAL VAL A . n 
A 1 117 ASN 117 96  96  ASN ASN A . n 
A 1 118 TYR 118 97  97  TYR TYR A . n 
A 1 119 TYR 119 98  98  TYR TYR A . n 
A 1 120 ASP 120 99  99  ASP ASP A . n 
A 1 121 GLU 121 100 100 GLU GLU A . n 
A 1 122 GLU 122 101 101 GLU GLU A . n 
A 1 123 GLY 123 102 102 GLY GLY A . n 
A 1 124 SER 124 103 103 SER SER A . n 
A 1 125 ILE 125 104 104 ILE ILE A . n 
A 1 126 PRO 126 105 105 PRO PRO A . n 
A 1 127 ILE 127 106 106 ILE ILE A . n 
A 1 128 ASP 128 107 107 ASP ASP A . n 
A 1 129 GLN 129 108 108 GLN GLN A . n 
A 1 130 ALA 130 109 109 ALA ALA A . n 
A 1 131 GLY 131 110 110 GLY GLY A . n 
A 1 132 LEU 132 111 111 LEU LEU A . n 
A 1 133 PHE 133 112 112 PHE PHE A . n 
A 1 134 LEU 134 113 113 LEU LEU A . n 
A 1 135 THR 135 114 114 THR THR A . n 
A 1 136 ALA 136 115 115 ALA ALA A . n 
A 1 137 ILE 137 116 116 ILE ILE A . n 
A 1 138 GLU 138 117 117 GLU GLU A . n 
A 1 139 ILE 139 118 118 ILE ILE A . n 
A 1 140 SER 140 119 119 SER SER A . n 
A 1 141 LEU 141 120 120 LEU LEU A . n 
A 1 142 ASP 142 121 121 ASP ASP A . n 
A 1 143 VAL 143 122 122 VAL VAL A . n 
A 1 144 ASP 144 123 123 ASP ASP A . n 
A 1 145 ALA 145 124 124 ALA ALA A . n 
A 1 146 ASP 146 125 125 ASP ASP A . n 
A 1 147 ARG 147 126 126 ARG ARG A . n 
A 1 148 ASP 148 127 127 ASP ASP A . n 
A 1 149 GLY 149 128 128 GLY GLY A . n 
A 1 150 VAL 150 129 129 VAL VAL A . n 
A 1 151 VAL 151 130 130 VAL VAL A . n 
A 1 152 GLU 152 131 131 GLU GLU A . n 
A 1 153 LYS 153 132 132 LYS LYS A . n 
A 1 154 ASN 154 133 133 ASN ASN A . n 
A 1 155 ASN 155 134 134 ASN ASN A . n 
A 1 156 PRO 156 135 135 PRO PRO A . n 
A 1 157 LYS 157 136 136 LYS LYS A . n 
A 1 158 LYS 158 137 137 LYS LYS A . n 
A 1 159 ALA 159 138 138 ALA ALA A . n 
A 1 160 SER 160 139 139 SER SER A . n 
A 1 161 TRP 161 140 140 TRP TRP A . n 
A 1 162 THR 162 141 141 THR THR A . n 
A 1 163 TRP 163 142 142 TRP TRP A . n 
A 1 164 GLY 164 143 143 GLY GLY A . n 
A 1 165 PRO 165 144 144 PRO PRO A . n 
A 1 166 GLU 166 145 145 GLU GLU A . n 
A 1 167 GLY 167 146 146 GLY GLY A . n 
A 1 168 GLN 168 147 147 GLN GLN A . n 
A 1 169 GLY 169 148 148 GLY GLY A . n 
A 1 170 ALA 170 149 149 ALA ALA A . n 
A 1 171 ILE 171 150 150 ILE ILE A . n 
A 1 172 LEU 172 151 151 LEU LEU A . n 
A 1 173 LEU 173 152 152 LEU LEU A . n 
A 1 174 VAL 174 153 153 VAL VAL A . n 
A 1 175 ASN 175 154 154 ASN ASN A . n 
A 1 176 CYS 176 155 155 CYS CYS A . n 
A 1 177 ASP 177 156 156 ASP ASP A . n 
A 1 178 ARG 178 157 157 ARG ARG A . n 
A 1 179 GLU 179 158 158 GLU GLU A . n 
A 1 180 THR 180 159 159 THR THR A . n 
A 1 181 PRO 181 160 160 PRO PRO A . n 
A 1 182 TRP 182 161 161 TRP TRP A . n 
A 1 183 LEU 183 162 162 LEU LEU A . n 
A 1 184 PRO 184 163 163 PRO PRO A . n 
A 1 185 LYS 185 164 164 LYS LYS A . n 
A 1 186 GLU 186 165 165 GLU GLU A . n 
A 1 187 ASP 187 166 166 ASP ASP A . n 
A 1 188 CYS 188 167 167 CYS CYS A . n 
A 1 189 ARG 189 168 168 ARG ARG A . n 
A 1 190 ASP 190 169 169 ASP ASP A . n 
A 1 191 GLU 191 170 170 GLU GLU A . n 
A 1 192 LYS 192 171 171 LYS LYS A . n 
A 1 193 VAL 193 172 172 VAL VAL A . n 
A 1 194 TYR 194 173 173 TYR TYR A . n 
A 1 195 SER 195 174 174 SER SER A . n 
A 1 196 LYS 196 175 175 LYS LYS A . n 
A 1 197 GLU 197 176 176 GLU GLU A . n 
A 1 198 ASP 198 177 177 ASP ASP A . n 
A 1 199 LEU 199 178 178 LEU LEU A . n 
A 1 200 LYS 200 179 179 LYS LYS A . n 
A 1 201 ASP 201 180 180 ASP ASP A . n 
A 1 202 MET 202 181 181 MET MET A . n 
A 1 203 SER 203 182 182 SER SER A . n 
A 1 204 GLN 204 183 183 GLN GLN A . n 
A 1 205 MET 205 184 184 MET MET A . n 
A 1 206 ILE 206 185 185 ILE ILE A . n 
A 1 207 LEU 207 186 186 LEU LEU A . n 
A 1 208 ARG 208 187 187 ARG ARG A . n 
A 1 209 THR 209 188 188 THR THR A . n 
A 1 210 LYS 210 189 189 LYS LYS A . n 
A 1 211 GLY 211 190 190 GLY GLY A . n 
A 1 212 PRO 212 191 191 PRO PRO A . n 
A 1 213 ASP 213 192 192 ASP ASP A . n 
A 1 214 ARG 214 193 193 ARG ARG A . n 
A 1 215 LEU 215 194 194 LEU LEU A . n 
A 1 216 PRO 216 195 195 PRO PRO A . n 
A 1 217 ALA 217 196 196 ALA ALA A . n 
A 1 218 GLY 218 197 197 GLY GLY A . n 
A 1 219 TYR 219 198 198 TYR TYR A . n 
A 1 220 GLU 220 199 199 GLU GLU A . n 
A 1 221 ILE 221 200 200 ILE ILE A . n 
A 1 222 VAL 222 201 201 VAL VAL A . n 
A 1 223 LEU 223 202 202 LEU LEU A . n 
A 1 224 TYR 224 203 203 TYR TYR A . n 
A 1 225 ILE 225 204 204 ILE ILE A . n 
A 1 226 SER 226 205 205 SER SER A . n 
A 1 227 MET 227 206 206 MET MET A . n 
A 1 228 SER 228 207 207 SER SER A . n 
A 1 229 ASP 229 208 208 ASP ASP A . n 
A 1 230 SER 230 209 209 SER SER A . n 
A 1 231 ASP 231 210 210 ASP ASP A . n 
A 1 232 LYS 232 211 211 LYS LYS A . n 
A 1 233 VAL 233 212 212 VAL VAL A . n 
A 1 234 GLY 234 213 213 GLY GLY A . n 
A 1 235 VAL 235 214 214 VAL VAL A . n 
A 1 236 PHE 236 215 215 PHE PHE A . n 
A 1 237 TYR 237 216 216 TYR TYR A . n 
A 1 238 VAL 238 217 217 VAL VAL A . n 
A 1 239 GLU 239 218 218 GLU GLU A . n 
A 1 240 ASN 240 219 219 ASN ASN A . n 
A 1 241 PRO 241 220 220 PRO PRO A . n 
A 1 242 PHE 242 221 221 PHE PHE A . n 
A 1 243 PHE 243 222 222 PHE PHE A . n 
A 1 244 GLY 244 223 223 GLY GLY A . n 
A 1 245 GLN 245 224 224 GLN GLN A . n 
A 1 246 ARG 246 225 225 ARG ARG A . n 
A 1 247 TYR 247 226 226 TYR TYR A . n 
A 1 248 ILE 248 227 227 ILE ILE A . n 
A 1 249 HIS 249 228 228 HIS HIS A . n 
A 1 250 ILE 250 229 229 ILE ILE A . n 
A 1 251 LEU 251 230 230 LEU LEU A . n 
A 1 252 GLY 252 231 231 GLY GLY A . n 
A 1 253 ARG 253 232 232 ARG ARG A . n 
A 1 254 ARG 254 233 233 ARG ARG A . n 
A 1 255 LYS 255 234 234 LYS LYS A . n 
A 1 256 LEU 256 235 235 LEU LEU A . n 
A 1 257 TYR 257 236 236 TYR TYR A . n 
A 1 258 HIS 258 237 237 HIS HIS A . n 
A 1 259 VAL 259 238 238 VAL VAL A . n 
A 1 260 VAL 260 239 239 VAL VAL A . n 
A 1 261 LYS 261 240 240 LYS LYS A . n 
A 1 262 TYR 262 241 241 TYR TYR A . n 
A 1 263 THR 263 242 242 THR THR A . n 
A 1 264 GLY 264 243 243 GLY GLY A . n 
A 1 265 GLY 265 244 244 GLY GLY A . n 
A 1 266 SER 266 245 245 SER SER A . n 
A 1 267 ALA 267 246 246 ALA ALA A . n 
A 1 268 GLU 268 247 247 GLU GLU A . n 
A 1 269 LEU 269 248 248 LEU LEU A . n 
A 1 270 LEU 270 249 249 LEU LEU A . n 
A 1 271 PHE 271 250 250 PHE PHE A . n 
A 1 272 PHE 272 251 251 PHE PHE A . n 
A 1 273 VAL 273 252 252 VAL VAL A . n 
A 1 274 GLU 274 253 253 GLU GLU A . n 
A 1 275 GLY 275 254 254 GLY GLY A . n 
A 1 276 LEU 276 255 255 LEU LEU A . n 
A 1 277 CYS 277 256 256 CYS CYS A . n 
A 1 278 PHE 278 257 257 PHE PHE A . n 
A 1 279 PRO 279 258 258 PRO PRO A . n 
A 1 280 ASP 280 259 259 ASP ASP A . n 
A 1 281 GLU 281 260 260 GLU GLU A . n 
A 1 282 GLY 282 261 261 GLY GLY A . n 
A 1 283 PHE 283 262 262 PHE PHE A . n 
A 1 284 SER 284 263 263 SER SER A . n 
A 1 285 GLY 285 264 264 GLY GLY A . n 
A 1 286 LEU 286 265 265 LEU LEU A . n 
A 1 287 VAL 287 266 266 VAL VAL A . n 
A 1 288 SER 288 267 267 SER SER A . n 
A 1 289 ILE 289 268 268 ILE ILE A . n 
A 1 290 HIS 290 269 269 HIS HIS A . n 
A 1 291 VAL 291 270 270 VAL VAL A . n 
A 1 292 SER 292 271 271 SER SER A . n 
A 1 293 LEU 293 272 272 LEU LEU A . n 
A 1 294 LEU 294 273 273 LEU LEU A . n 
A 1 295 GLU 295 274 274 GLU GLU A . n 
A 1 296 TYR 296 275 275 TYR TYR A . n 
A 1 297 MET 297 276 276 MET MET A . n 
A 1 298 ALA 298 277 277 ALA ALA A . n 
A 1 299 GLN 299 278 278 GLN GLN A . n 
A 1 300 ASP 300 279 279 ASP ASP A . n 
A 1 301 ILE 301 280 280 ILE ILE A . n 
A 1 302 PRO 302 281 281 PRO PRO A . n 
A 1 303 LEU 303 282 282 LEU LEU A . n 
A 1 304 THR 304 283 283 THR THR A . n 
A 1 305 PRO 305 284 284 PRO PRO A . n 
A 1 306 ILE 306 285 285 ILE ILE A . n 
A 1 307 PHE 307 286 286 PHE PHE A . n 
A 1 308 THR 308 287 287 THR THR A . n 
A 1 309 ASP 309 288 288 ASP ASP A . n 
A 1 310 THR 310 289 289 THR THR A . n 
A 1 311 VAL 311 290 290 VAL VAL A . n 
A 1 312 ILE 312 291 291 ILE ILE A . n 
A 1 313 PHE 313 292 292 PHE PHE A . n 
A 1 314 ARG 314 293 293 ARG ARG A . n 
A 1 315 ILE 315 294 294 ILE ILE A . n 
A 1 316 ALA 316 295 295 ALA ALA A . n 
A 1 317 PRO 317 296 296 PRO PRO A . n 
A 1 318 TRP 318 297 297 TRP TRP A . n 
A 1 319 ILE 319 298 298 ILE ILE A . n 
A 1 320 MET 320 299 299 MET MET A . n 
A 1 321 THR 321 300 300 THR THR A . n 
A 1 322 PRO 322 301 301 PRO PRO A . n 
A 1 323 ASN 323 302 302 ASN ASN A . n 
A 1 324 ILE 324 303 303 ILE ILE A . n 
A 1 325 LEU 325 304 304 LEU LEU A . n 
A 1 326 PRO 326 305 305 PRO PRO A . n 
A 1 327 PRO 327 306 306 PRO PRO A . n 
A 1 328 VAL 328 307 307 VAL VAL A . n 
A 1 329 SER 329 308 308 SER SER A . n 
A 1 330 VAL 330 309 309 VAL VAL A . n 
A 1 331 PHE 331 310 310 PHE PHE A . n 
A 1 332 VAL 332 311 311 VAL VAL A . n 
A 1 333 CYS 333 312 312 CYS CYS A . n 
A 1 334 CYS 334 313 313 CYS CYS A . n 
A 1 335 MET 335 314 314 MET MET A . n 
A 1 336 LYS 336 315 315 LYS LYS A . n 
A 1 337 ASP 337 316 316 ASP ASP A . n 
A 1 338 ASN 338 317 317 ASN ASN A . n 
A 1 339 TYR 339 318 318 TYR TYR A . n 
A 1 340 LEU 340 319 319 LEU LEU A . n 
A 1 341 PHE 341 320 320 PHE PHE A . n 
A 1 342 LEU 342 321 321 LEU LEU A . n 
A 1 343 LYS 343 322 322 LYS LYS A . n 
A 1 344 GLU 344 323 323 GLU GLU A . n 
A 1 345 VAL 345 324 324 VAL VAL A . n 
A 1 346 LYS 346 325 325 LYS LYS A . n 
A 1 347 ASN 347 326 326 ASN ASN A . n 
A 1 348 LEU 348 327 327 LEU LEU A . n 
A 1 349 VAL 349 328 328 VAL VAL A . n 
A 1 350 GLU 350 329 329 GLU GLU A . n 
A 1 351 LYS 351 330 330 LYS LYS A . n 
A 1 352 THR 352 331 331 THR THR A . n 
A 1 353 ASN 353 332 332 ASN ASN A . n 
A 1 354 CYS 354 333 333 CYS CYS A . n 
A 1 355 GLU 355 334 334 GLU GLU A . n 
A 1 356 LEU 356 335 335 LEU LEU A . n 
A 1 357 LYS 357 336 336 LYS LYS A . n 
A 1 358 VAL 358 337 337 VAL VAL A . n 
A 1 359 CYS 359 338 338 CYS CYS A . n 
A 1 360 PHE 360 339 339 PHE PHE A . n 
A 1 361 GLN 361 340 ?   ?   ?   A . n 
A 1 362 TYR 362 341 ?   ?   ?   A . n 
A 1 363 LEU 363 342 ?   ?   ?   A . n 
A 1 364 ASN 364 343 ?   ?   ?   A . n 
A 1 365 ARG 365 344 ?   ?   ?   A . n 
A 1 366 GLY 366 345 ?   ?   ?   A . n 
A 1 367 ASP 367 346 346 ASP ASP A . n 
A 1 368 ARG 368 347 347 ARG ARG A . n 
A 1 369 TRP 369 348 348 TRP TRP A . n 
A 1 370 ILE 370 349 349 ILE ILE A . n 
A 1 371 GLN 371 350 350 GLN GLN A . n 
A 1 372 ASP 372 351 351 ASP ASP A . n 
A 1 373 GLU 373 352 352 GLU GLU A . n 
A 1 374 ILE 374 353 353 ILE ILE A . n 
A 1 375 GLU 375 354 354 GLU GLU A . n 
A 1 376 PHE 376 355 355 PHE PHE A . n 
A 1 377 GLY 377 356 356 GLY GLY A . n 
A 1 378 TYR 378 357 357 TYR TYR A . n 
A 1 379 ILE 379 358 358 ILE ILE A . n 
A 1 380 GLU 380 359 359 GLU GLU A . n 
A 1 381 ALA 381 360 360 ALA ALA A . n 
A 1 382 PRO 382 361 361 PRO PRO A . n 
A 1 383 HIS 383 362 362 HIS HIS A . n 
A 1 384 LYS 384 363 363 LYS LYS A . n 
A 1 385 GLY 385 364 364 GLY GLY A . n 
A 1 386 PHE 386 365 365 PHE PHE A . n 
A 1 387 PRO 387 366 366 PRO PRO A . n 
A 1 388 VAL 388 367 367 VAL VAL A . n 
A 1 389 VAL 389 368 368 VAL VAL A . n 
A 1 390 LEU 390 369 369 LEU LEU A . n 
A 1 391 ASP 391 370 370 ASP ASP A . n 
A 1 392 SER 392 371 371 SER SER A . n 
A 1 393 PRO 393 372 372 PRO PRO A . n 
A 1 394 ARG 394 373 373 ARG ARG A . n 
A 1 395 ASP 395 374 ?   ?   ?   A . n 
A 1 396 GLY 396 375 ?   ?   ?   A . n 
A 1 397 ASN 397 376 ?   ?   ?   A . n 
A 1 398 LEU 398 377 ?   ?   ?   A . n 
A 1 399 LYS 399 378 ?   ?   ?   A . n 
A 1 400 ASP 400 379 ?   ?   ?   A . n 
A 1 401 PHE 401 380 380 PHE PHE A . n 
A 1 402 PRO 402 381 381 PRO PRO A . n 
A 1 403 VAL 403 382 382 VAL VAL A . n 
A 1 404 LYS 404 383 383 LYS LYS A . n 
A 1 405 GLU 405 384 384 GLU GLU A . n 
A 1 406 LEU 406 385 385 LEU LEU A . n 
A 1 407 LEU 407 386 386 LEU LEU A . n 
A 1 408 GLY 408 387 387 GLY GLY A . n 
A 1 409 PRO 409 388 388 PRO PRO A . n 
A 1 410 ASP 410 389 389 ASP ASP A . n 
A 1 411 PHE 411 390 390 PHE PHE A . n 
A 1 412 GLY 412 391 391 GLY GLY A . n 
A 1 413 TYR 413 392 392 TYR TYR A . n 
A 1 414 VAL 414 393 393 VAL VAL A . n 
A 1 415 THR 415 394 394 THR THR A . n 
A 1 416 ARG 416 395 395 ARG ARG A . n 
A 1 417 GLU 417 396 396 GLU GLU A . n 
A 1 418 PRO 418 397 397 PRO PRO A . n 
A 1 419 LEU 419 398 398 LEU LEU A . n 
A 1 420 PHE 420 399 ?   ?   ?   A . n 
A 1 421 GLU 421 400 ?   ?   ?   A . n 
A 1 422 SER 422 401 ?   ?   ?   A . n 
A 1 423 VAL 423 402 402 VAL VAL A . n 
A 1 424 THR 424 403 403 THR THR A . n 
A 1 425 SER 425 404 404 SER SER A . n 
A 1 426 LEU 426 405 405 LEU LEU A . n 
A 1 427 ASP 427 406 406 ASP ASP A . n 
A 1 428 SER 428 407 407 SER SER A . n 
A 1 429 PHE 429 408 408 PHE PHE A . n 
A 1 430 GLY 430 409 409 GLY GLY A . n 
A 1 431 ASN 431 410 410 ASN ASN A . n 
A 1 432 LEU 432 411 411 LEU LEU A . n 
A 1 433 GLU 433 412 412 GLU GLU A . n 
A 1 434 VAL 434 413 413 VAL VAL A . n 
A 1 435 SER 435 414 414 SER SER A . n 
A 1 436 PRO 436 415 415 PRO PRO A . n 
A 1 437 PRO 437 416 416 PRO PRO A . n 
A 1 438 VAL 438 417 417 VAL VAL A . n 
A 1 439 THR 439 418 418 THR THR A . n 
A 1 440 VAL 440 419 419 VAL VAL A . n 
A 1 441 ASN 441 420 420 ASN ASN A . n 
A 1 442 GLY 442 421 421 GLY GLY A . n 
A 1 443 LYS 443 422 422 LYS LYS A . n 
A 1 444 THR 444 423 423 THR THR A . n 
A 1 445 TYR 445 424 424 TYR TYR A . n 
A 1 446 PRO 446 425 425 PRO PRO A . n 
A 1 447 LEU 447 426 426 LEU LEU A . n 
A 1 448 GLY 448 427 427 GLY GLY A . n 
A 1 449 ARG 449 428 428 ARG ARG A . n 
A 1 450 ILE 450 429 429 ILE ILE A . n 
A 1 451 LEU 451 430 430 LEU LEU A . n 
A 1 452 ILE 452 431 431 ILE ILE A . n 
A 1 453 GLY 453 432 432 GLY GLY A . n 
A 1 454 SER 454 433 433 SER SER A . n 
A 1 455 SER 455 434 434 SER SER A . n 
A 1 456 PHE 456 435 435 PHE PHE A . n 
A 1 457 PRO 457 436 436 PRO PRO A . n 
A 1 458 LEU 458 437 437 LEU LEU A . n 
A 1 459 SER 459 438 438 SER SER A . n 
A 1 460 GLY 460 439 439 GLY GLY A . n 
A 1 461 GLY 461 440 440 GLY GLY A . n 
A 1 462 ARG 462 441 441 ARG ARG A . n 
A 1 463 ARG 463 442 442 ARG ARG A . n 
A 1 464 MET 464 443 443 MET MET A . n 
A 1 465 THR 465 444 444 THR THR A . n 
A 1 466 LYS 466 445 445 LYS LYS A . n 
A 1 467 VAL 467 446 446 VAL VAL A . n 
A 1 468 VAL 468 447 447 VAL VAL A . n 
A 1 469 ARG 469 448 448 ARG ARG A . n 
A 1 470 ASP 470 449 449 ASP ASP A . n 
A 1 471 PHE 471 450 450 PHE PHE A . n 
A 1 472 LEU 472 451 451 LEU LEU A . n 
A 1 473 LYS 473 452 452 LYS LYS A . n 
A 1 474 ALA 474 453 453 ALA ALA A . n 
A 1 475 GLN 475 454 454 GLN GLN A . n 
A 1 476 GLN 476 455 455 GLN GLN A . n 
A 1 477 VAL 477 456 456 VAL VAL A . n 
A 1 478 GLN 478 457 457 GLN GLN A . n 
A 1 479 ALA 479 458 458 ALA ALA A . n 
A 1 480 PRO 480 459 459 PRO PRO A . n 
A 1 481 VAL 481 460 460 VAL VAL A . n 
A 1 482 GLU 482 461 461 GLU GLU A . n 
A 1 483 LEU 483 462 462 LEU LEU A . n 
A 1 484 TYR 484 463 463 TYR TYR A . n 
A 1 485 SER 485 464 464 SER SER A . n 
A 1 486 ASP 486 465 465 ASP ASP A . n 
A 1 487 TRP 487 466 466 TRP TRP A . n 
A 1 488 LEU 488 467 467 LEU LEU A . n 
A 1 489 THR 489 468 468 THR THR A . n 
A 1 490 VAL 490 469 469 VAL VAL A . n 
A 1 491 GLY 491 470 470 GLY GLY A . n 
A 1 492 HIS 492 471 471 HIS HIS A . n 
A 1 493 VAL 493 472 472 VAL VAL A . n 
A 1 494 ASP 494 473 473 ASP ASP A . n 
A 1 495 GLU 495 474 474 GLU GLU A . n 
A 1 496 PHE 496 475 475 PHE PHE A . n 
A 1 497 MET 497 476 476 MET MET A . n 
A 1 498 SER 498 477 477 SER SER A . n 
A 1 499 PHE 499 478 478 PHE PHE A . n 
A 1 500 VAL 500 479 479 VAL VAL A . n 
A 1 501 PRO 501 480 480 PRO PRO A . n 
A 1 502 ILE 502 481 481 ILE ILE A . n 
A 1 503 PRO 503 482 482 PRO PRO A . n 
A 1 504 GLY 504 483 483 GLY GLY A . n 
A 1 505 THR 505 484 484 THR THR A . n 
A 1 506 LYS 506 485 485 LYS LYS A . n 
A 1 507 LYS 507 486 486 LYS LYS A . n 
A 1 508 PHE 508 487 487 PHE PHE A . n 
A 1 509 LEU 509 488 488 LEU LEU A . n 
A 1 510 LEU 510 489 489 LEU LEU A . n 
A 1 511 LEU 511 490 490 LEU LEU A . n 
A 1 512 MET 512 491 491 MET MET A . n 
A 1 513 ALA 513 492 492 ALA ALA A . n 
A 1 514 SER 514 493 493 SER SER A . n 
A 1 515 THR 515 494 494 THR THR A . n 
A 1 516 SER 516 495 495 SER SER A . n 
A 1 517 ALA 517 496 496 ALA ALA A . n 
A 1 518 CYS 518 497 497 CYS CYS A . n 
A 1 519 TYR 519 498 498 TYR TYR A . n 
A 1 520 LYS 520 499 499 LYS LYS A . n 
A 1 521 LEU 521 500 500 LEU LEU A . n 
A 1 522 PHE 522 501 501 PHE PHE A . n 
A 1 523 ARG 523 502 502 ARG ARG A . n 
A 1 524 GLU 524 503 503 GLU GLU A . n 
A 1 525 LYS 525 504 504 LYS LYS A . n 
A 1 526 GLN 526 505 505 GLN GLN A . n 
A 1 527 LYS 527 506 506 LYS LYS A . n 
A 1 528 ASP 528 507 507 ASP ASP A . n 
A 1 529 GLY 529 508 508 GLY GLY A . n 
A 1 530 HIS 530 509 509 HIS HIS A . n 
A 1 531 GLY 531 510 510 GLY GLY A . n 
A 1 532 GLU 532 511 511 GLU GLU A . n 
A 1 533 ALA 533 512 512 ALA ALA A . n 
A 1 534 ILE 534 513 513 ILE ILE A . n 
A 1 535 MET 535 514 514 MET MET A . n 
A 1 536 PHE 536 515 515 PHE PHE A . n 
A 1 537 LYS 537 516 516 LYS LYS A . n 
A 1 538 GLY 538 517 517 GLY GLY A . n 
A 1 539 LEU 539 518 518 LEU LEU A . n 
A 1 540 GLY 540 519 519 GLY GLY A . n 
A 1 541 GLY 541 520 520 GLY GLY A . n 
A 1 542 MET 542 521 521 MET MET A . n 
A 1 543 SER 543 522 ?   ?   ?   A . n 
A 1 544 SER 544 523 ?   ?   ?   A . n 
A 1 545 LYS 545 524 524 LYS LYS A . n 
A 1 546 ARG 546 525 525 ARG ARG A . n 
A 1 547 ILE 547 526 526 ILE ILE A . n 
A 1 548 THR 548 527 527 THR THR A . n 
A 1 549 ILE 549 528 528 ILE ILE A . n 
A 1 550 ASN 550 529 529 ASN ASN A . n 
A 1 551 LYS 551 530 530 LYS LYS A . n 
A 1 552 ILE 552 531 531 ILE ILE A . n 
A 1 553 LEU 553 532 532 LEU LEU A . n 
A 1 554 SER 554 533 533 SER SER A . n 
A 1 555 ASN 555 534 534 ASN ASN A . n 
A 1 556 GLU 556 535 535 GLU GLU A . n 
A 1 557 SER 557 536 536 SER SER A . n 
A 1 558 LEU 558 537 537 LEU LEU A . n 
A 1 559 VAL 559 538 538 VAL VAL A . n 
A 1 560 GLN 560 539 539 GLN GLN A . n 
A 1 561 GLU 561 540 540 GLU GLU A . n 
A 1 562 ASN 562 541 541 ASN ASN A . n 
A 1 563 LEU 563 542 542 LEU LEU A . n 
A 1 564 TYR 564 543 543 TYR TYR A . n 
A 1 565 PHE 565 544 544 PHE PHE A . n 
A 1 566 GLN 566 545 545 GLN GLN A . n 
A 1 567 ARG 567 546 546 ARG ARG A . n 
A 1 568 CYS 568 547 547 CYS CYS A . n 
A 1 569 LEU 569 548 548 LEU LEU A . n 
A 1 570 ASP 570 549 549 ASP ASP A . n 
A 1 571 TRP 571 550 550 TRP TRP A . n 
A 1 572 ASN 572 551 551 ASN ASN A . n 
A 1 573 ARG 573 552 552 ARG ARG A . n 
A 1 574 ASP 574 553 553 ASP ASP A . n 
A 1 575 ILE 575 554 554 ILE ILE A . n 
A 1 576 LEU 576 555 555 LEU LEU A . n 
A 1 577 LYS 577 556 556 LYS LYS A . n 
A 1 578 LYS 578 557 557 LYS LYS A . n 
A 1 579 GLU 579 558 558 GLU GLU A . n 
A 1 580 LEU 580 559 559 LEU LEU A . n 
A 1 581 GLY 581 560 560 GLY GLY A . n 
A 1 582 LEU 582 561 561 LEU LEU A . n 
A 1 583 THR 583 562 562 THR THR A . n 
A 1 584 GLU 584 563 563 GLU GLU A . n 
A 1 585 GLN 585 564 564 GLN GLN A . n 
A 1 586 ASP 586 565 565 ASP ASP A . n 
A 1 587 ILE 587 566 566 ILE ILE A . n 
A 1 588 ILE 588 567 567 ILE ILE A . n 
A 1 589 ASP 589 568 568 ASP ASP A . n 
A 1 590 LEU 590 569 569 LEU LEU A . n 
A 1 591 PRO 591 570 570 PRO PRO A . n 
A 1 592 ALA 592 571 571 ALA ALA A . n 
A 1 593 LEU 593 572 572 LEU LEU A . n 
A 1 594 PHE 594 573 573 PHE PHE A . n 
A 1 595 LYS 595 574 574 LYS LYS A . n 
A 1 596 MET 596 575 575 MET MET A . n 
A 1 597 ASP 597 576 576 ASP ASP A . n 
A 1 598 GLU 598 577 577 GLU GLU A . n 
A 1 599 ASP 599 578 578 ASP ASP A . n 
A 1 600 HIS 600 579 579 HIS HIS A . n 
A 1 601 ARG 601 580 580 ARG ARG A . n 
A 1 602 ALA 602 581 581 ALA ALA A . n 
A 1 603 ARG 603 582 582 ARG ARG A . n 
A 1 604 ALA 604 583 583 ALA ALA A . n 
A 1 605 PHE 605 584 584 PHE PHE A . n 
A 1 606 PHE 606 585 585 PHE PHE A . n 
A 1 607 PRO 607 586 586 PRO PRO A . n 
A 1 608 ASN 608 587 587 ASN ASN A . n 
A 1 609 MET 609 588 588 MET MET A . n 
A 1 610 VAL 610 589 589 VAL VAL A . n 
A 1 611 ASN 611 590 590 ASN ASN A . n 
A 1 612 MET 612 591 591 MET MET A . n 
A 1 613 ILE 613 592 592 ILE ILE A . n 
A 1 614 VAL 614 593 593 VAL VAL A . n 
A 1 615 LEU 615 594 594 LEU LEU A . n 
A 1 616 ASP 616 595 595 ASP ASP A . n 
A 1 617 LYS 617 596 596 LYS LYS A . n 
A 1 618 ASP 618 597 597 ASP ASP A . n 
A 1 619 LEU 619 598 598 LEU LEU A . n 
A 1 620 GLY 620 599 599 GLY GLY A . n 
A 1 621 ILE 621 600 600 ILE ILE A . n 
A 1 622 PRO 622 601 601 PRO PRO A . n 
A 1 623 LYS 623 602 602 LYS LYS A . n 
A 1 624 PRO 624 603 603 PRO PRO A . n 
A 1 625 PHE 625 604 604 PHE PHE A . n 
A 1 626 GLY 626 605 605 GLY GLY A . n 
A 1 627 PRO 627 606 606 PRO PRO A . n 
A 1 628 GLN 628 607 607 GLN GLN A . n 
A 1 629 VAL 629 608 608 VAL VAL A . n 
A 1 630 GLU 630 609 609 GLU GLU A . n 
A 1 631 GLU 631 610 610 GLU GLU A . n 
A 1 632 GLU 632 611 611 GLU GLU A . n 
A 1 633 CYS 633 612 612 CYS CYS A . n 
A 1 634 CYS 634 613 613 CYS CYS A . n 
A 1 635 LEU 635 614 614 LEU LEU A . n 
A 1 636 GLU 636 615 615 GLU GLU A . n 
A 1 637 MET 637 616 616 MET MET A . n 
A 1 638 HIS 638 617 617 HIS HIS A . n 
A 1 639 VAL 639 618 618 VAL VAL A . n 
A 1 640 ARG 640 619 619 ARG ARG A . n 
A 1 641 GLY 641 620 620 GLY GLY A . n 
A 1 642 LEU 642 621 621 LEU LEU A . n 
A 1 643 LEU 643 622 622 LEU LEU A . n 
A 1 644 GLU 644 623 623 GLU GLU A . n 
A 1 645 PRO 645 624 624 PRO PRO A . n 
A 1 646 LEU 646 625 625 LEU LEU A . n 
A 1 647 GLY 647 626 626 GLY GLY A . n 
A 1 648 LEU 648 627 627 LEU LEU A . n 
A 1 649 GLU 649 628 628 GLU GLU A . n 
A 1 650 CYS 650 629 629 CYS CYS A . n 
A 1 651 THR 651 630 630 THR THR A . n 
A 1 652 PHE 652 631 631 PHE PHE A . n 
A 1 653 ILE 653 632 632 ILE ILE A . n 
A 1 654 ASP 654 633 633 ASP ASP A . n 
A 1 655 ASP 655 634 634 ASP ASP A . n 
A 1 656 ILE 656 635 635 ILE ILE A . n 
A 1 657 SER 657 636 636 SER SER A . n 
A 1 658 ALA 658 637 637 ALA ALA A . n 
A 1 659 TYR 659 638 638 TYR TYR A . n 
A 1 660 HIS 660 639 639 HIS HIS A . n 
A 1 661 LYS 661 640 640 LYS LYS A . n 
A 1 662 PHE 662 641 641 PHE PHE A . n 
A 1 663 LEU 663 642 642 LEU LEU A . n 
A 1 664 GLY 664 643 643 GLY GLY A . n 
A 1 665 GLU 665 644 644 GLU GLU A . n 
A 1 666 VAL 666 645 645 VAL VAL A . n 
A 1 667 HIS 667 646 646 HIS HIS A . n 
A 1 668 CYS 668 647 647 CYS CYS A . n 
A 1 669 GLY 669 648 648 GLY GLY A . n 
A 1 670 THR 670 649 649 THR THR A . n 
A 1 671 ASN 671 650 650 ASN ASN A . n 
A 1 672 VAL 672 651 651 VAL VAL A . n 
A 1 673 ARG 673 652 652 ARG ARG A . n 
A 1 674 ARG 674 653 653 ARG ARG A . n 
A 1 675 LYS 675 654 654 LYS LYS A . n 
A 1 676 PRO 676 655 655 PRO PRO A . n 
A 1 677 PHE 677 656 656 PHE PHE A . n 
A 1 678 THR 678 657 657 THR THR A . n 
A 1 679 PHE 679 658 658 PHE PHE A . n 
A 1 680 LYS 680 659 659 LYS LYS A . n 
A 1 681 TRP 681 660 660 TRP TRP A . n 
A 1 682 TRP 682 661 661 TRP TRP A . n 
A 1 683 HIS 683 662 662 HIS HIS A . n 
A 1 684 MET 684 663 663 MET MET A . n 
A 1 685 VAL 685 664 664 VAL VAL A . n 
A 1 686 PRO 686 665 665 PRO PRO A . n 
A 1 687 SER 687 666 666 SER SER A . n 
A 1 688 ARG 688 667 667 ARG ARG A . n 
A 1 689 ARG 689 668 ?   ?   ?   A . n 
A 1 690 SER 690 669 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A8O 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A8O 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CA    1   701  704  CA    CA  A . 
C 2 CA    1   702  703  CA    CA  A . 
D 2 CA    1   703  705  CA    CA  A . 
E 2 CA    1   704  706  CA    CA  A . 
F 3 A1A8O 1   705  4000 A1A8O PFE A . 
G 4 HOH   1   801  439  HOH   HOH A . 
G 4 HOH   2   802  345  HOH   HOH A . 
G 4 HOH   3   803  346  HOH   HOH A . 
G 4 HOH   4   804  448  HOH   HOH A . 
G 4 HOH   5   805  39   HOH   HOH A . 
G 4 HOH   6   806  309  HOH   HOH A . 
G 4 HOH   7   807  173  HOH   HOH A . 
G 4 HOH   8   808  402  HOH   HOH A . 
G 4 HOH   9   809  74   HOH   HOH A . 
G 4 HOH   10  810  496  HOH   HOH A . 
G 4 HOH   11  811  487  HOH   HOH A . 
G 4 HOH   12  812  59   HOH   HOH A . 
G 4 HOH   13  813  438  HOH   HOH A . 
G 4 HOH   14  814  133  HOH   HOH A . 
G 4 HOH   15  815  235  HOH   HOH A . 
G 4 HOH   16  816  40   HOH   HOH A . 
G 4 HOH   17  817  302  HOH   HOH A . 
G 4 HOH   18  818  386  HOH   HOH A . 
G 4 HOH   19  819  121  HOH   HOH A . 
G 4 HOH   20  820  108  HOH   HOH A . 
G 4 HOH   21  821  126  HOH   HOH A . 
G 4 HOH   22  822  319  HOH   HOH A . 
G 4 HOH   23  823  318  HOH   HOH A . 
G 4 HOH   24  824  393  HOH   HOH A . 
G 4 HOH   25  825  290  HOH   HOH A . 
G 4 HOH   26  826  4    HOH   HOH A . 
G 4 HOH   27  827  244  HOH   HOH A . 
G 4 HOH   28  828  243  HOH   HOH A . 
G 4 HOH   29  829  220  HOH   HOH A . 
G 4 HOH   30  830  372  HOH   HOH A . 
G 4 HOH   31  831  15   HOH   HOH A . 
G 4 HOH   32  832  251  HOH   HOH A . 
G 4 HOH   33  833  410  HOH   HOH A . 
G 4 HOH   34  834  52   HOH   HOH A . 
G 4 HOH   35  835  106  HOH   HOH A . 
G 4 HOH   36  836  90   HOH   HOH A . 
G 4 HOH   37  837  481  HOH   HOH A . 
G 4 HOH   38  838  13   HOH   HOH A . 
G 4 HOH   39  839  500  HOH   HOH A . 
G 4 HOH   40  840  105  HOH   HOH A . 
G 4 HOH   41  841  28   HOH   HOH A . 
G 4 HOH   42  842  473  HOH   HOH A . 
G 4 HOH   43  843  210  HOH   HOH A . 
G 4 HOH   44  844  85   HOH   HOH A . 
G 4 HOH   45  845  96   HOH   HOH A . 
G 4 HOH   46  846  179  HOH   HOH A . 
G 4 HOH   47  847  110  HOH   HOH A . 
G 4 HOH   48  848  117  HOH   HOH A . 
G 4 HOH   49  849  1    HOH   HOH A . 
G 4 HOH   50  850  109  HOH   HOH A . 
G 4 HOH   51  851  310  HOH   HOH A . 
G 4 HOH   52  852  349  HOH   HOH A . 
G 4 HOH   53  853  161  HOH   HOH A . 
G 4 HOH   54  854  204  HOH   HOH A . 
G 4 HOH   55  855  494  HOH   HOH A . 
G 4 HOH   56  856  435  HOH   HOH A . 
G 4 HOH   57  857  75   HOH   HOH A . 
G 4 HOH   58  858  307  HOH   HOH A . 
G 4 HOH   59  859  55   HOH   HOH A . 
G 4 HOH   60  860  285  HOH   HOH A . 
G 4 HOH   61  861  414  HOH   HOH A . 
G 4 HOH   62  862  120  HOH   HOH A . 
G 4 HOH   63  863  459  HOH   HOH A . 
G 4 HOH   64  864  353  HOH   HOH A . 
G 4 HOH   65  865  18   HOH   HOH A . 
G 4 HOH   66  866  65   HOH   HOH A . 
G 4 HOH   67  867  88   HOH   HOH A . 
G 4 HOH   68  868  22   HOH   HOH A . 
G 4 HOH   69  869  425  HOH   HOH A . 
G 4 HOH   70  870  338  HOH   HOH A . 
G 4 HOH   71  871  7    HOH   HOH A . 
G 4 HOH   72  872  206  HOH   HOH A . 
G 4 HOH   73  873  182  HOH   HOH A . 
G 4 HOH   74  874  240  HOH   HOH A . 
G 4 HOH   75  875  170  HOH   HOH A . 
G 4 HOH   76  876  111  HOH   HOH A . 
G 4 HOH   77  877  60   HOH   HOH A . 
G 4 HOH   78  878  390  HOH   HOH A . 
G 4 HOH   79  879  116  HOH   HOH A . 
G 4 HOH   80  880  298  HOH   HOH A . 
G 4 HOH   81  881  131  HOH   HOH A . 
G 4 HOH   82  882  27   HOH   HOH A . 
G 4 HOH   83  883  9    HOH   HOH A . 
G 4 HOH   84  884  314  HOH   HOH A . 
G 4 HOH   85  885  485  HOH   HOH A . 
G 4 HOH   86  886  492  HOH   HOH A . 
G 4 HOH   87  887  348  HOH   HOH A . 
G 4 HOH   88  888  67   HOH   HOH A . 
G 4 HOH   89  889  479  HOH   HOH A . 
G 4 HOH   90  890  37   HOH   HOH A . 
G 4 HOH   91  891  93   HOH   HOH A . 
G 4 HOH   92  892  241  HOH   HOH A . 
G 4 HOH   93  893  486  HOH   HOH A . 
G 4 HOH   94  894  160  HOH   HOH A . 
G 4 HOH   95  895  38   HOH   HOH A . 
G 4 HOH   96  896  242  HOH   HOH A . 
G 4 HOH   97  897  403  HOH   HOH A . 
G 4 HOH   98  898  124  HOH   HOH A . 
G 4 HOH   99  899  31   HOH   HOH A . 
G 4 HOH   100 900  339  HOH   HOH A . 
G 4 HOH   101 901  454  HOH   HOH A . 
G 4 HOH   102 902  107  HOH   HOH A . 
G 4 HOH   103 903  113  HOH   HOH A . 
G 4 HOH   104 904  3    HOH   HOH A . 
G 4 HOH   105 905  187  HOH   HOH A . 
G 4 HOH   106 906  321  HOH   HOH A . 
G 4 HOH   107 907  342  HOH   HOH A . 
G 4 HOH   108 908  17   HOH   HOH A . 
G 4 HOH   109 909  223  HOH   HOH A . 
G 4 HOH   110 910  475  HOH   HOH A . 
G 4 HOH   111 911  46   HOH   HOH A . 
G 4 HOH   112 912  324  HOH   HOH A . 
G 4 HOH   113 913  199  HOH   HOH A . 
G 4 HOH   114 914  248  HOH   HOH A . 
G 4 HOH   115 915  69   HOH   HOH A . 
G 4 HOH   116 916  226  HOH   HOH A . 
G 4 HOH   117 917  397  HOH   HOH A . 
G 4 HOH   118 918  373  HOH   HOH A . 
G 4 HOH   119 919  201  HOH   HOH A . 
G 4 HOH   120 920  216  HOH   HOH A . 
G 4 HOH   121 921  444  HOH   HOH A . 
G 4 HOH   122 922  118  HOH   HOH A . 
G 4 HOH   123 923  11   HOH   HOH A . 
G 4 HOH   124 924  207  HOH   HOH A . 
G 4 HOH   125 925  203  HOH   HOH A . 
G 4 HOH   126 926  144  HOH   HOH A . 
G 4 HOH   127 927  178  HOH   HOH A . 
G 4 HOH   128 928  16   HOH   HOH A . 
G 4 HOH   129 929  68   HOH   HOH A . 
G 4 HOH   130 930  157  HOH   HOH A . 
G 4 HOH   131 931  34   HOH   HOH A . 
G 4 HOH   132 932  101  HOH   HOH A . 
G 4 HOH   133 933  57   HOH   HOH A . 
G 4 HOH   134 934  23   HOH   HOH A . 
G 4 HOH   135 935  63   HOH   HOH A . 
G 4 HOH   136 936  247  HOH   HOH A . 
G 4 HOH   137 937  215  HOH   HOH A . 
G 4 HOH   138 938  165  HOH   HOH A . 
G 4 HOH   139 939  472  HOH   HOH A . 
G 4 HOH   140 940  418  HOH   HOH A . 
G 4 HOH   141 941  36   HOH   HOH A . 
G 4 HOH   142 942  148  HOH   HOH A . 
G 4 HOH   143 943  8    HOH   HOH A . 
G 4 HOH   144 944  43   HOH   HOH A . 
G 4 HOH   145 945  61   HOH   HOH A . 
G 4 HOH   146 946  329  HOH   HOH A . 
G 4 HOH   147 947  73   HOH   HOH A . 
G 4 HOH   148 948  20   HOH   HOH A . 
G 4 HOH   149 949  164  HOH   HOH A . 
G 4 HOH   150 950  158  HOH   HOH A . 
G 4 HOH   151 951  5    HOH   HOH A . 
G 4 HOH   152 952  195  HOH   HOH A . 
G 4 HOH   153 953  62   HOH   HOH A . 
G 4 HOH   154 954  169  HOH   HOH A . 
G 4 HOH   155 955  246  HOH   HOH A . 
G 4 HOH   156 956  103  HOH   HOH A . 
G 4 HOH   157 957  25   HOH   HOH A . 
G 4 HOH   158 958  6    HOH   HOH A . 
G 4 HOH   159 959  58   HOH   HOH A . 
G 4 HOH   160 960  183  HOH   HOH A . 
G 4 HOH   161 961  32   HOH   HOH A . 
G 4 HOH   162 962  48   HOH   HOH A . 
G 4 HOH   163 963  54   HOH   HOH A . 
G 4 HOH   164 964  114  HOH   HOH A . 
G 4 HOH   165 965  260  HOH   HOH A . 
G 4 HOH   166 966  82   HOH   HOH A . 
G 4 HOH   167 967  162  HOH   HOH A . 
G 4 HOH   168 968  134  HOH   HOH A . 
G 4 HOH   169 969  468  HOH   HOH A . 
G 4 HOH   170 970  102  HOH   HOH A . 
G 4 HOH   171 971  300  HOH   HOH A . 
G 4 HOH   172 972  465  HOH   HOH A . 
G 4 HOH   173 973  41   HOH   HOH A . 
G 4 HOH   174 974  497  HOH   HOH A . 
G 4 HOH   175 975  29   HOH   HOH A . 
G 4 HOH   176 976  125  HOH   HOH A . 
G 4 HOH   177 977  493  HOH   HOH A . 
G 4 HOH   178 978  233  HOH   HOH A . 
G 4 HOH   179 979  77   HOH   HOH A . 
G 4 HOH   180 980  202  HOH   HOH A . 
G 4 HOH   181 981  413  HOH   HOH A . 
G 4 HOH   182 982  24   HOH   HOH A . 
G 4 HOH   183 983  10   HOH   HOH A . 
G 4 HOH   184 984  26   HOH   HOH A . 
G 4 HOH   185 985  35   HOH   HOH A . 
G 4 HOH   186 986  19   HOH   HOH A . 
G 4 HOH   187 987  70   HOH   HOH A . 
G 4 HOH   188 988  478  HOH   HOH A . 
G 4 HOH   189 989  399  HOH   HOH A . 
G 4 HOH   190 990  33   HOH   HOH A . 
G 4 HOH   191 991  21   HOH   HOH A . 
G 4 HOH   192 992  193  HOH   HOH A . 
G 4 HOH   193 993  283  HOH   HOH A . 
G 4 HOH   194 994  198  HOH   HOH A . 
G 4 HOH   195 995  2    HOH   HOH A . 
G 4 HOH   196 996  408  HOH   HOH A . 
G 4 HOH   197 997  50   HOH   HOH A . 
G 4 HOH   198 998  181  HOH   HOH A . 
G 4 HOH   199 999  238  HOH   HOH A . 
G 4 HOH   200 1000 49   HOH   HOH A . 
G 4 HOH   201 1001 271  HOH   HOH A . 
G 4 HOH   202 1002 97   HOH   HOH A . 
G 4 HOH   203 1003 159  HOH   HOH A . 
G 4 HOH   204 1004 415  HOH   HOH A . 
G 4 HOH   205 1005 458  HOH   HOH A . 
G 4 HOH   206 1006 12   HOH   HOH A . 
G 4 HOH   207 1007 405  HOH   HOH A . 
G 4 HOH   208 1008 237  HOH   HOH A . 
G 4 HOH   209 1009 78   HOH   HOH A . 
G 4 HOH   210 1010 115  HOH   HOH A . 
G 4 HOH   211 1011 94   HOH   HOH A . 
G 4 HOH   212 1012 316  HOH   HOH A . 
G 4 HOH   213 1013 236  HOH   HOH A . 
G 4 HOH   214 1014 334  HOH   HOH A . 
G 4 HOH   215 1015 184  HOH   HOH A . 
G 4 HOH   216 1016 230  HOH   HOH A . 
G 4 HOH   217 1017 190  HOH   HOH A . 
G 4 HOH   218 1018 336  HOH   HOH A . 
G 4 HOH   219 1019 209  HOH   HOH A . 
G 4 HOH   220 1020 213  HOH   HOH A . 
G 4 HOH   221 1021 250  HOH   HOH A . 
G 4 HOH   222 1022 176  HOH   HOH A . 
G 4 HOH   223 1023 156  HOH   HOH A . 
G 4 HOH   224 1024 167  HOH   HOH A . 
G 4 HOH   225 1025 326  HOH   HOH A . 
G 4 HOH   226 1026 398  HOH   HOH A . 
G 4 HOH   227 1027 154  HOH   HOH A . 
G 4 HOH   228 1028 71   HOH   HOH A . 
G 4 HOH   229 1029 495  HOH   HOH A . 
G 4 HOH   230 1030 72   HOH   HOH A . 
G 4 HOH   231 1031 356  HOH   HOH A . 
G 4 HOH   232 1032 219  HOH   HOH A . 
G 4 HOH   233 1033 463  HOH   HOH A . 
G 4 HOH   234 1034 289  HOH   HOH A . 
G 4 HOH   235 1035 422  HOH   HOH A . 
G 4 HOH   236 1036 476  HOH   HOH A . 
G 4 HOH   237 1037 312  HOH   HOH A . 
G 4 HOH   238 1038 276  HOH   HOH A . 
G 4 HOH   239 1039 456  HOH   HOH A . 
G 4 HOH   240 1040 87   HOH   HOH A . 
G 4 HOH   241 1041 469  HOH   HOH A . 
G 4 HOH   242 1042 404  HOH   HOH A . 
G 4 HOH   243 1043 239  HOH   HOH A . 
G 4 HOH   244 1044 442  HOH   HOH A . 
G 4 HOH   245 1045 104  HOH   HOH A . 
G 4 HOH   246 1046 284  HOH   HOH A . 
G 4 HOH   247 1047 227  HOH   HOH A . 
G 4 HOH   248 1048 42   HOH   HOH A . 
G 4 HOH   249 1049 200  HOH   HOH A . 
G 4 HOH   250 1050 168  HOH   HOH A . 
G 4 HOH   251 1051 258  HOH   HOH A . 
G 4 HOH   252 1052 446  HOH   HOH A . 
G 4 HOH   253 1053 98   HOH   HOH A . 
G 4 HOH   254 1054 395  HOH   HOH A . 
G 4 HOH   255 1055 461  HOH   HOH A . 
G 4 HOH   256 1056 296  HOH   HOH A . 
G 4 HOH   257 1057 229  HOH   HOH A . 
G 4 HOH   258 1058 53   HOH   HOH A . 
G 4 HOH   259 1059 89   HOH   HOH A . 
G 4 HOH   260 1060 331  HOH   HOH A . 
G 4 HOH   261 1061 256  HOH   HOH A . 
G 4 HOH   262 1062 142  HOH   HOH A . 
G 4 HOH   263 1063 64   HOH   HOH A . 
G 4 HOH   264 1064 358  HOH   HOH A . 
G 4 HOH   265 1065 122  HOH   HOH A . 
G 4 HOH   266 1066 112  HOH   HOH A . 
G 4 HOH   267 1067 151  HOH   HOH A . 
G 4 HOH   268 1068 47   HOH   HOH A . 
G 4 HOH   269 1069 100  HOH   HOH A . 
G 4 HOH   270 1070 132  HOH   HOH A . 
G 4 HOH   271 1071 504  HOH   HOH A . 
G 4 HOH   272 1072 501  HOH   HOH A . 
G 4 HOH   273 1073 56   HOH   HOH A . 
G 4 HOH   274 1074 214  HOH   HOH A . 
G 4 HOH   275 1075 323  HOH   HOH A . 
G 4 HOH   276 1076 186  HOH   HOH A . 
G 4 HOH   277 1077 212  HOH   HOH A . 
G 4 HOH   278 1078 51   HOH   HOH A . 
G 4 HOH   279 1079 409  HOH   HOH A . 
G 4 HOH   280 1080 189  HOH   HOH A . 
G 4 HOH   281 1081 389  HOH   HOH A . 
G 4 HOH   282 1082 166  HOH   HOH A . 
G 4 HOH   283 1083 228  HOH   HOH A . 
G 4 HOH   284 1084 275  HOH   HOH A . 
G 4 HOH   285 1085 385  HOH   HOH A . 
G 4 HOH   286 1086 375  HOH   HOH A . 
G 4 HOH   287 1087 299  HOH   HOH A . 
G 4 HOH   288 1088 263  HOH   HOH A . 
G 4 HOH   289 1089 150  HOH   HOH A . 
G 4 HOH   290 1090 376  HOH   HOH A . 
G 4 HOH   291 1091 483  HOH   HOH A . 
G 4 HOH   292 1092 45   HOH   HOH A . 
G 4 HOH   293 1093 280  HOH   HOH A . 
G 4 HOH   294 1094 286  HOH   HOH A . 
G 4 HOH   295 1095 155  HOH   HOH A . 
G 4 HOH   296 1096 315  HOH   HOH A . 
G 4 HOH   297 1097 153  HOH   HOH A . 
G 4 HOH   298 1098 377  HOH   HOH A . 
G 4 HOH   299 1099 83   HOH   HOH A . 
G 4 HOH   300 1100 412  HOH   HOH A . 
G 4 HOH   301 1101 66   HOH   HOH A . 
G 4 HOH   302 1102 257  HOH   HOH A . 
G 4 HOH   303 1103 368  HOH   HOH A . 
G 4 HOH   304 1104 188  HOH   HOH A . 
G 4 HOH   305 1105 441  HOH   HOH A . 
G 4 HOH   306 1106 452  HOH   HOH A . 
G 4 HOH   307 1107 273  HOH   HOH A . 
G 4 HOH   308 1108 352  HOH   HOH A . 
G 4 HOH   309 1109 453  HOH   HOH A . 
G 4 HOH   310 1110 84   HOH   HOH A . 
G 4 HOH   311 1111 99   HOH   HOH A . 
G 4 HOH   312 1112 152  HOH   HOH A . 
G 4 HOH   313 1113 177  HOH   HOH A . 
G 4 HOH   314 1114 365  HOH   HOH A . 
G 4 HOH   315 1115 317  HOH   HOH A . 
G 4 HOH   316 1116 225  HOH   HOH A . 
G 4 HOH   317 1117 311  HOH   HOH A . 
G 4 HOH   318 1118 123  HOH   HOH A . 
G 4 HOH   319 1119 282  HOH   HOH A . 
G 4 HOH   320 1120 484  HOH   HOH A . 
G 4 HOH   321 1121 119  HOH   HOH A . 
G 4 HOH   322 1122 249  HOH   HOH A . 
G 4 HOH   323 1123 231  HOH   HOH A . 
G 4 HOH   324 1124 211  HOH   HOH A . 
G 4 HOH   325 1125 499  HOH   HOH A . 
G 4 HOH   326 1126 272  HOH   HOH A . 
G 4 HOH   327 1127 378  HOH   HOH A . 
G 4 HOH   328 1128 253  HOH   HOH A . 
G 4 HOH   329 1129 221  HOH   HOH A . 
G 4 HOH   330 1130 361  HOH   HOH A . 
G 4 HOH   331 1131 172  HOH   HOH A . 
G 4 HOH   332 1132 127  HOH   HOH A . 
G 4 HOH   333 1133 277  HOH   HOH A . 
G 4 HOH   334 1134 217  HOH   HOH A . 
G 4 HOH   335 1135 129  HOH   HOH A . 
G 4 HOH   336 1136 498  HOH   HOH A . 
G 4 HOH   337 1137 218  HOH   HOH A . 
G 4 HOH   338 1138 406  HOH   HOH A . 
G 4 HOH   339 1139 396  HOH   HOH A . 
G 4 HOH   340 1140 76   HOH   HOH A . 
G 4 HOH   341 1141 344  HOH   HOH A . 
G 4 HOH   342 1142 379  HOH   HOH A . 
G 4 HOH   343 1143 491  HOH   HOH A . 
G 4 HOH   344 1144 145  HOH   HOH A . 
G 4 HOH   345 1145 440  HOH   HOH A . 
G 4 HOH   346 1146 137  HOH   HOH A . 
G 4 HOH   347 1147 306  HOH   HOH A . 
G 4 HOH   348 1148 86   HOH   HOH A . 
G 4 HOH   349 1149 143  HOH   HOH A . 
G 4 HOH   350 1150 279  HOH   HOH A . 
G 4 HOH   351 1151 128  HOH   HOH A . 
G 4 HOH   352 1152 175  HOH   HOH A . 
G 4 HOH   353 1153 382  HOH   HOH A . 
G 4 HOH   354 1154 354  HOH   HOH A . 
G 4 HOH   355 1155 362  HOH   HOH A . 
G 4 HOH   356 1156 303  HOH   HOH A . 
G 4 HOH   357 1157 44   HOH   HOH A . 
G 4 HOH   358 1158 197  HOH   HOH A . 
G 4 HOH   359 1159 270  HOH   HOH A . 
G 4 HOH   360 1160 174  HOH   HOH A . 
G 4 HOH   361 1161 394  HOH   HOH A . 
G 4 HOH   362 1162 171  HOH   HOH A . 
G 4 HOH   363 1163 192  HOH   HOH A . 
G 4 HOH   364 1164 252  HOH   HOH A . 
G 4 HOH   365 1165 434  HOH   HOH A . 
G 4 HOH   366 1166 490  HOH   HOH A . 
G 4 HOH   367 1167 30   HOH   HOH A . 
G 4 HOH   368 1168 369  HOH   HOH A . 
G 4 HOH   369 1169 95   HOH   HOH A . 
G 4 HOH   370 1170 224  HOH   HOH A . 
G 4 HOH   371 1171 180  HOH   HOH A . 
G 4 HOH   372 1172 380  HOH   HOH A . 
G 4 HOH   373 1173 503  HOH   HOH A . 
G 4 HOH   374 1174 234  HOH   HOH A . 
G 4 HOH   375 1175 502  HOH   HOH A . 
G 4 HOH   376 1176 355  HOH   HOH A . 
G 4 HOH   377 1177 392  HOH   HOH A . 
G 4 HOH   378 1178 359  HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A MET 1   ? CG  ? A MET 22  CG  
2  1 Y 1 A MET 1   ? SD  ? A MET 22  SD  
3  1 Y 1 A MET 1   ? CE  ? A MET 22  CE  
4  1 Y 1 A LEU 2   ? CG  ? A LEU 23  CG  
5  1 Y 1 A LEU 2   ? CD1 ? A LEU 23  CD1 
6  1 Y 1 A LEU 2   ? CD2 ? A LEU 23  CD2 
7  1 Y 1 A ARG 54  ? CG  ? A ARG 75  CG  
8  1 Y 1 A ARG 54  ? CD  ? A ARG 75  CD  
9  1 Y 1 A ARG 54  ? NE  ? A ARG 75  NE  
10 1 Y 1 A ARG 54  ? CZ  ? A ARG 75  CZ  
11 1 Y 1 A ARG 54  ? NH1 ? A ARG 75  NH1 
12 1 Y 1 A ARG 54  ? NH2 ? A ARG 75  NH2 
13 1 Y 1 A ASP 55  ? CG  ? A ASP 76  CG  
14 1 Y 1 A ASP 55  ? OD1 ? A ASP 76  OD1 
15 1 Y 1 A ASP 55  ? OD2 ? A ASP 76  OD2 
16 1 Y 1 A GLU 57  ? CG  ? A GLU 78  CG  
17 1 Y 1 A GLU 57  ? CD  ? A GLU 78  CD  
18 1 Y 1 A GLU 57  ? OE1 ? A GLU 78  OE1 
19 1 Y 1 A GLU 57  ? OE2 ? A GLU 78  OE2 
20 1 Y 1 A GLN 83  ? CG  ? A GLN 104 CG  
21 1 Y 1 A GLN 83  ? CD  ? A GLN 104 CD  
22 1 Y 1 A GLN 83  ? OE1 ? A GLN 104 OE1 
23 1 Y 1 A GLN 83  ? NE2 ? A GLN 104 NE2 
24 1 Y 1 A GLU 100 ? CG  ? A GLU 121 CG  
25 1 Y 1 A GLU 100 ? CD  ? A GLU 121 CD  
26 1 Y 1 A GLU 100 ? OE1 ? A GLU 121 OE1 
27 1 Y 1 A GLU 100 ? OE2 ? A GLU 121 OE2 
28 1 Y 1 A TRP 161 ? CG  ? A TRP 182 CG  
29 1 Y 1 A TRP 161 ? CD1 ? A TRP 182 CD1 
30 1 Y 1 A TRP 161 ? CD2 ? A TRP 182 CD2 
31 1 Y 1 A TRP 161 ? NE1 ? A TRP 182 NE1 
32 1 Y 1 A TRP 161 ? CE2 ? A TRP 182 CE2 
33 1 Y 1 A TRP 161 ? CE3 ? A TRP 182 CE3 
34 1 Y 1 A TRP 161 ? CZ2 ? A TRP 182 CZ2 
35 1 Y 1 A TRP 161 ? CZ3 ? A TRP 182 CZ3 
36 1 Y 1 A TRP 161 ? CH2 ? A TRP 182 CH2 
37 1 Y 1 A LYS 179 ? CG  ? A LYS 200 CG  
38 1 Y 1 A LYS 179 ? CD  ? A LYS 200 CD  
39 1 Y 1 A LYS 179 ? CE  ? A LYS 200 CE  
40 1 Y 1 A LYS 179 ? NZ  ? A LYS 200 NZ  
41 1 Y 1 A LYS 189 ? CG  ? A LYS 210 CG  
42 1 Y 1 A LYS 189 ? CD  ? A LYS 210 CD  
43 1 Y 1 A LYS 189 ? CE  ? A LYS 210 CE  
44 1 Y 1 A LYS 189 ? NZ  ? A LYS 210 NZ  
45 1 Y 1 A LYS 240 ? CG  ? A LYS 261 CG  
46 1 Y 1 A LYS 240 ? CD  ? A LYS 261 CD  
47 1 Y 1 A LYS 240 ? CE  ? A LYS 261 CE  
48 1 Y 1 A LYS 240 ? NZ  ? A LYS 261 NZ  
49 1 Y 1 A GLN 278 ? CG  ? A GLN 299 CG  
50 1 Y 1 A GLN 278 ? CD  ? A GLN 299 CD  
51 1 Y 1 A GLN 278 ? OE1 ? A GLN 299 OE1 
52 1 Y 1 A GLN 278 ? NE2 ? A GLN 299 NE2 
53 1 Y 1 A LYS 325 ? CG  ? A LYS 346 CG  
54 1 Y 1 A LYS 325 ? CD  ? A LYS 346 CD  
55 1 Y 1 A LYS 325 ? CE  ? A LYS 346 CE  
56 1 Y 1 A LYS 325 ? NZ  ? A LYS 346 NZ  
57 1 Y 1 A ASP 346 ? CG  ? A ASP 367 CG  
58 1 Y 1 A ASP 346 ? OD1 ? A ASP 367 OD1 
59 1 Y 1 A ASP 346 ? OD2 ? A ASP 367 OD2 
60 1 Y 1 A ARG 373 ? CG  ? A ARG 394 CG  
61 1 Y 1 A ARG 373 ? CD  ? A ARG 394 CD  
62 1 Y 1 A ARG 373 ? NE  ? A ARG 394 NE  
63 1 Y 1 A ARG 373 ? CZ  ? A ARG 394 CZ  
64 1 Y 1 A ARG 373 ? NH1 ? A ARG 394 NH1 
65 1 Y 1 A ARG 373 ? NH2 ? A ARG 394 NH2 
66 1 Y 1 A LYS 383 ? CG  ? A LYS 404 CG  
67 1 Y 1 A LYS 383 ? CD  ? A LYS 404 CD  
68 1 Y 1 A LYS 383 ? CE  ? A LYS 404 CE  
69 1 Y 1 A LYS 383 ? NZ  ? A LYS 404 NZ  
70 1 Y 1 A GLU 384 ? CG  ? A GLU 405 CG  
71 1 Y 1 A GLU 384 ? CD  ? A GLU 405 CD  
72 1 Y 1 A GLU 384 ? OE1 ? A GLU 405 OE1 
73 1 Y 1 A GLU 384 ? OE2 ? A GLU 405 OE2 
74 1 Y 1 A LEU 398 ? CG  ? A LEU 419 CG  
75 1 Y 1 A LEU 398 ? CD1 ? A LEU 419 CD1 
76 1 Y 1 A LEU 398 ? CD2 ? A LEU 419 CD2 
77 1 Y 1 A ARG 525 ? CG  ? A ARG 546 CG  
78 1 Y 1 A ARG 525 ? CD  ? A ARG 546 CD  
79 1 Y 1 A ARG 525 ? NE  ? A ARG 546 NE  
80 1 Y 1 A ARG 525 ? CZ  ? A ARG 546 CZ  
81 1 Y 1 A ARG 525 ? NH1 ? A ARG 546 NH1 
82 1 Y 1 A ARG 525 ? NH2 ? A ARG 546 NH2 
83 1 Y 1 A LYS 574 ? CG  ? A LYS 595 CG  
84 1 Y 1 A LYS 574 ? CD  ? A LYS 595 CD  
85 1 Y 1 A LYS 574 ? CE  ? A LYS 595 CE  
86 1 Y 1 A LYS 574 ? NZ  ? A LYS 595 NZ  
87 1 Y 1 A ARG 667 ? CG  ? A ARG 688 CG  
88 1 Y 1 A ARG 667 ? CD  ? A ARG 688 CD  
89 1 Y 1 A ARG 667 ? NE  ? A ARG 688 NE  
90 1 Y 1 A ARG 667 ? CZ  ? A ARG 688 CZ  
91 1 Y 1 A ARG 667 ? NH1 ? A ARG 688 NH1 
92 1 Y 1 A ARG 667 ? NH2 ? A ARG 688 NH2 
# 
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    ? ? ? '(1.20_4459: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.28 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DOL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     201.127 
_cell.length_a_esd                 ? 
_cell.length_b                     51.051 
_cell.length_b_esd                 ? 
_cell.length_c                     76.208 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DOL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DOL 
_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             2.39 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.47 
_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.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;protein at 8 mg/mL in buffer 20 mM Tris pH 7.5, 10% glycerol, 500 mM NaCl, 0.5 mM TCEP, and 1 mM EDTA, and well solution composed of 0.1 M magnesium acetate, 50 mM MES pH 5.5, and 9-16%
methyl 2,4-pentane diol
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-09-02 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_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   1.0 
_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 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DOL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.77 
_reflns.d_resolution_low                               96.6 
_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                                     40310 
_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                           92.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.6 
_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                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.05 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.77 
_reflns_shell.d_res_low                                     2.02 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2014 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_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                               ? 
_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                                  0.722 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.74 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DOL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.77 
_refine.ls_d_res_low                             96.53 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     40305 
_refine.ls_number_reflns_R_free                  1899 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    55.54 
_refine.ls_percent_reflns_R_free                 4.71 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1869 
_refine.ls_R_factor_R_free                       0.2271 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1849 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 33.50 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.77 
_refine_hist.d_res_low                        96.53 
_refine_hist.number_atoms_solvent             378 
_refine_hist.number_atoms_total               5525 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5110 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         37 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003  ? 5337 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.597  ? 7265 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.960 ? 1974 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.045  ? 806  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 957  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.77 1.82  . . 6   53   1.00   . . . . 0.4206 . . . . . . . . . . . 0.2979 
'X-RAY DIFFRACTION' 1.82 1.86  . . 6   195  4.00   . . . . 0.3469 . . . . . . . . . . . 0.3146 
'X-RAY DIFFRACTION' 1.87 1.92  . . 31  440  9.00   . . . . 0.3090 . . . . . . . . . . . 0.3668 
'X-RAY DIFFRACTION' 1.92 1.98  . . 27  708  14.00  . . . . 0.2829 . . . . . . . . . . . 0.2886 
'X-RAY DIFFRACTION' 1.98 2.05  . . 54  1079 22.00  . . . . 0.2678 . . . . . . . . . . . 0.3017 
'X-RAY DIFFRACTION' 2.05 2.13  . . 81  1573 32.00  . . . . 0.2708 . . . . . . . . . . . 0.2935 
'X-RAY DIFFRACTION' 2.14 2.23  . . 113 2371 48.00  . . . . 0.2633 . . . . . . . . . . . 0.3017 
'X-RAY DIFFRACTION' 2.23 2.35  . . 157 3336 68.00  . . . . 0.2638 . . . . . . . . . . . 0.2773 
'X-RAY DIFFRACTION' 2.35 2.50  . . 196 4135 84.00  . . . . 0.2528 . . . . . . . . . . . 0.2636 
'X-RAY DIFFRACTION' 2.50 2.69  . . 247 4867 98.00  . . . . 0.2333 . . . . . . . . . . . 0.2612 
'X-RAY DIFFRACTION' 2.69 2.96  . . 253 4899 100.00 . . . . 0.2099 . . . . . . . . . . . 0.2784 
'X-RAY DIFFRACTION' 2.96 3.39  . . 252 4918 99.00  . . . . 0.1775 . . . . . . . . . . . 0.2428 
'X-RAY DIFFRACTION' 3.39 4.27  . . 220 4934 98.00  . . . . 0.1437 . . . . . . . . . . . 0.1898 
'X-RAY DIFFRACTION' 4.27 96.53 . . 256 4898 96.00  . . . . 0.1598 . . . . . . . . . . . 0.1925 
# 
_struct.entry_id                     9DOL 
_struct.title                        
'Potent inhibition of the protein arginine deiminases (PAD1-4) by targeting a Ca2+ dependent allosteric binding site' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9DOL 
_struct_keywords.text            'peptylarginine deiminase, inhibitor, allosteric, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PADI2_HUMAN 
_struct_ref.pdbx_db_accession          Q9Y2J8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MLRERTVRLQYGSRVEAVYVLGTYLWTDVYSAAPAGAQTFSLKHSEHVWVEVVRDGEAEEVATNGKQRWLLSPSTTLRVT
MSQASTEASSDKVTVNYYDEEGSIPIDQAGLFLTAIEISLDVDADRDGVVEKNNPKKASWTWGPEGQGAILLVNCDRETP
WLPKEDCRDEKVYSKEDLKDMSQMILRTKGPDRLPAGYEIVLYISMSDSDKVGVFYVENPFFGQRYIHILGRRKLYHVVK
YTGGSAELLFFVEGLCFPDEGFSGLVSIHVSLLEYMAQDIPLTPIFTDTVIFRIAPWIMTPNILPPVSVFVCCMKDNYLF
LKEVKNLVEKTNCELKVCFQYLNRGDRWIQDEIEFGYIEAPHKGFPVVLDSPRDGNLKDFPVKELLGPDFGYVTREPLFE
SVTSLDSFGNLEVSPPVTVNGKTYPLGRILIGSSFPLSGGRRMTKVVRDFLKAQQVQAPVELYSDWLTVGHVDEFMSFVP
IPGTKKFLLLMASTSACYKLFREKQKDGHGEAIMFKGLGGMSSKRITINKILSNESLVQENLYFQRCLDWNRDILKKELG
LTEQDIIDLPALFKMDEDHRARAFFPNMVNMIVLDKDLGIPKPFGPQVEEECCLEMHVRGLLEPLGLECTFIDDISAYHK
FLGEVHCGTNVRRKPFTFKWWHMVP
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9DOL 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 22 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 686 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9Y2J8 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  665 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       665 
# 
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 9DOL MET A 1   ? UNP Q9Y2J8 ? ? 'initiating methionine' -20 1  
1 9DOL GLY A 2   ? UNP Q9Y2J8 ? ? 'expression tag'        -19 2  
1 9DOL HIS A 3   ? UNP Q9Y2J8 ? ? 'expression tag'        -18 3  
1 9DOL HIS A 4   ? UNP Q9Y2J8 ? ? 'expression tag'        -17 4  
1 9DOL HIS A 5   ? UNP Q9Y2J8 ? ? 'expression tag'        -16 5  
1 9DOL HIS A 6   ? UNP Q9Y2J8 ? ? 'expression tag'        -15 6  
1 9DOL HIS A 7   ? UNP Q9Y2J8 ? ? 'expression tag'        -14 7  
1 9DOL HIS A 8   ? UNP Q9Y2J8 ? ? 'expression tag'        -13 8  
1 9DOL HIS A 9   ? UNP Q9Y2J8 ? ? 'expression tag'        -12 9  
1 9DOL HIS A 10  ? UNP Q9Y2J8 ? ? 'expression tag'        -11 10 
1 9DOL HIS A 11  ? UNP Q9Y2J8 ? ? 'expression tag'        -10 11 
1 9DOL HIS A 12  ? UNP Q9Y2J8 ? ? 'expression tag'        -9  12 
1 9DOL SER A 13  ? UNP Q9Y2J8 ? ? 'expression tag'        -8  13 
1 9DOL SER A 14  ? UNP Q9Y2J8 ? ? 'expression tag'        -7  14 
1 9DOL GLY A 15  ? UNP Q9Y2J8 ? ? 'expression tag'        -6  15 
1 9DOL HIS A 16  ? UNP Q9Y2J8 ? ? 'expression tag'        -5  16 
1 9DOL ILE A 17  ? UNP Q9Y2J8 ? ? 'expression tag'        -4  17 
1 9DOL GLU A 18  ? UNP Q9Y2J8 ? ? 'expression tag'        -3  18 
1 9DOL GLY A 19  ? UNP Q9Y2J8 ? ? 'expression tag'        -2  19 
1 9DOL ARG A 20  ? UNP Q9Y2J8 ? ? 'expression tag'        -1  20 
1 9DOL HIS A 21  ? UNP Q9Y2J8 ? ? 'expression tag'        0   21 
1 9DOL SER A 687 ? UNP Q9Y2J8 ? ? 'expression tag'        666 22 
1 9DOL ARG A 688 ? UNP Q9Y2J8 ? ? 'expression tag'        667 23 
1 9DOL ARG A 689 ? UNP Q9Y2J8 ? ? 'expression tag'        668 24 
1 9DOL SER A 690 ? UNP Q9Y2J8 ? ? 'expression tag'        669 25 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   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_
_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 GLU A 186 ? ASP A 190 ? GLU A 165 ASP A 169 5 ? 5  
HELX_P HELX_P2  AA2 SER A 195 ? MET A 202 ? SER A 174 MET A 181 5 ? 8  
HELX_P HELX_P3  AA3 MET A 227 ? ASP A 231 ? MET A 206 ASP A 210 5 ? 5  
HELX_P HELX_P4  AA4 ASN A 338 ? LYS A 351 ? ASN A 317 LYS A 330 1 ? 14 
HELX_P HELX_P5  AA5 ARG A 368 ? GLU A 373 ? ARG A 347 GLU A 352 1 ? 6  
HELX_P HELX_P6  AA6 SER A 428 ? GLY A 430 ? SER A 407 GLY A 409 5 ? 3  
HELX_P HELX_P7  AA7 THR A 465 ? GLN A 475 ? THR A 444 GLN A 454 1 ? 11 
HELX_P HELX_P8  AA8 HIS A 492 ? GLU A 495 ? HIS A 471 GLU A 474 5 ? 4  
HELX_P HELX_P9  AA9 THR A 515 ? ASP A 528 ? THR A 494 ASP A 507 1 ? 14 
HELX_P HELX_P10 AB1 THR A 548 ? SER A 554 ? THR A 527 SER A 533 1 ? 7  
HELX_P HELX_P11 AB2 ASN A 555 ? GLY A 581 ? ASN A 534 GLY A 560 1 ? 27 
HELX_P HELX_P12 AB3 THR A 583 ? GLN A 585 ? THR A 562 GLN A 564 5 ? 3  
HELX_P HELX_P13 AB4 CYS A 633 ? GLU A 644 ? CYS A 612 GLU A 623 1 ? 12 
HELX_P HELX_P14 AB5 PRO A 645 ? GLY A 647 ? PRO A 624 GLY A 626 5 ? 3  
HELX_P HELX_P15 AB6 ILE A 656 ? HIS A 660 ? ILE A 635 HIS A 639 5 ? 5  
HELX_P HELX_P16 AB7 LYS A 680 ? MET A 684 ? LYS A 659 MET A 663 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 144 OD1 ? ? ? 1_555 E CA  . CA ? ? A ASP 123 A CA  704  1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc2  metalc ? ? A ASP 146 OD1 ? ? ? 1_555 E CA  . CA ? ? A ASP 125 A CA  704  1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc3  metalc ? ? A ASP 146 OD2 ? ? ? 1_555 E CA  . CA ? ? A ASP 125 A CA  704  1_555 ? ? ? ? ? ? ? 3.116 ? ? 
metalc4  metalc ? ? A ASP 148 OD1 ? ? ? 1_555 E CA  . CA ? ? A ASP 127 A CA  704  1_555 ? ? ? ? ? ? ? 2.118 ? ? 
metalc5  metalc ? ? A VAL 150 O   ? ? ? 1_555 E CA  . CA ? ? A VAL 129 A CA  704  1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc6  metalc ? ? A GLU 152 OE1 ? ? ? 1_555 E CA  . CA ? ? A GLU 131 A CA  704  1_555 ? ? ? ? ? ? ? 2.216 ? ? 
metalc7  metalc ? ? A ASN 175 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASN 154 A CA  702  1_555 ? ? ? ? ? ? ? 2.281 ? ? 
metalc8  metalc ? ? A ASP 177 OD2 ? ? ? 1_555 B CA  . CA ? ? A ASP 156 A CA  701  1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc9  metalc ? ? A ASP 177 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 156 A CA  702  1_555 ? ? ? ? ? ? ? 2.306 ? ? 
metalc10 metalc ? ? A GLU 179 OE2 ? ? ? 1_555 B CA  . CA ? ? A GLU 158 A CA  701  1_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc11 metalc ? ? A GLU 179 OE2 ? ? ? 1_555 C CA  . CA ? ? A GLU 158 A CA  702  1_555 ? ? ? ? ? ? ? 2.391 ? ? 
metalc12 metalc ? ? A ASP 187 OD2 ? ? ? 1_555 C CA  . CA ? ? A ASP 166 A CA  702  1_555 ? ? ? ? ? ? ? 2.185 ? ? 
metalc13 metalc ? ? A ASP 187 O   ? ? ? 1_555 D CA  . CA ? ? A ASP 166 A CA  703  1_555 ? ? ? ? ? ? ? 2.215 ? ? 
metalc14 metalc ? ? A ASP 190 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 169 A CA  703  1_555 ? ? ? ? ? ? ? 2.227 ? ? 
metalc15 metalc ? ? A LYS 192 O   ? ? ? 1_555 D CA  . CA ? ? A LYS 171 A CA  703  1_555 ? ? ? ? ? ? ? 2.181 ? ? 
metalc16 metalc ? ? A ASP 198 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 177 A CA  702  1_555 ? ? ? ? ? ? ? 2.491 ? ? 
metalc17 metalc ? ? A ASP 201 OD1 ? ? ? 1_555 B CA  . CA ? ? A ASP 180 A CA  701  1_555 ? ? ? ? ? ? ? 2.768 ? ? 
metalc18 metalc ? ? A ASP 201 OD2 ? ? ? 1_555 B CA  . CA ? ? A ASP 180 A CA  701  1_555 ? ? ? ? ? ? ? 2.353 ? ? 
metalc19 metalc ? ? A ASP 201 OD2 ? ? ? 1_555 C CA  . CA ? ? A ASP 180 A CA  702  1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc20 metalc ? ? A ASP 410 OD1 ? ? ? 1_555 B CA  . CA ? ? A ASP 389 A CA  701  1_555 ? ? ? ? ? ? ? 2.811 ? ? 
metalc21 metalc ? ? B CA  .   CA  ? ? ? 1_555 G HOH . O  ? ? A CA  701 A HOH 868  1_555 ? ? ? ? ? ? ? 2.580 ? ? 
metalc22 metalc ? ? D CA  .   CA  ? ? ? 1_555 G HOH . O  ? ? A CA  703 A HOH 811  1_555 ? ? ? ? ? ? ? 2.354 ? ? 
metalc23 metalc ? ? D CA  .   CA  ? ? ? 1_555 G HOH . O  ? ? A CA  703 A HOH 893  1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc24 metalc ? ? D CA  .   CA  ? ? ? 1_555 G HOH . O  ? ? A CA  703 A HOH 1052 1_555 ? ? ? ? ? ? ? 2.504 ? ? 
metalc25 metalc ? ? E CA  .   CA  ? ? ? 1_555 G HOH . O  ? ? A CA  704 A HOH 885  1_555 ? ? ? ? ? ? ? 2.174 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 144 ? A ASP 123 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 OD1 ? A ASP 146 ? A ASP 125  ? 1_555 82.4  ? 
2  OD1 ? A ASP 144 ? A ASP 123 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 OD2 ? A ASP 146 ? A ASP 125  ? 1_555 125.3 ? 
3  OD1 ? A ASP 146 ? A ASP 125 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 OD2 ? A ASP 146 ? A ASP 125  ? 1_555 44.6  ? 
4  OD1 ? A ASP 144 ? A ASP 123 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 OD1 ? A ASP 148 ? A ASP 127  ? 1_555 79.3  ? 
5  OD1 ? A ASP 146 ? A ASP 125 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 OD1 ? A ASP 148 ? A ASP 127  ? 1_555 83.7  ? 
6  OD2 ? A ASP 146 ? A ASP 125 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 OD1 ? A ASP 148 ? A ASP 127  ? 1_555 102.5 ? 
7  OD1 ? A ASP 144 ? A ASP 123 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 O   ? A VAL 150 ? A VAL 129  ? 1_555 89.0  ? 
8  OD1 ? A ASP 146 ? A ASP 125 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 O   ? A VAL 150 ? A VAL 129  ? 1_555 171.3 ? 
9  OD2 ? A ASP 146 ? A ASP 125 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 O   ? A VAL 150 ? A VAL 129  ? 1_555 144.0 ? 
10 OD1 ? A ASP 148 ? A ASP 127 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 O   ? A VAL 150 ? A VAL 129  ? 1_555 93.8  ? 
11 OD1 ? A ASP 144 ? A ASP 123 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 OE1 ? A GLU 152 ? A GLU 131  ? 1_555 108.5 ? 
12 OD1 ? A ASP 146 ? A ASP 125 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 OE1 ? A GLU 152 ? A GLU 131  ? 1_555 97.1  ? 
13 OD2 ? A ASP 146 ? A ASP 125 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 OE1 ? A GLU 152 ? A GLU 131  ? 1_555 73.2  ? 
14 OD1 ? A ASP 148 ? A ASP 127 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 OE1 ? A GLU 152 ? A GLU 131  ? 1_555 172.1 ? 
15 O   ? A VAL 150 ? A VAL 129 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 OE1 ? A GLU 152 ? A GLU 131  ? 1_555 86.5  ? 
16 OD1 ? A ASP 144 ? A ASP 123 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 O   ? G HOH .   ? A HOH 885  ? 1_555 162.3 ? 
17 OD1 ? A ASP 146 ? A ASP 125 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 O   ? G HOH .   ? A HOH 885  ? 1_555 93.6  ? 
18 OD2 ? A ASP 146 ? A ASP 125 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 O   ? G HOH .   ? A HOH 885  ? 1_555 56.7  ? 
19 OD1 ? A ASP 148 ? A ASP 127 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 O   ? G HOH .   ? A HOH 885  ? 1_555 83.1  ? 
20 O   ? A VAL 150 ? A VAL 129 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 O   ? G HOH .   ? A HOH 885  ? 1_555 94.4  ? 
21 OE1 ? A GLU 152 ? A GLU 131 ? 1_555 CA ? E CA . ? A CA 704 ? 1_555 O   ? G HOH .   ? A HOH 885  ? 1_555 89.0  ? 
22 OD1 ? A ASN 175 ? A ASN 154 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OD1 ? A ASP 177 ? A ASP 156  ? 1_555 77.6  ? 
23 OD1 ? A ASN 175 ? A ASN 154 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OE2 ? A GLU 179 ? A GLU 158  ? 1_555 158.3 ? 
24 OD1 ? A ASP 177 ? A ASP 156 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OE2 ? A GLU 179 ? A GLU 158  ? 1_555 99.5  ? 
25 OD1 ? A ASN 175 ? A ASN 154 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OD2 ? A ASP 187 ? A ASP 166  ? 1_555 101.7 ? 
26 OD1 ? A ASP 177 ? A ASP 156 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OD2 ? A ASP 187 ? A ASP 166  ? 1_555 90.0  ? 
27 OE2 ? A GLU 179 ? A GLU 158 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OD2 ? A ASP 187 ? A ASP 166  ? 1_555 99.9  ? 
28 OD1 ? A ASN 175 ? A ASN 154 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OD1 ? A ASP 198 ? A ASP 177  ? 1_555 86.4  ? 
29 OD1 ? A ASP 177 ? A ASP 156 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OD1 ? A ASP 198 ? A ASP 177  ? 1_555 161.8 ? 
30 OE2 ? A GLU 179 ? A GLU 158 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OD1 ? A ASP 198 ? A ASP 177  ? 1_555 98.6  ? 
31 OD2 ? A ASP 187 ? A ASP 166 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OD1 ? A ASP 198 ? A ASP 177  ? 1_555 84.8  ? 
32 OD1 ? A ASN 175 ? A ASN 154 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OD2 ? A ASP 201 ? A ASP 180  ? 1_555 87.9  ? 
33 OD1 ? A ASP 177 ? A ASP 156 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OD2 ? A ASP 201 ? A ASP 180  ? 1_555 80.3  ? 
34 OE2 ? A GLU 179 ? A GLU 158 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OD2 ? A ASP 201 ? A ASP 180  ? 1_555 70.4  ? 
35 OD2 ? A ASP 187 ? A ASP 166 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OD2 ? A ASP 201 ? A ASP 180  ? 1_555 164.7 ? 
36 OD1 ? A ASP 198 ? A ASP 177 ? 1_555 CA ? C CA . ? A CA 702 ? 1_555 OD2 ? A ASP 201 ? A ASP 180  ? 1_555 107.9 ? 
37 OD2 ? A ASP 177 ? A ASP 156 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OE2 ? A GLU 179 ? A GLU 158  ? 1_555 74.8  ? 
38 OD2 ? A ASP 177 ? A ASP 156 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OD1 ? A ASP 201 ? A ASP 180  ? 1_555 110.7 ? 
39 OE2 ? A GLU 179 ? A GLU 158 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OD1 ? A ASP 201 ? A ASP 180  ? 1_555 116.0 ? 
40 OD2 ? A ASP 177 ? A ASP 156 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OD2 ? A ASP 201 ? A ASP 180  ? 1_555 78.3  ? 
41 OE2 ? A GLU 179 ? A GLU 158 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OD2 ? A ASP 201 ? A ASP 180  ? 1_555 71.4  ? 
42 OD1 ? A ASP 201 ? A ASP 180 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OD2 ? A ASP 201 ? A ASP 180  ? 1_555 50.1  ? 
43 OD2 ? A ASP 177 ? A ASP 156 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OD1 ? A ASP 410 ? A ASP 389  ? 1_555 101.4 ? 
44 OE2 ? A GLU 179 ? A GLU 158 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OD1 ? A ASP 410 ? A ASP 389  ? 1_555 160.5 ? 
45 OD1 ? A ASP 201 ? A ASP 180 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OD1 ? A ASP 410 ? A ASP 389  ? 1_555 83.3  ? 
46 OD2 ? A ASP 201 ? A ASP 180 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 OD1 ? A ASP 410 ? A ASP 389  ? 1_555 127.1 ? 
47 OD2 ? A ASP 177 ? A ASP 156 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? G HOH .   ? A HOH 868  ? 1_555 165.3 ? 
48 OE2 ? A GLU 179 ? A GLU 158 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? G HOH .   ? A HOH 868  ? 1_555 90.6  ? 
49 OD1 ? A ASP 201 ? A ASP 180 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? G HOH .   ? A HOH 868  ? 1_555 77.5  ? 
50 OD2 ? A ASP 201 ? A ASP 180 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? G HOH .   ? A HOH 868  ? 1_555 99.5  ? 
51 OD1 ? A ASP 410 ? A ASP 389 ? 1_555 CA ? B CA . ? A CA 701 ? 1_555 O   ? G HOH .   ? A HOH 868  ? 1_555 91.5  ? 
52 O   ? A ASP 187 ? A ASP 166 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 OD1 ? A ASP 190 ? A ASP 169  ? 1_555 82.1  ? 
53 O   ? A ASP 187 ? A ASP 166 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? A LYS 192 ? A LYS 171  ? 1_555 168.5 ? 
54 OD1 ? A ASP 190 ? A ASP 169 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? A LYS 192 ? A LYS 171  ? 1_555 86.5  ? 
55 O   ? A ASP 187 ? A ASP 166 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? G HOH .   ? A HOH 811  ? 1_555 82.7  ? 
56 OD1 ? A ASP 190 ? A ASP 169 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? G HOH .   ? A HOH 811  ? 1_555 82.6  ? 
57 O   ? A LYS 192 ? A LYS 171 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? G HOH .   ? A HOH 811  ? 1_555 95.0  ? 
58 O   ? A ASP 187 ? A ASP 166 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? G HOH .   ? A HOH 893  ? 1_555 94.0  ? 
59 OD1 ? A ASP 190 ? A ASP 169 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? G HOH .   ? A HOH 893  ? 1_555 164.1 ? 
60 O   ? A LYS 192 ? A LYS 171 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? G HOH .   ? A HOH 893  ? 1_555 96.8  ? 
61 O   ? G HOH .   ? A HOH 811 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? G HOH .   ? A HOH 893  ? 1_555 81.6  ? 
62 O   ? A ASP 187 ? A ASP 166 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? G HOH .   ? A HOH 1052 ? 1_555 89.4  ? 
63 OD1 ? A ASP 190 ? A ASP 169 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? G HOH .   ? A HOH 1052 ? 1_555 83.5  ? 
64 O   ? A LYS 192 ? A LYS 171 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? G HOH .   ? A HOH 1052 ? 1_555 90.2  ? 
65 O   ? G HOH .   ? A HOH 811 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? G HOH .   ? A HOH 1052 ? 1_555 164.9 ? 
66 O   ? G HOH .   ? A HOH 893 ? 1_555 CA ? D CA . ? A CA 703 ? 1_555 O   ? G HOH .   ? A HOH 1052 ? 1_555 112.0 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
AA4 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 3 ? 
AA7 ? 3 ? 
AA8 ? 2 ? 
AA9 ? 3 ? 
AB1 ? 2 ? 
AB2 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? parallel      
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 24  ? THR A 27  ? ARG A 3   THR A 6   
AA1 2 THR A 44  ? THR A 48  ? THR A 23  THR A 27  
AA1 3 THR A 96  ? THR A 101 ? THR A 75  THR A 80  
AA1 4 TRP A 70  ? ARG A 75  ? TRP A 49  ARG A 54  
AA1 5 ALA A 79  ? GLU A 81  ? ALA A 58  GLU A 60  
AA2 1 ARG A 35  ? VAL A 41  ? ARG A 14  VAL A 20  
AA2 2 ASP A 128 ? ASP A 142 ? ASP A 107 ASP A 121 
AA2 3 ASP A 112 ? TYR A 119 ? ASP A 91  TYR A 98  
AA2 4 THR A 60  ? HIS A 65  ? THR A 39  HIS A 44  
AA2 5 TRP A 90  ? LEU A 91  ? TRP A 69  LEU A 70  
AA3 1 ARG A 35  ? VAL A 41  ? ARG A 14  VAL A 20  
AA3 2 ASP A 128 ? ASP A 142 ? ASP A 107 ASP A 121 
AA3 3 SER A 203 ? LYS A 210 ? SER A 182 LYS A 189 
AA3 4 ALA A 267 ? GLY A 275 ? ALA A 246 GLY A 254 
AA3 5 VAL A 233 ? GLU A 239 ? VAL A 212 GLU A 218 
AA3 6 ARG A 246 ? LEU A 251 ? ARG A 225 LEU A 230 
AA4 1 ALA A 170 ? LEU A 172 ? ALA A 149 LEU A 151 
AA4 2 THR A 304 ? ILE A 315 ? THR A 283 ILE A 294 
AA4 3 LEU A 286 ? GLU A 295 ? LEU A 265 GLU A 274 
AA4 4 TYR A 219 ? TYR A 224 ? TYR A 198 TYR A 203 
AA4 5 TYR A 257 ? VAL A 260 ? TYR A 236 VAL A 239 
AA5 1 ILE A 319 ? MET A 320 ? ILE A 298 MET A 299 
AA5 2 ILE A 374 ? GLU A 380 ? ILE A 353 GLU A 359 
AA5 3 GLY A 385 ? ASP A 391 ? GLY A 364 ASP A 370 
AA5 4 GLY A 412 ? THR A 415 ? GLY A 391 THR A 394 
AA6 1 GLU A 355 ? CYS A 359 ? GLU A 334 CYS A 338 
AA6 2 PRO A 327 ? CYS A 333 ? PRO A 306 CYS A 312 
AA6 3 GLY A 669 ? ARG A 674 ? GLY A 648 ARG A 653 
AA7 1 LEU A 432 ? VAL A 434 ? LEU A 411 VAL A 413 
AA7 2 ILE A 450 ? SER A 454 ? ILE A 429 SER A 433 
AA7 3 VAL A 481 ? TYR A 484 ? VAL A 460 TYR A 463 
AA8 1 VAL A 438 ? VAL A 440 ? VAL A 417 VAL A 419 
AA8 2 LYS A 443 ? TYR A 445 ? LYS A 422 TYR A 424 
AA9 1 MET A 497 ? PRO A 501 ? MET A 476 PRO A 480 
AA9 2 PHE A 508 ? SER A 514 ? PHE A 487 SER A 493 
AA9 3 ILE A 587 ? PRO A 591 ? ILE A 566 PRO A 570 
AB1 1 PHE A 594 ? MET A 596 ? PHE A 573 MET A 575 
AB1 2 ALA A 602 ? ALA A 604 ? ALA A 581 ALA A 583 
AB2 1 ILE A 613 ? LEU A 615 ? ILE A 592 LEU A 594 
AB2 2 ASP A 618 ? PRO A 622 ? ASP A 597 PRO A 601 
AB2 3 GLU A 649 ? ILE A 653 ? GLU A 628 ILE A 632 
# 
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 ARG A 26  ? N ARG A 5   O TRP A 47  ? O TRP A 26  
AA1 2 3 N LEU A 46  ? N LEU A 25  O VAL A 100 ? O VAL A 79  
AA1 3 4 O THR A 97  ? O THR A 76  N VAL A 74  ? N VAL A 53  
AA1 4 5 N VAL A 73  ? N VAL A 52  O GLU A 80  ? O GLU A 59  
AA2 1 2 N VAL A 36  ? N VAL A 15  O PHE A 133 ? O PHE A 112 
AA2 2 3 O LEU A 134 ? O LEU A 113 N ASP A 112 ? N ASP A 91  
AA2 3 4 O THR A 115 ? O THR A 94  N LYS A 64  ? N LYS A 43  
AA2 4 5 N PHE A 61  ? N PHE A 40  O TRP A 90  ? O TRP A 69  
AA3 1 2 N VAL A 36  ? N VAL A 15  O PHE A 133 ? O PHE A 112 
AA3 2 3 N ASP A 142 ? N ASP A 121 O ILE A 206 ? O ILE A 185 
AA3 3 4 N LEU A 207 ? N LEU A 186 O LEU A 269 ? O LEU A 248 
AA3 4 5 O PHE A 272 ? O PHE A 251 N PHE A 236 ? N PHE A 215 
AA3 5 6 N TYR A 237 ? N TYR A 216 O ILE A 248 ? O ILE A 227 
AA4 1 2 N LEU A 172 ? N LEU A 151 O ARG A 314 ? O ARG A 293 
AA4 2 3 O PHE A 313 ? O PHE A 292 N VAL A 287 ? N VAL A 266 
AA4 3 4 O LEU A 294 ? O LEU A 273 N GLU A 220 ? N GLU A 199 
AA4 4 5 N ILE A 221 ? N ILE A 200 O VAL A 260 ? O VAL A 239 
AA5 1 2 N ILE A 319 ? N ILE A 298 O TYR A 378 ? O TYR A 357 
AA5 2 3 N GLY A 377 ? N GLY A 356 O VAL A 388 ? O VAL A 367 
AA5 3 4 N PRO A 387 ? N PRO A 366 O GLY A 412 ? O GLY A 391 
AA6 1 2 O GLU A 355 ? O GLU A 334 N VAL A 330 ? N VAL A 309 
AA6 2 3 N PHE A 331 ? N PHE A 310 O ASN A 671 ? O ASN A 650 
AA7 1 2 N GLU A 433 ? N GLU A 412 O LEU A 451 ? O LEU A 430 
AA7 2 3 N ILE A 452 ? N ILE A 431 O LEU A 483 ? O LEU A 462 
AA8 1 2 N VAL A 438 ? N VAL A 417 O TYR A 445 ? O TYR A 424 
AA9 1 2 N SER A 498 ? N SER A 477 O LEU A 511 ? O LEU A 490 
AA9 2 3 N MET A 512 ? N MET A 491 O LEU A 590 ? O LEU A 569 
AB1 1 2 N LYS A 595 ? N LYS A 574 O ARG A 603 ? O ARG A 582 
AB2 1 2 N LEU A 615 ? N LEU A 594 O ASP A 618 ? O ASP A 597 
AB2 2 3 N ILE A 621 ? N ILE A 600 O THR A 651 ? O THR A 630 
# 
_pdbx_entry_details.entry_id                   9DOL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
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 A HOH 1105 ? ? O A HOH 1138 ? ? 1.80 
2  1 O A HOH 1109 ? ? O A HOH 1117 ? ? 1.83 
3  1 O A HOH 1005 ? ? O A HOH 1167 ? ? 1.97 
4  1 O A HOH 996  ? ? O A HOH 1055 ? ? 1.99 
5  1 O A HOH 907  ? ? O A HOH 989  ? ? 2.03 
6  1 O A HOH 1033 ? ? O A HOH 1050 ? ? 2.06 
7  1 O A HOH 1005 ? ? O A HOH 1147 ? ? 2.06 
8  1 O A HOH 1100 ? ? O A HOH 1148 ? ? 2.13 
9  1 O A HOH 847  ? ? O A HOH 981  ? ? 2.14 
10 1 O A HOH 1056 ? ? O A HOH 1121 ? ? 2.17 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 2   ? ? -144.95 -40.66  
2  1 TYR A 11  ? ? -44.95  107.34  
3  1 ASP A 55  ? ? 80.07   46.64   
4  1 THR A 86  ? ? -116.32 -163.83 
5  1 GLU A 101 ? ? -66.55  -88.52  
6  1 SER A 119 ? ? -160.12 116.01  
7  1 PHE A 222 ? ? -131.78 -127.22 
8  1 ALA A 277 ? ? 176.65  170.15  
9  1 ASP A 279 ? ? 82.70   -9.20   
10 1 CYS A 313 ? ? -173.96 -176.70 
11 1 GLU A 384 ? ? -77.27  26.96   
12 1 LEU A 385 ? ? -130.68 -68.50  
13 1 GLN A 455 ? ? 73.20   -45.84  
14 1 ALA A 458 ? ? -1.93   88.56   
15 1 LEU A 594 ? ? -118.99 75.72   
16 1 ASP A 595 ? ? 53.82   -124.38 
17 1 ILE A 635 ? ? -141.74 -18.05  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_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[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 338.3037 10.7853 67.5758  0.2097 ? 0.0438  ? -0.0070 ? 0.2384 ? -0.1271 ? 0.3687 ? 4.6606 ? 
-2.5387 ? 1.5680 ? 3.3720 ? -1.7757 ? 6.4765 ? 0.1974  ? 0.2809  ? 0.2712  ? -0.2657 ? -0.0942 ? 0.1393  ? -0.4371 ? 0.0082  ? 
-0.1048 ? 
2 'X-RAY DIFFRACTION' ? refined 357.0611 -3.0900 87.1952  0.1882 ? -0.0177 ? 0.0881  ? 0.3550 ? 0.0424  ? 0.2387 ? 3.7254 ? 
-0.7875 ? 1.5285 ? 0.9440 ? -0.1899 ? 1.5449 ? -0.0745 ? -0.8374 ? -0.2254 ? 0.0767  ? 0.0695  ? 0.1465  ? 0.0740  ? -0.4157 ? 
0.0092  ? 
3 'X-RAY DIFFRACTION' ? refined 390.9500 -6.8661 101.4121 0.2925 ? 0.0141  ? 0.0479  ? 0.3844 ? 0.0693  ? 0.1931 ? 4.0934 ? 
-0.0953 ? 2.3584 ? 0.8115 ? 0.2116  ? 2.3604 ? 0.1182  ? -0.7299 ? -0.3092 ? 0.3008  ? 0.0756  ? -0.1633 ? 0.3098  ? -0.0994 ? 
-0.2172 ? 
4 'X-RAY DIFFRACTION' ? refined 406.6226 -6.1838 90.8916  0.1484 ? 0.0351  ? 0.0014  ? 0.1049 ? 0.0388  ? 0.1322 ? 3.9885 ? 
-0.1013 ? 0.7601 ? 1.1109 ? 0.1529  ? 1.9706 ? -0.0566 ? -0.2082 ? -0.1836 ? 0.2246  ? 0.0699  ? -0.1584 ? 0.1045  ? 0.1054  ? 
0.0113  ? 
5 'X-RAY DIFFRACTION' ? refined 404.8930 -3.6712 100.7721 0.3209 ? 0.0195  ? -0.0219 ? 0.3592 ? 0.0203  ? 0.2301 ? 5.1202 ? 0.5176 
? 0.7597 ? 1.0472 ? 0.2236  ? 1.2757 ? -0.0411 ? -0.7927 ? -0.2601 ? 0.3982  ? 0.0611  ? -0.2103 ? 0.0135  ? 0.0679  ? -0.0270 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 75 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 76 through 282 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 283 through 359 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 360 through 601 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 602 through 668 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1176 ? 6.39 . 
2 1 O ? A HOH 1177 ? 6.54 . 
3 1 O ? A HOH 1178 ? 7.13 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -20 ? A MET 1   
2  1 Y 1 A GLY -19 ? A GLY 2   
3  1 Y 1 A HIS -18 ? A HIS 3   
4  1 Y 1 A HIS -17 ? A HIS 4   
5  1 Y 1 A HIS -16 ? A HIS 5   
6  1 Y 1 A HIS -15 ? A HIS 6   
7  1 Y 1 A HIS -14 ? A HIS 7   
8  1 Y 1 A HIS -13 ? A HIS 8   
9  1 Y 1 A HIS -12 ? A HIS 9   
10 1 Y 1 A HIS -11 ? A HIS 10  
11 1 Y 1 A HIS -10 ? A HIS 11  
12 1 Y 1 A HIS -9  ? A HIS 12  
13 1 Y 1 A SER -8  ? A SER 13  
14 1 Y 1 A SER -7  ? A SER 14  
15 1 Y 1 A GLY -6  ? A GLY 15  
16 1 Y 1 A HIS -5  ? A HIS 16  
17 1 Y 1 A ILE -4  ? A ILE 17  
18 1 Y 1 A GLU -3  ? A GLU 18  
19 1 Y 1 A GLY -2  ? A GLY 19  
20 1 Y 1 A ARG -1  ? A ARG 20  
21 1 Y 1 A HIS 0   ? A HIS 21  
22 1 Y 1 A GLN 340 ? A GLN 361 
23 1 Y 1 A TYR 341 ? A TYR 362 
24 1 Y 1 A LEU 342 ? A LEU 363 
25 1 Y 1 A ASN 343 ? A ASN 364 
26 1 Y 1 A ARG 344 ? A ARG 365 
27 1 Y 1 A GLY 345 ? A GLY 366 
28 1 Y 1 A ASP 374 ? A ASP 395 
29 1 Y 1 A GLY 375 ? A GLY 396 
30 1 Y 1 A ASN 376 ? A ASN 397 
31 1 Y 1 A LEU 377 ? A LEU 398 
32 1 Y 1 A LYS 378 ? A LYS 399 
33 1 Y 1 A ASP 379 ? A ASP 400 
34 1 Y 1 A PHE 399 ? A PHE 420 
35 1 Y 1 A GLU 400 ? A GLU 421 
36 1 Y 1 A SER 401 ? A SER 422 
37 1 Y 1 A SER 522 ? A SER 543 
38 1 Y 1 A SER 523 ? A SER 544 
39 1 Y 1 A ARG 668 ? A ARG 689 
40 1 Y 1 A SER 669 ? A SER 690 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1A8O C4   C  Y N 1   
A1A8O C6   C  Y N 2   
A1A8O C13  C  N N 3   
A1A8O C20  C  N N 4   
A1A8O C21  C  N N 5   
A1A8O C8   C  Y N 6   
A1A8O C16  C  N N 7   
A1A8O O17  O  N N 8   
A1A8O C19  C  N N 9   
A1A8O C26  C  Y N 10  
A1A8O C1   C  Y N 11  
A1A8O C10  C  N N 12  
A1A8O C11  C  N N 13  
A1A8O C12  C  N N 14  
A1A8O C14  C  N N 15  
A1A8O C15  C  N S 16  
A1A8O C2   C  Y N 17  
A1A8O C22  C  N N 18  
A1A8O C24  C  Y N 19  
A1A8O C25  C  Y N 20  
A1A8O C27  C  Y N 21  
A1A8O C28  C  Y N 22  
A1A8O C29  C  Y N 23  
A1A8O C3   C  Y N 24  
A1A8O C30  C  Y N 25  
A1A8O C5   C  Y N 26  
A1A8O N18  N  N N 27  
A1A8O N23  N  N N 28  
A1A8O N31  N  Y N 29  
A1A8O N7   N  Y N 30  
A1A8O N9   N  N N 31  
A1A8O CL1  CL N N 32  
A1A8O CL2  CL N N 33  
A1A8O H1   H  N N 34  
A1A8O H2   H  N N 35  
A1A8O H3   H  N N 36  
A1A8O H4   H  N N 37  
A1A8O H5   H  N N 38  
A1A8O H6   H  N N 39  
A1A8O H7   H  N N 40  
A1A8O H8   H  N N 41  
A1A8O H9   H  N N 42  
A1A8O H10  H  N N 43  
A1A8O H11  H  N N 44  
A1A8O H12  H  N N 45  
A1A8O H13  H  N N 46  
A1A8O H14  H  N N 47  
A1A8O H15  H  N N 48  
A1A8O H16  H  N N 49  
A1A8O H17  H  N N 50  
A1A8O H18  H  N N 51  
A1A8O H19  H  N N 52  
A1A8O H20  H  N N 53  
A1A8O H21  H  N N 54  
A1A8O H22  H  N N 55  
A1A8O H23  H  N N 56  
A1A8O H24  H  N N 57  
A1A8O H25  H  N N 58  
A1A8O H26  H  N N 59  
A1A8O H27  H  N N 60  
ALA   N    N  N N 61  
ALA   CA   C  N S 62  
ALA   C    C  N N 63  
ALA   O    O  N N 64  
ALA   CB   C  N N 65  
ALA   OXT  O  N N 66  
ALA   H    H  N N 67  
ALA   H2   H  N N 68  
ALA   HA   H  N N 69  
ALA   HB1  H  N N 70  
ALA   HB2  H  N N 71  
ALA   HB3  H  N N 72  
ALA   HXT  H  N N 73  
ARG   N    N  N N 74  
ARG   CA   C  N S 75  
ARG   C    C  N N 76  
ARG   O    O  N N 77  
ARG   CB   C  N N 78  
ARG   CG   C  N N 79  
ARG   CD   C  N N 80  
ARG   NE   N  N N 81  
ARG   CZ   C  N N 82  
ARG   NH1  N  N N 83  
ARG   NH2  N  N N 84  
ARG   OXT  O  N N 85  
ARG   H    H  N N 86  
ARG   H2   H  N N 87  
ARG   HA   H  N N 88  
ARG   HB2  H  N N 89  
ARG   HB3  H  N N 90  
ARG   HG2  H  N N 91  
ARG   HG3  H  N N 92  
ARG   HD2  H  N N 93  
ARG   HD3  H  N N 94  
ARG   HE   H  N N 95  
ARG   HH11 H  N N 96  
ARG   HH12 H  N N 97  
ARG   HH21 H  N N 98  
ARG   HH22 H  N N 99  
ARG   HXT  H  N N 100 
ASN   N    N  N N 101 
ASN   CA   C  N S 102 
ASN   C    C  N N 103 
ASN   O    O  N N 104 
ASN   CB   C  N N 105 
ASN   CG   C  N N 106 
ASN   OD1  O  N N 107 
ASN   ND2  N  N N 108 
ASN   OXT  O  N N 109 
ASN   H    H  N N 110 
ASN   H2   H  N N 111 
ASN   HA   H  N N 112 
ASN   HB2  H  N N 113 
ASN   HB3  H  N N 114 
ASN   HD21 H  N N 115 
ASN   HD22 H  N N 116 
ASN   HXT  H  N N 117 
ASP   N    N  N N 118 
ASP   CA   C  N S 119 
ASP   C    C  N N 120 
ASP   O    O  N N 121 
ASP   CB   C  N N 122 
ASP   CG   C  N N 123 
ASP   OD1  O  N N 124 
ASP   OD2  O  N N 125 
ASP   OXT  O  N N 126 
ASP   H    H  N N 127 
ASP   H2   H  N N 128 
ASP   HA   H  N N 129 
ASP   HB2  H  N N 130 
ASP   HB3  H  N N 131 
ASP   HD2  H  N N 132 
ASP   HXT  H  N N 133 
CA    CA   CA N N 134 
CYS   N    N  N N 135 
CYS   CA   C  N R 136 
CYS   C    C  N N 137 
CYS   O    O  N N 138 
CYS   CB   C  N N 139 
CYS   SG   S  N N 140 
CYS   OXT  O  N N 141 
CYS   H    H  N N 142 
CYS   H2   H  N N 143 
CYS   HA   H  N N 144 
CYS   HB2  H  N N 145 
CYS   HB3  H  N N 146 
CYS   HG   H  N N 147 
CYS   HXT  H  N N 148 
GLN   N    N  N N 149 
GLN   CA   C  N S 150 
GLN   C    C  N N 151 
GLN   O    O  N N 152 
GLN   CB   C  N N 153 
GLN   CG   C  N N 154 
GLN   CD   C  N N 155 
GLN   OE1  O  N N 156 
GLN   NE2  N  N N 157 
GLN   OXT  O  N N 158 
GLN   H    H  N N 159 
GLN   H2   H  N N 160 
GLN   HA   H  N N 161 
GLN   HB2  H  N N 162 
GLN   HB3  H  N N 163 
GLN   HG2  H  N N 164 
GLN   HG3  H  N N 165 
GLN   HE21 H  N N 166 
GLN   HE22 H  N N 167 
GLN   HXT  H  N N 168 
GLU   N    N  N N 169 
GLU   CA   C  N S 170 
GLU   C    C  N N 171 
GLU   O    O  N N 172 
GLU   CB   C  N N 173 
GLU   CG   C  N N 174 
GLU   CD   C  N N 175 
GLU   OE1  O  N N 176 
GLU   OE2  O  N N 177 
GLU   OXT  O  N N 178 
GLU   H    H  N N 179 
GLU   H2   H  N N 180 
GLU   HA   H  N N 181 
GLU   HB2  H  N N 182 
GLU   HB3  H  N N 183 
GLU   HG2  H  N N 184 
GLU   HG3  H  N N 185 
GLU   HE2  H  N N 186 
GLU   HXT  H  N N 187 
GLY   N    N  N N 188 
GLY   CA   C  N N 189 
GLY   C    C  N N 190 
GLY   O    O  N N 191 
GLY   OXT  O  N N 192 
GLY   H    H  N N 193 
GLY   H2   H  N N 194 
GLY   HA2  H  N N 195 
GLY   HA3  H  N N 196 
GLY   HXT  H  N N 197 
HIS   N    N  N N 198 
HIS   CA   C  N S 199 
HIS   C    C  N N 200 
HIS   O    O  N N 201 
HIS   CB   C  N N 202 
HIS   CG   C  Y N 203 
HIS   ND1  N  Y N 204 
HIS   CD2  C  Y N 205 
HIS   CE1  C  Y N 206 
HIS   NE2  N  Y N 207 
HIS   OXT  O  N N 208 
HIS   H    H  N N 209 
HIS   H2   H  N N 210 
HIS   HA   H  N N 211 
HIS   HB2  H  N N 212 
HIS   HB3  H  N N 213 
HIS   HD1  H  N N 214 
HIS   HD2  H  N N 215 
HIS   HE1  H  N N 216 
HIS   HE2  H  N N 217 
HIS   HXT  H  N N 218 
HOH   O    O  N N 219 
HOH   H1   H  N N 220 
HOH   H2   H  N N 221 
ILE   N    N  N N 222 
ILE   CA   C  N S 223 
ILE   C    C  N N 224 
ILE   O    O  N N 225 
ILE   CB   C  N S 226 
ILE   CG1  C  N N 227 
ILE   CG2  C  N N 228 
ILE   CD1  C  N N 229 
ILE   OXT  O  N N 230 
ILE   H    H  N N 231 
ILE   H2   H  N N 232 
ILE   HA   H  N N 233 
ILE   HB   H  N N 234 
ILE   HG12 H  N N 235 
ILE   HG13 H  N N 236 
ILE   HG21 H  N N 237 
ILE   HG22 H  N N 238 
ILE   HG23 H  N N 239 
ILE   HD11 H  N N 240 
ILE   HD12 H  N N 241 
ILE   HD13 H  N N 242 
ILE   HXT  H  N N 243 
LEU   N    N  N N 244 
LEU   CA   C  N S 245 
LEU   C    C  N N 246 
LEU   O    O  N N 247 
LEU   CB   C  N N 248 
LEU   CG   C  N N 249 
LEU   CD1  C  N N 250 
LEU   CD2  C  N N 251 
LEU   OXT  O  N N 252 
LEU   H    H  N N 253 
LEU   H2   H  N N 254 
LEU   HA   H  N N 255 
LEU   HB2  H  N N 256 
LEU   HB3  H  N N 257 
LEU   HG   H  N N 258 
LEU   HD11 H  N N 259 
LEU   HD12 H  N N 260 
LEU   HD13 H  N N 261 
LEU   HD21 H  N N 262 
LEU   HD22 H  N N 263 
LEU   HD23 H  N N 264 
LEU   HXT  H  N N 265 
LYS   N    N  N N 266 
LYS   CA   C  N S 267 
LYS   C    C  N N 268 
LYS   O    O  N N 269 
LYS   CB   C  N N 270 
LYS   CG   C  N N 271 
LYS   CD   C  N N 272 
LYS   CE   C  N N 273 
LYS   NZ   N  N N 274 
LYS   OXT  O  N N 275 
LYS   H    H  N N 276 
LYS   H2   H  N N 277 
LYS   HA   H  N N 278 
LYS   HB2  H  N N 279 
LYS   HB3  H  N N 280 
LYS   HG2  H  N N 281 
LYS   HG3  H  N N 282 
LYS   HD2  H  N N 283 
LYS   HD3  H  N N 284 
LYS   HE2  H  N N 285 
LYS   HE3  H  N N 286 
LYS   HZ1  H  N N 287 
LYS   HZ2  H  N N 288 
LYS   HZ3  H  N N 289 
LYS   HXT  H  N N 290 
MET   N    N  N N 291 
MET   CA   C  N S 292 
MET   C    C  N N 293 
MET   O    O  N N 294 
MET   CB   C  N N 295 
MET   CG   C  N N 296 
MET   SD   S  N N 297 
MET   CE   C  N N 298 
MET   OXT  O  N N 299 
MET   H    H  N N 300 
MET   H2   H  N N 301 
MET   HA   H  N N 302 
MET   HB2  H  N N 303 
MET   HB3  H  N N 304 
MET   HG2  H  N N 305 
MET   HG3  H  N N 306 
MET   HE1  H  N N 307 
MET   HE2  H  N N 308 
MET   HE3  H  N N 309 
MET   HXT  H  N N 310 
PHE   N    N  N N 311 
PHE   CA   C  N S 312 
PHE   C    C  N N 313 
PHE   O    O  N N 314 
PHE   CB   C  N N 315 
PHE   CG   C  Y N 316 
PHE   CD1  C  Y N 317 
PHE   CD2  C  Y N 318 
PHE   CE1  C  Y N 319 
PHE   CE2  C  Y N 320 
PHE   CZ   C  Y N 321 
PHE   OXT  O  N N 322 
PHE   H    H  N N 323 
PHE   H2   H  N N 324 
PHE   HA   H  N N 325 
PHE   HB2  H  N N 326 
PHE   HB3  H  N N 327 
PHE   HD1  H  N N 328 
PHE   HD2  H  N N 329 
PHE   HE1  H  N N 330 
PHE   HE2  H  N N 331 
PHE   HZ   H  N N 332 
PHE   HXT  H  N N 333 
PRO   N    N  N N 334 
PRO   CA   C  N S 335 
PRO   C    C  N N 336 
PRO   O    O  N N 337 
PRO   CB   C  N N 338 
PRO   CG   C  N N 339 
PRO   CD   C  N N 340 
PRO   OXT  O  N N 341 
PRO   H    H  N N 342 
PRO   HA   H  N N 343 
PRO   HB2  H  N N 344 
PRO   HB3  H  N N 345 
PRO   HG2  H  N N 346 
PRO   HG3  H  N N 347 
PRO   HD2  H  N N 348 
PRO   HD3  H  N N 349 
PRO   HXT  H  N N 350 
SER   N    N  N N 351 
SER   CA   C  N S 352 
SER   C    C  N N 353 
SER   O    O  N N 354 
SER   CB   C  N N 355 
SER   OG   O  N N 356 
SER   OXT  O  N N 357 
SER   H    H  N N 358 
SER   H2   H  N N 359 
SER   HA   H  N N 360 
SER   HB2  H  N N 361 
SER   HB3  H  N N 362 
SER   HG   H  N N 363 
SER   HXT  H  N N 364 
THR   N    N  N N 365 
THR   CA   C  N S 366 
THR   C    C  N N 367 
THR   O    O  N N 368 
THR   CB   C  N R 369 
THR   OG1  O  N N 370 
THR   CG2  C  N N 371 
THR   OXT  O  N N 372 
THR   H    H  N N 373 
THR   H2   H  N N 374 
THR   HA   H  N N 375 
THR   HB   H  N N 376 
THR   HG1  H  N N 377 
THR   HG21 H  N N 378 
THR   HG22 H  N N 379 
THR   HG23 H  N N 380 
THR   HXT  H  N N 381 
TRP   N    N  N N 382 
TRP   CA   C  N S 383 
TRP   C    C  N N 384 
TRP   O    O  N N 385 
TRP   CB   C  N N 386 
TRP   CG   C  Y N 387 
TRP   CD1  C  Y N 388 
TRP   CD2  C  Y N 389 
TRP   NE1  N  Y N 390 
TRP   CE2  C  Y N 391 
TRP   CE3  C  Y N 392 
TRP   CZ2  C  Y N 393 
TRP   CZ3  C  Y N 394 
TRP   CH2  C  Y N 395 
TRP   OXT  O  N N 396 
TRP   H    H  N N 397 
TRP   H2   H  N N 398 
TRP   HA   H  N N 399 
TRP   HB2  H  N N 400 
TRP   HB3  H  N N 401 
TRP   HD1  H  N N 402 
TRP   HE1  H  N N 403 
TRP   HE3  H  N N 404 
TRP   HZ2  H  N N 405 
TRP   HZ3  H  N N 406 
TRP   HH2  H  N N 407 
TRP   HXT  H  N N 408 
TYR   N    N  N N 409 
TYR   CA   C  N S 410 
TYR   C    C  N N 411 
TYR   O    O  N N 412 
TYR   CB   C  N N 413 
TYR   CG   C  Y N 414 
TYR   CD1  C  Y N 415 
TYR   CD2  C  Y N 416 
TYR   CE1  C  Y N 417 
TYR   CE2  C  Y N 418 
TYR   CZ   C  Y N 419 
TYR   OH   O  N N 420 
TYR   OXT  O  N N 421 
TYR   H    H  N N 422 
TYR   H2   H  N N 423 
TYR   HA   H  N N 424 
TYR   HB2  H  N N 425 
TYR   HB3  H  N N 426 
TYR   HD1  H  N N 427 
TYR   HD2  H  N N 428 
TYR   HE1  H  N N 429 
TYR   HE2  H  N N 430 
TYR   HH   H  N N 431 
TYR   HXT  H  N N 432 
VAL   N    N  N N 433 
VAL   CA   C  N S 434 
VAL   C    C  N N 435 
VAL   O    O  N N 436 
VAL   CB   C  N N 437 
VAL   CG1  C  N N 438 
VAL   CG2  C  N N 439 
VAL   OXT  O  N N 440 
VAL   H    H  N N 441 
VAL   H2   H  N N 442 
VAL   HA   H  N N 443 
VAL   HB   H  N N 444 
VAL   HG11 H  N N 445 
VAL   HG12 H  N N 446 
VAL   HG13 H  N N 447 
VAL   HG21 H  N N 448 
VAL   HG22 H  N N 449 
VAL   HG23 H  N N 450 
VAL   HXT  H  N N 451 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1A8O C21 C22  sing N N 1   
A1A8O C21 C20  sing N N 2   
A1A8O C22 N18  sing N N 3   
A1A8O C20 C19  sing N N 4   
A1A8O N18 C19  sing N N 5   
A1A8O N18 C16  sing N N 6   
A1A8O O17 C16  doub N N 7   
A1A8O C16 C15  sing N N 8   
A1A8O N23 C15  sing N N 9   
A1A8O C15 C12  sing N N 10  
A1A8O C12 C13  sing N N 11  
A1A8O C12 C11  sing N N 12  
A1A8O C13 C14  sing N N 13  
A1A8O C11 C10  sing N N 14  
A1A8O C14 N9   sing N N 15  
A1A8O C10 N9   sing N N 16  
A1A8O N9  C8   sing N N 17  
A1A8O C8  N7   doub Y N 18  
A1A8O C8  C3   sing Y N 19  
A1A8O C2  C3   sing Y N 20  
A1A8O C2  C1   doub Y N 21  
A1A8O N7  C6   sing Y N 22  
A1A8O C3  C4   doub Y N 23  
A1A8O C1  C25  sing Y N 24  
A1A8O C6  C5   doub Y N 25  
A1A8O C4  C5   sing Y N 26  
A1A8O C4  C24  sing Y N 27  
A1A8O C25 C24  doub Y N 28  
A1A8O C24 C26  sing N N 29  
A1A8O CL2 C27  sing N N 30  
A1A8O C26 C27  doub Y N 31  
A1A8O C26 N31  sing Y N 32  
A1A8O C27 C28  sing Y N 33  
A1A8O N31 C30  doub Y N 34  
A1A8O C28 C29  doub Y N 35  
A1A8O C30 C29  sing Y N 36  
A1A8O C29 CL1  sing N N 37  
A1A8O C6  H1   sing N N 38  
A1A8O C13 H2   sing N N 39  
A1A8O C13 H3   sing N N 40  
A1A8O C20 H4   sing N N 41  
A1A8O C20 H5   sing N N 42  
A1A8O C21 H6   sing N N 43  
A1A8O C21 H7   sing N N 44  
A1A8O C19 H8   sing N N 45  
A1A8O C19 H9   sing N N 46  
A1A8O C1  H10  sing N N 47  
A1A8O C10 H11  sing N N 48  
A1A8O C10 H12  sing N N 49  
A1A8O C11 H13  sing N N 50  
A1A8O C11 H14  sing N N 51  
A1A8O C12 H15  sing N N 52  
A1A8O C14 H16  sing N N 53  
A1A8O C14 H17  sing N N 54  
A1A8O C15 H18  sing N N 55  
A1A8O C2  H19  sing N N 56  
A1A8O C22 H20  sing N N 57  
A1A8O C22 H21  sing N N 58  
A1A8O C25 H22  sing N N 59  
A1A8O C28 H23  sing N N 60  
A1A8O C30 H24  sing N N 61  
A1A8O C5  H25  sing N N 62  
A1A8O N23 H26  sing N N 63  
A1A8O N23 H27  sing N N 64  
ALA   N   CA   sing N N 65  
ALA   N   H    sing N N 66  
ALA   N   H2   sing N N 67  
ALA   CA  C    sing N N 68  
ALA   CA  CB   sing N N 69  
ALA   CA  HA   sing N N 70  
ALA   C   O    doub N N 71  
ALA   C   OXT  sing N N 72  
ALA   CB  HB1  sing N N 73  
ALA   CB  HB2  sing N N 74  
ALA   CB  HB3  sing N N 75  
ALA   OXT HXT  sing N N 76  
ARG   N   CA   sing N N 77  
ARG   N   H    sing N N 78  
ARG   N   H2   sing N N 79  
ARG   CA  C    sing N N 80  
ARG   CA  CB   sing N N 81  
ARG   CA  HA   sing N N 82  
ARG   C   O    doub N N 83  
ARG   C   OXT  sing N N 84  
ARG   CB  CG   sing N N 85  
ARG   CB  HB2  sing N N 86  
ARG   CB  HB3  sing N N 87  
ARG   CG  CD   sing N N 88  
ARG   CG  HG2  sing N N 89  
ARG   CG  HG3  sing N N 90  
ARG   CD  NE   sing N N 91  
ARG   CD  HD2  sing N N 92  
ARG   CD  HD3  sing N N 93  
ARG   NE  CZ   sing N N 94  
ARG   NE  HE   sing N N 95  
ARG   CZ  NH1  sing N N 96  
ARG   CZ  NH2  doub N N 97  
ARG   NH1 HH11 sing N N 98  
ARG   NH1 HH12 sing N N 99  
ARG   NH2 HH21 sing N N 100 
ARG   NH2 HH22 sing N N 101 
ARG   OXT HXT  sing N N 102 
ASN   N   CA   sing N N 103 
ASN   N   H    sing N N 104 
ASN   N   H2   sing N N 105 
ASN   CA  C    sing N N 106 
ASN   CA  CB   sing N N 107 
ASN   CA  HA   sing N N 108 
ASN   C   O    doub N N 109 
ASN   C   OXT  sing N N 110 
ASN   CB  CG   sing N N 111 
ASN   CB  HB2  sing N N 112 
ASN   CB  HB3  sing N N 113 
ASN   CG  OD1  doub N N 114 
ASN   CG  ND2  sing N N 115 
ASN   ND2 HD21 sing N N 116 
ASN   ND2 HD22 sing N N 117 
ASN   OXT HXT  sing N N 118 
ASP   N   CA   sing N N 119 
ASP   N   H    sing N N 120 
ASP   N   H2   sing N N 121 
ASP   CA  C    sing N N 122 
ASP   CA  CB   sing N N 123 
ASP   CA  HA   sing N N 124 
ASP   C   O    doub N N 125 
ASP   C   OXT  sing N N 126 
ASP   CB  CG   sing N N 127 
ASP   CB  HB2  sing N N 128 
ASP   CB  HB3  sing N N 129 
ASP   CG  OD1  doub N N 130 
ASP   CG  OD2  sing N N 131 
ASP   OD2 HD2  sing N N 132 
ASP   OXT HXT  sing N N 133 
CYS   N   CA   sing N N 134 
CYS   N   H    sing N N 135 
CYS   N   H2   sing N N 136 
CYS   CA  C    sing N N 137 
CYS   CA  CB   sing N N 138 
CYS   CA  HA   sing N N 139 
CYS   C   O    doub N N 140 
CYS   C   OXT  sing N N 141 
CYS   CB  SG   sing N N 142 
CYS   CB  HB2  sing N N 143 
CYS   CB  HB3  sing N N 144 
CYS   SG  HG   sing N N 145 
CYS   OXT HXT  sing N N 146 
GLN   N   CA   sing N N 147 
GLN   N   H    sing N N 148 
GLN   N   H2   sing N N 149 
GLN   CA  C    sing N N 150 
GLN   CA  CB   sing N N 151 
GLN   CA  HA   sing N N 152 
GLN   C   O    doub N N 153 
GLN   C   OXT  sing N N 154 
GLN   CB  CG   sing N N 155 
GLN   CB  HB2  sing N N 156 
GLN   CB  HB3  sing N N 157 
GLN   CG  CD   sing N N 158 
GLN   CG  HG2  sing N N 159 
GLN   CG  HG3  sing N N 160 
GLN   CD  OE1  doub N N 161 
GLN   CD  NE2  sing N N 162 
GLN   NE2 HE21 sing N N 163 
GLN   NE2 HE22 sing N N 164 
GLN   OXT HXT  sing N N 165 
GLU   N   CA   sing N N 166 
GLU   N   H    sing N N 167 
GLU   N   H2   sing N N 168 
GLU   CA  C    sing N N 169 
GLU   CA  CB   sing N N 170 
GLU   CA  HA   sing N N 171 
GLU   C   O    doub N N 172 
GLU   C   OXT  sing N N 173 
GLU   CB  CG   sing N N 174 
GLU   CB  HB2  sing N N 175 
GLU   CB  HB3  sing N N 176 
GLU   CG  CD   sing N N 177 
GLU   CG  HG2  sing N N 178 
GLU   CG  HG3  sing N N 179 
GLU   CD  OE1  doub N N 180 
GLU   CD  OE2  sing N N 181 
GLU   OE2 HE2  sing N N 182 
GLU   OXT HXT  sing N N 183 
GLY   N   CA   sing N N 184 
GLY   N   H    sing N N 185 
GLY   N   H2   sing N N 186 
GLY   CA  C    sing N N 187 
GLY   CA  HA2  sing N N 188 
GLY   CA  HA3  sing N N 189 
GLY   C   O    doub N N 190 
GLY   C   OXT  sing N N 191 
GLY   OXT HXT  sing N N 192 
HIS   N   CA   sing N N 193 
HIS   N   H    sing N N 194 
HIS   N   H2   sing N N 195 
HIS   CA  C    sing N N 196 
HIS   CA  CB   sing N N 197 
HIS   CA  HA   sing N N 198 
HIS   C   O    doub N N 199 
HIS   C   OXT  sing N N 200 
HIS   CB  CG   sing N N 201 
HIS   CB  HB2  sing N N 202 
HIS   CB  HB3  sing N N 203 
HIS   CG  ND1  sing Y N 204 
HIS   CG  CD2  doub Y N 205 
HIS   ND1 CE1  doub Y N 206 
HIS   ND1 HD1  sing N N 207 
HIS   CD2 NE2  sing Y N 208 
HIS   CD2 HD2  sing N N 209 
HIS   CE1 NE2  sing Y N 210 
HIS   CE1 HE1  sing N N 211 
HIS   NE2 HE2  sing N N 212 
HIS   OXT HXT  sing N N 213 
HOH   O   H1   sing N N 214 
HOH   O   H2   sing N N 215 
ILE   N   CA   sing N N 216 
ILE   N   H    sing N N 217 
ILE   N   H2   sing N N 218 
ILE   CA  C    sing N N 219 
ILE   CA  CB   sing N N 220 
ILE   CA  HA   sing N N 221 
ILE   C   O    doub N N 222 
ILE   C   OXT  sing N N 223 
ILE   CB  CG1  sing N N 224 
ILE   CB  CG2  sing N N 225 
ILE   CB  HB   sing N N 226 
ILE   CG1 CD1  sing N N 227 
ILE   CG1 HG12 sing N N 228 
ILE   CG1 HG13 sing N N 229 
ILE   CG2 HG21 sing N N 230 
ILE   CG2 HG22 sing N N 231 
ILE   CG2 HG23 sing N N 232 
ILE   CD1 HD11 sing N N 233 
ILE   CD1 HD12 sing N N 234 
ILE   CD1 HD13 sing N N 235 
ILE   OXT HXT  sing N N 236 
LEU   N   CA   sing N N 237 
LEU   N   H    sing N N 238 
LEU   N   H2   sing N N 239 
LEU   CA  C    sing N N 240 
LEU   CA  CB   sing N N 241 
LEU   CA  HA   sing N N 242 
LEU   C   O    doub N N 243 
LEU   C   OXT  sing N N 244 
LEU   CB  CG   sing N N 245 
LEU   CB  HB2  sing N N 246 
LEU   CB  HB3  sing N N 247 
LEU   CG  CD1  sing N N 248 
LEU   CG  CD2  sing N N 249 
LEU   CG  HG   sing N N 250 
LEU   CD1 HD11 sing N N 251 
LEU   CD1 HD12 sing N N 252 
LEU   CD1 HD13 sing N N 253 
LEU   CD2 HD21 sing N N 254 
LEU   CD2 HD22 sing N N 255 
LEU   CD2 HD23 sing N N 256 
LEU   OXT HXT  sing N N 257 
LYS   N   CA   sing N N 258 
LYS   N   H    sing N N 259 
LYS   N   H2   sing N N 260 
LYS   CA  C    sing N N 261 
LYS   CA  CB   sing N N 262 
LYS   CA  HA   sing N N 263 
LYS   C   O    doub N N 264 
LYS   C   OXT  sing N N 265 
LYS   CB  CG   sing N N 266 
LYS   CB  HB2  sing N N 267 
LYS   CB  HB3  sing N N 268 
LYS   CG  CD   sing N N 269 
LYS   CG  HG2  sing N N 270 
LYS   CG  HG3  sing N N 271 
LYS   CD  CE   sing N N 272 
LYS   CD  HD2  sing N N 273 
LYS   CD  HD3  sing N N 274 
LYS   CE  NZ   sing N N 275 
LYS   CE  HE2  sing N N 276 
LYS   CE  HE3  sing N N 277 
LYS   NZ  HZ1  sing N N 278 
LYS   NZ  HZ2  sing N N 279 
LYS   NZ  HZ3  sing N N 280 
LYS   OXT HXT  sing N N 281 
MET   N   CA   sing N N 282 
MET   N   H    sing N N 283 
MET   N   H2   sing N N 284 
MET   CA  C    sing N N 285 
MET   CA  CB   sing N N 286 
MET   CA  HA   sing N N 287 
MET   C   O    doub N N 288 
MET   C   OXT  sing N N 289 
MET   CB  CG   sing N N 290 
MET   CB  HB2  sing N N 291 
MET   CB  HB3  sing N N 292 
MET   CG  SD   sing N N 293 
MET   CG  HG2  sing N N 294 
MET   CG  HG3  sing N N 295 
MET   SD  CE   sing N N 296 
MET   CE  HE1  sing N N 297 
MET   CE  HE2  sing N N 298 
MET   CE  HE3  sing N N 299 
MET   OXT HXT  sing N N 300 
PHE   N   CA   sing N N 301 
PHE   N   H    sing N N 302 
PHE   N   H2   sing N N 303 
PHE   CA  C    sing N N 304 
PHE   CA  CB   sing N N 305 
PHE   CA  HA   sing N N 306 
PHE   C   O    doub N N 307 
PHE   C   OXT  sing N N 308 
PHE   CB  CG   sing N N 309 
PHE   CB  HB2  sing N N 310 
PHE   CB  HB3  sing N N 311 
PHE   CG  CD1  doub Y N 312 
PHE   CG  CD2  sing Y N 313 
PHE   CD1 CE1  sing Y N 314 
PHE   CD1 HD1  sing N N 315 
PHE   CD2 CE2  doub Y N 316 
PHE   CD2 HD2  sing N N 317 
PHE   CE1 CZ   doub Y N 318 
PHE   CE1 HE1  sing N N 319 
PHE   CE2 CZ   sing Y N 320 
PHE   CE2 HE2  sing N N 321 
PHE   CZ  HZ   sing N N 322 
PHE   OXT HXT  sing N N 323 
PRO   N   CA   sing N N 324 
PRO   N   CD   sing N N 325 
PRO   N   H    sing N N 326 
PRO   CA  C    sing N N 327 
PRO   CA  CB   sing N N 328 
PRO   CA  HA   sing N N 329 
PRO   C   O    doub N N 330 
PRO   C   OXT  sing N N 331 
PRO   CB  CG   sing N N 332 
PRO   CB  HB2  sing N N 333 
PRO   CB  HB3  sing N N 334 
PRO   CG  CD   sing N N 335 
PRO   CG  HG2  sing N N 336 
PRO   CG  HG3  sing N N 337 
PRO   CD  HD2  sing N N 338 
PRO   CD  HD3  sing N N 339 
PRO   OXT HXT  sing N N 340 
SER   N   CA   sing N N 341 
SER   N   H    sing N N 342 
SER   N   H2   sing N N 343 
SER   CA  C    sing N N 344 
SER   CA  CB   sing N N 345 
SER   CA  HA   sing N N 346 
SER   C   O    doub N N 347 
SER   C   OXT  sing N N 348 
SER   CB  OG   sing N N 349 
SER   CB  HB2  sing N N 350 
SER   CB  HB3  sing N N 351 
SER   OG  HG   sing N N 352 
SER   OXT HXT  sing N N 353 
THR   N   CA   sing N N 354 
THR   N   H    sing N N 355 
THR   N   H2   sing N N 356 
THR   CA  C    sing N N 357 
THR   CA  CB   sing N N 358 
THR   CA  HA   sing N N 359 
THR   C   O    doub N N 360 
THR   C   OXT  sing N N 361 
THR   CB  OG1  sing N N 362 
THR   CB  CG2  sing N N 363 
THR   CB  HB   sing N N 364 
THR   OG1 HG1  sing N N 365 
THR   CG2 HG21 sing N N 366 
THR   CG2 HG22 sing N N 367 
THR   CG2 HG23 sing N N 368 
THR   OXT HXT  sing N N 369 
TRP   N   CA   sing N N 370 
TRP   N   H    sing N N 371 
TRP   N   H2   sing N N 372 
TRP   CA  C    sing N N 373 
TRP   CA  CB   sing N N 374 
TRP   CA  HA   sing N N 375 
TRP   C   O    doub N N 376 
TRP   C   OXT  sing N N 377 
TRP   CB  CG   sing N N 378 
TRP   CB  HB2  sing N N 379 
TRP   CB  HB3  sing N N 380 
TRP   CG  CD1  doub Y N 381 
TRP   CG  CD2  sing Y N 382 
TRP   CD1 NE1  sing Y N 383 
TRP   CD1 HD1  sing N N 384 
TRP   CD2 CE2  doub Y N 385 
TRP   CD2 CE3  sing Y N 386 
TRP   NE1 CE2  sing Y N 387 
TRP   NE1 HE1  sing N N 388 
TRP   CE2 CZ2  sing Y N 389 
TRP   CE3 CZ3  doub Y N 390 
TRP   CE3 HE3  sing N N 391 
TRP   CZ2 CH2  doub Y N 392 
TRP   CZ2 HZ2  sing N N 393 
TRP   CZ3 CH2  sing Y N 394 
TRP   CZ3 HZ3  sing N N 395 
TRP   CH2 HH2  sing N N 396 
TRP   OXT HXT  sing N N 397 
TYR   N   CA   sing N N 398 
TYR   N   H    sing N N 399 
TYR   N   H2   sing N N 400 
TYR   CA  C    sing N N 401 
TYR   CA  CB   sing N N 402 
TYR   CA  HA   sing N N 403 
TYR   C   O    doub N N 404 
TYR   C   OXT  sing N N 405 
TYR   CB  CG   sing N N 406 
TYR   CB  HB2  sing N N 407 
TYR   CB  HB3  sing N N 408 
TYR   CG  CD1  doub Y N 409 
TYR   CG  CD2  sing Y N 410 
TYR   CD1 CE1  sing Y N 411 
TYR   CD1 HD1  sing N N 412 
TYR   CD2 CE2  doub Y N 413 
TYR   CD2 HD2  sing N N 414 
TYR   CE1 CZ   doub Y N 415 
TYR   CE1 HE1  sing N N 416 
TYR   CE2 CZ   sing Y N 417 
TYR   CE2 HE2  sing N N 418 
TYR   CZ  OH   sing N N 419 
TYR   OH  HH   sing N N 420 
TYR   OXT HXT  sing N N 421 
VAL   N   CA   sing N N 422 
VAL   N   H    sing N N 423 
VAL   N   H2   sing N N 424 
VAL   CA  C    sing N N 425 
VAL   CA  CB   sing N N 426 
VAL   CA  HA   sing N N 427 
VAL   C   O    doub N N 428 
VAL   C   OXT  sing N N 429 
VAL   CB  CG1  sing N N 430 
VAL   CB  CG2  sing N N 431 
VAL   CB  HB   sing N N 432 
VAL   CG1 HG11 sing N N 433 
VAL   CG1 HG12 sing N N 434 
VAL   CG1 HG13 sing N N 435 
VAL   CG2 HG21 sing N N 436 
VAL   CG2 HG22 sing N N 437 
VAL   CG2 HG23 sing N N 438 
VAL   OXT HXT  sing N N 439 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4N2B 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DOL 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.004972 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001452 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.019588 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.013670 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
CL 
H  
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    . MET   A 1 22  ? 352.168 12.894  77.899  1.00 84.10  ? 1    MET   A N    1 
ATOM   2    C  CA   . MET   A 1 22  ? 351.561 12.741  76.583  1.00 81.44  ? 1    MET   A CA   1 
ATOM   3    C  C    . MET   A 1 22  ? 352.608 12.904  75.483  1.00 92.62  ? 1    MET   A C    1 
ATOM   4    O  O    . MET   A 1 22  ? 352.875 14.019  75.033  1.00 101.99 ? 1    MET   A O    1 
ATOM   5    C  CB   . MET   A 1 22  ? 350.427 13.752  76.396  1.00 76.79  ? 1    MET   A CB   1 
ATOM   6    N  N    . LEU   A 1 23  ? 353.196 11.787  75.051  1.00 72.78  ? 2    LEU   A N    1 
ATOM   7    C  CA   . LEU   A 1 23  ? 354.278 11.828  74.073  1.00 74.04  ? 2    LEU   A CA   1 
ATOM   8    C  C    . LEU   A 1 23  ? 354.241 10.638  73.116  1.00 76.08  ? 2    LEU   A C    1 
ATOM   9    O  O    . LEU   A 1 23  ? 354.482 10.806  71.916  1.00 75.73  ? 2    LEU   A O    1 
ATOM   10   C  CB   . LEU   A 1 23  ? 355.630 11.898  74.789  1.00 68.99  ? 2    LEU   A CB   1 
ATOM   11   N  N    . ARG   A 1 24  ? 353.948 9.438   73.623  1.00 62.50  ? 3    ARG   A N    1 
ATOM   12   C  CA   . ARG   A 1 24  ? 353.821 8.265   72.763  1.00 56.12  ? 3    ARG   A CA   1 
ATOM   13   C  C    . ARG   A 1 24  ? 352.443 8.246   72.111  1.00 47.35  ? 3    ARG   A C    1 
ATOM   14   O  O    . ARG   A 1 24  ? 351.425 8.354   72.801  1.00 49.05  ? 3    ARG   A O    1 
ATOM   15   C  CB   . ARG   A 1 24  ? 354.016 6.966   73.550  1.00 54.21  ? 3    ARG   A CB   1 
ATOM   16   C  CG   . ARG   A 1 24  ? 354.957 6.997   74.751  1.00 60.73  ? 3    ARG   A CG   1 
ATOM   17   C  CD   . ARG   A 1 24  ? 354.987 5.601   75.389  1.00 59.62  ? 3    ARG   A CD   1 
ATOM   18   N  NE   . ARG   A 1 24  ? 355.728 5.527   76.644  1.00 68.41  ? 3    ARG   A NE   1 
ATOM   19   C  CZ   . ARG   A 1 24  ? 356.115 4.392   77.215  1.00 64.49  ? 3    ARG   A CZ   1 
ATOM   20   N  NH1  . ARG   A 1 24  ? 355.846 3.217   76.669  1.00 61.91  ? 3    ARG   A NH1  1 
ATOM   21   N  NH2  . ARG   A 1 24  ? 356.801 4.439   78.355  1.00 47.61  ? 3    ARG   A NH2  1 
ATOM   22   N  N    . GLU   A 1 25  ? 352.403 8.089   70.787  1.00 44.42  ? 4    GLU   A N    1 
ATOM   23   C  CA   . GLU   A 1 25  ? 351.134 7.991   70.076  1.00 45.97  ? 4    GLU   A CA   1 
ATOM   24   C  C    . GLU   A 1 25  ? 350.748 6.525   69.918  1.00 38.42  ? 4    GLU   A C    1 
ATOM   25   O  O    . GLU   A 1 25  ? 351.581 5.690   69.550  1.00 40.19  ? 4    GLU   A O    1 
ATOM   26   C  CB   . GLU   A 1 25  ? 351.194 8.674   68.707  1.00 43.98  ? 4    GLU   A CB   1 
ATOM   27   C  CG   . GLU   A 1 25  ? 349.797 8.904   68.111  1.00 44.97  ? 4    GLU   A CG   1 
ATOM   28   C  CD   . GLU   A 1 25  ? 349.779 9.775   66.860  1.00 54.20  ? 4    GLU   A CD   1 
ATOM   29   O  OE1  . GLU   A 1 25  ? 350.563 9.515   65.923  1.00 49.77  ? 4    GLU   A OE1  1 
ATOM   30   O  OE2  . GLU   A 1 25  ? 348.960 10.718  66.811  1.00 59.26  ? 4    GLU   A OE2  1 
ATOM   31   N  N    . ARG   A 1 26  ? 349.487 6.219   70.199  1.00 37.43  ? 5    ARG   A N    1 
ATOM   32   C  CA   . ARG   A 1 26  ? 348.970 4.862   70.120  1.00 32.77  ? 5    ARG   A CA   1 
ATOM   33   C  C    . ARG   A 1 26  ? 347.724 4.864   69.249  1.00 34.56  ? 5    ARG   A C    1 
ATOM   34   O  O    . ARG   A 1 26  ? 346.885 5.763   69.358  1.00 37.03  ? 5    ARG   A O    1 
ATOM   35   C  CB   . ARG   A 1 26  ? 348.663 4.323   71.524  1.00 34.28  ? 5    ARG   A CB   1 
ATOM   36   C  CG   . ARG   A 1 26  ? 347.965 2.981   71.575  1.00 36.77  ? 5    ARG   A CG   1 
ATOM   37   C  CD   . ARG   A 1 26  ? 347.659 2.615   73.021  1.00 37.32  ? 5    ARG   A CD   1 
ATOM   38   N  NE   . ARG   A 1 26  ? 346.626 1.593   73.120  1.00 34.18  ? 5    ARG   A NE   1 
ATOM   39   C  CZ   . ARG   A 1 26  ? 345.771 1.487   74.126  1.00 38.20  ? 5    ARG   A CZ   1 
ATOM   40   N  NH1  . ARG   A 1 26  ? 345.808 2.318   75.157  1.00 30.79  ? 5    ARG   A NH1  1 
ATOM   41   N  NH2  . ARG   A 1 26  ? 344.844 0.534   74.091  1.00 37.12  ? 5    ARG   A NH2  1 
ATOM   42   N  N    . THR   A 1 27  ? 347.616 3.869   68.371  1.00 31.67  ? 6    THR   A N    1 
ATOM   43   C  CA   . THR   A 1 27  ? 346.495 3.774   67.444  1.00 31.66  ? 6    THR   A CA   1 
ATOM   44   C  C    . THR   A 1 27  ? 345.338 3.036   68.103  1.00 34.35  ? 6    THR   A C    1 
ATOM   45   O  O    . THR   A 1 27  ? 345.471 1.863   68.470  1.00 37.28  ? 6    THR   A O    1 
ATOM   46   C  CB   . THR   A 1 27  ? 346.893 3.053   66.158  1.00 35.20  ? 6    THR   A CB   1 
ATOM   47   O  OG1  . THR   A 1 27  ? 347.935 3.778   65.496  1.00 38.23  ? 6    THR   A OG1  1 
ATOM   48   C  CG2  . THR   A 1 27  ? 345.688 2.933   65.232  1.00 34.50  ? 6    THR   A CG2  1 
ATOM   49   N  N    . VAL   A 1 28  ? 344.204 3.714   68.234  1.00 34.83  ? 7    VAL   A N    1 
ATOM   50   C  CA   . VAL   A 1 28  ? 342.965 3.105   68.697  1.00 35.14  ? 7    VAL   A CA   1 
ATOM   51   C  C    . VAL   A 1 28  ? 341.881 3.487   67.702  1.00 38.08  ? 7    VAL   A C    1 
ATOM   52   O  O    . VAL   A 1 28  ? 341.523 4.666   67.591  1.00 47.91  ? 7    VAL   A O    1 
ATOM   53   C  CB   . VAL   A 1 28  ? 342.590 3.552   70.116  1.00 37.40  ? 7    VAL   A CB   1 
ATOM   54   C  CG1  . VAL   A 1 28  ? 341.166 3.132   70.441  1.00 35.75  ? 7    VAL   A CG1  1 
ATOM   55   C  CG2  . VAL   A 1 28  ? 343.571 2.973   71.125  1.00 36.79  ? 7    VAL   A CG2  1 
ATOM   56   N  N    . ARG   A 1 29  ? 341.362 2.501   66.975  1.00 36.65  ? 8    ARG   A N    1 
ATOM   57   C  CA   . ARG   A 1 29  ? 340.335 2.741   65.972  1.00 42.12  ? 8    ARG   A CA   1 
ATOM   58   C  C    . ARG   A 1 29  ? 338.943 2.535   66.550  1.00 45.76  ? 8    ARG   A C    1 
ATOM   59   O  O    . ARG   A 1 29  ? 338.709 1.605   67.326  1.00 42.65  ? 8    ARG   A O    1 
ATOM   60   C  CB   . ARG   A 1 29  ? 340.514 1.811   64.773  1.00 43.22  ? 8    ARG   A CB   1 
ATOM   61   C  CG   . ARG   A 1 29  ? 341.864 1.899   64.122  1.00 41.81  ? 8    ARG   A CG   1 
ATOM   62   C  CD   . ARG   A 1 29  ? 341.911 1.066   62.863  1.00 36.23  ? 8    ARG   A CD   1 
ATOM   63   N  NE   . ARG   A 1 29  ? 343.237 1.132   62.264  1.00 41.58  ? 8    ARG   A NE   1 
ATOM   64   C  CZ   . ARG   A 1 29  ? 343.615 2.050   61.387  1.00 45.07  ? 8    ARG   A CZ   1 
ATOM   65   N  NH1  . ARG   A 1 29  ? 342.773 2.970   60.943  1.00 46.61  ? 8    ARG   A NH1  1 
ATOM   66   N  NH2  . ARG   A 1 29  ? 344.871 2.047   60.946  1.00 36.71  ? 8    ARG   A NH2  1 
ATOM   67   N  N    . LEU   A 1 30  ? 338.021 3.406   66.154  1.00 40.28  ? 9    LEU   A N    1 
ATOM   68   C  CA   . LEU   A 1 30  ? 336.611 3.157   66.409  1.00 39.41  ? 9    LEU   A CA   1 
ATOM   69   C  C    . LEU   A 1 30  ? 336.134 2.005   65.537  1.00 42.85  ? 9    LEU   A C    1 
ATOM   70   O  O    . LEU   A 1 30  ? 336.578 1.845   64.396  1.00 42.80  ? 9    LEU   A O    1 
ATOM   71   C  CB   . LEU   A 1 30  ? 335.786 4.409   66.127  1.00 37.93  ? 9    LEU   A CB   1 
ATOM   72   C  CG   . LEU   A 1 30  ? 336.197 5.622   66.956  1.00 38.35  ? 9    LEU   A CG   1 
ATOM   73   C  CD1  . LEU   A 1 30  ? 335.249 6.779   66.712  1.00 41.82  ? 9    LEU   A CD1  1 
ATOM   74   C  CD2  . LEU   A 1 30  ? 336.236 5.248   68.425  1.00 38.07  ? 9    LEU   A CD2  1 
ATOM   75   N  N    . GLN   A 1 31  ? 335.233 1.196   66.080  1.00 47.95  ? 10   GLN   A N    1 
ATOM   76   C  CA   . GLN   A 1 31  ? 334.749 0.006   65.396  1.00 50.64  ? 10   GLN   A CA   1 
ATOM   77   C  C    . GLN   A 1 31  ? 333.365 0.262   64.814  1.00 53.14  ? 10   GLN   A C    1 
ATOM   78   O  O    . GLN   A 1 31  ? 332.507 0.864   65.465  1.00 50.63  ? 10   GLN   A O    1 
ATOM   79   C  CB   . GLN   A 1 31  ? 334.715 -1.189  66.352  1.00 51.83  ? 10   GLN   A CB   1 
ATOM   80   C  CG   . GLN   A 1 31  ? 334.270 -2.498  65.714  1.00 65.38  ? 10   GLN   A CG   1 
ATOM   81   C  CD   . GLN   A 1 31  ? 334.246 -3.648  66.706  1.00 65.34  ? 10   GLN   A CD   1 
ATOM   82   O  OE1  . GLN   A 1 31  ? 334.928 -3.614  67.729  1.00 69.00  ? 10   GLN   A OE1  1 
ATOM   83   N  NE2  . GLN   A 1 31  ? 333.453 -4.671  66.408  1.00 59.03  ? 10   GLN   A NE2  1 
ATOM   84   N  N    . TYR   A 1 32  ? 333.164 -0.197  63.579  1.00 51.71  ? 11   TYR   A N    1 
ATOM   85   C  CA   . TYR   A 1 32  ? 331.920 -0.001  62.844  1.00 55.95  ? 11   TYR   A CA   1 
ATOM   86   C  C    . TYR   A 1 32  ? 330.708 -0.280  63.719  1.00 60.18  ? 11   TYR   A C    1 
ATOM   87   O  O    . TYR   A 1 32  ? 330.412 -1.436  64.040  1.00 56.18  ? 11   TYR   A O    1 
ATOM   88   C  CB   . TYR   A 1 32  ? 331.902 -0.893  61.600  1.00 58.07  ? 11   TYR   A CB   1 
ATOM   89   C  CG   . TYR   A 1 32  ? 330.813 -0.575  60.596  1.00 57.58  ? 11   TYR   A CG   1 
ATOM   90   C  CD1  . TYR   A 1 32  ? 330.679 0.702   60.066  1.00 57.59  ? 11   TYR   A CD1  1 
ATOM   91   C  CD2  . TYR   A 1 32  ? 329.937 -1.560  60.156  1.00 62.44  ? 11   TYR   A CD2  1 
ATOM   92   C  CE1  . TYR   A 1 32  ? 329.690 0.994   59.141  1.00 56.21  ? 11   TYR   A CE1  1 
ATOM   93   C  CE2  . TYR   A 1 32  ? 328.947 -1.277  59.230  1.00 61.34  ? 11   TYR   A CE2  1 
ATOM   94   C  CZ   . TYR   A 1 32  ? 328.827 0.001   58.725  1.00 63.37  ? 11   TYR   A CZ   1 
ATOM   95   O  OH   . TYR   A 1 32  ? 327.843 0.285   57.805  1.00 69.87  ? 11   TYR   A OH   1 
ATOM   96   N  N    . GLY   A 1 33  ? 330.007 0.776   64.107  1.00 58.09  ? 12   GLY   A N    1 
ATOM   97   C  CA   . GLY   A 1 33  ? 328.785 0.640   64.915  1.00 58.20  ? 12   GLY   A CA   1 
ATOM   98   C  C    . GLY   A 1 33  ? 329.000 0.264   66.352  1.00 69.44  ? 12   GLY   A C    1 
ATOM   99   O  O    . GLY   A 1 33  ? 328.375 0.846   67.240  1.00 74.82  ? 12   GLY   A O    1 
ATOM   100  N  N    . SER   A 1 34  ? 329.896 -0.683  66.615  1.00 73.99  ? 13   SER   A N    1 
ATOM   101  C  CA   . SER   A 1 34  ? 330.124 -1.150  67.972  1.00 71.14  ? 13   SER   A CA   1 
ATOM   102  C  C    . SER   A 1 34  ? 330.835 -0.075  68.796  1.00 69.34  ? 13   SER   A C    1 
ATOM   103  O  O    . SER   A 1 34  ? 331.301 0.945   68.278  1.00 65.44  ? 13   SER   A O    1 
ATOM   104  C  CB   . SER   A 1 34  ? 330.932 -2.447  67.953  1.00 68.80  ? 13   SER   A CB   1 
ATOM   105  O  OG   . SER   A 1 34  ? 330.978 -3.043  69.236  1.00 73.91  ? 13   SER   A OG   1 
ATOM   106  N  N    . ARG   A 1 35  ? 330.901 -0.313  70.105  1.00 72.63  ? 14   ARG   A N    1 
ATOM   107  C  CA   . ARG   A 1 35  ? 331.604 0.555   71.040  1.00 66.37  ? 14   ARG   A CA   1 
ATOM   108  C  C    . ARG   A 1 35  ? 332.921 -0.091  71.447  1.00 62.55  ? 14   ARG   A C    1 
ATOM   109  O  O    . ARG   A 1 35  ? 332.974 -1.292  71.727  1.00 64.63  ? 14   ARG   A O    1 
ATOM   110  C  CB   . ARG   A 1 35  ? 330.762 0.823   72.289  1.00 65.63  ? 14   ARG   A CB   1 
ATOM   111  C  CG   . ARG   A 1 35  ? 330.759 -0.345  73.270  1.00 77.08  ? 14   ARG   A CG   1 
ATOM   112  C  CD   . ARG   A 1 35  ? 329.671 -0.223  74.325  1.00 84.34  ? 14   ARG   A CD   1 
ATOM   113  N  NE   . ARG   A 1 35  ? 330.180 0.267   75.600  1.00 86.07  ? 14   ARG   A NE   1 
ATOM   114  C  CZ   . ARG   A 1 35  ? 329.437 0.443   76.685  1.00 84.01  ? 14   ARG   A CZ   1 
ATOM   115  N  NH1  . ARG   A 1 35  ? 328.142 0.169   76.687  1.00 76.90  ? 14   ARG   A NH1  1 
ATOM   116  N  NH2  . ARG   A 1 35  ? 330.008 0.906   77.794  1.00 78.50  ? 14   ARG   A NH2  1 
ATOM   117  N  N    . VAL   A 1 36  ? 333.981 0.711   71.488  1.00 52.33  ? 15   VAL   A N    1 
ATOM   118  C  CA   . VAL   A 1 36  ? 335.311 0.247   71.863  1.00 47.13  ? 15   VAL   A CA   1 
ATOM   119  C  C    . VAL   A 1 36  ? 335.619 0.753   73.263  1.00 44.86  ? 15   VAL   A C    1 
ATOM   120  O  O    . VAL   A 1 36  ? 335.480 1.950   73.544  1.00 45.02  ? 15   VAL   A O    1 
ATOM   121  C  CB   . VAL   A 1 36  ? 336.380 0.716   70.862  1.00 46.26  ? 15   VAL   A CB   1 
ATOM   122  C  CG1  . VAL   A 1 36  ? 337.768 0.363   71.370  1.00 47.46  ? 15   VAL   A CG1  1 
ATOM   123  C  CG2  . VAL   A 1 36  ? 336.135 0.096   69.495  1.00 42.10  ? 15   VAL   A CG2  1 
ATOM   124  N  N    . GLU   A 1 37  ? 336.032 -0.157  74.137  1.00 46.30  ? 16   GLU   A N    1 
ATOM   125  C  CA   . GLU   A 1 37  ? 336.452 0.175   75.490  1.00 43.52  ? 16   GLU   A CA   1 
ATOM   126  C  C    . GLU   A 1 37  ? 337.934 -0.131  75.618  1.00 46.22  ? 16   GLU   A C    1 
ATOM   127  O  O    . GLU   A 1 37  ? 338.378 -1.230  75.268  1.00 49.56  ? 16   GLU   A O    1 
ATOM   128  C  CB   . GLU   A 1 37  ? 335.640 -0.610  76.521  1.00 47.41  ? 16   GLU   A CB   1 
ATOM   129  C  CG   . GLU   A 1 37  ? 334.140 -0.478  76.315  1.00 58.96  ? 16   GLU   A CG   1 
ATOM   130  C  CD   . GLU   A 1 37  ? 333.332 -1.290  77.303  1.00 63.95  ? 16   GLU   A CD   1 
ATOM   131  O  OE1  . GLU   A 1 37  ? 333.919 -1.789  78.286  1.00 71.02  ? 16   GLU   A OE1  1 
ATOM   132  O  OE2  . GLU   A 1 37  ? 332.108 -1.430  77.095  1.00 68.03  ? 16   GLU   A OE2  1 
ATOM   133  N  N    . ALA   A 1 38  ? 338.699 0.842   76.102  1.00 39.33  ? 17   ALA   A N    1 
ATOM   134  C  CA   . ALA   A 1 38  ? 340.144 0.717   76.123  1.00 31.14  ? 17   ALA   A CA   1 
ATOM   135  C  C    . ALA   A 1 38  ? 340.699 1.315   77.404  1.00 36.88  ? 17   ALA   A C    1 
ATOM   136  O  O    . ALA   A 1 38  ? 340.168 2.295   77.933  1.00 36.51  ? 17   ALA   A O    1 
ATOM   137  C  CB   . ALA   A 1 38  ? 340.780 1.402   74.906  1.00 32.47  ? 17   ALA   A CB   1 
ATOM   138  N  N    . VAL   A 1 39  ? 341.769 0.704   77.900  1.00 37.56  ? 18   VAL   A N    1 
ATOM   139  C  CA   . VAL   A 1 39  ? 342.564 1.302   78.964  1.00 37.37  ? 18   VAL   A CA   1 
ATOM   140  C  C    . VAL   A 1 39  ? 343.518 2.313   78.345  1.00 32.45  ? 18   VAL   A C    1 
ATOM   141  O  O    . VAL   A 1 39  ? 344.184 2.027   77.343  1.00 38.74  ? 18   VAL   A O    1 
ATOM   142  C  CB   . VAL   A 1 39  ? 343.327 0.224   79.749  1.00 40.09  ? 18   VAL   A CB   1 
ATOM   143  C  CG1  . VAL   A 1 39  ? 344.405 0.860   80.616  1.00 36.45  ? 18   VAL   A CG1  1 
ATOM   144  C  CG2  . VAL   A 1 39  ? 342.365 -0.582  80.602  1.00 40.70  ? 18   VAL   A CG2  1 
ATOM   145  N  N    . TYR   A 1 40  ? 343.571 3.501   78.930  1.00 32.19  ? 19   TYR   A N    1 
ATOM   146  C  CA   . TYR   A 1 40  ? 344.447 4.575   78.482  1.00 35.38  ? 19   TYR   A CA   1 
ATOM   147  C  C    . TYR   A 1 40  ? 345.538 4.751   79.531  1.00 31.26  ? 19   TYR   A C    1 
ATOM   148  O  O    . TYR   A 1 40  ? 345.235 5.002   80.703  1.00 34.01  ? 19   TYR   A O    1 
ATOM   149  C  CB   . TYR   A 1 40  ? 343.639 5.862   78.282  1.00 34.39  ? 19   TYR   A CB   1 
ATOM   150  C  CG   . TYR   A 1 40  ? 344.427 7.082   77.857  1.00 39.03  ? 19   TYR   A CG   1 
ATOM   151  C  CD1  . TYR   A 1 40  ? 345.267 7.738   78.748  1.00 44.67  ? 19   TYR   A CD1  1 
ATOM   152  C  CD2  . TYR   A 1 40  ? 344.298 7.604   76.577  1.00 39.01  ? 19   TYR   A CD2  1 
ATOM   153  C  CE1  . TYR   A 1 40  ? 345.977 8.860   78.368  1.00 43.08  ? 19   TYR   A CE1  1 
ATOM   154  C  CE2  . TYR   A 1 40  ? 345.002 8.727   76.189  1.00 38.53  ? 19   TYR   A CE2  1 
ATOM   155  C  CZ   . TYR   A 1 40  ? 345.840 9.351   77.087  1.00 39.63  ? 19   TYR   A CZ   1 
ATOM   156  O  OH   . TYR   A 1 40  ? 346.544 10.469  76.704  1.00 40.77  ? 19   TYR   A OH   1 
ATOM   157  N  N    . VAL   A 1 41  ? 346.796 4.598   79.124  1.00 34.24  ? 20   VAL   A N    1 
ATOM   158  C  CA   . VAL   A 1 41  ? 347.924 4.753   80.038  1.00 35.21  ? 20   VAL   A CA   1 
ATOM   159  C  C    . VAL   A 1 41  ? 348.448 6.179   79.932  1.00 36.17  ? 20   VAL   A C    1 
ATOM   160  O  O    . VAL   A 1 41  ? 348.805 6.641   78.842  1.00 40.31  ? 20   VAL   A O    1 
ATOM   161  C  CB   . VAL   A 1 41  ? 349.034 3.736   79.739  1.00 34.77  ? 20   VAL   A CB   1 
ATOM   162  C  CG1  . VAL   A 1 41  ? 350.170 3.871   80.757  1.00 30.93  ? 20   VAL   A CG1  1 
ATOM   163  C  CG2  . VAL   A 1 41  ? 348.481 2.326   79.745  1.00 36.42  ? 20   VAL   A CG2  1 
ATOM   164  N  N    . LEU   A 1 42  ? 348.493 6.878   81.063  1.00 33.54  ? 21   LEU   A N    1 
ATOM   165  C  CA   . LEU   A 1 42  ? 349.015 8.236   81.081  1.00 36.92  ? 21   LEU   A CA   1 
ATOM   166  C  C    . LEU   A 1 42  ? 350.452 8.263   80.573  1.00 39.11  ? 21   LEU   A C    1 
ATOM   167  O  O    . LEU   A 1 42  ? 351.224 7.320   80.768  1.00 37.36  ? 21   LEU   A O    1 
ATOM   168  C  CB   . LEU   A 1 42  ? 348.936 8.817   82.492  1.00 35.75  ? 21   LEU   A CB   1 
ATOM   169  C  CG   . LEU   A 1 42  ? 347.532 8.890   83.093  1.00 41.98  ? 21   LEU   A CG   1 
ATOM   170  C  CD1  . LEU   A 1 42  ? 347.560 9.515   84.481  1.00 40.12  ? 21   LEU   A CD1  1 
ATOM   171  C  CD2  . LEU   A 1 42  ? 346.589 9.657   82.176  1.00 41.89  ? 21   LEU   A CD2  1 
ATOM   172  N  N    . GLY   A 1 43  ? 350.811 9.370   79.925  1.00 37.89  ? 22   GLY   A N    1 
ATOM   173  C  CA   . GLY   A 1 43  ? 352.061 9.471   79.209  1.00 43.22  ? 22   GLY   A CA   1 
ATOM   174  C  C    . GLY   A 1 43  ? 351.963 9.118   77.742  1.00 41.26  ? 22   GLY   A C    1 
ATOM   175  O  O    . GLY   A 1 43  ? 352.943 9.295   77.008  1.00 43.50  ? 22   GLY   A O    1 
ATOM   176  N  N    . THR   A 1 44  ? 350.820 8.615   77.297  1.00 42.06  ? 23   THR   A N    1 
ATOM   177  C  CA   . THR   A 1 44  ? 350.558 8.336   75.897  1.00 39.40  ? 23   THR   A CA   1 
ATOM   178  C  C    . THR   A 1 44  ? 349.374 9.175   75.444  1.00 44.45  ? 23   THR   A C    1 
ATOM   179  O  O    . THR   A 1 44  ? 348.705 9.835   76.243  1.00 44.79  ? 23   THR   A O    1 
ATOM   180  C  CB   . THR   A 1 44  ? 350.262 6.847   75.669  1.00 41.66  ? 23   THR   A CB   1 
ATOM   181  O  OG1  . THR   A 1 44  ? 348.868 6.594   75.892  1.00 41.97  ? 23   THR   A OG1  1 
ATOM   182  C  CG2  . THR   A 1 44  ? 351.081 5.992   76.622  1.00 39.44  ? 23   THR   A CG2  1 
ATOM   183  N  N    . TYR   A 1 45  ? 349.123 9.157   74.141  1.00 41.96  ? 24   TYR   A N    1 
ATOM   184  C  CA   . TYR   A 1 45  ? 347.870 9.667   73.616  1.00 42.32  ? 24   TYR   A CA   1 
ATOM   185  C  C    . TYR   A 1 45  ? 347.452 8.792   72.447  1.00 37.94  ? 24   TYR   A C    1 
ATOM   186  O  O    . TYR   A 1 45  ? 348.250 8.037   71.888  1.00 37.13  ? 24   TYR   A O    1 
ATOM   187  C  CB   . TYR   A 1 45  ? 347.962 11.144  73.202  1.00 45.36  ? 24   TYR   A CB   1 
ATOM   188  C  CG   . TYR   A 1 45  ? 348.908 11.439  72.064  1.00 47.59  ? 24   TYR   A CG   1 
ATOM   189  C  CD1  . TYR   A 1 45  ? 350.236 11.764  72.308  1.00 50.24  ? 24   TYR   A CD1  1 
ATOM   190  C  CD2  . TYR   A 1 45  ? 348.469 11.418  70.746  1.00 52.05  ? 24   TYR   A CD2  1 
ATOM   191  C  CE1  . TYR   A 1 45  ? 351.105 12.045  71.269  1.00 54.80  ? 24   TYR   A CE1  1 
ATOM   192  C  CE2  . TYR   A 1 45  ? 349.332 11.698  69.701  1.00 53.52  ? 24   TYR   A CE2  1 
ATOM   193  C  CZ   . TYR   A 1 45  ? 350.648 12.011  69.967  1.00 59.02  ? 24   TYR   A CZ   1 
ATOM   194  O  OH   . TYR   A 1 45  ? 351.508 12.290  68.928  1.00 65.34  ? 24   TYR   A OH   1 
ATOM   195  N  N    . LEU   A 1 46  ? 346.177 8.884   72.104  1.00 37.61  ? 25   LEU   A N    1 
ATOM   196  C  CA   . LEU   A 1 46  ? 345.597 8.053   71.067  1.00 39.96  ? 25   LEU   A CA   1 
ATOM   197  C  C    . LEU   A 1 46  ? 345.423 8.860   69.793  1.00 38.78  ? 25   LEU   A C    1 
ATOM   198  O  O    . LEU   A 1 46  ? 345.056 10.038  69.835  1.00 41.42  ? 25   LEU   A O    1 
ATOM   199  C  CB   . LEU   A 1 46  ? 344.244 7.498   71.509  1.00 35.58  ? 25   LEU   A CB   1 
ATOM   200  C  CG   . LEU   A 1 46  ? 344.172 6.982   72.942  1.00 35.81  ? 25   LEU   A CG   1 
ATOM   201  C  CD1  . LEU   A 1 46  ? 342.799 6.390   73.201  1.00 35.66  ? 25   LEU   A CD1  1 
ATOM   202  C  CD2  . LEU   A 1 46  ? 345.273 5.965   73.201  1.00 35.41  ? 25   LEU   A CD2  1 
ATOM   203  N  N    . TRP   A 1 47  ? 345.716 8.229   68.665  1.00 36.66  ? 26   TRP   A N    1 
ATOM   204  C  CA   . TRP   A 1 47  ? 345.188 8.663   67.384  1.00 36.88  ? 26   TRP   A CA   1 
ATOM   205  C  C    . TRP   A 1 47  ? 344.050 7.714   67.044  1.00 33.49  ? 26   TRP   A C    1 
ATOM   206  O  O    . TRP   A 1 47  ? 344.206 6.492   67.145  1.00 36.01  ? 26   TRP   A O    1 
ATOM   207  C  CB   . TRP   A 1 47  ? 346.270 8.679   66.299  1.00 40.25  ? 26   TRP   A CB   1 
ATOM   208  C  CG   . TRP   A 1 47  ? 346.248 7.530   65.334  1.00 43.85  ? 26   TRP   A CG   1 
ATOM   209  C  CD1  . TRP   A 1 47  ? 347.036 6.418   65.366  1.00 43.46  ? 26   TRP   A CD1  1 
ATOM   210  C  CD2  . TRP   A 1 47  ? 345.416 7.396   64.172  1.00 44.54  ? 26   TRP   A CD2  1 
ATOM   211  N  NE1  . TRP   A 1 47  ? 346.739 5.591   64.305  1.00 46.16  ? 26   TRP   A NE1  1 
ATOM   212  C  CE2  . TRP   A 1 47  ? 345.746 6.169   63.558  1.00 44.47  ? 26   TRP   A CE2  1 
ATOM   213  C  CE3  . TRP   A 1 47  ? 344.417 8.188   63.597  1.00 49.19  ? 26   TRP   A CE3  1 
ATOM   214  C  CZ2  . TRP   A 1 47  ? 345.114 5.720   62.399  1.00 46.55  ? 26   TRP   A CZ2  1 
ATOM   215  C  CZ3  . TRP   A 1 47  ? 343.791 7.738   62.446  1.00 52.84  ? 26   TRP   A CZ3  1 
ATOM   216  C  CH2  . TRP   A 1 47  ? 344.142 6.517   61.861  1.00 49.18  ? 26   TRP   A CH2  1 
ATOM   217  N  N    . THR   A 1 48  ? 342.893 8.271   66.708  1.00 33.66  ? 27   THR   A N    1 
ATOM   218  C  CA   . THR   A 1 48  ? 341.673 7.490   66.568  1.00 37.53  ? 27   THR   A CA   1 
ATOM   219  C  C    . THR   A 1 48  ? 341.100 7.688   65.175  1.00 34.60  ? 27   THR   A C    1 
ATOM   220  O  O    . THR   A 1 48  ? 340.777 8.815   64.784  1.00 38.13  ? 27   THR   A O    1 
ATOM   221  C  CB   . THR   A 1 48  ? 340.650 7.881   67.636  1.00 34.84  ? 27   THR   A CB   1 
ATOM   222  O  OG1  . THR   A 1 48  ? 341.227 7.696   68.933  1.00 41.87  ? 27   THR   A OG1  1 
ATOM   223  C  CG2  . THR   A 1 48  ? 339.403 7.021   67.521  1.00 37.52  ? 27   THR   A CG2  1 
ATOM   224  N  N    . ASP   A 1 49  ? 340.986 6.593   64.432  1.00 34.14  ? 28   ASP   A N    1 
ATOM   225  C  CA   . ASP   A 1 49  ? 340.294 6.586   63.151  1.00 39.73  ? 28   ASP   A CA   1 
ATOM   226  C  C    . ASP   A 1 49  ? 338.787 6.602   63.391  1.00 41.08  ? 28   ASP   A C    1 
ATOM   227  O  O    . ASP   A 1 49  ? 338.248 5.693   64.032  1.00 39.58  ? 28   ASP   A O    1 
ATOM   228  C  CB   . ASP   A 1 49  ? 340.710 5.352   62.352  1.00 40.45  ? 28   ASP   A CB   1 
ATOM   229  C  CG   . ASP   A 1 49  ? 339.832 5.104   61.137  1.00 42.48  ? 28   ASP   A CG   1 
ATOM   230  O  OD1  . ASP   A 1 49  ? 339.016 5.981   60.779  1.00 49.42  ? 28   ASP   A OD1  1 
ATOM   231  O  OD2  . ASP   A 1 49  ? 339.959 4.018   60.535  1.00 51.39  ? 28   ASP   A OD2  1 
ATOM   232  N  N    . VAL   A 1 50  ? 338.107 7.634   62.880  1.00 37.70  ? 29   VAL   A N    1 
ATOM   233  C  CA   . VAL   A 1 50  ? 336.644 7.665   62.879  1.00 43.92  ? 29   VAL   A CA   1 
ATOM   234  C  C    . VAL   A 1 50  ? 336.059 7.328   61.514  1.00 40.43  ? 29   VAL   A C    1 
ATOM   235  O  O    . VAL   A 1 50  ? 334.845 7.079   61.416  1.00 44.20  ? 29   VAL   A O    1 
ATOM   236  C  CB   . VAL   A 1 50  ? 336.099 9.036   63.346  1.00 41.80  ? 29   VAL   A CB   1 
ATOM   237  C  CG1  . VAL   A 1 50  ? 336.596 9.363   64.743  1.00 36.37  ? 29   VAL   A CG1  1 
ATOM   238  C  CG2  . VAL   A 1 50  ? 336.477 10.136  62.359  1.00 37.50  ? 29   VAL   A CG2  1 
ATOM   239  N  N    . TYR   A 1 51  ? 336.882 7.292   60.465  1.00 39.61  ? 30   TYR   A N    1 
ATOM   240  C  CA   . TYR   A 1 51  ? 336.392 7.134   59.101  1.00 44.44  ? 30   TYR   A CA   1 
ATOM   241  C  C    . TYR   A 1 51  ? 336.020 5.688   58.785  1.00 50.73  ? 30   TYR   A C    1 
ATOM   242  O  O    . TYR   A 1 51  ? 335.016 5.441   58.105  1.00 46.95  ? 30   TYR   A O    1 
ATOM   243  C  CB   . TYR   A 1 51  ? 337.452 7.646   58.124  1.00 46.92  ? 30   TYR   A CB   1 
ATOM   244  C  CG   . TYR   A 1 51  ? 337.095 7.482   56.667  1.00 47.58  ? 30   TYR   A CG   1 
ATOM   245  C  CD1  . TYR   A 1 51  ? 336.252 8.384   56.034  1.00 50.44  ? 30   TYR   A CD1  1 
ATOM   246  C  CD2  . TYR   A 1 51  ? 337.613 6.433   55.921  1.00 47.99  ? 30   TYR   A CD2  1 
ATOM   247  C  CE1  . TYR   A 1 51  ? 335.927 8.240   54.700  1.00 50.93  ? 30   TYR   A CE1  1 
ATOM   248  C  CE2  . TYR   A 1 51  ? 337.295 6.282   54.586  1.00 44.94  ? 30   TYR   A CE2  1 
ATOM   249  C  CZ   . TYR   A 1 51  ? 336.451 7.188   53.979  1.00 46.20  ? 30   TYR   A CZ   1 
ATOM   250  O  OH   . TYR   A 1 51  ? 336.131 7.041   52.650  1.00 59.55  ? 30   TYR   A OH   1 
ATOM   251  N  N    A SER   A 1 52  ? 336.810 4.725   59.262  0.50 45.16  ? 31   SER   A N    1 
ATOM   252  N  N    B SER   A 1 52  ? 336.810 4.723   59.266  0.50 45.16  ? 31   SER   A N    1 
ATOM   253  C  CA   A SER   A 1 52  ? 336.536 3.326   58.947  0.50 46.24  ? 31   SER   A CA   1 
ATOM   254  C  CA   B SER   A 1 52  ? 336.539 3.323   58.953  0.50 46.25  ? 31   SER   A CA   1 
ATOM   255  C  C    A SER   A 1 52  ? 335.261 2.832   59.620  0.50 48.13  ? 31   SER   A C    1 
ATOM   256  C  C    B SER   A 1 52  ? 335.263 2.831   59.622  0.50 48.13  ? 31   SER   A C    1 
ATOM   257  O  O    A SER   A 1 52  ? 334.613 1.910   59.112  0.50 51.86  ? 31   SER   A O    1 
ATOM   258  O  O    B SER   A 1 52  ? 334.614 1.909   59.113  0.50 51.86  ? 31   SER   A O    1 
ATOM   259  C  CB   A SER   A 1 52  ? 337.722 2.452   59.352  0.50 48.06  ? 31   SER   A CB   1 
ATOM   260  C  CB   B SER   A 1 52  ? 337.724 2.445   59.364  0.50 48.05  ? 31   SER   A CB   1 
ATOM   261  O  OG   A SER   A 1 52  ? 338.903 2.845   58.672  0.50 44.61  ? 31   SER   A OG   1 
ATOM   262  O  OG   B SER   A 1 52  ? 337.868 2.384   60.774  0.50 51.44  ? 31   SER   A OG   1 
ATOM   263  N  N    . ALA   A 1 53  ? 334.887 3.424   60.754  1.00 43.16  ? 32   ALA   A N    1 
ATOM   264  C  CA   . ALA   A 1 53  ? 333.673 3.027   61.454  1.00 45.11  ? 32   ALA   A CA   1 
ATOM   265  C  C    . ALA   A 1 53  ? 332.427 3.709   60.908  1.00 46.52  ? 32   ALA   A C    1 
ATOM   266  O  O    . ALA   A 1 53  ? 331.314 3.322   61.281  1.00 49.03  ? 32   ALA   A O    1 
ATOM   267  C  CB   . ALA   A 1 53  ? 333.807 3.324   62.950  1.00 49.46  ? 32   ALA   A CB   1 
ATOM   268  N  N    . ALA   A 1 54  ? 332.584 4.705   60.042  1.00 49.80  ? 33   ALA   A N    1 
ATOM   269  C  CA   . ALA   A 1 54  ? 331.428 5.395   59.494  1.00 46.00  ? 33   ALA   A CA   1 
ATOM   270  C  C    . ALA   A 1 54  ? 330.607 4.440   58.632  1.00 47.23  ? 33   ALA   A C    1 
ATOM   271  O  O    . ALA   A 1 54  ? 331.170 3.663   57.855  1.00 49.43  ? 33   ALA   A O    1 
ATOM   272  C  CB   . ALA   A 1 54  ? 331.864 6.601   58.662  1.00 41.09  ? 33   ALA   A CB   1 
ATOM   273  N  N    . PRO   A 1 55  ? 329.281 4.466   58.751  1.00 52.28  ? 34   PRO   A N    1 
ATOM   274  C  CA   . PRO   A 1 55  ? 328.451 3.656   57.856  1.00 50.45  ? 34   PRO   A CA   1 
ATOM   275  C  C    . PRO   A 1 55  ? 328.659 4.088   56.415  1.00 47.23  ? 34   PRO   A C    1 
ATOM   276  O  O    . PRO   A 1 55  ? 329.049 5.222   56.125  1.00 49.33  ? 34   PRO   A O    1 
ATOM   277  C  CB   . PRO   A 1 55  ? 327.018 3.949   58.323  1.00 52.04  ? 34   PRO   A CB   1 
ATOM   278  C  CG   . PRO   A 1 55  ? 327.163 4.550   59.687  1.00 49.43  ? 34   PRO   A CG   1 
ATOM   279  C  CD   . PRO   A 1 55  ? 328.476 5.268   59.683  1.00 46.93  ? 34   PRO   A CD   1 
ATOM   280  N  N    . ALA   A 1 56  ? 328.404 3.161   55.498  1.00 48.80  ? 35   ALA   A N    1 
ATOM   281  C  CA   . ALA   A 1 56  ? 328.504 3.502   54.087  1.00 51.13  ? 35   ALA   A CA   1 
ATOM   282  C  C    . ALA   A 1 56  ? 327.583 4.674   53.774  1.00 52.97  ? 35   ALA   A C    1 
ATOM   283  O  O    . ALA   A 1 56  ? 326.496 4.802   54.344  1.00 54.20  ? 35   ALA   A O    1 
ATOM   284  C  CB   . ALA   A 1 56  ? 328.150 2.299   53.213  1.00 55.58  ? 35   ALA   A CB   1 
ATOM   285  N  N    . GLY   A 1 57  ? 328.034 5.547   52.873  1.00 52.18  ? 36   GLY   A N    1 
ATOM   286  C  CA   . GLY   A 1 57  ? 327.266 6.706   52.477  1.00 52.94  ? 36   GLY   A CA   1 
ATOM   287  C  C    . GLY   A 1 57  ? 327.284 7.861   53.452  1.00 50.54  ? 36   GLY   A C    1 
ATOM   288  O  O    . GLY   A 1 57  ? 326.933 8.983   53.065  1.00 56.17  ? 36   GLY   A O    1 
ATOM   289  N  N    . ALA   A 1 58  ? 327.680 7.630   54.703  1.00 50.70  ? 37   ALA   A N    1 
ATOM   290  C  CA   . ALA   A 1 58  ? 327.758 8.708   55.679  1.00 50.50  ? 37   ALA   A CA   1 
ATOM   291  C  C    . ALA   A 1 58  ? 328.705 9.799   55.194  1.00 52.25  ? 37   ALA   A C    1 
ATOM   292  O  O    . ALA   A 1 58  ? 329.756 9.519   54.612  1.00 51.54  ? 37   ALA   A O    1 
ATOM   293  C  CB   . ALA   A 1 58  ? 328.220 8.163   57.031  1.00 48.13  ? 37   ALA   A CB   1 
ATOM   294  N  N    . GLN   A 1 59  ? 328.332 11.053  55.447  1.00 49.45  ? 38   GLN   A N    1 
ATOM   295  C  CA   . GLN   A 1 59  ? 329.037 12.195  54.880  1.00 50.96  ? 38   GLN   A CA   1 
ATOM   296  C  C    . GLN   A 1 59  ? 329.767 13.049  55.906  1.00 52.10  ? 38   GLN   A C    1 
ATOM   297  O  O    . GLN   A 1 59  ? 330.835 13.580  55.596  1.00 50.91  ? 38   GLN   A O    1 
ATOM   298  C  CB   . GLN   A 1 59  ? 328.057 13.084  54.102  1.00 55.34  ? 38   GLN   A CB   1 
ATOM   299  C  CG   . GLN   A 1 59  ? 328.696 13.960  53.028  1.00 67.66  ? 38   GLN   A CG   1 
ATOM   300  C  CD   . GLN   A 1 59  ? 328.995 13.205  51.741  1.00 74.04  ? 38   GLN   A CD   1 
ATOM   301  O  OE1  . GLN   A 1 59  ? 329.070 11.977  51.728  1.00 71.68  ? 38   GLN   A OE1  1 
ATOM   302  N  NE2  . GLN   A 1 59  ? 329.164 13.944  50.650  1.00 77.42  ? 38   GLN   A NE2  1 
ATOM   303  N  N    . THR   A 1 60  ? 329.228 13.192  57.115  1.00 52.24  ? 39   THR   A N    1 
ATOM   304  C  CA   . THR   A 1 60  ? 329.823 14.046  58.132  1.00 49.56  ? 39   THR   A CA   1 
ATOM   305  C  C    . THR   A 1 60  ? 329.767 13.339  59.477  1.00 47.29  ? 39   THR   A C    1 
ATOM   306  O  O    . THR   A 1 60  ? 329.085 12.325  59.646  1.00 45.37  ? 39   THR   A O    1 
ATOM   307  C  CB   . THR   A 1 60  ? 329.108 15.401  58.216  1.00 46.92  ? 39   THR   A CB   1 
ATOM   308  O  OG1  . THR   A 1 60  ? 327.735 15.196  58.576  1.00 48.89  ? 39   THR   A OG1  1 
ATOM   309  C  CG2  . THR   A 1 60  ? 329.170 16.115  56.876  1.00 47.18  ? 39   THR   A CG2  1 
ATOM   310  N  N    . PHE   A 1 61  ? 330.495 13.888  60.446  1.00 41.56  ? 40   PHE   A N    1 
ATOM   311  C  CA   . PHE   A 1 61  ? 330.464 13.371  61.804  1.00 42.59  ? 40   PHE   A CA   1 
ATOM   312  C  C    . PHE   A 1 61  ? 330.598 14.518  62.794  1.00 43.42  ? 40   PHE   A C    1 
ATOM   313  O  O    . PHE   A 1 61  ? 331.218 15.544  62.508  1.00 47.12  ? 40   PHE   A O    1 
ATOM   314  C  CB   . PHE   A 1 61  ? 331.579 12.347  62.054  1.00 39.51  ? 40   PHE   A CB   1 
ATOM   315  C  CG   . PHE   A 1 61  ? 332.945 12.954  62.156  1.00 39.05  ? 40   PHE   A CG   1 
ATOM   316  C  CD1  . PHE   A 1 61  ? 333.679 13.233  61.015  1.00 40.90  ? 40   PHE   A CD1  1 
ATOM   317  C  CD2  . PHE   A 1 61  ? 333.496 13.247  63.392  1.00 37.42  ? 40   PHE   A CD2  1 
ATOM   318  C  CE1  . PHE   A 1 61  ? 334.939 13.793  61.105  1.00 38.73  ? 40   PHE   A CE1  1 
ATOM   319  C  CE2  . PHE   A 1 61  ? 334.755 13.807  63.490  1.00 37.46  ? 40   PHE   A CE2  1 
ATOM   320  C  CZ   . PHE   A 1 61  ? 335.479 14.080  62.346  1.00 36.00  ? 40   PHE   A CZ   1 
ATOM   321  N  N    . SER   A 1 62  ? 329.991 14.335  63.955  1.00 41.64  ? 41   SER   A N    1 
ATOM   322  C  CA   . SER   A 1 62  ? 330.176 15.190  65.114  1.00 41.48  ? 41   SER   A CA   1 
ATOM   323  C  C    . SER   A 1 62  ? 330.621 14.314  66.278  1.00 39.06  ? 41   SER   A C    1 
ATOM   324  O  O    . SER   A 1 62  ? 330.713 13.089  66.156  1.00 34.70  ? 41   SER   A O    1 
ATOM   325  C  CB   . SER   A 1 62  ? 328.890 15.948  65.444  1.00 40.76  ? 41   SER   A CB   1 
ATOM   326  O  OG   . SER   A 1 62  ? 327.835 15.042  65.696  1.00 43.20  ? 41   SER   A OG   1 
ATOM   327  N  N    . LEU   A 1 63  ? 330.898 14.938  67.418  1.00 40.91  ? 42   LEU   A N    1 
ATOM   328  C  CA   . LEU   A 1 63  ? 331.407 14.143  68.524  1.00 42.46  ? 42   LEU   A CA   1 
ATOM   329  C  C    . LEU   A 1 63  ? 331.093 14.822  69.845  1.00 38.52  ? 42   LEU   A C    1 
ATOM   330  O  O    . LEU   A 1 63  ? 330.938 16.045  69.916  1.00 48.43  ? 42   LEU   A O    1 
ATOM   331  C  CB   . LEU   A 1 63  ? 332.916 13.906  68.388  1.00 38.32  ? 42   LEU   A CB   1 
ATOM   332  C  CG   . LEU   A 1 63  ? 333.840 15.120  68.477  1.00 43.93  ? 42   LEU   A CG   1 
ATOM   333  C  CD1  . LEU   A 1 63  ? 334.153 15.466  69.928  1.00 40.12  ? 42   LEU   A CD1  1 
ATOM   334  C  CD2  . LEU   A 1 63  ? 335.114 14.868  67.686  1.00 36.68  ? 42   LEU   A CD2  1 
ATOM   335  N  N    . LYS   A 1 64  ? 330.995 14.002  70.886  1.00 39.46  ? 43   LYS   A N    1 
ATOM   336  C  CA   . LYS   A 1 64  ? 330.907 14.441  72.266  1.00 46.00  ? 43   LYS   A CA   1 
ATOM   337  C  C    . LYS   A 1 64  ? 332.039 13.786  73.045  1.00 39.27  ? 43   LYS   A C    1 
ATOM   338  O  O    . LYS   A 1 64  ? 332.593 12.767  72.625  1.00 40.56  ? 43   LYS   A O    1 
ATOM   339  C  CB   . LYS   A 1 64  ? 329.558 14.064  72.897  1.00 45.90  ? 43   LYS   A CB   1 
ATOM   340  C  CG   . LYS   A 1 64  ? 328.331 14.356  72.046  1.00 47.38  ? 43   LYS   A CG   1 
ATOM   341  C  CD   . LYS   A 1 64  ? 328.028 15.842  71.980  1.00 60.12  ? 43   LYS   A CD   1 
ATOM   342  C  CE   . LYS   A 1 64  ? 326.527 16.094  72.031  1.00 67.58  ? 43   LYS   A CE   1 
ATOM   343  N  NZ   . LYS   A 1 64  ? 325.777 15.243  71.065  1.00 71.34  ? 43   LYS   A NZ   1 
ATOM   344  N  N    . HIS   A 1 65  ? 332.384 14.371  74.189  1.00 40.14  ? 44   HIS   A N    1 
ATOM   345  C  CA   . HIS   A 1 65  ? 333.371 13.734  75.051  1.00 39.42  ? 44   HIS   A CA   1 
ATOM   346  C  C    . HIS   A 1 65  ? 333.239 14.281  76.463  1.00 42.69  ? 44   HIS   A C    1 
ATOM   347  O  O    . HIS   A 1 65  ? 332.682 15.359  76.686  1.00 44.00  ? 44   HIS   A O    1 
ATOM   348  C  CB   . HIS   A 1 65  ? 334.797 13.921  74.515  1.00 39.96  ? 44   HIS   A CB   1 
ATOM   349  C  CG   . HIS   A 1 65  ? 335.272 15.340  74.516  1.00 43.96  ? 44   HIS   A CG   1 
ATOM   350  N  ND1  . HIS   A 1 65  ? 335.725 15.973  75.654  1.00 39.94  ? 44   HIS   A ND1  1 
ATOM   351  C  CD2  . HIS   A 1 65  ? 335.383 16.244  73.514  1.00 40.61  ? 44   HIS   A CD2  1 
ATOM   352  C  CE1  . HIS   A 1 65  ? 336.087 17.208  75.354  1.00 44.54  ? 44   HIS   A CE1  1 
ATOM   353  N  NE2  . HIS   A 1 65  ? 335.890 17.398  74.062  1.00 40.63  ? 44   HIS   A NE2  1 
ATOM   354  N  N    . SER   A 1 66  ? 333.755 13.511  77.418  1.00 43.07  ? 45   SER   A N    1 
ATOM   355  C  CA   . SER   A 1 66  ? 333.641 13.870  78.821  1.00 43.38  ? 45   SER   A CA   1 
ATOM   356  C  C    . SER   A 1 66  ? 334.719 14.885  79.205  1.00 44.08  ? 45   SER   A C    1 
ATOM   357  O  O    . SER   A 1 66  ? 335.611 15.220  78.420  1.00 43.02  ? 45   SER   A O    1 
ATOM   358  C  CB   . SER   A 1 66  ? 333.723 12.622  79.699  1.00 41.74  ? 45   SER   A CB   1 
ATOM   359  O  OG   . SER   A 1 66  ? 334.813 11.801  79.319  1.00 42.79  ? 45   SER   A OG   1 
ATOM   360  N  N    . GLU   A 1 67  ? 334.628 15.370  80.445  1.00 48.50  ? 46   GLU   A N    1 
ATOM   361  C  CA   . GLU   A 1 67  ? 335.429 16.522  80.846  1.00 49.12  ? 46   GLU   A CA   1 
ATOM   362  C  C    . GLU   A 1 67  ? 336.919 16.207  80.861  1.00 48.23  ? 46   GLU   A C    1 
ATOM   363  O  O    . GLU   A 1 67  ? 337.738 17.051  80.479  1.00 52.14  ? 46   GLU   A O    1 
ATOM   364  C  CB   . GLU   A 1 67  ? 334.971 17.022  82.213  1.00 51.28  ? 46   GLU   A CB   1 
ATOM   365  C  CG   . GLU   A 1 67  ? 333.778 17.951  82.132  1.00 64.99  ? 46   GLU   A CG   1 
ATOM   366  C  CD   . GLU   A 1 67  ? 334.071 19.184  81.300  1.00 70.57  ? 46   GLU   A CD   1 
ATOM   367  O  OE1  . GLU   A 1 67  ? 335.211 19.692  81.368  1.00 74.07  ? 46   GLU   A OE1  1 
ATOM   368  O  OE2  . GLU   A 1 67  ? 333.165 19.642  80.573  1.00 74.13  ? 46   GLU   A OE2  1 
ATOM   369  N  N    . HIS   A 1 68  ? 337.293 15.007  81.296  1.00 47.81  ? 47   HIS   A N    1 
ATOM   370  C  CA   . HIS   A 1 68  ? 338.694 14.661  81.493  1.00 46.74  ? 47   HIS   A CA   1 
ATOM   371  C  C    . HIS   A 1 68  ? 339.328 14.019  80.268  1.00 44.20  ? 47   HIS   A C    1 
ATOM   372  O  O    . HIS   A 1 68  ? 340.446 13.500  80.362  1.00 43.71  ? 47   HIS   A O    1 
ATOM   373  C  CB   . HIS   A 1 68  ? 338.834 13.746  82.708  1.00 45.13  ? 47   HIS   A CB   1 
ATOM   374  C  CG   . HIS   A 1 68  ? 338.342 14.372  83.975  1.00 52.35  ? 47   HIS   A CG   1 
ATOM   375  N  ND1  . HIS   A 1 68  ? 337.509 13.719  84.857  1.00 59.58  ? 47   HIS   A ND1  1 
ATOM   376  C  CD2  . HIS   A 1 68  ? 338.552 15.604  84.495  1.00 49.59  ? 47   HIS   A CD2  1 
ATOM   377  C  CE1  . HIS   A 1 68  ? 337.233 14.520  85.872  1.00 61.36  ? 47   HIS   A CE1  1 
ATOM   378  N  NE2  . HIS   A 1 68  ? 337.854 15.669  85.677  1.00 60.54  ? 47   HIS   A NE2  1 
ATOM   379  N  N    . VAL   A 1 69  ? 338.648 14.048  79.127  1.00 44.91  ? 48   VAL   A N    1 
ATOM   380  C  CA   . VAL   A 1 69  ? 339.207 13.604  77.858  1.00 46.29  ? 48   VAL   A CA   1 
ATOM   381  C  C    . VAL   A 1 69  ? 339.329 14.823  76.957  1.00 43.32  ? 48   VAL   A C    1 
ATOM   382  O  O    . VAL   A 1 69  ? 338.323 15.461  76.624  1.00 46.91  ? 48   VAL   A O    1 
ATOM   383  C  CB   . VAL   A 1 69  ? 338.343 12.517  77.200  1.00 41.46  ? 48   VAL   A CB   1 
ATOM   384  C  CG1  . VAL   A 1 69  ? 338.957 12.086  75.877  1.00 34.71  ? 48   VAL   A CG1  1 
ATOM   385  C  CG2  . VAL   A 1 69  ? 338.175 11.326  78.135  1.00 39.65  ? 48   VAL   A CG2  1 
ATOM   386  N  N    . TRP   A 1 70  ? 340.559 15.165  76.588  1.00 43.65  ? 49   TRP   A N    1 
ATOM   387  C  CA   . TRP   A 1 70  ? 340.783 16.174  75.566  1.00 41.22  ? 49   TRP   A CA   1 
ATOM   388  C  C    . TRP   A 1 70  ? 340.688 15.522  74.195  1.00 42.07  ? 49   TRP   A C    1 
ATOM   389  O  O    . TRP   A 1 70  ? 341.225 14.434  73.973  1.00 42.75  ? 49   TRP   A O    1 
ATOM   390  C  CB   . TRP   A 1 70  ? 342.156 16.829  75.738  1.00 46.04  ? 49   TRP   A CB   1 
ATOM   391  C  CG   . TRP   A 1 70  ? 342.385 17.504  77.068  1.00 52.02  ? 49   TRP   A CG   1 
ATOM   392  C  CD1  . TRP   A 1 70  ? 342.838 16.923  78.219  1.00 52.61  ? 49   TRP   A CD1  1 
ATOM   393  C  CD2  . TRP   A 1 70  ? 342.197 18.894  77.369  1.00 63.78  ? 49   TRP   A CD2  1 
ATOM   394  N  NE1  . TRP   A 1 70  ? 342.932 17.864  79.220  1.00 63.47  ? 49   TRP   A NE1  1 
ATOM   395  C  CE2  . TRP   A 1 70  ? 342.545 19.080  78.723  1.00 64.56  ? 49   TRP   A CE2  1 
ATOM   396  C  CE3  . TRP   A 1 70  ? 341.762 19.996  76.627  1.00 67.53  ? 49   TRP   A CE3  1 
ATOM   397  C  CZ2  . TRP   A 1 70  ? 342.471 20.325  79.348  1.00 67.09  ? 49   TRP   A CZ2  1 
ATOM   398  C  CZ3  . TRP   A 1 70  ? 341.691 21.232  77.251  1.00 69.32  ? 49   TRP   A CZ3  1 
ATOM   399  C  CH2  . TRP   A 1 70  ? 342.043 21.385  78.597  1.00 69.39  ? 49   TRP   A CH2  1 
ATOM   400  N  N    . VAL   A 1 71  ? 339.985 16.175  73.277  1.00 42.29  ? 50   VAL   A N    1 
ATOM   401  C  CA   . VAL   A 1 71  ? 339.762 15.632  71.942  1.00 41.76  ? 50   VAL   A CA   1 
ATOM   402  C  C    . VAL   A 1 71  ? 340.078 16.704  70.913  1.00 42.09  ? 50   VAL   A C    1 
ATOM   403  O  O    . VAL   A 1 71  ? 339.576 17.830  71.005  1.00 45.63  ? 50   VAL   A O    1 
ATOM   404  C  CB   . VAL   A 1 71  ? 338.322 15.120  71.762  1.00 42.64  ? 50   VAL   A CB   1 
ATOM   405  C  CG1  . VAL   A 1 71  ? 338.118 14.595  70.343  1.00 38.37  ? 50   VAL   A CG1  1 
ATOM   406  C  CG2  . VAL   A 1 71  ? 338.017 14.041  72.787  1.00 41.28  ? 50   VAL   A CG2  1 
ATOM   407  N  N    . GLU   A 1 72  ? 340.909 16.354  69.940  1.00 43.01  ? 51   GLU   A N    1 
ATOM   408  C  CA   . GLU   A 1 72  ? 341.230 17.222  68.821  1.00 43.01  ? 51   GLU   A CA   1 
ATOM   409  C  C    . GLU   A 1 72  ? 340.821 16.539  67.528  1.00 43.60  ? 51   GLU   A C    1 
ATOM   410  O  O    . GLU   A 1 72  ? 341.053 15.338  67.351  1.00 39.94  ? 51   GLU   A O    1 
ATOM   411  C  CB   . GLU   A 1 72  ? 342.722 17.541  68.768  1.00 42.66  ? 51   GLU   A CB   1 
ATOM   412  C  CG   . GLU   A 1 72  ? 343.265 18.251  69.984  1.00 47.70  ? 51   GLU   A CG   1 
ATOM   413  C  CD   . GLU   A 1 72  ? 344.775 18.199  70.034  1.00 52.16  ? 51   GLU   A CD   1 
ATOM   414  O  OE1  . GLU   A 1 72  ? 345.316 17.154  70.455  1.00 49.59  ? 51   GLU   A OE1  1 
ATOM   415  O  OE2  . GLU   A 1 72  ? 345.422 19.190  69.632  1.00 51.00  ? 51   GLU   A OE2  1 
ATOM   416  N  N    . VAL   A 1 73  ? 340.205 17.297  66.635  1.00 41.66  ? 52   VAL   A N    1 
ATOM   417  C  CA   . VAL   A 1 73  ? 340.020 16.859  65.259  1.00 42.68  ? 52   VAL   A CA   1 
ATOM   418  C  C    . VAL   A 1 73  ? 341.234 17.317  64.465  1.00 43.31  ? 52   VAL   A C    1 
ATOM   419  O  O    . VAL   A 1 73  ? 341.645 18.479  64.560  1.00 44.92  ? 52   VAL   A O    1 
ATOM   420  C  CB   . VAL   A 1 73  ? 338.714 17.414  64.665  1.00 48.78  ? 52   VAL   A CB   1 
ATOM   421  C  CG1  . VAL   A 1 73  ? 338.523 16.905  63.241  1.00 40.04  ? 52   VAL   A CG1  1 
ATOM   422  C  CG2  . VAL   A 1 73  ? 337.525 17.027  65.532  1.00 47.49  ? 52   VAL   A CG2  1 
ATOM   423  N  N    . VAL   A 1 74  ? 341.829 16.399  63.711  1.00 47.57  ? 53   VAL   A N    1 
ATOM   424  C  CA   . VAL   A 1 74  ? 343.055 16.652  62.964  1.00 46.95  ? 53   VAL   A CA   1 
ATOM   425  C  C    . VAL   A 1 74  ? 342.742 16.454  61.485  1.00 49.52  ? 53   VAL   A C    1 
ATOM   426  O  O    . VAL   A 1 74  ? 342.371 15.344  61.067  1.00 48.62  ? 53   VAL   A O    1 
ATOM   427  C  CB   . VAL   A 1 74  ? 344.191 15.726  63.428  1.00 47.74  ? 53   VAL   A CB   1 
ATOM   428  C  CG1  . VAL   A 1 74  ? 345.458 16.003  62.647  1.00 52.61  ? 53   VAL   A CG1  1 
ATOM   429  C  CG2  . VAL   A 1 74  ? 344.434 15.886  64.929  1.00 44.74  ? 53   VAL   A CG2  1 
ATOM   430  N  N    . ARG   A 1 75  ? 342.894 17.524  60.698  1.00 55.42  ? 54   ARG   A N    1 
ATOM   431  C  CA   . ARG   A 1 75  ? 342.456 17.555  59.302  1.00 55.98  ? 54   ARG   A CA   1 
ATOM   432  C  C    . ARG   A 1 75  ? 343.632 17.897  58.400  1.00 64.94  ? 54   ARG   A C    1 
ATOM   433  O  O    . ARG   A 1 75  ? 343.756 19.023  57.926  1.00 75.66  ? 54   ARG   A O    1 
ATOM   434  C  CB   . ARG   A 1 75  ? 341.301 18.561  59.132  1.00 56.14  ? 54   ARG   A CB   1 
ATOM   435  N  N    . ASP   A 1 76  ? 344.476 16.901  58.139  1.00 64.59  ? 55   ASP   A N    1 
ATOM   436  C  CA   . ASP   A 1 76  ? 345.681 17.063  57.331  1.00 65.47  ? 55   ASP   A CA   1 
ATOM   437  C  C    . ASP   A 1 76  ? 346.793 17.679  58.172  1.00 66.30  ? 55   ASP   A C    1 
ATOM   438  O  O    . ASP   A 1 76  ? 347.473 18.613  57.733  1.00 73.45  ? 55   ASP   A O    1 
ATOM   439  C  CB   . ASP   A 1 76  ? 345.404 17.924  56.090  1.00 70.69  ? 55   ASP   A CB   1 
ATOM   440  N  N    . GLY   A 1 77  ? 346.988 17.152  59.377  1.00 66.18  ? 56   GLY   A N    1 
ATOM   441  C  CA   . GLY   A 1 77  ? 348.046 17.587  60.255  1.00 66.93  ? 56   GLY   A CA   1 
ATOM   442  C  C    . GLY   A 1 77  ? 347.704 18.755  61.157  1.00 71.19  ? 56   GLY   A C    1 
ATOM   443  O  O    . GLY   A 1 77  ? 348.448 19.013  62.114  1.00 69.26  ? 56   GLY   A O    1 
ATOM   444  N  N    . GLU   A 1 78  ? 346.611 19.466  60.889  1.00 73.18  ? 57   GLU   A N    1 
ATOM   445  C  CA   . GLU   A 1 78  ? 346.202 20.620  61.683  1.00 69.62  ? 57   GLU   A CA   1 
ATOM   446  C  C    . GLU   A 1 78  ? 345.131 20.189  62.678  1.00 55.51  ? 57   GLU   A C    1 
ATOM   447  O  O    . GLU   A 1 78  ? 344.055 19.732  62.278  1.00 55.60  ? 57   GLU   A O    1 
ATOM   448  C  CB   . GLU   A 1 78  ? 345.686 21.743  60.782  1.00 61.71  ? 57   GLU   A CB   1 
ATOM   449  N  N    . ALA   A 1 79  ? 345.426 20.340  63.967  1.00 54.78  ? 58   ALA   A N    1 
ATOM   450  C  CA   . ALA   A 1 79  ? 344.561 19.868  65.038  1.00 52.84  ? 58   ALA   A CA   1 
ATOM   451  C  C    . ALA   A 1 79  ? 343.706 21.005  65.581  1.00 55.97  ? 58   ALA   A C    1 
ATOM   452  O  O    . ALA   A 1 79  ? 344.156 22.152  65.665  1.00 64.06  ? 58   ALA   A O    1 
ATOM   453  C  CB   . ALA   A 1 79  ? 345.387 19.257  66.171  1.00 51.74  ? 58   ALA   A CB   1 
ATOM   454  N  N    . GLU   A 1 80  ? 342.471 20.677  65.960  1.00 56.31  ? 59   GLU   A N    1 
ATOM   455  C  CA   . GLU   A 1 80  ? 341.539 21.643  66.531  1.00 52.53  ? 59   GLU   A CA   1 
ATOM   456  C  C    . GLU   A 1 80  ? 340.929 21.051  67.792  1.00 51.79  ? 59   GLU   A C    1 
ATOM   457  O  O    . GLU   A 1 80  ? 340.353 19.959  67.753  1.00 52.90  ? 59   GLU   A O    1 
ATOM   458  C  CB   . GLU   A 1 80  ? 340.442 22.022  65.532  1.00 50.48  ? 59   GLU   A CB   1 
ATOM   459  C  CG   . GLU   A 1 80  ? 339.496 23.090  66.052  1.00 71.38  ? 59   GLU   A CG   1 
ATOM   460  C  CD   . GLU   A 1 80  ? 338.515 23.563  65.000  1.00 82.18  ? 59   GLU   A CD   1 
ATOM   461  O  OE1  . GLU   A 1 80  ? 337.969 22.713  64.266  1.00 72.75  ? 59   GLU   A OE1  1 
ATOM   462  O  OE2  . GLU   A 1 80  ? 338.297 24.789  64.903  1.00 96.16  ? 59   GLU   A OE2  1 
ATOM   463  N  N    . GLU   A 1 81  ? 341.045 21.777  68.899  1.00 52.74  ? 60   GLU   A N    1 
ATOM   464  C  CA   . GLU   A 1 81  ? 340.483 21.325  70.164  1.00 48.20  ? 60   GLU   A CA   1 
ATOM   465  C  C    . GLU   A 1 81  ? 338.965 21.458  70.133  1.00 47.45  ? 60   GLU   A C    1 
ATOM   466  O  O    . GLU   A 1 81  ? 338.432 22.524  69.810  1.00 55.14  ? 60   GLU   A O    1 
ATOM   467  C  CB   . GLU   A 1 81  ? 341.073 22.142  71.311  1.00 45.94  ? 60   GLU   A CB   1 
ATOM   468  C  CG   . GLU   A 1 81  ? 341.049 21.461  72.665  1.00 56.09  ? 60   GLU   A CG   1 
ATOM   469  C  CD   . GLU   A 1 81  ? 341.811 22.248  73.716  1.00 71.76  ? 60   GLU   A CD   1 
ATOM   470  O  OE1  . GLU   A 1 81  ? 341.573 23.468  73.842  1.00 71.15  ? 60   GLU   A OE1  1 
ATOM   471  O  OE2  . GLU   A 1 81  ? 342.661 21.649  74.408  1.00 74.37  ? 60   GLU   A OE2  1 
ATOM   472  N  N    . VAL   A 1 82  ? 338.267 20.377  70.472  1.00 43.32  ? 61   VAL   A N    1 
ATOM   473  C  CA   . VAL   A 1 82  ? 336.813 20.311  70.371  1.00 44.77  ? 61   VAL   A CA   1 
ATOM   474  C  C    . VAL   A 1 82  ? 336.210 20.339  71.768  1.00 48.07  ? 61   VAL   A C    1 
ATOM   475  O  O    . VAL   A 1 82  ? 336.744 19.726  72.700  1.00 42.86  ? 61   VAL   A O    1 
ATOM   476  C  CB   . VAL   A 1 82  ? 336.368 19.050  69.605  1.00 45.18  ? 61   VAL   A CB   1 
ATOM   477  C  CG1  . VAL   A 1 82  ? 334.862 19.056  69.404  1.00 53.76  ? 61   VAL   A CG1  1 
ATOM   478  C  CG2  . VAL   A 1 82  ? 337.090 18.965  68.272  1.00 50.35  ? 61   VAL   A CG2  1 
ATOM   479  N  N    . ALA   A 1 83  ? 335.088 21.044  71.908  1.00 51.40  ? 62   ALA   A N    1 
ATOM   480  C  CA   . ALA   A 1 83  ? 334.388 21.110  73.181  1.00 46.89  ? 62   ALA   A CA   1 
ATOM   481  C  C    . ALA   A 1 83  ? 333.759 19.759  73.520  1.00 52.05  ? 62   ALA   A C    1 
ATOM   482  O  O    . ALA   A 1 83  ? 333.673 18.850  72.689  1.00 50.10  ? 62   ALA   A O    1 
ATOM   483  C  CB   . ALA   A 1 83  ? 333.316 22.199  73.152  1.00 48.34  ? 62   ALA   A CB   1 
ATOM   484  N  N    . THR   A 1 84  ? 333.303 19.643  74.770  1.00 56.26  ? 63   THR   A N    1 
ATOM   485  C  CA   . THR   A 1 84  ? 332.716 18.392  75.238  1.00 47.89  ? 63   THR   A CA   1 
ATOM   486  C  C    . THR   A 1 84  ? 331.390 18.108  74.542  1.00 52.53  ? 63   THR   A C    1 
ATOM   487  O  O    . THR   A 1 84  ? 331.162 16.998  74.048  1.00 52.93  ? 63   THR   A O    1 
ATOM   488  C  CB   . THR   A 1 84  ? 332.524 18.435  76.756  1.00 48.91  ? 63   THR   A CB   1 
ATOM   489  O  OG1  . THR   A 1 84  ? 331.786 19.611  77.116  1.00 51.30  ? 63   THR   A OG1  1 
ATOM   490  C  CG2  . THR   A 1 84  ? 333.870 18.453  77.462  1.00 46.58  ? 63   THR   A CG2  1 
ATOM   491  N  N    . ASN   A 1 85  ? 330.498 19.101  74.494  1.00 64.57  ? 64   ASN   A N    1 
ATOM   492  C  CA   . ASN   A 1 85  ? 329.144 18.934  73.953  1.00 67.10  ? 64   ASN   A CA   1 
ATOM   493  C  C    . ASN   A 1 85  ? 328.928 20.004  72.883  1.00 64.39  ? 64   ASN   A C    1 
ATOM   494  O  O    . ASN   A 1 85  ? 328.231 20.995  73.102  1.00 74.15  ? 64   ASN   A O    1 
ATOM   495  C  CB   . ASN   A 1 85  ? 328.096 19.010  75.060  1.00 61.53  ? 64   ASN   A CB   1 
ATOM   496  C  CG   . ASN   A 1 85  ? 326.811 18.291  74.696  1.00 72.35  ? 64   ASN   A CG   1 
ATOM   497  O  OD1  . ASN   A 1 85  ? 326.721 17.069  74.804  1.00 71.76  ? 64   ASN   A OD1  1 
ATOM   498  N  ND2  . ASN   A 1 85  ? 325.809 19.048  74.263  1.00 77.98  ? 64   ASN   A ND2  1 
ATOM   499  N  N    . GLY   A 1 86  ? 329.529 19.794  71.715  1.00 76.65  ? 65   GLY   A N    1 
ATOM   500  C  CA   . GLY   A 1 86  ? 329.356 20.675  70.577  1.00 75.67  ? 65   GLY   A CA   1 
ATOM   501  C  C    . GLY   A 1 86  ? 328.588 19.963  69.479  1.00 76.12  ? 65   GLY   A C    1 
ATOM   502  O  O    . GLY   A 1 86  ? 328.628 18.734  69.367  1.00 76.92  ? 65   GLY   A O    1 
ATOM   503  N  N    . LYS   A 1 87  ? 327.879 20.744  68.671  1.00 60.40  ? 66   LYS   A N    1 
ATOM   504  C  CA   . LYS   A 1 87  ? 327.115 20.220  67.549  1.00 52.89  ? 66   LYS   A CA   1 
ATOM   505  C  C    . LYS   A 1 87  ? 327.852 20.366  66.224  1.00 51.06  ? 66   LYS   A C    1 
ATOM   506  O  O    . LYS   A 1 87  ? 327.235 20.225  65.163  1.00 53.44  ? 66   LYS   A O    1 
ATOM   507  C  CB   . LYS   A 1 87  ? 325.756 20.916  67.463  1.00 48.68  ? 66   LYS   A CB   1 
ATOM   508  C  CG   . LYS   A 1 87  ? 324.820 20.614  68.617  1.00 49.47  ? 66   LYS   A CG   1 
ATOM   509  C  CD   . LYS   A 1 87  ? 323.582 21.496  68.545  1.00 52.11  ? 66   LYS   A CD   1 
ATOM   510  C  CE   . LYS   A 1 87  ? 322.490 21.012  69.483  1.00 55.67  ? 66   LYS   A CE   1 
ATOM   511  N  NZ   . LYS   A 1 87  ? 321.985 19.669  69.082  1.00 61.10  ? 66   LYS   A NZ   1 
ATOM   512  N  N    . GLN   A 1 88  ? 329.150 20.651  66.258  1.00 48.81  ? 67   GLN   A N    1 
ATOM   513  C  CA   . GLN   A 1 88  ? 329.886 20.876  65.024  1.00 47.26  ? 67   GLN   A CA   1 
ATOM   514  C  C    . GLN   A 1 88  ? 330.044 19.576  64.249  1.00 47.39  ? 67   GLN   A C    1 
ATOM   515  O  O    . GLN   A 1 88  ? 330.227 18.503  64.829  1.00 44.53  ? 67   GLN   A O    1 
ATOM   516  C  CB   . GLN   A 1 88  ? 331.257 21.482  65.318  1.00 51.99  ? 67   GLN   A CB   1 
ATOM   517  C  CG   . GLN   A 1 88  ? 332.102 21.704  64.074  1.00 57.01  ? 67   GLN   A CG   1 
ATOM   518  C  CD   . GLN   A 1 88  ? 333.345 22.527  64.350  1.00 67.49  ? 67   GLN   A CD   1 
ATOM   519  O  OE1  . GLN   A 1 88  ? 333.754 22.692  65.500  1.00 73.89  ? 67   GLN   A OE1  1 
ATOM   520  N  NE2  . GLN   A 1 88  ? 333.950 23.055  63.292  1.00 71.02  ? 67   GLN   A NE2  1 
ATOM   521  N  N    . ARG   A 1 89  ? 329.970 19.681  62.926  1.00 46.40  ? 68   ARG   A N    1 
ATOM   522  C  CA   . ARG   A 1 89  ? 330.150 18.549  62.033  1.00 43.83  ? 68   ARG   A CA   1 
ATOM   523  C  C    . ARG   A 1 89  ? 331.375 18.769  61.158  1.00 46.59  ? 68   ARG   A C    1 
ATOM   524  O  O    . ARG   A 1 89  ? 331.694 19.899  60.776  1.00 46.36  ? 68   ARG   A O    1 
ATOM   525  C  CB   . ARG   A 1 89  ? 328.915 18.329  61.151  1.00 42.26  ? 68   ARG   A CB   1 
ATOM   526  C  CG   . ARG   A 1 89  ? 327.782 17.605  61.854  1.00 48.78  ? 68   ARG   A CG   1 
ATOM   527  C  CD   . ARG   A 1 89  ? 326.509 17.612  61.026  1.00 45.70  ? 68   ARG   A CD   1 
ATOM   528  N  NE   . ARG   A 1 89  ? 325.871 18.923  61.003  1.00 51.28  ? 68   ARG   A NE   1 
ATOM   529  C  CZ   . ARG   A 1 89  ? 324.711 19.178  60.413  1.00 52.07  ? 68   ARG   A CZ   1 
ATOM   530  N  NH1  . ARG   A 1 89  ? 324.026 18.228  59.796  1.00 53.95  ? 68   ARG   A NH1  1 
ATOM   531  N  NH2  . ARG   A 1 89  ? 324.226 20.416  60.442  1.00 50.25  ? 68   ARG   A NH2  1 
ATOM   532  N  N    . TRP   A 1 90  ? 332.063 17.674  60.854  1.00 43.23  ? 69   TRP   A N    1 
ATOM   533  C  CA   . TRP   A 1 90  ? 333.192 17.676  59.941  1.00 43.90  ? 69   TRP   A CA   1 
ATOM   534  C  C    . TRP   A 1 90  ? 332.939 16.675  58.825  1.00 47.98  ? 69   TRP   A C    1 
ATOM   535  O  O    . TRP   A 1 90  ? 332.287 15.646  59.027  1.00 46.14  ? 69   TRP   A O    1 
ATOM   536  C  CB   . TRP   A 1 90  ? 334.501 17.317  60.653  1.00 43.35  ? 69   TRP   A CB   1 
ATOM   537  C  CG   . TRP   A 1 90  ? 334.876 18.249  61.758  1.00 52.06  ? 69   TRP   A CG   1 
ATOM   538  C  CD1  . TRP   A 1 90  ? 335.733 19.309  61.682  1.00 51.59  ? 69   TRP   A CD1  1 
ATOM   539  C  CD2  . TRP   A 1 90  ? 334.415 18.202  63.113  1.00 51.10  ? 69   TRP   A CD2  1 
ATOM   540  N  NE1  . TRP   A 1 90  ? 335.831 19.927  62.906  1.00 52.61  ? 69   TRP   A NE1  1 
ATOM   541  C  CE2  . TRP   A 1 90  ? 335.031 19.266  63.802  1.00 53.77  ? 69   TRP   A CE2  1 
ATOM   542  C  CE3  . TRP   A 1 90  ? 333.538 17.364  63.811  1.00 44.57  ? 69   TRP   A CE3  1 
ATOM   543  C  CZ2  . TRP   A 1 90  ? 334.799 19.515  65.153  1.00 52.62  ? 69   TRP   A CZ2  1 
ATOM   544  C  CZ3  . TRP   A 1 90  ? 333.310 17.613  65.153  1.00 49.31  ? 69   TRP   A CZ3  1 
ATOM   545  C  CH2  . TRP   A 1 90  ? 333.938 18.679  65.809  1.00 52.05  ? 69   TRP   A CH2  1 
ATOM   546  N  N    . LEU   A 1 91  ? 333.463 16.984  57.644  1.00 51.23  ? 70   LEU   A N    1 
ATOM   547  C  CA   . LEU   A 1 91  ? 333.383 16.047  56.535  1.00 47.00  ? 70   LEU   A CA   1 
ATOM   548  C  C    . LEU   A 1 91  ? 334.198 14.801  56.854  1.00 46.65  ? 70   LEU   A C    1 
ATOM   549  O  O    . LEU   A 1 91  ? 335.342 14.893  57.311  1.00 49.96  ? 70   LEU   A O    1 
ATOM   550  C  CB   . LEU   A 1 91  ? 333.883 16.700  55.248  1.00 50.21  ? 70   LEU   A CB   1 
ATOM   551  C  CG   . LEU   A 1 91  ? 332.873 17.564  54.488  1.00 58.48  ? 70   LEU   A CG   1 
ATOM   552  C  CD1  . LEU   A 1 91  ? 332.068 18.444  55.435  1.00 65.53  ? 70   LEU   A CD1  1 
ATOM   553  C  CD2  . LEU   A 1 91  ? 333.578 18.411  53.439  1.00 72.87  ? 70   LEU   A CD2  1 
ATOM   554  N  N    . LEU   A 1 92  ? 333.597 13.635  56.633  1.00 51.60  ? 71   LEU   A N    1 
ATOM   555  C  CA   . LEU   A 1 92  ? 334.307 12.378  56.822  1.00 45.54  ? 71   LEU   A CA   1 
ATOM   556  C  C    . LEU   A 1 92  ? 335.404 12.233  55.777  1.00 45.78  ? 71   LEU   A C    1 
ATOM   557  O  O    . LEU   A 1 92  ? 335.146 12.333  54.573  1.00 45.15  ? 71   LEU   A O    1 
ATOM   558  C  CB   . LEU   A 1 92  ? 333.335 11.204  56.729  1.00 39.08  ? 71   LEU   A CB   1 
ATOM   559  C  CG   . LEU   A 1 92  ? 332.521 10.874  57.975  1.00 38.86  ? 71   LEU   A CG   1 
ATOM   560  C  CD1  . LEU   A 1 92  ? 331.312 10.034  57.604  1.00 43.50  ? 71   LEU   A CD1  1 
ATOM   561  C  CD2  . LEU   A 1 92  ? 333.393 10.138  58.975  1.00 45.19  ? 71   LEU   A CD2  1 
ATOM   562  N  N    . SER   A 1 93  ? 336.633 11.989  56.238  1.00 47.91  ? 72   SER   A N    1 
ATOM   563  C  CA   . SER   A 1 93  ? 337.767 11.808  55.350  1.00 47.64  ? 72   SER   A CA   1 
ATOM   564  C  C    . SER   A 1 93  ? 338.786 10.899  56.018  1.00 48.61  ? 72   SER   A C    1 
ATOM   565  O  O    . SER   A 1 93  ? 338.953 10.970  57.244  1.00 49.77  ? 72   SER   A O    1 
ATOM   566  C  CB   . SER   A 1 93  ? 338.425 13.143  54.991  1.00 50.42  ? 72   SER   A CB   1 
ATOM   567  O  OG   . SER   A 1 93  ? 339.726 12.938  54.469  1.00 55.46  ? 72   SER   A OG   1 
ATOM   568  N  N    . PRO   A 1 94  ? 339.476 10.045  55.259  1.00 51.55  ? 73   PRO   A N    1 
ATOM   569  C  CA   . PRO   A 1 94  ? 340.547 9.249   55.878  1.00 52.89  ? 73   PRO   A CA   1 
ATOM   570  C  C    . PRO   A 1 94  ? 341.625 10.106  56.516  1.00 51.17  ? 73   PRO   A C    1 
ATOM   571  O  O    . PRO   A 1 94  ? 342.281 9.656   57.464  1.00 51.64  ? 73   PRO   A O    1 
ATOM   572  C  CB   . PRO   A 1 94  ? 341.093 8.416   54.708  1.00 46.95  ? 73   PRO   A CB   1 
ATOM   573  C  CG   . PRO   A 1 94  ? 340.625 9.118   53.469  1.00 49.08  ? 73   PRO   A CG   1 
ATOM   574  C  CD   . PRO   A 1 94  ? 339.313 9.740   53.828  1.00 50.14  ? 73   PRO   A CD   1 
ATOM   575  N  N    . SER   A 1 95  ? 341.815 11.333  56.037  1.00 49.43  ? 74   SER   A N    1 
ATOM   576  C  CA   . SER   A 1 95  ? 342.840 12.226  56.561  1.00 52.79  ? 74   SER   A CA   1 
ATOM   577  C  C    . SER   A 1 95  ? 342.333 13.125  57.680  1.00 52.19  ? 74   SER   A C    1 
ATOM   578  O  O    . SER   A 1 95  ? 343.084 13.984  58.153  1.00 49.81  ? 74   SER   A O    1 
ATOM   579  C  CB   . SER   A 1 95  ? 343.421 13.084  55.432  1.00 52.28  ? 74   SER   A CB   1 
ATOM   580  O  OG   . SER   A 1 95  ? 342.460 13.998  54.939  1.00 50.93  ? 74   SER   A OG   1 
ATOM   581  N  N    . THR   A 1 96  ? 341.084 12.959  58.103  1.00 53.81  ? 75   THR   A N    1 
ATOM   582  C  CA   . THR   A 1 96  ? 340.545 13.646  59.271  1.00 48.92  ? 75   THR   A CA   1 
ATOM   583  C  C    . THR   A 1 96  ? 340.368 12.621  60.382  1.00 45.11  ? 75   THR   A C    1 
ATOM   584  O  O    . THR   A 1 96  ? 339.613 11.654  60.226  1.00 43.14  ? 75   THR   A O    1 
ATOM   585  C  CB   . THR   A 1 96  ? 339.219 14.339  58.952  1.00 50.13  ? 75   THR   A CB   1 
ATOM   586  O  OG1  . THR   A 1 96  ? 339.427 15.327  57.935  1.00 52.63  ? 75   THR   A OG1  1 
ATOM   587  C  CG2  . THR   A 1 96  ? 338.665 15.016  60.198  1.00 42.56  ? 75   THR   A CG2  1 
ATOM   588  N  N    . THR   A 1 97  ? 341.068 12.830  61.495  1.00 46.19  ? 76   THR   A N    1 
ATOM   589  C  CA   . THR   A 1 97  ? 341.096 11.875  62.592  1.00 47.01  ? 76   THR   A CA   1 
ATOM   590  C  C    . THR   A 1 97  ? 340.924 12.623  63.905  1.00 40.15  ? 76   THR   A C    1 
ATOM   591  O  O    . THR   A 1 97  ? 340.785 13.849  63.937  1.00 39.47  ? 76   THR   A O    1 
ATOM   592  C  CB   . THR   A 1 97  ? 342.404 11.076  62.604  1.00 42.67  ? 76   THR   A CB   1 
ATOM   593  O  OG1  . THR   A 1 97  ? 343.498 11.960  62.883  1.00 44.04  ? 76   THR   A OG1  1 
ATOM   594  C  CG2  . THR   A 1 97  ? 342.633 10.412  61.260  1.00 44.06  ? 76   THR   A CG2  1 
ATOM   595  N  N    . LEU   A 1 98  ? 340.941 11.871  64.998  1.00 36.76  ? 77   LEU   A N    1 
ATOM   596  C  CA   . LEU   A 1 98  ? 340.954 12.441  66.333  1.00 38.17  ? 77   LEU   A CA   1 
ATOM   597  C  C    . LEU   A 1 98  ? 342.279 12.122  67.011  1.00 38.21  ? 77   LEU   A C    1 
ATOM   598  O  O    . LEU   A 1 98  ? 342.883 11.070  66.777  1.00 35.71  ? 77   LEU   A O    1 
ATOM   599  C  CB   . LEU   A 1 98  ? 339.793 11.908  67.183  1.00 34.07  ? 77   LEU   A CB   1 
ATOM   600  C  CG   . LEU   A 1 98  ? 338.414 11.835  66.525  1.00 33.12  ? 77   LEU   A CG   1 
ATOM   601  C  CD1  . LEU   A 1 98  ? 337.375 11.265  67.484  1.00 34.90  ? 77   LEU   A CD1  1 
ATOM   602  C  CD2  . LEU   A 1 98  ? 337.977 13.197  66.013  1.00 39.48  ? 77   LEU   A CD2  1 
ATOM   603  N  N    . ARG   A 1 99  ? 342.738 13.061  67.829  1.00 36.79  ? 78   ARG   A N    1 
ATOM   604  C  CA   . ARG   A 1 99  ? 343.794 12.823  68.801  1.00 35.34  ? 78   ARG   A CA   1 
ATOM   605  C  C    . ARG   A 1 99  ? 343.155 12.922  70.178  1.00 38.34  ? 78   ARG   A C    1 
ATOM   606  O  O    . ARG   A 1 99  ? 342.517 13.932  70.495  1.00 43.26  ? 78   ARG   A O    1 
ATOM   607  C  CB   . ARG   A 1 99  ? 344.938 13.824  68.639  1.00 45.36  ? 78   ARG   A CB   1 
ATOM   608  C  CG   . ARG   A 1 99  ? 346.153 13.490  69.483  1.00 47.71  ? 78   ARG   A CG   1 
ATOM   609  C  CD   . ARG   A 1 99  ? 347.426 14.125  68.943  1.00 55.35  ? 78   ARG   A CD   1 
ATOM   610  N  NE   . ARG   A 1 99  ? 347.463 15.572  69.117  1.00 58.52  ? 78   ARG   A NE   1 
ATOM   611  C  CZ   . ARG   A 1 99  ? 347.565 16.443  68.123  1.00 63.66  ? 78   ARG   A CZ   1 
ATOM   612  N  NH1  . ARG   A 1 99  ? 347.643 16.048  66.862  1.00 65.14  ? 78   ARG   A NH1  1 
ATOM   613  N  NH2  . ARG   A 1 99  ? 347.600 17.744  68.401  1.00 62.13  ? 78   ARG   A NH2  1 
ATOM   614  N  N    . VAL   A 1 100 ? 343.295 11.867  70.978  1.00 35.43  ? 79   VAL   A N    1 
ATOM   615  C  CA   . VAL   A 1 100 ? 342.613 11.749  72.263  1.00 37.89  ? 79   VAL   A CA   1 
ATOM   616  C  C    . VAL   A 1 100 ? 343.670 11.677  73.352  1.00 36.99  ? 79   VAL   A C    1 
ATOM   617  O  O    . VAL   A 1 100 ? 344.543 10.800  73.320  1.00 37.97  ? 79   VAL   A O    1 
ATOM   618  C  CB   . VAL   A 1 100 ? 341.692 10.519  72.317  1.00 37.67  ? 79   VAL   A CB   1 
ATOM   619  C  CG1  . VAL   A 1 100 ? 341.162 10.315  73.728  1.00 34.57  ? 79   VAL   A CG1  1 
ATOM   620  C  CG2  . VAL   A 1 100 ? 340.544 10.669  71.334  1.00 31.75  ? 79   VAL   A CG2  1 
ATOM   621  N  N    . THR   A 1 101 ? 343.584 12.581  74.322  1.00 39.29  ? 80   THR   A N    1 
ATOM   622  C  CA   A THR   A 1 101 ? 344.562 12.646  75.395  0.50 41.09  ? 80   THR   A CA   1 
ATOM   623  C  CA   B THR   A 1 101 ? 344.563 12.661  75.394  0.50 41.13  ? 80   THR   A CA   1 
ATOM   624  C  C    . THR   A 1 101 ? 343.857 12.823  76.731  1.00 38.44  ? 80   THR   A C    1 
ATOM   625  O  O    . THR   A 1 101 ? 342.795 13.444  76.819  1.00 40.04  ? 80   THR   A O    1 
ATOM   626  C  CB   A THR   A 1 101 ? 345.561 13.790  75.179  0.50 37.64  ? 80   THR   A CB   1 
ATOM   627  C  CB   B THR   A 1 101 ? 345.534 13.830  75.182  0.50 39.12  ? 80   THR   A CB   1 
ATOM   628  O  OG1  A THR   A 1 101 ? 346.498 13.817  76.263  0.50 41.12  ? 80   THR   A OG1  1 
ATOM   629  O  OG1  B THR   A 1 101 ? 344.823 15.067  75.300  0.50 45.01  ? 80   THR   A OG1  1 
ATOM   630  C  CG2  A THR   A 1 101 ? 344.835 15.120  75.110  0.50 44.97  ? 80   THR   A CG2  1 
ATOM   631  C  CG2  B THR   A 1 101 ? 346.161 13.753  73.800  0.50 40.06  ? 80   THR   A CG2  1 
ATOM   632  N  N    . MET   A 1 102 ? 344.465 12.257  77.768  1.00 39.63  ? 81   MET   A N    1 
ATOM   633  C  CA   . MET   A 1 102 ? 344.015 12.397  79.141  1.00 40.33  ? 81   MET   A CA   1 
ATOM   634  C  C    . MET   A 1 102 ? 345.231 12.700  80.004  1.00 40.51  ? 81   MET   A C    1 
ATOM   635  O  O    . MET   A 1 102 ? 346.357 12.335  79.658  1.00 43.96  ? 81   MET   A O    1 
ATOM   636  C  CB   . MET   A 1 102 ? 343.305 11.129  79.644  1.00 40.55  ? 81   MET   A CB   1 
ATOM   637  C  CG   . MET   A 1 102 ? 342.134 10.688  78.779  1.00 41.88  ? 81   MET   A CG   1 
ATOM   638  S  SD   . MET   A 1 102 ? 341.268 9.244   79.430  1.00 37.98  ? 81   MET   A SD   1 
ATOM   639  C  CE   . MET   A 1 102 ? 340.649 9.871   80.990  1.00 34.64  ? 81   MET   A CE   1 
ATOM   640  N  N    . SER   A 1 103 ? 345.005 13.383  81.123  1.00 44.48  ? 82   SER   A N    1 
ATOM   641  C  CA   . SER   A 1 103 ? 346.094 13.711  82.032  1.00 48.69  ? 82   SER   A CA   1 
ATOM   642  C  C    . SER   A 1 103 ? 345.863 13.255  83.464  1.00 49.29  ? 82   SER   A C    1 
ATOM   643  O  O    . SER   A 1 103 ? 346.793 13.342  84.273  1.00 54.54  ? 82   SER   A O    1 
ATOM   644  C  CB   . SER   A 1 103 ? 346.360 15.224  82.034  1.00 45.02  ? 82   SER   A CB   1 
ATOM   645  O  OG   . SER   A 1 103 ? 345.224 15.933  82.490  1.00 52.84  ? 82   SER   A OG   1 
ATOM   646  N  N    . GLN   A 1 104 ? 344.671 12.781  83.805  1.00 46.41  ? 83   GLN   A N    1 
ATOM   647  C  CA   . GLN   A 1 104 ? 344.375 12.272  85.134  1.00 43.55  ? 83   GLN   A CA   1 
ATOM   648  C  C    . GLN   A 1 104 ? 343.847 10.851  85.018  1.00 42.95  ? 83   GLN   A C    1 
ATOM   649  O  O    . GLN   A 1 104 ? 343.132 10.518  84.068  1.00 40.96  ? 83   GLN   A O    1 
ATOM   650  C  CB   . GLN   A 1 104 ? 343.353 13.155  85.856  1.00 43.51  ? 83   GLN   A CB   1 
ATOM   651  N  N    . ALA   A 1 105 ? 344.211 10.013  85.981  1.00 41.95  ? 84   ALA   A N    1 
ATOM   652  C  CA   . ALA   A 1 105 ? 343.727 8.643   85.991  1.00 43.89  ? 84   ALA   A CA   1 
ATOM   653  C  C    . ALA   A 1 105 ? 342.242 8.605   86.331  1.00 42.16  ? 84   ALA   A C    1 
ATOM   654  O  O    . ALA   A 1 105 ? 341.719 9.471   87.038  1.00 43.54  ? 84   ALA   A O    1 
ATOM   655  C  CB   . ALA   A 1 105 ? 344.523 7.804   86.991  1.00 40.12  ? 84   ALA   A CB   1 
ATOM   656  N  N    . SER   A 1 106 ? 341.556 7.594   85.805  1.00 38.30  ? 85   SER   A N    1 
ATOM   657  C  CA   . SER   A 1 106 ? 340.143 7.422   86.105  1.00 46.94  ? 85   SER   A CA   1 
ATOM   658  C  C    . SER   A 1 106 ? 339.957 6.967   87.547  1.00 50.48  ? 85   SER   A C    1 
ATOM   659  O  O    . SER   A 1 106 ? 340.842 6.353   88.149  1.00 50.62  ? 85   SER   A O    1 
ATOM   660  C  CB   . SER   A 1 106 ? 339.511 6.403   85.157  1.00 39.62  ? 85   SER   A CB   1 
ATOM   661  O  OG   . SER   A 1 106 ? 339.792 6.713   83.804  1.00 42.94  ? 85   SER   A OG   1 
ATOM   662  N  N    . THR   A 1 107 ? 338.787 7.283   88.103  1.00 53.31  ? 86   THR   A N    1 
ATOM   663  C  CA   . THR   A 1 107 ? 338.388 6.759   89.403  1.00 54.23  ? 86   THR   A CA   1 
ATOM   664  C  C    . THR   A 1 107 ? 337.151 5.883   89.236  1.00 54.20  ? 86   THR   A C    1 
ATOM   665  O  O    . THR   A 1 107 ? 336.826 5.466   88.119  1.00 56.16  ? 86   THR   A O    1 
ATOM   666  C  CB   . THR   A 1 107 ? 338.119 7.893   90.399  1.00 57.06  ? 86   THR   A CB   1 
ATOM   667  O  OG1  . THR   A 1 107 ? 336.989 8.664   89.970  1.00 54.42  ? 86   THR   A OG1  1 
ATOM   668  C  CG2  . THR   A 1 107 ? 339.333 8.806   90.510  1.00 51.64  ? 86   THR   A CG2  1 
ATOM   669  N  N    . GLU   A 1 108 ? 336.456 5.591   90.335  1.00 63.48  ? 87   GLU   A N    1 
ATOM   670  C  CA   . GLU   A 1 108 ? 335.217 4.829   90.233  1.00 70.54  ? 87   GLU   A CA   1 
ATOM   671  C  C    . GLU   A 1 108 ? 334.066 5.679   89.707  1.00 69.93  ? 87   GLU   A C    1 
ATOM   672  O  O    . GLU   A 1 108 ? 333.127 5.140   89.111  1.00 73.87  ? 87   GLU   A O    1 
ATOM   673  C  CB   . GLU   A 1 108 ? 334.858 4.225   91.593  1.00 75.04  ? 87   GLU   A CB   1 
ATOM   674  C  CG   . GLU   A 1 108 ? 335.781 3.092   92.013  1.00 75.97  ? 87   GLU   A CG   1 
ATOM   675  C  CD   . GLU   A 1 108 ? 335.716 1.910   91.063  1.00 78.07  ? 87   GLU   A CD   1 
ATOM   676  O  OE1  . GLU   A 1 108 ? 334.622 1.327   90.915  1.00 80.95  ? 87   GLU   A OE1  1 
ATOM   677  O  OE2  . GLU   A 1 108 ? 336.756 1.570   90.458  1.00 70.74  ? 87   GLU   A OE2  1 
ATOM   678  N  N    . ALA   A 1 109 ? 334.121 6.995   89.910  1.00 77.39  ? 88   ALA   A N    1 
ATOM   679  C  CA   . ALA   A 1 109 ? 333.103 7.916   89.421  1.00 76.18  ? 88   ALA   A CA   1 
ATOM   680  C  C    . ALA   A 1 109 ? 333.391 8.420   88.012  1.00 71.92  ? 88   ALA   A C    1 
ATOM   681  O  O    . ALA   A 1 109 ? 332.710 9.340   87.545  1.00 67.59  ? 88   ALA   A O    1 
ATOM   682  C  CB   . ALA   A 1 109 ? 332.962 9.103   90.379  1.00 67.60  ? 88   ALA   A CB   1 
ATOM   683  N  N    . SER   A 1 110 ? 334.378 7.844   87.331  1.00 65.99  ? 89   SER   A N    1 
ATOM   684  C  CA   . SER   A 1 110 ? 334.743 8.294   85.997  1.00 67.22  ? 89   SER   A CA   1 
ATOM   685  C  C    . SER   A 1 110 ? 333.833 7.676   84.945  1.00 65.01  ? 89   SER   A C    1 
ATOM   686  O  O    . SER   A 1 110 ? 333.432 6.513   85.046  1.00 66.54  ? 89   SER   A O    1 
ATOM   687  C  CB   . SER   A 1 110 ? 336.199 7.942   85.688  1.00 53.09  ? 89   SER   A CB   1 
ATOM   688  O  OG   . SER   A 1 110 ? 337.097 8.779   86.397  1.00 53.01  ? 89   SER   A OG   1 
ATOM   689  N  N    . SER   A 1 111 ? 333.498 8.480   83.939  1.00 59.47  ? 90   SER   A N    1 
ATOM   690  C  CA   . SER   A 1 111 ? 332.839 8.019   82.720  1.00 58.08  ? 90   SER   A CA   1 
ATOM   691  C  C    . SER   A 1 111 ? 333.546 8.651   81.523  1.00 53.48  ? 90   SER   A C    1 
ATOM   692  O  O    . SER   A 1 111 ? 332.977 9.448   80.777  1.00 58.15  ? 90   SER   A O    1 
ATOM   693  C  CB   . SER   A 1 111 ? 331.345 8.349   82.725  1.00 57.26  ? 90   SER   A CB   1 
ATOM   694  O  OG   . SER   A 1 111 ? 330.665 7.655   83.762  1.00 61.64  ? 90   SER   A OG   1 
ATOM   695  N  N    . ASP   A 1 112 ? 334.821 8.307   81.367  1.00 46.22  ? 91   ASP   A N    1 
ATOM   696  C  CA   . ASP   A 1 112 ? 335.655 8.904   80.331  1.00 45.61  ? 91   ASP   A CA   1 
ATOM   697  C  C    . ASP   A 1 112 ? 335.277 8.302   78.985  1.00 43.23  ? 91   ASP   A C    1 
ATOM   698  O  O    . ASP   A 1 112 ? 335.517 7.116   78.736  1.00 47.83  ? 91   ASP   A O    1 
ATOM   699  C  CB   . ASP   A 1 112 ? 337.128 8.673   80.641  1.00 49.33  ? 91   ASP   A CB   1 
ATOM   700  C  CG   . ASP   A 1 112 ? 337.503 9.122   82.035  1.00 47.34  ? 91   ASP   A CG   1 
ATOM   701  O  OD1  . ASP   A 1 112 ? 337.051 10.209  82.453  1.00 52.72  ? 91   ASP   A OD1  1 
ATOM   702  O  OD2  . ASP   A 1 112 ? 338.241 8.382   82.717  1.00 57.33  ? 91   ASP   A OD2  1 
ATOM   703  N  N    . LYS   A 1 113 ? 334.697 9.113   78.106  1.00 42.82  ? 92   LYS   A N    1 
ATOM   704  C  CA   . LYS   A 1 113 ? 334.212 8.589   76.841  1.00 45.38  ? 92   LYS   A CA   1 
ATOM   705  C  C    . LYS   A 1 113 ? 334.373 9.623   75.738  1.00 43.38  ? 92   LYS   A C    1 
ATOM   706  O  O    . LYS   A 1 113 ? 334.461 10.830  75.985  1.00 42.79  ? 92   LYS   A O    1 
ATOM   707  C  CB   . LYS   A 1 113 ? 332.745 8.150   76.946  1.00 43.10  ? 92   LYS   A CB   1 
ATOM   708  C  CG   . LYS   A 1 113 ? 331.821 9.207   77.530  1.00 51.50  ? 92   LYS   A CG   1 
ATOM   709  C  CD   . LYS   A 1 113 ? 330.417 8.658   77.751  1.00 58.82  ? 92   LYS   A CD   1 
ATOM   710  C  CE   . LYS   A 1 113 ? 330.433 7.396   78.605  1.00 63.68  ? 92   LYS   A CE   1 
ATOM   711  N  NZ   . LYS   A 1 113 ? 329.064 6.979   79.025  1.00 70.88  ? 92   LYS   A NZ   1 
ATOM   712  N  N    . VAL   A 1 114 ? 334.430 9.115   74.511  1.00 48.94  ? 93   VAL   A N    1 
ATOM   713  C  CA   . VAL   A 1 114 ? 334.330 9.910   73.296  1.00 42.84  ? 93   VAL   A CA   1 
ATOM   714  C  C    . VAL   A 1 114 ? 333.281 9.249   72.418  1.00 45.22  ? 93   VAL   A C    1 
ATOM   715  O  O    . VAL   A 1 114 ? 333.308 8.028   72.228  1.00 46.32  ? 93   VAL   A O    1 
ATOM   716  C  CB   . VAL   A 1 114 ? 335.676 10.011  72.554  1.00 42.81  ? 93   VAL   A CB   1 
ATOM   717  C  CG1  . VAL   A 1 114 ? 335.555 10.950  71.362  1.00 37.36  ? 93   VAL   A CG1  1 
ATOM   718  C  CG2  . VAL   A 1 114 ? 336.765 10.471  73.499  1.00 38.26  ? 93   VAL   A CG2  1 
ATOM   719  N  N    . THR   A 1 115 ? 332.354 10.047  71.895  1.00 37.08  ? 94   THR   A N    1 
ATOM   720  C  CA   . THR   A 1 115 ? 331.253 9.540   71.089  1.00 40.15  ? 94   THR   A CA   1 
ATOM   721  C  C    . THR   A 1 115 ? 331.235 10.256  69.750  1.00 41.60  ? 94   THR   A C    1 
ATOM   722  O  O    . THR   A 1 115 ? 331.247 11.490  69.700  1.00 43.64  ? 94   THR   A O    1 
ATOM   723  C  CB   . THR   A 1 115 ? 329.911 9.727   71.799  1.00 44.03  ? 94   THR   A CB   1 
ATOM   724  O  OG1  . THR   A 1 115 ? 329.859 8.878   72.951  1.00 48.79  ? 94   THR   A OG1  1 
ATOM   725  C  CG2  . THR   A 1 115 ? 328.760 9.381   70.862  1.00 55.24  ? 94   THR   A CG2  1 
ATOM   726  N  N    . VAL   A 1 116 ? 331.193 9.480   68.674  1.00 41.23  ? 95   VAL   A N    1 
ATOM   727  C  CA   . VAL   A 1 116 ? 331.136 10.007  67.318  1.00 42.34  ? 95   VAL   A CA   1 
ATOM   728  C  C    . VAL   A 1 116 ? 329.768 9.687   66.737  1.00 45.25  ? 95   VAL   A C    1 
ATOM   729  O  O    . VAL   A 1 116 ? 329.336 8.528   66.747  1.00 42.82  ? 95   VAL   A O    1 
ATOM   730  C  CB   . VAL   A 1 116 ? 332.260 9.425   66.444  1.00 36.53  ? 95   VAL   A CB   1 
ATOM   731  C  CG1  . VAL   A 1 116 ? 332.085 9.858   65.000  1.00 37.72  ? 95   VAL   A CG1  1 
ATOM   732  C  CG2  . VAL   A 1 116 ? 333.615 9.859   66.980  1.00 35.36  ? 95   VAL   A CG2  1 
ATOM   733  N  N    . ASN   A 1 117 ? 329.081 10.715  66.252  1.00 40.82  ? 96   ASN   A N    1 
ATOM   734  C  CA   . ASN   A 1 117 ? 327.832 10.551  65.527  1.00 40.72  ? 96   ASN   A CA   1 
ATOM   735  C  C    . ASN   A 1 117 ? 328.090 10.724  64.039  1.00 37.70  ? 96   ASN   A C    1 
ATOM   736  O  O    . ASN   A 1 117 ? 328.914 11.549  63.633  1.00 38.78  ? 96   ASN   A O    1 
ATOM   737  C  CB   . ASN   A 1 117 ? 326.779 11.557  65.991  1.00 45.80  ? 96   ASN   A CB   1 
ATOM   738  C  CG   . ASN   A 1 117 ? 326.236 11.238  67.366  1.00 47.29  ? 96   ASN   A CG   1 
ATOM   739  O  OD1  . ASN   A 1 117 ? 325.998 12.135  68.175  1.00 61.15  ? 96   ASN   A OD1  1 
ATOM   740  N  ND2  . ASN   A 1 117 ? 326.039 9.954   67.640  1.00 52.47  ? 96   ASN   A ND2  1 
ATOM   741  N  N    . TYR   A 1 118 ? 327.384 9.940   63.230  1.00 38.96  ? 97   TYR   A N    1 
ATOM   742  C  CA   . TYR   A 1 118 ? 327.548 9.945   61.784  1.00 42.11  ? 97   TYR   A CA   1 
ATOM   743  C  C    . TYR   A 1 118 ? 326.256 10.404  61.127  1.00 42.86  ? 97   TYR   A C    1 
ATOM   744  O  O    . TYR   A 1 118 ? 325.170 9.938   61.488  1.00 46.27  ? 97   TYR   A O    1 
ATOM   745  C  CB   . TYR   A 1 118 ? 327.941 8.558   61.270  1.00 40.50  ? 97   TYR   A CB   1 
ATOM   746  C  CG   . TYR   A 1 118 ? 329.271 8.062   61.790  1.00 40.41  ? 97   TYR   A CG   1 
ATOM   747  C  CD1  . TYR   A 1 118 ? 330.466 8.570   61.297  1.00 39.44  ? 97   TYR   A CD1  1 
ATOM   748  C  CD2  . TYR   A 1 118 ? 329.332 7.074   62.766  1.00 41.60  ? 97   TYR   A CD2  1 
ATOM   749  C  CE1  . TYR   A 1 118 ? 331.685 8.114   61.765  1.00 37.36  ? 97   TYR   A CE1  1 
ATOM   750  C  CE2  . TYR   A 1 118 ? 330.545 6.612   63.239  1.00 39.90  ? 97   TYR   A CE2  1 
ATOM   751  C  CZ   . TYR   A 1 118 ? 331.719 7.135   62.734  1.00 37.72  ? 97   TYR   A CZ   1 
ATOM   752  O  OH   . TYR   A 1 118 ? 332.930 6.679   63.201  1.00 40.03  ? 97   TYR   A OH   1 
ATOM   753  N  N    . TYR   A 1 119 ? 326.379 11.310  60.160  1.00 49.11  ? 98   TYR   A N    1 
ATOM   754  C  CA   . TYR   A 1 119 ? 325.244 11.861  59.436  1.00 49.01  ? 98   TYR   A CA   1 
ATOM   755  C  C    . TYR   A 1 119 ? 325.406 11.592  57.948  1.00 53.61  ? 98   TYR   A C    1 
ATOM   756  O  O    . TYR   A 1 119 ? 326.519 11.656  57.415  1.00 47.04  ? 98   TYR   A O    1 
ATOM   757  C  CB   . TYR   A 1 119 ? 325.115 13.373  59.670  1.00 41.85  ? 98   TYR   A CB   1 
ATOM   758  C  CG   . TYR   A 1 119 ? 325.147 13.783  61.124  1.00 41.97  ? 98   TYR   A CG   1 
ATOM   759  C  CD1  . TYR   A 1 119 ? 326.353 13.954  61.788  1.00 39.11  ? 98   TYR   A CD1  1 
ATOM   760  C  CD2  . TYR   A 1 119 ? 323.973 14.005  61.832  1.00 44.36  ? 98   TYR   A CD2  1 
ATOM   761  C  CE1  . TYR   A 1 119 ? 326.392 14.328  63.114  1.00 41.96  ? 98   TYR   A CE1  1 
ATOM   762  C  CE2  . TYR   A 1 119 ? 324.002 14.380  63.163  1.00 44.51  ? 98   TYR   A CE2  1 
ATOM   763  C  CZ   . TYR   A 1 119 ? 325.216 14.540  63.799  1.00 47.12  ? 98   TYR   A CZ   1 
ATOM   764  O  OH   . TYR   A 1 119 ? 325.263 14.912  65.120  1.00 52.38  ? 98   TYR   A OH   1 
ATOM   765  N  N    . ASP   A 1 120 ? 324.297 11.286  57.280  1.00 55.04  ? 99   ASP   A N    1 
ATOM   766  C  CA   . ASP   A 1 120 ? 324.284 11.264  55.828  1.00 59.98  ? 99   ASP   A CA   1 
ATOM   767  C  C    . ASP   A 1 120 ? 324.015 12.678  55.313  1.00 61.61  ? 99   ASP   A C    1 
ATOM   768  O  O    . ASP   A 1 120 ? 323.783 13.613  56.082  1.00 64.65  ? 99   ASP   A O    1 
ATOM   769  C  CB   . ASP   A 1 120 ? 323.257 10.259  55.304  1.00 59.13  ? 99   ASP   A CB   1 
ATOM   770  C  CG   . ASP   A 1 120 ? 321.856 10.525  55.818  1.00 71.44  ? 99   ASP   A CG   1 
ATOM   771  O  OD1  . ASP   A 1 120 ? 321.363 11.659  55.651  1.00 78.06  ? 99   ASP   A OD1  1 
ATOM   772  O  OD2  . ASP   A 1 120 ? 321.242 9.592   56.379  1.00 76.42  ? 99   ASP   A OD2  1 
ATOM   773  N  N    . GLU   A 1 121 ? 324.057 12.845  53.990  1.00 68.17  ? 100  GLU   A N    1 
ATOM   774  C  CA   . GLU   A 1 121 ? 323.831 14.165  53.410  1.00 72.92  ? 100  GLU   A CA   1 
ATOM   775  C  C    . GLU   A 1 121 ? 322.434 14.695  53.709  1.00 73.81  ? 100  GLU   A C    1 
ATOM   776  O  O    . GLU   A 1 121 ? 322.230 15.914  53.703  1.00 77.30  ? 100  GLU   A O    1 
ATOM   777  C  CB   . GLU   A 1 121 ? 324.058 14.120  51.897  1.00 66.70  ? 100  GLU   A CB   1 
ATOM   778  N  N    . GLU   A 1 122 ? 321.481 13.808  53.993  1.00 88.91  ? 101  GLU   A N    1 
ATOM   779  C  CA   . GLU   A 1 122 ? 320.076 14.171  54.134  1.00 89.65  ? 101  GLU   A CA   1 
ATOM   780  C  C    . GLU   A 1 122 ? 319.821 15.062  55.346  1.00 93.53  ? 101  GLU   A C    1 
ATOM   781  O  O    . GLU   A 1 122 ? 319.852 16.291  55.233  1.00 101.94 ? 101  GLU   A O    1 
ATOM   782  C  CB   . GLU   A 1 122 ? 319.225 12.900  54.215  1.00 86.17  ? 101  GLU   A CB   1 
ATOM   783  C  CG   . GLU   A 1 122 ? 317.769 13.084  53.824  1.00 105.84 ? 101  GLU   A CG   1 
ATOM   784  C  CD   . GLU   A 1 122 ? 317.198 11.857  53.140  1.00 118.73 ? 101  GLU   A CD   1 
ATOM   785  O  OE1  . GLU   A 1 122 ? 317.981 11.097  52.532  1.00 123.31 ? 101  GLU   A OE1  1 
ATOM   786  O  OE2  . GLU   A 1 122 ? 315.968 11.652  53.210  1.00 119.55 ? 101  GLU   A OE2  1 
ATOM   787  N  N    . GLY   A 1 123 ? 319.567 14.459  56.509  1.00 80.82  ? 102  GLY   A N    1 
ATOM   788  C  CA   . GLY   A 1 123 ? 319.121 15.189  57.675  1.00 67.32  ? 102  GLY   A CA   1 
ATOM   789  C  C    . GLY   A 1 123 ? 320.209 15.404  58.720  1.00 60.02  ? 102  GLY   A C    1 
ATOM   790  O  O    . GLY   A 1 123 ? 321.359 15.000  58.572  1.00 55.12  ? 102  GLY   A O    1 
ATOM   791  N  N    . SER   A 1 124 ? 319.803 16.062  59.807  1.00 55.69  ? 103  SER   A N    1 
ATOM   792  C  CA   . SER   A 1 124 ? 320.688 16.400  60.914  1.00 48.02  ? 103  SER   A CA   1 
ATOM   793  C  C    . SER   A 1 124 ? 320.553 15.451  62.096  1.00 45.91  ? 103  SER   A C    1 
ATOM   794  O  O    . SER   A 1 124 ? 321.120 15.717  63.159  1.00 49.01  ? 103  SER   A O    1 
ATOM   795  C  CB   . SER   A 1 124 ? 320.429 17.835  61.376  1.00 48.90  ? 103  SER   A CB   1 
ATOM   796  O  OG   . SER   A 1 124 ? 320.641 18.752  60.319  1.00 58.03  ? 103  SER   A OG   1 
ATOM   797  N  N    . ILE   A 1 125 ? 319.809 14.366  61.947  1.00 51.44  ? 104  ILE   A N    1 
ATOM   798  C  CA   . ILE   A 1 125 ? 319.685 13.340  62.978  1.00 48.64  ? 104  ILE   A CA   1 
ATOM   799  C  C    . ILE   A 1 125 ? 320.693 12.239  62.669  1.00 46.55  ? 104  ILE   A C    1 
ATOM   800  O  O    . ILE   A 1 125 ? 320.681 11.708  61.550  1.00 49.71  ? 104  ILE   A O    1 
ATOM   801  C  CB   . ILE   A 1 125 ? 318.255 12.770  63.049  1.00 54.69  ? 104  ILE   A CB   1 
ATOM   802  C  CG1  . ILE   A 1 125 ? 317.247 13.885  63.366  1.00 49.70  ? 104  ILE   A CG1  1 
ATOM   803  C  CG2  . ILE   A 1 125 ? 318.171 11.644  64.072  1.00 46.25  ? 104  ILE   A CG2  1 
ATOM   804  C  CD1  . ILE   A 1 125 ? 317.574 14.686  64.615  1.00 48.74  ? 104  ILE   A CD1  1 
ATOM   805  N  N    . PRO   A 1 126 ? 321.575 11.885  63.603  1.00 44.57  ? 105  PRO   A N    1 
ATOM   806  C  CA   . PRO   A 1 126 ? 322.621 10.903  63.291  1.00 42.82  ? 105  PRO   A CA   1 
ATOM   807  C  C    . PRO   A 1 126 ? 322.033 9.584   62.813  1.00 47.59  ? 105  PRO   A C    1 
ATOM   808  O  O    . PRO   A 1 126 ? 320.944 9.176   63.222  1.00 54.39  ? 105  PRO   A O    1 
ATOM   809  C  CB   . PRO   A 1 126 ? 323.368 10.738  64.621  1.00 44.34  ? 105  PRO   A CB   1 
ATOM   810  C  CG   . PRO   A 1 126 ? 322.450 11.295  65.666  1.00 50.48  ? 105  PRO   A CG   1 
ATOM   811  C  CD   . PRO   A 1 126 ? 321.656 12.364  64.992  1.00 48.42  ? 105  PRO   A CD   1 
ATOM   812  N  N    . ILE   A 1 127 ? 322.769 8.922   61.920  1.00 41.23  ? 106  ILE   A N    1 
ATOM   813  C  CA   . ILE   A 1 127 ? 322.346 7.631   61.388  1.00 50.32  ? 106  ILE   A CA   1 
ATOM   814  C  C    . ILE   A 1 127 ? 323.046 6.464   62.075  1.00 53.16  ? 106  ILE   A C    1 
ATOM   815  O  O    . ILE   A 1 127 ? 322.552 5.328   61.997  1.00 53.17  ? 106  ILE   A O    1 
ATOM   816  C  CB   . ILE   A 1 127 ? 322.574 7.553   59.864  1.00 56.76  ? 106  ILE   A CB   1 
ATOM   817  C  CG1  . ILE   A 1 127 ? 324.071 7.529   59.545  1.00 49.75  ? 106  ILE   A CG1  1 
ATOM   818  C  CG2  . ILE   A 1 127 ? 321.893 8.720   59.167  1.00 57.90  ? 106  ILE   A CG2  1 
ATOM   819  C  CD1  . ILE   A 1 127 ? 324.370 7.415   58.065  1.00 55.80  ? 106  ILE   A CD1  1 
ATOM   820  N  N    . ASP   A 1 128 ? 324.176 6.701   62.726  1.00 48.16  ? 107  ASP   A N    1 
ATOM   821  C  CA   . ASP   A 1 128 ? 324.839 5.673   63.511  1.00 50.27  ? 107  ASP   A CA   1 
ATOM   822  C  C    . ASP   A 1 128 ? 325.745 6.375   64.510  1.00 45.80  ? 107  ASP   A C    1 
ATOM   823  O  O    . ASP   A 1 128 ? 325.861 7.603   64.517  1.00 42.87  ? 107  ASP   A O    1 
ATOM   824  C  CB   . ASP   A 1 128 ? 325.610 4.696   62.619  1.00 51.44  ? 107  ASP   A CB   1 
ATOM   825  C  CG   . ASP   A 1 128 ? 325.951 3.405   63.333  1.00 57.99  ? 107  ASP   A CG   1 
ATOM   826  O  OD1  . ASP   A 1 128 ? 325.561 3.252   64.510  1.00 53.04  ? 107  ASP   A OD1  1 
ATOM   827  O  OD2  . ASP   A 1 128 ? 326.610 2.543   62.717  1.00 66.10  ? 107  ASP   A OD2  1 
ATOM   828  N  N    . GLN   A 1 129 ? 326.389 5.585   65.359  1.00 47.74  ? 108  GLN   A N    1 
ATOM   829  C  CA   . GLN   A 1 129 ? 327.161 6.151   66.452  1.00 43.76  ? 108  GLN   A CA   1 
ATOM   830  C  C    . GLN   A 1 129 ? 328.258 5.173   66.833  1.00 44.84  ? 108  GLN   A C    1 
ATOM   831  O  O    . GLN   A 1 129 ? 327.985 3.991   67.061  1.00 53.93  ? 108  GLN   A O    1 
ATOM   832  C  CB   . GLN   A 1 129 ? 326.251 6.449   67.648  1.00 46.91  ? 108  GLN   A CB   1 
ATOM   833  C  CG   . GLN   A 1 129 ? 326.917 7.186   68.793  1.00 55.13  ? 108  GLN   A CG   1 
ATOM   834  C  CD   . GLN   A 1 129 ? 325.921 7.615   69.855  1.00 65.77  ? 108  GLN   A CD   1 
ATOM   835  O  OE1  . GLN   A 1 129 ? 324.931 8.287   69.560  1.00 65.97  ? 108  GLN   A OE1  1 
ATOM   836  N  NE2  . GLN   A 1 129 ? 326.175 7.222   71.098  1.00 61.92  ? 108  GLN   A NE2  1 
ATOM   837  N  N    . ALA   A 1 130 ? 329.493 5.662   66.879  1.00 46.20  ? 109  ALA   A N    1 
ATOM   838  C  CA   . ALA   A 1 130 ? 330.636 4.884   67.332  1.00 44.84  ? 109  ALA   A CA   1 
ATOM   839  C  C    . ALA   A 1 130 ? 331.194 5.521   68.594  1.00 43.23  ? 109  ALA   A C    1 
ATOM   840  O  O    . ALA   A 1 130 ? 331.307 6.748   68.682  1.00 42.85  ? 109  ALA   A O    1 
ATOM   841  C  CB   . ALA   A 1 130 ? 331.721 4.802   66.256  1.00 42.62  ? 109  ALA   A CB   1 
ATOM   842  N  N    . GLY   A 1 131 ? 331.543 4.690   69.566  1.00 45.53  ? 110  GLY   A N    1 
ATOM   843  C  CA   . GLY   A 1 131 ? 331.961 5.181   70.862  1.00 45.73  ? 110  GLY   A CA   1 
ATOM   844  C  C    . GLY   A 1 131 ? 333.283 4.593   71.306  1.00 45.04  ? 110  GLY   A C    1 
ATOM   845  O  O    . GLY   A 1 131 ? 333.604 3.437   71.030  1.00 47.61  ? 110  GLY   A O    1 
ATOM   846  N  N    . LEU   A 1 132 ? 334.051 5.421   72.007  1.00 38.75  ? 111  LEU   A N    1 
ATOM   847  C  CA   . LEU   A 1 132 ? 335.279 5.008   72.669  1.00 40.89  ? 111  LEU   A CA   1 
ATOM   848  C  C    . LEU   A 1 132 ? 335.110 5.277   74.156  1.00 41.83  ? 111  LEU   A C    1 
ATOM   849  O  O    . LEU   A 1 132 ? 334.865 6.419   74.558  1.00 43.41  ? 111  LEU   A O    1 
ATOM   850  C  CB   . LEU   A 1 132 ? 336.488 5.758   72.108  1.00 40.36  ? 111  LEU   A CB   1 
ATOM   851  C  CG   . LEU   A 1 132 ? 337.859 5.427   72.696  1.00 43.75  ? 111  LEU   A CG   1 
ATOM   852  C  CD1  . LEU   A 1 132 ? 338.183 3.953   72.512  1.00 45.32  ? 111  LEU   A CD1  1 
ATOM   853  C  CD2  . LEU   A 1 132 ? 338.915 6.301   72.043  1.00 38.65  ? 111  LEU   A CD2  1 
ATOM   854  N  N    . PHE   A 1 133 ? 335.212 4.230   74.965  1.00 40.41  ? 112  PHE   A N    1 
ATOM   855  C  CA   . PHE   A 1 133 ? 335.096 4.345   76.411  1.00 41.74  ? 112  PHE   A CA   1 
ATOM   856  C  C    . PHE   A 1 133 ? 336.457 4.061   77.025  1.00 39.71  ? 112  PHE   A C    1 
ATOM   857  O  O    . PHE   A 1 133 ? 337.080 3.038   76.720  1.00 40.75  ? 112  PHE   A O    1 
ATOM   858  C  CB   . PHE   A 1 133 ? 334.028 3.392   76.952  1.00 45.53  ? 112  PHE   A CB   1 
ATOM   859  C  CG   . PHE   A 1 133 ? 332.658 3.643   76.386  1.00 56.14  ? 112  PHE   A CG   1 
ATOM   860  C  CD1  . PHE   A 1 133 ? 331.858 4.655   76.894  1.00 60.59  ? 112  PHE   A CD1  1 
ATOM   861  C  CD2  . PHE   A 1 133 ? 332.176 2.877   75.337  1.00 64.26  ? 112  PHE   A CD2  1 
ATOM   862  C  CE1  . PHE   A 1 133 ? 330.597 4.894   76.369  1.00 65.52  ? 112  PHE   A CE1  1 
ATOM   863  C  CE2  . PHE   A 1 133 ? 330.916 3.111   74.808  1.00 65.74  ? 112  PHE   A CE2  1 
ATOM   864  C  CZ   . PHE   A 1 133 ? 330.126 4.120   75.325  1.00 67.27  ? 112  PHE   A CZ   1 
ATOM   865  N  N    . LEU   A 1 134 ? 336.920 4.971   77.873  1.00 38.80  ? 113  LEU   A N    1 
ATOM   866  C  CA   . LEU   A 1 134 ? 338.308 4.995   78.302  1.00 39.54  ? 113  LEU   A CA   1 
ATOM   867  C  C    . LEU   A 1 134 ? 338.410 4.828   79.810  1.00 37.11  ? 113  LEU   A C    1 
ATOM   868  O  O    . LEU   A 1 134 ? 337.611 5.387   80.566  1.00 39.63  ? 113  LEU   A O    1 
ATOM   869  C  CB   . LEU   A 1 134 ? 338.979 6.303   77.873  1.00 41.41  ? 113  LEU   A CB   1 
ATOM   870  C  CG   . LEU   A 1 134 ? 339.105 6.505   76.361  1.00 42.67  ? 113  LEU   A CG   1 
ATOM   871  C  CD1  . LEU   A 1 134 ? 339.702 7.865   76.044  1.00 39.23  ? 113  LEU   A CD1  1 
ATOM   872  C  CD2  . LEU   A 1 134 ? 339.945 5.392   75.755  1.00 33.51  ? 113  LEU   A CD2  1 
ATOM   873  N  N    . THR   A 1 135 ? 339.393 4.042   80.235  1.00 36.14  ? 114  THR   A N    1 
ATOM   874  C  CA   . THR   A 1 135 ? 339.794 3.957   81.634  1.00 39.59  ? 114  THR   A CA   1 
ATOM   875  C  C    . THR   A 1 135 ? 341.263 4.348   81.686  1.00 36.19  ? 114  THR   A C    1 
ATOM   876  O  O    . THR   A 1 135 ? 342.124 3.619   81.182  1.00 33.11  ? 114  THR   A O    1 
ATOM   877  C  CB   . THR   A 1 135 ? 339.568 2.557   82.208  1.00 37.13  ? 114  THR   A CB   1 
ATOM   878  O  OG1  . THR   A 1 135 ? 338.200 2.174   82.016  1.00 42.15  ? 114  THR   A OG1  1 
ATOM   879  C  CG2  . THR   A 1 135 ? 339.881 2.539   83.697  1.00 39.81  ? 114  THR   A CG2  1 
ATOM   880  N  N    . ALA   A 1 136 ? 341.546 5.512   82.259  1.00 35.92  ? 115  ALA   A N    1 
ATOM   881  C  CA   . ALA   A 1 136 ? 342.907 6.020   82.324  1.00 32.54  ? 115  ALA   A CA   1 
ATOM   882  C  C    . ALA   A 1 136 ? 343.573 5.526   83.596  1.00 38.88  ? 115  ALA   A C    1 
ATOM   883  O  O    . ALA   A 1 136 ? 343.016 5.659   84.691  1.00 40.06  ? 115  ALA   A O    1 
ATOM   884  C  CB   . ALA   A 1 136 ? 342.930 7.548   82.271  1.00 37.73  ? 115  ALA   A CB   1 
ATOM   885  N  N    A ILE   A 1 137 ? 344.747 4.924   83.447  0.50 35.35  ? 116  ILE   A N    1 
ATOM   886  N  N    B ILE   A 1 137 ? 344.778 4.982   83.449  0.50 35.97  ? 116  ILE   A N    1 
ATOM   887  C  CA   A ILE   A 1 137 ? 345.541 4.499   84.585  0.50 35.32  ? 116  ILE   A CA   1 
ATOM   888  C  CA   B ILE   A 1 137 ? 345.545 4.428   84.558  0.50 35.65  ? 116  ILE   A CA   1 
ATOM   889  C  C    A ILE   A 1 137 ? 346.947 5.041   84.405  0.50 37.08  ? 116  ILE   A C    1 
ATOM   890  C  C    B ILE   A 1 137 ? 346.998 4.857   84.404  0.50 37.08  ? 116  ILE   A C    1 
ATOM   891  O  O    A ILE   A 1 137 ? 347.391 5.340   83.294  0.50 36.88  ? 116  ILE   A O    1 
ATOM   892  O  O    B ILE   A 1 137 ? 347.526 4.904   83.288  0.50 37.27  ? 116  ILE   A O    1 
ATOM   893  C  CB   A ILE   A 1 137 ? 345.573 2.966   84.754  0.50 37.19  ? 116  ILE   A CB   1 
ATOM   894  C  CB   B ILE   A 1 137 ? 345.424 2.890   84.607  0.50 37.12  ? 116  ILE   A CB   1 
ATOM   895  C  CG1  A ILE   A 1 137 ? 346.221 2.310   83.537  0.50 34.46  ? 116  ILE   A CG1  1 
ATOM   896  C  CG1  B ILE   A 1 137 ? 343.966 2.483   84.829  0.50 40.40  ? 116  ILE   A CG1  1 
ATOM   897  C  CG2  A ILE   A 1 137 ? 344.171 2.425   84.981  0.50 40.32  ? 116  ILE   A CG2  1 
ATOM   898  C  CG2  B ILE   A 1 137 ? 346.308 2.315   85.695  0.50 40.56  ? 116  ILE   A CG2  1 
ATOM   899  C  CD1  A ILE   A 1 137 ? 346.302 0.810   83.638  0.50 36.13  ? 116  ILE   A CD1  1 
ATOM   900  C  CD1  B ILE   A 1 137 ? 343.709 1.008   84.641  0.50 40.11  ? 116  ILE   A CD1  1 
ATOM   901  N  N    . GLU   A 1 138 ? 347.641 5.179   85.525  1.00 36.31  ? 117  GLU   A N    1 
ATOM   902  C  CA   . GLU   A 1 138 ? 349.040 5.568   85.540  1.00 35.72  ? 117  GLU   A CA   1 
ATOM   903  C  C    . GLU   A 1 138 ? 349.869 4.340   85.886  1.00 36.79  ? 117  GLU   A C    1 
ATOM   904  O  O    . GLU   A 1 138 ? 349.579 3.648   86.866  1.00 37.72  ? 117  GLU   A O    1 
ATOM   905  C  CB   . GLU   A 1 138 ? 349.279 6.695   86.547  1.00 38.90  ? 117  GLU   A CB   1 
ATOM   906  C  CG   . GLU   A 1 138 ? 350.696 7.230   86.567  1.00 46.42  ? 117  GLU   A CG   1 
ATOM   907  C  CD   . GLU   A 1 138 ? 350.868 8.371   87.547  1.00 54.76  ? 117  GLU   A CD   1 
ATOM   908  O  OE1  . GLU   A 1 138 ? 349.847 8.959   87.964  1.00 60.89  ? 117  GLU   A OE1  1 
ATOM   909  O  OE2  . GLU   A 1 138 ? 352.026 8.678   87.902  1.00 63.31  ? 117  GLU   A OE2  1 
ATOM   910  N  N    . ILE   A 1 139 ? 350.871 4.051   85.059  1.00 31.25  ? 118  ILE   A N    1 
ATOM   911  C  CA   . ILE   A 1 139 ? 351.790 2.939   85.274  1.00 29.38  ? 118  ILE   A CA   1 
ATOM   912  C  C    . ILE   A 1 139 ? 353.205 3.456   85.070  1.00 37.50  ? 118  ILE   A C    1 
ATOM   913  O  O    . ILE   A 1 139 ? 353.492 4.114   84.063  1.00 42.00  ? 118  ILE   A O    1 
ATOM   914  C  CB   . ILE   A 1 139 ? 351.511 1.759   84.324  1.00 33.15  ? 118  ILE   A CB   1 
ATOM   915  C  CG1  . ILE   A 1 139 ? 350.056 1.309   84.418  1.00 37.67  ? 118  ILE   A CG1  1 
ATOM   916  C  CG2  . ILE   A 1 139 ? 352.427 0.588   84.640  1.00 37.37  ? 118  ILE   A CG2  1 
ATOM   917  C  CD1  . ILE   A 1 139 ? 349.732 0.190   83.459  1.00 34.59  ? 118  ILE   A CD1  1 
ATOM   918  N  N    . SER   A 1 140 ? 354.087 3.160   86.020  1.00 35.91  ? 119  SER   A N    1 
ATOM   919  C  CA   . SER   A 1 140 ? 355.446 3.690   85.975  1.00 32.38  ? 119  SER   A CA   1 
ATOM   920  C  C    . SER   A 1 140 ? 356.329 2.826   86.858  1.00 32.49  ? 119  SER   A C    1 
ATOM   921  O  O    . SER   A 1 140 ? 356.114 2.759   88.073  1.00 32.64  ? 119  SER   A O    1 
ATOM   922  C  CB   . SER   A 1 140 ? 355.473 5.148   86.433  1.00 29.97  ? 119  SER   A CB   1 
ATOM   923  O  OG   . SER   A 1 140 ? 356.746 5.728   86.221  1.00 36.56  ? 119  SER   A OG   1 
ATOM   924  N  N    . LEU   A 1 141 ? 357.303 2.157   86.249  1.00 36.48  ? 120  LEU   A N    1 
ATOM   925  C  CA   . LEU   A 1 141 ? 358.298 1.381   86.979  1.00 35.89  ? 120  LEU   A CA   1 
ATOM   926  C  C    . LEU   A 1 141 ? 359.477 2.303   87.265  1.00 33.02  ? 120  LEU   A C    1 
ATOM   927  O  O    . LEU   A 1 141 ? 360.186 2.717   86.343  1.00 32.82  ? 120  LEU   A O    1 
ATOM   928  C  CB   . LEU   A 1 141 ? 358.720 0.160   86.168  1.00 30.86  ? 120  LEU   A CB   1 
ATOM   929  C  CG   . LEU   A 1 141 ? 359.569 -0.893  86.879  1.00 32.57  ? 120  LEU   A CG   1 
ATOM   930  C  CD1  . LEU   A 1 141 ? 358.818 -1.488  88.061  1.00 29.38  ? 120  LEU   A CD1  1 
ATOM   931  C  CD2  . LEU   A 1 141 ? 359.977 -1.975  85.894  1.00 30.46  ? 120  LEU   A CD2  1 
ATOM   932  N  N    . ASP   A 1 142 ? 359.683 2.631   88.537  1.00 33.79  ? 121  ASP   A N    1 
ATOM   933  C  CA   . ASP   A 1 142 ? 360.605 3.684   88.935  1.00 34.37  ? 121  ASP   A CA   1 
ATOM   934  C  C    . ASP   A 1 142 ? 361.833 3.109   89.632  1.00 32.57  ? 121  ASP   A C    1 
ATOM   935  O  O    . ASP   A 1 142 ? 361.725 2.182   90.441  1.00 36.71  ? 121  ASP   A O    1 
ATOM   936  C  CB   . ASP   A 1 142 ? 359.902 4.693   89.849  1.00 36.18  ? 121  ASP   A CB   1 
ATOM   937  C  CG   . ASP   A 1 142 ? 358.869 5.523   89.110  1.00 36.93  ? 121  ASP   A CG   1 
ATOM   938  O  OD1  . ASP   A 1 142 ? 358.880 5.512   87.860  1.00 35.25  ? 121  ASP   A OD1  1 
ATOM   939  O  OD2  . ASP   A 1 142 ? 358.046 6.186   89.777  1.00 34.91  ? 121  ASP   A OD2  1 
ATOM   940  N  N    . VAL   A 1 143 ? 363.003 3.667   89.308  1.00 29.73  ? 122  VAL   A N    1 
ATOM   941  C  CA   . VAL   A 1 143 ? 364.264 3.321   89.955  1.00 30.35  ? 122  VAL   A CA   1 
ATOM   942  C  C    . VAL   A 1 143 ? 365.023 4.609   90.252  1.00 27.75  ? 122  VAL   A C    1 
ATOM   943  O  O    . VAL   A 1 143 ? 364.641 5.697   89.817  1.00 31.85  ? 122  VAL   A O    1 
ATOM   944  C  CB   . VAL   A 1 143 ? 365.126 2.364   89.103  1.00 29.79  ? 122  VAL   A CB   1 
ATOM   945  C  CG1  . VAL   A 1 143 ? 364.438 1.018   88.978  1.00 24.12  ? 122  VAL   A CG1  1 
ATOM   946  C  CG2  . VAL   A 1 143 ? 365.403 2.957   87.727  1.00 27.91  ? 122  VAL   A CG2  1 
ATOM   947  N  N    . ASP   A 1 144 ? 366.110 4.475   91.014  1.00 32.84  ? 123  ASP   A N    1 
ATOM   948  C  CA   . ASP   A 1 144 ? 366.913 5.624   91.437  1.00 35.00  ? 123  ASP   A CA   1 
ATOM   949  C  C    . ASP   A 1 144 ? 367.990 5.903   90.388  1.00 35.15  ? 123  ASP   A C    1 
ATOM   950  O  O    . ASP   A 1 144 ? 369.195 5.774   90.617  1.00 35.56  ? 123  ASP   A O    1 
ATOM   951  C  CB   . ASP   A 1 144 ? 367.507 5.375   92.819  1.00 37.88  ? 123  ASP   A CB   1 
ATOM   952  C  CG   . ASP   A 1 144 ? 368.489 6.455   93.238  1.00 41.61  ? 123  ASP   A CG   1 
ATOM   953  O  OD1  . ASP   A 1 144 ? 368.218 7.641   92.966  1.00 40.61  ? 123  ASP   A OD1  1 
ATOM   954  O  OD2  . ASP   A 1 144 ? 369.528 6.119   93.845  1.00 37.70  ? 123  ASP   A OD2  1 
ATOM   955  N  N    . ALA   A 1 145 ? 367.517 6.301   89.205  1.00 33.05  ? 124  ALA   A N    1 
ATOM   956  C  CA   . ALA   A 1 145 ? 368.408 6.531   88.076  1.00 34.73  ? 124  ALA   A CA   1 
ATOM   957  C  C    . ALA   A 1 145 ? 369.277 7.769   88.259  1.00 33.47  ? 124  ALA   A C    1 
ATOM   958  O  O    . ALA   A 1 145 ? 370.318 7.880   87.602  1.00 36.79  ? 124  ALA   A O    1 
ATOM   959  C  CB   . ALA   A 1 145 ? 367.596 6.644   86.785  1.00 30.86  ? 124  ALA   A CB   1 
ATOM   960  N  N    . ASP   A 1 146 ? 368.883 8.696   89.129  1.00 33.12  ? 125  ASP   A N    1 
ATOM   961  C  CA   . ASP   A 1 146 ? 369.691 9.877   89.398  1.00 38.15  ? 125  ASP   A CA   1 
ATOM   962  C  C    . ASP   A 1 146 ? 370.678 9.668   90.539  1.00 37.50  ? 125  ASP   A C    1 
ATOM   963  O  O    . ASP   A 1 146 ? 371.396 10.605  90.901  1.00 42.66  ? 125  ASP   A O    1 
ATOM   964  C  CB   . ASP   A 1 146 ? 368.792 11.084  89.686  1.00 36.21  ? 125  ASP   A CB   1 
ATOM   965  C  CG   . ASP   A 1 146 ? 367.937 10.894  90.916  1.00 38.63  ? 125  ASP   A CG   1 
ATOM   966  O  OD1  . ASP   A 1 146 ? 368.275 10.029  91.748  1.00 38.16  ? 125  ASP   A OD1  1 
ATOM   967  O  OD2  . ASP   A 1 146 ? 366.922 11.609  91.048  1.00 41.30  ? 125  ASP   A OD2  1 
ATOM   968  N  N    . ARG   A 1 147 ? 370.708 8.474   91.132  1.00 40.01  ? 126  ARG   A N    1 
ATOM   969  C  CA   . ARG   A 1 147 ? 371.836 8.033   91.950  1.00 40.79  ? 126  ARG   A CA   1 
ATOM   970  C  C    . ARG   A 1 147 ? 371.965 8.831   93.246  1.00 41.18  ? 126  ARG   A C    1 
ATOM   971  O  O    . ARG   A 1 147 ? 373.069 9.180   93.666  1.00 48.62  ? 126  ARG   A O    1 
ATOM   972  C  CB   . ARG   A 1 147 ? 373.134 8.097   91.143  1.00 34.55  ? 126  ARG   A CB   1 
ATOM   973  C  CG   . ARG   A 1 147 ? 373.078 7.263   89.877  1.00 35.12  ? 126  ARG   A CG   1 
ATOM   974  C  CD   . ARG   A 1 147 ? 374.174 7.609   88.892  1.00 31.58  ? 126  ARG   A CD   1 
ATOM   975  N  NE   . ARG   A 1 147 ? 374.028 6.830   87.668  1.00 27.85  ? 126  ARG   A NE   1 
ATOM   976  C  CZ   . ARG   A 1 147 ? 374.783 6.977   86.587  1.00 31.19  ? 126  ARG   A CZ   1 
ATOM   977  N  NH1  . ARG   A 1 147 ? 375.761 7.866   86.543  1.00 32.55  ? 126  ARG   A NH1  1 
ATOM   978  N  NH2  . ARG   A 1 147 ? 374.547 6.214   85.523  1.00 31.39  ? 126  ARG   A NH2  1 
ATOM   979  N  N    . ASP   A 1 148 ? 370.838 9.115   93.896  1.00 40.58  ? 127  ASP   A N    1 
ATOM   980  C  CA   . ASP   A 1 148 ? 370.866 9.754   95.205  1.00 43.21  ? 127  ASP   A CA   1 
ATOM   981  C  C    . ASP   A 1 148 ? 370.309 8.853   96.299  1.00 48.40  ? 127  ASP   A C    1 
ATOM   982  O  O    . ASP   A 1 148 ? 370.148 9.306   97.440  1.00 50.21  ? 127  ASP   A O    1 
ATOM   983  C  CB   . ASP   A 1 148 ? 370.106 11.085  95.176  1.00 45.74  ? 127  ASP   A CB   1 
ATOM   984  C  CG   . ASP   A 1 148 ? 368.633 10.913  94.861  1.00 44.43  ? 127  ASP   A CG   1 
ATOM   985  O  OD1  . ASP   A 1 148 ? 368.223 9.786   94.516  1.00 49.56  ? 127  ASP   A OD1  1 
ATOM   986  O  OD2  . ASP   A 1 148 ? 367.884 11.907  94.964  1.00 47.19  ? 127  ASP   A OD2  1 
ATOM   987  N  N    . GLY   A 1 149 ? 370.019 7.591   95.987  1.00 47.19  ? 128  GLY   A N    1 
ATOM   988  C  CA   . GLY   A 1 149 ? 369.496 6.668   96.972  1.00 42.56  ? 128  GLY   A CA   1 
ATOM   989  C  C    . GLY   A 1 149 ? 368.023 6.809   97.275  1.00 46.35  ? 128  GLY   A C    1 
ATOM   990  O  O    . GLY   A 1 149 ? 367.546 6.192   98.235  1.00 49.04  ? 128  GLY   A O    1 
ATOM   991  N  N    . VAL   A 1 150 ? 367.288 7.604   96.500  1.00 44.78  ? 129  VAL   A N    1 
ATOM   992  C  CA   . VAL   A 1 150 ? 365.844 7.740   96.640  1.00 43.78  ? 129  VAL   A CA   1 
ATOM   993  C  C    . VAL   A 1 150 ? 365.209 7.555   95.271  1.00 46.22  ? 129  VAL   A C    1 
ATOM   994  O  O    . VAL   A 1 150 ? 365.708 8.079   94.270  1.00 44.33  ? 129  VAL   A O    1 
ATOM   995  C  CB   . VAL   A 1 150 ? 365.449 9.105   97.240  1.00 50.51  ? 129  VAL   A CB   1 
ATOM   996  C  CG1  . VAL   A 1 150 ? 363.939 9.253   97.240  1.00 50.11  ? 129  VAL   A CG1  1 
ATOM   997  C  CG2  . VAL   A 1 150 ? 366.004 9.245   98.647  1.00 56.58  ? 129  VAL   A CG2  1 
ATOM   998  N  N    . VAL   A 1 151 ? 364.104 6.815   95.223  1.00 45.37  ? 130  VAL   A N    1 
ATOM   999  C  CA   . VAL   A 1 151 ? 363.499 6.420   93.956  1.00 41.85  ? 130  VAL   A CA   1 
ATOM   1000 C  C    . VAL   A 1 151 ? 362.581 7.551   93.501  1.00 36.19  ? 130  VAL   A C    1 
ATOM   1001 O  O    . VAL   A 1 151 ? 361.435 7.657   93.938  1.00 39.41  ? 130  VAL   A O    1 
ATOM   1002 C  CB   . VAL   A 1 151 ? 362.754 5.090   94.075  1.00 35.96  ? 130  VAL   A CB   1 
ATOM   1003 C  CG1  . VAL   A 1 151 ? 362.202 4.675   92.722  1.00 35.00  ? 130  VAL   A CG1  1 
ATOM   1004 C  CG2  . VAL   A 1 151 ? 363.682 4.018   94.621  1.00 37.83  ? 130  VAL   A CG2  1 
ATOM   1005 N  N    . GLU   A 1 152 ? 363.090 8.399   92.609  1.00 36.76  ? 131  GLU   A N    1 
ATOM   1006 C  CA   . GLU   A 1 152 ? 362.294 9.492   92.078  1.00 37.93  ? 131  GLU   A CA   1 
ATOM   1007 C  C    . GLU   A 1 152 ? 361.186 8.949   91.176  1.00 38.32  ? 131  GLU   A C    1 
ATOM   1008 O  O    . GLU   A 1 152 ? 361.172 7.774   90.795  1.00 37.06  ? 131  GLU   A O    1 
ATOM   1009 C  CB   . GLU   A 1 152 ? 363.175 10.479  91.313  1.00 35.72  ? 131  GLU   A CB   1 
ATOM   1010 C  CG   . GLU   A 1 152 ? 363.798 9.918   90.041  1.00 39.59  ? 131  GLU   A CG   1 
ATOM   1011 C  CD   . GLU   A 1 152 ? 365.101 9.183   90.293  1.00 40.60  ? 131  GLU   A CD   1 
ATOM   1012 O  OE1  . GLU   A 1 152 ? 365.345 8.783   91.449  1.00 40.36  ? 131  GLU   A OE1  1 
ATOM   1013 O  OE2  . GLU   A 1 152 ? 365.886 9.015   89.334  1.00 35.53  ? 131  GLU   A OE2  1 
ATOM   1014 N  N    . LYS   A 1 153 ? 360.244 9.823   90.830  1.00 39.58  ? 132  LYS   A N    1 
ATOM   1015 C  CA   . LYS   A 1 153 ? 359.073 9.427   90.053  1.00 40.74  ? 132  LYS   A CA   1 
ATOM   1016 C  C    . LYS   A 1 153 ? 359.396 9.504   88.565  1.00 41.48  ? 132  LYS   A C    1 
ATOM   1017 O  O    . LYS   A 1 153 ? 359.642 10.589  88.027  1.00 41.15  ? 132  LYS   A O    1 
ATOM   1018 C  CB   . LYS   A 1 153 ? 357.870 10.297  90.410  1.00 43.27  ? 132  LYS   A CB   1 
ATOM   1019 C  CG   . LYS   A 1 153 ? 357.272 9.976   91.776  1.00 48.42  ? 132  LYS   A CG   1 
ATOM   1020 C  CD   . LYS   A 1 153 ? 356.202 10.980  92.177  1.00 62.34  ? 132  LYS   A CD   1 
ATOM   1021 C  CE   . LYS   A 1 153 ? 355.532 10.597  93.494  1.00 66.69  ? 132  LYS   A CE   1 
ATOM   1022 N  NZ   . LYS   A 1 153 ? 354.504 9.527   93.328  1.00 67.32  ? 132  LYS   A NZ   1 
ATOM   1023 N  N    . ASN   A 1 154 ? 359.413 8.346   87.910  1.00 37.02  ? 133  ASN   A N    1 
ATOM   1024 C  CA   . ASN   A 1 154 ? 359.501 8.234   86.457  1.00 37.44  ? 133  ASN   A CA   1 
ATOM   1025 C  C    . ASN   A 1 154 ? 360.610 9.117   85.881  1.00 37.68  ? 133  ASN   A C    1 
ATOM   1026 O  O    . ASN   A 1 154 ? 360.375 10.011  85.068  1.00 45.14  ? 133  ASN   A O    1 
ATOM   1027 C  CB   . ASN   A 1 154 ? 358.154 8.565   85.815  1.00 42.21  ? 133  ASN   A CB   1 
ATOM   1028 C  CG   . ASN   A 1 154 ? 358.154 8.330   84.325  1.00 34.49  ? 133  ASN   A CG   1 
ATOM   1029 O  OD1  . ASN   A 1 154 ? 358.877 7.468   83.824  1.00 36.31  ? 133  ASN   A OD1  1 
ATOM   1030 N  ND2  . ASN   A 1 154 ? 357.350 9.101   83.603  1.00 39.17  ? 133  ASN   A ND2  1 
ATOM   1031 N  N    . ASN   A 1 155 ? 361.832 8.842   86.304  1.00 36.57  ? 134  ASN   A N    1 
ATOM   1032 C  CA   . ASN   A 1 155 ? 362.981 9.515   85.715  1.00 38.87  ? 134  ASN   A CA   1 
ATOM   1033 C  C    . ASN   A 1 155 ? 362.970 9.286   84.206  1.00 37.19  ? 134  ASN   A C    1 
ATOM   1034 O  O    . ASN   A 1 155 ? 362.924 8.128   83.767  1.00 34.84  ? 134  ASN   A O    1 
ATOM   1035 C  CB   . ASN   A 1 155 ? 364.275 9.002   86.339  1.00 36.36  ? 134  ASN   A CB   1 
ATOM   1036 C  CG   . ASN   A 1 155 ? 365.493 9.780   85.886  1.00 38.29  ? 134  ASN   A CG   1 
ATOM   1037 O  OD1  . ASN   A 1 155 ? 365.617 10.140  84.715  1.00 38.54  ? 134  ASN   A OD1  1 
ATOM   1038 N  ND2  . ASN   A 1 155 ? 366.403 10.043  86.815  1.00 31.60  ? 134  ASN   A ND2  1 
ATOM   1039 N  N    . PRO   A 1 156 ? 362.995 10.338  83.386  1.00 37.68  ? 135  PRO   A N    1 
ATOM   1040 C  CA   . PRO   A 1 156 ? 362.885 10.130  81.931  1.00 33.72  ? 135  PRO   A CA   1 
ATOM   1041 C  C    . PRO   A 1 156 ? 364.032 9.339   81.340  1.00 38.93  ? 135  PRO   A C    1 
ATOM   1042 O  O    . PRO   A 1 156 ? 363.858 8.714   80.287  1.00 42.12  ? 135  PRO   A O    1 
ATOM   1043 C  CB   . PRO   A 1 156 ? 362.840 11.560  81.371  1.00 38.62  ? 135  PRO   A CB   1 
ATOM   1044 C  CG   . PRO   A 1 156 ? 363.428 12.418  82.446  1.00 37.49  ? 135  PRO   A CG   1 
ATOM   1045 C  CD   . PRO   A 1 156 ? 363.052 11.765  83.740  1.00 39.00  ? 135  PRO   A CD   1 
ATOM   1046 N  N    . LYS   A 1 157 ? 365.197 9.331   81.981  1.00 35.62  ? 136  LYS   A N    1 
ATOM   1047 C  CA   . LYS   A 1 157 ? 366.343 8.583   81.486  1.00 36.02  ? 136  LYS   A CA   1 
ATOM   1048 C  C    . LYS   A 1 157 ? 366.495 7.228   82.170  1.00 34.22  ? 136  LYS   A C    1 
ATOM   1049 O  O    . LYS   A 1 157 ? 367.576 6.633   82.118  1.00 33.15  ? 136  LYS   A O    1 
ATOM   1050 C  CB   . LYS   A 1 157 ? 367.613 9.417   81.646  1.00 39.00  ? 136  LYS   A CB   1 
ATOM   1051 C  CG   . LYS   A 1 157 ? 367.566 10.722  80.874  1.00 41.19  ? 136  LYS   A CG   1 
ATOM   1052 C  CD   . LYS   A 1 157 ? 368.882 11.467  80.965  1.00 55.63  ? 136  LYS   A CD   1 
ATOM   1053 C  CE   . LYS   A 1 157 ? 368.957 12.569  79.922  1.00 65.04  ? 136  LYS   A CE   1 
ATOM   1054 N  NZ   . LYS   A 1 157 ? 368.829 12.025  78.541  1.00 69.22  ? 136  LYS   A NZ   1 
ATOM   1055 N  N    . LYS   A 1 158 ? 365.424 6.718   82.787  1.00 32.81  ? 137  LYS   A N    1 
ATOM   1056 C  CA   . LYS   A 1 158 ? 365.519 5.499   83.585  1.00 32.13  ? 137  LYS   A CA   1 
ATOM   1057 C  C    . LYS   A 1 158 ? 365.701 4.245   82.740  1.00 33.27  ? 137  LYS   A C    1 
ATOM   1058 O  O    . LYS   A 1 158 ? 366.072 3.197   83.283  1.00 31.72  ? 137  LYS   A O    1 
ATOM   1059 C  CB   . LYS   A 1 158 ? 364.275 5.344   84.460  1.00 29.48  ? 137  LYS   A CB   1 
ATOM   1060 C  CG   . LYS   A 1 158 ? 363.010 5.017   83.682  1.00 29.49  ? 137  LYS   A CG   1 
ATOM   1061 C  CD   . LYS   A 1 158 ? 361.800 5.008   84.599  1.00 31.82  ? 137  LYS   A CD   1 
ATOM   1062 C  CE   . LYS   A 1 158 ? 360.554 4.490   83.898  1.00 31.11  ? 137  LYS   A CE   1 
ATOM   1063 N  NZ   . LYS   A 1 158 ? 359.350 4.687   84.755  1.00 32.51  ? 137  LYS   A NZ   1 
ATOM   1064 N  N    . ALA   A 1 159 ? 365.439 4.318   81.437  1.00 33.93  ? 138  ALA   A N    1 
ATOM   1065 C  CA   . ALA   A 1 159 ? 365.609 3.181   80.543  1.00 29.65  ? 138  ALA   A CA   1 
ATOM   1066 C  C    . ALA   A 1 159 ? 366.962 3.179   79.845  1.00 31.07  ? 138  ALA   A C    1 
ATOM   1067 O  O    . ALA   A 1 159 ? 367.196 2.341   78.971  1.00 35.69  ? 138  ALA   A O    1 
ATOM   1068 C  CB   . ALA   A 1 159 ? 364.488 3.150   79.503  1.00 26.03  ? 138  ALA   A CB   1 
ATOM   1069 N  N    . SER   A 1 160 ? 367.854 4.096   80.200  1.00 32.69  ? 139  SER   A N    1 
ATOM   1070 C  CA   . SER   A 1 160 ? 369.195 4.122   79.641  1.00 38.97  ? 139  SER   A CA   1 
ATOM   1071 C  C    . SER   A 1 160 ? 370.199 4.293   80.772  1.00 31.83  ? 139  SER   A C    1 
ATOM   1072 O  O    . SER   A 1 160 ? 369.846 4.648   81.900  1.00 34.42  ? 139  SER   A O    1 
ATOM   1073 C  CB   . SER   A 1 160 ? 369.358 5.244   78.611  1.00 39.28  ? 139  SER   A CB   1 
ATOM   1074 O  OG   . SER   A 1 160 ? 369.374 6.508   79.251  1.00 45.58  ? 139  SER   A OG   1 
ATOM   1075 N  N    . TRP   A 1 161 ? 371.468 4.039   80.458  1.00 38.66  ? 140  TRP   A N    1 
ATOM   1076 C  CA   . TRP   A 1 161 ? 372.535 4.134   81.445  1.00 31.99  ? 140  TRP   A CA   1 
ATOM   1077 C  C    . TRP   A 1 161 ? 373.722 4.843   80.812  1.00 34.00  ? 140  TRP   A C    1 
ATOM   1078 O  O    . TRP   A 1 161 ? 374.294 4.348   79.836  1.00 35.11  ? 140  TRP   A O    1 
ATOM   1079 C  CB   . TRP   A 1 161 ? 372.937 2.749   81.963  1.00 30.55  ? 140  TRP   A CB   1 
ATOM   1080 C  CG   . TRP   A 1 161 ? 373.522 2.822   83.332  1.00 32.27  ? 140  TRP   A CG   1 
ATOM   1081 C  CD1  . TRP   A 1 161 ? 372.882 2.591   84.514  1.00 31.10  ? 140  TRP   A CD1  1 
ATOM   1082 C  CD2  . TRP   A 1 161 ? 374.861 3.195   83.665  1.00 33.14  ? 140  TRP   A CD2  1 
ATOM   1083 N  NE1  . TRP   A 1 161 ? 373.748 2.783   85.565  1.00 30.43  ? 140  TRP   A NE1  1 
ATOM   1084 C  CE2  . TRP   A 1 161 ? 374.969 3.155   85.069  1.00 31.55  ? 140  TRP   A CE2  1 
ATOM   1085 C  CE3  . TRP   A 1 161 ? 375.983 3.552   82.911  1.00 30.92  ? 140  TRP   A CE3  1 
ATOM   1086 C  CZ2  . TRP   A 1 161 ? 376.154 3.459   85.734  1.00 29.32  ? 140  TRP   A CZ2  1 
ATOM   1087 C  CZ3  . TRP   A 1 161 ? 377.157 3.853   83.572  1.00 32.32  ? 140  TRP   A CZ3  1 
ATOM   1088 C  CH2  . TRP   A 1 161 ? 377.234 3.804   84.969  1.00 32.68  ? 140  TRP   A CH2  1 
ATOM   1089 N  N    . THR   A 1 162 ? 374.092 5.999   81.363  1.00 33.36  ? 141  THR   A N    1 
ATOM   1090 C  CA   . THR   A 1 162 ? 375.164 6.816   80.811  1.00 40.06  ? 141  THR   A CA   1 
ATOM   1091 C  C    . THR   A 1 162 ? 376.180 7.160   81.890  1.00 37.83  ? 141  THR   A C    1 
ATOM   1092 O  O    . THR   A 1 162 ? 375.818 7.412   83.044  1.00 33.26  ? 141  THR   A O    1 
ATOM   1093 C  CB   . THR   A 1 162 ? 374.617 8.104   80.186  1.00 38.75  ? 141  THR   A CB   1 
ATOM   1094 O  OG1  . THR   A 1 162 ? 373.889 8.844   81.173  1.00 35.06  ? 141  THR   A OG1  1 
ATOM   1095 C  CG2  . THR   A 1 162 ? 373.697 7.771   79.020  1.00 34.86  ? 141  THR   A CG2  1 
ATOM   1096 N  N    . TRP   A 1 163 ? 377.452 7.172   81.499  1.00 36.60  ? 142  TRP   A N    1 
ATOM   1097 C  CA   . TRP   A 1 163 ? 378.554 7.462   82.400  1.00 37.79  ? 142  TRP   A CA   1 
ATOM   1098 C  C    . TRP   A 1 163 ? 378.693 8.964   82.627  1.00 34.53  ? 142  TRP   A C    1 
ATOM   1099 O  O    . TRP   A 1 163 ? 378.193 9.787   81.856  1.00 37.25  ? 142  TRP   A O    1 
ATOM   1100 C  CB   . TRP   A 1 163 ? 379.867 6.918   81.835  1.00 40.25  ? 142  TRP   A CB   1 
ATOM   1101 C  CG   . TRP   A 1 163 ? 379.927 5.432   81.742  1.00 39.07  ? 142  TRP   A CG   1 
ATOM   1102 C  CD1  . TRP   A 1 163 ? 379.480 4.653   80.716  1.00 34.63  ? 142  TRP   A CD1  1 
ATOM   1103 C  CD2  . TRP   A 1 163 ? 380.480 4.540   82.714  1.00 31.66  ? 142  TRP   A CD2  1 
ATOM   1104 N  NE1  . TRP   A 1 163 ? 379.716 3.327   80.992  1.00 35.33  ? 142  TRP   A NE1  1 
ATOM   1105 C  CE2  . TRP   A 1 163 ? 380.330 3.232   82.213  1.00 34.89  ? 142  TRP   A CE2  1 
ATOM   1106 C  CE3  . TRP   A 1 163 ? 381.085 4.720   83.961  1.00 31.25  ? 142  TRP   A CE3  1 
ATOM   1107 C  CZ2  . TRP   A 1 163 ? 380.763 2.110   82.916  1.00 33.66  ? 142  TRP   A CZ2  1 
ATOM   1108 C  CZ3  . TRP   A 1 163 ? 381.515 3.607   84.657  1.00 29.07  ? 142  TRP   A CZ3  1 
ATOM   1109 C  CH2  . TRP   A 1 163 ? 381.351 2.318   84.133  1.00 32.07  ? 142  TRP   A CH2  1 
ATOM   1110 N  N    . GLY   A 1 164 ? 379.398 9.315   83.698  1.00 36.70  ? 143  GLY   A N    1 
ATOM   1111 C  CA   . GLY   A 1 164 ? 379.788 10.684  83.929  1.00 41.68  ? 143  GLY   A CA   1 
ATOM   1112 C  C    . GLY   A 1 164 ? 379.043 11.350  85.067  1.00 43.25  ? 143  GLY   A C    1 
ATOM   1113 O  O    . GLY   A 1 164 ? 378.024 10.853  85.559  1.00 40.01  ? 143  GLY   A O    1 
ATOM   1114 N  N    . PRO   A 1 165 ? 379.550 12.504  85.506  1.00 44.27  ? 144  PRO   A N    1 
ATOM   1115 C  CA   . PRO   A 1 165 ? 378.850 13.250  86.562  1.00 46.75  ? 144  PRO   A CA   1 
ATOM   1116 C  C    . PRO   A 1 165 ? 377.461 13.690  86.146  1.00 53.18  ? 144  PRO   A C    1 
ATOM   1117 O  O    . PRO   A 1 165 ? 376.582 13.839  87.004  1.00 53.74  ? 144  PRO   A O    1 
ATOM   1118 C  CB   . PRO   A 1 165 ? 379.775 14.451  86.818  1.00 49.72  ? 144  PRO   A CB   1 
ATOM   1119 C  CG   . PRO   A 1 165 ? 381.093 14.083  86.191  1.00 47.30  ? 144  PRO   A CG   1 
ATOM   1120 C  CD   . PRO   A 1 165 ? 380.750 13.210  85.030  1.00 44.71  ? 144  PRO   A CD   1 
ATOM   1121 N  N    . GLU   A 1 166 ? 377.234 13.901  84.851  1.00 54.73  ? 145  GLU   A N    1 
ATOM   1122 C  CA   . GLU   A 1 166 ? 375.915 14.241  84.338  1.00 57.34  ? 145  GLU   A CA   1 
ATOM   1123 C  C    . GLU   A 1 166 ? 375.147 13.023  83.841  1.00 52.08  ? 145  GLU   A C    1 
ATOM   1124 O  O    . GLU   A 1 166 ? 374.040 13.177  83.317  1.00 58.19  ? 145  GLU   A O    1 
ATOM   1125 C  CB   . GLU   A 1 166 ? 376.036 15.274  83.212  1.00 60.29  ? 145  GLU   A CB   1 
ATOM   1126 C  CG   . GLU   A 1 166 ? 376.914 16.472  83.559  1.00 70.96  ? 145  GLU   A CG   1 
ATOM   1127 C  CD   . GLU   A 1 166 ? 376.418 17.239  84.773  1.00 87.45  ? 145  GLU   A CD   1 
ATOM   1128 O  OE1  . GLU   A 1 166 ? 375.190 17.271  84.999  1.00 90.89  ? 145  GLU   A OE1  1 
ATOM   1129 O  OE2  . GLU   A 1 166 ? 377.257 17.809  85.505  1.00 86.12  ? 145  GLU   A OE2  1 
ATOM   1130 N  N    . GLY   A 1 167 ? 375.705 11.821  83.990  1.00 40.47  ? 146  GLY   A N    1 
ATOM   1131 C  CA   . GLY   A 1 167 ? 375.027 10.628  83.537  1.00 38.21  ? 146  GLY   A CA   1 
ATOM   1132 C  C    . GLY   A 1 167 ? 373.968 10.160  84.511  1.00 38.75  ? 146  GLY   A C    1 
ATOM   1133 O  O    . GLY   A 1 167 ? 373.872 10.628  85.645  1.00 40.66  ? 146  GLY   A O    1 
ATOM   1134 N  N    . GLN   A 1 168 ? 373.156 9.212   84.049  1.00 34.82  ? 147  GLN   A N    1 
ATOM   1135 C  CA   . GLN   A 1 168 ? 372.086 8.678   84.877  1.00 34.80  ? 147  GLN   A CA   1 
ATOM   1136 C  C    . GLN   A 1 168 ? 371.836 7.222   84.522  1.00 33.85  ? 147  GLN   A C    1 
ATOM   1137 O  O    . GLN   A 1 168 ? 372.285 6.727   83.484  1.00 32.77  ? 147  GLN   A O    1 
ATOM   1138 C  CB   . GLN   A 1 168 ? 370.801 9.495   84.725  1.00 38.98  ? 147  GLN   A CB   1 
ATOM   1139 C  CG   . GLN   A 1 168 ? 370.911 10.883  85.300  1.00 41.06  ? 147  GLN   A CG   1 
ATOM   1140 C  CD   . GLN   A 1 168 ? 369.564 11.532  85.446  1.00 44.66  ? 147  GLN   A CD   1 
ATOM   1141 O  OE1  . GLN   A 1 168 ? 368.787 11.174  86.329  1.00 46.28  ? 147  GLN   A OE1  1 
ATOM   1142 N  NE2  . GLN   A 1 168 ? 369.264 12.478  84.567  1.00 53.29  ? 147  GLN   A NE2  1 
ATOM   1143 N  N    . GLY   A 1 169 ? 371.107 6.543   85.408  1.00 33.64  ? 148  GLY   A N    1 
ATOM   1144 C  CA   . GLY   A 1 169 ? 370.846 5.122   85.295  1.00 32.33  ? 148  GLY   A CA   1 
ATOM   1145 C  C    . GLY   A 1 169 ? 371.079 4.437   86.626  1.00 29.56  ? 148  GLY   A C    1 
ATOM   1146 O  O    . GLY   A 1 169 ? 372.085 4.704   87.288  1.00 33.24  ? 148  GLY   A O    1 
ATOM   1147 N  N    . ALA   A 1 170 ? 370.166 3.562   87.037  1.00 33.07  ? 149  ALA   A N    1 
ATOM   1148 C  CA   . ALA   A 1 170 ? 370.247 2.987   88.373  1.00 35.11  ? 149  ALA   A CA   1 
ATOM   1149 C  C    . ALA   A 1 170 ? 371.377 1.967   88.465  1.00 34.47  ? 149  ALA   A C    1 
ATOM   1150 O  O    . ALA   A 1 170 ? 371.735 1.310   87.485  1.00 32.33  ? 149  ALA   A O    1 
ATOM   1151 C  CB   . ALA   A 1 170 ? 368.920 2.336   88.759  1.00 28.46  ? 149  ALA   A CB   1 
ATOM   1152 N  N    . ILE   A 1 171 ? 371.937 1.832   89.666  1.00 30.34  ? 150  ILE   A N    1 
ATOM   1153 C  CA   . ILE   A 1 171 ? 373.080 0.959   89.899  1.00 27.57  ? 150  ILE   A CA   1 
ATOM   1154 C  C    . ILE   A 1 171 ? 372.667 -0.184  90.813  1.00 30.21  ? 150  ILE   A C    1 
ATOM   1155 O  O    . ILE   A 1 171 ? 371.849 -0.024  91.726  1.00 31.98  ? 150  ILE   A O    1 
ATOM   1156 C  CB   . ILE   A 1 171 ? 374.277 1.729   90.490  1.00 29.72  ? 150  ILE   A CB   1 
ATOM   1157 C  CG1  . ILE   A 1 171 ? 374.706 2.838   89.533  1.00 26.75  ? 150  ILE   A CG1  1 
ATOM   1158 C  CG2  . ILE   A 1 171 ? 375.440 0.785   90.763  1.00 32.80  ? 150  ILE   A CG2  1 
ATOM   1159 C  CD1  . ILE   A 1 171 ? 375.731 3.768   90.119  1.00 32.21  ? 150  ILE   A CD1  1 
ATOM   1160 N  N    . LEU   A 1 172 ? 373.258 -1.347  90.564  1.00 31.34  ? 151  LEU   A N    1 
ATOM   1161 C  CA   . LEU   A 1 172 ? 372.876 -2.584  91.224  1.00 28.55  ? 151  LEU   A CA   1 
ATOM   1162 C  C    . LEU   A 1 172 ? 374.128 -3.274  91.744  1.00 27.98  ? 151  LEU   A C    1 
ATOM   1163 O  O    . LEU   A 1 172 ? 375.129 -3.367  91.030  1.00 29.26  ? 151  LEU   A O    1 
ATOM   1164 C  CB   . LEU   A 1 172 ? 372.122 -3.489  90.248  1.00 25.19  ? 151  LEU   A CB   1 
ATOM   1165 C  CG   . LEU   A 1 172 ? 371.528 -4.799  90.746  1.00 32.02  ? 151  LEU   A CG   1 
ATOM   1166 C  CD1  . LEU   A 1 172 ? 370.508 -4.530  91.842  1.00 27.61  ? 151  LEU   A CD1  1 
ATOM   1167 C  CD2  . LEU   A 1 172 ? 370.904 -5.537  89.570  1.00 25.65  ? 151  LEU   A CD2  1 
ATOM   1168 N  N    . LEU   A 1 173 ? 374.077 -3.744  92.985  1.00 29.85  ? 152  LEU   A N    1 
ATOM   1169 C  CA   . LEU   A 1 173 ? 375.196 -4.467  93.567  1.00 28.57  ? 152  LEU   A CA   1 
ATOM   1170 C  C    . LEU   A 1 173 ? 375.044 -5.964  93.336  1.00 28.64  ? 152  LEU   A C    1 
ATOM   1171 O  O    . LEU   A 1 173 ? 373.930 -6.496  93.283  1.00 31.56  ? 152  LEU   A O    1 
ATOM   1172 C  CB   . LEU   A 1 173 ? 375.302 -4.203  95.071  1.00 34.86  ? 152  LEU   A CB   1 
ATOM   1173 C  CG   . LEU   A 1 173 ? 375.646 -2.807  95.587  1.00 37.76  ? 152  LEU   A CG   1 
ATOM   1174 C  CD1  . LEU   A 1 173 ? 375.727 -2.819  97.111  1.00 38.38  ? 152  LEU   A CD1  1 
ATOM   1175 C  CD2  . LEU   A 1 173 ? 376.945 -2.313  94.976  1.00 31.56  ? 152  LEU   A CD2  1 
ATOM   1176 N  N    . VAL   A 1 174 ? 376.178 -6.644  93.200  1.00 29.89  ? 153  VAL   A N    1 
ATOM   1177 C  CA   . VAL   A 1 174 ? 376.199 -8.099  93.292  1.00 33.39  ? 153  VAL   A CA   1 
ATOM   1178 C  C    . VAL   A 1 174 ? 376.096 -8.466  94.765  1.00 32.87  ? 153  VAL   A C    1 
ATOM   1179 O  O    . VAL   A 1 174 ? 376.961 -8.100  95.567  1.00 32.88  ? 153  VAL   A O    1 
ATOM   1180 C  CB   . VAL   A 1 174 ? 377.468 -8.689  92.664  1.00 32.71  ? 153  VAL   A CB   1 
ATOM   1181 C  CG1  . VAL   A 1 174 ? 377.478 -10.202 92.833  1.00 31.48  ? 153  VAL   A CG1  1 
ATOM   1182 C  CG2  . VAL   A 1 174 ? 377.568 -8.303  91.197  1.00 32.40  ? 153  VAL   A CG2  1 
ATOM   1183 N  N    . ASN   A 1 175 ? 375.028 -9.175  95.127  1.00 29.99  ? 154  ASN   A N    1 
ATOM   1184 C  CA   . ASN   A 1 175 ? 374.746 -9.495  96.525  1.00 32.12  ? 154  ASN   A CA   1 
ATOM   1185 C  C    . ASN   A 1 175 ? 375.574 -10.711 96.940  1.00 35.08  ? 154  ASN   A C    1 
ATOM   1186 O  O    . ASN   A 1 175 ? 375.068 -11.812 97.164  1.00 39.34  ? 154  ASN   A O    1 
ATOM   1187 C  CB   . ASN   A 1 175 ? 373.255 -9.733  96.714  1.00 38.12  ? 154  ASN   A CB   1 
ATOM   1188 C  CG   . ASN   A 1 175 ? 372.846 -9.736  98.168  1.00 41.10  ? 154  ASN   A CG   1 
ATOM   1189 O  OD1  . ASN   A 1 175 ? 373.638 -9.404  99.050  1.00 36.00  ? 154  ASN   A OD1  1 
ATOM   1190 N  ND2  . ASN   A 1 175 ? 371.598 -10.102 98.429  1.00 37.80  ? 154  ASN   A ND2  1 
ATOM   1191 N  N    . CYS   A 1 176 ? 376.884 -10.489 97.042  1.00 34.00  ? 155  CYS   A N    1 
ATOM   1192 C  CA   . CYS   A 1 176 ? 377.837 -11.568 97.255  1.00 40.03  ? 155  CYS   A CA   1 
ATOM   1193 C  C    . CYS   A 1 176 ? 378.408 -11.600 98.667  1.00 38.45  ? 155  CYS   A C    1 
ATOM   1194 O  O    . CYS   A 1 176 ? 379.412 -12.281 98.899  1.00 41.10  ? 155  CYS   A O    1 
ATOM   1195 C  CB   . CYS   A 1 176 ? 378.972 -11.481 96.228  1.00 35.93  ? 155  CYS   A CB   1 
ATOM   1196 S  SG   . CYS   A 1 176 ? 379.892 -9.923  96.207  1.00 36.76  ? 155  CYS   A SG   1 
ATOM   1197 N  N    . ASP   A 1 177 ? 377.802 -10.895 99.614  1.00 40.30  ? 156  ASP   A N    1 
ATOM   1198 C  CA   . ASP   A 1 177 ? 378.162 -11.083 101.009 1.00 45.67  ? 156  ASP   A CA   1 
ATOM   1199 C  C    . ASP   A 1 177 ? 377.293 -12.205 101.582 1.00 50.92  ? 156  ASP   A C    1 
ATOM   1200 O  O    . ASP   A 1 177 ? 376.658 -12.960 100.840 1.00 44.27  ? 156  ASP   A O    1 
ATOM   1201 C  CB   . ASP   A 1 177 ? 378.041 -9.766  101.775 1.00 45.91  ? 156  ASP   A CB   1 
ATOM   1202 C  CG   . ASP   A 1 177 ? 376.625 -9.231  101.808 1.00 43.87  ? 156  ASP   A CG   1 
ATOM   1203 O  OD1  . ASP   A 1 177 ? 375.838 -9.550  100.893 1.00 43.79  ? 156  ASP   A OD1  1 
ATOM   1204 O  OD2  . ASP   A 1 177 ? 376.303 -8.482  102.754 1.00 43.88  ? 156  ASP   A OD2  1 
ATOM   1205 N  N    . ARG   A 1 178 ? 377.262 -12.341 102.908 1.00 54.78  ? 157  ARG   A N    1 
ATOM   1206 C  CA   . ARG   A 1 178 ? 376.476 -13.391 103.556 1.00 59.52  ? 157  ARG   A CA   1 
ATOM   1207 C  C    . ARG   A 1 178 ? 375.858 -12.836 104.832 1.00 57.38  ? 157  ARG   A C    1 
ATOM   1208 O  O    . ARG   A 1 178 ? 376.569 -12.585 105.811 1.00 57.35  ? 157  ARG   A O    1 
ATOM   1209 C  CB   . ARG   A 1 178 ? 377.335 -14.618 103.859 1.00 60.32  ? 157  ARG   A CB   1 
ATOM   1210 C  CG   . ARG   A 1 178 ? 376.527 -15.857 104.203 1.00 67.83  ? 157  ARG   A CG   1 
ATOM   1211 C  CD   . ARG   A 1 178 ? 377.422 -17.073 104.308 1.00 75.00  ? 157  ARG   A CD   1 
ATOM   1212 N  NE   . ARG   A 1 178 ? 378.355 -16.960 105.421 1.00 77.96  ? 157  ARG   A NE   1 
ATOM   1213 C  CZ   . ARG   A 1 178 ? 379.350 -17.805 105.651 1.00 80.91  ? 157  ARG   A CZ   1 
ATOM   1214 N  NH1  . ARG   A 1 178 ? 379.587 -18.829 104.847 1.00 78.96  ? 157  ARG   A NH1  1 
ATOM   1215 N  NH2  . ARG   A 1 178 ? 380.127 -17.619 106.714 1.00 84.29  ? 157  ARG   A NH2  1 
ATOM   1216 N  N    . GLU   A 1 179 ? 374.531 -12.671 104.831 1.00 53.71  ? 158  GLU   A N    1 
ATOM   1217 C  CA   . GLU   A 1 179 ? 373.843 -12.103 105.985 1.00 58.06  ? 158  GLU   A CA   1 
ATOM   1218 C  C    . GLU   A 1 179 ? 373.699 -13.102 107.130 1.00 69.42  ? 158  GLU   A C    1 
ATOM   1219 O  O    . GLU   A 1 179 ? 373.674 -12.696 108.297 1.00 71.36  ? 158  GLU   A O    1 
ATOM   1220 C  CB   . GLU   A 1 179 ? 372.464 -11.580 105.574 1.00 51.54  ? 158  GLU   A CB   1 
ATOM   1221 C  CG   . GLU   A 1 179 ? 372.472 -10.649 104.364 1.00 53.09  ? 158  GLU   A CG   1 
ATOM   1222 C  CD   . GLU   A 1 179 ? 373.313 -9.403  104.580 1.00 53.91  ? 158  GLU   A CD   1 
ATOM   1223 O  OE1  . GLU   A 1 179 ? 373.666 -9.111  105.742 1.00 58.84  ? 158  GLU   A OE1  1 
ATOM   1224 O  OE2  . GLU   A 1 179 ? 373.624 -8.714  103.586 1.00 51.60  ? 158  GLU   A OE2  1 
ATOM   1225 N  N    . THR   A 1 180 ? 373.598 -14.398 106.828 1.00 71.92  ? 159  THR   A N    1 
ATOM   1226 C  CA   . THR   A 1 180 ? 373.445 -15.422 107.854 1.00 76.96  ? 159  THR   A CA   1 
ATOM   1227 C  C    . THR   A 1 180 ? 374.492 -16.513 107.654 1.00 75.49  ? 159  THR   A C    1 
ATOM   1228 O  O    . THR   A 1 180 ? 374.650 -17.022 106.530 1.00 76.07  ? 159  THR   A O    1 
ATOM   1229 C  CB   . THR   A 1 180 ? 372.037 -16.030 107.827 1.00 82.46  ? 159  THR   A CB   1 
ATOM   1230 O  OG1  . THR   A 1 180 ? 371.760 -16.539 106.518 1.00 83.78  ? 159  THR   A OG1  1 
ATOM   1231 C  CG2  . THR   A 1 180 ? 370.993 -14.981 108.196 1.00 81.58  ? 159  THR   A CG2  1 
ATOM   1232 N  N    . PRO   A 1 181 ? 375.207 -16.916 108.711 1.00 81.81  ? 160  PRO   A N    1 
ATOM   1233 C  CA   . PRO   A 1 181 ? 376.279 -17.912 108.549 1.00 84.52  ? 160  PRO   A CA   1 
ATOM   1234 C  C    . PRO   A 1 181 ? 375.777 -19.331 108.344 1.00 83.16  ? 160  PRO   A C    1 
ATOM   1235 O  O    . PRO   A 1 181 ? 376.582 -20.201 107.988 1.00 80.20  ? 160  PRO   A O    1 
ATOM   1236 C  CB   . PRO   A 1 181 ? 377.062 -17.793 109.860 1.00 85.42  ? 160  PRO   A CB   1 
ATOM   1237 C  CG   . PRO   A 1 181 ? 376.006 -17.413 110.857 1.00 81.21  ? 160  PRO   A CG   1 
ATOM   1238 C  CD   . PRO   A 1 181 ? 375.039 -16.512 110.118 1.00 84.18  ? 160  PRO   A CD   1 
ATOM   1239 N  N    . TRP   A 1 182 ? 374.489 -19.597 108.570 1.00 87.17  ? 161  TRP   A N    1 
ATOM   1240 C  CA   . TRP   A 1 182 ? 373.961 -20.951 108.426 1.00 88.74  ? 161  TRP   A CA   1 
ATOM   1241 C  C    . TRP   A 1 182 ? 374.282 -21.524 107.050 1.00 87.53  ? 161  TRP   A C    1 
ATOM   1242 O  O    . TRP   A 1 182 ? 374.887 -22.595 106.929 1.00 91.19  ? 161  TRP   A O    1 
ATOM   1243 C  CB   . TRP   A 1 182 ? 372.450 -20.948 108.677 1.00 79.46  ? 161  TRP   A CB   1 
ATOM   1244 N  N    . LEU   A 1 183 ? 373.880 -20.819 105.995 1.00 87.98  ? 162  LEU   A N    1 
ATOM   1245 C  CA   . LEU   A 1 183 ? 374.199 -21.284 104.656 1.00 79.58  ? 162  LEU   A CA   1 
ATOM   1246 C  C    . LEU   A 1 183 ? 375.635 -20.903 104.291 1.00 80.93  ? 162  LEU   A C    1 
ATOM   1247 O  O    . LEU   A 1 183 ? 376.162 -19.903 104.784 1.00 86.00  ? 162  LEU   A O    1 
ATOM   1248 C  CB   . LEU   A 1 183 ? 373.219 -20.701 103.641 1.00 81.35  ? 162  LEU   A CB   1 
ATOM   1249 C  CG   . LEU   A 1 183 ? 373.094 -19.178 103.577 1.00 83.59  ? 162  LEU   A CG   1 
ATOM   1250 C  CD1  . LEU   A 1 183 ? 374.245 -18.586 102.803 1.00 88.27  ? 162  LEU   A CD1  1 
ATOM   1251 C  CD2  . LEU   A 1 183 ? 371.770 -18.765 102.959 1.00 80.24  ? 162  LEU   A CD2  1 
ATOM   1252 N  N    . PRO   A 1 184 ? 376.289 -21.688 103.427 1.00 80.96  ? 163  PRO   A N    1 
ATOM   1253 C  CA   . PRO   A 1 184 ? 377.732 -21.507 103.209 1.00 82.39  ? 163  PRO   A CA   1 
ATOM   1254 C  C    . PRO   A 1 184 ? 378.096 -20.503 102.123 1.00 78.37  ? 163  PRO   A C    1 
ATOM   1255 O  O    . PRO   A 1 184 ? 379.176 -19.906 102.171 1.00 80.85  ? 163  PRO   A O    1 
ATOM   1256 C  CB   . PRO   A 1 184 ? 378.190 -22.916 102.823 1.00 82.58  ? 163  PRO   A CB   1 
ATOM   1257 C  CG   . PRO   A 1 184 ? 377.011 -23.475 102.089 1.00 81.25  ? 163  PRO   A CG   1 
ATOM   1258 C  CD   . PRO   A 1 184 ? 375.778 -22.896 102.755 1.00 75.44  ? 163  PRO   A CD   1 
ATOM   1259 N  N    . LYS   A 1 185 ? 377.224 -20.319 101.138 1.00 78.74  ? 164  LYS   A N    1 
ATOM   1260 C  CA   . LYS   A 1 185 ? 377.521 -19.494 99.976  1.00 70.27  ? 164  LYS   A CA   1 
ATOM   1261 C  C    . LYS   A 1 185 ? 376.906 -18.105 100.121 1.00 65.36  ? 164  LYS   A C    1 
ATOM   1262 O  O    . LYS   A 1 185 ? 376.044 -17.858 100.964 1.00 67.26  ? 164  LYS   A O    1 
ATOM   1263 C  CB   . LYS   A 1 185 ? 377.019 -20.180 98.702  1.00 70.67  ? 164  LYS   A CB   1 
ATOM   1264 C  CG   . LYS   A 1 185 ? 377.543 -21.593 98.543  1.00 74.49  ? 164  LYS   A CG   1 
ATOM   1265 C  CD   . LYS   A 1 185 ? 377.031 -22.248 97.276  1.00 82.15  ? 164  LYS   A CD   1 
ATOM   1266 C  CE   . LYS   A 1 185 ? 377.629 -23.635 97.114  1.00 88.77  ? 164  LYS   A CE   1 
ATOM   1267 N  NZ   . LYS   A 1 185 ? 379.117 -23.603 97.190  1.00 84.64  ? 164  LYS   A NZ   1 
ATOM   1268 N  N    . GLU   A 1 186 ? 377.359 -17.189 99.270  1.00 57.93  ? 165  GLU   A N    1 
ATOM   1269 C  CA   . GLU   A 1 186 ? 376.887 -15.814 99.335  1.00 54.48  ? 165  GLU   A CA   1 
ATOM   1270 C  C    . GLU   A 1 186 ? 375.374 -15.754 99.109  1.00 52.25  ? 165  GLU   A C    1 
ATOM   1271 O  O    . GLU   A 1 186 ? 374.737 -16.724 98.687  1.00 55.29  ? 165  GLU   A O    1 
ATOM   1272 C  CB   . GLU   A 1 186 ? 377.623 -14.946 98.313  1.00 53.77  ? 165  GLU   A CB   1 
ATOM   1273 C  CG   . GLU   A 1 186 ? 377.295 -15.257 96.861  1.00 55.60  ? 165  GLU   A CG   1 
ATOM   1274 C  CD   . GLU   A 1 186 ? 377.849 -16.591 96.394  1.00 65.04  ? 165  GLU   A CD   1 
ATOM   1275 O  OE1  . GLU   A 1 186 ? 378.810 -17.094 97.015  1.00 61.20  ? 165  GLU   A OE1  1 
ATOM   1276 O  OE2  . GLU   A 1 186 ? 377.319 -17.137 95.403  1.00 68.83  ? 165  GLU   A OE2  1 
ATOM   1277 N  N    . ASP   A 1 187 ? 374.798 -14.583 99.397  1.00 48.01  ? 166  ASP   A N    1 
ATOM   1278 C  CA   . ASP   A 1 187 ? 373.343 -14.451 99.385  1.00 47.24  ? 166  ASP   A CA   1 
ATOM   1279 C  C    . ASP   A 1 187 ? 372.764 -14.684 97.996  1.00 48.31  ? 166  ASP   A C    1 
ATOM   1280 O  O    . ASP   A 1 187 ? 371.693 -15.283 97.856  1.00 49.14  ? 166  ASP   A O    1 
ATOM   1281 C  CB   . ASP   A 1 187 ? 372.935 -13.072 99.897  1.00 46.67  ? 166  ASP   A CB   1 
ATOM   1282 C  CG   . ASP   A 1 187 ? 373.366 -12.830 101.324 1.00 50.86  ? 166  ASP   A CG   1 
ATOM   1283 O  OD1  . ASP   A 1 187 ? 373.477 -13.810 102.089 1.00 59.29  ? 166  ASP   A OD1  1 
ATOM   1284 O  OD2  . ASP   A 1 187 ? 373.592 -11.655 101.681 1.00 48.89  ? 166  ASP   A OD2  1 
ATOM   1285 N  N    . CYS   A 1 188 ? 373.440 -14.206 96.959  1.00 49.31  ? 167  CYS   A N    1 
ATOM   1286 C  CA   . CYS   A 1 188 ? 372.879 -14.281 95.617  1.00 48.54  ? 167  CYS   A CA   1 
ATOM   1287 C  C    . CYS   A 1 188 ? 372.938 -15.680 95.016  1.00 47.73  ? 167  CYS   A C    1 
ATOM   1288 O  O    . CYS   A 1 188 ? 372.440 -15.875 93.902  1.00 49.04  ? 167  CYS   A O    1 
ATOM   1289 C  CB   . CYS   A 1 188 ? 373.596 -13.297 94.693  1.00 40.48  ? 167  CYS   A CB   1 
ATOM   1290 S  SG   . CYS   A 1 188 ? 375.368 -13.558 94.630  1.00 46.62  ? 167  CYS   A SG   1 
ATOM   1291 N  N    . ARG   A 1 189 ? 373.522 -16.656 95.713  1.00 50.80  ? 168  ARG   A N    1 
ATOM   1292 C  CA   . ARG   A 1 189 ? 373.614 -18.000 95.154  1.00 54.71  ? 168  ARG   A CA   1 
ATOM   1293 C  C    . ARG   A 1 189 ? 372.260 -18.696 95.093  1.00 52.88  ? 168  ARG   A C    1 
ATOM   1294 O  O    . ARG   A 1 189 ? 372.101 -19.647 94.320  1.00 54.75  ? 168  ARG   A O    1 
ATOM   1295 C  CB   . ARG   A 1 189 ? 374.596 -18.849 95.965  1.00 57.28  ? 168  ARG   A CB   1 
ATOM   1296 C  CG   . ARG   A 1 189 ? 375.090 -20.088 95.229  1.00 61.13  ? 168  ARG   A CG   1 
ATOM   1297 C  CD   . ARG   A 1 189 ? 375.994 -19.720 94.058  1.00 71.17  ? 168  ARG   A CD   1 
ATOM   1298 N  NE   . ARG   A 1 189 ? 377.358 -19.436 94.491  1.00 74.36  ? 168  ARG   A NE   1 
ATOM   1299 C  CZ   . ARG   A 1 189 ? 378.317 -20.347 94.578  1.00 76.19  ? 168  ARG   A CZ   1 
ATOM   1300 N  NH1  . ARG   A 1 189 ? 378.103 -21.611 94.247  1.00 73.79  ? 168  ARG   A NH1  1 
ATOM   1301 N  NH2  . ARG   A 1 189 ? 379.522 -19.982 95.010  1.00 82.52  ? 168  ARG   A NH2  1 
ATOM   1302 N  N    . ASP   A 1 190 ? 371.289 -18.249 95.879  1.00 51.20  ? 169  ASP   A N    1 
ATOM   1303 C  CA   . ASP   A 1 190 ? 369.961 -18.845 95.907  1.00 53.30  ? 169  ASP   A CA   1 
ATOM   1304 C  C    . ASP   A 1 190 ? 368.926 -17.815 95.461  1.00 55.94  ? 169  ASP   A C    1 
ATOM   1305 O  O    . ASP   A 1 190 ? 369.254 -16.685 95.090  1.00 50.92  ? 169  ASP   A O    1 
ATOM   1306 C  CB   . ASP   A 1 190 ? 369.641 -19.401 97.301  1.00 52.53  ? 169  ASP   A CB   1 
ATOM   1307 C  CG   . ASP   A 1 190 ? 369.664 -18.333 98.389  1.00 55.32  ? 169  ASP   A CG   1 
ATOM   1308 O  OD1  . ASP   A 1 190 ? 369.457 -17.143 98.077  1.00 51.96  ? 169  ASP   A OD1  1 
ATOM   1309 O  OD2  . ASP   A 1 190 ? 369.893 -18.689 99.565  1.00 56.51  ? 169  ASP   A OD2  1 
ATOM   1310 N  N    . GLU   A 1 191 ? 367.662 -18.231 95.482  1.00 54.21  ? 170  GLU   A N    1 
ATOM   1311 C  CA   . GLU   A 1 191 ? 366.526 -17.361 95.200  1.00 47.39  ? 170  GLU   A CA   1 
ATOM   1312 C  C    . GLU   A 1 191 ? 365.725 -17.108 96.472  1.00 51.08  ? 170  GLU   A C    1 
ATOM   1313 O  O    . GLU   A 1 191 ? 364.494 -17.055 96.458  1.00 52.06  ? 170  GLU   A O    1 
ATOM   1314 C  CB   . GLU   A 1 191 ? 365.636 -17.954 94.109  1.00 52.21  ? 170  GLU   A CB   1 
ATOM   1315 C  CG   . GLU   A 1 191 ? 366.331 -18.154 92.765  1.00 51.41  ? 170  GLU   A CG   1 
ATOM   1316 C  CD   . GLU   A 1 191 ? 367.232 -19.374 92.745  1.00 59.28  ? 170  GLU   A CD   1 
ATOM   1317 O  OE1  . GLU   A 1 191 ? 366.707 -20.502 92.626  1.00 65.48  ? 170  GLU   A OE1  1 
ATOM   1318 O  OE2  . GLU   A 1 191 ? 368.465 -19.206 92.858  1.00 57.94  ? 170  GLU   A OE2  1 
ATOM   1319 N  N    . LYS   A 1 192 ? 366.431 -16.963 97.591  1.00 51.26  ? 171  LYS   A N    1 
ATOM   1320 C  CA   . LYS   A 1 192 ? 365.823 -16.744 98.892  1.00 54.47  ? 171  LYS   A CA   1 
ATOM   1321 C  C    . LYS   A 1 192 ? 366.412 -15.497 99.534  1.00 55.06  ? 171  LYS   A C    1 
ATOM   1322 O  O    . LYS   A 1 192 ? 367.557 -15.121 99.272  1.00 53.51  ? 171  LYS   A O    1 
ATOM   1323 C  CB   . LYS   A 1 192 ? 366.033 -17.949 99.831  1.00 53.79  ? 171  LYS   A CB   1 
ATOM   1324 C  CG   . LYS   A 1 192 ? 364.956 -19.025 99.748  1.00 62.70  ? 171  LYS   A CG   1 
ATOM   1325 C  CD   . LYS   A 1 192 ? 365.040 -19.809 98.448  1.00 64.11  ? 171  LYS   A CD   1 
ATOM   1326 C  CE   . LYS   A 1 192 ? 363.832 -20.719 98.265  1.00 69.64  ? 171  LYS   A CE   1 
ATOM   1327 N  NZ   . LYS   A 1 192 ? 363.672 -21.693 99.381  1.00 75.10  ? 171  LYS   A NZ   1 
ATOM   1328 N  N    . VAL   A 1 193 ? 365.604 -14.853 100.369 1.00 55.09  ? 172  VAL   A N    1 
ATOM   1329 C  CA   . VAL   A 1 193 ? 366.059 -13.814 101.282 1.00 51.65  ? 172  VAL   A CA   1 
ATOM   1330 C  C    . VAL   A 1 193 ? 365.626 -14.235 102.675 1.00 58.82  ? 172  VAL   A C    1 
ATOM   1331 O  O    . VAL   A 1 193 ? 364.427 -14.398 102.933 1.00 65.31  ? 172  VAL   A O    1 
ATOM   1332 C  CB   . VAL   A 1 193 ? 365.491 -12.431 100.929 1.00 52.69  ? 172  VAL   A CB   1 
ATOM   1333 C  CG1  . VAL   A 1 193 ? 365.771 -11.447 102.060 1.00 49.45  ? 172  VAL   A CG1  1 
ATOM   1334 C  CG2  . VAL   A 1 193 ? 366.081 -11.929 99.623  1.00 46.75  ? 172  VAL   A CG2  1 
ATOM   1335 N  N    . TYR   A 1 194 ? 366.594 -14.430 103.564 1.00 55.13  ? 173  TYR   A N    1 
ATOM   1336 C  CA   . TYR   A 1 194 ? 366.294 -14.878 104.916 1.00 61.90  ? 173  TYR   A CA   1 
ATOM   1337 C  C    . TYR   A 1 194 ? 366.269 -13.746 105.931 1.00 65.53  ? 173  TYR   A C    1 
ATOM   1338 O  O    . TYR   A 1 194 ? 365.522 -13.826 106.911 1.00 79.94  ? 173  TYR   A O    1 
ATOM   1339 C  CB   . TYR   A 1 194 ? 367.311 -15.937 105.358 1.00 69.26  ? 173  TYR   A CB   1 
ATOM   1340 C  CG   . TYR   A 1 194 ? 367.327 -17.169 104.476 1.00 70.48  ? 173  TYR   A CG   1 
ATOM   1341 C  CD1  . TYR   A 1 194 ? 366.341 -18.141 104.590 1.00 68.95  ? 173  TYR   A CD1  1 
ATOM   1342 C  CD2  . TYR   A 1 194 ? 368.328 -17.361 103.530 1.00 65.88  ? 173  TYR   A CD2  1 
ATOM   1343 C  CE1  . TYR   A 1 194 ? 366.348 -19.268 103.788 1.00 68.39  ? 173  TYR   A CE1  1 
ATOM   1344 C  CE2  . TYR   A 1 194 ? 368.345 -18.488 102.722 1.00 65.26  ? 173  TYR   A CE2  1 
ATOM   1345 C  CZ   . TYR   A 1 194 ? 367.351 -19.438 102.857 1.00 73.37  ? 173  TYR   A CZ   1 
ATOM   1346 O  OH   . TYR   A 1 194 ? 367.356 -20.561 102.061 1.00 74.36  ? 173  TYR   A OH   1 
ATOM   1347 N  N    . SER   A 1 195 ? 367.051 -12.694 105.717 1.00 61.23  ? 174  SER   A N    1 
ATOM   1348 C  CA   . SER   A 1 195 ? 367.136 -11.579 106.647 1.00 62.71  ? 174  SER   A CA   1 
ATOM   1349 C  C    . SER   A 1 195 ? 366.755 -10.290 105.934 1.00 60.31  ? 174  SER   A C    1 
ATOM   1350 O  O    . SER   A 1 195 ? 367.160 -10.061 104.789 1.00 58.06  ? 174  SER   A O    1 
ATOM   1351 C  CB   . SER   A 1 195 ? 368.546 -11.461 107.232 1.00 63.77  ? 174  SER   A CB   1 
ATOM   1352 O  OG   . SER   A 1 195 ? 368.591 -10.491 108.263 1.00 77.80  ? 174  SER   A OG   1 
ATOM   1353 N  N    . LYS   A 1 196 ? 365.970 -9.448  106.611 1.00 53.18  ? 175  LYS   A N    1 
ATOM   1354 C  CA   . LYS   A 1 196 ? 365.611 -8.164  106.022 1.00 59.27  ? 175  LYS   A CA   1 
ATOM   1355 C  C    . LYS   A 1 196 ? 366.812 -7.235  105.910 1.00 56.87  ? 175  LYS   A C    1 
ATOM   1356 O  O    . LYS   A 1 196 ? 366.755 -6.256  105.158 1.00 54.96  ? 175  LYS   A O    1 
ATOM   1357 C  CB   . LYS   A 1 196 ? 364.495 -7.494  106.828 1.00 59.94  ? 175  LYS   A CB   1 
ATOM   1358 C  CG   . LYS   A 1 196 ? 364.952 -6.792  108.097 1.00 57.21  ? 175  LYS   A CG   1 
ATOM   1359 C  CD   . LYS   A 1 196 ? 363.788 -6.062  108.759 1.00 55.78  ? 175  LYS   A CD   1 
ATOM   1360 C  CE   . LYS   A 1 196 ? 364.254 -5.142  109.886 1.00 75.79  ? 175  LYS   A CE   1 
ATOM   1361 N  NZ   . LYS   A 1 196 ? 364.876 -5.865  111.034 1.00 65.51  ? 175  LYS   A NZ   1 
ATOM   1362 N  N    . GLU   A 1 197 ? 367.893 -7.519  106.640 1.00 57.74  ? 176  GLU   A N    1 
ATOM   1363 C  CA   . GLU   A 1 197 ? 369.137 -6.791  106.431 1.00 54.73  ? 176  GLU   A CA   1 
ATOM   1364 C  C    . GLU   A 1 197 ? 369.696 -7.032  105.036 1.00 53.52  ? 176  GLU   A C    1 
ATOM   1365 O  O    . GLU   A 1 197 ? 370.456 -6.200  104.528 1.00 49.07  ? 176  GLU   A O    1 
ATOM   1366 C  CB   . GLU   A 1 197 ? 370.163 -7.194  107.493 1.00 67.52  ? 176  GLU   A CB   1 
ATOM   1367 C  CG   . GLU   A 1 197 ? 371.266 -6.175  107.699 1.00 75.45  ? 176  GLU   A CG   1 
ATOM   1368 C  CD   . GLU   A 1 197 ? 370.723 -4.793  108.008 1.00 85.13  ? 176  GLU   A CD   1 
ATOM   1369 O  OE1  . GLU   A 1 197 ? 369.612 -4.700  108.572 1.00 83.65  ? 176  GLU   A OE1  1 
ATOM   1370 O  OE2  . GLU   A 1 197 ? 371.403 -3.799  107.676 1.00 87.88  ? 176  GLU   A OE2  1 
ATOM   1371 N  N    . ASP   A 1 198 ? 369.330 -8.153  104.408 1.00 52.27  ? 177  ASP   A N    1 
ATOM   1372 C  CA   . ASP   A 1 198 ? 369.748 -8.417  103.037 1.00 48.90  ? 177  ASP   A CA   1 
ATOM   1373 C  C    . ASP   A 1 198 ? 369.205 -7.365  102.081 1.00 48.29  ? 177  ASP   A C    1 
ATOM   1374 O  O    . ASP   A 1 198 ? 369.822 -7.086  101.047 1.00 42.81  ? 177  ASP   A O    1 
ATOM   1375 C  CB   . ASP   A 1 198 ? 369.281 -9.813  102.618 1.00 47.57  ? 177  ASP   A CB   1 
ATOM   1376 C  CG   . ASP   A 1 198 ? 370.056 -10.362 101.437 1.00 48.86  ? 177  ASP   A CG   1 
ATOM   1377 O  OD1  . ASP   A 1 198 ? 371.111 -9.789  101.091 1.00 44.94  ? 177  ASP   A OD1  1 
ATOM   1378 O  OD2  . ASP   A 1 198 ? 369.609 -11.373 100.857 1.00 45.76  ? 177  ASP   A OD2  1 
ATOM   1379 N  N    . LEU   A 1 199 ? 368.055 -6.770  102.410 1.00 44.96  ? 178  LEU   A N    1 
ATOM   1380 C  CA   . LEU   A 1 199 ? 367.439 -5.787  101.526 1.00 39.87  ? 178  LEU   A CA   1 
ATOM   1381 C  C    . LEU   A 1 199 ? 368.273 -4.517  101.419 1.00 40.41  ? 178  LEU   A C    1 
ATOM   1382 O  O    . LEU   A 1 199 ? 368.183 -3.800  100.416 1.00 44.37  ? 178  LEU   A O    1 
ATOM   1383 C  CB   . LEU   A 1 199 ? 366.031 -5.455  102.019 1.00 41.74  ? 178  LEU   A CB   1 
ATOM   1384 C  CG   . LEU   A 1 199 ? 365.087 -6.649  102.179 1.00 49.40  ? 178  LEU   A CG   1 
ATOM   1385 C  CD1  . LEU   A 1 199 ? 363.695 -6.197  102.602 1.00 48.14  ? 178  LEU   A CD1  1 
ATOM   1386 C  CD2  . LEU   A 1 199 ? 365.026 -7.461  100.893 1.00 45.43  ? 178  LEU   A CD2  1 
ATOM   1387 N  N    . LYS   A 1 200 ? 369.079 -4.217  102.438 1.00 47.24  ? 179  LYS   A N    1 
ATOM   1388 C  CA   . LYS   A 1 200 ? 369.930 -3.036  102.382 1.00 43.29  ? 179  LYS   A CA   1 
ATOM   1389 C  C    . LYS   A 1 200 ? 370.948 -3.116  101.251 1.00 46.85  ? 179  LYS   A C    1 
ATOM   1390 O  O    . LYS   A 1 200 ? 371.413 -2.074  100.775 1.00 40.60  ? 179  LYS   A O    1 
ATOM   1391 C  CB   . LYS   A 1 200 ? 370.638 -2.839  103.725 1.00 46.50  ? 179  LYS   A CB   1 
ATOM   1392 N  N    . ASP   A 1 201 ? 371.300 -4.326  100.809 1.00 41.91  ? 180  ASP   A N    1 
ATOM   1393 C  CA   . ASP   A 1 201 ? 372.224 -4.520  99.698  1.00 40.07  ? 180  ASP   A CA   1 
ATOM   1394 C  C    . ASP   A 1 201 ? 371.566 -4.371  98.339  1.00 39.73  ? 180  ASP   A C    1 
ATOM   1395 O  O    . ASP   A 1 201 ? 372.275 -4.248  97.334  1.00 39.88  ? 180  ASP   A O    1 
ATOM   1396 C  CB   . ASP   A 1 201 ? 372.862 -5.907  99.767  1.00 40.76  ? 180  ASP   A CB   1 
ATOM   1397 C  CG   . ASP   A 1 201 ? 373.792 -6.063  100.938 1.00 38.90  ? 180  ASP   A CG   1 
ATOM   1398 O  OD1  . ASP   A 1 201 ? 374.295 -5.036  101.439 1.00 41.79  ? 180  ASP   A OD1  1 
ATOM   1399 O  OD2  . ASP   A 1 201 ? 374.028 -7.218  101.351 1.00 44.39  ? 180  ASP   A OD2  1 
ATOM   1400 N  N    . MET   A 1 202 ? 370.244 -4.395  98.279  1.00 35.19  ? 181  MET   A N    1 
ATOM   1401 C  CA   . MET   A 1 202 ? 369.532 -4.439  97.017  1.00 33.85  ? 181  MET   A CA   1 
ATOM   1402 C  C    . MET   A 1 202 ? 369.071 -3.045  96.612  1.00 33.14  ? 181  MET   A C    1 
ATOM   1403 O  O    . MET   A 1 202 ? 368.972 -2.131  97.433  1.00 39.78  ? 181  MET   A O    1 
ATOM   1404 C  CB   . MET   A 1 202 ? 368.346 -5.397  97.120  1.00 33.95  ? 181  MET   A CB   1 
ATOM   1405 C  CG   . MET   A 1 202 ? 368.771 -6.813  97.477  1.00 30.10  ? 181  MET   A CG   1 
ATOM   1406 S  SD   . MET   A 1 202 ? 367.395 -7.967  97.560  1.00 39.26  ? 181  MET   A SD   1 
ATOM   1407 C  CE   . MET   A 1 202 ? 368.193 -9.376  98.323  1.00 40.05  ? 181  MET   A CE   1 
ATOM   1408 N  N    . SER   A 1 203 ? 368.817 -2.886  95.319  1.00 33.27  ? 182  SER   A N    1 
ATOM   1409 C  CA   . SER   A 1 203 ? 368.285 -1.639  94.795  1.00 37.99  ? 182  SER   A CA   1 
ATOM   1410 C  C    . SER   A 1 203 ? 366.763 -1.691  94.807  1.00 34.52  ? 182  SER   A C    1 
ATOM   1411 O  O    . SER   A 1 203 ? 366.162 -2.732  94.523  1.00 34.01  ? 182  SER   A O    1 
ATOM   1412 C  CB   . SER   A 1 203 ? 368.801 -1.383  93.378  1.00 30.86  ? 182  SER   A CB   1 
ATOM   1413 O  OG   . SER   A 1 203 ? 370.219 -1.354  93.351  1.00 33.39  ? 182  SER   A OG   1 
ATOM   1414 N  N    . GLN   A 1 204 ? 366.142 -0.568  95.151  1.00 39.09  ? 183  GLN   A N    1 
ATOM   1415 C  CA   . GLN   A 1 204 ? 364.691 -0.497  95.212  1.00 36.94  ? 183  GLN   A CA   1 
ATOM   1416 C  C    . GLN   A 1 204 ? 364.109 -0.165  93.847  1.00 36.39  ? 183  GLN   A C    1 
ATOM   1417 O  O    . GLN   A 1 204 ? 364.632 0.680   93.118  1.00 34.51  ? 183  GLN   A O    1 
ATOM   1418 C  CB   . GLN   A 1 204 ? 364.235 0.540   96.237  1.00 36.20  ? 183  GLN   A CB   1 
ATOM   1419 C  CG   . GLN   A 1 204 ? 364.483 0.111   97.662  1.00 41.76  ? 183  GLN   A CG   1 
ATOM   1420 C  CD   . GLN   A 1 204 ? 364.148 1.197   98.655  1.00 48.96  ? 183  GLN   A CD   1 
ATOM   1421 O  OE1  . GLN   A 1 204 ? 363.238 1.997   98.437  1.00 46.52  ? 183  GLN   A OE1  1 
ATOM   1422 N  NE2  . GLN   A 1 204 ? 364.890 1.239   99.752  1.00 52.83  ? 183  GLN   A NE2  1 
ATOM   1423 N  N    . MET   A 1 205 ? 363.023 -0.852  93.510  1.00 37.24  ? 184  MET   A N    1 
ATOM   1424 C  CA   . MET   A 1 205 ? 362.286 -0.643  92.273  1.00 34.19  ? 184  MET   A CA   1 
ATOM   1425 C  C    . MET   A 1 205 ? 360.813 -0.600  92.640  1.00 36.27  ? 184  MET   A C    1 
ATOM   1426 O  O    . MET   A 1 205 ? 360.286 -1.567  93.200  1.00 41.71  ? 184  MET   A O    1 
ATOM   1427 C  CB   . MET   A 1 205 ? 362.575 -1.760  91.268  1.00 31.13  ? 184  MET   A CB   1 
ATOM   1428 C  CG   . MET   A 1 205 ? 361.839 -1.633  89.952  1.00 33.64  ? 184  MET   A CG   1 
ATOM   1429 S  SD   . MET   A 1 205 ? 362.205 -3.021  88.863  1.00 34.90  ? 184  MET   A SD   1 
ATOM   1430 C  CE   . MET   A 1 205 ? 361.525 -4.383  89.807  1.00 33.17  ? 184  MET   A CE   1 
ATOM   1431 N  N    . ILE   A 1 206 ? 360.159 0.520   92.357  1.00 33.97  ? 185  ILE   A N    1 
ATOM   1432 C  CA   . ILE   A 1 206 ? 358.787 0.758   92.789  1.00 34.56  ? 185  ILE   A CA   1 
ATOM   1433 C  C    . ILE   A 1 206 ? 357.887 0.781   91.566  1.00 34.15  ? 185  ILE   A C    1 
ATOM   1434 O  O    . ILE   A 1 206 ? 358.129 1.544   90.623  1.00 37.20  ? 185  ILE   A O    1 
ATOM   1435 C  CB   . ILE   A 1 206 ? 358.664 2.071   93.579  1.00 35.83  ? 185  ILE   A CB   1 
ATOM   1436 C  CG1  . ILE   A 1 206 ? 359.679 2.098   94.723  1.00 39.66  ? 185  ILE   A CG1  1 
ATOM   1437 C  CG2  . ILE   A 1 206 ? 357.246 2.238   94.108  1.00 41.26  ? 185  ILE   A CG2  1 
ATOM   1438 C  CD1  . ILE   A 1 206 ? 359.616 3.348   95.566  1.00 39.04  ? 185  ILE   A CD1  1 
ATOM   1439 N  N    . LEU   A 1 207 ? 356.852 -0.053  91.579  1.00 39.23  ? 186  LEU   A N    1 
ATOM   1440 C  CA   . LEU   A 1 207 ? 355.797 0.011   90.575  1.00 39.17  ? 186  LEU   A CA   1 
ATOM   1441 C  C    . LEU   A 1 207 ? 354.731 0.973   91.084  1.00 33.72  ? 186  LEU   A C    1 
ATOM   1442 O  O    . LEU   A 1 207 ? 353.983 0.650   92.012  1.00 36.29  ? 186  LEU   A O    1 
ATOM   1443 C  CB   . LEU   A 1 207 ? 355.212 -1.371  90.299  1.00 36.52  ? 186  LEU   A CB   1 
ATOM   1444 C  CG   . LEU   A 1 207 ? 354.096 -1.400  89.252  1.00 33.51  ? 186  LEU   A CG   1 
ATOM   1445 C  CD1  . LEU   A 1 207 ? 354.594 -0.841  87.928  1.00 28.70  ? 186  LEU   A CD1  1 
ATOM   1446 C  CD2  . LEU   A 1 207 ? 353.565 -2.812  89.075  1.00 33.82  ? 186  LEU   A CD2  1 
ATOM   1447 N  N    . ARG   A 1 208 ? 354.679 2.163   90.495  1.00 33.55  ? 187  ARG   A N    1 
ATOM   1448 C  CA   . ARG   A 1 208 ? 353.724 3.187   90.889  1.00 36.41  ? 187  ARG   A CA   1 
ATOM   1449 C  C    . ARG   A 1 208 ? 352.552 3.181   89.919  1.00 38.70  ? 187  ARG   A C    1 
ATOM   1450 O  O    . ARG   A 1 208 ? 352.748 3.217   88.700  1.00 36.50  ? 187  ARG   A O    1 
ATOM   1451 C  CB   . ARG   A 1 208 ? 354.382 4.566   90.924  1.00 38.14  ? 187  ARG   A CB   1 
ATOM   1452 C  CG   . ARG   A 1 208 ? 355.516 4.684   91.926  1.00 37.45  ? 187  ARG   A CG   1 
ATOM   1453 C  CD   . ARG   A 1 208 ? 355.842 6.139   92.196  1.00 42.41  ? 187  ARG   A CD   1 
ATOM   1454 N  NE   . ARG   A 1 208 ? 356.703 6.301   93.361  1.00 43.31  ? 187  ARG   A NE   1 
ATOM   1455 C  CZ   . ARG   A 1 208 ? 358.020 6.442   93.305  1.00 45.78  ? 187  ARG   A CZ   1 
ATOM   1456 N  NH1  . ARG   A 1 208 ? 358.666 6.448   92.151  1.00 38.12  ? 187  ARG   A NH1  1 
ATOM   1457 N  NH2  . ARG   A 1 208 ? 358.706 6.585   94.436  1.00 47.10  ? 187  ARG   A NH2  1 
ATOM   1458 N  N    . THR   A 1 209 ? 351.341 3.127   90.464  1.00 38.13  ? 188  THR   A N    1 
ATOM   1459 C  CA   . THR   A 1 209 ? 350.139 3.074   89.650  1.00 38.66  ? 188  THR   A CA   1 
ATOM   1460 C  C    . THR   A 1 209 ? 349.059 3.940   90.275  1.00 41.41  ? 188  THR   A C    1 
ATOM   1461 O  O    . THR   A 1 209 ? 349.039 4.166   91.488  1.00 40.35  ? 188  THR   A O    1 
ATOM   1462 C  CB   . THR   A 1 209 ? 349.607 1.639   89.486  1.00 40.90  ? 188  THR   A CB   1 
ATOM   1463 O  OG1  . THR   A 1 209 ? 349.134 1.152   90.749  1.00 45.26  ? 188  THR   A OG1  1 
ATOM   1464 C  CG2  . THR   A 1 209 ? 350.700 0.717   88.969  1.00 41.35  ? 188  THR   A CG2  1 
ATOM   1465 N  N    A LYS   A 1 210 ? 348.166 4.435   89.425  0.50 42.26  ? 189  LYS   A N    1 
ATOM   1466 N  N    B LYS   A 1 210 ? 348.157 4.424   89.427  0.50 42.26  ? 189  LYS   A N    1 
ATOM   1467 C  CA   A LYS   A 1 210 ? 346.991 5.171   89.861  0.50 41.94  ? 189  LYS   A CA   1 
ATOM   1468 C  CA   B LYS   A 1 210 ? 346.991 5.172   89.873  0.50 41.85  ? 189  LYS   A CA   1 
ATOM   1469 C  C    A LYS   A 1 210 ? 345.850 4.811   88.926  0.50 40.93  ? 189  LYS   A C    1 
ATOM   1470 C  C    B LYS   A 1 210 ? 345.843 4.847   88.931  0.50 40.88  ? 189  LYS   A C    1 
ATOM   1471 O  O    A LYS   A 1 210 ? 346.026 4.810   87.704  0.50 40.92  ? 189  LYS   A O    1 
ATOM   1472 O  O    B LYS   A 1 210 ? 346.008 4.910   87.709  0.50 39.98  ? 189  LYS   A O    1 
ATOM   1473 C  CB   A LYS   A 1 210 ? 347.238 6.684   89.860  0.50 42.47  ? 189  LYS   A CB   1 
ATOM   1474 C  CB   B LYS   A 1 210 ? 347.265 6.679   89.898  0.50 42.50  ? 189  LYS   A CB   1 
ATOM   1475 N  N    . GLY   A 1 211 ? 344.696 4.485   89.499  1.00 41.86  ? 190  GLY   A N    1 
ATOM   1476 C  CA   . GLY   A 1 211 ? 343.546 4.107   88.716  1.00 41.93  ? 190  GLY   A CA   1 
ATOM   1477 C  C    . GLY   A 1 211 ? 342.388 3.661   89.583  1.00 44.06  ? 190  GLY   A C    1 
ATOM   1478 O  O    . GLY   A 1 211 ? 342.408 3.799   90.810  1.00 43.15  ? 190  GLY   A O    1 
ATOM   1479 N  N    . PRO   A 1 212 ? 341.357 3.109   88.958  1.00 47.58  ? 191  PRO   A N    1 
ATOM   1480 C  CA   . PRO   A 1 212 ? 340.148 2.722   89.690  1.00 51.48  ? 191  PRO   A CA   1 
ATOM   1481 C  C    . PRO   A 1 212 ? 340.377 1.442   90.490  1.00 45.39  ? 191  PRO   A C    1 
ATOM   1482 O  O    . PRO   A 1 212 ? 341.471 0.880   90.519  1.00 42.86  ? 191  PRO   A O    1 
ATOM   1483 C  CB   . PRO   A 1 212 ? 339.116 2.526   88.576  1.00 48.58  ? 191  PRO   A CB   1 
ATOM   1484 C  CG   . PRO   A 1 212 ? 339.924 2.138   87.384  1.00 46.54  ? 191  PRO   A CG   1 
ATOM   1485 C  CD   . PRO   A 1 212 ? 341.252 2.834   87.514  1.00 42.78  ? 191  PRO   A CD   1 
ATOM   1486 N  N    . ASP   A 1 213 ? 339.308 0.988   91.152  1.00 48.94  ? 192  ASP   A N    1 
ATOM   1487 C  CA   . ASP   A 1 213 ? 339.419 -0.157  92.052  1.00 54.80  ? 192  ASP   A CA   1 
ATOM   1488 C  C    . ASP   A 1 213 ? 339.975 -1.381  91.339  1.00 53.65  ? 192  ASP   A C    1 
ATOM   1489 O  O    . ASP   A 1 213 ? 340.719 -2.171  91.932  1.00 56.82  ? 192  ASP   A O    1 
ATOM   1490 C  CB   . ASP   A 1 213 ? 338.057 -0.479  92.663  1.00 57.57  ? 192  ASP   A CB   1 
ATOM   1491 C  CG   . ASP   A 1 213 ? 337.536 0.636   93.539  1.00 73.75  ? 192  ASP   A CG   1 
ATOM   1492 O  OD1  . ASP   A 1 213 ? 338.366 1.394   94.087  1.00 73.56  ? 192  ASP   A OD1  1 
ATOM   1493 O  OD2  . ASP   A 1 213 ? 336.301 0.753   93.685  1.00 82.29  ? 192  ASP   A OD2  1 
ATOM   1494 N  N    . ARG   A 1 214 ? 339.619 -1.563  90.072  1.00 52.65  ? 193  ARG   A N    1 
ATOM   1495 C  CA   . ARG   A 1 214 ? 340.032 -2.734  89.320  1.00 54.80  ? 193  ARG   A CA   1 
ATOM   1496 C  C    . ARG   A 1 214 ? 340.427 -2.307  87.917  1.00 50.32  ? 193  ARG   A C    1 
ATOM   1497 O  O    . ARG   A 1 214 ? 339.994 -1.268  87.411  1.00 45.22  ? 193  ARG   A O    1 
ATOM   1498 C  CB   . ARG   A 1 214 ? 338.916 -3.784  89.253  1.00 56.54  ? 193  ARG   A CB   1 
ATOM   1499 C  CG   . ARG   A 1 214 ? 338.263 -4.065  90.593  1.00 66.80  ? 193  ARG   A CG   1 
ATOM   1500 C  CD   . ARG   A 1 214 ? 336.956 -4.826  90.444  1.00 74.15  ? 193  ARG   A CD   1 
ATOM   1501 N  NE   . ARG   A 1 214 ? 336.009 -4.451  91.488  1.00 78.40  ? 193  ARG   A NE   1 
ATOM   1502 C  CZ   . ARG   A 1 214 ? 336.083 -4.855  92.749  1.00 82.08  ? 193  ARG   A CZ   1 
ATOM   1503 N  NH1  . ARG   A 1 214 ? 337.046 -5.663  93.161  1.00 81.18  ? 193  ARG   A NH1  1 
ATOM   1504 N  NH2  . ARG   A 1 214 ? 335.170 -4.432  93.620  1.00 90.66  ? 193  ARG   A NH2  1 
ATOM   1505 N  N    . LEU   A 1 215 ? 341.270 -3.121  87.297  1.00 49.03  ? 194  LEU   A N    1 
ATOM   1506 C  CA   . LEU   A 1 215 ? 341.469 -3.003  85.866  1.00 45.21  ? 194  LEU   A CA   1 
ATOM   1507 C  C    . LEU   A 1 215 ? 340.221 -3.507  85.147  1.00 49.08  ? 194  LEU   A C    1 
ATOM   1508 O  O    . LEU   A 1 215 ? 339.578 -4.454  85.613  1.00 49.21  ? 194  LEU   A O    1 
ATOM   1509 C  CB   . LEU   A 1 215 ? 342.687 -3.808  85.424  1.00 42.92  ? 194  LEU   A CB   1 
ATOM   1510 C  CG   . LEU   A 1 215 ? 344.041 -3.336  85.944  1.00 45.41  ? 194  LEU   A CG   1 
ATOM   1511 C  CD1  . LEU   A 1 215 ? 345.112 -4.356  85.609  1.00 42.53  ? 194  LEU   A CD1  1 
ATOM   1512 C  CD2  . LEU   A 1 215 ? 344.381 -1.980  85.352  1.00 39.37  ? 194  LEU   A CD2  1 
ATOM   1513 N  N    . PRO   A 1 216 ? 339.844 -2.897  84.025  1.00 46.65  ? 195  PRO   A N    1 
ATOM   1514 C  CA   . PRO   A 1 216 ? 338.722 -3.435  83.251  1.00 44.98  ? 195  PRO   A CA   1 
ATOM   1515 C  C    . PRO   A 1 216 ? 338.976 -4.892  82.896  1.00 46.78  ? 195  PRO   A C    1 
ATOM   1516 O  O    . PRO   A 1 216 ? 340.112 -5.369  82.901  1.00 45.07  ? 195  PRO   A O    1 
ATOM   1517 C  CB   . PRO   A 1 216 ? 338.687 -2.548  81.999  1.00 47.33  ? 195  PRO   A CB   1 
ATOM   1518 C  CG   . PRO   A 1 216 ? 339.423 -1.302  82.389  1.00 46.08  ? 195  PRO   A CG   1 
ATOM   1519 C  CD   . PRO   A 1 216 ? 340.468 -1.735  83.371  1.00 44.08  ? 195  PRO   A CD   1 
ATOM   1520 N  N    . ALA   A 1 217 ? 337.894 -5.607  82.596  1.00 44.22  ? 196  ALA   A N    1 
ATOM   1521 C  CA   . ALA   A 1 217 ? 338.020 -7.000  82.197  1.00 39.41  ? 196  ALA   A CA   1 
ATOM   1522 C  C    . ALA   A 1 217 ? 338.994 -7.136  81.034  1.00 47.05  ? 196  ALA   A C    1 
ATOM   1523 O  O    . ALA   A 1 217 ? 338.984 -6.335  80.096  1.00 42.14  ? 196  ALA   A O    1 
ATOM   1524 C  CB   . ALA   A 1 217 ? 336.652 -7.568  81.810  1.00 43.15  ? 196  ALA   A CB   1 
ATOM   1525 N  N    . GLY   A 1 218 ? 339.854 -8.149  81.112  1.00 39.64  ? 197  GLY   A N    1 
ATOM   1526 C  CA   . GLY   A 1 218 ? 340.748 -8.475  80.021  1.00 36.35  ? 197  GLY   A CA   1 
ATOM   1527 C  C    . GLY   A 1 218 ? 342.117 -7.836  80.068  1.00 42.03  ? 197  GLY   A C    1 
ATOM   1528 O  O    . GLY   A 1 218 ? 342.837 -7.887  79.062  1.00 45.39  ? 197  GLY   A O    1 
ATOM   1529 N  N    . TYR   A 1 219 ? 342.507 -7.239  81.191  1.00 40.71  ? 198  TYR   A N    1 
ATOM   1530 C  CA   . TYR   A 1 219 ? 343.822 -6.631  81.321  1.00 37.29  ? 198  TYR   A CA   1 
ATOM   1531 C  C    . TYR   A 1 219 ? 344.537 -7.193  82.540  1.00 38.26  ? 198  TYR   A C    1 
ATOM   1532 O  O    . TYR   A 1 219 ? 343.907 -7.606  83.517  1.00 39.49  ? 198  TYR   A O    1 
ATOM   1533 C  CB   . TYR   A 1 219 ? 343.735 -5.103  81.436  1.00 38.60  ? 198  TYR   A CB   1 
ATOM   1534 C  CG   . TYR   A 1 219 ? 343.198 -4.411  80.203  1.00 38.40  ? 198  TYR   A CG   1 
ATOM   1535 C  CD1  . TYR   A 1 219 ? 344.043 -4.040  79.163  1.00 38.69  ? 198  TYR   A CD1  1 
ATOM   1536 C  CD2  . TYR   A 1 219 ? 341.846 -4.120  80.083  1.00 38.52  ? 198  TYR   A CD2  1 
ATOM   1537 C  CE1  . TYR   A 1 219 ? 343.551 -3.402  78.034  1.00 38.98  ? 198  TYR   A CE1  1 
ATOM   1538 C  CE2  . TYR   A 1 219 ? 341.348 -3.485  78.962  1.00 44.06  ? 198  TYR   A CE2  1 
ATOM   1539 C  CZ   . TYR   A 1 219 ? 342.201 -3.128  77.941  1.00 42.56  ? 198  TYR   A CZ   1 
ATOM   1540 O  OH   . TYR   A 1 219 ? 341.691 -2.496  76.829  1.00 45.89  ? 198  TYR   A OH   1 
ATOM   1541 N  N    . GLU   A 1 220 ? 345.866 -7.206  82.469  1.00 40.08  ? 199  GLU   A N    1 
ATOM   1542 C  CA   . GLU   A 1 220 ? 346.692 -7.549  83.615  1.00 40.66  ? 199  GLU   A CA   1 
ATOM   1543 C  C    . GLU   A 1 220 ? 348.052 -6.888  83.450  1.00 34.23  ? 199  GLU   A C    1 
ATOM   1544 O  O    . GLU   A 1 220 ? 348.498 -6.621  82.331  1.00 36.91  ? 199  GLU   A O    1 
ATOM   1545 C  CB   . GLU   A 1 220 ? 346.852 -9.065  83.776  1.00 43.33  ? 199  GLU   A CB   1 
ATOM   1546 C  CG   . GLU   A 1 220 ? 347.745 -9.728  82.742  1.00 45.62  ? 199  GLU   A CG   1 
ATOM   1547 C  CD   . GLU   A 1 220 ? 347.865 -11.221 82.971  1.00 50.17  ? 199  GLU   A CD   1 
ATOM   1548 O  OE1  . GLU   A 1 220 ? 347.248 -11.716 83.937  1.00 44.99  ? 199  GLU   A OE1  1 
ATOM   1549 O  OE2  . GLU   A 1 220 ? 348.570 -11.898 82.192  1.00 61.22  ? 199  GLU   A OE2  1 
ATOM   1550 N  N    . ILE   A 1 221 ? 348.707 -6.622  84.578  1.00 39.28  ? 200  ILE   A N    1 
ATOM   1551 C  CA   . ILE   A 1 221 ? 350.025 -5.997  84.604  1.00 36.86  ? 200  ILE   A CA   1 
ATOM   1552 C  C    . ILE   A 1 221 ? 351.055 -7.066  84.938  1.00 34.79  ? 200  ILE   A C    1 
ATOM   1553 O  O    . ILE   A 1 221 ? 350.886 -7.819  85.905  1.00 37.15  ? 200  ILE   A O    1 
ATOM   1554 C  CB   . ILE   A 1 221 ? 350.082 -4.840  85.615  1.00 33.30  ? 200  ILE   A CB   1 
ATOM   1555 C  CG1  . ILE   A 1 221 ? 349.102 -3.739  85.206  1.00 35.49  ? 200  ILE   A CG1  1 
ATOM   1556 C  CG2  . ILE   A 1 221 ? 351.493 -4.292  85.709  1.00 31.14  ? 200  ILE   A CG2  1 
ATOM   1557 C  CD1  . ILE   A 1 221 ? 348.936 -2.644  86.235  1.00 37.17  ? 200  ILE   A CD1  1 
ATOM   1558 N  N    . VAL   A 1 222 ? 352.124 -7.127  84.145  1.00 36.83  ? 201  VAL   A N    1 
ATOM   1559 C  CA   . VAL   A 1 222 ? 353.120 -8.188  84.249  1.00 38.79  ? 201  VAL   A CA   1 
ATOM   1560 C  C    . VAL   A 1 222 ? 354.510 -7.571  84.299  1.00 34.72  ? 201  VAL   A C    1 
ATOM   1561 O  O    . VAL   A 1 222 ? 354.851 -6.723  83.466  1.00 35.54  ? 201  VAL   A O    1 
ATOM   1562 C  CB   . VAL   A 1 222 ? 353.018 -9.184  83.077  1.00 33.11  ? 201  VAL   A CB   1 
ATOM   1563 C  CG1  . VAL   A 1 222 ? 354.065 -10.277 83.215  1.00 35.93  ? 201  VAL   A CG1  1 
ATOM   1564 C  CG2  . VAL   A 1 222 ? 351.628 -9.786  83.017  1.00 32.89  ? 201  VAL   A CG2  1 
ATOM   1565 N  N    . LEU   A 1 223 ? 355.306 -7.993  85.278  1.00 36.61  ? 202  LEU   A N    1 
ATOM   1566 C  CA   . LEU   A 1 223 ? 356.733 -7.705  85.311  1.00 32.22  ? 202  LEU   A CA   1 
ATOM   1567 C  C    . LEU   A 1 223 ? 357.481 -8.856  84.656  1.00 32.67  ? 202  LEU   A C    1 
ATOM   1568 O  O    . LEU   A 1 223 ? 357.141 -10.023 84.865  1.00 37.99  ? 202  LEU   A O    1 
ATOM   1569 C  CB   . LEU   A 1 223 ? 357.220 -7.525  86.750  1.00 35.79  ? 202  LEU   A CB   1 
ATOM   1570 C  CG   . LEU   A 1 223 ? 356.797 -6.278  87.526  1.00 38.84  ? 202  LEU   A CG   1 
ATOM   1571 C  CD1  . LEU   A 1 223 ? 356.944 -6.516  89.020  1.00 40.04  ? 202  LEU   A CD1  1 
ATOM   1572 C  CD2  . LEU   A 1 223 ? 357.625 -5.077  87.096  1.00 32.80  ? 202  LEU   A CD2  1 
ATOM   1573 N  N    . TYR   A 1 224 ? 358.499 -8.537  83.864  1.00 27.65  ? 203  TYR   A N    1 
ATOM   1574 C  CA   . TYR   A 1 224 ? 359.226 -9.618  83.217  1.00 31.42  ? 203  TYR   A CA   1 
ATOM   1575 C  C    . TYR   A 1 224 ? 360.658 -9.205  82.908  1.00 30.15  ? 203  TYR   A C    1 
ATOM   1576 O  O    . TYR   A 1 224 ? 361.005 -8.021  82.887  1.00 29.73  ? 203  TYR   A O    1 
ATOM   1577 C  CB   . TYR   A 1 224 ? 358.502 -10.092 81.948  1.00 33.38  ? 203  TYR   A CB   1 
ATOM   1578 C  CG   . TYR   A 1 224 ? 358.463 -9.089  80.819  1.00 30.98  ? 203  TYR   A CG   1 
ATOM   1579 C  CD1  . TYR   A 1 224 ? 357.471 -8.117  80.749  1.00 31.08  ? 203  TYR   A CD1  1 
ATOM   1580 C  CD2  . TYR   A 1 224 ? 359.409 -9.131  79.806  1.00 33.36  ? 203  TYR   A CD2  1 
ATOM   1581 C  CE1  . TYR   A 1 224 ? 357.436 -7.206  79.701  1.00 32.25  ? 203  TYR   A CE1  1 
ATOM   1582 C  CE2  . TYR   A 1 224 ? 359.382 -8.230  78.763  1.00 38.27  ? 203  TYR   A CE2  1 
ATOM   1583 C  CZ   . TYR   A 1 224 ? 358.398 -7.270  78.711  1.00 37.09  ? 203  TYR   A CZ   1 
ATOM   1584 O  OH   . TYR   A 1 224 ? 358.391 -6.381  77.660  1.00 40.95  ? 203  TYR   A OH   1 
ATOM   1585 N  N    . ILE   A 1 225 ? 361.490 -10.223 82.687  1.00 33.27  ? 204  ILE   A N    1 
ATOM   1586 C  CA   . ILE   A 1 225 ? 362.884 -10.085 82.295  1.00 30.60  ? 204  ILE   A CA   1 
ATOM   1587 C  C    . ILE   A 1 225 ? 363.145 -11.063 81.159  1.00 32.85  ? 204  ILE   A C    1 
ATOM   1588 O  O    . ILE   A 1 225 ? 362.386 -12.007 80.936  1.00 31.32  ? 204  ILE   A O    1 
ATOM   1589 C  CB   . ILE   A 1 225 ? 363.854 -10.367 83.461  1.00 25.39  ? 204  ILE   A CB   1 
ATOM   1590 C  CG1  . ILE   A 1 225 ? 363.628 -11.785 83.988  1.00 30.42  ? 204  ILE   A CG1  1 
ATOM   1591 C  CG2  . ILE   A 1 225 ? 363.667 -9.363  84.573  1.00 31.82  ? 204  ILE   A CG2  1 
ATOM   1592 C  CD1  . ILE   A 1 225 ? 364.594 -12.196 85.073  1.00 29.80  ? 204  ILE   A CD1  1 
ATOM   1593 N  N    . SER   A 1 226 ? 364.244 -10.835 80.448  1.00 30.69  ? 205  SER   A N    1 
ATOM   1594 C  CA   . SER   A 1 226 ? 364.663 -11.786 79.432  1.00 31.16  ? 205  SER   A CA   1 
ATOM   1595 C  C    . SER   A 1 226 ? 365.249 -13.031 80.088  1.00 33.31  ? 205  SER   A C    1 
ATOM   1596 O  O    . SER   A 1 226 ? 365.714 -13.006 81.230  1.00 38.51  ? 205  SER   A O    1 
ATOM   1597 C  CB   . SER   A 1 226 ? 365.702 -11.166 78.501  1.00 30.77  ? 205  SER   A CB   1 
ATOM   1598 O  OG   . SER   A 1 226 ? 366.941 -11.006 79.171  1.00 34.03  ? 205  SER   A OG   1 
ATOM   1599 N  N    . MET   A 1 227 ? 365.225 -14.138 79.343  1.00 34.92  ? 206  MET   A N    1 
ATOM   1600 C  CA   . MET   A 1 227 ? 365.907 -15.342 79.805  1.00 37.19  ? 206  MET   A CA   1 
ATOM   1601 C  C    . MET   A 1 227 ? 367.382 -15.064 80.069  1.00 38.40  ? 206  MET   A C    1 
ATOM   1602 O  O    . MET   A 1 227 ? 367.956 -15.572 81.040  1.00 36.25  ? 206  MET   A O    1 
ATOM   1603 C  CB   . MET   A 1 227 ? 365.740 -16.460 78.775  1.00 35.43  ? 206  MET   A CB   1 
ATOM   1604 C  CG   . MET   A 1 227 ? 366.500 -17.743 79.087  1.00 38.54  ? 206  MET   A CG   1 
ATOM   1605 S  SD   . MET   A 1 227 ? 365.734 -18.731 80.387  1.00 55.18  ? 206  MET   A SD   1 
ATOM   1606 C  CE   . MET   A 1 227 ? 366.919 -20.064 80.562  1.00 54.89  ? 206  MET   A CE   1 
ATOM   1607 N  N    . SER   A 1 228 ? 368.008 -14.242 79.223  1.00 39.57  ? 207  SER   A N    1 
ATOM   1608 C  CA   . SER   A 1 228 ? 369.431 -13.959 79.382  1.00 39.12  ? 207  SER   A CA   1 
ATOM   1609 C  C    . SER   A 1 228 ? 369.721 -13.306 80.726  1.00 35.03  ? 207  SER   A C    1 
ATOM   1610 O  O    . SER   A 1 228 ? 370.687 -13.670 81.407  1.00 36.57  ? 207  SER   A O    1 
ATOM   1611 C  CB   . SER   A 1 228 ? 369.921 -13.066 78.242  1.00 39.34  ? 207  SER   A CB   1 
ATOM   1612 O  OG   . SER   A 1 228 ? 371.289 -12.739 78.414  1.00 48.84  ? 207  SER   A OG   1 
ATOM   1613 N  N    . ASP   A 1 229 ? 368.900 -12.335 81.123  1.00 36.41  ? 208  ASP   A N    1 
ATOM   1614 C  CA   . ASP   A 1 229 ? 369.085 -11.639 82.389  1.00 35.98  ? 208  ASP   A CA   1 
ATOM   1615 C  C    . ASP   A 1 229 ? 368.642 -12.461 83.592  1.00 32.10  ? 208  ASP   A C    1 
ATOM   1616 O  O    . ASP   A 1 229 ? 368.790 -11.992 84.726  1.00 34.12  ? 208  ASP   A O    1 
ATOM   1617 C  CB   . ASP   A 1 229 ? 368.324 -10.308 82.378  1.00 27.40  ? 208  ASP   A CB   1 
ATOM   1618 C  CG   . ASP   A 1 229 ? 368.995 -9.256  81.519  1.00 39.84  ? 208  ASP   A CG   1 
ATOM   1619 O  OD1  . ASP   A 1 229 ? 370.212 -9.380  81.265  1.00 44.54  ? 208  ASP   A OD1  1 
ATOM   1620 O  OD2  . ASP   A 1 229 ? 368.306 -8.299  81.103  1.00 36.96  ? 208  ASP   A OD2  1 
ATOM   1621 N  N    . SER   A 1 230 ? 368.119 -13.672 83.382  1.00 31.75  ? 209  SER   A N    1 
ATOM   1622 C  CA   . SER   A 1 230 ? 367.524 -14.421 84.483  1.00 37.06  ? 209  SER   A CA   1 
ATOM   1623 C  C    . SER   A 1 230 ? 368.561 -14.949 85.469  1.00 39.64  ? 209  SER   A C    1 
ATOM   1624 O  O    . SER   A 1 230 ? 368.205 -15.260 86.610  1.00 41.17  ? 209  SER   A O    1 
ATOM   1625 C  CB   . SER   A 1 230 ? 366.664 -15.569 83.941  1.00 36.11  ? 209  SER   A CB   1 
ATOM   1626 O  OG   . SER   A 1 230 ? 367.438 -16.551 83.273  1.00 41.71  ? 209  SER   A OG   1 
ATOM   1627 N  N    . ASP   A 1 231 ? 369.827 -15.054 85.073  1.00 36.13  ? 210  ASP   A N    1 
ATOM   1628 C  CA   . ASP   A 1 231 ? 370.890 -15.395 86.008  1.00 36.83  ? 210  ASP   A CA   1 
ATOM   1629 C  C    . ASP   A 1 231 ? 371.715 -14.180 86.408  1.00 35.86  ? 210  ASP   A C    1 
ATOM   1630 O  O    . ASP   A 1 231 ? 372.793 -14.336 86.992  1.00 31.45  ? 210  ASP   A O    1 
ATOM   1631 C  CB   . ASP   A 1 231 ? 371.790 -16.485 85.420  1.00 39.83  ? 210  ASP   A CB   1 
ATOM   1632 C  CG   . ASP   A 1 231 ? 372.375 -16.099 84.080  1.00 45.14  ? 210  ASP   A CG   1 
ATOM   1633 O  OD1  . ASP   A 1 231 ? 372.183 -14.941 83.656  1.00 45.70  ? 210  ASP   A OD1  1 
ATOM   1634 O  OD2  . ASP   A 1 231 ? 373.023 -16.957 83.445  1.00 55.93  ? 210  ASP   A OD2  1 
ATOM   1635 N  N    . LYS   A 1 232 ? 371.224 -12.978 86.107  1.00 32.40  ? 211  LYS   A N    1 
ATOM   1636 C  CA   . LYS   A 1 232 ? 371.897 -11.723 86.416  1.00 30.32  ? 211  LYS   A CA   1 
ATOM   1637 C  C    . LYS   A 1 232 ? 371.244 -10.940 87.543  1.00 35.73  ? 211  LYS   A C    1 
ATOM   1638 O  O    . LYS   A 1 232 ? 371.924 -10.145 88.198  1.00 31.63  ? 211  LYS   A O    1 
ATOM   1639 C  CB   . LYS   A 1 232 ? 371.948 -10.826 85.171  1.00 30.53  ? 211  LYS   A CB   1 
ATOM   1640 C  CG   . LYS   A 1 232 ? 372.487 -11.492 83.914  1.00 28.66  ? 211  LYS   A CG   1 
ATOM   1641 C  CD   . LYS   A 1 232 ? 373.887 -12.047 84.125  1.00 31.51  ? 211  LYS   A CD   1 
ATOM   1642 C  CE   . LYS   A 1 232 ? 374.556 -12.376 82.798  1.00 33.86  ? 211  LYS   A CE   1 
ATOM   1643 N  NZ   . LYS   A 1 232 ? 373.684 -13.198 81.913  1.00 39.28  ? 211  LYS   A NZ   1 
ATOM   1644 N  N    . VAL   A 1 233 ? 369.946 -11.135 87.780  1.00 34.75  ? 212  VAL   A N    1 
ATOM   1645 C  CA   . VAL   A 1 233 ? 369.211 -10.369 88.778  1.00 34.38  ? 212  VAL   A CA   1 
ATOM   1646 C  C    . VAL   A 1 233 ? 368.322 -11.294 89.594  1.00 36.49  ? 212  VAL   A C    1 
ATOM   1647 O  O    . VAL   A 1 233 ? 367.929 -12.372 89.140  1.00 37.54  ? 212  VAL   A O    1 
ATOM   1648 C  CB   . VAL   A 1 233 ? 368.340 -9.261  88.140  1.00 33.97  ? 212  VAL   A CB   1 
ATOM   1649 C  CG1  . VAL   A 1 233 ? 369.187 -8.328  87.295  1.00 31.28  ? 212  VAL   A CG1  1 
ATOM   1650 C  CG2  . VAL   A 1 233 ? 367.221 -9.875  87.315  1.00 36.01  ? 212  VAL   A CG2  1 
ATOM   1651 N  N    . GLY   A 1 234 ? 368.025 -10.862 90.808  1.00 36.12  ? 213  GLY   A N    1 
ATOM   1652 C  CA   . GLY   A 1 234 ? 366.913 -11.411 91.566  1.00 33.99  ? 213  GLY   A CA   1 
ATOM   1653 C  C    . GLY   A 1 234 ? 366.024 -10.270 92.007  1.00 38.15  ? 213  GLY   A C    1 
ATOM   1654 O  O    . GLY   A 1 234 ? 366.508 -9.202  92.384  1.00 37.69  ? 213  GLY   A O    1 
ATOM   1655 N  N    . VAL   A 1 235 ? 364.715 -10.494 91.936  1.00 33.93  ? 214  VAL   A N    1 
ATOM   1656 C  CA   . VAL   A 1 235 ? 363.727 -9.479  92.287  1.00 35.73  ? 214  VAL   A CA   1 
ATOM   1657 C  C    . VAL   A 1 235 ? 362.820 -10.047 93.367  1.00 39.00  ? 214  VAL   A C    1 
ATOM   1658 O  O    . VAL   A 1 235 ? 362.226 -11.117 93.189  1.00 38.79  ? 214  VAL   A O    1 
ATOM   1659 C  CB   . VAL   A 1 235 ? 362.910 -9.024  91.063  1.00 35.82  ? 214  VAL   A CB   1 
ATOM   1660 C  CG1  . VAL   A 1 235 ? 361.837 -8.034  91.480  1.00 32.17  ? 214  VAL   A CG1  1 
ATOM   1661 C  CG2  . VAL   A 1 235 ? 363.824 -8.391  90.032  1.00 31.76  ? 214  VAL   A CG2  1 
ATOM   1662 N  N    . PHE   A 1 236 ? 362.710 -9.327  94.481  1.00 42.08  ? 215  PHE   A N    1 
ATOM   1663 C  CA   . PHE   A 1 236 ? 361.962 -9.788  95.637  1.00 43.58  ? 215  PHE   A CA   1 
ATOM   1664 C  C    . PHE   A 1 236 ? 360.901 -8.772  96.039  1.00 40.46  ? 215  PHE   A C    1 
ATOM   1665 O  O    . PHE   A 1 236 ? 361.008 -7.573  95.764  1.00 42.19  ? 215  PHE   A O    1 
ATOM   1666 C  CB   . PHE   A 1 236 ? 362.891 -10.059 96.825  1.00 40.91  ? 215  PHE   A CB   1 
ATOM   1667 C  CG   . PHE   A 1 236 ? 363.811 -11.222 96.616  1.00 44.87  ? 215  PHE   A CG   1 
ATOM   1668 C  CD1  . PHE   A 1 236 ? 365.017 -11.057 95.955  1.00 42.85  ? 215  PHE   A CD1  1 
ATOM   1669 C  CD2  . PHE   A 1 236 ? 363.470 -12.482 97.077  1.00 46.78  ? 215  PHE   A CD2  1 
ATOM   1670 C  CE1  . PHE   A 1 236 ? 365.868 -12.128 95.760  1.00 47.82  ? 215  PHE   A CE1  1 
ATOM   1671 C  CE2  . PHE   A 1 236 ? 364.315 -13.558 96.887  1.00 48.91  ? 215  PHE   A CE2  1 
ATOM   1672 C  CZ   . PHE   A 1 236 ? 365.517 -13.381 96.226  1.00 47.54  ? 215  PHE   A CZ   1 
ATOM   1673 N  N    . TYR   A 1 237 ? 359.877 -9.284  96.712  1.00 47.05  ? 216  TYR   A N    1 
ATOM   1674 C  CA   . TYR   A 1 237 ? 358.767 -8.505  97.235  1.00 49.54  ? 216  TYR   A CA   1 
ATOM   1675 C  C    . TYR   A 1 237 ? 358.578 -8.873  98.700  1.00 52.78  ? 216  TYR   A C    1 
ATOM   1676 O  O    . TYR   A 1 237 ? 358.652 -10.052 99.061  1.00 54.92  ? 216  TYR   A O    1 
ATOM   1677 C  CB   . TYR   A 1 237 ? 357.490 -8.784  96.424  1.00 46.03  ? 216  TYR   A CB   1 
ATOM   1678 C  CG   . TYR   A 1 237 ? 356.234 -8.094  96.910  1.00 54.32  ? 216  TYR   A CG   1 
ATOM   1679 C  CD1  . TYR   A 1 237 ? 355.913 -6.811  96.482  1.00 54.87  ? 216  TYR   A CD1  1 
ATOM   1680 C  CD2  . TYR   A 1 237 ? 355.351 -8.739  97.768  1.00 55.41  ? 216  TYR   A CD2  1 
ATOM   1681 C  CE1  . TYR   A 1 237 ? 354.756 -6.180  96.913  1.00 59.48  ? 216  TYR   A CE1  1 
ATOM   1682 C  CE2  . TYR   A 1 237 ? 354.192 -8.117  98.204  1.00 55.42  ? 216  TYR   A CE2  1 
ATOM   1683 C  CZ   . TYR   A 1 237 ? 353.899 -6.837  97.773  1.00 61.24  ? 216  TYR   A CZ   1 
ATOM   1684 O  OH   . TYR   A 1 237 ? 352.747 -6.212  98.204  1.00 66.31  ? 216  TYR   A OH   1 
ATOM   1685 N  N    . VAL   A 1 238 ? 358.363 -7.871  99.546  1.00 55.01  ? 217  VAL   A N    1 
ATOM   1686 C  CA   . VAL   A 1 238 ? 358.152 -8.098  100.974 1.00 58.77  ? 217  VAL   A CA   1 
ATOM   1687 C  C    . VAL   A 1 238 ? 356.659 -8.266  101.226 1.00 60.18  ? 217  VAL   A C    1 
ATOM   1688 O  O    . VAL   A 1 238 ? 355.870 -7.353  100.962 1.00 59.03  ? 217  VAL   A O    1 
ATOM   1689 C  CB   . VAL   A 1 238 ? 358.726 -6.948  101.817 1.00 63.79  ? 217  VAL   A CB   1 
ATOM   1690 C  CG1  . VAL   A 1 238 ? 358.385 -7.144  103.292 1.00 66.31  ? 217  VAL   A CG1  1 
ATOM   1691 C  CG2  . VAL   A 1 238 ? 360.231 -6.847  101.622 1.00 56.85  ? 217  VAL   A CG2  1 
ATOM   1692 N  N    A GLU   A 1 239 ? 356.272 -9.433  101.737 0.50 63.42  ? 218  GLU   A N    1 
ATOM   1693 N  N    B GLU   A 1 239 ? 356.270 -9.432  101.732 0.50 63.42  ? 218  GLU   A N    1 
ATOM   1694 C  CA   A GLU   A 1 239 ? 354.888 -9.728  102.083 0.50 68.01  ? 218  GLU   A CA   1 
ATOM   1695 C  CA   B GLU   A 1 239 ? 354.883 -9.707  102.077 0.50 68.02  ? 218  GLU   A CA   1 
ATOM   1696 C  C    A GLU   A 1 239 ? 354.681 -9.582  103.586 0.50 70.23  ? 218  GLU   A C    1 
ATOM   1697 C  C    B GLU   A 1 239 ? 354.679 -9.583  103.581 0.50 70.22  ? 218  GLU   A C    1 
ATOM   1698 O  O    A GLU   A 1 239 ? 355.540 -9.974  104.382 0.50 68.65  ? 218  GLU   A O    1 
ATOM   1699 O  O    B GLU   A 1 239 ? 355.535 -9.990  104.372 0.50 68.65  ? 218  GLU   A O    1 
ATOM   1700 C  CB   A GLU   A 1 239 ? 354.499 -11.141 101.639 0.50 66.99  ? 218  GLU   A CB   1 
ATOM   1701 C  CB   B GLU   A 1 239 ? 354.459 -11.101 101.609 0.50 66.99  ? 218  GLU   A CB   1 
ATOM   1702 C  CG   A GLU   A 1 239 ? 353.161 -11.629 102.193 0.50 66.37  ? 218  GLU   A CG   1 
ATOM   1703 C  CG   B GLU   A 1 239 ? 353.906 -11.136 100.197 0.50 61.79  ? 218  GLU   A CG   1 
ATOM   1704 C  CD   A GLU   A 1 239 ? 353.320 -12.669 103.292 0.50 68.32  ? 218  GLU   A CD   1 
ATOM   1705 C  CD   B GLU   A 1 239 ? 352.931 -12.277 99.985  0.50 62.53  ? 218  GLU   A CD   1 
ATOM   1706 O  OE1  A GLU   A 1 239 ? 354.241 -13.507 103.193 0.50 65.97  ? 218  GLU   A OE1  1 
ATOM   1707 O  OE1  B GLU   A 1 239 ? 353.064 -13.311 100.672 0.50 63.88  ? 218  GLU   A OE1  1 
ATOM   1708 O  OE2  A GLU   A 1 239 ? 352.524 -12.648 104.256 0.50 65.17  ? 218  GLU   A OE2  1 
ATOM   1709 O  OE2  B GLU   A 1 239 ? 352.023 -12.134 99.139  0.50 63.59  ? 218  GLU   A OE2  1 
ATOM   1710 N  N    . ASN   A 1 240 ? 353.538 -9.019  103.965 1.00 72.89  ? 219  ASN   A N    1 
ATOM   1711 C  CA   . ASN   A 1 240 ? 353.177 -8.828  105.365 1.00 69.77  ? 219  ASN   A CA   1 
ATOM   1712 C  C    . ASN   A 1 240 ? 354.278 -8.090  106.131 1.00 79.97  ? 219  ASN   A C    1 
ATOM   1713 O  O    . ASN   A 1 240 ? 354.818 -8.611  107.109 1.00 78.33  ? 219  ASN   A O    1 
ATOM   1714 C  CB   . ASN   A 1 240 ? 352.864 -10.165 106.025 1.00 73.17  ? 219  ASN   A CB   1 
ATOM   1715 C  CG   . ASN   A 1 240 ? 352.265 -10.010 107.415 1.00 76.83  ? 219  ASN   A CG   1 
ATOM   1716 O  OD1  . ASN   A 1 240 ? 351.486 -9.091  107.672 1.00 81.03  ? 219  ASN   A OD1  1 
ATOM   1717 N  ND2  . ASN   A 1 240 ? 352.630 -10.913 108.319 1.00 78.66  ? 219  ASN   A ND2  1 
ATOM   1718 N  N    . PRO   A 1 241 ? 354.631 -6.870  105.709 1.00 80.59  ? 220  PRO   A N    1 
ATOM   1719 C  CA   . PRO   A 1 241 ? 355.725 -6.155  106.386 1.00 85.37  ? 220  PRO   A CA   1 
ATOM   1720 C  C    . PRO   A 1 241 ? 355.403 -5.759  107.818 1.00 87.11  ? 220  PRO   A C    1 
ATOM   1721 O  O    . PRO   A 1 241 ? 356.334 -5.594  108.618 1.00 86.04  ? 220  PRO   A O    1 
ATOM   1722 C  CB   . PRO   A 1 241 ? 355.943 -4.916  105.502 1.00 83.86  ? 220  PRO   A CB   1 
ATOM   1723 C  CG   . PRO   A 1 241 ? 355.211 -5.202  104.214 1.00 80.27  ? 220  PRO   A CG   1 
ATOM   1724 C  CD   . PRO   A 1 241 ? 354.068 -6.086  104.597 1.00 72.00  ? 220  PRO   A CD   1 
ATOM   1725 N  N    . PHE   A 1 242 ? 354.127 -5.612  108.171 1.00 92.89  ? 221  PHE   A N    1 
ATOM   1726 C  CA   . PHE   A 1 242 ? 353.725 -5.100  109.475 1.00 90.59  ? 221  PHE   A CA   1 
ATOM   1727 C  C    . PHE   A 1 242 ? 353.629 -6.181  110.549 1.00 92.72  ? 221  PHE   A C    1 
ATOM   1728 O  O    . PHE   A 1 242 ? 353.314 -5.859  111.700 1.00 95.81  ? 221  PHE   A O    1 
ATOM   1729 C  CB   . PHE   A 1 242 ? 352.382 -4.367  109.361 1.00 92.32  ? 221  PHE   A CB   1 
ATOM   1730 C  CG   . PHE   A 1 242 ? 352.384 -3.236  108.366 1.00 100.07 ? 221  PHE   A CG   1 
ATOM   1731 C  CD1  . PHE   A 1 242 ? 352.218 -3.484  107.012 1.00 105.13 ? 221  PHE   A CD1  1 
ATOM   1732 C  CD2  . PHE   A 1 242 ? 352.540 -1.925  108.786 1.00 93.89  ? 221  PHE   A CD2  1 
ATOM   1733 C  CE1  . PHE   A 1 242 ? 352.216 -2.448  106.096 1.00 102.30 ? 221  PHE   A CE1  1 
ATOM   1734 C  CE2  . PHE   A 1 242 ? 352.538 -0.884  107.875 1.00 100.83 ? 221  PHE   A CE2  1 
ATOM   1735 C  CZ   . PHE   A 1 242 ? 352.376 -1.146  106.528 1.00 107.60 ? 221  PHE   A CZ   1 
ATOM   1736 N  N    . PHE   A 1 243 ? 353.882 -7.445  110.208 1.00 81.52  ? 222  PHE   A N    1 
ATOM   1737 C  CA   . PHE   A 1 243 ? 353.916 -8.520  111.197 1.00 78.14  ? 222  PHE   A CA   1 
ATOM   1738 C  C    . PHE   A 1 243 ? 355.173 -9.366  111.010 1.00 78.47  ? 222  PHE   A C    1 
ATOM   1739 O  O    . PHE   A 1 243 ? 356.287 -8.829  110.987 1.00 76.19  ? 222  PHE   A O    1 
ATOM   1740 C  CB   . PHE   A 1 243 ? 352.653 -9.383  111.100 1.00 76.22  ? 222  PHE   A CB   1 
ATOM   1741 C  CG   . PHE   A 1 243 ? 351.397 -8.686  111.563 1.00 79.67  ? 222  PHE   A CG   1 
ATOM   1742 C  CD1  . PHE   A 1 243 ? 351.036 -8.696  112.902 1.00 77.39  ? 222  PHE   A CD1  1 
ATOM   1743 C  CD2  . PHE   A 1 243 ? 350.575 -8.027  110.662 1.00 83.75  ? 222  PHE   A CD2  1 
ATOM   1744 C  CE1  . PHE   A 1 243 ? 349.884 -8.059  113.334 1.00 79.90  ? 222  PHE   A CE1  1 
ATOM   1745 C  CE2  . PHE   A 1 243 ? 349.420 -7.389  111.089 1.00 73.67  ? 222  PHE   A CE2  1 
ATOM   1746 C  CZ   . PHE   A 1 243 ? 349.075 -7.406  112.428 1.00 78.02  ? 222  PHE   A CZ   1 
ATOM   1747 N  N    . GLY   A 1 244 ? 355.013 -10.684 110.888 1.00 77.79  ? 223  GLY   A N    1 
ATOM   1748 C  CA   . GLY   A 1 244 ? 356.126 -11.550 110.542 1.00 78.80  ? 223  GLY   A CA   1 
ATOM   1749 C  C    . GLY   A 1 244 ? 356.482 -11.441 109.071 1.00 76.82  ? 223  GLY   A C    1 
ATOM   1750 O  O    . GLY   A 1 244 ? 355.693 -11.837 108.208 1.00 72.75  ? 223  GLY   A O    1 
ATOM   1751 N  N    . GLN   A 1 245 ? 357.668 -10.913 108.773 1.00 72.17  ? 224  GLN   A N    1 
ATOM   1752 C  CA   . GLN   A 1 245 ? 358.014 -10.544 107.406 1.00 75.05  ? 224  GLN   A CA   1 
ATOM   1753 C  C    . GLN   A 1 245 ? 358.468 -11.745 106.586 1.00 76.30  ? 224  GLN   A C    1 
ATOM   1754 O  O    . GLN   A 1 245 ? 359.190 -12.619 107.076 1.00 76.07  ? 224  GLN   A O    1 
ATOM   1755 C  CB   . GLN   A 1 245 ? 359.108 -9.475  107.405 1.00 70.67  ? 224  GLN   A CB   1 
ATOM   1756 C  CG   . GLN   A 1 245 ? 358.576 -8.069  107.194 1.00 75.78  ? 224  GLN   A CG   1 
ATOM   1757 C  CD   . GLN   A 1 245 ? 359.656 -7.011  107.274 1.00 70.64  ? 224  GLN   A CD   1 
ATOM   1758 O  OE1  . GLN   A 1 245 ? 360.843 -7.302  107.123 1.00 65.81  ? 224  GLN   A OE1  1 
ATOM   1759 N  NE2  . GLN   A 1 245 ? 359.248 -5.771  107.518 1.00 67.72  ? 224  GLN   A NE2  1 
ATOM   1760 N  N    . ARG   A 1 246 ? 358.042 -11.768 105.321 1.00 69.30  ? 225  ARG   A N    1 
ATOM   1761 C  CA   . ARG   A 1 246 ? 358.444 -12.785 104.361 1.00 69.60  ? 225  ARG   A CA   1 
ATOM   1762 C  C    . ARG   A 1 246 ? 358.786 -12.106 103.041 1.00 66.30  ? 225  ARG   A C    1 
ATOM   1763 O  O    . ARG   A 1 246 ? 358.232 -11.056 102.707 1.00 62.97  ? 225  ARG   A O    1 
ATOM   1764 C  CB   . ARG   A 1 246 ? 357.343 -13.837 104.161 1.00 68.83  ? 225  ARG   A CB   1 
ATOM   1765 C  CG   . ARG   A 1 246 ? 356.946 -14.577 105.438 1.00 78.12  ? 225  ARG   A CG   1 
ATOM   1766 C  CD   . ARG   A 1 246 ? 358.153 -15.239 106.098 1.00 79.33  ? 225  ARG   A CD   1 
ATOM   1767 N  NE   . ARG   A 1 246 ? 357.777 -16.133 107.189 1.00 90.62  ? 225  ARG   A NE   1 
ATOM   1768 C  CZ   . ARG   A 1 246 ? 357.889 -15.843 108.479 1.00 90.67  ? 225  ARG   A CZ   1 
ATOM   1769 N  NH1  . ARG   A 1 246 ? 358.368 -14.679 108.889 1.00 89.32  ? 225  ARG   A NH1  1 
ATOM   1770 N  NH2  . ARG   A 1 246 ? 357.516 -16.746 109.383 1.00 89.48  ? 225  ARG   A NH2  1 
ATOM   1771 N  N    . TYR   A 1 247 ? 359.702 -12.720 102.289 1.00 66.83  ? 226  TYR   A N    1 
ATOM   1772 C  CA   . TYR   A 1 247 ? 360.290 -12.112 101.097 1.00 60.69  ? 226  TYR   A CA   1 
ATOM   1773 C  C    . TYR   A 1 247 ? 360.133 -13.069 99.925  1.00 50.54  ? 226  TYR   A C    1 
ATOM   1774 O  O    . TYR   A 1 247 ? 360.673 -14.180 99.954  1.00 54.82  ? 226  TYR   A O    1 
ATOM   1775 C  CB   . TYR   A 1 247 ? 361.763 -11.777 101.346 1.00 55.62  ? 226  TYR   A CB   1 
ATOM   1776 C  CG   . TYR   A 1 247 ? 361.993 -11.212 102.730 1.00 60.25  ? 226  TYR   A CG   1 
ATOM   1777 C  CD1  . TYR   A 1 247 ? 361.821 -9.857  102.985 1.00 60.09  ? 226  TYR   A CD1  1 
ATOM   1778 C  CD2  . TYR   A 1 247 ? 362.352 -12.037 103.788 1.00 62.23  ? 226  TYR   A CD2  1 
ATOM   1779 C  CE1  . TYR   A 1 247 ? 362.014 -9.338  104.253 1.00 63.03  ? 226  TYR   A CE1  1 
ATOM   1780 C  CE2  . TYR   A 1 247 ? 362.548 -11.527 105.058 1.00 62.72  ? 226  TYR   A CE2  1 
ATOM   1781 C  CZ   . TYR   A 1 247 ? 362.378 -10.178 105.285 1.00 67.00  ? 226  TYR   A CZ   1 
ATOM   1782 O  OH   . TYR   A 1 247 ? 362.574 -9.672  106.549 1.00 67.95  ? 226  TYR   A OH   1 
ATOM   1783 N  N    A ILE   A 1 248 ? 359.410 -12.636 98.893  0.50 46.73  ? 227  ILE   A N    1 
ATOM   1784 N  N    B ILE   A 1 248 ? 359.403 -12.640 98.895  0.50 46.87  ? 227  ILE   A N    1 
ATOM   1785 C  CA   A ILE   A 1 248 ? 359.011 -13.500 97.786  0.50 48.98  ? 227  ILE   A CA   1 
ATOM   1786 C  CA   B ILE   A 1 248 ? 359.015 -13.512 97.791  0.50 48.78  ? 227  ILE   A CA   1 
ATOM   1787 C  C    A ILE   A 1 248 ? 359.882 -13.207 96.573  0.50 48.78  ? 227  ILE   A C    1 
ATOM   1788 C  C    B ILE   A 1 248 ? 359.880 -13.210 96.575  0.50 48.70  ? 227  ILE   A C    1 
ATOM   1789 O  O    A ILE   A 1 248 ? 360.017 -12.049 96.155  0.50 44.68  ? 227  ILE   A O    1 
ATOM   1790 O  O    B ILE   A 1 248 ? 360.012 -12.051 96.161  0.50 46.56  ? 227  ILE   A O    1 
ATOM   1791 C  CB   A ILE   A 1 248 ? 357.521 -13.320 97.448  0.50 50.26  ? 227  ILE   A CB   1 
ATOM   1792 C  CB   B ILE   A 1 248 ? 357.521 -13.361 97.456  0.50 50.15  ? 227  ILE   A CB   1 
ATOM   1793 C  CG1  A ILE   A 1 248 ? 356.641 -13.992 98.507  0.50 50.69  ? 227  ILE   A CG1  1 
ATOM   1794 C  CG1  B ILE   A 1 248 ? 357.089 -14.453 96.477  0.50 48.77  ? 227  ILE   A CG1  1 
ATOM   1795 C  CG2  A ILE   A 1 248 ? 357.215 -13.873 96.062  0.50 47.84  ? 227  ILE   A CG2  1 
ATOM   1796 C  CG2  B ILE   A 1 248 ? 357.228 -11.985 96.879  0.50 50.58  ? 227  ILE   A CG2  1 
ATOM   1797 C  CD1  A ILE   A 1 248 ? 356.706 -13.345 99.874  0.50 54.51  ? 227  ILE   A CD1  1 
ATOM   1798 C  CD1  B ILE   A 1 248 ? 357.358 -15.855 96.980  0.50 51.43  ? 227  ILE   A CD1  1 
ATOM   1799 N  N    . HIS   A 1 249 ? 360.464 -14.260 96.001  1.00 45.41  ? 228  HIS   A N    1 
ATOM   1800 C  CA   . HIS   A 1 249 ? 361.274 -14.156 94.792  1.00 42.93  ? 228  HIS   A CA   1 
ATOM   1801 C  C    . HIS   A 1 249 ? 360.342 -14.187 93.585  1.00 46.66  ? 228  HIS   A C    1 
ATOM   1802 O  O    . HIS   A 1 249 ? 359.693 -15.204 93.321  1.00 51.50  ? 228  HIS   A O    1 
ATOM   1803 C  CB   . HIS   A 1 249 ? 362.279 -15.305 94.757  1.00 48.24  ? 228  HIS   A CB   1 
ATOM   1804 C  CG   . HIS   A 1 249 ? 363.148 -15.330 93.539  1.00 46.53  ? 228  HIS   A CG   1 
ATOM   1805 N  ND1  . HIS   A 1 249 ? 362.935 -16.200 92.491  1.00 44.04  ? 228  HIS   A ND1  1 
ATOM   1806 C  CD2  . HIS   A 1 249 ? 364.251 -14.615 93.216  1.00 41.41  ? 228  HIS   A CD2  1 
ATOM   1807 C  CE1  . HIS   A 1 249 ? 363.861 -16.009 91.568  1.00 44.85  ? 228  HIS   A CE1  1 
ATOM   1808 N  NE2  . HIS   A 1 249 ? 364.671 -15.053 91.984  1.00 41.38  ? 228  HIS   A NE2  1 
ATOM   1809 N  N    . ILE   A 1 250 ? 360.260 -13.078 92.852  1.00 43.68  ? 229  ILE   A N    1 
ATOM   1810 C  CA   . ILE   A 1 250 ? 359.287 -12.954 91.775  1.00 41.71  ? 229  ILE   A CA   1 
ATOM   1811 C  C    . ILE   A 1 250 ? 359.921 -12.899 90.389  1.00 41.93  ? 229  ILE   A C    1 
ATOM   1812 O  O    . ILE   A 1 250 ? 359.211 -13.123 89.396  1.00 37.59  ? 229  ILE   A O    1 
ATOM   1813 C  CB   . ILE   A 1 250 ? 358.372 -11.730 91.983  1.00 46.01  ? 229  ILE   A CB   1 
ATOM   1814 C  CG1  . ILE   A 1 250 ? 359.173 -10.435 91.846  1.00 40.98  ? 229  ILE   A CG1  1 
ATOM   1815 C  CG2  . ILE   A 1 250 ? 357.660 -11.816 93.331  1.00 48.41  ? 229  ILE   A CG2  1 
ATOM   1816 C  CD1  . ILE   A 1 250 ? 358.348 -9.271  91.351  1.00 43.90  ? 229  ILE   A CD1  1 
ATOM   1817 N  N    . LEU   A 1 251 ? 361.212 -12.593 90.281  1.00 43.20  ? 230  LEU   A N    1 
ATOM   1818 C  CA   . LEU   A 1 251 ? 361.898 -12.586 88.998  1.00 38.63  ? 230  LEU   A CA   1 
ATOM   1819 C  C    . LEU   A 1 251 ? 363.344 -12.999 89.219  1.00 37.46  ? 230  LEU   A C    1 
ATOM   1820 O  O    . LEU   A 1 251 ? 363.933 -12.714 90.265  1.00 34.13  ? 230  LEU   A O    1 
ATOM   1821 C  CB   . LEU   A 1 251 ? 361.846 -11.213 88.312  1.00 37.85  ? 230  LEU   A CB   1 
ATOM   1822 C  CG   . LEU   A 1 251 ? 360.504 -10.648 87.834  1.00 38.29  ? 230  LEU   A CG   1 
ATOM   1823 C  CD1  . LEU   A 1 251 ? 360.694 -9.255  87.254  1.00 28.54  ? 230  LEU   A CD1  1 
ATOM   1824 C  CD2  . LEU   A 1 251 ? 359.853 -11.560 86.809  1.00 34.58  ? 230  LEU   A CD2  1 
ATOM   1825 N  N    . GLY   A 1 252 ? 363.908 -13.671 88.221  1.00 35.76  ? 231  GLY   A N    1 
ATOM   1826 C  CA   . GLY   A 1 252 ? 365.274 -14.142 88.310  1.00 37.58  ? 231  GLY   A CA   1 
ATOM   1827 C  C    . GLY   A 1 252 ? 365.411 -15.565 87.817  1.00 41.98  ? 231  GLY   A C    1 
ATOM   1828 O  O    . GLY   A 1 252 ? 364.751 -15.952 86.849  1.00 40.30  ? 231  GLY   A O    1 
ATOM   1829 N  N    . ARG   A 1 253 ? 366.249 -16.359 88.476  1.00 40.32  ? 232  ARG   A N    1 
ATOM   1830 C  CA   . ARG   A 1 253 ? 366.510 -17.715 88.014  1.00 38.62  ? 232  ARG   A CA   1 
ATOM   1831 C  C    . ARG   A 1 253 ? 365.211 -18.488 87.852  1.00 43.72  ? 232  ARG   A C    1 
ATOM   1832 O  O    . ARG   A 1 253 ? 364.488 -18.726 88.825  1.00 47.21  ? 232  ARG   A O    1 
ATOM   1833 C  CB   . ARG   A 1 253 ? 367.436 -18.426 89.003  1.00 48.34  ? 232  ARG   A CB   1 
ATOM   1834 C  CG   . ARG   A 1 253 ? 368.804 -17.776 89.135  1.00 42.15  ? 232  ARG   A CG   1 
ATOM   1835 C  CD   . ARG   A 1 253 ? 369.796 -18.694 89.824  1.00 43.13  ? 232  ARG   A CD   1 
ATOM   1836 N  NE   . ARG   A 1 253 ? 371.114 -18.080 89.941  1.00 42.37  ? 232  ARG   A NE   1 
ATOM   1837 C  CZ   . ARG   A 1 253 ? 371.572 -17.490 91.036  1.00 46.21  ? 232  ARG   A CZ   1 
ATOM   1838 N  NH1  . ARG   A 1 253 ? 370.839 -17.409 92.135  1.00 44.42  ? 232  ARG   A NH1  1 
ATOM   1839 N  NH2  . ARG   A 1 253 ? 372.799 -16.971 91.029  1.00 38.98  ? 232  ARG   A NH2  1 
ATOM   1840 N  N    . ARG   A 1 254 ? 364.908 -18.861 86.613  1.00 43.12  ? 233  ARG   A N    1 
ATOM   1841 C  CA   . ARG   A 1 254 ? 363.754 -19.693 86.296  1.00 48.71  ? 233  ARG   A CA   1 
ATOM   1842 C  C    . ARG   A 1 254 ? 362.421 -19.003 86.574  1.00 48.57  ? 233  ARG   A C    1 
ATOM   1843 O  O    . ARG   A 1 254 ? 361.383 -19.669 86.638  1.00 52.75  ? 233  ARG   A O    1 
ATOM   1844 C  CB   . ARG   A 1 254 ? 363.819 -21.025 87.051  1.00 45.64  ? 233  ARG   A CB   1 
ATOM   1845 C  CG   . ARG   A 1 254 ? 364.939 -21.942 86.572  1.00 50.72  ? 233  ARG   A CG   1 
ATOM   1846 C  CD   . ARG   A 1 254 ? 365.055 -23.208 87.407  1.00 62.58  ? 233  ARG   A CD   1 
ATOM   1847 N  NE   . ARG   A 1 254 ? 365.417 -22.933 88.793  1.00 66.29  ? 233  ARG   A NE   1 
ATOM   1848 C  CZ   . ARG   A 1 254 ? 366.640 -22.622 89.204  1.00 66.83  ? 233  ARG   A CZ   1 
ATOM   1849 N  NH1  . ARG   A 1 254 ? 367.648 -22.511 88.353  1.00 62.73  ? 233  ARG   A NH1  1 
ATOM   1850 N  NH2  . ARG   A 1 254 ? 366.855 -22.409 90.500  1.00 59.74  ? 233  ARG   A NH2  1 
ATOM   1851 N  N    . LYS   A 1 255 ? 362.414 -17.682 86.746  1.00 43.11  ? 234  LYS   A N    1 
ATOM   1852 C  CA   . LYS   A 1 255 ? 361.180 -16.900 86.860  1.00 41.73  ? 234  LYS   A CA   1 
ATOM   1853 C  C    . LYS   A 1 255 ? 361.315 -15.693 85.937  1.00 39.84  ? 234  LYS   A C    1 
ATOM   1854 O  O    . LYS   A 1 255 ? 361.917 -14.682 86.312  1.00 38.67  ? 234  LYS   A O    1 
ATOM   1855 C  CB   . LYS   A 1 255 ? 360.916 -16.465 88.301  1.00 45.19  ? 234  LYS   A CB   1 
ATOM   1856 C  CG   . LYS   A 1 255 ? 360.645 -17.605 89.276  1.00 44.80  ? 234  LYS   A CG   1 
ATOM   1857 C  CD   . LYS   A 1 255 ? 360.467 -17.089 90.702  1.00 52.58  ? 234  LYS   A CD   1 
ATOM   1858 C  CE   . LYS   A 1 255 ? 360.552 -18.214 91.732  1.00 55.69  ? 234  LYS   A CE   1 
ATOM   1859 N  NZ   . LYS   A 1 255 ? 361.893 -18.870 91.777  1.00 55.48  ? 234  LYS   A NZ   1 
ATOM   1860 N  N    . LEU   A 1 256 ? 360.754 -15.791 84.731  1.00 40.37  ? 235  LEU   A N    1 
ATOM   1861 C  CA   . LEU   A 1 256 ? 360.934 -14.741 83.738  1.00 37.77  ? 235  LEU   A CA   1 
ATOM   1862 C  C    . LEU   A 1 256 ? 359.870 -13.657 83.804  1.00 33.55  ? 235  LEU   A C    1 
ATOM   1863 O  O    . LEU   A 1 256 ? 360.109 -12.544 83.322  1.00 31.33  ? 235  LEU   A O    1 
ATOM   1864 C  CB   . LEU   A 1 256 ? 360.955 -15.342 82.331  1.00 34.19  ? 235  LEU   A CB   1 
ATOM   1865 C  CG   . LEU   A 1 256 ? 362.071 -16.364 82.106  1.00 39.03  ? 235  LEU   A CG   1 
ATOM   1866 C  CD1  . LEU   A 1 256 ? 362.192 -16.738 80.637  1.00 43.31  ? 235  LEU   A CD1  1 
ATOM   1867 C  CD2  . LEU   A 1 256 ? 363.394 -15.837 82.644  1.00 34.32  ? 235  LEU   A CD2  1 
ATOM   1868 N  N    . TYR   A 1 257 ? 358.713 -13.945 84.387  1.00 34.93  ? 236  TYR   A N    1 
ATOM   1869 C  CA   . TYR   A 1 257 ? 357.647 -12.961 84.441  1.00 37.87  ? 236  TYR   A CA   1 
ATOM   1870 C  C    . TYR   A 1 257 ? 356.875 -13.144 85.735  1.00 37.34  ? 236  TYR   A C    1 
ATOM   1871 O  O    . TYR   A 1 257 ? 356.972 -14.179 86.401  1.00 38.12  ? 236  TYR   A O    1 
ATOM   1872 C  CB   . TYR   A 1 257 ? 356.710 -13.077 83.234  1.00 37.15  ? 236  TYR   A CB   1 
ATOM   1873 C  CG   . TYR   A 1 257 ? 355.864 -14.331 83.233  1.00 40.86  ? 236  TYR   A CG   1 
ATOM   1874 C  CD1  . TYR   A 1 257 ? 354.634 -14.363 83.879  1.00 42.00  ? 236  TYR   A CD1  1 
ATOM   1875 C  CD2  . TYR   A 1 257 ? 356.290 -15.481 82.581  1.00 42.94  ? 236  TYR   A CD2  1 
ATOM   1876 C  CE1  . TYR   A 1 257 ? 353.857 -15.504 83.880  1.00 44.17  ? 236  TYR   A CE1  1 
ATOM   1877 C  CE2  . TYR   A 1 257 ? 355.518 -16.626 82.576  1.00 44.55  ? 236  TYR   A CE2  1 
ATOM   1878 C  CZ   . TYR   A 1 257 ? 354.302 -16.634 83.226  1.00 47.68  ? 236  TYR   A CZ   1 
ATOM   1879 O  OH   . TYR   A 1 257 ? 353.532 -17.774 83.221  1.00 49.22  ? 236  TYR   A OH   1 
ATOM   1880 N  N    . HIS   A 1 258 ? 356.100 -12.124 86.082  1.00 36.44  ? 237  HIS   A N    1 
ATOM   1881 C  CA   . HIS   A 1 258 ? 355.294 -12.180 87.293  1.00 35.96  ? 237  HIS   A CA   1 
ATOM   1882 C  C    . HIS   A 1 258 ? 354.070 -11.299 87.118  1.00 36.46  ? 237  HIS   A C    1 
ATOM   1883 O  O    . HIS   A 1 258 ? 354.201 -10.095 86.879  1.00 37.16  ? 237  HIS   A O    1 
ATOM   1884 C  CB   . HIS   A 1 258 ? 356.099 -11.741 88.511  1.00 38.96  ? 237  HIS   A CB   1 
ATOM   1885 C  CG   . HIS   A 1 258 ? 355.345 -11.878 89.792  1.00 45.05  ? 237  HIS   A CG   1 
ATOM   1886 N  ND1  . HIS   A 1 258 ? 354.799 -10.800 90.454  1.00 41.83  ? 237  HIS   A ND1  1 
ATOM   1887 C  CD2  . HIS   A 1 258 ? 355.011 -12.973 90.512  1.00 39.12  ? 237  HIS   A CD2  1 
ATOM   1888 C  CE1  . HIS   A 1 258 ? 354.177 -11.225 91.539  1.00 42.19  ? 237  HIS   A CE1  1 
ATOM   1889 N  NE2  . HIS   A 1 258 ? 354.291 -12.540 91.597  1.00 49.39  ? 237  HIS   A NE2  1 
ATOM   1890 N  N    . VAL   A 1 259 ? 352.890 -11.902 87.245  1.00 40.16  ? 238  VAL   A N    1 
ATOM   1891 C  CA   . VAL   A 1 259 ? 351.638 -11.159 87.164  1.00 40.78  ? 238  VAL   A CA   1 
ATOM   1892 C  C    . VAL   A 1 259 ? 351.459 -10.353 88.443  1.00 37.89  ? 238  VAL   A C    1 
ATOM   1893 O  O    . VAL   A 1 259 ? 351.402 -10.912 89.544  1.00 38.25  ? 238  VAL   A O    1 
ATOM   1894 C  CB   . VAL   A 1 259 ? 350.454 -12.104 86.935  1.00 41.81  ? 238  VAL   A CB   1 
ATOM   1895 C  CG1  . VAL   A 1 259 ? 349.146 -11.320 86.902  1.00 39.21  ? 238  VAL   A CG1  1 
ATOM   1896 C  CG2  . VAL   A 1 259 ? 350.652 -12.894 85.653  1.00 41.76  ? 238  VAL   A CG2  1 
ATOM   1897 N  N    . VAL   A 1 260 ? 351.358 -9.038  88.301  1.00 39.71  ? 239  VAL   A N    1 
ATOM   1898 C  CA   . VAL   A 1 260 ? 351.224 -8.151  89.449  1.00 36.21  ? 239  VAL   A CA   1 
ATOM   1899 C  C    . VAL   A 1 260 ? 349.766 -8.096  89.879  1.00 43.16  ? 239  VAL   A C    1 
ATOM   1900 O  O    . VAL   A 1 260 ? 348.866 -7.919  89.049  1.00 49.02  ? 239  VAL   A O    1 
ATOM   1901 C  CB   . VAL   A 1 260 ? 351.746 -6.747  89.111  1.00 42.34  ? 239  VAL   A CB   1 
ATOM   1902 C  CG1  . VAL   A 1 260 ? 351.469 -5.795  90.260  1.00 47.15  ? 239  VAL   A CG1  1 
ATOM   1903 C  CG2  . VAL   A 1 260 ? 353.231 -6.795  88.791  1.00 35.97  ? 239  VAL   A CG2  1 
ATOM   1904 N  N    . LYS   A 1 261 ? 349.528 -8.241  91.181  1.00 45.40  ? 240  LYS   A N    1 
ATOM   1905 C  CA   . LYS   A 1 261 ? 348.206 -7.986  91.737  1.00 47.31  ? 240  LYS   A CA   1 
ATOM   1906 C  C    . LYS   A 1 261 ? 347.948 -6.484  91.738  1.00 49.18  ? 240  LYS   A C    1 
ATOM   1907 O  O    . LYS   A 1 261 ? 348.656 -5.727  92.410  1.00 55.86  ? 240  LYS   A O    1 
ATOM   1908 C  CB   . LYS   A 1 261 ? 348.103 -8.556  93.150  1.00 41.67  ? 240  LYS   A CB   1 
ATOM   1909 N  N    . TYR   A 1 262 ? 346.947 -6.050  90.979  1.00 46.56  ? 241  TYR   A N    1 
ATOM   1910 C  CA   . TYR   A 1 262 ? 346.665 -4.628  90.839  1.00 51.36  ? 241  TYR   A CA   1 
ATOM   1911 C  C    . TYR   A 1 262 ? 345.873 -4.113  92.035  1.00 56.36  ? 241  TYR   A C    1 
ATOM   1912 O  O    . TYR   A 1 262 ? 344.904 -4.744  92.469  1.00 53.89  ? 241  TYR   A O    1 
ATOM   1913 C  CB   . TYR   A 1 262 ? 345.897 -4.364  89.543  1.00 47.02  ? 241  TYR   A CB   1 
ATOM   1914 C  CG   . TYR   A 1 262 ? 345.350 -2.958  89.438  1.00 46.10  ? 241  TYR   A CG   1 
ATOM   1915 C  CD1  . TYR   A 1 262 ? 346.143 -1.917  88.976  1.00 48.24  ? 241  TYR   A CD1  1 
ATOM   1916 C  CD2  . TYR   A 1 262 ? 344.040 -2.674  89.802  1.00 47.18  ? 241  TYR   A CD2  1 
ATOM   1917 C  CE1  . TYR   A 1 262 ? 345.648 -0.630  88.880  1.00 46.96  ? 241  TYR   A CE1  1 
ATOM   1918 C  CE2  . TYR   A 1 262 ? 343.536 -1.391  89.710  1.00 48.23  ? 241  TYR   A CE2  1 
ATOM   1919 C  CZ   . TYR   A 1 262 ? 344.344 -0.372  89.247  1.00 48.38  ? 241  TYR   A CZ   1 
ATOM   1920 O  OH   . TYR   A 1 262 ? 343.847 0.908   89.152  1.00 44.17  ? 241  TYR   A OH   1 
ATOM   1921 N  N    . THR   A 1 263 ? 346.287 -2.962  92.563  1.00 49.90  ? 242  THR   A N    1 
ATOM   1922 C  CA   . THR   A 1 263 ? 345.583 -2.269  93.635  1.00 53.70  ? 242  THR   A CA   1 
ATOM   1923 C  C    . THR   A 1 263 ? 345.080 -0.932  93.108  1.00 53.40  ? 242  THR   A C    1 
ATOM   1924 O  O    . THR   A 1 263 ? 345.826 -0.204  92.444  1.00 53.88  ? 242  THR   A O    1 
ATOM   1925 C  CB   . THR   A 1 263 ? 346.491 -2.051  94.850  1.00 58.37  ? 242  THR   A CB   1 
ATOM   1926 O  OG1  . THR   A 1 263 ? 346.826 -3.315  95.436  1.00 67.81  ? 242  THR   A OG1  1 
ATOM   1927 C  CG2  . THR   A 1 263 ? 345.798 -1.181  95.890  1.00 56.67  ? 242  THR   A CG2  1 
ATOM   1928 N  N    . GLY   A 1 264 ? 343.824 -0.612  93.402  1.00 51.01  ? 243  GLY   A N    1 
ATOM   1929 C  CA   . GLY   A 1 264 ? 343.215 0.604   92.907  1.00 48.30  ? 243  GLY   A CA   1 
ATOM   1930 C  C    . GLY   A 1 264 ? 343.769 1.855   93.570  1.00 48.93  ? 243  GLY   A C    1 
ATOM   1931 O  O    . GLY   A 1 264 ? 344.604 1.815   94.475  1.00 54.94  ? 243  GLY   A O    1 
ATOM   1932 N  N    . GLY   A 1 265 ? 343.278 3.000   93.099  1.00 48.61  ? 244  GLY   A N    1 
ATOM   1933 C  CA   . GLY   A 1 265 ? 343.744 4.266   93.627  1.00 47.97  ? 244  GLY   A CA   1 
ATOM   1934 C  C    . GLY   A 1 265 ? 345.240 4.438   93.404  1.00 46.12  ? 244  GLY   A C    1 
ATOM   1935 O  O    . GLY   A 1 265 ? 345.848 3.832   92.520  1.00 49.35  ? 244  GLY   A O    1 
ATOM   1936 N  N    . SER   A 1 266 ? 345.833 5.294   94.232  1.00 45.72  ? 245  SER   A N    1 
ATOM   1937 C  CA   . SER   A 1 266 ? 347.275 5.515   94.207  1.00 46.12  ? 245  SER   A CA   1 
ATOM   1938 C  C    . SER   A 1 266 ? 347.954 4.374   94.951  1.00 50.52  ? 245  SER   A C    1 
ATOM   1939 O  O    . SER   A 1 266 ? 347.780 4.223   96.164  1.00 55.68  ? 245  SER   A O    1 
ATOM   1940 C  CB   . SER   A 1 266 ? 347.628 6.862   94.829  1.00 50.34  ? 245  SER   A CB   1 
ATOM   1941 O  OG   . SER   A 1 266 ? 348.047 7.781   93.840  1.00 60.50  ? 245  SER   A OG   1 
ATOM   1942 N  N    . ALA   A 1 267 ? 348.720 3.566   94.230  1.00 45.67  ? 246  ALA   A N    1 
ATOM   1943 C  CA   . ALA   A 1 267 ? 349.382 2.416   94.821  1.00 38.17  ? 246  ALA   A CA   1 
ATOM   1944 C  C    . ALA   A 1 267 ? 350.843 2.400   94.414  1.00 46.44  ? 246  ALA   A C    1 
ATOM   1945 O  O    . ALA   A 1 267 ? 351.197 2.789   93.295  1.00 48.48  ? 246  ALA   A O    1 
ATOM   1946 C  CB   . ALA   A 1 267 ? 348.715 1.100   94.403  1.00 42.90  ? 246  ALA   A CB   1 
ATOM   1947 N  N    . GLU   A 1 268 ? 351.686 1.961   95.338  1.00 45.17  ? 247  GLU   A N    1 
ATOM   1948 C  CA   . GLU   A 1 268 ? 353.092 1.729   95.069  1.00 41.26  ? 247  GLU   A CA   1 
ATOM   1949 C  C    . GLU   A 1 268 ? 353.410 0.303   95.478  1.00 47.22  ? 247  GLU   A C    1 
ATOM   1950 O  O    . GLU   A 1 268 ? 353.043 -0.125  96.576  1.00 50.13  ? 247  GLU   A O    1 
ATOM   1951 C  CB   . GLU   A 1 268 ? 353.979 2.723   95.823  1.00 41.46  ? 247  GLU   A CB   1 
ATOM   1952 C  CG   . GLU   A 1 268 ? 353.731 4.173   95.447  1.00 46.56  ? 247  GLU   A CG   1 
ATOM   1953 C  CD   . GLU   A 1 268 ? 354.815 5.103   95.953  1.00 55.44  ? 247  GLU   A CD   1 
ATOM   1954 O  OE1  . GLU   A 1 268 ? 355.727 4.626   96.661  1.00 52.87  ? 247  GLU   A OE1  1 
ATOM   1955 O  OE2  . GLU   A 1 268 ? 354.758 6.311   95.639  1.00 56.97  ? 247  GLU   A OE2  1 
ATOM   1956 N  N    . LEU   A 1 269 ? 354.055 -0.436  94.586  1.00 38.05  ? 248  LEU   A N    1 
ATOM   1957 C  CA   . LEU   A 1 269 ? 354.578 -1.759  94.894  1.00 39.81  ? 248  LEU   A CA   1 
ATOM   1958 C  C    . LEU   A 1 269 ? 356.096 -1.665  94.955  1.00 33.97  ? 248  LEU   A C    1 
ATOM   1959 O  O    . LEU   A 1 269 ? 356.742 -1.304  93.964  1.00 37.91  ? 248  LEU   A O    1 
ATOM   1960 C  CB   . LEU   A 1 269 ? 354.121 -2.787  93.860  1.00 35.81  ? 248  LEU   A CB   1 
ATOM   1961 C  CG   . LEU   A 1 269 ? 352.613 -3.039  93.888  1.00 43.07  ? 248  LEU   A CG   1 
ATOM   1962 C  CD1  . LEU   A 1 269 ? 352.174 -3.828  92.668  1.00 43.06  ? 248  LEU   A CD1  1 
ATOM   1963 C  CD2  . LEU   A 1 269 ? 352.213 -3.756  95.172  1.00 44.14  ? 248  LEU   A CD2  1 
ATOM   1964 N  N    . LEU   A 1 270 ? 356.652 -1.970  96.124  1.00 41.65  ? 249  LEU   A N    1 
ATOM   1965 C  CA   . LEU   A 1 270 ? 358.083 -1.876  96.370  1.00 38.13  ? 249  LEU   A CA   1 
ATOM   1966 C  C    . LEU   A 1 270 ? 358.739 -3.222  96.089  1.00 37.67  ? 249  LEU   A C    1 
ATOM   1967 O  O    . LEU   A 1 270 ? 358.360 -4.239  96.681  1.00 41.91  ? 249  LEU   A O    1 
ATOM   1968 C  CB   . LEU   A 1 270 ? 358.347 -1.445  97.814  1.00 35.38  ? 249  LEU   A CB   1 
ATOM   1969 C  CG   . LEU   A 1 270 ? 359.817 -1.405  98.243  1.00 40.11  ? 249  LEU   A CG   1 
ATOM   1970 C  CD1  . LEU   A 1 270 ? 360.623 -0.484  97.334  1.00 42.92  ? 249  LEU   A CD1  1 
ATOM   1971 C  CD2  . LEU   A 1 270 ? 359.941 -0.980  99.699  1.00 38.12  ? 249  LEU   A CD2  1 
ATOM   1972 N  N    . PHE   A 1 271 ? 359.718 -3.226  95.190  1.00 34.41  ? 250  PHE   A N    1 
ATOM   1973 C  CA   . PHE   A 1 271 ? 360.505 -4.411  94.893  1.00 36.01  ? 250  PHE   A CA   1 
ATOM   1974 C  C    . PHE   A 1 271 ? 361.963 -4.159  95.240  1.00 36.13  ? 250  PHE   A C    1 
ATOM   1975 O  O    . PHE   A 1 271 ? 362.445 -3.024  95.178  1.00 37.03  ? 250  PHE   A O    1 
ATOM   1976 C  CB   . PHE   A 1 271 ? 360.382 -4.809  93.420  1.00 29.96  ? 250  PHE   A CB   1 
ATOM   1977 C  CG   . PHE   A 1 271 ? 358.984 -5.113  93.007  1.00 37.11  ? 250  PHE   A CG   1 
ATOM   1978 C  CD1  . PHE   A 1 271 ? 358.413 -6.332  93.321  1.00 35.16  ? 250  PHE   A CD1  1 
ATOM   1979 C  CD2  . PHE   A 1 271 ? 358.226 -4.171  92.334  1.00 36.10  ? 250  PHE   A CD2  1 
ATOM   1980 C  CE1  . PHE   A 1 271 ? 357.117 -6.615  92.957  1.00 36.21  ? 250  PHE   A CE1  1 
ATOM   1981 C  CE2  . PHE   A 1 271 ? 356.927 -4.447  91.966  1.00 36.28  ? 250  PHE   A CE2  1 
ATOM   1982 C  CZ   . PHE   A 1 271 ? 356.371 -5.672  92.278  1.00 39.37  ? 250  PHE   A CZ   1 
ATOM   1983 N  N    . PHE   A 1 272 ? 362.658 -5.230  95.613  1.00 35.53  ? 251  PHE   A N    1 
ATOM   1984 C  CA   . PHE   A 1 272 ? 364.088 -5.185  95.887  1.00 30.89  ? 251  PHE   A CA   1 
ATOM   1985 C  C    . PHE   A 1 272 ? 364.812 -6.049  94.865  1.00 35.85  ? 251  PHE   A C    1 
ATOM   1986 O  O    . PHE   A 1 272 ? 364.428 -7.201  94.637  1.00 35.66  ? 251  PHE   A O    1 
ATOM   1987 C  CB   . PHE   A 1 272 ? 364.388 -5.641  97.319  1.00 31.09  ? 251  PHE   A CB   1 
ATOM   1988 C  CG   . PHE   A 1 272 ? 363.799 -4.738  98.371  1.00 39.06  ? 251  PHE   A CG   1 
ATOM   1989 C  CD1  . PHE   A 1 272 ? 362.496 -4.922  98.812  1.00 41.81  ? 251  PHE   A CD1  1 
ATOM   1990 C  CD2  . PHE   A 1 272 ? 364.542 -3.698  98.907  1.00 42.99  ? 251  PHE   A CD2  1 
ATOM   1991 C  CE1  . PHE   A 1 272 ? 361.947 -4.089  99.772  1.00 39.33  ? 251  PHE   A CE1  1 
ATOM   1992 C  CE2  . PHE   A 1 272 ? 363.998 -2.861  99.870  1.00 37.85  ? 251  PHE   A CE2  1 
ATOM   1993 C  CZ   . PHE   A 1 272 ? 362.699 -3.058  100.302 1.00 45.43  ? 251  PHE   A CZ   1 
ATOM   1994 N  N    . VAL   A 1 273 ? 365.846 -5.483  94.247  1.00 30.09  ? 252  VAL   A N    1 
ATOM   1995 C  CA   . VAL   A 1 273 ? 366.575 -6.105  93.148  1.00 27.82  ? 252  VAL   A CA   1 
ATOM   1996 C  C    . VAL   A 1 273 ? 367.999 -6.383  93.612  1.00 31.76  ? 252  VAL   A C    1 
ATOM   1997 O  O    . VAL   A 1 273 ? 368.665 -5.492  94.154  1.00 33.91  ? 252  VAL   A O    1 
ATOM   1998 C  CB   . VAL   A 1 273 ? 366.569 -5.200  91.902  1.00 27.48  ? 252  VAL   A CB   1 
ATOM   1999 C  CG1  . VAL   A 1 273 ? 367.198 -5.904  90.704  1.00 28.93  ? 252  VAL   A CG1  1 
ATOM   2000 C  CG2  . VAL   A 1 273 ? 365.151 -4.734  91.581  1.00 28.79  ? 252  VAL   A CG2  1 
ATOM   2001 N  N    . GLU   A 1 274 ? 368.468 -7.611  93.400  1.00 29.06  ? 253  GLU   A N    1 
ATOM   2002 C  CA   . GLU   A 1 274 ? 369.846 -7.975  93.702  1.00 31.49  ? 253  GLU   A CA   1 
ATOM   2003 C  C    . GLU   A 1 274 ? 370.565 -8.393  92.427  1.00 36.50  ? 253  GLU   A C    1 
ATOM   2004 O  O    . GLU   A 1 274 ? 369.984 -9.052  91.559  1.00 32.48  ? 253  GLU   A O    1 
ATOM   2005 C  CB   . GLU   A 1 274 ? 369.920 -9.109  94.734  1.00 31.79  ? 253  GLU   A CB   1 
ATOM   2006 C  CG   . GLU   A 1 274 ? 369.258 -10.398 94.282  1.00 37.53  ? 253  GLU   A CG   1 
ATOM   2007 C  CD   . GLU   A 1 274 ? 369.467 -11.549 95.250  1.00 44.45  ? 253  GLU   A CD   1 
ATOM   2008 O  OE1  . GLU   A 1 274 ? 370.039 -11.333 96.342  1.00 39.99  ? 253  GLU   A OE1  1 
ATOM   2009 O  OE2  . GLU   A 1 274 ? 369.054 -12.678 94.911  1.00 45.85  ? 253  GLU   A OE2  1 
ATOM   2010 N  N    . GLY   A 1 275 ? 371.830 -7.994  92.316  1.00 31.41  ? 254  GLY   A N    1 
ATOM   2011 C  CA   . GLY   A 1 275 ? 372.671 -8.492  91.242  1.00 27.32  ? 254  GLY   A CA   1 
ATOM   2012 C  C    . GLY   A 1 275 ? 373.249 -9.851  91.605  1.00 32.50  ? 254  GLY   A C    1 
ATOM   2013 O  O    . GLY   A 1 275 ? 373.591 -10.117 92.757  1.00 31.42  ? 254  GLY   A O    1 
ATOM   2014 N  N    . LEU   A 1 276 ? 373.339 -10.724 90.602  1.00 32.10  ? 255  LEU   A N    1 
ATOM   2015 C  CA   . LEU   A 1 276 ? 373.882 -12.062 90.790  1.00 34.69  ? 255  LEU   A CA   1 
ATOM   2016 C  C    . LEU   A 1 276 ? 375.204 -12.292 90.076  1.00 36.57  ? 255  LEU   A C    1 
ATOM   2017 O  O    . LEU   A 1 276 ? 375.826 -13.338 90.290  1.00 36.38  ? 255  LEU   A O    1 
ATOM   2018 C  CB   . LEU   A 1 276 ? 372.882 -13.122 90.304  1.00 32.20  ? 255  LEU   A CB   1 
ATOM   2019 C  CG   . LEU   A 1 276 ? 371.424 -13.001 90.736  1.00 32.44  ? 255  LEU   A CG   1 
ATOM   2020 C  CD1  . LEU   A 1 276 ? 370.652 -14.214 90.254  1.00 35.28  ? 255  LEU   A CD1  1 
ATOM   2021 C  CD2  . LEU   A 1 276 ? 371.318 -12.857 92.241  1.00 32.54  ? 255  LEU   A CD2  1 
ATOM   2022 N  N    . CYS   A 1 277 ? 375.654 -11.355 89.246  1.00 30.17  ? 256  CYS   A N    1 
ATOM   2023 C  CA   . CYS   A 1 277 ? 376.753 -11.633 88.333  1.00 30.15  ? 256  CYS   A CA   1 
ATOM   2024 C  C    . CYS   A 1 277 ? 377.513 -10.348 88.044  1.00 27.55  ? 256  CYS   A C    1 
ATOM   2025 O  O    . CYS   A 1 277 ? 376.900 -9.325  87.725  1.00 27.73  ? 256  CYS   A O    1 
ATOM   2026 C  CB   . CYS   A 1 277 ? 376.211 -12.251 87.038  1.00 32.17  ? 256  CYS   A CB   1 
ATOM   2027 S  SG   . CYS   A 1 277 ? 377.439 -12.765 85.824  1.00 45.30  ? 256  CYS   A SG   1 
ATOM   2028 N  N    . PHE   A 1 278 ? 378.838 -10.396 88.168  1.00 28.62  ? 257  PHE   A N    1 
ATOM   2029 C  CA   . PHE   A 1 278 ? 379.649 -9.251  87.799  1.00 27.35  ? 257  PHE   A CA   1 
ATOM   2030 C  C    . PHE   A 1 278 ? 379.716 -9.126  86.282  1.00 29.78  ? 257  PHE   A C    1 
ATOM   2031 O  O    . PHE   A 1 278 ? 379.452 -10.089 85.557  1.00 27.74  ? 257  PHE   A O    1 
ATOM   2032 C  CB   . PHE   A 1 278 ? 381.061 -9.376  88.368  1.00 23.91  ? 257  PHE   A CB   1 
ATOM   2033 C  CG   . PHE   A 1 278 ? 381.163 -9.010  89.817  1.00 31.91  ? 257  PHE   A CG   1 
ATOM   2034 C  CD1  . PHE   A 1 278 ? 381.256 -7.683  90.201  1.00 26.34  ? 257  PHE   A CD1  1 
ATOM   2035 C  CD2  . PHE   A 1 278 ? 381.164 -9.989  90.795  1.00 31.80  ? 257  PHE   A CD2  1 
ATOM   2036 C  CE1  . PHE   A 1 278 ? 381.345 -7.338  91.536  1.00 27.56  ? 257  PHE   A CE1  1 
ATOM   2037 C  CE2  . PHE   A 1 278 ? 381.254 -9.650  92.132  1.00 33.14  ? 257  PHE   A CE2  1 
ATOM   2038 C  CZ   . PHE   A 1 278 ? 381.345 -8.322  92.503  1.00 32.25  ? 257  PHE   A CZ   1 
ATOM   2039 N  N    . PRO   A 1 279 ? 380.049 -7.939  85.777  1.00 26.87  ? 258  PRO   A N    1 
ATOM   2040 C  CA   . PRO   A 1 279 ? 380.384 -7.819  84.355  1.00 29.05  ? 258  PRO   A CA   1 
ATOM   2041 C  C    . PRO   A 1 279 ? 381.509 -8.775  84.000  1.00 29.50  ? 258  PRO   A C    1 
ATOM   2042 O  O    . PRO   A 1 279 ? 382.415 -9.020  84.798  1.00 29.18  ? 258  PRO   A O    1 
ATOM   2043 C  CB   . PRO   A 1 279 ? 380.821 -6.357  84.213  1.00 26.47  ? 258  PRO   A CB   1 
ATOM   2044 C  CG   . PRO   A 1 279 ? 380.169 -5.651  85.354  1.00 27.25  ? 258  PRO   A CG   1 
ATOM   2045 C  CD   . PRO   A 1 279 ? 380.116 -6.645  86.479  1.00 25.77  ? 258  PRO   A CD   1 
ATOM   2046 N  N    . ASP   A 1 280 ? 381.449 -9.320  82.793  1.00 29.79  ? 259  ASP   A N    1 
ATOM   2047 C  CA   A ASP   A 1 280 ? 382.421 -10.305 82.345  0.50 34.58  ? 259  ASP   A CA   1 
ATOM   2048 C  CA   B ASP   A 1 280 ? 382.477 -10.250 82.345  0.50 35.11  ? 259  ASP   A CA   1 
ATOM   2049 C  C    . ASP   A 1 280 ? 382.471 -10.266 80.823  1.00 32.76  ? 259  ASP   A C    1 
ATOM   2050 O  O    . ASP   A 1 280 ? 381.799 -9.454  80.180  1.00 33.56  ? 259  ASP   A O    1 
ATOM   2051 C  CB   A ASP   A 1 280 ? 382.051 -11.695 82.867  0.50 36.34  ? 259  ASP   A CB   1 
ATOM   2052 C  CB   B ASP   A 1 280 ? 382.260 -11.645 82.945  0.50 36.21  ? 259  ASP   A CB   1 
ATOM   2053 C  CG   A ASP   A 1 280 ? 383.250 -12.598 83.029  0.50 34.03  ? 259  ASP   A CG   1 
ATOM   2054 C  CG   B ASP   A 1 280 ? 381.129 -12.405 82.275  0.50 37.05  ? 259  ASP   A CG   1 
ATOM   2055 O  OD1  A ASP   A 1 280 ? 384.235 -12.430 82.281  0.50 34.40  ? 259  ASP   A OD1  1 
ATOM   2056 O  OD1  B ASP   A 1 280 ? 380.253 -11.759 81.664  0.50 38.05  ? 259  ASP   A OD1  1 
ATOM   2057 O  OD2  A ASP   A 1 280 ? 383.203 -13.480 83.912  0.50 34.32  ? 259  ASP   A OD2  1 
ATOM   2058 O  OD2  B ASP   A 1 280 ? 381.115 -13.651 82.361  0.50 41.67  ? 259  ASP   A OD2  1 
ATOM   2059 N  N    . GLU   A 1 281 ? 383.256 -11.168 80.245  1.00 36.37  ? 260  GLU   A N    1 
ATOM   2060 C  CA   . GLU   A 1 281 ? 383.224 -11.345 78.803  1.00 41.73  ? 260  GLU   A CA   1 
ATOM   2061 C  C    . GLU   A 1 281 ? 381.800 -11.681 78.382  1.00 42.04  ? 260  GLU   A C    1 
ATOM   2062 O  O    . GLU   A 1 281 ? 381.200 -12.628 78.901  1.00 47.48  ? 260  GLU   A O    1 
ATOM   2063 C  CB   . GLU   A 1 281 ? 384.187 -12.455 78.386  1.00 38.51  ? 260  GLU   A CB   1 
ATOM   2064 C  CG   . GLU   A 1 281 ? 384.245 -12.691 76.889  1.00 43.92  ? 260  GLU   A CG   1 
ATOM   2065 C  CD   . GLU   A 1 281 ? 385.005 -11.604 76.161  1.00 53.05  ? 260  GLU   A CD   1 
ATOM   2066 O  OE1  . GLU   A 1 281 ? 385.616 -10.751 76.840  1.00 54.65  ? 260  GLU   A OE1  1 
ATOM   2067 O  OE2  . GLU   A 1 281 ? 384.995 -11.603 74.912  1.00 63.19  ? 260  GLU   A OE2  1 
ATOM   2068 N  N    . GLY   A 1 282 ? 381.241 -10.889 77.473  1.00 40.99  ? 261  GLY   A N    1 
ATOM   2069 C  CA   . GLY   A 1 282 ? 379.901 -11.152 76.994  1.00 42.05  ? 261  GLY   A CA   1 
ATOM   2070 C  C    . GLY   A 1 282 ? 378.767 -10.728 77.907  1.00 44.61  ? 261  GLY   A C    1 
ATOM   2071 O  O    . GLY   A 1 282 ? 377.602 -10.950 77.552  1.00 46.68  ? 261  GLY   A O    1 
ATOM   2072 N  N    . PHE   A 1 283 ? 379.054 -10.145 79.072  1.00 38.30  ? 262  PHE   A N    1 
ATOM   2073 C  CA   . PHE   A 1 283 ? 378.030 -9.518  79.908  1.00 31.32  ? 262  PHE   A CA   1 
ATOM   2074 C  C    . PHE   A 1 283 ? 378.519 -8.133  80.302  1.00 32.52  ? 262  PHE   A C    1 
ATOM   2075 O  O    . PHE   A 1 283 ? 379.463 -8.005  81.088  1.00 32.43  ? 262  PHE   A O    1 
ATOM   2076 C  CB   . PHE   A 1 283 ? 377.705 -10.348 81.151  1.00 34.91  ? 262  PHE   A CB   1 
ATOM   2077 C  CG   . PHE   A 1 283 ? 376.762 -9.656  82.106  1.00 31.18  ? 262  PHE   A CG   1 
ATOM   2078 C  CD1  . PHE   A 1 283 ? 375.555 -9.138  81.656  1.00 34.25  ? 262  PHE   A CD1  1 
ATOM   2079 C  CD2  . PHE   A 1 283 ? 377.080 -9.524  83.449  1.00 27.53  ? 262  PHE   A CD2  1 
ATOM   2080 C  CE1  . PHE   A 1 283 ? 374.684 -8.500  82.527  1.00 31.40  ? 262  PHE   A CE1  1 
ATOM   2081 C  CE2  . PHE   A 1 283 ? 376.212 -8.888  84.328  1.00 27.79  ? 262  PHE   A CE2  1 
ATOM   2082 C  CZ   . PHE   A 1 283 ? 375.012 -8.375  83.865  1.00 27.24  ? 262  PHE   A CZ   1 
ATOM   2083 N  N    . SER   A 1 284 ? 377.867 -7.101  79.772  1.00 31.91  ? 263  SER   A N    1 
ATOM   2084 C  CA   . SER   A 1 284 ? 378.333 -5.730  79.927  1.00 29.80  ? 263  SER   A CA   1 
ATOM   2085 C  C    . SER   A 1 284 ? 378.042 -5.134  81.297  1.00 31.52  ? 263  SER   A C    1 
ATOM   2086 O  O    . SER   A 1 284 ? 378.565 -4.056  81.603  1.00 34.46  ? 263  SER   A O    1 
ATOM   2087 C  CB   . SER   A 1 284 ? 377.681 -4.846  78.873  1.00 31.88  ? 263  SER   A CB   1 
ATOM   2088 O  OG   . SER   A 1 284 ? 376.288 -4.773  79.127  1.00 35.98  ? 263  SER   A OG   1 
ATOM   2089 N  N    . GLY   A 1 285 ? 377.214 -5.784  82.114  1.00 27.10  ? 264  GLY   A N    1 
ATOM   2090 C  CA   . GLY   A 1 285 ? 376.763 -5.228  83.371  1.00 25.67  ? 264  GLY   A CA   1 
ATOM   2091 C  C    . GLY   A 1 285 ? 375.375 -4.620  83.334  1.00 26.53  ? 264  GLY   A C    1 
ATOM   2092 O  O    . GLY   A 1 285 ? 374.839 -4.279  84.395  1.00 31.30  ? 264  GLY   A O    1 
ATOM   2093 N  N    . LEU   A 1 286 ? 374.776 -4.482  82.153  1.00 30.94  ? 265  LEU   A N    1 
ATOM   2094 C  CA   . LEU   A 1 286 ? 373.470 -3.853  82.008  1.00 23.32  ? 265  LEU   A CA   1 
ATOM   2095 C  C    . LEU   A 1 286 ? 372.368 -4.904  82.011  1.00 25.21  ? 265  LEU   A C    1 
ATOM   2096 O  O    . LEU   A 1 286 ? 372.431 -5.882  81.259  1.00 29.08  ? 265  LEU   A O    1 
ATOM   2097 C  CB   . LEU   A 1 286 ? 373.414 -3.039  80.715  1.00 25.59  ? 265  LEU   A CB   1 
ATOM   2098 C  CG   . LEU   A 1 286 ? 374.341 -1.826  80.687  1.00 31.62  ? 265  LEU   A CG   1 
ATOM   2099 C  CD1  . LEU   A 1 286 ? 374.295 -1.152  79.329  1.00 24.66  ? 265  LEU   A CD1  1 
ATOM   2100 C  CD2  . LEU   A 1 286 ? 373.939 -0.860  81.784  1.00 25.94  ? 265  LEU   A CD2  1 
ATOM   2101 N  N    . VAL   A 1 287 ? 371.353 -4.690  82.848  1.00 26.24  ? 266  VAL   A N    1 
ATOM   2102 C  CA   . VAL   A 1 287 ? 370.196 -5.572  82.927  1.00 27.89  ? 266  VAL   A CA   1 
ATOM   2103 C  C    . VAL   A 1 287 ? 368.934 -4.725  82.861  1.00 28.28  ? 266  VAL   A C    1 
ATOM   2104 O  O    . VAL   A 1 287 ? 368.900 -3.589  83.345  1.00 34.36  ? 266  VAL   A O    1 
ATOM   2105 C  CB   . VAL   A 1 287 ? 370.211 -6.441  84.207  1.00 29.09  ? 266  VAL   A CB   1 
ATOM   2106 C  CG1  . VAL   A 1 287 ? 371.426 -7.355  84.213  1.00 30.26  ? 266  VAL   A CG1  1 
ATOM   2107 C  CG2  . VAL   A 1 287 ? 370.190 -5.569  85.455  1.00 27.68  ? 266  VAL   A CG2  1 
ATOM   2108 N  N    . SER   A 1 288 ? 367.891 -5.284  82.248  1.00 27.52  ? 267  SER   A N    1 
ATOM   2109 C  CA   . SER   A 1 288 ? 366.626 -4.591  82.041  1.00 28.37  ? 267  SER   A CA   1 
ATOM   2110 C  C    . SER   A 1 288 ? 365.500 -5.329  82.746  1.00 26.29  ? 267  SER   A C    1 
ATOM   2111 O  O    . SER   A 1 288 ? 365.427 -6.561  82.699  1.00 31.43  ? 267  SER   A O    1 
ATOM   2112 C  CB   . SER   A 1 288 ? 366.291 -4.466  80.551  1.00 29.30  ? 267  SER   A CB   1 
ATOM   2113 O  OG   . SER   A 1 288 ? 367.126 -3.521  79.909  1.00 43.74  ? 267  SER   A OG   1 
ATOM   2114 N  N    . ILE   A 1 289 ? 364.621 -4.572  83.394  1.00 28.98  ? 268  ILE   A N    1 
ATOM   2115 C  CA   . ILE   A 1 289 ? 363.381 -5.099  83.943  1.00 27.84  ? 268  ILE   A CA   1 
ATOM   2116 C  C    . ILE   A 1 289 ? 362.232 -4.326  83.317  1.00 29.44  ? 268  ILE   A C    1 
ATOM   2117 O  O    . ILE   A 1 289 ? 362.314 -3.105  83.141  1.00 29.89  ? 268  ILE   A O    1 
ATOM   2118 C  CB   . ILE   A 1 289 ? 363.338 -5.012  85.482  1.00 30.70  ? 268  ILE   A CB   1 
ATOM   2119 C  CG1  . ILE   A 1 289 ? 364.599 -5.641  86.077  1.00 31.47  ? 268  ILE   A CG1  1 
ATOM   2120 C  CG2  . ILE   A 1 289 ? 362.092 -5.706  86.019  1.00 30.13  ? 268  ILE   A CG2  1 
ATOM   2121 C  CD1  . ILE   A 1 289 ? 364.647 -5.621  87.587  1.00 33.72  ? 268  ILE   A CD1  1 
ATOM   2122 N  N    . HIS   A 1 290 ? 361.172 -5.040  82.964  1.00 28.20  ? 269  HIS   A N    1 
ATOM   2123 C  CA   . HIS   A 1 290 ? 360.060 -4.466  82.230  1.00 27.15  ? 269  HIS   A CA   1 
ATOM   2124 C  C    . HIS   A 1 290 ? 358.768 -4.653  83.007  1.00 28.61  ? 269  HIS   A C    1 
ATOM   2125 O  O    . HIS   A 1 290 ? 358.624 -5.594  83.793  1.00 31.12  ? 269  HIS   A O    1 
ATOM   2126 C  CB   . HIS   A 1 290 ? 359.914 -5.108  80.845  1.00 32.98  ? 269  HIS   A CB   1 
ATOM   2127 C  CG   . HIS   A 1 290 ? 361.192 -5.169  80.070  1.00 29.28  ? 269  HIS   A CG   1 
ATOM   2128 N  ND1  . HIS   A 1 290 ? 361.667 -4.105  79.335  1.00 25.27  ? 269  HIS   A ND1  1 
ATOM   2129 C  CD2  . HIS   A 1 290 ? 362.095 -6.167  79.916  1.00 24.73  ? 269  HIS   A CD2  1 
ATOM   2130 C  CE1  . HIS   A 1 290 ? 362.807 -4.444  78.762  1.00 27.97  ? 269  HIS   A CE1  1 
ATOM   2131 N  NE2  . HIS   A 1 290 ? 363.090 -5.689  79.099  1.00 27.43  ? 269  HIS   A NE2  1 
ATOM   2132 N  N    . VAL   A 1 291 ? 357.832 -3.737  82.782  1.00 31.59  ? 270  VAL   A N    1 
ATOM   2133 C  CA   . VAL   A 1 291 ? 356.444 -3.915  83.183  1.00 32.08  ? 270  VAL   A CA   1 
ATOM   2134 C  C    . VAL   A 1 291 ? 355.585 -3.677  81.953  1.00 34.12  ? 270  VAL   A C    1 
ATOM   2135 O  O    . VAL   A 1 291 ? 355.796 -2.702  81.223  1.00 32.17  ? 270  VAL   A O    1 
ATOM   2136 C  CB   . VAL   A 1 291 ? 356.032 -2.967  84.324  1.00 28.12  ? 270  VAL   A CB   1 
ATOM   2137 C  CG1  . VAL   A 1 291 ? 356.003 -1.525  83.839  1.00 27.77  ? 270  VAL   A CG1  1 
ATOM   2138 C  CG2  . VAL   A 1 291 ? 354.677 -3.381  84.877  1.00 29.98  ? 270  VAL   A CG2  1 
ATOM   2139 N  N    . SER   A 1 292 ? 354.636 -4.572  81.711  1.00 31.12  ? 271  SER   A N    1 
ATOM   2140 C  CA   . SER   A 1 292 ? 353.728 -4.437  80.586  1.00 30.78  ? 271  SER   A CA   1 
ATOM   2141 C  C    . SER   A 1 292 ? 352.291 -4.515  81.066  1.00 30.74  ? 271  SER   A C    1 
ATOM   2142 O  O    . SER   A 1 292 ? 351.963 -5.300  81.961  1.00 32.06  ? 271  SER   A O    1 
ATOM   2143 C  CB   . SER   A 1 292 ? 353.966 -5.516  79.525  1.00 34.90  ? 271  SER   A CB   1 
ATOM   2144 O  OG   . SER   A 1 292 ? 354.963 -5.120  78.604  1.00 39.29  ? 271  SER   A OG   1 
ATOM   2145 N  N    . LEU   A 1 293 ? 351.442 -3.689  80.469  1.00 31.66  ? 272  LEU   A N    1 
ATOM   2146 C  CA   . LEU   A 1 293 ? 350.004 -3.879  80.546  1.00 32.00  ? 272  LEU   A CA   1 
ATOM   2147 C  C    . LEU   A 1 293 ? 349.603 -4.770  79.375  1.00 29.07  ? 272  LEU   A C    1 
ATOM   2148 O  O    . LEU   A 1 293 ? 349.832 -4.413  78.215  1.00 30.48  ? 272  LEU   A O    1 
ATOM   2149 C  CB   . LEU   A 1 293 ? 349.274 -2.538  80.503  1.00 27.80  ? 272  LEU   A CB   1 
ATOM   2150 C  CG   . LEU   A 1 293 ? 347.743 -2.559  80.514  1.00 30.57  ? 272  LEU   A CG   1 
ATOM   2151 C  CD1  . LEU   A 1 293 ? 347.182 -2.963  81.875  1.00 31.04  ? 272  LEU   A CD1  1 
ATOM   2152 C  CD2  . LEU   A 1 293 ? 347.185 -1.212  80.077  1.00 33.92  ? 272  LEU   A CD2  1 
ATOM   2153 N  N    . LEU   A 1 294 ? 349.046 -5.938  79.680  1.00 29.04  ? 273  LEU   A N    1 
ATOM   2154 C  CA   . LEU   A 1 294 ? 348.690 -6.933  78.679  1.00 34.35  ? 273  LEU   A CA   1 
ATOM   2155 C  C    . LEU   A 1 294 ? 347.182 -6.959  78.478  1.00 36.85  ? 273  LEU   A C    1 
ATOM   2156 O  O    . LEU   A 1 294 ? 346.418 -6.850  79.441  1.00 36.53  ? 273  LEU   A O    1 
ATOM   2157 C  CB   . LEU   A 1 294 ? 349.168 -8.327  79.092  1.00 35.05  ? 273  LEU   A CB   1 
ATOM   2158 C  CG   . LEU   A 1 294 ? 350.661 -8.528  79.333  1.00 34.88  ? 273  LEU   A CG   1 
ATOM   2159 C  CD1  . LEU   A 1 294 ? 350.944 -9.987  79.639  1.00 41.05  ? 273  LEU   A CD1  1 
ATOM   2160 C  CD2  . LEU   A 1 294 ? 351.450 -8.074  78.123  1.00 29.97  ? 273  LEU   A CD2  1 
ATOM   2161 N  N    . GLU   A 1 295 ? 346.755 -7.120  77.227  1.00 39.47  ? 274  GLU   A N    1 
ATOM   2162 C  CA   . GLU   A 1 295 ? 345.341 -7.223  76.893  1.00 44.24  ? 274  GLU   A CA   1 
ATOM   2163 C  C    . GLU   A 1 295 ? 345.012 -8.640  76.448  1.00 44.98  ? 274  GLU   A C    1 
ATOM   2164 O  O    . GLU   A 1 295 ? 345.688 -9.200  75.577  1.00 38.66  ? 274  GLU   A O    1 
ATOM   2165 C  CB   . GLU   A 1 295 ? 344.940 -6.230  75.799  1.00 40.28  ? 274  GLU   A CB   1 
ATOM   2166 C  CG   . GLU   A 1 295 ? 343.464 -6.327  75.426  1.00 44.49  ? 274  GLU   A CG   1 
ATOM   2167 C  CD   . GLU   A 1 295 ? 343.037 -5.297  74.400  1.00 50.11  ? 274  GLU   A CD   1 
ATOM   2168 O  OE1  . GLU   A 1 295 ? 343.740 -4.275  74.248  1.00 47.96  ? 274  GLU   A OE1  1 
ATOM   2169 O  OE2  . GLU   A 1 295 ? 341.994 -5.512  73.744  1.00 57.16  ? 274  GLU   A OE2  1 
ATOM   2170 N  N    . TYR   A 1 296 ? 343.970 -9.207  77.047  1.00 43.10  ? 275  TYR   A N    1 
ATOM   2171 C  CA   . TYR   A 1 296 ? 343.483 -10.529 76.681  1.00 46.15  ? 275  TYR   A CA   1 
ATOM   2172 C  C    . TYR   A 1 296 ? 342.672 -10.427 75.396  1.00 51.52  ? 275  TYR   A C    1 
ATOM   2173 O  O    . TYR   A 1 296 ? 341.625 -9.771  75.365  1.00 50.34  ? 275  TYR   A O    1 
ATOM   2174 C  CB   . TYR   A 1 296 ? 342.645 -11.103 77.821  1.00 50.38  ? 275  TYR   A CB   1 
ATOM   2175 C  CG   . TYR   A 1 296 ? 341.804 -12.304 77.455  1.00 52.94  ? 275  TYR   A CG   1 
ATOM   2176 C  CD1  . TYR   A 1 296 ? 340.511 -12.149 76.972  1.00 53.99  ? 275  TYR   A CD1  1 
ATOM   2177 C  CD2  . TYR   A 1 296 ? 342.295 -13.593 77.613  1.00 53.24  ? 275  TYR   A CD2  1 
ATOM   2178 C  CE1  . TYR   A 1 296 ? 339.736 -13.242 76.644  1.00 55.74  ? 275  TYR   A CE1  1 
ATOM   2179 C  CE2  . TYR   A 1 296 ? 341.526 -14.692 77.289  1.00 54.70  ? 275  TYR   A CE2  1 
ATOM   2180 C  CZ   . TYR   A 1 296 ? 340.248 -14.511 76.805  1.00 51.43  ? 275  TYR   A CZ   1 
ATOM   2181 O  OH   . TYR   A 1 296 ? 339.481 -15.607 76.482  1.00 65.46  ? 275  TYR   A OH   1 
ATOM   2182 N  N    . MET   A 1 297 ? 343.164 -11.065 74.335  1.00 52.73  ? 276  MET   A N    1 
ATOM   2183 C  CA   . MET   A 1 297 ? 342.495 -11.054 73.040  1.00 52.07  ? 276  MET   A CA   1 
ATOM   2184 C  C    . MET   A 1 297 ? 341.533 -12.228 72.893  1.00 56.96  ? 276  MET   A C    1 
ATOM   2185 O  O    . MET   A 1 297 ? 340.397 -12.053 72.444  1.00 58.64  ? 276  MET   A O    1 
ATOM   2186 C  CB   . MET   A 1 297 ? 343.539 -11.071 71.917  1.00 55.26  ? 276  MET   A CB   1 
ATOM   2187 C  CG   . MET   A 1 297 ? 344.461 -9.862  71.922  1.00 49.02  ? 276  MET   A CG   1 
ATOM   2188 S  SD   . MET   A 1 297 ? 343.613 -8.373  71.357  1.00 56.72  ? 276  MET   A SD   1 
ATOM   2189 C  CE   . MET   A 1 297 ? 344.624 -7.091  72.093  1.00 54.42  ? 276  MET   A CE   1 
ATOM   2190 N  N    . ALA   A 1 298 ? 341.971 -13.424 73.273  1.00 59.74  ? 277  ALA   A N    1 
ATOM   2191 C  CA   . ALA   A 1 298 ? 341.135 -14.615 73.205  1.00 56.25  ? 277  ALA   A CA   1 
ATOM   2192 C  C    . ALA   A 1 298 ? 341.981 -15.805 73.636  1.00 63.12  ? 277  ALA   A C    1 
ATOM   2193 O  O    . ALA   A 1 298 ? 343.200 -15.699 73.803  1.00 61.98  ? 277  ALA   A O    1 
ATOM   2194 C  CB   . ALA   A 1 298 ? 340.563 -14.835 71.803  1.00 50.61  ? 277  ALA   A CB   1 
ATOM   2195 N  N    . GLN   A 1 299 ? 341.314 -16.939 73.826  1.00 61.91  ? 278  GLN   A N    1 
ATOM   2196 C  CA   . GLN   A 1 299 ? 342.023 -18.178 74.107  1.00 69.18  ? 278  GLN   A CA   1 
ATOM   2197 C  C    . GLN   A 1 299 ? 342.821 -18.605 72.883  1.00 69.48  ? 278  GLN   A C    1 
ATOM   2198 O  O    . GLN   A 1 299 ? 342.339 -18.525 71.750  1.00 68.25  ? 278  GLN   A O    1 
ATOM   2199 C  CB   . GLN   A 1 299 ? 341.040 -19.276 74.509  1.00 80.78  ? 278  GLN   A CB   1 
ATOM   2200 N  N    . ASP   A 1 300 ? 344.051 -19.053 73.115  1.00 69.61  ? 279  ASP   A N    1 
ATOM   2201 C  CA   . ASP   A 1 300 ? 344.999 -19.507 72.106  1.00 70.06  ? 279  ASP   A CA   1 
ATOM   2202 C  C    . ASP   A 1 300 ? 345.745 -18.338 71.466  1.00 67.04  ? 279  ASP   A C    1 
ATOM   2203 O  O    . ASP   A 1 300 ? 346.693 -18.573 70.716  1.00 70.03  ? 279  ASP   A O    1 
ATOM   2204 C  CB   . ASP   A 1 300 ? 344.341 -20.349 70.995  1.00 74.91  ? 279  ASP   A CB   1 
ATOM   2205 C  CG   . ASP   A 1 300 ? 343.409 -21.414 71.545  1.00 78.30  ? 279  ASP   A CG   1 
ATOM   2206 O  OD1  . ASP   A 1 300 ? 343.731 -22.000 72.600  1.00 84.20  ? 279  ASP   A OD1  1 
ATOM   2207 O  OD2  . ASP   A 1 300 ? 342.352 -21.660 70.926  1.00 78.35  ? 279  ASP   A OD2  1 
ATOM   2208 N  N    . ILE   A 1 301 ? 345.353 -17.094 71.725  1.00 61.53  ? 280  ILE   A N    1 
ATOM   2209 C  CA   . ILE   A 1 301 ? 346.072 -15.930 71.216  1.00 57.43  ? 280  ILE   A CA   1 
ATOM   2210 C  C    . ILE   A 1 301 ? 346.975 -15.392 72.317  1.00 60.57  ? 280  ILE   A C    1 
ATOM   2211 O  O    . ILE   A 1 301 ? 346.582 -15.388 73.493  1.00 60.90  ? 280  ILE   A O    1 
ATOM   2212 C  CB   . ILE   A 1 301 ? 345.111 -14.836 70.729  1.00 56.76  ? 280  ILE   A CB   1 
ATOM   2213 C  CG1  . ILE   A 1 301 ? 344.120 -15.401 69.718  1.00 55.20  ? 280  ILE   A CG1  1 
ATOM   2214 C  CG2  . ILE   A 1 301 ? 345.895 -13.692 70.105  1.00 54.19  ? 280  ILE   A CG2  1 
ATOM   2215 C  CD1  . ILE   A 1 301 ? 344.740 -15.696 68.389  1.00 55.23  ? 280  ILE   A CD1  1 
ATOM   2216 N  N    . PRO   A 1 302 ? 348.176 -14.924 71.993  1.00 60.72  ? 281  PRO   A N    1 
ATOM   2217 C  CA   . PRO   A 1 302 ? 349.010 -14.285 73.014  1.00 55.56  ? 281  PRO   A CA   1 
ATOM   2218 C  C    . PRO   A 1 302 ? 348.418 -12.953 73.443  1.00 50.93  ? 281  PRO   A C    1 
ATOM   2219 O  O    . PRO   A 1 302 ? 347.785 -12.244 72.657  1.00 53.52  ? 281  PRO   A O    1 
ATOM   2220 C  CB   . PRO   A 1 302 ? 350.355 -14.095 72.305  1.00 59.79  ? 281  PRO   A CB   1 
ATOM   2221 C  CG   . PRO   A 1 302 ? 349.992 -13.999 70.852  1.00 55.43  ? 281  PRO   A CG   1 
ATOM   2222 C  CD   . PRO   A 1 302 ? 348.826 -14.937 70.671  1.00 58.57  ? 281  PRO   A CD   1 
ATOM   2223 N  N    . LEU   A 1 303 ? 348.621 -12.619 74.714  1.00 53.59  ? 282  LEU   A N    1 
ATOM   2224 C  CA   . LEU   A 1 303 ? 348.148 -11.338 75.215  1.00 49.91  ? 282  LEU   A CA   1 
ATOM   2225 C  C    . LEU   A 1 303 ? 348.953 -10.207 74.591  1.00 45.09  ? 282  LEU   A C    1 
ATOM   2226 O  O    . LEU   A 1 303 ? 350.172 -10.310 74.423  1.00 43.41  ? 282  LEU   A O    1 
ATOM   2227 C  CB   . LEU   A 1 303 ? 348.246 -11.281 76.738  1.00 50.15  ? 282  LEU   A CB   1 
ATOM   2228 C  CG   . LEU   A 1 303 ? 347.333 -12.242 77.501  1.00 49.93  ? 282  LEU   A CG   1 
ATOM   2229 C  CD1  . LEU   A 1 303 ? 347.845 -13.669 77.391  1.00 56.47  ? 282  LEU   A CD1  1 
ATOM   2230 C  CD2  . LEU   A 1 303 ? 347.205 -11.817 78.955  1.00 44.83  ? 282  LEU   A CD2  1 
ATOM   2231 N  N    . THR   A 1 304 ? 348.264 -9.125  74.240  1.00 45.66  ? 283  THR   A N    1 
ATOM   2232 C  CA   . THR   A 1 304 ? 348.923 -8.030  73.538  1.00 45.47  ? 283  THR   A CA   1 
ATOM   2233 C  C    . THR   A 1 304 ? 349.529 -7.053  74.536  1.00 41.72  ? 283  THR   A C    1 
ATOM   2234 O  O    . THR   A 1 304 ? 348.827 -6.591  75.443  1.00 39.44  ? 283  THR   A O    1 
ATOM   2235 C  CB   . THR   A 1 304 ? 347.945 -7.287  72.636  1.00 45.96  ? 283  THR   A CB   1 
ATOM   2236 O  OG1  . THR   A 1 304 ? 347.418 -8.186  71.653  1.00 55.01  ? 283  THR   A OG1  1 
ATOM   2237 C  CG2  . THR   A 1 304 ? 348.646 -6.131  71.935  1.00 37.55  ? 283  THR   A CG2  1 
ATOM   2238 N  N    . PRO   A 1 305 ? 350.813 -6.719  74.408  1.00 40.05  ? 284  PRO   A N    1 
ATOM   2239 C  CA   . PRO   A 1 305 ? 351.378 -5.657  75.245  1.00 38.12  ? 284  PRO   A CA   1 
ATOM   2240 C  C    . PRO   A 1 305 ? 350.965 -4.295  74.717  1.00 36.66  ? 284  PRO   A C    1 
ATOM   2241 O  O    . PRO   A 1 305 ? 351.531 -3.814  73.731  1.00 43.72  ? 284  PRO   A O    1 
ATOM   2242 C  CB   . PRO   A 1 305 ? 352.895 -5.870  75.128  1.00 34.08  ? 284  PRO   A CB   1 
ATOM   2243 C  CG   . PRO   A 1 305 ? 353.084 -7.102  74.268  1.00 38.05  ? 284  PRO   A CG   1 
ATOM   2244 C  CD   . PRO   A 1 305 ? 351.818 -7.281  73.494  1.00 35.59  ? 284  PRO   A CD   1 
ATOM   2245 N  N    . ILE   A 1 306 ? 349.965 -3.669  75.343  1.00 37.04  ? 285  ILE   A N    1 
ATOM   2246 C  CA   . ILE   A 1 306 ? 349.511 -2.363  74.873  1.00 39.42  ? 285  ILE   A CA   1 
ATOM   2247 C  C    . ILE   A 1 306 ? 350.290 -1.219  75.502  1.00 39.12  ? 285  ILE   A C    1 
ATOM   2248 O  O    . ILE   A 1 306 ? 350.190 -0.077  75.025  1.00 37.93  ? 285  ILE   A O    1 
ATOM   2249 C  CB   . ILE   A 1 306 ? 348.001 -2.190  75.122  1.00 42.49  ? 285  ILE   A CB   1 
ATOM   2250 C  CG1  . ILE   A 1 306 ? 347.709 -1.997  76.607  1.00 33.83  ? 285  ILE   A CG1  1 
ATOM   2251 C  CG2  . ILE   A 1 306 ? 347.234 -3.399  74.603  1.00 41.54  ? 285  ILE   A CG2  1 
ATOM   2252 C  CD1  . ILE   A 1 306 ? 346.235 -1.900  76.900  1.00 41.45  ? 285  ILE   A CD1  1 
ATOM   2253 N  N    . PHE   A 1 307 ? 351.068 -1.486  76.549  1.00 38.78  ? 286  PHE   A N    1 
ATOM   2254 C  CA   . PHE   A 1 307 ? 351.936 -0.489  77.157  1.00 35.70  ? 286  PHE   A CA   1 
ATOM   2255 C  C    . PHE   A 1 307 ? 353.082 -1.205  77.852  1.00 33.94  ? 286  PHE   A C    1 
ATOM   2256 O  O    . PHE   A 1 307 ? 352.863 -2.197  78.553  1.00 32.00  ? 286  PHE   A O    1 
ATOM   2257 C  CB   . PHE   A 1 307 ? 351.188 0.392   78.165  1.00 33.97  ? 286  PHE   A CB   1 
ATOM   2258 C  CG   . PHE   A 1 307 ? 352.089 1.319   78.934  1.00 34.61  ? 286  PHE   A CG   1 
ATOM   2259 C  CD1  . PHE   A 1 307 ? 352.428 2.558   78.418  1.00 41.05  ? 286  PHE   A CD1  1 
ATOM   2260 C  CD2  . PHE   A 1 307 ? 352.616 0.942   80.160  1.00 38.64  ? 286  PHE   A CD2  1 
ATOM   2261 C  CE1  . PHE   A 1 307 ? 353.266 3.414   79.115  1.00 41.30  ? 286  PHE   A CE1  1 
ATOM   2262 C  CE2  . PHE   A 1 307 ? 353.455 1.792   80.864  1.00 35.65  ? 286  PHE   A CE2  1 
ATOM   2263 C  CZ   . PHE   A 1 307 ? 353.781 3.029   80.339  1.00 36.70  ? 286  PHE   A CZ   1 
ATOM   2264 N  N    . THR   A 1 308 ? 354.296 -0.687  77.665  1.00 33.94  ? 287  THR   A N    1 
ATOM   2265 C  CA   . THR   A 1 308 ? 355.488 -1.263  78.270  1.00 34.07  ? 287  THR   A CA   1 
ATOM   2266 C  C    . THR   A 1 308 ? 356.370 -0.158  78.826  1.00 35.49  ? 287  THR   A C    1 
ATOM   2267 O  O    . THR   A 1 308 ? 356.721 0.781   78.106  1.00 34.17  ? 287  THR   A O    1 
ATOM   2268 C  CB   . THR   A 1 308 ? 356.280 -2.098  77.255  1.00 30.26  ? 287  THR   A CB   1 
ATOM   2269 O  OG1  . THR   A 1 308 ? 355.462 -3.177  76.785  1.00 33.43  ? 287  THR   A OG1  1 
ATOM   2270 C  CG2  . THR   A 1 308 ? 357.548 -2.662  77.887  1.00 28.55  ? 287  THR   A CG2  1 
ATOM   2271 N  N    . ASP   A 1 309 ? 356.721 -0.277  80.103  1.00 37.97  ? 288  ASP   A N    1 
ATOM   2272 C  CA   . ASP   A 1 309 ? 357.697 0.588   80.749  1.00 34.86  ? 288  ASP   A CA   1 
ATOM   2273 C  C    . ASP   A 1 309 ? 358.932 -0.239  81.091  1.00 31.15  ? 288  ASP   A C    1 
ATOM   2274 O  O    . ASP   A 1 309 ? 358.819 -1.417  81.443  1.00 34.29  ? 288  ASP   A O    1 
ATOM   2275 C  CB   . ASP   A 1 309 ? 357.108 1.228   82.011  1.00 37.70  ? 288  ASP   A CB   1 
ATOM   2276 C  CG   . ASP   A 1 309 ? 357.760 2.552   82.355  1.00 34.71  ? 288  ASP   A CG   1 
ATOM   2277 O  OD1  . ASP   A 1 309 ? 358.408 3.151   81.471  1.00 36.93  ? 288  ASP   A OD1  1 
ATOM   2278 O  OD2  . ASP   A 1 309 ? 357.621 2.994   83.518  1.00 31.37  ? 288  ASP   A OD2  1 
ATOM   2279 N  N    . THR   A 1 310 ? 360.111 0.376   80.978  1.00 30.73  ? 289  THR   A N    1 
ATOM   2280 C  CA   . THR   A 1 310 ? 361.387 -0.315  81.125  1.00 33.33  ? 289  THR   A CA   1 
ATOM   2281 C  C    . THR   A 1 310 ? 362.327 0.480   82.019  1.00 32.55  ? 289  THR   A C    1 
ATOM   2282 O  O    . THR   A 1 310 ? 362.400 1.709   81.928  1.00 29.08  ? 289  THR   A O    1 
ATOM   2283 C  CB   . THR   A 1 310 ? 362.064 -0.547  79.757  1.00 29.08  ? 289  THR   A CB   1 
ATOM   2284 O  OG1  . THR   A 1 310 ? 361.329 -1.525  79.010  1.00 31.58  ? 289  THR   A OG1  1 
ATOM   2285 C  CG2  . THR   A 1 310 ? 363.508 -1.023  79.932  1.00 29.58  ? 289  THR   A CG2  1 
ATOM   2286 N  N    . VAL   A 1 311 ? 363.050 -0.235  82.877  1.00 30.96  ? 290  VAL   A N    1 
ATOM   2287 C  CA   . VAL   A 1 311 ? 364.131 0.330   83.670  1.00 26.49  ? 290  VAL   A CA   1 
ATOM   2288 C  C    . VAL   A 1 311 ? 365.374 -0.507  83.427  1.00 34.33  ? 290  VAL   A C    1 
ATOM   2289 O  O    . VAL   A 1 311 ? 365.294 -1.719  83.205  1.00 30.88  ? 290  VAL   A O    1 
ATOM   2290 C  CB   . VAL   A 1 311 ? 363.802 0.370   85.179  1.00 28.98  ? 290  VAL   A CB   1 
ATOM   2291 C  CG1  . VAL   A 1 311 ? 362.615 1.281   85.454  1.00 29.45  ? 290  VAL   A CG1  1 
ATOM   2292 C  CG2  . VAL   A 1 311 ? 363.544 -1.035  85.692  1.00 27.25  ? 290  VAL   A CG2  1 
ATOM   2293 N  N    . ILE   A 1 312 ? 366.529 0.146   83.469  1.00 29.36  ? 291  ILE   A N    1 
ATOM   2294 C  CA   . ILE   A 1 312 ? 367.812 -0.516  83.290  1.00 31.47  ? 291  ILE   A CA   1 
ATOM   2295 C  C    . ILE   A 1 312 ? 368.637 -0.331  84.554  1.00 30.06  ? 291  ILE   A C    1 
ATOM   2296 O  O    . ILE   A 1 312 ? 368.554 0.709   85.216  1.00 32.09  ? 291  ILE   A O    1 
ATOM   2297 C  CB   . ILE   A 1 312 ? 368.560 0.024   82.054  1.00 31.00  ? 291  ILE   A CB   1 
ATOM   2298 C  CG1  . ILE   A 1 312 ? 367.871 -0.456  80.775  1.00 34.73  ? 291  ILE   A CG1  1 
ATOM   2299 C  CG2  . ILE   A 1 312 ? 370.014 -0.406  82.067  1.00 37.61  ? 291  ILE   A CG2  1 
ATOM   2300 C  CD1  . ILE   A 1 312 ? 368.680 -0.215  79.529  1.00 51.25  ? 291  ILE   A CD1  1 
ATOM   2301 N  N    . PHE   A 1 313 ? 369.407 -1.358  84.900  1.00 30.10  ? 292  PHE   A N    1 
ATOM   2302 C  CA   . PHE   A 1 313 ? 370.384 -1.303  85.977  1.00 28.14  ? 292  PHE   A CA   1 
ATOM   2303 C  C    . PHE   A 1 313 ? 371.756 -1.600  85.398  1.00 25.56  ? 292  PHE   A C    1 
ATOM   2304 O  O    . PHE   A 1 313 ? 371.886 -2.421  84.484  1.00 26.09  ? 292  PHE   A O    1 
ATOM   2305 C  CB   . PHE   A 1 313 ? 370.085 -2.328  87.083  1.00 27.94  ? 292  PHE   A CB   1 
ATOM   2306 C  CG   . PHE   A 1 313 ? 368.893 -1.996  87.932  1.00 29.34  ? 292  PHE   A CG   1 
ATOM   2307 C  CD1  . PHE   A 1 313 ? 369.015 -1.143  89.016  1.00 30.97  ? 292  PHE   A CD1  1 
ATOM   2308 C  CD2  . PHE   A 1 313 ? 367.656 -2.561  87.666  1.00 28.07  ? 292  PHE   A CD2  1 
ATOM   2309 C  CE1  . PHE   A 1 313 ? 367.922 -0.845  89.803  1.00 30.56  ? 292  PHE   A CE1  1 
ATOM   2310 C  CE2  . PHE   A 1 313 ? 366.560 -2.265  88.453  1.00 27.41  ? 292  PHE   A CE2  1 
ATOM   2311 C  CZ   . PHE   A 1 313 ? 366.693 -1.406  89.522  1.00 26.81  ? 292  PHE   A CZ   1 
ATOM   2312 N  N    . ARG   A 1 314 ? 372.781 -0.939  85.922  1.00 27.67  ? 293  ARG   A N    1 
ATOM   2313 C  CA   . ARG   A 1 314 ? 374.150 -1.373  85.690  1.00 25.67  ? 293  ARG   A CA   1 
ATOM   2314 C  C    . ARG   A 1 314 ? 374.647 -2.057  86.953  1.00 27.91  ? 293  ARG   A C    1 
ATOM   2315 O  O    . ARG   A 1 314 ? 374.600 -1.474  88.041  1.00 27.46  ? 293  ARG   A O    1 
ATOM   2316 C  CB   . ARG   A 1 314 ? 375.086 -0.231  85.306  1.00 26.98  ? 293  ARG   A CB   1 
ATOM   2317 C  CG   . ARG   A 1 314 ? 376.493 -0.766  85.096  1.00 27.88  ? 293  ARG   A CG   1 
ATOM   2318 C  CD   . ARG   A 1 314 ? 377.460 0.263   84.571  1.00 28.43  ? 293  ARG   A CD   1 
ATOM   2319 N  NE   . ARG   A 1 314 ? 377.291 0.511   83.145  1.00 34.39  ? 293  ARG   A NE   1 
ATOM   2320 C  CZ   . ARG   A 1 314 ? 377.712 -0.302  82.184  1.00 30.91  ? 293  ARG   A CZ   1 
ATOM   2321 N  NH1  . ARG   A 1 314 ? 378.269 -1.470  82.460  1.00 29.78  ? 293  ARG   A NH1  1 
ATOM   2322 N  NH2  . ARG   A 1 314 ? 377.570 0.068   80.915  1.00 31.08  ? 293  ARG   A NH2  1 
ATOM   2323 N  N    . ILE   A 1 315 ? 375.113 -3.294  86.804  1.00 29.45  ? 294  ILE   A N    1 
ATOM   2324 C  CA   . ILE   A 1 315 ? 375.715 -4.001  87.924  1.00 27.24  ? 294  ILE   A CA   1 
ATOM   2325 C  C    . ILE   A 1 315 ? 377.079 -3.390  88.212  1.00 22.91  ? 294  ILE   A C    1 
ATOM   2326 O  O    . ILE   A 1 315 ? 377.882 -3.155  87.298  1.00 24.00  ? 294  ILE   A O    1 
ATOM   2327 C  CB   . ILE   A 1 315 ? 375.793 -5.506  87.625  1.00 27.48  ? 294  ILE   A CB   1 
ATOM   2328 C  CG1  . ILE   A 1 315 ? 374.380 -6.099  87.651  1.00 30.85  ? 294  ILE   A CG1  1 
ATOM   2329 C  CG2  . ILE   A 1 315 ? 376.696 -6.220  88.618  1.00 27.57  ? 294  ILE   A CG2  1 
ATOM   2330 C  CD1  . ILE   A 1 315 ? 374.325 -7.596  87.500  1.00 37.75  ? 294  ILE   A CD1  1 
ATOM   2331 N  N    . ALA   A 1 316 ? 377.325 -3.086  89.481  1.00 27.60  ? 295  ALA   A N    1 
ATOM   2332 C  CA   . ALA   A 1 316 ? 378.536 -2.376  89.857  1.00 25.86  ? 295  ALA   A CA   1 
ATOM   2333 C  C    . ALA   A 1 316 ? 379.762 -3.258  89.627  1.00 24.73  ? 295  ALA   A C    1 
ATOM   2334 O  O    . ALA   A 1 316 ? 379.740 -4.449  89.952  1.00 29.05  ? 295  ALA   A O    1 
ATOM   2335 C  CB   . ALA   A 1 316 ? 378.461 -1.946  91.322  1.00 25.08  ? 295  ALA   A CB   1 
ATOM   2336 N  N    . PRO   A 1 317 ? 380.843 -2.710  89.080  1.00 22.53  ? 296  PRO   A N    1 
ATOM   2337 C  CA   . PRO   A 1 317 ? 382.043 -3.517  88.846  1.00 27.15  ? 296  PRO   A CA   1 
ATOM   2338 C  C    . PRO   A 1 317 ? 382.828 -3.754  90.128  1.00 25.49  ? 296  PRO   A C    1 
ATOM   2339 O  O    . PRO   A 1 317 ? 382.669 -3.061  91.133  1.00 27.24  ? 296  PRO   A O    1 
ATOM   2340 C  CB   . PRO   A 1 317 ? 382.850 -2.663  87.864  1.00 22.26  ? 296  PRO   A CB   1 
ATOM   2341 C  CG   . PRO   A 1 317 ? 382.486 -1.268  88.239  1.00 25.00  ? 296  PRO   A CG   1 
ATOM   2342 C  CD   . PRO   A 1 317 ? 381.025 -1.317  88.625  1.00 21.02  ? 296  PRO   A CD   1 
ATOM   2343 N  N    . TRP   A 1 318 ? 383.691 -4.764  90.072  1.00 23.78  ? 297  TRP   A N    1 
ATOM   2344 C  CA   . TRP   A 1 318 ? 384.619 -5.032  91.161  1.00 27.28  ? 297  TRP   A CA   1 
ATOM   2345 C  C    . TRP   A 1 318 ? 385.828 -4.115  91.024  1.00 24.56  ? 297  TRP   A C    1 
ATOM   2346 O  O    . TRP   A 1 318 ? 386.451 -4.059  89.960  1.00 26.97  ? 297  TRP   A O    1 
ATOM   2347 C  CB   . TRP   A 1 318 ? 385.044 -6.499  91.138  1.00 28.19  ? 297  TRP   A CB   1 
ATOM   2348 C  CG   . TRP   A 1 318 ? 385.954 -6.897  92.251  1.00 29.44  ? 297  TRP   A CG   1 
ATOM   2349 C  CD1  . TRP   A 1 318 ? 385.616 -7.090  93.558  1.00 30.61  ? 297  TRP   A CD1  1 
ATOM   2350 C  CD2  . TRP   A 1 318 ? 387.356 -7.176  92.154  1.00 29.39  ? 297  TRP   A CD2  1 
ATOM   2351 N  NE1  . TRP   A 1 318 ? 386.723 -7.461  94.283  1.00 33.85  ? 297  TRP   A NE1  1 
ATOM   2352 C  CE2  . TRP   A 1 318 ? 387.804 -7.522  93.444  1.00 34.34  ? 297  TRP   A CE2  1 
ATOM   2353 C  CE3  . TRP   A 1 318 ? 388.278 -7.161  91.101  1.00 30.46  ? 297  TRP   A CE3  1 
ATOM   2354 C  CZ2  . TRP   A 1 318 ? 389.131 -7.851  93.711  1.00 36.59  ? 297  TRP   A CZ2  1 
ATOM   2355 C  CZ3  . TRP   A 1 318 ? 389.595 -7.489  91.368  1.00 36.17  ? 297  TRP   A CZ3  1 
ATOM   2356 C  CH2  . TRP   A 1 318 ? 390.009 -7.828  92.661  1.00 34.99  ? 297  TRP   A CH2  1 
ATOM   2357 N  N    . ILE   A 1 319 ? 386.157 -3.384  92.087  1.00 24.45  ? 298  ILE   A N    1 
ATOM   2358 C  CA   . ILE   A 1 319 ? 387.212 -2.377  92.033  1.00 25.40  ? 298  ILE   A CA   1 
ATOM   2359 C  C    . ILE   A 1 319 ? 388.322 -2.755  93.005  1.00 28.39  ? 298  ILE   A C    1 
ATOM   2360 O  O    . ILE   A 1 319 ? 388.051 -3.120  94.155  1.00 30.04  ? 298  ILE   A O    1 
ATOM   2361 C  CB   . ILE   A 1 319 ? 386.673 -0.967  92.341  1.00 25.94  ? 298  ILE   A CB   1 
ATOM   2362 C  CG1  . ILE   A 1 319 ? 385.503 -0.619  91.414  1.00 25.53  ? 298  ILE   A CG1  1 
ATOM   2363 C  CG2  . ILE   A 1 319 ? 387.779 0.054   92.173  1.00 25.42  ? 298  ILE   A CG2  1 
ATOM   2364 C  CD1  . ILE   A 1 319 ? 384.722 0.618   91.843  1.00 24.28  ? 298  ILE   A CD1  1 
ATOM   2365 N  N    . MET   A 1 320 ? 389.567 -2.652  92.541  1.00 31.96  ? 299  MET   A N    1 
ATOM   2366 C  CA   . MET   A 1 320 ? 390.741 -2.908  93.363  1.00 29.98  ? 299  MET   A CA   1 
ATOM   2367 C  C    . MET   A 1 320 ? 391.263 -1.609  93.965  1.00 28.59  ? 299  MET   A C    1 
ATOM   2368 O  O    . MET   A 1 320 ? 391.072 -0.524  93.411  1.00 29.75  ? 299  MET   A O    1 
ATOM   2369 C  CB   . MET   A 1 320 ? 391.842 -3.580  92.542  1.00 27.95  ? 299  MET   A CB   1 
ATOM   2370 C  CG   . MET   A 1 320 ? 391.519 -4.995  92.117  1.00 35.88  ? 299  MET   A CG   1 
ATOM   2371 S  SD   . MET   A 1 320 ? 392.831 -5.707  91.115  1.00 46.01  ? 299  MET   A SD   1 
ATOM   2372 C  CE   . MET   A 1 320 ? 394.273 -5.241  92.067  1.00 35.28  ? 299  MET   A CE   1 
ATOM   2373 N  N    . THR   A 1 321 ? 391.941 -1.733  95.107  1.00 28.10  ? 300  THR   A N    1 
ATOM   2374 C  CA   . THR   A 1 321 ? 392.368 -0.573  95.881  1.00 27.88  ? 300  THR   A CA   1 
ATOM   2375 C  C    . THR   A 1 321 ? 393.883 -0.444  95.863  1.00 31.85  ? 300  THR   A C    1 
ATOM   2376 O  O    . THR   A 1 321 ? 394.582 -1.339  96.360  1.00 31.16  ? 300  THR   A O    1 
ATOM   2377 C  CB   . THR   A 1 321 ? 391.864 -0.681  97.318  1.00 30.00  ? 300  THR   A CB   1 
ATOM   2378 O  OG1  . THR   A 1 321 ? 392.230 -1.959  97.854  1.00 33.53  ? 300  THR   A OG1  1 
ATOM   2379 C  CG2  . THR   A 1 321 ? 390.346 -0.526  97.367  1.00 28.52  ? 300  THR   A CG2  1 
ATOM   2380 N  N    . PRO   A 1 322 ? 394.431 0.638   95.318  1.00 30.79  ? 301  PRO   A N    1 
ATOM   2381 C  CA   . PRO   A 1 322 ? 395.886 0.817   95.321  1.00 29.81  ? 301  PRO   A CA   1 
ATOM   2382 C  C    . PRO   A 1 322 ? 396.404 1.164   96.710  1.00 34.41  ? 301  PRO   A C    1 
ATOM   2383 O  O    . PRO   A 1 322 ? 395.657 1.526   97.622  1.00 33.30  ? 301  PRO   A O    1 
ATOM   2384 C  CB   . PRO   A 1 322 ? 396.107 1.966   94.333  1.00 29.72  ? 301  PRO   A CB   1 
ATOM   2385 C  CG   . PRO   A 1 322 ? 394.826 2.731   94.362  1.00 31.01  ? 301  PRO   A CG   1 
ATOM   2386 C  CD   . PRO   A 1 322 ? 393.734 1.729   94.616  1.00 31.04  ? 301  PRO   A CD   1 
ATOM   2387 N  N    . ASN   A 1 323 ? 397.732 1.056   96.846  1.00 39.37  ? 302  ASN   A N    1 
ATOM   2388 C  CA   . ASN   A 1 323 ? 398.408 1.257   98.126  1.00 37.47  ? 302  ASN   A CA   1 
ATOM   2389 C  C    . ASN   A 1 323 ? 398.288 2.682   98.654  1.00 40.35  ? 302  ASN   A C    1 
ATOM   2390 O  O    . ASN   A 1 323 ? 398.591 2.921   99.829  1.00 38.08  ? 302  ASN   A O    1 
ATOM   2391 C  CB   . ASN   A 1 323 ? 399.891 0.905   97.999  1.00 38.67  ? 302  ASN   A CB   1 
ATOM   2392 C  CG   . ASN   A 1 323 ? 400.117 -0.554  97.668  1.00 40.37  ? 302  ASN   A CG   1 
ATOM   2393 O  OD1  . ASN   A 1 323 ? 399.297 -1.410  97.995  1.00 46.06  ? 302  ASN   A OD1  1 
ATOM   2394 N  ND2  . ASN   A 1 323 ? 401.241 -0.848  97.021  1.00 45.80  ? 302  ASN   A ND2  1 
ATOM   2395 N  N    . ILE   A 1 324 ? 397.887 3.643   97.815  1.00 34.78  ? 303  ILE   A N    1 
ATOM   2396 C  CA   . ILE   A 1 324 ? 397.735 5.017   98.294  1.00 38.81  ? 303  ILE   A CA   1 
ATOM   2397 C  C    . ILE   A 1 324 ? 396.452 5.223   99.082  1.00 42.15  ? 303  ILE   A C    1 
ATOM   2398 O  O    . ILE   A 1 324 ? 396.267 6.295   99.675  1.00 44.25  ? 303  ILE   A O    1 
ATOM   2399 C  CB   . ILE   A 1 324 ? 397.793 6.031   97.133  1.00 36.57  ? 303  ILE   A CB   1 
ATOM   2400 C  CG1  . ILE   A 1 324 ? 396.664 5.788   96.129  1.00 33.77  ? 303  ILE   A CG1  1 
ATOM   2401 C  CG2  . ILE   A 1 324 ? 399.150 5.981   96.444  1.00 34.64  ? 303  ILE   A CG2  1 
ATOM   2402 C  CD1  . ILE   A 1 324 ? 395.443 6.652   96.365  1.00 39.27  ? 303  ILE   A CD1  1 
ATOM   2403 N  N    . LEU   A 1 325 ? 395.562 4.228   99.121  1.00 39.52  ? 304  LEU   A N    1 
ATOM   2404 C  CA   . LEU   A 1 325 ? 394.314 4.409   99.850  1.00 36.09  ? 304  LEU   A CA   1 
ATOM   2405 C  C    . LEU   A 1 325 ? 394.511 4.092   101.331 1.00 40.91  ? 304  LEU   A C    1 
ATOM   2406 O  O    . LEU   A 1 325 ? 395.244 3.160   101.675 1.00 39.90  ? 304  LEU   A O    1 
ATOM   2407 C  CB   . LEU   A 1 325 ? 393.215 3.526   99.262  1.00 32.97  ? 304  LEU   A CB   1 
ATOM   2408 C  CG   . LEU   A 1 325 ? 392.741 3.983   97.884  1.00 33.91  ? 304  LEU   A CG   1 
ATOM   2409 C  CD1  . LEU   A 1 325 ? 391.743 3.003   97.285  1.00 30.60  ? 304  LEU   A CD1  1 
ATOM   2410 C  CD2  . LEU   A 1 325 ? 392.139 5.375   97.987  1.00 37.75  ? 304  LEU   A CD2  1 
ATOM   2411 N  N    . PRO   A 1 326 ? 393.869 4.844   102.221 1.00 41.37  ? 305  PRO   A N    1 
ATOM   2412 C  CA   . PRO   A 1 326 ? 394.104 4.668   103.660 1.00 39.73  ? 305  PRO   A CA   1 
ATOM   2413 C  C    . PRO   A 1 326 ? 393.816 3.242   104.086 1.00 41.33  ? 305  PRO   A C    1 
ATOM   2414 O  O    . PRO   A 1 326 ? 392.781 2.669   103.711 1.00 41.16  ? 305  PRO   A O    1 
ATOM   2415 C  CB   . PRO   A 1 326 ? 393.118 5.654   104.307 1.00 41.79  ? 305  PRO   A CB   1 
ATOM   2416 C  CG   . PRO   A 1 326 ? 392.784 6.636   103.227 1.00 48.24  ? 305  PRO   A CG   1 
ATOM   2417 C  CD   . PRO   A 1 326 ? 392.841 5.862   101.946 1.00 41.81  ? 305  PRO   A CD   1 
ATOM   2418 N  N    . PRO   A 1 327 ? 394.707 2.628   104.862 1.00 41.37  ? 306  PRO   A N    1 
ATOM   2419 C  CA   . PRO   A 1 327 ? 394.471 1.249   105.300 1.00 42.39  ? 306  PRO   A CA   1 
ATOM   2420 C  C    . PRO   A 1 327 ? 393.460 1.193   106.433 1.00 44.86  ? 306  PRO   A C    1 
ATOM   2421 O  O    . PRO   A 1 327 ? 393.465 2.023   107.344 1.00 45.46  ? 306  PRO   A O    1 
ATOM   2422 C  CB   . PRO   A 1 327 ? 395.857 0.786   105.765 1.00 38.02  ? 306  PRO   A CB   1 
ATOM   2423 C  CG   . PRO   A 1 327 ? 396.518 2.039   106.223 1.00 37.48  ? 306  PRO   A CG   1 
ATOM   2424 C  CD   . PRO   A 1 327 ? 396.014 3.137   105.316 1.00 41.38  ? 306  PRO   A CD   1 
ATOM   2425 N  N    . VAL   A 1 328 ? 392.578 0.204   106.361 1.00 43.29  ? 307  VAL   A N    1 
ATOM   2426 C  CA   . VAL   A 1 328 ? 391.604 -0.049  107.415 1.00 48.26  ? 307  VAL   A CA   1 
ATOM   2427 C  C    . VAL   A 1 328 ? 392.076 -1.153  108.345 1.00 45.12  ? 307  VAL   A C    1 
ATOM   2428 O  O    . VAL   A 1 328 ? 392.118 -0.978  109.563 1.00 56.28  ? 307  VAL   A O    1 
ATOM   2429 C  CB   . VAL   A 1 328 ? 390.224 -0.382  106.805 1.00 49.74  ? 307  VAL   A CB   1 
ATOM   2430 C  CG1  . VAL   A 1 328 ? 389.290 -0.916  107.879 1.00 52.47  ? 307  VAL   A CG1  1 
ATOM   2431 C  CG2  . VAL   A 1 328 ? 389.629 0.848   106.143 1.00 48.95  ? 307  VAL   A CG2  1 
ATOM   2432 N  N    . SER   A 1 329 ? 392.446 -2.298  107.783 1.00 50.30  ? 308  SER   A N    1 
ATOM   2433 C  CA   . SER   A 1 329 ? 392.888 -3.429  108.578 1.00 53.38  ? 308  SER   A CA   1 
ATOM   2434 C  C    . SER   A 1 329 ? 393.830 -4.274  107.736 1.00 45.92  ? 308  SER   A C    1 
ATOM   2435 O  O    . SER   A 1 329 ? 393.690 -4.356  106.513 1.00 39.83  ? 308  SER   A O    1 
ATOM   2436 C  CB   . SER   A 1 329 ? 391.699 -4.258  109.074 1.00 61.09  ? 308  SER   A CB   1 
ATOM   2437 O  OG   . SER   A 1 329 ? 390.766 -4.486  108.031 1.00 54.32  ? 308  SER   A OG   1 
ATOM   2438 N  N    . VAL   A 1 330 ? 394.796 -4.892  108.406 1.00 48.53  ? 309  VAL   A N    1 
ATOM   2439 C  CA   . VAL   A 1 330 ? 395.834 -5.685  107.760 1.00 46.95  ? 309  VAL   A CA   1 
ATOM   2440 C  C    . VAL   A 1 330 ? 395.552 -7.154  108.032 1.00 49.69  ? 309  VAL   A C    1 
ATOM   2441 O  O    . VAL   A 1 330 ? 395.408 -7.561  109.192 1.00 46.43  ? 309  VAL   A O    1 
ATOM   2442 C  CB   . VAL   A 1 330 ? 397.232 -5.290  108.264 1.00 44.93  ? 309  VAL   A CB   1 
ATOM   2443 C  CG1  . VAL   A 1 330 ? 398.310 -6.034  107.491 1.00 47.90  ? 309  VAL   A CG1  1 
ATOM   2444 C  CG2  . VAL   A 1 330 ? 397.422 -3.783  108.164 1.00 41.97  ? 309  VAL   A CG2  1 
ATOM   2445 N  N    . PHE   A 1 331 ? 395.470 -7.946  106.969 1.00 48.08  ? 310  PHE   A N    1 
ATOM   2446 C  CA   . PHE   A 1 331 ? 395.292 -9.386  107.082 1.00 50.32  ? 310  PHE   A CA   1 
ATOM   2447 C  C    . PHE   A 1 331 ? 396.648 -10.057 106.915 1.00 48.46  ? 310  PHE   A C    1 
ATOM   2448 O  O    . PHE   A 1 331 ? 397.381 -9.758  105.967 1.00 50.54  ? 310  PHE   A O    1 
ATOM   2449 C  CB   . PHE   A 1 331 ? 394.302 -9.907  106.037 1.00 53.33  ? 310  PHE   A CB   1 
ATOM   2450 C  CG   . PHE   A 1 331 ? 393.512 -11.105 106.492 1.00 60.84  ? 310  PHE   A CG   1 
ATOM   2451 C  CD1  . PHE   A 1 331 ? 394.103 -12.357 106.572 1.00 69.49  ? 310  PHE   A CD1  1 
ATOM   2452 C  CD2  . PHE   A 1 331 ? 392.175 -10.979 106.835 1.00 63.16  ? 310  PHE   A CD2  1 
ATOM   2453 C  CE1  . PHE   A 1 331 ? 393.376 -13.463 106.991 1.00 70.18  ? 310  PHE   A CE1  1 
ATOM   2454 C  CE2  . PHE   A 1 331 ? 391.443 -12.080 107.254 1.00 74.98  ? 310  PHE   A CE2  1 
ATOM   2455 C  CZ   . PHE   A 1 331 ? 392.045 -13.323 107.331 1.00 71.58  ? 310  PHE   A CZ   1 
ATOM   2456 N  N    . VAL   A 1 332 ? 396.983 -10.950 107.842 1.00 47.31  ? 311  VAL   A N    1 
ATOM   2457 C  CA   . VAL   A 1 332 ? 398.294 -11.585 107.881 1.00 53.62  ? 311  VAL   A CA   1 
ATOM   2458 C  C    . VAL   A 1 332 ? 398.105 -13.091 107.979 1.00 53.13  ? 311  VAL   A C    1 
ATOM   2459 O  O    . VAL   A 1 332 ? 397.359 -13.574 108.838 1.00 52.97  ? 311  VAL   A O    1 
ATOM   2460 C  CB   . VAL   A 1 332 ? 399.140 -11.069 109.061 1.00 54.02  ? 311  VAL   A CB   1 
ATOM   2461 C  CG1  . VAL   A 1 332 ? 400.384 -11.923 109.241 1.00 49.78  ? 311  VAL   A CG1  1 
ATOM   2462 C  CG2  . VAL   A 1 332 ? 399.518 -9.615  108.839 1.00 53.12  ? 311  VAL   A CG2  1 
ATOM   2463 N  N    . CYS   A 1 333 ? 398.773 -13.829 107.096 1.00 55.91  ? 312  CYS   A N    1 
ATOM   2464 C  CA   . CYS   A 1 333 ? 398.838 -15.280 107.164 1.00 58.01  ? 312  CYS   A CA   1 
ATOM   2465 C  C    . CYS   A 1 333 ? 400.284 -15.696 107.388 1.00 60.04  ? 312  CYS   A C    1 
ATOM   2466 O  O    . CYS   A 1 333 ? 401.201 -15.148 106.767 1.00 57.61  ? 312  CYS   A O    1 
ATOM   2467 C  CB   . CYS   A 1 333 ? 398.293 -15.938 105.887 1.00 65.58  ? 312  CYS   A CB   1 
ATOM   2468 S  SG   . CYS   A 1 333 ? 399.467 -16.060 104.507 1.00 70.32  ? 312  CYS   A SG   1 
ATOM   2469 N  N    . CYS   A 1 334 ? 400.484 -16.653 108.284 1.00 61.16  ? 313  CYS   A N    1 
ATOM   2470 C  CA   . CYS   A 1 334 ? 401.811 -17.194 108.556 1.00 63.02  ? 313  CYS   A CA   1 
ATOM   2471 C  C    . CYS   A 1 334 ? 401.641 -18.364 109.516 1.00 69.72  ? 313  CYS   A C    1 
ATOM   2472 O  O    . CYS   A 1 334 ? 400.521 -18.743 109.874 1.00 74.41  ? 313  CYS   A O    1 
ATOM   2473 C  CB   . CYS   A 1 334 ? 402.750 -16.126 109.123 1.00 60.42  ? 313  CYS   A CB   1 
ATOM   2474 S  SG   . CYS   A 1 334 ? 402.292 -15.507 110.760 1.00 65.70  ? 313  CYS   A SG   1 
ATOM   2475 N  N    . MET   A 1 335 ? 402.765 -18.938 109.928 1.00 70.72  ? 314  MET   A N    1 
ATOM   2476 C  CA   . MET   A 1 335 ? 402.741 -20.038 110.876 1.00 75.31  ? 314  MET   A CA   1 
ATOM   2477 C  C    . MET   A 1 335 ? 402.733 -19.513 112.307 1.00 73.61  ? 314  MET   A C    1 
ATOM   2478 O  O    . MET   A 1 335 ? 403.064 -18.356 112.580 1.00 67.93  ? 314  MET   A O    1 
ATOM   2479 C  CB   . MET   A 1 335 ? 403.926 -20.975 110.652 1.00 76.49  ? 314  MET   A CB   1 
ATOM   2480 C  CG   . MET   A 1 335 ? 403.785 -21.805 109.392 1.00 80.20  ? 314  MET   A CG   1 
ATOM   2481 S  SD   . MET   A 1 335 ? 402.080 -22.353 109.163 1.00 117.78 ? 314  MET   A SD   1 
ATOM   2482 C  CE   . MET   A 1 335 ? 401.833 -23.350 110.631 1.00 81.43  ? 314  MET   A CE   1 
ATOM   2483 N  N    . LYS   A 1 336 ? 402.348 -20.397 113.227 1.00 72.22  ? 315  LYS   A N    1 
ATOM   2484 C  CA   . LYS   A 1 336 ? 402.085 -19.993 114.601 1.00 74.75  ? 315  LYS   A CA   1 
ATOM   2485 C  C    . LYS   A 1 336 ? 403.353 -19.632 115.365 1.00 75.80  ? 315  LYS   A C    1 
ATOM   2486 O  O    . LYS   A 1 336 ? 403.272 -18.913 116.367 1.00 78.04  ? 315  LYS   A O    1 
ATOM   2487 C  CB   . LYS   A 1 336 ? 401.333 -21.114 115.318 1.00 82.26  ? 315  LYS   A CB   1 
ATOM   2488 C  CG   . LYS   A 1 336 ? 400.229 -21.730 114.466 1.00 89.50  ? 315  LYS   A CG   1 
ATOM   2489 C  CD   . LYS   A 1 336 ? 399.824 -23.102 114.974 1.00 97.89  ? 315  LYS   A CD   1 
ATOM   2490 C  CE   . LYS   A 1 336 ? 398.868 -23.789 114.010 1.00 95.77  ? 315  LYS   A CE   1 
ATOM   2491 N  NZ   . LYS   A 1 336 ? 398.538 -25.172 114.455 1.00 90.24  ? 315  LYS   A NZ   1 
ATOM   2492 N  N    . ASP   A 1 337 ? 404.516 -20.104 114.917 1.00 74.97  ? 316  ASP   A N    1 
ATOM   2493 C  CA   . ASP   A 1 337 ? 405.774 -19.864 115.612 1.00 71.29  ? 316  ASP   A CA   1 
ATOM   2494 C  C    . ASP   A 1 337 ? 406.648 -18.833 114.908 1.00 69.23  ? 316  ASP   A C    1 
ATOM   2495 O  O    . ASP   A 1 337 ? 407.807 -18.648 115.296 1.00 75.30  ? 316  ASP   A O    1 
ATOM   2496 C  CB   . ASP   A 1 337 ? 406.541 -21.177 115.790 1.00 66.06  ? 316  ASP   A CB   1 
ATOM   2497 C  CG   . ASP   A 1 337 ? 407.030 -21.756 114.474 1.00 64.07  ? 316  ASP   A CG   1 
ATOM   2498 O  OD1  . ASP   A 1 337 ? 406.426 -21.459 113.421 1.00 67.41  ? 316  ASP   A OD1  1 
ATOM   2499 O  OD2  . ASP   A 1 337 ? 408.022 -22.516 114.497 1.00 63.84  ? 316  ASP   A OD2  1 
ATOM   2500 N  N    . ASN   A 1 338 ? 406.126 -18.158 113.885 1.00 67.38  ? 317  ASN   A N    1 
ATOM   2501 C  CA   . ASN   A 1 338 ? 406.846 -17.067 113.228 1.00 67.30  ? 317  ASN   A CA   1 
ATOM   2502 C  C    . ASN   A 1 338 ? 406.698 -15.822 114.101 1.00 66.55  ? 317  ASN   A C    1 
ATOM   2503 O  O    . ASN   A 1 338 ? 405.941 -14.893 113.805 1.00 67.47  ? 317  ASN   A O    1 
ATOM   2504 C  CB   . ASN   A 1 338 ? 406.315 -16.848 111.817 1.00 62.93  ? 317  ASN   A CB   1 
ATOM   2505 C  CG   . ASN   A 1 338 ? 407.338 -16.211 110.900 1.00 69.07  ? 317  ASN   A CG   1 
ATOM   2506 O  OD1  . ASN   A 1 338 ? 408.258 -15.533 111.357 1.00 77.45  ? 317  ASN   A OD1  1 
ATOM   2507 N  ND2  . ASN   A 1 338 ? 407.192 -16.437 109.601 1.00 69.98  ? 317  ASN   A ND2  1 
ATOM   2508 N  N    . TYR   A 1 339 ? 407.451 -15.812 115.204 1.00 65.53  ? 318  TYR   A N    1 
ATOM   2509 C  CA   . TYR   A 1 339 ? 407.281 -14.778 116.224 1.00 65.55  ? 318  TYR   A CA   1 
ATOM   2510 C  C    . TYR   A 1 339 ? 407.857 -13.438 115.769 1.00 63.11  ? 318  TYR   A C    1 
ATOM   2511 O  O    . TYR   A 1 339 ? 407.228 -12.389 115.952 1.00 63.11  ? 318  TYR   A O    1 
ATOM   2512 C  CB   . TYR   A 1 339 ? 407.927 -15.229 117.536 1.00 74.09  ? 318  TYR   A CB   1 
ATOM   2513 C  CG   . TYR   A 1 339 ? 407.293 -16.466 118.133 1.00 72.08  ? 318  TYR   A CG   1 
ATOM   2514 C  CD1  . TYR   A 1 339 ? 405.914 -16.637 118.128 1.00 76.07  ? 318  TYR   A CD1  1 
ATOM   2515 C  CD2  . TYR   A 1 339 ? 408.074 -17.470 118.692 1.00 68.88  ? 318  TYR   A CD2  1 
ATOM   2516 C  CE1  . TYR   A 1 339 ? 405.330 -17.768 118.668 1.00 72.95  ? 318  TYR   A CE1  1 
ATOM   2517 C  CE2  . TYR   A 1 339 ? 407.499 -18.607 119.234 1.00 70.16  ? 318  TYR   A CE2  1 
ATOM   2518 C  CZ   . TYR   A 1 339 ? 406.126 -18.750 119.219 1.00 74.49  ? 318  TYR   A CZ   1 
ATOM   2519 O  OH   . TYR   A 1 339 ? 405.546 -19.877 119.756 1.00 77.93  ? 318  TYR   A OH   1 
ATOM   2520 N  N    . LEU   A 1 340 ? 409.061 -13.448 115.191 1.00 62.71  ? 319  LEU   A N    1 
ATOM   2521 C  CA   . LEU   A 1 340 ? 409.664 -12.198 114.730 1.00 65.85  ? 319  LEU   A CA   1 
ATOM   2522 C  C    . LEU   A 1 340 ? 408.764 -11.498 113.719 1.00 62.25  ? 319  LEU   A C    1 
ATOM   2523 O  O    . LEU   A 1 340 ? 408.553 -10.281 113.791 1.00 62.36  ? 319  LEU   A O    1 
ATOM   2524 C  CB   . LEU   A 1 340 ? 411.045 -12.465 114.126 1.00 62.59  ? 319  LEU   A CB   1 
ATOM   2525 C  CG   . LEU   A 1 340 ? 412.123 -13.007 115.063 1.00 72.76  ? 319  LEU   A CG   1 
ATOM   2526 C  CD1  . LEU   A 1 340 ? 413.372 -13.376 114.277 1.00 79.02  ? 319  LEU   A CD1  1 
ATOM   2527 C  CD2  . LEU   A 1 340 ? 412.446 -11.995 116.151 1.00 76.11  ? 319  LEU   A CD2  1 
ATOM   2528 N  N    . PHE   A 1 341 ? 408.230 -12.252 112.758 1.00 61.29  ? 320  PHE   A N    1 
ATOM   2529 C  CA   . PHE   A 1 341 ? 407.342 -11.665 111.761 1.00 56.51  ? 320  PHE   A CA   1 
ATOM   2530 C  C    . PHE   A 1 341 ? 406.099 -11.071 112.415 1.00 55.64  ? 320  PHE   A C    1 
ATOM   2531 O  O    . PHE   A 1 341 ? 405.727 -9.923  112.147 1.00 46.77  ? 320  PHE   A O    1 
ATOM   2532 C  CB   . PHE   A 1 341 ? 406.957 -12.718 110.722 1.00 54.52  ? 320  PHE   A CB   1 
ATOM   2533 C  CG   . PHE   A 1 341 ? 405.983 -12.226 109.692 1.00 53.06  ? 320  PHE   A CG   1 
ATOM   2534 C  CD1  . PHE   A 1 341 ? 406.408 -11.422 108.649 1.00 45.24  ? 320  PHE   A CD1  1 
ATOM   2535 C  CD2  . PHE   A 1 341 ? 404.644 -12.573 109.762 1.00 50.52  ? 320  PHE   A CD2  1 
ATOM   2536 C  CE1  . PHE   A 1 341 ? 405.516 -10.968 107.699 1.00 45.48  ? 320  PHE   A CE1  1 
ATOM   2537 C  CE2  . PHE   A 1 341 ? 403.748 -12.122 108.814 1.00 51.91  ? 320  PHE   A CE2  1 
ATOM   2538 C  CZ   . PHE   A 1 341 ? 404.184 -11.318 107.781 1.00 46.18  ? 320  PHE   A CZ   1 
ATOM   2539 N  N    . LEU   A 1 342 ? 405.443 -11.846 113.280 1.00 55.22  ? 321  LEU   A N    1 
ATOM   2540 C  CA   . LEU   A 1 342 ? 404.238 -11.362 113.945 1.00 54.89  ? 321  LEU   A CA   1 
ATOM   2541 C  C    . LEU   A 1 342 ? 404.528 -10.119 114.775 1.00 55.41  ? 321  LEU   A C    1 
ATOM   2542 O  O    . LEU   A 1 342 ? 403.801 -9.121  114.697 1.00 53.49  ? 321  LEU   A O    1 
ATOM   2543 C  CB   . LEU   A 1 342 ? 403.647 -12.470 114.814 1.00 56.96  ? 321  LEU   A CB   1 
ATOM   2544 C  CG   . LEU   A 1 342 ? 402.798 -13.468 114.031 1.00 58.29  ? 321  LEU   A CG   1 
ATOM   2545 C  CD1  . LEU   A 1 342 ? 402.469 -14.686 114.876 1.00 65.69  ? 321  LEU   A CD1  1 
ATOM   2546 C  CD2  . LEU   A 1 342 ? 401.529 -12.784 113.545 1.00 59.35  ? 321  LEU   A CD2  1 
ATOM   2547 N  N    . LYS   A 1 343 ? 405.593 -10.160 115.577 1.00 52.28  ? 322  LYS   A N    1 
ATOM   2548 C  CA   . LYS   A 1 343 ? 405.922 -9.023  116.431 1.00 57.80  ? 322  LYS   A CA   1 
ATOM   2549 C  C    . LYS   A 1 343 ? 406.134 -7.759  115.605 1.00 54.30  ? 322  LYS   A C    1 
ATOM   2550 O  O    . LYS   A 1 343 ? 405.565 -6.703  115.907 1.00 56.67  ? 322  LYS   A O    1 
ATOM   2551 C  CB   . LYS   A 1 343 ? 407.164 -9.344  117.263 1.00 59.37  ? 322  LYS   A CB   1 
ATOM   2552 C  CG   . LYS   A 1 343 ? 407.481 -8.324  118.345 1.00 65.19  ? 322  LYS   A CG   1 
ATOM   2553 C  CD   . LYS   A 1 343 ? 408.752 -8.702  119.094 1.00 78.10  ? 322  LYS   A CD   1 
ATOM   2554 C  CE   . LYS   A 1 343 ? 409.951 -8.769  118.156 1.00 77.11  ? 322  LYS   A CE   1 
ATOM   2555 N  NZ   . LYS   A 1 343 ? 411.138 -9.401  118.799 1.00 80.56  ? 322  LYS   A NZ   1 
ATOM   2556 N  N    . GLU   A 1 344 ? 406.944 -7.851  114.548 1.00 52.41  ? 323  GLU   A N    1 
ATOM   2557 C  CA   . GLU   A 1 344 ? 407.269 -6.668  113.758 1.00 52.16  ? 323  GLU   A CA   1 
ATOM   2558 C  C    . GLU   A 1 344 ? 406.074 -6.177  112.951 1.00 50.64  ? 323  GLU   A C    1 
ATOM   2559 O  O    . GLU   A 1 344 ? 405.926 -4.967  112.742 1.00 49.59  ? 323  GLU   A O    1 
ATOM   2560 C  CB   . GLU   A 1 344 ? 408.462 -6.967  112.848 1.00 48.45  ? 323  GLU   A CB   1 
ATOM   2561 C  CG   . GLU   A 1 344 ? 409.755 -7.217  113.622 1.00 59.41  ? 323  GLU   A CG   1 
ATOM   2562 C  CD   . GLU   A 1 344 ? 410.816 -7.931  112.804 1.00 57.87  ? 323  GLU   A CD   1 
ATOM   2563 O  OE1  . GLU   A 1 344 ? 410.535 -8.282  111.639 1.00 54.07  ? 323  GLU   A OE1  1 
ATOM   2564 O  OE2  . GLU   A 1 344 ? 411.930 -8.146  113.328 1.00 64.81  ? 323  GLU   A OE2  1 
ATOM   2565 N  N    . VAL   A 1 345 ? 405.212 -7.085  112.493 1.00 49.02  ? 324  VAL   A N    1 
ATOM   2566 C  CA   . VAL   A 1 345 ? 403.994 -6.646  111.820 1.00 47.54  ? 324  VAL   A CA   1 
ATOM   2567 C  C    . VAL   A 1 345 ? 403.038 -6.011  112.821 1.00 47.04  ? 324  VAL   A C    1 
ATOM   2568 O  O    . VAL   A 1 345 ? 402.347 -5.035  112.507 1.00 46.65  ? 324  VAL   A O    1 
ATOM   2569 C  CB   . VAL   A 1 345 ? 403.337 -7.816  111.066 1.00 46.57  ? 324  VAL   A CB   1 
ATOM   2570 C  CG1  . VAL   A 1 345 ? 401.971 -7.405  110.548 1.00 45.52  ? 324  VAL   A CG1  1 
ATOM   2571 C  CG2  . VAL   A 1 345 ? 404.222 -8.264  109.914 1.00 42.55  ? 324  VAL   A CG2  1 
ATOM   2572 N  N    . LYS   A 1 346 ? 402.984 -6.548  114.043 1.00 51.03  ? 325  LYS   A N    1 
ATOM   2573 C  CA   . LYS   A 1 346 ? 402.167 -5.930  115.083 1.00 48.82  ? 325  LYS   A CA   1 
ATOM   2574 C  C    . LYS   A 1 346 ? 402.704 -4.551  115.444 1.00 53.52  ? 325  LYS   A C    1 
ATOM   2575 O  O    . LYS   A 1 346 ? 401.944 -3.578  115.516 1.00 56.73  ? 325  LYS   A O    1 
ATOM   2576 C  CB   . LYS   A 1 346 ? 402.110 -6.832  116.317 1.00 49.35  ? 325  LYS   A CB   1 
ATOM   2577 N  N    . ASN   A 1 347 ? 404.018 -4.448  115.669 1.00 53.98  ? 326  ASN   A N    1 
ATOM   2578 C  CA   . ASN   A 1 347 ? 404.640 -3.150  115.917 1.00 57.26  ? 326  ASN   A CA   1 
ATOM   2579 C  C    . ASN   A 1 347 ? 404.323 -2.169  114.793 1.00 62.01  ? 326  ASN   A C    1 
ATOM   2580 O  O    . ASN   A 1 347 ? 403.981 -1.006  115.038 1.00 63.24  ? 326  ASN   A O    1 
ATOM   2581 C  CB   . ASN   A 1 347 ? 406.157 -3.307  116.068 1.00 58.20  ? 326  ASN   A CB   1 
ATOM   2582 C  CG   . ASN   A 1 347 ? 406.558 -3.979  117.368 1.00 70.54  ? 326  ASN   A CG   1 
ATOM   2583 O  OD1  . ASN   A 1 347 ? 405.759 -4.104  118.293 1.00 72.82  ? 326  ASN   A OD1  1 
ATOM   2584 N  ND2  . ASN   A 1 347 ? 407.814 -4.406  117.444 1.00 74.84  ? 326  ASN   A ND2  1 
ATOM   2585 N  N    . LEU   A 1 348 ? 404.448 -2.622  113.544 1.00 55.38  ? 327  LEU   A N    1 
ATOM   2586 C  CA   . LEU   A 1 348 ? 404.186 -1.747  112.405 1.00 52.34  ? 327  LEU   A CA   1 
ATOM   2587 C  C    . LEU   A 1 348 ? 402.742 -1.257  112.408 1.00 54.83  ? 327  LEU   A C    1 
ATOM   2588 O  O    . LEU   A 1 348 ? 402.479 -0.060  112.250 1.00 57.42  ? 327  LEU   A O    1 
ATOM   2589 C  CB   . LEU   A 1 348 ? 404.510 -2.478  111.100 1.00 53.31  ? 327  LEU   A CB   1 
ATOM   2590 C  CG   . LEU   A 1 348 ? 404.224 -1.740  109.790 1.00 53.61  ? 327  LEU   A CG   1 
ATOM   2591 C  CD1  . LEU   A 1 348 ? 405.191 -0.581  109.590 1.00 49.90  ? 327  LEU   A CD1  1 
ATOM   2592 C  CD2  . LEU   A 1 348 ? 404.268 -2.701  108.610 1.00 44.58  ? 327  LEU   A CD2  1 
ATOM   2593 N  N    . VAL   A 1 349 ? 401.787 -2.174  112.587 1.00 53.36  ? 328  VAL   A N    1 
ATOM   2594 C  CA   . VAL   A 1 349 ? 400.380 -1.789  112.565 1.00 53.52  ? 328  VAL   A CA   1 
ATOM   2595 C  C    . VAL   A 1 349 ? 400.012 -0.897  113.744 1.00 59.07  ? 328  VAL   A C    1 
ATOM   2596 O  O    . VAL   A 1 349 ? 399.038 -0.140  113.659 1.00 57.44  ? 328  VAL   A O    1 
ATOM   2597 C  CB   . VAL   A 1 349 ? 399.477 -3.037  112.533 1.00 49.05  ? 328  VAL   A CB   1 
ATOM   2598 C  CG1  . VAL   A 1 349 ? 398.025 -2.646  112.759 1.00 54.51  ? 328  VAL   A CG1  1 
ATOM   2599 C  CG2  . VAL   A 1 349 ? 399.630 -3.761  111.207 1.00 47.27  ? 328  VAL   A CG2  1 
ATOM   2600 N  N    . GLU   A 1 350 ? 400.767 -0.961  114.844 1.00 59.61  ? 329  GLU   A N    1 
ATOM   2601 C  CA   . GLU   A 1 350 ? 400.493 -0.109  115.996 1.00 64.16  ? 329  GLU   A CA   1 
ATOM   2602 C  C    . GLU   A 1 350 ? 400.974 1.322   115.806 1.00 65.50  ? 329  GLU   A C    1 
ATOM   2603 O  O    . GLU   A 1 350 ? 400.496 2.217   116.510 1.00 70.00  ? 329  GLU   A O    1 
ATOM   2604 C  CB   . GLU   A 1 350 ? 401.125 -0.699  117.255 1.00 64.07  ? 329  GLU   A CB   1 
ATOM   2605 C  CG   . GLU   A 1 350 ? 400.315 -1.822  117.860 1.00 72.26  ? 329  GLU   A CG   1 
ATOM   2606 C  CD   . GLU   A 1 350 ? 401.029 -2.499  119.004 1.00 80.26  ? 329  GLU   A CD   1 
ATOM   2607 O  OE1  . GLU   A 1 350 ? 402.009 -1.920  119.518 1.00 83.09  ? 329  GLU   A OE1  1 
ATOM   2608 O  OE2  . GLU   A 1 350 ? 400.613 -3.613  119.382 1.00 93.78  ? 329  GLU   A OE2  1 
ATOM   2609 N  N    . LYS   A 1 351 ? 401.915 1.559   114.891 1.00 65.50  ? 330  LYS   A N    1 
ATOM   2610 C  CA   . LYS   A 1 351 ? 402.203 2.927   114.482 1.00 60.70  ? 330  LYS   A CA   1 
ATOM   2611 C  C    . LYS   A 1 351 ? 401.035 3.559   113.741 1.00 61.10  ? 330  LYS   A C    1 
ATOM   2612 O  O    . LYS   A 1 351 ? 401.019 4.782   113.568 1.00 64.90  ? 330  LYS   A O    1 
ATOM   2613 C  CB   . LYS   A 1 351 ? 403.450 2.966   113.598 1.00 55.27  ? 330  LYS   A CB   1 
ATOM   2614 C  CG   . LYS   A 1 351 ? 404.705 2.472   114.283 1.00 52.63  ? 330  LYS   A CG   1 
ATOM   2615 C  CD   . LYS   A 1 351 ? 405.834 2.286   113.288 1.00 59.03  ? 330  LYS   A CD   1 
ATOM   2616 C  CE   . LYS   A 1 351 ? 407.033 1.629   113.949 1.00 63.95  ? 330  LYS   A CE   1 
ATOM   2617 N  NZ   . LYS   A 1 351 ? 408.084 1.241   112.967 1.00 62.63  ? 330  LYS   A NZ   1 
ATOM   2618 N  N    . THR   A 1 352 ? 400.068 2.760   113.310 1.00 57.86  ? 331  THR   A N    1 
ATOM   2619 C  CA   . THR   A 1 352 ? 398.932 3.213   112.528 1.00 62.06  ? 331  THR   A CA   1 
ATOM   2620 C  C    . THR   A 1 352 ? 397.647 2.990   113.316 1.00 63.52  ? 331  THR   A C    1 
ATOM   2621 O  O    . THR   A 1 352 ? 397.652 2.479   114.437 1.00 68.70  ? 331  THR   A O    1 
ATOM   2622 C  CB   . THR   A 1 352 ? 398.868 2.481   111.185 1.00 59.67  ? 331  THR   A CB   1 
ATOM   2623 O  OG1  . THR   A 1 352 ? 398.278 1.189   111.374 1.00 57.86  ? 331  THR   A OG1  1 
ATOM   2624 C  CG2  . THR   A 1 352 ? 400.264 2.305   110.609 1.00 52.21  ? 331  THR   A CG2  1 
ATOM   2625 N  N    . ASN   A 1 353 ? 396.534 3.374   112.700 1.00 59.41  ? 332  ASN   A N    1 
ATOM   2626 C  CA   . ASN   A 1 353 ? 395.210 3.224   113.280 1.00 65.97  ? 332  ASN   A CA   1 
ATOM   2627 C  C    . ASN   A 1 353 ? 394.515 1.950   112.821 1.00 66.48  ? 332  ASN   A C    1 
ATOM   2628 O  O    . ASN   A 1 353 ? 393.303 1.811   113.012 1.00 68.87  ? 332  ASN   A O    1 
ATOM   2629 C  CB   . ASN   A 1 353 ? 394.359 4.438   112.921 1.00 75.58  ? 332  ASN   A CB   1 
ATOM   2630 C  CG   . ASN   A 1 353 ? 394.549 4.864   111.477 1.00 80.37  ? 332  ASN   A CG   1 
ATOM   2631 O  OD1  . ASN   A 1 353 ? 395.408 5.692   111.172 1.00 76.68  ? 332  ASN   A OD1  1 
ATOM   2632 N  ND2  . ASN   A 1 353 ? 393.764 4.282   110.578 1.00 78.14  ? 332  ASN   A ND2  1 
ATOM   2633 N  N    . CYS   A 1 354 ? 395.252 1.021   112.222 1.00 57.70  ? 333  CYS   A N    1 
ATOM   2634 C  CA   . CYS   A 1 354 ? 394.652 -0.129  111.564 1.00 57.79  ? 333  CYS   A CA   1 
ATOM   2635 C  C    . CYS   A 1 354 ? 394.433 -1.281  112.533 1.00 55.40  ? 333  CYS   A C    1 
ATOM   2636 O  O    . CYS   A 1 354 ? 395.129 -1.419  113.543 1.00 55.23  ? 333  CYS   A O    1 
ATOM   2637 C  CB   . CYS   A 1 354 ? 395.531 -0.604  110.409 1.00 52.89  ? 333  CYS   A CB   1 
ATOM   2638 S  SG   . CYS   A 1 354 ? 396.068 0.732   109.339 1.00 60.66  ? 333  CYS   A SG   1 
ATOM   2639 N  N    . GLU   A 1 355 ? 393.449 -2.109  112.208 1.00 56.92  ? 334  GLU   A N    1 
ATOM   2640 C  CA   . GLU   A 1 355 ? 393.273 -3.377  112.889 1.00 58.23  ? 334  GLU   A CA   1 
ATOM   2641 C  C    . GLU   A 1 355 ? 394.195 -4.422  112.275 1.00 53.97  ? 334  GLU   A C    1 
ATOM   2642 O  O    . GLU   A 1 355 ? 394.569 -4.341  111.101 1.00 53.46  ? 334  GLU   A O    1 
ATOM   2643 C  CB   . GLU   A 1 355 ? 391.820 -3.841  112.792 1.00 68.59  ? 334  GLU   A CB   1 
ATOM   2644 C  CG   . GLU   A 1 355 ? 391.570 -5.230  113.356 1.00 80.28  ? 334  GLU   A CG   1 
ATOM   2645 C  CD   . GLU   A 1 355 ? 390.391 -5.922  112.698 1.00 86.03  ? 334  GLU   A CD   1 
ATOM   2646 O  OE1  . GLU   A 1 355 ? 390.096 -5.608  111.526 1.00 85.13  ? 334  GLU   A OE1  1 
ATOM   2647 O  OE2  . GLU   A 1 355 ? 389.761 -6.779  113.352 1.00 90.22  ? 334  GLU   A OE2  1 
ATOM   2648 N  N    . LEU   A 1 356 ? 394.567 -5.406  113.086 1.00 56.77  ? 335  LEU   A N    1 
ATOM   2649 C  CA   . LEU   A 1 356 ? 395.351 -6.544  112.632 1.00 51.95  ? 335  LEU   A CA   1 
ATOM   2650 C  C    . LEU   A 1 356 ? 394.524 -7.811  112.787 1.00 55.94  ? 335  LEU   A C    1 
ATOM   2651 O  O    . LEU   A 1 356 ? 393.938 -8.050  113.849 1.00 57.32  ? 335  LEU   A O    1 
ATOM   2652 C  CB   . LEU   A 1 356 ? 396.660 -6.665  113.412 1.00 47.77  ? 335  LEU   A CB   1 
ATOM   2653 C  CG   . LEU   A 1 356 ? 397.588 -7.808  112.998 1.00 45.13  ? 335  LEU   A CG   1 
ATOM   2654 C  CD1  . LEU   A 1 356 ? 397.961 -7.708  111.528 1.00 48.99  ? 335  LEU   A CD1  1 
ATOM   2655 C  CD2  . LEU   A 1 356 ? 398.830 -7.783  113.858 1.00 44.52  ? 335  LEU   A CD2  1 
ATOM   2656 N  N    . LYS   A 1 357 ? 394.467 -8.610  111.723 1.00 56.05  ? 336  LYS   A N    1 
ATOM   2657 C  CA   . LYS   A 1 357 ? 393.775 -9.894  111.726 1.00 52.92  ? 336  LYS   A CA   1 
ATOM   2658 C  C    . LYS   A 1 357 ? 394.757 -10.956 111.257 1.00 54.55  ? 336  LYS   A C    1 
ATOM   2659 O  O    . LYS   A 1 357 ? 395.343 -10.827 110.176 1.00 53.50  ? 336  LYS   A O    1 
ATOM   2660 C  CB   . LYS   A 1 357 ? 392.536 -9.857  110.827 1.00 59.17  ? 336  LYS   A CB   1 
ATOM   2661 C  CG   . LYS   A 1 357 ? 391.736 -11.149 110.813 1.00 67.27  ? 336  LYS   A CG   1 
ATOM   2662 C  CD   . LYS   A 1 357 ? 391.276 -11.525 112.211 1.00 64.36  ? 336  LYS   A CD   1 
ATOM   2663 C  CE   . LYS   A 1 357 ? 390.505 -12.835 112.208 1.00 64.75  ? 336  LYS   A CE   1 
ATOM   2664 N  NZ   . LYS   A 1 357 ? 390.239 -13.313 113.593 1.00 63.49  ? 336  LYS   A NZ   1 
ATOM   2665 N  N    . VAL   A 1 358 ? 394.940 -11.997 112.064 1.00 58.46  ? 337  VAL   A N    1 
ATOM   2666 C  CA   . VAL   A 1 358 ? 395.941 -13.028 111.812 1.00 60.68  ? 337  VAL   A CA   1 
ATOM   2667 C  C    . VAL   A 1 358 ? 395.244 -14.350 111.526 1.00 64.48  ? 337  VAL   A C    1 
ATOM   2668 O  O    . VAL   A 1 358 ? 394.217 -14.672 112.136 1.00 65.80  ? 337  VAL   A O    1 
ATOM   2669 C  CB   . VAL   A 1 358 ? 396.913 -13.171 113.000 1.00 59.23  ? 337  VAL   A CB   1 
ATOM   2670 C  CG1  . VAL   A 1 358 ? 397.850 -14.351 112.781 1.00 62.09  ? 337  VAL   A CG1  1 
ATOM   2671 C  CG2  . VAL   A 1 358 ? 397.702 -11.887 113.200 1.00 53.26  ? 337  VAL   A CG2  1 
ATOM   2672 N  N    . CYS   A 1 359 ? 395.813 -15.116 110.595 1.00 77.53  ? 338  CYS   A N    1 
ATOM   2673 C  CA   . CYS   A 1 359 ? 395.373 -16.470 110.288 1.00 81.77  ? 338  CYS   A CA   1 
ATOM   2674 C  C    . CYS   A 1 359 ? 396.578 -17.395 110.364 1.00 79.32  ? 338  CYS   A C    1 
ATOM   2675 O  O    . CYS   A 1 359 ? 397.639 -17.082 109.814 1.00 79.17  ? 338  CYS   A O    1 
ATOM   2676 C  CB   . CYS   A 1 359 ? 394.724 -16.545 108.900 1.00 82.09  ? 338  CYS   A CB   1 
ATOM   2677 S  SG   . CYS   A 1 359 ? 394.119 -18.186 108.432 1.00 94.50  ? 338  CYS   A SG   1 
ATOM   2678 N  N    . PHE   A 1 360 ? 396.421 -18.523 111.051 1.00 79.55  ? 339  PHE   A N    1 
ATOM   2679 C  CA   . PHE   A 1 360 ? 397.519 -19.473 111.213 1.00 83.03  ? 339  PHE   A CA   1 
ATOM   2680 C  C    . PHE   A 1 360 ? 397.321 -20.708 110.337 1.00 83.97  ? 339  PHE   A C    1 
ATOM   2681 O  O    . PHE   A 1 360 ? 398.191 -21.060 109.539 1.00 87.31  ? 339  PHE   A O    1 
ATOM   2682 C  CB   . PHE   A 1 360 ? 397.660 -19.886 112.681 1.00 84.01  ? 339  PHE   A CB   1 
ATOM   2683 C  CG   . PHE   A 1 360 ? 398.164 -18.787 113.579 1.00 85.95  ? 339  PHE   A CG   1 
ATOM   2684 C  CD1  . PHE   A 1 360 ? 399.209 -17.969 113.182 1.00 84.72  ? 339  PHE   A CD1  1 
ATOM   2685 C  CD2  . PHE   A 1 360 ? 397.590 -18.573 114.821 1.00 88.28  ? 339  PHE   A CD2  1 
ATOM   2686 C  CE1  . PHE   A 1 360 ? 399.673 -16.959 114.010 1.00 79.38  ? 339  PHE   A CE1  1 
ATOM   2687 C  CE2  . PHE   A 1 360 ? 398.049 -17.564 115.652 1.00 79.61  ? 339  PHE   A CE2  1 
ATOM   2688 C  CZ   . PHE   A 1 360 ? 399.091 -16.757 115.245 1.00 73.66  ? 339  PHE   A CZ   1 
ATOM   2689 N  N    . ASP   A 1 367 ? 401.149 -20.671 101.024 1.00 78.05  ? 346  ASP   A N    1 
ATOM   2690 C  CA   . ASP   A 1 367 ? 401.913 -20.020 102.082 1.00 85.63  ? 346  ASP   A CA   1 
ATOM   2691 C  C    . ASP   A 1 367 ? 401.696 -18.512 102.044 1.00 88.81  ? 346  ASP   A C    1 
ATOM   2692 O  O    . ASP   A 1 367 ? 401.492 -17.879 103.078 1.00 85.91  ? 346  ASP   A O    1 
ATOM   2693 C  CB   . ASP   A 1 367 ? 403.402 -20.350 101.956 1.00 78.85  ? 346  ASP   A CB   1 
ATOM   2694 N  N    . ARG   A 1 368 ? 401.754 -17.940 100.841 1.00 94.26  ? 347  ARG   A N    1 
ATOM   2695 C  CA   . ARG   A 1 368 ? 401.411 -16.543 100.611 1.00 92.59  ? 347  ARG   A CA   1 
ATOM   2696 C  C    . ARG   A 1 368 ? 399.975 -16.377 100.131 1.00 83.16  ? 347  ARG   A C    1 
ATOM   2697 O  O    . ARG   A 1 368 ? 399.630 -15.331 99.572  1.00 78.86  ? 347  ARG   A O    1 
ATOM   2698 C  CB   . ARG   A 1 368 ? 402.375 -15.910 99.607  1.00 88.24  ? 347  ARG   A CB   1 
ATOM   2699 C  CG   . ARG   A 1 368 ? 403.667 -15.381 100.218 1.00 97.79  ? 347  ARG   A CG   1 
ATOM   2700 C  CD   . ARG   A 1 368 ? 403.914 -13.929 99.825  1.00 97.62  ? 347  ARG   A CD   1 
ATOM   2701 N  NE   . ARG   A 1 368 ? 405.192 -13.754 99.144  1.00 102.71 ? 347  ARG   A NE   1 
ATOM   2702 C  CZ   . ARG   A 1 368 ? 405.342 -13.716 97.827  1.00 102.15 ? 347  ARG   A CZ   1 
ATOM   2703 N  NH1  . ARG   A 1 368 ? 404.305 -13.813 97.011  1.00 98.70  ? 347  ARG   A NH1  1 
ATOM   2704 N  NH2  . ARG   A 1 368 ? 406.562 -13.577 97.316  1.00 99.85  ? 347  ARG   A NH2  1 
ATOM   2705 N  N    . TRP   A 1 369 ? 399.132 -17.388 100.350 1.00 69.47  ? 348  TRP   A N    1 
ATOM   2706 C  CA   . TRP   A 1 369 ? 397.783 -17.376 99.796  1.00 60.99  ? 348  TRP   A CA   1 
ATOM   2707 C  C    . TRP   A 1 369 ? 397.032 -16.093 100.130 1.00 60.17  ? 348  TRP   A C    1 
ATOM   2708 O  O    . TRP   A 1 369 ? 396.183 -15.654 99.347  1.00 58.61  ? 348  TRP   A O    1 
ATOM   2709 C  CB   . TRP   A 1 369 ? 397.005 -18.598 100.292 1.00 62.71  ? 348  TRP   A CB   1 
ATOM   2710 C  CG   . TRP   A 1 369 ? 396.857 -18.660 101.779 1.00 63.44  ? 348  TRP   A CG   1 
ATOM   2711 C  CD1  . TRP   A 1 369 ? 397.672 -19.311 102.660 1.00 67.47  ? 348  TRP   A CD1  1 
ATOM   2712 C  CD2  . TRP   A 1 369 ? 395.828 -18.047 102.562 1.00 61.73  ? 348  TRP   A CD2  1 
ATOM   2713 N  NE1  . TRP   A 1 369 ? 397.212 -19.140 103.944 1.00 72.77  ? 348  TRP   A NE1  1 
ATOM   2714 C  CE2  . TRP   A 1 369 ? 396.081 -18.367 103.910 1.00 68.15  ? 348  TRP   A CE2  1 
ATOM   2715 C  CE3  . TRP   A 1 369 ? 394.716 -17.258 102.253 1.00 56.62  ? 348  TRP   A CE3  1 
ATOM   2716 C  CZ2  . TRP   A 1 369 ? 395.262 -17.925 104.948 1.00 68.83  ? 348  TRP   A CZ2  1 
ATOM   2717 C  CZ3  . TRP   A 1 369 ? 393.905 -16.821 103.283 1.00 65.57  ? 348  TRP   A CZ3  1 
ATOM   2718 C  CH2  . TRP   A 1 369 ? 394.182 -17.155 104.615 1.00 69.36  ? 348  TRP   A CH2  1 
ATOM   2719 N  N    . ILE   A 1 370 ? 397.327 -15.471 101.276 1.00 62.43  ? 349  ILE   A N    1 
ATOM   2720 C  CA   . ILE   A 1 370 ? 396.650 -14.228 101.635 1.00 65.32  ? 349  ILE   A CA   1 
ATOM   2721 C  C    . ILE   A 1 370 ? 397.056 -13.068 100.743 1.00 63.13  ? 349  ILE   A C    1 
ATOM   2722 O  O    . ILE   A 1 370 ? 396.410 -12.014 100.781 1.00 56.68  ? 349  ILE   A O    1 
ATOM   2723 C  CB   . ILE   A 1 370 ? 396.908 -13.848 103.107 1.00 62.53  ? 349  ILE   A CB   1 
ATOM   2724 C  CG1  . ILE   A 1 370 ? 395.887 -12.809 103.574 1.00 60.32  ? 349  ILE   A CG1  1 
ATOM   2725 C  CG2  . ILE   A 1 370 ? 398.304 -13.284 103.267 1.00 63.09  ? 349  ILE   A CG2  1 
ATOM   2726 C  CD1  . ILE   A 1 370 ? 394.445 -13.207 103.328 1.00 67.70  ? 349  ILE   A CD1  1 
ATOM   2727 N  N    . GLN   A 1 371 ? 398.107 -13.233 99.945  1.00 64.08  ? 350  GLN   A N    1 
ATOM   2728 C  CA   . GLN   A 1 371 ? 398.526 -12.222 98.988  1.00 63.96  ? 350  GLN   A CA   1 
ATOM   2729 C  C    . GLN   A 1 371 ? 398.466 -12.687 97.541  1.00 62.83  ? 350  GLN   A C    1 
ATOM   2730 O  O    . GLN   A 1 371 ? 398.221 -11.862 96.658  1.00 59.99  ? 350  GLN   A O    1 
ATOM   2731 C  CB   . GLN   A 1 371 ? 399.954 -11.749 99.299  1.00 66.55  ? 350  GLN   A CB   1 
ATOM   2732 C  CG   . GLN   A 1 371 ? 400.455 -10.669 98.360  1.00 71.55  ? 350  GLN   A CG   1 
ATOM   2733 C  CD   . GLN   A 1 371 ? 401.957 -10.496 98.427  1.00 81.55  ? 350  GLN   A CD   1 
ATOM   2734 O  OE1  . GLN   A 1 371 ? 402.712 -11.369 98.000  1.00 81.41  ? 350  GLN   A OE1  1 
ATOM   2735 N  NE2  . GLN   A 1 371 ? 402.401 -9.368  98.966  1.00 79.31  ? 350  GLN   A NE2  1 
ATOM   2736 N  N    . ASP   A 1 372 ? 398.678 -13.977 97.271  1.00 49.77  ? 351  ASP   A N    1 
ATOM   2737 C  CA   . ASP   A 1 372 ? 398.615 -14.495 95.910  1.00 48.19  ? 351  ASP   A CA   1 
ATOM   2738 C  C    . ASP   A 1 372 ? 397.281 -15.141 95.560  1.00 47.72  ? 351  ASP   A C    1 
ATOM   2739 O  O    . ASP   A 1 372 ? 396.952 -15.234 94.373  1.00 40.64  ? 351  ASP   A O    1 
ATOM   2740 C  CB   . ASP   A 1 372 ? 399.733 -15.518 95.672  1.00 52.33  ? 351  ASP   A CB   1 
ATOM   2741 C  CG   . ASP   A 1 372 ? 401.107 -14.890 95.666  1.00 60.97  ? 351  ASP   A CG   1 
ATOM   2742 O  OD1  . ASP   A 1 372 ? 401.222 -13.703 96.029  1.00 61.36  ? 351  ASP   A OD1  1 
ATOM   2743 O  OD2  . ASP   A 1 372 ? 402.074 -15.586 95.290  1.00 64.90  ? 351  ASP   A OD2  1 
ATOM   2744 N  N    . GLU   A 1 373 ? 396.511 -15.596 96.550  1.00 44.32  ? 352  GLU   A N    1 
ATOM   2745 C  CA   . GLU   A 1 373 ? 395.230 -16.234 96.286  1.00 43.32  ? 352  GLU   A CA   1 
ATOM   2746 C  C    . GLU   A 1 373 ? 394.031 -15.362 96.621  1.00 37.86  ? 352  GLU   A C    1 
ATOM   2747 O  O    . GLU   A 1 373 ? 392.929 -15.647 96.144  1.00 38.43  ? 352  GLU   A O    1 
ATOM   2748 C  CB   . GLU   A 1 373 ? 395.120 -17.553 97.065  1.00 47.14  ? 352  GLU   A CB   1 
ATOM   2749 C  CG   . GLU   A 1 373 ? 396.188 -18.564 96.697  1.00 51.48  ? 352  GLU   A CG   1 
ATOM   2750 C  CD   . GLU   A 1 373 ? 395.982 -19.904 97.368  1.00 54.94  ? 352  GLU   A CD   1 
ATOM   2751 O  OE1  . GLU   A 1 373 ? 394.854 -20.174 97.830  1.00 61.78  ? 352  GLU   A OE1  1 
ATOM   2752 O  OE2  . GLU   A 1 373 ? 396.952 -20.687 97.435  1.00 55.97  ? 352  GLU   A OE2  1 
ATOM   2753 N  N    . ILE   A 1 374 ? 394.220 -14.309 97.410  1.00 42.72  ? 353  ILE   A N    1 
ATOM   2754 C  CA   . ILE   A 1 374 ? 393.144 -13.447 97.875  1.00 45.97  ? 353  ILE   A CA   1 
ATOM   2755 C  C    . ILE   A 1 374 ? 393.461 -12.009 97.486  1.00 43.51  ? 353  ILE   A C    1 
ATOM   2756 O  O    . ILE   A 1 374 ? 394.625 -11.601 97.431  1.00 40.31  ? 353  ILE   A O    1 
ATOM   2757 C  CB   . ILE   A 1 374 ? 392.945 -13.577 99.404  1.00 43.26  ? 353  ILE   A CB   1 
ATOM   2758 C  CG1  . ILE   A 1 374 ? 391.814 -14.556 99.724  1.00 45.17  ? 353  ILE   A CG1  1 
ATOM   2759 C  CG2  . ILE   A 1 374 ? 392.681 -12.221 100.037 1.00 53.59  ? 353  ILE   A CG2  1 
ATOM   2760 C  CD1  . ILE   A 1 374 ? 391.978 -15.913 99.088  1.00 49.18  ? 353  ILE   A CD1  1 
ATOM   2761 N  N    . GLU   A 1 375 ? 392.411 -11.239 97.210  1.00 36.90  ? 354  GLU   A N    1 
ATOM   2762 C  CA   . GLU   A 1 375 ? 392.556 -9.835  96.846  1.00 34.93  ? 354  GLU   A CA   1 
ATOM   2763 C  C    . GLU   A 1 375 ? 391.338 -9.075  97.346  1.00 34.44  ? 354  GLU   A C    1 
ATOM   2764 O  O    . GLU   A 1 375 ? 390.203 -9.461  97.055  1.00 33.16  ? 354  GLU   A O    1 
ATOM   2765 C  CB   . GLU   A 1 375 ? 392.705 -9.668  95.328  1.00 37.50  ? 354  GLU   A CB   1 
ATOM   2766 C  CG   . GLU   A 1 375 ? 392.871 -8.230  94.863  1.00 36.34  ? 354  GLU   A CG   1 
ATOM   2767 C  CD   . GLU   A 1 375 ? 394.182 -7.620  95.308  1.00 43.60  ? 354  GLU   A CD   1 
ATOM   2768 O  OE1  . GLU   A 1 375 ? 395.166 -8.371  95.475  1.00 50.01  ? 354  GLU   A OE1  1 
ATOM   2769 O  OE2  . GLU   A 1 375 ? 394.229 -6.385  95.496  1.00 52.01  ? 354  GLU   A OE2  1 
ATOM   2770 N  N    . PHE   A 1 376 ? 391.575 -8.006  98.100  1.00 36.23  ? 355  PHE   A N    1 
ATOM   2771 C  CA   . PHE   A 1 376 ? 390.496 -7.192  98.639  1.00 38.08  ? 355  PHE   A CA   1 
ATOM   2772 C  C    . PHE   A 1 376 ? 390.163 -6.073  97.662  1.00 33.71  ? 355  PHE   A C    1 
ATOM   2773 O  O    . PHE   A 1 376 ? 391.001 -5.208  97.389  1.00 37.54  ? 355  PHE   A O    1 
ATOM   2774 C  CB   . PHE   A 1 376 ? 390.880 -6.615  100.002 1.00 37.99  ? 355  PHE   A CB   1 
ATOM   2775 C  CG   . PHE   A 1 376 ? 391.043 -7.654  101.073 1.00 43.56  ? 355  PHE   A CG   1 
ATOM   2776 C  CD1  . PHE   A 1 376 ? 390.482 -8.912  100.923 1.00 52.11  ? 355  PHE   A CD1  1 
ATOM   2777 C  CD2  . PHE   A 1 376 ? 391.754 -7.378  102.225 1.00 50.96  ? 355  PHE   A CD2  1 
ATOM   2778 C  CE1  . PHE   A 1 376 ? 390.628 -9.872  101.903 1.00 51.10  ? 355  PHE   A CE1  1 
ATOM   2779 C  CE2  . PHE   A 1 376 ? 391.903 -8.338  103.207 1.00 55.29  ? 355  PHE   A CE2  1 
ATOM   2780 C  CZ   . PHE   A 1 376 ? 391.338 -9.585  103.044 1.00 50.28  ? 355  PHE   A CZ   1 
ATOM   2781 N  N    . GLY   A 1 377 ? 388.953 -6.106  97.122  1.00 32.82  ? 356  GLY   A N    1 
ATOM   2782 C  CA   . GLY   A 1 377 ? 388.456 -4.992  96.347  1.00 31.26  ? 356  GLY   A CA   1 
ATOM   2783 C  C    . GLY   A 1 377 ? 387.207 -4.455  97.005  1.00 30.57  ? 356  GLY   A C    1 
ATOM   2784 O  O    . GLY   A 1 377 ? 386.991 -4.678  98.199  1.00 30.99  ? 356  GLY   A O    1 
ATOM   2785 N  N    . TYR   A 1 378 ? 386.363 -3.763  96.252  1.00 27.68  ? 357  TYR   A N    1 
ATOM   2786 C  CA   . TYR   A 1 378 ? 385.094 -3.327  96.812  1.00 32.78  ? 357  TYR   A CA   1 
ATOM   2787 C  C    . TYR   A 1 378 ? 384.111 -3.097  95.677  1.00 30.92  ? 357  TYR   A C    1 
ATOM   2788 O  O    . TYR   A 1 378 ? 384.481 -3.041  94.502  1.00 26.55  ? 357  TYR   A O    1 
ATOM   2789 C  CB   . TYR   A 1 378 ? 385.259 -2.065  97.664  1.00 29.17  ? 357  TYR   A CB   1 
ATOM   2790 C  CG   . TYR   A 1 378 ? 385.574 -0.829  96.857  1.00 30.31  ? 357  TYR   A CG   1 
ATOM   2791 C  CD1  . TYR   A 1 378 ? 386.882 -0.520  96.516  1.00 29.66  ? 357  TYR   A CD1  1 
ATOM   2792 C  CD2  . TYR   A 1 378 ? 384.564 0.026   96.428  1.00 30.40  ? 357  TYR   A CD2  1 
ATOM   2793 C  CE1  . TYR   A 1 378 ? 387.181 0.605   95.776  1.00 32.32  ? 357  TYR   A CE1  1 
ATOM   2794 C  CE2  . TYR   A 1 378 ? 384.855 1.157   95.684  1.00 33.01  ? 357  TYR   A CE2  1 
ATOM   2795 C  CZ   . TYR   A 1 378 ? 386.170 1.440   95.362  1.00 32.52  ? 357  TYR   A CZ   1 
ATOM   2796 O  OH   . TYR   A 1 378 ? 386.490 2.558   94.624  1.00 35.96  ? 357  TYR   A OH   1 
ATOM   2797 N  N    . ILE   A 1 379 ? 382.845 -2.986  96.055  1.00 33.08  ? 358  ILE   A N    1 
ATOM   2798 C  CA   . ILE   A 1 379 ? 381.772 -2.586  95.161  1.00 28.95  ? 358  ILE   A CA   1 
ATOM   2799 C  C    . ILE   A 1 379 ? 381.046 -1.432  95.828  1.00 32.25  ? 358  ILE   A C    1 
ATOM   2800 O  O    . ILE   A 1 379 ? 381.049 -1.302  97.056  1.00 33.67  ? 358  ILE   A O    1 
ATOM   2801 C  CB   . ILE   A 1 379 ? 380.799 -3.745  94.861  1.00 28.06  ? 358  ILE   A CB   1 
ATOM   2802 C  CG1  . ILE   A 1 379 ? 380.180 -4.263  96.163  1.00 25.29  ? 358  ILE   A CG1  1 
ATOM   2803 C  CG2  . ILE   A 1 379 ? 381.514 -4.852  94.093  1.00 25.32  ? 358  ILE   A CG2  1 
ATOM   2804 C  CD1  . ILE   A 1 379 ? 379.207 -5.412  95.977  1.00 27.03  ? 358  ILE   A CD1  1 
ATOM   2805 N  N    . GLU   A 1 380 ? 380.428 -0.580  95.018  1.00 31.74  ? 359  GLU   A N    1 
ATOM   2806 C  CA   . GLU   A 1 380 ? 379.705 0.549   95.576  1.00 31.70  ? 359  GLU   A CA   1 
ATOM   2807 C  C    . GLU   A 1 380 ? 378.529 0.901   94.684  1.00 36.29  ? 359  GLU   A C    1 
ATOM   2808 O  O    . GLU   A 1 380 ? 378.646 0.904   93.456  1.00 31.07  ? 359  GLU   A O    1 
ATOM   2809 C  CB   . GLU   A 1 380 ? 380.611 1.770   95.751  1.00 34.64  ? 359  GLU   A CB   1 
ATOM   2810 C  CG   . GLU   A 1 380 ? 379.909 2.927   96.431  1.00 37.62  ? 359  GLU   A CG   1 
ATOM   2811 C  CD   . GLU   A 1 380 ? 380.801 4.132   96.625  1.00 47.58  ? 359  GLU   A CD   1 
ATOM   2812 O  OE1  . GLU   A 1 380 ? 381.892 4.172   96.022  1.00 49.74  ? 359  GLU   A OE1  1 
ATOM   2813 O  OE2  . GLU   A 1 380 ? 380.409 5.041   97.386  1.00 50.59  ? 359  GLU   A OE2  1 
ATOM   2814 N  N    . ALA   A 1 381 ? 377.397 1.182   95.314  1.00 37.13  ? 360  ALA   A N    1 
ATOM   2815 C  CA   . ALA   A 1 381 ? 376.256 1.801   94.657  1.00 33.20  ? 360  ALA   A CA   1 
ATOM   2816 C  C    . ALA   A 1 381 ? 375.985 3.104   95.394  1.00 38.89  ? 360  ALA   A C    1 
ATOM   2817 O  O    . ALA   A 1 381 ? 376.601 3.355   96.437  1.00 38.90  ? 360  ALA   A O    1 
ATOM   2818 C  CB   . ALA   A 1 381 ? 375.034 0.882   94.671  1.00 34.40  ? 360  ALA   A CB   1 
ATOM   2819 N  N    . PRO   A 1 382 ? 375.102 3.968   94.892  1.00 39.65  ? 361  PRO   A N    1 
ATOM   2820 C  CA   . PRO   A 1 382 ? 374.827 5.214   95.626  1.00 38.23  ? 361  PRO   A CA   1 
ATOM   2821 C  C    . PRO   A 1 382 ? 374.252 4.970   97.007  1.00 44.50  ? 361  PRO   A C    1 
ATOM   2822 O  O    . PRO   A 1 382 ? 374.445 5.796   97.908  1.00 48.20  ? 361  PRO   A O    1 
ATOM   2823 C  CB   . PRO   A 1 382 ? 373.827 5.947   94.720  1.00 43.26  ? 361  PRO   A CB   1 
ATOM   2824 C  CG   . PRO   A 1 382 ? 373.997 5.324   93.373  1.00 36.55  ? 361  PRO   A CG   1 
ATOM   2825 C  CD   . PRO   A 1 382 ? 374.347 3.889   93.632  1.00 42.69  ? 361  PRO   A CD   1 
ATOM   2826 N  N    . HIS   A 1 383 ? 373.554 3.851   97.198  1.00 45.67  ? 362  HIS   A N    1 
ATOM   2827 C  CA   . HIS   A 1 383 ? 372.919 3.527   98.467  1.00 46.16  ? 362  HIS   A CA   1 
ATOM   2828 C  C    . HIS   A 1 383 ? 373.793 2.672   99.375  1.00 46.87  ? 362  HIS   A C    1 
ATOM   2829 O  O    . HIS   A 1 383 ? 373.609 2.709   100.597 1.00 47.60  ? 362  HIS   A O    1 
ATOM   2830 C  CB   . HIS   A 1 383 ? 371.591 2.799   98.213  1.00 41.51  ? 362  HIS   A CB   1 
ATOM   2831 C  CG   . HIS   A 1 383 ? 371.721 1.611   97.310  1.00 45.71  ? 362  HIS   A CG   1 
ATOM   2832 N  ND1  . HIS   A 1 383 ? 371.746 1.722   95.936  1.00 43.39  ? 362  HIS   A ND1  1 
ATOM   2833 C  CD2  . HIS   A 1 383 ? 371.855 0.291   97.583  1.00 44.36  ? 362  HIS   A CD2  1 
ATOM   2834 C  CE1  . HIS   A 1 383 ? 371.883 0.521   95.401  1.00 44.11  ? 362  HIS   A CE1  1 
ATOM   2835 N  NE2  . HIS   A 1 383 ? 371.951 -0.365  96.379  1.00 50.75  ? 362  HIS   A NE2  1 
ATOM   2836 N  N    . LYS   A 1 384 ? 374.737 1.913   98.822  1.00 45.80  ? 363  LYS   A N    1 
ATOM   2837 C  CA   . LYS   A 1 384 ? 375.443 0.925   99.625  1.00 44.40  ? 363  LYS   A CA   1 
ATOM   2838 C  C    . LYS   A 1 384 ? 376.727 0.506   98.927  1.00 42.76  ? 363  LYS   A C    1 
ATOM   2839 O  O    . LYS   A 1 384 ? 376.860 0.604   97.705  1.00 42.61  ? 363  LYS   A O    1 
ATOM   2840 C  CB   . LYS   A 1 384 ? 374.558 -0.297  99.895  1.00 45.16  ? 363  LYS   A CB   1 
ATOM   2841 C  CG   . LYS   A 1 384 ? 375.197 -1.367  100.765 1.00 47.01  ? 363  LYS   A CG   1 
ATOM   2842 C  CD   . LYS   A 1 384 ? 375.385 -0.878  102.190 1.00 49.32  ? 363  LYS   A CD   1 
ATOM   2843 C  CE   . LYS   A 1 384 ? 375.948 -1.972  103.078 1.00 55.32  ? 363  LYS   A CE   1 
ATOM   2844 N  NZ   . LYS   A 1 384 ? 375.006 -3.117  103.199 1.00 53.88  ? 363  LYS   A NZ   1 
ATOM   2845 N  N    . GLY   A 1 385 ? 377.670 0.038   99.734  1.00 42.73  ? 364  GLY   A N    1 
ATOM   2846 C  CA   . GLY   A 1 385 ? 378.903 -0.536  99.237  1.00 36.54  ? 364  GLY   A CA   1 
ATOM   2847 C  C    . GLY   A 1 385 ? 379.609 -1.240  100.370 1.00 39.38  ? 364  GLY   A C    1 
ATOM   2848 O  O    . GLY   A 1 385 ? 379.377 -0.945  101.547 1.00 46.21  ? 364  GLY   A O    1 
ATOM   2849 N  N    . PHE   A 1 386 ? 380.459 -2.192  100.007 1.00 35.42  ? 365  PHE   A N    1 
ATOM   2850 C  CA   . PHE   A 1 386 ? 381.209 -2.933  101.010 1.00 39.40  ? 365  PHE   A CA   1 
ATOM   2851 C  C    . PHE   A 1 386 ? 382.402 -3.589  100.336 1.00 41.51  ? 365  PHE   A C    1 
ATOM   2852 O  O    . PHE   A 1 386 ? 382.501 -3.606  99.100  1.00 35.76  ? 365  PHE   A O    1 
ATOM   2853 C  CB   . PHE   A 1 386 ? 380.325 -3.972  101.727 1.00 41.25  ? 365  PHE   A CB   1 
ATOM   2854 C  CG   . PHE   A 1 386 ? 379.502 -4.840  100.805 1.00 42.63  ? 365  PHE   A CG   1 
ATOM   2855 C  CD1  . PHE   A 1 386 ? 380.085 -5.880  100.100 1.00 42.03  ? 365  PHE   A CD1  1 
ATOM   2856 C  CD2  . PHE   A 1 386 ? 378.133 -4.640  100.678 1.00 43.51  ? 365  PHE   A CD2  1 
ATOM   2857 C  CE1  . PHE   A 1 386 ? 379.327 -6.689  99.262  1.00 36.45  ? 365  PHE   A CE1  1 
ATOM   2858 C  CE2  . PHE   A 1 386 ? 377.370 -5.446  99.844  1.00 40.18  ? 365  PHE   A CE2  1 
ATOM   2859 C  CZ   . PHE   A 1 386 ? 377.970 -6.473  99.137  1.00 36.70  ? 365  PHE   A CZ   1 
ATOM   2860 N  N    . PRO   A 1 387 ? 383.343 -4.114  101.116 1.00 39.67  ? 366  PRO   A N    1 
ATOM   2861 C  CA   . PRO   A 1 387 ? 384.486 -4.806  100.520 1.00 36.41  ? 366  PRO   A CA   1 
ATOM   2862 C  C    . PRO   A 1 387 ? 384.058 -6.132  99.918  1.00 32.34  ? 366  PRO   A C    1 
ATOM   2863 O  O    . PRO   A 1 387 ? 383.129 -6.790  100.392 1.00 35.32  ? 366  PRO   A O    1 
ATOM   2864 C  CB   . PRO   A 1 387 ? 385.442 -5.013  101.704 1.00 40.70  ? 366  PRO   A CB   1 
ATOM   2865 C  CG   . PRO   A 1 387 ? 384.928 -4.104  102.799 1.00 41.89  ? 366  PRO   A CG   1 
ATOM   2866 C  CD   . PRO   A 1 387 ? 383.453 -4.023  102.581 1.00 43.20  ? 366  PRO   A CD   1 
ATOM   2867 N  N    . VAL   A 1 388 ? 384.741 -6.510  98.843  1.00 35.34  ? 367  VAL   A N    1 
ATOM   2868 C  CA   . VAL   A 1 388 ? 384.538 -7.795  98.188  1.00 34.34  ? 367  VAL   A CA   1 
ATOM   2869 C  C    . VAL   A 1 388 ? 385.910 -8.390  97.921  1.00 37.73  ? 367  VAL   A C    1 
ATOM   2870 O  O    . VAL   A 1 388 ? 386.755 -7.751  97.283  1.00 33.21  ? 367  VAL   A O    1 
ATOM   2871 C  CB   . VAL   A 1 388 ? 383.736 -7.665  96.882  1.00 34.09  ? 367  VAL   A CB   1 
ATOM   2872 C  CG1  . VAL   A 1 388 ? 383.665 -9.011  96.170  1.00 31.08  ? 367  VAL   A CG1  1 
ATOM   2873 C  CG2  . VAL   A 1 388 ? 382.340 -7.137  97.167  1.00 30.57  ? 367  VAL   A CG2  1 
ATOM   2874 N  N    . VAL   A 1 389 ? 386.142 -9.594  98.428  1.00 34.60  ? 368  VAL   A N    1 
ATOM   2875 C  CA   . VAL   A 1 389 ? 387.391 -10.307 98.207  1.00 37.29  ? 368  VAL   A CA   1 
ATOM   2876 C  C    . VAL   A 1 389 ? 387.151 -11.368 97.144  1.00 35.03  ? 368  VAL   A C    1 
ATOM   2877 O  O    . VAL   A 1 389 ? 386.162 -12.111 97.207  1.00 38.44  ? 368  VAL   A O    1 
ATOM   2878 C  CB   . VAL   A 1 389 ? 387.924 -10.924 99.515  1.00 40.42  ? 368  VAL   A CB   1 
ATOM   2879 C  CG1  . VAL   A 1 389 ? 386.827 -11.690 100.240 1.00 49.04  ? 368  VAL   A CG1  1 
ATOM   2880 C  CG2  . VAL   A 1 389 ? 389.118 -11.825 99.238  1.00 46.60  ? 368  VAL   A CG2  1 
ATOM   2881 N  N    . LEU   A 1 390 ? 388.028 -11.414 96.148  1.00 32.82  ? 369  LEU   A N    1 
ATOM   2882 C  CA   . LEU   A 1 390 ? 388.035 -12.490 95.167  1.00 39.54  ? 369  LEU   A CA   1 
ATOM   2883 C  C    . LEU   A 1 390 ? 389.055 -13.532 95.599  1.00 34.35  ? 369  LEU   A C    1 
ATOM   2884 O  O    . LEU   A 1 390 ? 390.177 -13.187 95.987  1.00 37.47  ? 369  LEU   A O    1 
ATOM   2885 C  CB   . LEU   A 1 390 ? 388.365 -11.975 93.765  1.00 34.65  ? 369  LEU   A CB   1 
ATOM   2886 C  CG   . LEU   A 1 390 ? 387.418 -10.962 93.114  1.00 39.32  ? 369  LEU   A CG   1 
ATOM   2887 C  CD1  . LEU   A 1 390 ? 387.439 -11.122 91.601  1.00 36.12  ? 369  LEU   A CD1  1 
ATOM   2888 C  CD2  . LEU   A 1 390 ? 386.001 -11.087 93.652  1.00 35.59  ? 369  LEU   A CD2  1 
ATOM   2889 N  N    . ASP   A 1 391 ? 388.662 -14.801 95.541  1.00 38.15  ? 370  ASP   A N    1 
ATOM   2890 C  CA   . ASP   A 1 391 ? 389.511 -15.912 95.950  1.00 45.39  ? 370  ASP   A CA   1 
ATOM   2891 C  C    . ASP   A 1 391 ? 389.764 -16.803 94.744  1.00 43.98  ? 370  ASP   A C    1 
ATOM   2892 O  O    . ASP   A 1 391 ? 388.816 -17.285 94.115  1.00 43.34  ? 370  ASP   A O    1 
ATOM   2893 C  CB   . ASP   A 1 391 ? 388.859 -16.708 97.084  1.00 42.07  ? 370  ASP   A CB   1 
ATOM   2894 C  CG   . ASP   A 1 391 ? 389.764 -17.795 97.637  1.00 46.91  ? 370  ASP   A CG   1 
ATOM   2895 O  OD1  . ASP   A 1 391 ? 390.893 -17.955 97.126  1.00 50.62  ? 370  ASP   A OD1  1 
ATOM   2896 O  OD2  . ASP   A 1 391 ? 389.347 -18.490 98.588  1.00 51.76  ? 370  ASP   A OD2  1 
ATOM   2897 N  N    . SER   A 1 392 ? 391.039 -17.022 94.422  1.00 41.73  ? 371  SER   A N    1 
ATOM   2898 C  CA   . SER   A 1 392 ? 391.442 -17.931 93.350  1.00 42.56  ? 371  SER   A CA   1 
ATOM   2899 C  C    . SER   A 1 392 ? 392.387 -18.977 93.928  1.00 49.63  ? 371  SER   A C    1 
ATOM   2900 O  O    . SER   A 1 392 ? 393.609 -18.761 93.978  1.00 51.10  ? 371  SER   A O    1 
ATOM   2901 C  CB   . SER   A 1 392 ? 392.095 -17.167 92.201  1.00 45.21  ? 371  SER   A CB   1 
ATOM   2902 O  OG   . SER   A 1 392 ? 392.430 -18.037 91.134  1.00 50.93  ? 371  SER   A OG   1 
ATOM   2903 N  N    . PRO   A 1 393 ? 391.873 -20.120 94.384  1.00 55.10  ? 372  PRO   A N    1 
ATOM   2904 C  CA   . PRO   A 1 393 ? 392.759 -21.168 94.906  1.00 54.29  ? 372  PRO   A CA   1 
ATOM   2905 C  C    . PRO   A 1 393 ? 393.623 -21.769 93.808  1.00 60.40  ? 372  PRO   A C    1 
ATOM   2906 O  O    . PRO   A 1 393 ? 393.258 -21.774 92.630  1.00 67.27  ? 372  PRO   A O    1 
ATOM   2907 C  CB   . PRO   A 1 393 ? 391.788 -22.210 95.476  1.00 43.93  ? 372  PRO   A CB   1 
ATOM   2908 C  CG   . PRO   A 1 393 ? 390.481 -21.495 95.629  1.00 49.57  ? 372  PRO   A CG   1 
ATOM   2909 C  CD   . PRO   A 1 393 ? 390.451 -20.467 94.542  1.00 50.91  ? 372  PRO   A CD   1 
ATOM   2910 N  N    . ARG   A 1 394 ? 394.776 -22.294 94.210  1.00 62.20  ? 373  ARG   A N    1 
ATOM   2911 C  CA   . ARG   A 1 394 ? 395.736 -22.839 93.251  1.00 61.35  ? 373  ARG   A CA   1 
ATOM   2912 C  C    . ARG   A 1 394 ? 395.645 -24.361 93.137  1.00 59.45  ? 373  ARG   A C    1 
ATOM   2913 O  O    . ARG   A 1 394 ? 394.611 -24.962 93.430  1.00 55.94  ? 373  ARG   A O    1 
ATOM   2914 C  CB   . ARG   A 1 394 ? 397.160 -22.431 93.636  1.00 56.83  ? 373  ARG   A CB   1 
ATOM   2915 N  N    . PHE   A 1 401 ? 388.612 -23.894 100.412 1.00 100.00 ? 380  PHE   A N    1 
ATOM   2916 C  CA   . PHE   A 1 401 ? 387.609 -23.483 101.388 1.00 104.56 ? 380  PHE   A CA   1 
ATOM   2917 C  C    . PHE   A 1 401 ? 387.649 -21.972 101.595 1.00 105.08 ? 380  PHE   A C    1 
ATOM   2918 O  O    . PHE   A 1 401 ? 388.727 -21.384 101.682 1.00 100.09 ? 380  PHE   A O    1 
ATOM   2919 C  CB   . PHE   A 1 401 ? 387.827 -24.204 102.719 1.00 103.50 ? 380  PHE   A CB   1 
ATOM   2920 C  CG   . PHE   A 1 401 ? 388.193 -25.654 102.570 1.00 108.14 ? 380  PHE   A CG   1 
ATOM   2921 C  CD1  . PHE   A 1 401 ? 389.520 -26.038 102.465 1.00 99.60  ? 380  PHE   A CD1  1 
ATOM   2922 C  CD2  . PHE   A 1 401 ? 387.213 -26.632 102.539 1.00 113.01 ? 380  PHE   A CD2  1 
ATOM   2923 C  CE1  . PHE   A 1 401 ? 389.863 -27.369 102.330 1.00 98.44  ? 380  PHE   A CE1  1 
ATOM   2924 C  CE2  . PHE   A 1 401 ? 387.550 -27.966 102.404 1.00 111.55 ? 380  PHE   A CE2  1 
ATOM   2925 C  CZ   . PHE   A 1 401 ? 388.877 -28.336 102.299 1.00 104.14 ? 380  PHE   A CZ   1 
ATOM   2926 N  N    . PRO   A 1 402 ? 386.477 -21.342 101.681 1.00 114.29 ? 381  PRO   A N    1 
ATOM   2927 C  CA   . PRO   A 1 402 ? 386.430 -19.881 101.841 1.00 103.83 ? 381  PRO   A CA   1 
ATOM   2928 C  C    . PRO   A 1 402 ? 387.002 -19.481 103.192 1.00 106.64 ? 381  PRO   A C    1 
ATOM   2929 O  O    . PRO   A 1 402 ? 386.552 -19.961 104.234 1.00 113.55 ? 381  PRO   A O    1 
ATOM   2930 C  CB   . PRO   A 1 402 ? 384.933 -19.555 101.741 1.00 96.35  ? 381  PRO   A CB   1 
ATOM   2931 C  CG   . PRO   A 1 402 ? 384.278 -20.806 101.213 1.00 109.36 ? 381  PRO   A CG   1 
ATOM   2932 C  CD   . PRO   A 1 402 ? 385.132 -21.937 101.681 1.00 109.40 ? 381  PRO   A CD   1 
ATOM   2933 N  N    . VAL   A 1 403 ? 388.007 -18.606 103.169 1.00 86.40  ? 382  VAL   A N    1 
ATOM   2934 C  CA   . VAL   A 1 403 ? 388.610 -18.107 104.399 1.00 76.46  ? 382  VAL   A CA   1 
ATOM   2935 C  C    . VAL   A 1 403 ? 387.489 -17.659 105.328 1.00 88.08  ? 382  VAL   A C    1 
ATOM   2936 O  O    . VAL   A 1 403 ? 386.695 -16.777 104.981 1.00 77.45  ? 382  VAL   A O    1 
ATOM   2937 C  CB   . VAL   A 1 403 ? 389.608 -16.969 104.115 1.00 70.75  ? 382  VAL   A CB   1 
ATOM   2938 C  CG1  . VAL   A 1 403 ? 390.431 -16.661 105.358 1.00 72.97  ? 382  VAL   A CG1  1 
ATOM   2939 C  CG2  . VAL   A 1 403 ? 390.513 -17.339 102.945 1.00 63.23  ? 382  VAL   A CG2  1 
ATOM   2940 N  N    . LYS   A 1 404 ? 387.405 -18.287 106.507 1.00 92.60  ? 383  LYS   A N    1 
ATOM   2941 C  CA   . LYS   A 1 404 ? 386.275 -18.058 107.403 1.00 84.32  ? 383  LYS   A CA   1 
ATOM   2942 C  C    . LYS   A 1 404 ? 386.301 -16.662 108.010 1.00 81.69  ? 383  LYS   A C    1 
ATOM   2943 O  O    . LYS   A 1 404 ? 385.239 -16.071 108.244 1.00 79.76  ? 383  LYS   A O    1 
ATOM   2944 C  CB   . LYS   A 1 404 ? 386.262 -19.118 108.507 1.00 80.46  ? 383  LYS   A CB   1 
ATOM   2945 N  N    . GLU   A 1 405 ? 387.491 -16.121 108.274 1.00 83.00  ? 384  GLU   A N    1 
ATOM   2946 C  CA   . GLU   A 1 405 ? 387.614 -14.777 108.824 1.00 78.69  ? 384  GLU   A CA   1 
ATOM   2947 C  C    . GLU   A 1 405 ? 387.398 -13.711 107.754 1.00 83.63  ? 384  GLU   A C    1 
ATOM   2948 O  O    . GLU   A 1 405 ? 387.923 -12.599 107.872 1.00 83.96  ? 384  GLU   A O    1 
ATOM   2949 C  CB   . GLU   A 1 405 ? 388.986 -14.592 109.478 1.00 69.60  ? 384  GLU   A CB   1 
ATOM   2950 N  N    . LEU   A 1 406 ? 386.629 -14.032 106.708 1.00 79.24  ? 385  LEU   A N    1 
ATOM   2951 C  CA   . LEU   A 1 406 ? 386.414 -13.088 105.615 1.00 70.21  ? 385  LEU   A CA   1 
ATOM   2952 C  C    . LEU   A 1 406 ? 384.939 -12.924 105.252 1.00 67.22  ? 385  LEU   A C    1 
ATOM   2953 O  O    . LEU   A 1 406 ? 384.369 -11.853 105.478 1.00 71.69  ? 385  LEU   A O    1 
ATOM   2954 C  CB   . LEU   A 1 406 ? 387.226 -13.505 104.385 1.00 64.35  ? 385  LEU   A CB   1 
ATOM   2955 C  CG   . LEU   A 1 406 ? 388.727 -13.233 104.523 1.00 62.98  ? 385  LEU   A CG   1 
ATOM   2956 C  CD1  . LEU   A 1 406 ? 389.462 -13.465 103.211 1.00 61.28  ? 385  LEU   A CD1  1 
ATOM   2957 C  CD2  . LEU   A 1 406 ? 388.962 -11.818 105.032 1.00 59.50  ? 385  LEU   A CD2  1 
ATOM   2958 N  N    . LEU   A 1 407 ? 384.308 -13.953 104.687 1.00 64.63  ? 386  LEU   A N    1 
ATOM   2959 C  CA   . LEU   A 1 407 ? 382.918 -13.812 104.263 1.00 65.53  ? 386  LEU   A CA   1 
ATOM   2960 C  C    . LEU   A 1 407 ? 382.010 -13.588 105.469 1.00 71.80  ? 386  LEU   A C    1 
ATOM   2961 O  O    . LEU   A 1 407 ? 382.239 -14.132 106.554 1.00 68.28  ? 386  LEU   A O    1 
ATOM   2962 C  CB   . LEU   A 1 407 ? 382.456 -15.038 103.468 1.00 62.27  ? 386  LEU   A CB   1 
ATOM   2963 C  CG   . LEU   A 1 407 ? 381.033 -14.995 102.883 1.00 67.27  ? 386  LEU   A CG   1 
ATOM   2964 C  CD1  . LEU   A 1 407 ? 380.828 -13.785 101.974 1.00 51.85  ? 386  LEU   A CD1  1 
ATOM   2965 C  CD2  . LEU   A 1 407 ? 380.678 -16.282 102.138 1.00 62.14  ? 386  LEU   A CD2  1 
ATOM   2966 N  N    . GLY   A 1 408 ? 380.977 -12.771 105.271 1.00 60.40  ? 387  GLY   A N    1 
ATOM   2967 C  CA   . GLY   A 1 408 ? 380.090 -12.371 106.337 1.00 55.99  ? 387  GLY   A CA   1 
ATOM   2968 C  C    . GLY   A 1 408 ? 379.303 -11.126 105.979 1.00 53.37  ? 387  GLY   A C    1 
ATOM   2969 O  O    . GLY   A 1 408 ? 379.223 -10.730 104.812 1.00 54.10  ? 387  GLY   A O    1 
ATOM   2970 N  N    . PRO   A 1 409 ? 378.709 -10.478 106.983 1.00 49.67  ? 388  PRO   A N    1 
ATOM   2971 C  CA   . PRO   A 1 409 ? 377.869 -9.300  106.712 1.00 47.63  ? 388  PRO   A CA   1 
ATOM   2972 C  C    . PRO   A 1 409 ? 378.697 -8.130  106.198 1.00 48.08  ? 388  PRO   A C    1 
ATOM   2973 O  O    . PRO   A 1 409 ? 379.693 -7.738  106.811 1.00 48.72  ? 388  PRO   A O    1 
ATOM   2974 C  CB   . PRO   A 1 409 ? 377.240 -8.986  108.076 1.00 50.78  ? 388  PRO   A CB   1 
ATOM   2975 C  CG   . PRO   A 1 409 ? 377.446 -10.222 108.903 1.00 53.15  ? 388  PRO   A CG   1 
ATOM   2976 C  CD   . PRO   A 1 409 ? 378.712 -10.840 108.408 1.00 50.99  ? 388  PRO   A CD   1 
ATOM   2977 N  N    . ASP   A 1 410 ? 378.263 -7.563  105.070 1.00 45.72  ? 389  ASP   A N    1 
ATOM   2978 C  CA   . ASP   A 1 410 ? 378.947 -6.437  104.431 1.00 44.71  ? 389  ASP   A CA   1 
ATOM   2979 C  C    . ASP   A 1 410 ? 380.407 -6.753  104.130 1.00 46.11  ? 389  ASP   A C    1 
ATOM   2980 O  O    . ASP   A 1 410 ? 381.266 -5.867  104.145 1.00 45.30  ? 389  ASP   A O    1 
ATOM   2981 C  CB   . ASP   A 1 410 ? 378.842 -5.163  105.272 1.00 50.00  ? 389  ASP   A CB   1 
ATOM   2982 C  CG   . ASP   A 1 410 ? 377.467 -4.536  105.201 1.00 57.48  ? 389  ASP   A CG   1 
ATOM   2983 O  OD1  . ASP   A 1 410 ? 376.740 -4.797  104.217 1.00 55.17  ? 389  ASP   A OD1  1 
ATOM   2984 O  OD2  . ASP   A 1 410 ? 377.114 -3.777  106.127 1.00 68.60  ? 389  ASP   A OD2  1 
ATOM   2985 N  N    . PHE   A 1 411 ? 380.697 -8.021  103.858 1.00 44.84  ? 390  PHE   A N    1 
ATOM   2986 C  CA   . PHE   A 1 411 ? 382.002 -8.429  103.349 1.00 45.20  ? 390  PHE   A CA   1 
ATOM   2987 C  C    . PHE   A 1 411 ? 381.741 -9.467  102.270 1.00 40.52  ? 390  PHE   A C    1 
ATOM   2988 O  O    . PHE   A 1 411 ? 381.317 -10.587 102.573 1.00 45.40  ? 390  PHE   A O    1 
ATOM   2989 C  CB   . PHE   A 1 411 ? 382.893 -8.990  104.458 1.00 51.27  ? 390  PHE   A CB   1 
ATOM   2990 C  CG   . PHE   A 1 411 ? 384.341 -8.624  104.311 1.00 44.71  ? 390  PHE   A CG   1 
ATOM   2991 C  CD1  . PHE   A 1 411 ? 385.170 -9.345  103.469 1.00 48.01  ? 390  PHE   A CD1  1 
ATOM   2992 C  CD2  . PHE   A 1 411 ? 384.872 -7.554  105.012 1.00 49.11  ? 390  PHE   A CD2  1 
ATOM   2993 C  CE1  . PHE   A 1 411 ? 386.505 -9.008  103.330 1.00 42.94  ? 390  PHE   A CE1  1 
ATOM   2994 C  CE2  . PHE   A 1 411 ? 386.204 -7.213  104.878 1.00 53.82  ? 390  PHE   A CE2  1 
ATOM   2995 C  CZ   . PHE   A 1 411 ? 387.021 -7.942  104.035 1.00 48.75  ? 390  PHE   A CZ   1 
ATOM   2996 N  N    . GLY   A 1 412 ? 381.956 -9.087  101.015 1.00 40.90  ? 391  GLY   A N    1 
ATOM   2997 C  CA   . GLY   A 1 412 ? 381.687 -9.992  99.920  1.00 39.10  ? 391  GLY   A CA   1 
ATOM   2998 C  C    . GLY   A 1 412 ? 382.830 -10.961 99.688  1.00 39.91  ? 391  GLY   A C    1 
ATOM   2999 O  O    . GLY   A 1 412 ? 383.997 -10.663 99.939  1.00 39.42  ? 391  GLY   A O    1 
ATOM   3000 N  N    . TYR   A 1 413 ? 382.481 -12.147 99.198  1.00 37.93  ? 392  TYR   A N    1 
ATOM   3001 C  CA   . TYR   A 1 413 ? 383.465 -13.185 98.919  1.00 39.42  ? 392  TYR   A CA   1 
ATOM   3002 C  C    . TYR   A 1 413 ? 383.066 -13.893 97.637  1.00 39.14  ? 392  TYR   A C    1 
ATOM   3003 O  O    . TYR   A 1 413 ? 381.989 -14.494 97.568  1.00 42.14  ? 392  TYR   A O    1 
ATOM   3004 C  CB   . TYR   A 1 413 ? 383.558 -14.178 100.078 1.00 45.94  ? 392  TYR   A CB   1 
ATOM   3005 C  CG   . TYR   A 1 413 ? 384.825 -15.001 100.088 1.00 51.05  ? 392  TYR   A CG   1 
ATOM   3006 C  CD1  . TYR   A 1 413 ? 384.954 -16.130 99.289  1.00 47.81  ? 392  TYR   A CD1  1 
ATOM   3007 C  CD2  . TYR   A 1 413 ? 385.887 -14.657 100.911 1.00 49.80  ? 392  TYR   A CD2  1 
ATOM   3008 C  CE1  . TYR   A 1 413 ? 386.112 -16.888 99.306  1.00 50.47  ? 392  TYR   A CE1  1 
ATOM   3009 C  CE2  . TYR   A 1 413 ? 387.046 -15.405 100.934 1.00 59.27  ? 392  TYR   A CE2  1 
ATOM   3010 C  CZ   . TYR   A 1 413 ? 387.155 -16.518 100.132 1.00 59.54  ? 392  TYR   A CZ   1 
ATOM   3011 O  OH   . TYR   A 1 413 ? 388.313 -17.262 100.160 1.00 62.00  ? 392  TYR   A OH   1 
ATOM   3012 N  N    . VAL   A 1 414 ? 383.931 -13.825 96.630  1.00 39.83  ? 393  VAL   A N    1 
ATOM   3013 C  CA   . VAL   A 1 414 ? 383.687 -14.445 95.334  1.00 43.78  ? 393  VAL   A CA   1 
ATOM   3014 C  C    . VAL   A 1 414 ? 384.852 -15.375 95.031  1.00 43.65  ? 393  VAL   A C    1 
ATOM   3015 O  O    . VAL   A 1 414 ? 386.006 -14.933 94.965  1.00 39.59  ? 393  VAL   A O    1 
ATOM   3016 C  CB   . VAL   A 1 414 ? 383.518 -13.397 94.223  1.00 44.56  ? 393  VAL   A CB   1 
ATOM   3017 C  CG1  . VAL   A 1 414 ? 383.219 -14.080 92.901  1.00 44.33  ? 393  VAL   A CG1  1 
ATOM   3018 C  CG2  . VAL   A 1 414 ? 382.416 -12.413 94.585  1.00 41.98  ? 393  VAL   A CG2  1 
ATOM   3019 N  N    . THR   A 1 415 ? 384.551 -16.656 94.847  1.00 47.63  ? 394  THR   A N    1 
ATOM   3020 C  CA   . THR   A 1 415 ? 385.553 -17.661 94.529  1.00 47.76  ? 394  THR   A CA   1 
ATOM   3021 C  C    . THR   A 1 415 ? 385.572 -17.942 93.032  1.00 53.57  ? 394  THR   A C    1 
ATOM   3022 O  O    . THR   A 1 415 ? 384.554 -17.825 92.344  1.00 55.12  ? 394  THR   A O    1 
ATOM   3023 C  CB   . THR   A 1 415 ? 385.293 -18.962 95.292  1.00 49.67  ? 394  THR   A CB   1 
ATOM   3024 O  OG1  . THR   A 1 415 ? 385.174 -18.683 96.692  1.00 58.46  ? 394  THR   A OG1  1 
ATOM   3025 C  CG2  . THR   A 1 415 ? 386.437 -19.941 95.073  1.00 48.37  ? 394  THR   A CG2  1 
ATOM   3026 N  N    . ARG   A 1 416 ? 386.747 -18.318 92.537  1.00 53.49  ? 395  ARG   A N    1 
ATOM   3027 C  CA   . ARG   A 1 416 ? 386.904 -18.657 91.130  1.00 56.31  ? 395  ARG   A CA   1 
ATOM   3028 C  C    . ARG   A 1 416 ? 386.271 -20.012 90.833  1.00 64.72  ? 395  ARG   A C    1 
ATOM   3029 O  O    . ARG   A 1 416 ? 386.320 -20.931 91.655  1.00 70.25  ? 395  ARG   A O    1 
ATOM   3030 C  CB   . ARG   A 1 416 ? 388.388 -18.674 90.764  1.00 51.72  ? 395  ARG   A CB   1 
ATOM   3031 C  CG   . ARG   A 1 416 ? 388.685 -18.970 89.304  1.00 53.40  ? 395  ARG   A CG   1 
ATOM   3032 C  CD   . ARG   A 1 416 ? 389.431 -17.812 88.664  1.00 47.87  ? 395  ARG   A CD   1 
ATOM   3033 N  NE   . ARG   A 1 416 ? 389.993 -18.162 87.365  1.00 50.15  ? 395  ARG   A NE   1 
ATOM   3034 C  CZ   . ARG   A 1 416 ? 391.291 -18.241 87.107  1.00 55.11  ? 395  ARG   A CZ   1 
ATOM   3035 N  NH1  . ARG   A 1 416 ? 392.197 -17.999 88.041  1.00 52.76  ? 395  ARG   A NH1  1 
ATOM   3036 N  NH2  . ARG   A 1 416 ? 391.691 -18.561 85.879  1.00 56.26  ? 395  ARG   A NH2  1 
ATOM   3037 N  N    . GLU   A 1 417 ? 385.665 -20.133 89.654  1.00 76.06  ? 396  GLU   A N    1 
ATOM   3038 C  CA   . GLU   A 1 417 ? 385.130 -21.424 89.227  1.00 83.90  ? 396  GLU   A CA   1 
ATOM   3039 C  C    . GLU   A 1 417 ? 386.264 -22.300 88.702  1.00 94.48  ? 396  GLU   A C    1 
ATOM   3040 O  O    . GLU   A 1 417 ? 387.011 -21.872 87.817  1.00 91.12  ? 396  GLU   A O    1 
ATOM   3041 C  CB   . GLU   A 1 417 ? 384.054 -21.243 88.156  1.00 86.07  ? 396  GLU   A CB   1 
ATOM   3042 C  CG   . GLU   A 1 417 ? 382.695 -20.802 88.702  1.00 92.02  ? 396  GLU   A CG   1 
ATOM   3043 C  CD   . GLU   A 1 417 ? 382.291 -19.409 88.249  1.00 91.29  ? 396  GLU   A CD   1 
ATOM   3044 O  OE1  . GLU   A 1 417 ? 382.857 -18.917 87.251  1.00 90.39  ? 396  GLU   A OE1  1 
ATOM   3045 O  OE2  . GLU   A 1 417 ? 381.406 -18.805 88.892  1.00 79.67  ? 396  GLU   A OE2  1 
ATOM   3046 N  N    . PRO   A 1 418 ? 386.419 -23.523 89.212  1.00 107.50 ? 397  PRO   A N    1 
ATOM   3047 C  CA   . PRO   A 1 418 ? 387.619 -24.309 88.896  1.00 102.28 ? 397  PRO   A CA   1 
ATOM   3048 C  C    . PRO   A 1 418 ? 387.720 -24.641 87.414  1.00 102.85 ? 397  PRO   A C    1 
ATOM   3049 O  O    . PRO   A 1 418 ? 386.717 -24.750 86.707  1.00 101.35 ? 397  PRO   A O    1 
ATOM   3050 C  CB   . PRO   A 1 418 ? 387.445 -25.581 89.738  1.00 106.15 ? 397  PRO   A CB   1 
ATOM   3051 C  CG   . PRO   A 1 418 ? 386.415 -25.235 90.774  1.00 106.04 ? 397  PRO   A CG   1 
ATOM   3052 C  CD   . PRO   A 1 418 ? 385.511 -24.239 90.122  1.00 105.49 ? 397  PRO   A CD   1 
ATOM   3053 N  N    . LEU   A 1 419 ? 388.959 -24.808 86.956  1.00 97.15  ? 398  LEU   A N    1 
ATOM   3054 C  CA   . LEU   A 1 419 ? 389.250 -25.244 85.590  1.00 90.23  ? 398  LEU   A CA   1 
ATOM   3055 C  C    . LEU   A 1 419 ? 388.461 -24.457 84.547  1.00 86.62  ? 398  LEU   A C    1 
ATOM   3056 O  O    . LEU   A 1 419 ? 388.921 -24.266 83.420  1.00 80.01  ? 398  LEU   A O    1 
ATOM   3057 C  CB   . LEU   A 1 419 ? 388.963 -26.741 85.442  1.00 76.92  ? 398  LEU   A CB   1 
ATOM   3058 N  N    . VAL   A 1 423 ? 396.305 -23.560 84.620  1.00 55.68  ? 402  VAL   A N    1 
ATOM   3059 C  CA   . VAL   A 1 423 ? 396.833 -22.210 84.774  1.00 54.32  ? 402  VAL   A CA   1 
ATOM   3060 C  C    . VAL   A 1 423 ? 398.316 -22.240 85.120  1.00 51.87  ? 402  VAL   A C    1 
ATOM   3061 O  O    . VAL   A 1 423 ? 398.818 -23.222 85.670  1.00 52.71  ? 402  VAL   A O    1 
ATOM   3062 C  CB   . VAL   A 1 423 ? 396.052 -21.418 85.844  1.00 50.40  ? 402  VAL   A CB   1 
ATOM   3063 C  CG1  . VAL   A 1 423 ? 394.585 -21.299 85.459  1.00 51.71  ? 402  VAL   A CG1  1 
ATOM   3064 C  CG2  . VAL   A 1 423 ? 396.208 -22.065 87.218  1.00 46.35  ? 402  VAL   A CG2  1 
ATOM   3065 N  N    . THR   A 1 424 ? 399.012 -21.157 84.793  1.00 47.41  ? 403  THR   A N    1 
ATOM   3066 C  CA   . THR   A 1 424 ? 400.414 -20.995 85.140  1.00 41.06  ? 403  THR   A CA   1 
ATOM   3067 C  C    . THR   A 1 424 ? 400.559 -20.049 86.323  1.00 43.95  ? 403  THR   A C    1 
ATOM   3068 O  O    . THR   A 1 424 ? 399.604 -19.408 86.771  1.00 41.91  ? 403  THR   A O    1 
ATOM   3069 C  CB   . THR   A 1 424 ? 401.225 -20.458 83.957  1.00 41.19  ? 403  THR   A CB   1 
ATOM   3070 O  OG1  . THR   A 1 424 ? 400.933 -19.066 83.777  1.00 39.78  ? 403  THR   A OG1  1 
ATOM   3071 C  CG2  . THR   A 1 424 ? 400.892 -21.217 82.681  1.00 40.15  ? 403  THR   A CG2  1 
ATOM   3072 N  N    . SER   A 1 425 ? 401.795 -19.948 86.808  1.00 38.98  ? 404  SER   A N    1 
ATOM   3073 C  CA   . SER   A 1 425 ? 402.094 -19.090 87.945  1.00 39.45  ? 404  SER   A CA   1 
ATOM   3074 C  C    . SER   A 1 425 ? 401.672 -17.645 87.717  1.00 39.04  ? 404  SER   A C    1 
ATOM   3075 O  O    . SER   A 1 425 ? 401.549 -16.891 88.688  1.00 40.35  ? 404  SER   A O    1 
ATOM   3076 C  CB   . SER   A 1 425 ? 403.588 -19.155 88.257  1.00 41.41  ? 404  SER   A CB   1 
ATOM   3077 O  OG   . SER   A 1 425 ? 403.913 -18.310 89.345  1.00 50.60  ? 404  SER   A OG   1 
ATOM   3078 N  N    . LEU   A 1 426 ? 401.454 -17.234 86.464  1.00 35.26  ? 405  LEU   A N    1 
ATOM   3079 C  CA   . LEU   A 1 426 ? 401.017 -15.865 86.213  1.00 37.99  ? 405  LEU   A CA   1 
ATOM   3080 C  C    . LEU   A 1 426 ? 399.577 -15.636 86.643  1.00 35.40  ? 405  LEU   A C    1 
ATOM   3081 O  O    . LEU   A 1 426 ? 399.178 -14.483 86.836  1.00 32.53  ? 405  LEU   A O    1 
ATOM   3082 C  CB   . LEU   A 1 426 ? 401.188 -15.508 84.736  1.00 29.66  ? 405  LEU   A CB   1 
ATOM   3083 C  CG   . LEU   A 1 426 ? 402.579 -14.980 84.375  1.00 28.06  ? 405  LEU   A CG   1 
ATOM   3084 C  CD1  . LEU   A 1 426 ? 403.639 -16.053 84.589  1.00 32.16  ? 405  LEU   A CD1  1 
ATOM   3085 C  CD2  . LEU   A 1 426 ? 402.620 -14.449 82.949  1.00 29.63  ? 405  LEU   A CD2  1 
ATOM   3086 N  N    . ASP   A 1 427 ? 398.796 -16.699 86.800  1.00 37.42  ? 406  ASP   A N    1 
ATOM   3087 C  CA   . ASP   A 1 427 ? 397.446 -16.596 87.346  1.00 38.67  ? 406  ASP   A CA   1 
ATOM   3088 C  C    . ASP   A 1 427 ? 397.563 -16.507 88.858  1.00 41.10  ? 406  ASP   A C    1 
ATOM   3089 O  O    . ASP   A 1 427 ? 397.519 -17.508 89.575  1.00 43.26  ? 406  ASP   A O    1 
ATOM   3090 C  CB   . ASP   A 1 427 ? 396.597 -17.779 86.911  1.00 38.09  ? 406  ASP   A CB   1 
ATOM   3091 C  CG   . ASP   A 1 427 ? 395.818 -17.490 85.659  1.00 49.67  ? 406  ASP   A CG   1 
ATOM   3092 O  OD1  . ASP   A 1 427 ? 396.451 -17.154 84.635  1.00 48.76  ? 406  ASP   A OD1  1 
ATOM   3093 O  OD2  . ASP   A 1 427 ? 394.574 -17.578 85.705  1.00 53.05  ? 406  ASP   A OD2  1 
ATOM   3094 N  N    . SER   A 1 428 ? 397.720 -15.283 89.347  1.00 34.07  ? 407  SER   A N    1 
ATOM   3095 C  CA   . SER   A 1 428 ? 397.939 -15.054 90.764  1.00 36.36  ? 407  SER   A CA   1 
ATOM   3096 C  C    . SER   A 1 428 ? 397.754 -13.574 91.038  1.00 28.90  ? 407  SER   A C    1 
ATOM   3097 O  O    . SER   A 1 428 ? 398.164 -12.738 90.231  1.00 29.12  ? 407  SER   A O    1 
ATOM   3098 C  CB   . SER   A 1 428 ? 399.344 -15.502 91.188  1.00 34.75  ? 407  SER   A CB   1 
ATOM   3099 O  OG   . SER   A 1 428 ? 399.745 -14.850 92.380  1.00 33.77  ? 407  SER   A OG   1 
ATOM   3100 N  N    . PHE   A 1 429 ? 397.129 -13.257 92.170  1.00 31.90  ? 408  PHE   A N    1 
ATOM   3101 C  CA   . PHE   A 1 429 ? 397.015 -11.858 92.556  1.00 32.17  ? 408  PHE   A CA   1 
ATOM   3102 C  C    . PHE   A 1 429 ? 398.368 -11.228 92.842  1.00 31.85  ? 408  PHE   A C    1 
ATOM   3103 O  O    . PHE   A 1 429 ? 398.450 -9.998  92.957  1.00 31.93  ? 408  PHE   A O    1 
ATOM   3104 C  CB   . PHE   A 1 429 ? 396.091 -11.724 93.761  1.00 31.95  ? 408  PHE   A CB   1 
ATOM   3105 C  CG   . PHE   A 1 429 ? 394.645 -11.923 93.422  1.00 32.75  ? 408  PHE   A CG   1 
ATOM   3106 C  CD1  . PHE   A 1 429 ? 393.971 -10.993 92.648  1.00 33.06  ? 408  PHE   A CD1  1 
ATOM   3107 C  CD2  . PHE   A 1 429 ? 393.962 -13.042 93.865  1.00 32.98  ? 408  PHE   A CD2  1 
ATOM   3108 C  CE1  . PHE   A 1 429 ? 392.642 -11.172 92.326  1.00 35.31  ? 408  PHE   A CE1  1 
ATOM   3109 C  CE2  . PHE   A 1 429 ? 392.631 -13.226 93.547  1.00 37.15  ? 408  PHE   A CE2  1 
ATOM   3110 C  CZ   . PHE   A 1 429 ? 391.970 -12.291 92.777  1.00 35.55  ? 408  PHE   A CZ   1 
ATOM   3111 N  N    . GLY   A 1 430 ? 399.425 -12.036 92.958  1.00 32.08  ? 409  GLY   A N    1 
ATOM   3112 C  CA   . GLY   A 1 430 ? 400.765 -11.479 92.981  1.00 30.02  ? 409  GLY   A CA   1 
ATOM   3113 C  C    . GLY   A 1 430 ? 401.168 -10.899 91.638  1.00 28.42  ? 409  GLY   A C    1 
ATOM   3114 O  O    . GLY   A 1 430 ? 402.013 -10.001 91.567  1.00 26.36  ? 409  GLY   A O    1 
ATOM   3115 N  N    . ASN   A 1 431 ? 400.576 -11.400 90.556  1.00 26.19  ? 410  ASN   A N    1 
ATOM   3116 C  CA   . ASN   A 1 431 ? 400.812 -10.867 89.222  1.00 27.86  ? 410  ASN   A CA   1 
ATOM   3117 C  C    . ASN   A 1 431 ? 399.812 -9.784  88.854  1.00 30.44  ? 410  ASN   A C    1 
ATOM   3118 O  O    . ASN   A 1 431 ? 399.610 -9.506  87.666  1.00 30.30  ? 410  ASN   A O    1 
ATOM   3119 C  CB   . ASN   A 1 431 ? 400.778 -11.992 88.182  1.00 30.77  ? 410  ASN   A CB   1 
ATOM   3120 C  CG   . ASN   A 1 431 ? 401.332 -11.562 86.844  1.00 27.75  ? 410  ASN   A CG   1 
ATOM   3121 O  OD1  . ASN   A 1 431 ? 402.240 -10.734 86.776  1.00 28.64  ? 410  ASN   A OD1  1 
ATOM   3122 N  ND2  . ASN   A 1 431 ? 400.775 -12.106 85.768  1.00 26.97  ? 410  ASN   A ND2  1 
ATOM   3123 N  N    . LEU   A 1 432 ? 399.178 -9.175  89.844  1.00 26.90  ? 411  LEU   A N    1 
ATOM   3124 C  CA   . LEU   A 1 432 ? 398.246 -8.088  89.616  1.00 27.01  ? 411  LEU   A CA   1 
ATOM   3125 C  C    . LEU   A 1 432 ? 398.603 -6.937  90.539  1.00 29.31  ? 411  LEU   A C    1 
ATOM   3126 O  O    . LEU   A 1 432 ? 398.893 -7.141  91.721  1.00 33.54  ? 411  LEU   A O    1 
ATOM   3127 C  CB   . LEU   A 1 432 ? 396.804 -8.532  89.855  1.00 28.62  ? 411  LEU   A CB   1 
ATOM   3128 C  CG   . LEU   A 1 432 ? 395.799 -8.240  88.744  1.00 38.52  ? 411  LEU   A CG   1 
ATOM   3129 C  CD1  . LEU   A 1 432 ? 396.197 -8.928  87.443  1.00 36.20  ? 411  LEU   A CD1  1 
ATOM   3130 C  CD2  . LEU   A 1 432 ? 394.418 -8.678  89.188  1.00 32.81  ? 411  LEU   A CD2  1 
ATOM   3131 N  N    . GLU   A 1 433 ? 398.599 -5.732  89.986  1.00 31.00  ? 412  GLU   A N    1 
ATOM   3132 C  CA   . GLU   A 1 433 ? 398.780 -4.520  90.764  1.00 29.44  ? 412  GLU   A CA   1 
ATOM   3133 C  C    . GLU   A 1 433 ? 397.759 -3.506  90.279  1.00 28.99  ? 412  GLU   A C    1 
ATOM   3134 O  O    . GLU   A 1 433 ? 397.204 -3.631  89.185  1.00 29.89  ? 412  GLU   A O    1 
ATOM   3135 C  CB   . GLU   A 1 433 ? 400.207 -3.963  90.634  1.00 30.24  ? 412  GLU   A CB   1 
ATOM   3136 C  CG   . GLU   A 1 433 ? 400.503 -2.782  91.551  1.00 46.81  ? 412  GLU   A CG   1 
ATOM   3137 C  CD   . GLU   A 1 433 ? 401.430 -3.140  92.699  1.00 56.85  ? 412  GLU   A CD   1 
ATOM   3138 O  OE1  . GLU   A 1 433 ? 402.363 -3.942  92.484  1.00 52.33  ? 412  GLU   A OE1  1 
ATOM   3139 O  OE2  . GLU   A 1 433 ? 401.226 -2.617  93.817  1.00 51.40  ? 412  GLU   A OE2  1 
ATOM   3140 N  N    . VAL   A 1 434 ? 397.501 -2.499  91.102  1.00 27.94  ? 413  VAL   A N    1 
ATOM   3141 C  CA   . VAL   A 1 434 ? 396.644 -1.391  90.709  1.00 27.32  ? 413  VAL   A CA   1 
ATOM   3142 C  C    . VAL   A 1 434 ? 397.376 -0.095  91.021  1.00 26.94  ? 413  VAL   A C    1 
ATOM   3143 O  O    . VAL   A 1 434 ? 397.934 0.064   92.112  1.00 30.23  ? 413  VAL   A O    1 
ATOM   3144 C  CB   . VAL   A 1 434 ? 395.273 -1.447  91.410  1.00 30.44  ? 413  VAL   A CB   1 
ATOM   3145 C  CG1  . VAL   A 1 434 ? 395.433 -1.298  92.911  1.00 31.36  ? 413  VAL   A CG1  1 
ATOM   3146 C  CG2  . VAL   A 1 434 ? 394.340 -0.385  90.838  1.00 25.85  ? 413  VAL   A CG2  1 
ATOM   3147 N  N    . SER   A 1 435 ? 397.398 0.811   90.056  1.00 29.76  ? 414  SER   A N    1 
ATOM   3148 C  CA   . SER   A 1 435 ? 398.108 2.064   90.214  1.00 28.24  ? 414  SER   A CA   1 
ATOM   3149 C  C    . SER   A 1 435 ? 397.252 3.081   90.955  1.00 30.50  ? 414  SER   A C    1 
ATOM   3150 O  O    . SER   A 1 435 ? 396.028 2.947   91.029  1.00 32.16  ? 414  SER   A O    1 
ATOM   3151 C  CB   . SER   A 1 435 ? 398.487 2.631   88.851  1.00 25.95  ? 414  SER   A CB   1 
ATOM   3152 O  OG   . SER   A 1 435 ? 397.371 3.297   88.282  1.00 28.37  ? 414  SER   A OG   1 
ATOM   3153 N  N    . PRO   A 1 436 ? 397.872 4.113   91.513  1.00 31.22  ? 415  PRO   A N    1 
ATOM   3154 C  CA   . PRO   A 1 436 ? 397.103 5.244   92.030  1.00 27.24  ? 415  PRO   A CA   1 
ATOM   3155 C  C    . PRO   A 1 436 ? 396.388 5.955   90.898  1.00 28.95  ? 415  PRO   A C    1 
ATOM   3156 O  O    . PRO   A 1 436 ? 396.680 5.708   89.718  1.00 32.63  ? 415  PRO   A O    1 
ATOM   3157 C  CB   . PRO   A 1 436 ? 398.176 6.146   92.662  1.00 33.02  ? 415  PRO   A CB   1 
ATOM   3158 C  CG   . PRO   A 1 436 ? 399.347 5.244   92.897  1.00 30.07  ? 415  PRO   A CG   1 
ATOM   3159 C  CD   . PRO   A 1 436 ? 399.314 4.257   91.774  1.00 29.17  ? 415  PRO   A CD   1 
ATOM   3160 N  N    . PRO   A 1 437 ? 395.438 6.833   91.207  1.00 31.01  ? 416  PRO   A N    1 
ATOM   3161 C  CA   . PRO   A 1 437 ? 394.825 7.644   90.152  1.00 31.48  ? 416  PRO   A CA   1 
ATOM   3162 C  C    . PRO   A 1 437 ? 395.892 8.342   89.322  1.00 30.93  ? 416  PRO   A C    1 
ATOM   3163 O  O    . PRO   A 1 437 ? 396.899 8.824   89.846  1.00 32.73  ? 416  PRO   A O    1 
ATOM   3164 C  CB   . PRO   A 1 437 ? 393.960 8.638   90.931  1.00 30.42  ? 416  PRO   A CB   1 
ATOM   3165 C  CG   . PRO   A 1 437 ? 393.611 7.905   92.188  1.00 31.39  ? 416  PRO   A CG   1 
ATOM   3166 C  CD   . PRO   A 1 437 ? 394.818 7.070   92.522  1.00 29.88  ? 416  PRO   A CD   1 
ATOM   3167 N  N    . VAL   A 1 438 ? 395.670 8.378   88.008  1.00 29.43  ? 417  VAL   A N    1 
ATOM   3168 C  CA   . VAL   A 1 438 ? 396.635 8.946   87.074  1.00 33.38  ? 417  VAL   A CA   1 
ATOM   3169 C  C    . VAL   A 1 438 ? 395.881 9.621   85.942  1.00 36.94  ? 417  VAL   A C    1 
ATOM   3170 O  O    . VAL   A 1 438 ? 394.729 9.296   85.651  1.00 35.37  ? 417  VAL   A O    1 
ATOM   3171 C  CB   . VAL   A 1 438 ? 397.603 7.883   86.498  1.00 33.31  ? 417  VAL   A CB   1 
ATOM   3172 C  CG1  . VAL   A 1 438 ? 398.515 7.337   87.587  1.00 31.23  ? 417  VAL   A CG1  1 
ATOM   3173 C  CG2  . VAL   A 1 438 ? 396.819 6.768   85.821  1.00 28.35  ? 417  VAL   A CG2  1 
ATOM   3174 N  N    . THR   A 1 439 ? 396.549 10.575  85.302  1.00 35.78  ? 418  THR   A N    1 
ATOM   3175 C  CA   . THR   A 1 439 ? 396.076 11.208  84.080  1.00 37.66  ? 418  THR   A CA   1 
ATOM   3176 C  C    . THR   A 1 439 ? 397.121 10.971  83.002  1.00 40.72  ? 418  THR   A C    1 
ATOM   3177 O  O    . THR   A 1 439 ? 398.314 11.190  83.233  1.00 41.69  ? 418  THR   A O    1 
ATOM   3178 C  CB   . THR   A 1 439 ? 395.842 12.708  84.280  1.00 45.06  ? 418  THR   A CB   1 
ATOM   3179 O  OG1  . THR   A 1 439 ? 394.850 12.907  85.296  1.00 44.52  ? 418  THR   A OG1  1 
ATOM   3180 C  CG2  . THR   A 1 439 ? 395.374 13.347  82.983  1.00 41.39  ? 418  THR   A CG2  1 
ATOM   3181 N  N    . VAL   A 1 440 ? 396.678 10.513  81.835  1.00 42.34  ? 419  VAL   A N    1 
ATOM   3182 C  CA   . VAL   A 1 440 ? 397.574 10.119  80.756  1.00 47.17  ? 419  VAL   A CA   1 
ATOM   3183 C  C    . VAL   A 1 440 ? 397.069 10.762  79.472  1.00 47.69  ? 419  VAL   A C    1 
ATOM   3184 O  O    . VAL   A 1 440 ? 395.976 10.433  78.996  1.00 48.53  ? 419  VAL   A O    1 
ATOM   3185 C  CB   . VAL   A 1 440 ? 397.663 8.594   80.608  1.00 43.66  ? 419  VAL   A CB   1 
ATOM   3186 C  CG1  . VAL   A 1 440 ? 398.781 8.220   79.645  1.00 46.34  ? 419  VAL   A CG1  1 
ATOM   3187 C  CG2  . VAL   A 1 440 ? 397.869 7.944   81.968  1.00 35.28  ? 419  VAL   A CG2  1 
ATOM   3188 N  N    . ASN   A 1 441 ? 397.868 11.663  78.904  1.00 54.72  ? 420  ASN   A N    1 
ATOM   3189 C  CA   . ASN   A 1 441 ? 397.514 12.363  77.672  1.00 56.26  ? 420  ASN   A CA   1 
ATOM   3190 C  C    . ASN   A 1 441 ? 396.103 12.939  77.763  1.00 56.69  ? 420  ASN   A C    1 
ATOM   3191 O  O    . ASN   A 1 441 ? 395.262 12.741  76.882  1.00 62.29  ? 420  ASN   A O    1 
ATOM   3192 C  CB   . ASN   A 1 441 ? 397.658 11.441  76.460  1.00 56.10  ? 420  ASN   A CB   1 
ATOM   3193 C  CG   . ASN   A 1 441 ? 399.023 10.784  76.388  1.00 72.77  ? 420  ASN   A CG   1 
ATOM   3194 O  OD1  . ASN   A 1 441 ? 399.140 9.562   76.468  1.00 77.21  ? 420  ASN   A OD1  1 
ATOM   3195 N  ND2  . ASN   A 1 441 ? 400.065 11.593  76.235  1.00 71.72  ? 420  ASN   A ND2  1 
ATOM   3196 N  N    . GLY   A 1 442 ? 395.843 13.650  78.859  1.00 53.11  ? 421  GLY   A N    1 
ATOM   3197 C  CA   . GLY   A 1 442 ? 394.558 14.271  79.085  1.00 51.24  ? 421  GLY   A CA   1 
ATOM   3198 C  C    . GLY   A 1 442 ? 393.444 13.335  79.501  1.00 51.68  ? 421  GLY   A C    1 
ATOM   3199 O  O    . GLY   A 1 442 ? 392.370 13.814  79.893  1.00 49.83  ? 421  GLY   A O    1 
ATOM   3200 N  N    . LYS   A 1 443 ? 393.651 12.022  79.431  1.00 46.60  ? 422  LYS   A N    1 
ATOM   3201 C  CA   . LYS   A 1 443 ? 392.626 11.057  79.809  1.00 43.34  ? 422  LYS   A CA   1 
ATOM   3202 C  C    . LYS   A 1 443 ? 392.842 10.650  81.260  1.00 45.46  ? 422  LYS   A C    1 
ATOM   3203 O  O    . LYS   A 1 443 ? 393.906 10.131  81.613  1.00 41.88  ? 422  LYS   A O    1 
ATOM   3204 C  CB   . LYS   A 1 443 ? 392.665 9.840   78.885  1.00 42.05  ? 422  LYS   A CB   1 
ATOM   3205 C  CG   . LYS   A 1 443 ? 391.342 9.094   78.768  1.00 45.85  ? 422  LYS   A CG   1 
ATOM   3206 C  CD   . LYS   A 1 443 ? 391.343 7.823   79.601  1.00 47.80  ? 422  LYS   A CD   1 
ATOM   3207 C  CE   . LYS   A 1 443 ? 390.094 6.989   79.355  1.00 46.56  ? 422  LYS   A CE   1 
ATOM   3208 N  NZ   . LYS   A 1 443 ? 388.853 7.688   79.789  1.00 57.62  ? 422  LYS   A NZ   1 
ATOM   3209 N  N    . THR   A 1 444 ? 391.840 10.887  82.098  1.00 43.93  ? 423  THR   A N    1 
ATOM   3210 C  CA   . THR   A 1 444 ? 391.969 10.629  83.523  1.00 42.18  ? 423  THR   A CA   1 
ATOM   3211 C  C    . THR   A 1 444 ? 391.513 9.217   83.862  1.00 39.18  ? 423  THR   A C    1 
ATOM   3212 O  O    . THR   A 1 444 ? 390.536 8.708   83.303  1.00 37.41  ? 423  THR   A O    1 
ATOM   3213 C  CB   . THR   A 1 444 ? 391.163 11.645  84.333  1.00 45.69  ? 423  THR   A CB   1 
ATOM   3214 O  OG1  . THR   A 1 444 ? 391.629 12.966  84.034  1.00 56.83  ? 423  THR   A OG1  1 
ATOM   3215 C  CG2  . THR   A 1 444 ? 391.331 11.385  85.824  1.00 40.34  ? 423  THR   A CG2  1 
ATOM   3216 N  N    . TYR   A 1 445 ? 392.245 8.583   84.777  1.00 35.91  ? 424  TYR   A N    1 
ATOM   3217 C  CA   . TYR   A 1 445 ? 391.890 7.285   85.343  1.00 34.02  ? 424  TYR   A CA   1 
ATOM   3218 C  C    . TYR   A 1 445 ? 391.729 7.505   86.841  1.00 32.21  ? 424  TYR   A C    1 
ATOM   3219 O  O    . TYR   A 1 445 ? 392.658 7.256   87.626  1.00 34.93  ? 424  TYR   A O    1 
ATOM   3220 C  CB   . TYR   A 1 445 ? 392.940 6.225   85.022  1.00 31.55  ? 424  TYR   A CB   1 
ATOM   3221 C  CG   . TYR   A 1 445 ? 393.161 6.049   83.539  1.00 33.44  ? 424  TYR   A CG   1 
ATOM   3222 C  CD1  . TYR   A 1 445 ? 394.043 6.871   82.850  1.00 34.96  ? 424  TYR   A CD1  1 
ATOM   3223 C  CD2  . TYR   A 1 445 ? 392.477 5.074   82.823  1.00 30.52  ? 424  TYR   A CD2  1 
ATOM   3224 C  CE1  . TYR   A 1 445 ? 394.246 6.723   81.494  1.00 34.27  ? 424  TYR   A CE1  1 
ATOM   3225 C  CE2  . TYR   A 1 445 ? 392.675 4.918   81.463  1.00 36.36  ? 424  TYR   A CE2  1 
ATOM   3226 C  CZ   . TYR   A 1 445 ? 393.562 5.747   80.805  1.00 35.94  ? 424  TYR   A CZ   1 
ATOM   3227 O  OH   . TYR   A 1 445 ? 393.773 5.611   79.451  1.00 35.98  ? 424  TYR   A OH   1 
ATOM   3228 N  N    . PRO   A 1 446 ? 390.564 7.993   87.274  1.00 34.45  ? 425  PRO   A N    1 
ATOM   3229 C  CA   . PRO   A 1 446 ? 390.403 8.389   88.681  1.00 30.59  ? 425  PRO   A CA   1 
ATOM   3230 C  C    . PRO   A 1 446 ? 390.484 7.236   89.663  1.00 29.30  ? 425  PRO   A C    1 
ATOM   3231 O  O    . PRO   A 1 446 ? 390.612 7.488   90.868  1.00 33.43  ? 425  PRO   A O    1 
ATOM   3232 C  CB   . PRO   A 1 446 ? 389.015 9.041   88.703  1.00 36.18  ? 425  PRO   A CB   1 
ATOM   3233 C  CG   . PRO   A 1 446 ? 388.294 8.435   87.540  1.00 35.48  ? 425  PRO   A CG   1 
ATOM   3234 C  CD   . PRO   A 1 446 ? 389.338 8.209   86.487  1.00 36.65  ? 425  PRO   A CD   1 
ATOM   3235 N  N    . LEU   A 1 447 ? 390.416 5.990   89.200  1.00 32.00  ? 426  LEU   A N    1 
ATOM   3236 C  CA   . LEU   A 1 447 ? 390.546 4.826   90.063  1.00 28.74  ? 426  LEU   A CA   1 
ATOM   3237 C  C    . LEU   A 1 447 ? 391.831 4.050   89.793  1.00 31.02  ? 426  LEU   A C    1 
ATOM   3238 O  O    . LEU   A 1 447 ? 391.966 2.910   90.254  1.00 27.42  ? 426  LEU   A O    1 
ATOM   3239 C  CB   . LEU   A 1 447 ? 389.320 3.920   89.906  1.00 29.32  ? 426  LEU   A CB   1 
ATOM   3240 C  CG   . LEU   A 1 447 ? 387.957 4.601   90.063  1.00 31.49  ? 426  LEU   A CG   1 
ATOM   3241 C  CD1  . LEU   A 1 447 ? 386.828 3.610   89.818  1.00 29.50  ? 426  LEU   A CD1  1 
ATOM   3242 C  CD2  . LEU   A 1 447 ? 387.802 5.257   91.432  1.00 33.66  ? 426  LEU   A CD2  1 
ATOM   3243 N  N    . GLY   A 1 448 ? 392.785 4.647   89.075  1.00 25.74  ? 427  GLY   A N    1 
ATOM   3244 C  CA   . GLY   A 1 448 ? 394.018 3.967   88.749  1.00 26.44  ? 427  GLY   A CA   1 
ATOM   3245 C  C    . GLY   A 1 448 ? 393.815 2.966   87.631  1.00 26.46  ? 427  GLY   A C    1 
ATOM   3246 O  O    . GLY   A 1 448 ? 392.734 2.826   87.056  1.00 29.68  ? 427  GLY   A O    1 
ATOM   3247 N  N    . ARG   A 1 449 ? 394.889 2.249   87.317  1.00 25.69  ? 428  ARG   A N    1 
ATOM   3248 C  CA   . ARG   A 1 449 ? 394.848 1.235   86.276  1.00 22.97  ? 428  ARG   A CA   1 
ATOM   3249 C  C    . ARG   A 1 449 ? 395.410 -0.069  86.816  1.00 26.40  ? 428  ARG   A C    1 
ATOM   3250 O  O    . ARG   A 1 449 ? 396.420 -0.076  87.527  1.00 28.02  ? 428  ARG   A O    1 
ATOM   3251 C  CB   . ARG   A 1 449 ? 395.628 1.681   85.034  1.00 23.95  ? 428  ARG   A CB   1 
ATOM   3252 C  CG   . ARG   A 1 449 ? 395.168 3.018   84.476  1.00 25.44  ? 428  ARG   A CG   1 
ATOM   3253 C  CD   . ARG   A 1 449 ? 395.840 3.337   83.154  1.00 26.66  ? 428  ARG   A CD   1 
ATOM   3254 N  NE   . ARG   A 1 449 ? 395.311 2.524   82.067  1.00 27.91  ? 428  ARG   A NE   1 
ATOM   3255 C  CZ   . ARG   A 1 449 ? 395.764 2.556   80.821  1.00 29.29  ? 428  ARG   A CZ   1 
ATOM   3256 N  NH1  . ARG   A 1 449 ? 396.773 3.336   80.472  1.00 27.72  ? 428  ARG   A NH1  1 
ATOM   3257 N  NH2  . ARG   A 1 449 ? 395.190 1.783   79.903  1.00 32.06  ? 428  ARG   A NH2  1 
ATOM   3258 N  N    . ILE   A 1 450 ? 394.744 -1.167  86.485  1.00 25.68  ? 429  ILE   A N    1 
ATOM   3259 C  CA   . ILE   A 1 450 ? 395.220 -2.486  86.876  1.00 24.38  ? 429  ILE   A CA   1 
ATOM   3260 C  C    . ILE   A 1 450 ? 396.377 -2.884  85.974  1.00 26.04  ? 429  ILE   A C    1 
ATOM   3261 O  O    . ILE   A 1 450 ? 396.353 -2.651  84.759  1.00 23.94  ? 429  ILE   A O    1 
ATOM   3262 C  CB   . ILE   A 1 450 ? 394.080 -3.515  86.815  1.00 24.39  ? 429  ILE   A CB   1 
ATOM   3263 C  CG1  . ILE   A 1 450 ? 393.083 -3.263  87.943  1.00 20.14  ? 429  ILE   A CG1  1 
ATOM   3264 C  CG2  . ILE   A 1 450 ? 394.636 -4.923  86.905  1.00 30.37  ? 429  ILE   A CG2  1 
ATOM   3265 C  CD1  . ILE   A 1 450 ? 391.818 -4.082  87.829  1.00 26.37  ? 429  ILE   A CD1  1 
ATOM   3266 N  N    . LEU   A 1 451 ? 397.400 -3.485  86.572  1.00 24.53  ? 430  LEU   A N    1 
ATOM   3267 C  CA   . LEU   A 1 451 ? 398.605 -3.888  85.865  1.00 24.53  ? 430  LEU   A CA   1 
ATOM   3268 C  C    . LEU   A 1 451 ? 398.731 -5.400  85.947  1.00 22.05  ? 430  LEU   A C    1 
ATOM   3269 O  O    . LEU   A 1 451 ? 398.604 -5.978  87.032  1.00 29.65  ? 430  LEU   A O    1 
ATOM   3270 C  CB   . LEU   A 1 451 ? 399.831 -3.199  86.461  1.00 25.82  ? 430  LEU   A CB   1 
ATOM   3271 C  CG   . LEU   A 1 451 ? 399.641 -1.678  86.506  1.00 28.67  ? 430  LEU   A CG   1 
ATOM   3272 C  CD1  . LEU   A 1 451 ? 400.605 -1.023  87.474  1.00 28.99  ? 430  LEU   A CD1  1 
ATOM   3273 C  CD2  . LEU   A 1 451 ? 399.789 -1.090  85.112  1.00 22.17  ? 430  LEU   A CD2  1 
ATOM   3274 N  N    . ILE   A 1 452 ? 398.968 -6.034  84.800  1.00 25.72  ? 431  ILE   A N    1 
ATOM   3275 C  CA   . ILE   A 1 452 ? 398.983 -7.487  84.675  1.00 24.56  ? 431  ILE   A CA   1 
ATOM   3276 C  C    . ILE   A 1 452 ? 400.308 -7.900  84.053  1.00 23.21  ? 431  ILE   A C    1 
ATOM   3277 O  O    . ILE   A 1 452 ? 400.666 -7.419  82.972  1.00 28.31  ? 431  ILE   A O    1 
ATOM   3278 C  CB   . ILE   A 1 452 ? 397.809 -7.993  83.812  1.00 26.37  ? 431  ILE   A CB   1 
ATOM   3279 C  CG1  . ILE   A 1 452 ? 396.472 -7.523  84.381  1.00 33.94  ? 431  ILE   A CG1  1 
ATOM   3280 C  CG2  . ILE   A 1 452 ? 397.834 -9.509  83.691  1.00 31.64  ? 431  ILE   A CG2  1 
ATOM   3281 C  CD1  . ILE   A 1 452 ? 395.289 -7.936  83.533  1.00 39.84  ? 431  ILE   A CD1  1 
ATOM   3282 N  N    . GLY   A 1 453 ? 401.032 -8.793  84.724  1.00 26.05  ? 432  GLY   A N    1 
ATOM   3283 C  CA   . GLY   A 1 453 ? 402.264 -9.307  84.153  1.00 23.22  ? 432  GLY   A CA   1 
ATOM   3284 C  C    . GLY   A 1 453 ? 401.978 -10.267 83.010  1.00 24.95  ? 432  GLY   A C    1 
ATOM   3285 O  O    . GLY   A 1 453 ? 401.067 -11.094 83.077  1.00 28.46  ? 432  GLY   A O    1 
ATOM   3286 N  N    . SER   A 1 454 ? 402.770 -10.156 81.947  1.00 26.11  ? 433  SER   A N    1 
ATOM   3287 C  CA   . SER   A 1 454 ? 402.546 -10.963 80.756  1.00 27.66  ? 433  SER   A CA   1 
ATOM   3288 C  C    . SER   A 1 454 ? 403.890 -11.236 80.087  1.00 33.07  ? 433  SER   A C    1 
ATOM   3289 O  O    . SER   A 1 454 ? 404.953 -10.987 80.662  1.00 29.48  ? 433  SER   A O    1 
ATOM   3290 C  CB   . SER   A 1 454 ? 401.561 -10.257 79.818  1.00 31.88  ? 433  SER   A CB   1 
ATOM   3291 O  OG   . SER   A 1 454 ? 401.232 -11.078 78.711  1.00 40.54  ? 433  SER   A OG   1 
ATOM   3292 N  N    . SER   A 1 455 ? 403.840 -11.767 78.871  1.00 30.30  ? 434  SER   A N    1 
ATOM   3293 C  CA   . SER   A 1 455 ? 405.018 -11.977 78.039  1.00 34.81  ? 434  SER   A CA   1 
ATOM   3294 C  C    . SER   A 1 455 ? 404.884 -11.171 76.751  1.00 35.35  ? 434  SER   A C    1 
ATOM   3295 O  O    . SER   A 1 455 ? 403.850 -10.557 76.480  1.00 34.15  ? 434  SER   A O    1 
ATOM   3296 C  CB   . SER   A 1 455 ? 405.217 -13.463 77.732  1.00 34.18  ? 434  SER   A CB   1 
ATOM   3297 O  OG   . SER   A 1 455 ? 404.071 -13.999 77.092  1.00 35.61  ? 434  SER   A OG   1 
ATOM   3298 N  N    . PHE   A 1 456 ? 405.945 -11.194 75.951  1.00 37.94  ? 435  PHE   A N    1 
ATOM   3299 C  CA   . PHE   A 1 456 ? 405.941 -10.494 74.680  1.00 36.39  ? 435  PHE   A CA   1 
ATOM   3300 C  C    . PHE   A 1 456 ? 405.058 -11.222 73.668  1.00 42.07  ? 435  PHE   A C    1 
ATOM   3301 O  O    . PHE   A 1 456 ? 404.954 -12.452 73.690  1.00 42.51  ? 435  PHE   A O    1 
ATOM   3302 C  CB   . PHE   A 1 456 ? 407.359 -10.373 74.132  1.00 36.96  ? 435  PHE   A CB   1 
ATOM   3303 C  CG   . PHE   A 1 456 ? 408.264 -9.506  74.961  1.00 40.62  ? 435  PHE   A CG   1 
ATOM   3304 C  CD1  . PHE   A 1 456 ? 407.774 -8.382  75.607  1.00 38.90  ? 435  PHE   A CD1  1 
ATOM   3305 C  CD2  . PHE   A 1 456 ? 409.608 -9.817  75.093  1.00 43.23  ? 435  PHE   A CD2  1 
ATOM   3306 C  CE1  . PHE   A 1 456 ? 408.610 -7.582  76.370  1.00 36.85  ? 435  PHE   A CE1  1 
ATOM   3307 C  CE2  . PHE   A 1 456 ? 410.451 -9.024  75.854  1.00 42.85  ? 435  PHE   A CE2  1 
ATOM   3308 C  CZ   . PHE   A 1 456 ? 409.950 -7.903  76.494  1.00 40.48  ? 435  PHE   A CZ   1 
ATOM   3309 N  N    . PRO   A 1 457 ? 404.431 -10.481 72.751  1.00 42.79  ? 436  PRO   A N    1 
ATOM   3310 C  CA   . PRO   A 1 457 ? 403.491 -11.114 71.806  1.00 46.23  ? 436  PRO   A CA   1 
ATOM   3311 C  C    . PRO   A 1 457 ? 404.052 -12.320 71.066  1.00 46.45  ? 436  PRO   A C    1 
ATOM   3312 O  O    . PRO   A 1 457 ? 403.381 -13.356 70.977  1.00 48.17  ? 436  PRO   A O    1 
ATOM   3313 C  CB   . PRO   A 1 457 ? 403.152 -9.963  70.849  1.00 38.60  ? 436  PRO   A CB   1 
ATOM   3314 C  CG   . PRO   A 1 457 ? 403.375 -8.724  71.654  1.00 40.51  ? 436  PRO   A CG   1 
ATOM   3315 C  CD   . PRO   A 1 457 ? 404.540 -9.027  72.544  1.00 39.08  ? 436  PRO   A CD   1 
ATOM   3316 N  N    . LEU   A 1 458 ? 405.262 -12.212 70.521  1.00 43.05  ? 437  LEU   A N    1 
ATOM   3317 C  CA   . LEU   A 1 458 ? 405.851 -13.271 69.711  1.00 46.87  ? 437  LEU   A CA   1 
ATOM   3318 C  C    . LEU   A 1 458 ? 406.732 -14.221 70.513  1.00 45.26  ? 437  LEU   A C    1 
ATOM   3319 O  O    . LEU   A 1 458 ? 407.475 -15.007 69.916  1.00 50.72  ? 437  LEU   A O    1 
ATOM   3320 C  CB   . LEU   A 1 458 ? 406.670 -12.663 68.568  1.00 39.92  ? 437  LEU   A CB   1 
ATOM   3321 C  CG   . LEU   A 1 458 ? 405.934 -11.714 67.623  1.00 45.11  ? 437  LEU   A CG   1 
ATOM   3322 C  CD1  . LEU   A 1 458 ? 406.857 -11.248 66.508  1.00 40.20  ? 437  LEU   A CD1  1 
ATOM   3323 C  CD2  . LEU   A 1 458 ? 404.678 -12.367 67.056  1.00 42.00  ? 437  LEU   A CD2  1 
ATOM   3324 N  N    . SER   A 1 459 ? 406.663 -14.174 71.841  1.00 45.45  ? 438  SER   A N    1 
ATOM   3325 C  CA   . SER   A 1 459 ? 407.602 -14.913 72.674  1.00 41.07  ? 438  SER   A CA   1 
ATOM   3326 C  C    . SER   A 1 459 ? 407.248 -16.381 72.840  1.00 44.09  ? 438  SER   A C    1 
ATOM   3327 O  O    . SER   A 1 459 ? 408.142 -17.187 73.118  1.00 45.56  ? 438  SER   A O    1 
ATOM   3328 C  CB   . SER   A 1 459 ? 407.675 -14.278 74.059  1.00 38.27  ? 438  SER   A CB   1 
ATOM   3329 O  OG   . SER   A 1 459 ? 406.436 -14.451 74.729  1.00 39.51  ? 438  SER   A OG   1 
ATOM   3330 N  N    . GLY   A 1 460 ? 405.980 -16.749 72.683  1.00 43.26  ? 439  GLY   A N    1 
ATOM   3331 C  CA   . GLY   A 1 460 ? 405.556 -18.054 73.130  1.00 38.80  ? 439  GLY   A CA   1 
ATOM   3332 C  C    . GLY   A 1 460 ? 405.622 -18.242 74.628  1.00 42.64  ? 439  GLY   A C    1 
ATOM   3333 O  O    . GLY   A 1 460 ? 405.510 -19.375 75.101  1.00 47.60  ? 439  GLY   A O    1 
ATOM   3334 N  N    . GLY   A 1 461 ? 405.798 -17.163 75.392  1.00 37.43  ? 440  GLY   A N    1 
ATOM   3335 C  CA   . GLY   A 1 461 ? 405.912 -17.256 76.830  1.00 36.78  ? 440  GLY   A CA   1 
ATOM   3336 C  C    . GLY   A 1 461 ? 404.564 -17.362 77.514  1.00 34.63  ? 440  GLY   A C    1 
ATOM   3337 O  O    . GLY   A 1 461 ? 403.509 -17.448 76.886  1.00 40.10  ? 440  GLY   A O    1 
ATOM   3338 N  N    . ARG   A 1 462 ? 404.608 -17.349 78.841  1.00 38.20  ? 441  ARG   A N    1 
ATOM   3339 C  CA   . ARG   A 1 462 ? 403.391 -17.496 79.622  1.00 38.57  ? 441  ARG   A CA   1 
ATOM   3340 C  C    . ARG   A 1 462 ? 402.574 -16.207 79.600  1.00 34.35  ? 441  ARG   A C    1 
ATOM   3341 O  O    . ARG   A 1 462 ? 403.087 -15.110 79.369  1.00 34.78  ? 441  ARG   A O    1 
ATOM   3342 C  CB   . ARG   A 1 462 ? 403.716 -17.889 81.065  1.00 32.56  ? 441  ARG   A CB   1 
ATOM   3343 C  CG   . ARG   A 1 462 ? 404.442 -19.221 81.209  1.00 33.99  ? 441  ARG   A CG   1 
ATOM   3344 C  CD   . ARG   A 1 462 ? 404.933 -19.432 82.636  1.00 37.84  ? 441  ARG   A CD   1 
ATOM   3345 N  NE   . ARG   A 1 462 ? 405.901 -18.416 83.038  1.00 36.01  ? 441  ARG   A NE   1 
ATOM   3346 C  CZ   . ARG   A 1 462 ? 406.336 -18.242 84.279  1.00 32.31  ? 441  ARG   A CZ   1 
ATOM   3347 N  NH1  . ARG   A 1 462 ? 405.903 -18.998 85.276  1.00 36.00  ? 441  ARG   A NH1  1 
ATOM   3348 N  NH2  . ARG   A 1 462 ? 407.223 -17.282 84.526  1.00 31.43  ? 441  ARG   A NH2  1 
ATOM   3349 N  N    . ARG   A 1 463 ? 401.278 -16.357 79.846  1.00 35.39  ? 442  ARG   A N    1 
ATOM   3350 C  CA   . ARG   A 1 463 ? 400.373 -15.223 79.886  1.00 33.89  ? 442  ARG   A CA   1 
ATOM   3351 C  C    . ARG   A 1 463 ? 399.270 -15.547 80.879  1.00 35.64  ? 442  ARG   A C    1 
ATOM   3352 O  O    . ARG   A 1 463 ? 398.868 -16.706 81.003  1.00 37.24  ? 442  ARG   A O    1 
ATOM   3353 C  CB   . ARG   A 1 463 ? 399.791 -14.929 78.499  1.00 33.81  ? 442  ARG   A CB   1 
ATOM   3354 C  CG   . ARG   A 1 463 ? 399.101 -13.583 78.386  1.00 45.22  ? 442  ARG   A CG   1 
ATOM   3355 C  CD   . ARG   A 1 463 ? 398.683 -13.279 76.955  1.00 44.92  ? 442  ARG   A CD   1 
ATOM   3356 N  NE   . ARG   A 1 463 ? 398.104 -11.944 76.845  1.00 50.99  ? 442  ARG   A NE   1 
ATOM   3357 C  CZ   . ARG   A 1 463 ? 397.518 -11.464 75.756  1.00 51.75  ? 442  ARG   A CZ   1 
ATOM   3358 N  NH1  . ARG   A 1 463 ? 397.411 -12.185 74.652  1.00 47.72  ? 442  ARG   A NH1  1 
ATOM   3359 N  NH2  . ARG   A 1 463 ? 397.022 -10.229 75.778  1.00 45.52  ? 442  ARG   A NH2  1 
ATOM   3360 N  N    . MET   A 1 464 ? 398.802 -14.534 81.602  1.00 32.46  ? 443  MET   A N    1 
ATOM   3361 C  CA   . MET   A 1 464 ? 397.642 -14.745 82.455  1.00 37.62  ? 443  MET   A CA   1 
ATOM   3362 C  C    . MET   A 1 464 ? 396.498 -15.293 81.614  1.00 35.88  ? 443  MET   A C    1 
ATOM   3363 O  O    . MET   A 1 464 ? 396.329 -14.917 80.451  1.00 35.58  ? 443  MET   A O    1 
ATOM   3364 C  CB   . MET   A 1 464 ? 397.232 -13.443 83.138  1.00 36.94  ? 443  MET   A CB   1 
ATOM   3365 C  CG   . MET   A 1 464 ? 396.250 -13.641 84.272  1.00 37.20  ? 443  MET   A CG   1 
ATOM   3366 S  SD   . MET   A 1 464 ? 396.041 -12.142 85.242  1.00 50.72  ? 443  MET   A SD   1 
ATOM   3367 C  CE   . MET   A 1 464 ? 397.419 -12.273 86.378  1.00 35.22  ? 443  MET   A CE   1 
ATOM   3368 N  N    . THR   A 1 465 ? 395.723 -16.209 82.192  1.00 33.81  ? 444  THR   A N    1 
ATOM   3369 C  CA   . THR   A 1 465 ? 394.666 -16.844 81.418  1.00 39.42  ? 444  THR   A CA   1 
ATOM   3370 C  C    . THR   A 1 465 ? 393.678 -15.799 80.913  1.00 34.67  ? 444  THR   A C    1 
ATOM   3371 O  O    . THR   A 1 465 ? 393.420 -14.783 81.564  1.00 35.52  ? 444  THR   A O    1 
ATOM   3372 C  CB   . THR   A 1 465 ? 393.936 -17.910 82.241  1.00 42.89  ? 444  THR   A CB   1 
ATOM   3373 O  OG1  . THR   A 1 465 ? 393.440 -17.338 83.456  1.00 46.43  ? 444  THR   A OG1  1 
ATOM   3374 C  CG2  . THR   A 1 465 ? 394.865 -19.069 82.565  1.00 43.90  ? 444  THR   A CG2  1 
ATOM   3375 N  N    . LYS   A 1 466 ? 393.128 -16.064 79.727  1.00 33.65  ? 445  LYS   A N    1 
ATOM   3376 C  CA   . LYS   A 1 466 ? 392.251 -15.099 79.074  1.00 38.29  ? 445  LYS   A CA   1 
ATOM   3377 C  C    . LYS   A 1 466 ? 391.023 -14.774 79.916  1.00 36.53  ? 445  LYS   A C    1 
ATOM   3378 O  O    . LYS   A 1 466 ? 390.523 -13.644 79.870  1.00 34.56  ? 445  LYS   A O    1 
ATOM   3379 C  CB   . LYS   A 1 466 ? 391.824 -15.629 77.705  1.00 37.88  ? 445  LYS   A CB   1 
ATOM   3380 C  CG   . LYS   A 1 466 ? 390.946 -14.674 76.924  1.00 40.61  ? 445  LYS   A CG   1 
ATOM   3381 C  CD   . LYS   A 1 466 ? 390.372 -15.330 75.680  1.00 50.51  ? 445  LYS   A CD   1 
ATOM   3382 C  CE   . LYS   A 1 466 ? 389.514 -14.346 74.905  1.00 52.08  ? 445  LYS   A CE   1 
ATOM   3383 N  NZ   . LYS   A 1 466 ? 390.272 -13.095 74.623  1.00 55.10  ? 445  LYS   A NZ   1 
ATOM   3384 N  N    . VAL   A 1 467 ? 390.514 -15.742 80.681  1.00 37.60  ? 446  VAL   A N    1 
ATOM   3385 C  CA   . VAL   A 1 467 ? 389.320 -15.482 81.482  1.00 36.05  ? 446  VAL   A CA   1 
ATOM   3386 C  C    . VAL   A 1 467 ? 389.594 -14.396 82.512  1.00 34.31  ? 446  VAL   A C    1 
ATOM   3387 O  O    . VAL   A 1 467 ? 388.753 -13.521 82.755  1.00 33.09  ? 446  VAL   A O    1 
ATOM   3388 C  CB   . VAL   A 1 467 ? 388.822 -16.772 82.155  1.00 41.02  ? 446  VAL   A CB   1 
ATOM   3389 C  CG1  . VAL   A 1 467 ? 389.884 -17.322 83.085  1.00 47.32  ? 446  VAL   A CG1  1 
ATOM   3390 C  CG2  . VAL   A 1 467 ? 387.540 -16.488 82.921  1.00 45.48  ? 446  VAL   A CG2  1 
ATOM   3391 N  N    . VAL   A 1 468 ? 390.764 -14.441 83.147  1.00 29.64  ? 447  VAL   A N    1 
ATOM   3392 C  CA   . VAL   A 1 468 ? 391.093 -13.429 84.144  1.00 30.97  ? 447  VAL   A CA   1 
ATOM   3393 C  C    . VAL   A 1 468 ? 391.222 -12.061 83.487  1.00 33.86  ? 447  VAL   A C    1 
ATOM   3394 O  O    . VAL   A 1 468 ? 390.615 -11.081 83.934  1.00 32.01  ? 447  VAL   A O    1 
ATOM   3395 C  CB   . VAL   A 1 468 ? 392.375 -13.811 84.905  1.00 30.83  ? 447  VAL   A CB   1 
ATOM   3396 C  CG1  . VAL   A 1 468 ? 392.731 -12.724 85.903  1.00 32.86  ? 447  VAL   A CG1  1 
ATOM   3397 C  CG2  . VAL   A 1 468 ? 392.197 -15.145 85.612  1.00 37.74  ? 447  VAL   A CG2  1 
ATOM   3398 N  N    . ARG   A 1 469 ? 392.007 -11.975 82.412  1.00 31.89  ? 448  ARG   A N    1 
ATOM   3399 C  CA   . ARG   A 1 469 ? 392.194 -10.694 81.741  1.00 30.51  ? 448  ARG   A CA   1 
ATOM   3400 C  C    . ARG   A 1 469 ? 390.870 -10.144 81.229  1.00 28.97  ? 448  ARG   A C    1 
ATOM   3401 O  O    . ARG   A 1 469 ? 390.601 -8.942  81.349  1.00 27.48  ? 448  ARG   A O    1 
ATOM   3402 C  CB   . ARG   A 1 469 ? 393.199 -10.841 80.598  1.00 32.39  ? 448  ARG   A CB   1 
ATOM   3403 C  CG   . ARG   A 1 469 ? 394.632 -11.043 81.061  1.00 36.38  ? 448  ARG   A CG   1 
ATOM   3404 C  CD   . ARG   A 1 469 ? 395.608 -11.043 79.894  1.00 41.10  ? 448  ARG   A CD   1 
ATOM   3405 N  NE   . ARG   A 1 469 ? 395.618 -12.310 79.171  1.00 38.47  ? 448  ARG   A NE   1 
ATOM   3406 C  CZ   . ARG   A 1 469 ? 395.007 -12.521 78.014  1.00 41.75  ? 448  ARG   A CZ   1 
ATOM   3407 N  NH1  . ARG   A 1 469 ? 394.316 -11.567 77.411  1.00 44.72  ? 448  ARG   A NH1  1 
ATOM   3408 N  NH2  . ARG   A 1 469 ? 395.096 -13.720 77.443  1.00 39.76  ? 448  ARG   A NH2  1 
ATOM   3409 N  N    . ASP   A 1 470 ? 390.028 -11.007 80.658  1.00 27.46  ? 449  ASP   A N    1 
ATOM   3410 C  CA   . ASP   A 1 470 ? 388.729 -10.555 80.171  1.00 29.59  ? 449  ASP   A CA   1 
ATOM   3411 C  C    . ASP   A 1 470 ? 387.854 -10.053 81.310  1.00 28.38  ? 449  ASP   A C    1 
ATOM   3412 O  O    . ASP   A 1 470 ? 387.125 -9.066  81.153  1.00 31.21  ? 449  ASP   A O    1 
ATOM   3413 C  CB   . ASP   A 1 470 ? 388.023 -11.683 79.424  1.00 33.56  ? 449  ASP   A CB   1 
ATOM   3414 C  CG   . ASP   A 1 470 ? 388.624 -11.940 78.067  1.00 43.73  ? 449  ASP   A CG   1 
ATOM   3415 O  OD1  . ASP   A 1 470 ? 389.414 -11.095 77.599  1.00 47.74  ? 449  ASP   A OD1  1 
ATOM   3416 O  OD2  . ASP   A 1 470 ? 388.311 -12.992 77.473  1.00 48.18  ? 449  ASP   A OD2  1 
ATOM   3417 N  N    . PHE   A 1 471 ? 387.895 -10.727 82.461  1.00 26.16  ? 450  PHE   A N    1 
ATOM   3418 C  CA   . PHE   A 1 471 ? 387.088 -10.274 83.589  1.00 27.10  ? 450  PHE   A CA   1 
ATOM   3419 C  C    . PHE   A 1 471 ? 387.540 -8.904  84.074  1.00 25.57  ? 450  PHE   A C    1 
ATOM   3420 O  O    . PHE   A 1 471 ? 386.708 -8.028  84.336  1.00 26.15  ? 450  PHE   A O    1 
ATOM   3421 C  CB   . PHE   A 1 471 ? 387.143 -11.284 84.735  1.00 30.35  ? 450  PHE   A CB   1 
ATOM   3422 C  CG   . PHE   A 1 471 ? 386.494 -10.794 86.001  1.00 29.45  ? 450  PHE   A CG   1 
ATOM   3423 C  CD1  . PHE   A 1 471 ? 385.120 -10.876 86.171  1.00 31.74  ? 450  PHE   A CD1  1 
ATOM   3424 C  CD2  . PHE   A 1 471 ? 387.258 -10.245 87.016  1.00 29.68  ? 450  PHE   A CD2  1 
ATOM   3425 C  CE1  . PHE   A 1 471 ? 384.522 -10.410 87.328  1.00 31.09  ? 450  PHE   A CE1  1 
ATOM   3426 C  CE2  . PHE   A 1 471 ? 386.666 -9.788  88.181  1.00 31.01  ? 450  PHE   A CE2  1 
ATOM   3427 C  CZ   . PHE   A 1 471 ? 385.297 -9.877  88.339  1.00 32.17  ? 450  PHE   A CZ   1 
ATOM   3428 N  N    . LEU   A 1 472 ? 388.854 -8.698  84.200  1.00 24.78  ? 451  LEU   A N    1 
ATOM   3429 C  CA   . LEU   A 1 472 ? 389.353 -7.413  84.682  1.00 26.34  ? 451  LEU   A CA   1 
ATOM   3430 C  C    . LEU   A 1 472 ? 389.024 -6.297  83.701  1.00 27.24  ? 451  LEU   A C    1 
ATOM   3431 O  O    . LEU   A 1 472 ? 388.625 -5.199  84.111  1.00 25.41  ? 451  LEU   A O    1 
ATOM   3432 C  CB   . LEU   A 1 472 ? 390.861 -7.489  84.929  1.00 25.11  ? 451  LEU   A CB   1 
ATOM   3433 C  CG   . LEU   A 1 472 ? 391.356 -8.417  86.044  1.00 33.01  ? 451  LEU   A CG   1 
ATOM   3434 C  CD1  . LEU   A 1 472 ? 392.878 -8.512  86.046  1.00 32.29  ? 451  LEU   A CD1  1 
ATOM   3435 C  CD2  . LEU   A 1 472 ? 390.850 -7.960  87.406  1.00 26.90  ? 451  LEU   A CD2  1 
ATOM   3436 N  N    . LYS   A 1 473 ? 389.179 -6.561  82.403  1.00 26.85  ? 452  LYS   A N    1 
ATOM   3437 C  CA   . LYS   A 1 473 ? 388.808 -5.567  81.404  1.00 29.42  ? 452  LYS   A CA   1 
ATOM   3438 C  C    . LYS   A 1 473 ? 387.314 -5.282  81.442  1.00 29.38  ? 452  LYS   A C    1 
ATOM   3439 O  O    . LYS   A 1 473 ? 386.887 -4.137  81.250  1.00 30.97  ? 452  LYS   A O    1 
ATOM   3440 C  CB   . LYS   A 1 473 ? 389.230 -6.036  80.010  1.00 26.87  ? 452  LYS   A CB   1 
ATOM   3441 C  CG   . LYS   A 1 473 ? 388.675 -5.171  78.892  1.00 43.98  ? 452  LYS   A CG   1 
ATOM   3442 C  CD   . LYS   A 1 473 ? 389.421 -5.359  77.579  1.00 59.45  ? 452  LYS   A CD   1 
ATOM   3443 C  CE   . LYS   A 1 473 ? 388.877 -6.520  76.761  1.00 58.08  ? 452  LYS   A CE   1 
ATOM   3444 N  NZ   . LYS   A 1 473 ? 389.535 -6.575  75.424  1.00 70.22  ? 452  LYS   A NZ   1 
ATOM   3445 N  N    . ALA   A 1 474 ? 386.500 -6.310  81.694  1.00 26.46  ? 453  ALA   A N    1 
ATOM   3446 C  CA   . ALA   A 1 474 ? 385.054 -6.127  81.703  1.00 25.09  ? 453  ALA   A CA   1 
ATOM   3447 C  C    . ALA   A 1 474 ? 384.589 -5.220  82.833  1.00 25.61  ? 453  ALA   A C    1 
ATOM   3448 O  O    . ALA   A 1 474 ? 383.492 -4.658  82.744  1.00 29.57  ? 453  ALA   A O    1 
ATOM   3449 C  CB   . ALA   A 1 474 ? 384.344 -7.478  81.800  1.00 27.23  ? 453  ALA   A CB   1 
ATOM   3450 N  N    . GLN   A 1 475 ? 385.384 -5.070  83.895  1.00 25.77  ? 454  GLN   A N    1 
ATOM   3451 C  CA   . GLN   A 1 475 ? 385.023 -4.116  84.937  1.00 28.36  ? 454  GLN   A CA   1 
ATOM   3452 C  C    . GLN   A 1 475 ? 385.190 -2.680  84.462  1.00 28.17  ? 454  GLN   A C    1 
ATOM   3453 O  O    . GLN   A 1 475 ? 384.606 -1.769  85.058  1.00 30.27  ? 454  GLN   A O    1 
ATOM   3454 C  CB   . GLN   A 1 475 ? 385.857 -4.347  86.199  1.00 24.94  ? 454  GLN   A CB   1 
ATOM   3455 C  CG   . GLN   A 1 475 ? 385.895 -5.783  86.689  1.00 24.01  ? 454  GLN   A CG   1 
ATOM   3456 C  CD   . GLN   A 1 475 ? 384.520 -6.417  86.775  1.00 23.86  ? 454  GLN   A CD   1 
ATOM   3457 O  OE1  . GLN   A 1 475 ? 383.696 -6.038  87.609  1.00 27.89  ? 454  GLN   A OE1  1 
ATOM   3458 N  NE2  . GLN   A 1 475 ? 384.265 -7.391  85.913  1.00 29.27  ? 454  GLN   A NE2  1 
ATOM   3459 N  N    . GLN   A 1 476 ? 385.999 -2.467  83.422  1.00 27.94  ? 455  GLN   A N    1 
ATOM   3460 C  CA   . GLN   A 1 476 ? 386.073 -1.204  82.695  1.00 30.98  ? 455  GLN   A CA   1 
ATOM   3461 C  C    . GLN   A 1 476 ? 386.778 -0.088  83.454  1.00 29.84  ? 455  GLN   A C    1 
ATOM   3462 O  O    . GLN   A 1 476 ? 387.616 0.618   82.884  1.00 34.27  ? 455  GLN   A O    1 
ATOM   3463 C  CB   . GLN   A 1 476 ? 384.669 -0.738  82.308  1.00 33.70  ? 455  GLN   A CB   1 
ATOM   3464 C  CG   . GLN   A 1 476 ? 384.064 -1.515  81.164  1.00 36.05  ? 455  GLN   A CG   1 
ATOM   3465 C  CD   . GLN   A 1 476 ? 382.854 -0.821  80.584  1.00 38.81  ? 455  GLN   A CD   1 
ATOM   3466 O  OE1  . GLN   A 1 476 ? 382.979 0.068   79.742  1.00 42.12  ? 455  GLN   A OE1  1 
ATOM   3467 N  NE2  . GLN   A 1 476 ? 381.671 -1.216  81.038  1.00 42.04  ? 455  GLN   A NE2  1 
ATOM   3468 N  N    . VAL   A 1 477 ? 386.445 0.088   84.734  1.00 25.54  ? 456  VAL   A N    1 
ATOM   3469 C  CA   . VAL   A 1 477 ? 386.797 1.332   85.416  1.00 22.73  ? 456  VAL   A CA   1 
ATOM   3470 C  C    . VAL   A 1 477 ? 388.269 1.438   85.782  1.00 22.27  ? 456  VAL   A C    1 
ATOM   3471 O  O    . VAL   A 1 477 ? 388.723 2.532   86.137  1.00 27.59  ? 456  VAL   A O    1 
ATOM   3472 C  CB   . VAL   A 1 477 ? 385.901 1.520   86.655  1.00 26.51  ? 456  VAL   A CB   1 
ATOM   3473 C  CG1  . VAL   A 1 477 ? 384.461 1.795   86.220  1.00 25.89  ? 456  VAL   A CG1  1 
ATOM   3474 C  CG2  . VAL   A 1 477 ? 385.962 0.300   87.554  1.00 24.21  ? 456  VAL   A CG2  1 
ATOM   3475 N  N    . GLN   A 1 478 ? 389.041 0.359   85.686  1.00 25.34  ? 457  GLN   A N    1 
ATOM   3476 C  CA   . GLN   A 1 478 ? 390.477 0.436   85.947  1.00 27.45  ? 457  GLN   A CA   1 
ATOM   3477 C  C    . GLN   A 1 478 ? 391.287 -0.089  84.769  1.00 24.35  ? 457  GLN   A C    1 
ATOM   3478 O  O    . GLN   A 1 478 ? 392.299 -0.774  84.945  1.00 27.09  ? 457  GLN   A O    1 
ATOM   3479 C  CB   . GLN   A 1 478 ? 390.836 -0.300  87.235  1.00 23.99  ? 457  GLN   A CB   1 
ATOM   3480 C  CG   . GLN   A 1 478 ? 390.372 0.447   88.468  1.00 25.70  ? 457  GLN   A CG   1 
ATOM   3481 C  CD   . GLN   A 1 478 ? 390.436 -0.394  89.718  1.00 23.79  ? 457  GLN   A CD   1 
ATOM   3482 O  OE1  . GLN   A 1 478 ? 390.050 -1.561  89.713  1.00 27.43  ? 457  GLN   A OE1  1 
ATOM   3483 N  NE2  . GLN   A 1 478 ? 390.925 0.195   90.803  1.00 22.75  ? 457  GLN   A NE2  1 
ATOM   3484 N  N    . ALA   A 1 479 ? 390.850 0.248   83.547  1.00 31.85  ? 458  ALA   A N    1 
ATOM   3485 C  CA   . ALA   A 1 479 ? 391.493 -0.011  82.258  1.00 33.97  ? 458  ALA   A CA   1 
ATOM   3486 C  C    . ALA   A 1 479 ? 392.842 -0.717  82.378  1.00 31.37  ? 458  ALA   A C    1 
ATOM   3487 O  O    . ALA   A 1 479 ? 393.888 -0.058  82.432  1.00 32.38  ? 458  ALA   A O    1 
ATOM   3488 C  CB   . ALA   A 1 479 ? 391.665 1.307   81.500  1.00 30.79  ? 458  ALA   A CB   1 
ATOM   3489 N  N    . PRO   A 1 480 ? 392.856 -2.049  82.397  1.00 26.81  ? 459  PRO   A N    1 
ATOM   3490 C  CA   . PRO   A 1 480 ? 394.096 -2.776  82.701  1.00 26.80  ? 459  PRO   A CA   1 
ATOM   3491 C  C    . PRO   A 1 480 ? 395.189 -2.591  81.657  1.00 33.07  ? 459  PRO   A C    1 
ATOM   3492 O  O    . PRO   A 1 480 ? 394.931 -2.377  80.470  1.00 28.02  ? 459  PRO   A O    1 
ATOM   3493 C  CB   . PRO   A 1 480 ? 393.637 -4.238  82.764  1.00 24.65  ? 459  PRO   A CB   1 
ATOM   3494 C  CG   . PRO   A 1 480 ? 392.173 -4.159  83.104  1.00 27.60  ? 459  PRO   A CG   1 
ATOM   3495 C  CD   . PRO   A 1 480 ? 391.674 -2.928  82.407  1.00 27.35  ? 459  PRO   A CD   1 
ATOM   3496 N  N    . VAL   A 1 481 ? 396.430 -2.692  82.134  1.00 28.41  ? 460  VAL   A N    1 
ATOM   3497 C  CA   . VAL   A 1 481 ? 397.641 -2.596  81.325  1.00 29.79  ? 460  VAL   A CA   1 
ATOM   3498 C  C    . VAL   A 1 481 ? 398.459 -3.859  81.554  1.00 28.93  ? 460  VAL   A C    1 
ATOM   3499 O  O    . VAL   A 1 481 ? 398.650 -4.276  82.702  1.00 28.86  ? 460  VAL   A O    1 
ATOM   3500 C  CB   . VAL   A 1 481 ? 398.474 -1.352  81.690  1.00 28.93  ? 460  VAL   A CB   1 
ATOM   3501 C  CG1  . VAL   A 1 481 ? 399.764 -1.304  80.878  1.00 29.71  ? 460  VAL   A CG1  1 
ATOM   3502 C  CG2  . VAL   A 1 481 ? 397.662 -0.082  81.503  1.00 29.60  ? 460  VAL   A CG2  1 
ATOM   3503 N  N    . GLU   A 1 482 ? 398.944 -4.462  80.470  1.00 30.36  ? 461  GLU   A N    1 
ATOM   3504 C  CA   . GLU   A 1 482 ? 399.804 -5.636  80.563  1.00 27.96  ? 461  GLU   A CA   1 
ATOM   3505 C  C    . GLU   A 1 482 ? 401.266 -5.222  80.638  1.00 27.91  ? 461  GLU   A C    1 
ATOM   3506 O  O    . GLU   A 1 482 ? 401.744 -4.430  79.821  1.00 25.24  ? 461  GLU   A O    1 
ATOM   3507 C  CB   . GLU   A 1 482 ? 399.593 -6.571  79.374  1.00 29.26  ? 461  GLU   A CB   1 
ATOM   3508 C  CG   . GLU   A 1 482 ? 398.459 -7.554  79.574  1.00 35.75  ? 461  GLU   A CG   1 
ATOM   3509 C  CD   . GLU   A 1 482 ? 398.349 -8.546  78.442  1.00 41.83  ? 461  GLU   A CD   1 
ATOM   3510 O  OE1  . GLU   A 1 482 ? 398.106 -8.115  77.294  1.00 52.25  ? 461  GLU   A OE1  1 
ATOM   3511 O  OE2  . GLU   A 1 482 ? 398.518 -9.757  78.699  1.00 45.67  ? 461  GLU   A OE2  1 
ATOM   3512 N  N    . LEU   A 1 483 ? 401.968 -5.769  81.611  1.00 25.52  ? 462  LEU   A N    1 
ATOM   3513 C  CA   . LEU   A 1 483 ? 403.388 -5.546  81.803  1.00 27.22  ? 462  LEU   A CA   1 
ATOM   3514 C  C    . LEU   A 1 483 ? 404.144 -6.797  81.375  1.00 25.00  ? 462  LEU   A C    1 
ATOM   3515 O  O    . LEU   A 1 483 ? 403.556 -7.773  80.900  1.00 26.68  ? 462  LEU   A O    1 
ATOM   3516 C  CB   . LEU   A 1 483 ? 403.674 -5.171  83.258  1.00 23.85  ? 462  LEU   A CB   1 
ATOM   3517 C  CG   . LEU   A 1 483 ? 402.998 -3.885  83.734  1.00 24.04  ? 462  LEU   A CG   1 
ATOM   3518 C  CD1  . LEU   A 1 483 ? 403.343 -3.625  85.187  1.00 26.92  ? 462  LEU   A CD1  1 
ATOM   3519 C  CD2  . LEU   A 1 483 ? 403.422 -2.714  82.867  1.00 25.18  ? 462  LEU   A CD2  1 
ATOM   3520 N  N    . TYR   A 1 484 ? 405.458 -6.763  81.548  1.00 25.87  ? 463  TYR   A N    1 
ATOM   3521 C  CA   . TYR   A 1 484 ? 406.330 -7.872  81.176  1.00 23.08  ? 463  TYR   A CA   1 
ATOM   3522 C  C    . TYR   A 1 484 ? 406.866 -8.495  82.459  1.00 25.97  ? 463  TYR   A C    1 
ATOM   3523 O  O    . TYR   A 1 484 ? 407.800 -7.970  83.072  1.00 24.37  ? 463  TYR   A O    1 
ATOM   3524 C  CB   . TYR   A 1 484 ? 407.453 -7.391  80.264  1.00 24.61  ? 463  TYR   A CB   1 
ATOM   3525 C  CG   . TYR   A 1 484 ? 408.498 -8.435  79.931  1.00 27.72  ? 463  TYR   A CG   1 
ATOM   3526 C  CD1  . TYR   A 1 484 ? 408.136 -9.742  79.632  1.00 30.96  ? 463  TYR   A CD1  1 
ATOM   3527 C  CD2  . TYR   A 1 484 ? 409.845 -8.103  79.888  1.00 29.07  ? 463  TYR   A CD2  1 
ATOM   3528 C  CE1  . TYR   A 1 484 ? 409.090 -10.691 79.316  1.00 32.32  ? 463  TYR   A CE1  1 
ATOM   3529 C  CE2  . TYR   A 1 484 ? 410.807 -9.046  79.572  1.00 32.67  ? 463  TYR   A CE2  1 
ATOM   3530 C  CZ   . TYR   A 1 484 ? 410.422 -10.340 79.286  1.00 37.31  ? 463  TYR   A CZ   1 
ATOM   3531 O  OH   . TYR   A 1 484 ? 411.371 -11.286 78.971  1.00 38.14  ? 463  TYR   A OH   1 
ATOM   3532 N  N    . SER   A 1 485 ? 406.264 -9.609  82.868  1.00 27.24  ? 464  SER   A N    1 
ATOM   3533 C  CA   . SER   A 1 485 ? 406.696 -10.316 84.062  1.00 29.45  ? 464  SER   A CA   1 
ATOM   3534 C  C    . SER   A 1 485 ? 407.209 -11.719 83.781  1.00 30.64  ? 464  SER   A C    1 
ATOM   3535 O  O    . SER   A 1 485 ? 407.631 -12.401 84.722  1.00 34.46  ? 464  SER   A O    1 
ATOM   3536 C  CB   . SER   A 1 485 ? 405.551 -10.402 85.080  1.00 26.57  ? 464  SER   A CB   1 
ATOM   3537 O  OG   . SER   A 1 485 ? 404.555 -11.311 84.639  1.00 26.83  ? 464  SER   A OG   1 
ATOM   3538 N  N    . ASP   A 1 486 ? 407.183 -12.179 82.528  1.00 29.33  ? 465  ASP   A N    1 
ATOM   3539 C  CA   . ASP   A 1 486 ? 407.586 -13.551 82.247  1.00 34.71  ? 465  ASP   A CA   1 
ATOM   3540 C  C    . ASP   A 1 486 ? 409.096 -13.749 82.268  1.00 33.24  ? 465  ASP   A C    1 
ATOM   3541 O  O    . ASP   A 1 486 ? 409.553 -14.884 82.092  1.00 34.93  ? 465  ASP   A O    1 
ATOM   3542 C  CB   . ASP   A 1 486 ? 407.032 -14.022 80.900  1.00 30.36  ? 465  ASP   A CB   1 
ATOM   3543 C  CG   . ASP   A 1 486 ? 406.909 -15.534 80.830  1.00 35.96  ? 465  ASP   A CG   1 
ATOM   3544 O  OD1  . ASP   A 1 486 ? 406.750 -16.157 81.902  1.00 37.22  ? 465  ASP   A OD1  1 
ATOM   3545 O  OD2  . ASP   A 1 486 ? 406.985 -16.104 79.720  1.00 37.57  ? 465  ASP   A OD2  1 
ATOM   3546 N  N    . TRP   A 1 487 ? 409.880 -12.688 82.463  1.00 28.19  ? 466  TRP   A N    1 
ATOM   3547 C  CA   . TRP   A 1 487 ? 411.305 -12.861 82.711  1.00 30.76  ? 466  TRP   A CA   1 
ATOM   3548 C  C    . TRP   A 1 487 ? 411.585 -13.360 84.122  1.00 30.27  ? 466  TRP   A C    1 
ATOM   3549 O  O    . TRP   A 1 487 ? 412.729 -13.721 84.422  1.00 30.01  ? 466  TRP   A O    1 
ATOM   3550 C  CB   . TRP   A 1 487 ? 412.057 -11.548 82.462  1.00 27.43  ? 466  TRP   A CB   1 
ATOM   3551 C  CG   . TRP   A 1 487 ? 411.592 -10.420 83.328  1.00 31.02  ? 466  TRP   A CG   1 
ATOM   3552 C  CD1  . TRP   A 1 487 ? 410.505 -9.626  83.121  1.00 27.23  ? 466  TRP   A CD1  1 
ATOM   3553 C  CD2  . TRP   A 1 487 ? 412.198 -9.963  84.544  1.00 29.22  ? 466  TRP   A CD2  1 
ATOM   3554 N  NE1  . TRP   A 1 487 ? 410.393 -8.701  84.134  1.00 27.87  ? 466  TRP   A NE1  1 
ATOM   3555 C  CE2  . TRP   A 1 487 ? 411.422 -8.888  85.019  1.00 26.38  ? 466  TRP   A CE2  1 
ATOM   3556 C  CE3  . TRP   A 1 487 ? 413.321 -10.359 85.276  1.00 27.83  ? 466  TRP   A CE3  1 
ATOM   3557 C  CZ2  . TRP   A 1 487 ? 411.732 -8.204  86.193  1.00 29.84  ? 466  TRP   A CZ2  1 
ATOM   3558 C  CZ3  . TRP   A 1 487 ? 413.628 -9.678  86.442  1.00 27.27  ? 466  TRP   A CZ3  1 
ATOM   3559 C  CH2  . TRP   A 1 487 ? 412.836 -8.613  86.888  1.00 29.09  ? 466  TRP   A CH2  1 
ATOM   3560 N  N    . LEU   A 1 488 ? 410.572 -13.394 84.983  1.00 30.55  ? 467  LEU   A N    1 
ATOM   3561 C  CA   . LEU   A 1 488 ? 410.702 -13.864 86.353  1.00 30.49  ? 467  LEU   A CA   1 
ATOM   3562 C  C    . LEU   A 1 488 ? 410.214 -15.302 86.455  1.00 31.03  ? 467  LEU   A C    1 
ATOM   3563 O  O    . LEU   A 1 488 ? 409.217 -15.674 85.829  1.00 32.13  ? 467  LEU   A O    1 
ATOM   3564 C  CB   . LEU   A 1 488 ? 409.903 -12.971 87.304  1.00 28.83  ? 467  LEU   A CB   1 
ATOM   3565 C  CG   . LEU   A 1 488 ? 410.444 -11.555 87.512  1.00 30.96  ? 467  LEU   A CG   1 
ATOM   3566 C  CD1  . LEU   A 1 488 ? 409.316 -10.608 87.880  1.00 29.91  ? 467  LEU   A CD1  1 
ATOM   3567 C  CD2  . LEU   A 1 488 ? 411.516 -11.560 88.589  1.00 27.70  ? 467  LEU   A CD2  1 
ATOM   3568 N  N    . THR   A 1 489 ? 410.922 -16.110 87.249  1.00 31.84  ? 468  THR   A N    1 
ATOM   3569 C  CA   . THR   A 1 489 ? 410.535 -17.510 87.402  1.00 38.04  ? 468  THR   A CA   1 
ATOM   3570 C  C    . THR   A 1 489 ? 409.086 -17.627 87.861  1.00 35.72  ? 468  THR   A C    1 
ATOM   3571 O  O    . THR   A 1 489 ? 408.285 -18.343 87.252  1.00 34.43  ? 468  THR   A O    1 
ATOM   3572 C  CB   . THR   A 1 489 ? 411.472 -18.220 88.381  1.00 38.32  ? 468  THR   A CB   1 
ATOM   3573 O  OG1  . THR   A 1 489 ? 412.824 -18.107 87.922  1.00 37.07  ? 468  THR   A OG1  1 
ATOM   3574 C  CG2  . THR   A 1 489 ? 411.113 -19.693 88.495  1.00 34.30  ? 468  THR   A CG2  1 
ATOM   3575 N  N    . VAL   A 1 490 ? 408.728 -16.917 88.933  1.00 34.64  ? 469  VAL   A N    1 
ATOM   3576 C  CA   . VAL   A 1 490 ? 407.349 -16.949 89.411  1.00 32.35  ? 469  VAL   A CA   1 
ATOM   3577 C  C    . VAL   A 1 490 ? 406.440 -16.169 88.469  1.00 36.18  ? 469  VAL   A C    1 
ATOM   3578 O  O    . VAL   A 1 490 ? 405.325 -16.604 88.159  1.00 38.97  ? 469  VAL   A O    1 
ATOM   3579 C  CB   . VAL   A 1 490 ? 407.271 -16.415 90.852  1.00 31.40  ? 469  VAL   A CB   1 
ATOM   3580 C  CG1  . VAL   A 1 490 ? 405.825 -16.233 91.265  1.00 34.96  ? 469  VAL   A CG1  1 
ATOM   3581 C  CG2  . VAL   A 1 490 ? 407.983 -17.365 91.801  1.00 33.09  ? 469  VAL   A CG2  1 
ATOM   3582 N  N    . GLY   A 1 491 ? 406.896 -15.008 88.007  1.00 32.39  ? 470  GLY   A N    1 
ATOM   3583 C  CA   . GLY   A 1 491 ? 406.192 -14.259 86.983  1.00 26.46  ? 470  GLY   A CA   1 
ATOM   3584 C  C    . GLY   A 1 491 ? 405.182 -13.251 87.499  1.00 30.13  ? 470  GLY   A C    1 
ATOM   3585 O  O    . GLY   A 1 491 ? 404.136 -13.046 86.877  1.00 31.66  ? 470  GLY   A O    1 
ATOM   3586 N  N    . HIS   A 1 492 ? 405.485 -12.598 88.618  1.00 27.39  ? 471  HIS   A N    1 
ATOM   3587 C  CA   . HIS   A 1 492 ? 404.559 -11.674 89.260  1.00 26.90  ? 471  HIS   A CA   1 
ATOM   3588 C  C    . HIS   A 1 492 ? 405.108 -10.254 89.218  1.00 27.37  ? 471  HIS   A C    1 
ATOM   3589 O  O    . HIS   A 1 492 ? 406.299 -10.033 89.456  1.00 30.59  ? 471  HIS   A O    1 
ATOM   3590 C  CB   . HIS   A 1 492 ? 404.295 -12.079 90.712  1.00 29.78  ? 471  HIS   A CB   1 
ATOM   3591 C  CG   . HIS   A 1 492 ? 403.667 -13.429 90.859  1.00 34.51  ? 471  HIS   A CG   1 
ATOM   3592 N  ND1  . HIS   A 1 492 ? 403.435 -14.012 92.087  1.00 32.05  ? 471  HIS   A ND1  1 
ATOM   3593 C  CD2  . HIS   A 1 492 ? 403.220 -14.312 89.934  1.00 34.11  ? 471  HIS   A CD2  1 
ATOM   3594 C  CE1  . HIS   A 1 492 ? 402.873 -15.194 91.912  1.00 30.55  ? 471  HIS   A CE1  1 
ATOM   3595 N  NE2  . HIS   A 1 492 ? 402.732 -15.401 90.615  1.00 33.92  ? 471  HIS   A NE2  1 
ATOM   3596 N  N    . VAL   A 1 493 ? 404.234 -9.288  88.923  1.00 27.10  ? 472  VAL   A N    1 
ATOM   3597 C  CA   . VAL   A 1 493 ? 404.688 -7.902  88.876  1.00 25.21  ? 472  VAL   A CA   1 
ATOM   3598 C  C    . VAL   A 1 493 ? 405.086 -7.419  90.262  1.00 28.50  ? 472  VAL   A C    1 
ATOM   3599 O  O    . VAL   A 1 493 ? 405.926 -6.522  90.395  1.00 29.50  ? 472  VAL   A O    1 
ATOM   3600 C  CB   . VAL   A 1 493 ? 403.614 -6.990  88.254  1.00 25.97  ? 472  VAL   A CB   1 
ATOM   3601 C  CG1  . VAL   A 1 493 ? 403.414 -7.323  86.780  1.00 23.91  ? 472  VAL   A CG1  1 
ATOM   3602 C  CG2  . VAL   A 1 493 ? 402.304 -7.091  89.024  1.00 24.40  ? 472  VAL   A CG2  1 
ATOM   3603 N  N    . ASP   A 1 494 ? 404.509 -7.997  91.314  1.00 29.39  ? 473  ASP   A N    1 
ATOM   3604 C  CA   . ASP   A 1 494 ? 404.877 -7.542  92.648  1.00 32.55  ? 473  ASP   A CA   1 
ATOM   3605 C  C    . ASP   A 1 494 ? 406.289 -7.962  93.040  1.00 29.51  ? 473  ASP   A C    1 
ATOM   3606 O  O    . ASP   A 1 494 ? 406.737 -7.615  94.138  1.00 36.00  ? 473  ASP   A O    1 
ATOM   3607 C  CB   . ASP   A 1 494 ? 403.848 -8.025  93.680  1.00 33.14  ? 473  ASP   A CB   1 
ATOM   3608 C  CG   . ASP   A 1 494 ? 403.972 -9.505  94.013  1.00 40.87  ? 473  ASP   A CG   1 
ATOM   3609 O  OD1  . ASP   A 1 494 ? 404.802 -10.208 93.402  1.00 42.71  ? 473  ASP   A OD1  1 
ATOM   3610 O  OD2  . ASP   A 1 494 ? 403.228 -9.967  94.906  1.00 47.49  ? 473  ASP   A OD2  1 
ATOM   3611 N  N    . GLU   A 1 495 ? 407.001 -8.683  92.171  1.00 31.28  ? 474  GLU   A N    1 
ATOM   3612 C  CA   . GLU   A 1 495 ? 408.409 -8.986  92.394  1.00 37.55  ? 474  GLU   A CA   1 
ATOM   3613 C  C    . GLU   A 1 495 ? 409.330 -7.833  92.019  1.00 31.06  ? 474  GLU   A C    1 
ATOM   3614 O  O    . GLU   A 1 495 ? 410.504 -7.855  92.404  1.00 36.92  ? 474  GLU   A O    1 
ATOM   3615 C  CB   . GLU   A 1 495 ? 408.823 -10.232 91.601  1.00 31.05  ? 474  GLU   A CB   1 
ATOM   3616 C  CG   . GLU   A 1 495 ? 408.015 -11.482 91.924  1.00 35.68  ? 474  GLU   A CG   1 
ATOM   3617 C  CD   . GLU   A 1 495 ? 408.557 -12.729 91.244  1.00 38.91  ? 474  GLU   A CD   1 
ATOM   3618 O  OE1  . GLU   A 1 495 ? 409.695 -13.141 91.559  1.00 41.22  ? 474  GLU   A OE1  1 
ATOM   3619 O  OE2  . GLU   A 1 495 ? 407.844 -13.300 90.392  1.00 36.96  ? 474  GLU   A OE2  1 
ATOM   3620 N  N    . PHE   A 1 496 ? 408.842 -6.832  91.284  1.00 29.18  ? 475  PHE   A N    1 
ATOM   3621 C  CA   . PHE   A 1 496 ? 409.728 -5.776  90.819  1.00 29.50  ? 475  PHE   A CA   1 
ATOM   3622 C  C    . PHE   A 1 496 ? 409.137 -4.375  90.874  1.00 30.03  ? 475  PHE   A C    1 
ATOM   3623 O  O    . PHE   A 1 496 ? 409.830 -3.426  90.495  1.00 29.56  ? 475  PHE   A O    1 
ATOM   3624 C  CB   . PHE   A 1 496 ? 410.205 -6.069  89.379  1.00 26.01  ? 475  PHE   A CB   1 
ATOM   3625 C  CG   . PHE   A 1 496 ? 409.112 -6.028  88.334  1.00 27.35  ? 475  PHE   A CG   1 
ATOM   3626 C  CD1  . PHE   A 1 496 ? 408.664 -4.819  87.819  1.00 26.94  ? 475  PHE   A CD1  1 
ATOM   3627 C  CD2  . PHE   A 1 496 ? 408.566 -7.202  87.834  1.00 28.77  ? 475  PHE   A CD2  1 
ATOM   3628 C  CE1  . PHE   A 1 496 ? 407.675 -4.780  86.851  1.00 28.52  ? 475  PHE   A CE1  1 
ATOM   3629 C  CE2  . PHE   A 1 496 ? 407.577 -7.169  86.863  1.00 26.86  ? 475  PHE   A CE2  1 
ATOM   3630 C  CZ   . PHE   A 1 496 ? 407.131 -5.956  86.371  1.00 24.09  ? 475  PHE   A CZ   1 
ATOM   3631 N  N    . MET   A 1 497 ? 407.902 -4.198  91.335  1.00 28.02  ? 476  MET   A N    1 
ATOM   3632 C  CA   . MET   A 1 497 ? 407.325 -2.864  91.329  1.00 27.88  ? 476  MET   A CA   1 
ATOM   3633 C  C    . MET   A 1 497 ? 406.312 -2.724  92.451  1.00 27.65  ? 476  MET   A C    1 
ATOM   3634 O  O    . MET   A 1 497 ? 405.754 -3.705  92.946  1.00 26.36  ? 476  MET   A O    1 
ATOM   3635 C  CB   . MET   A 1 497 ? 406.663 -2.550  89.989  1.00 30.57  ? 476  MET   A CB   1 
ATOM   3636 C  CG   . MET   A 1 497 ? 405.498 -3.454  89.669  1.00 32.61  ? 476  MET   A CG   1 
ATOM   3637 S  SD   . MET   A 1 497 ? 404.434 -2.700  88.437  1.00 38.30  ? 476  MET   A SD   1 
ATOM   3638 C  CE   . MET   A 1 497 ? 403.874 -1.264  89.348  1.00 29.58  ? 476  MET   A CE   1 
ATOM   3639 N  N    . SER   A 1 498 ? 406.078 -1.476  92.835  1.00 27.15  ? 477  SER   A N    1 
ATOM   3640 C  CA   . SER   A 1 498 ? 405.099 -1.138  93.856  1.00 28.97  ? 477  SER   A CA   1 
ATOM   3641 C  C    . SER   A 1 498 ? 404.909 0.369   93.817  1.00 31.06  ? 477  SER   A C    1 
ATOM   3642 O  O    . SER   A 1 498 ? 405.686 1.095   93.191  1.00 32.00  ? 477  SER   A O    1 
ATOM   3643 C  CB   . SER   A 1 498 ? 405.540 -1.601  95.245  1.00 32.49  ? 477  SER   A CB   1 
ATOM   3644 O  OG   . SER   A 1 498 ? 404.499 -1.406  96.186  1.00 45.49  ? 477  SER   A OG   1 
ATOM   3645 N  N    . PHE   A 1 499 ? 403.861 0.831   94.491  1.00 30.32  ? 478  PHE   A N    1 
ATOM   3646 C  CA   . PHE   A 1 499 ? 403.590 2.252   94.639  1.00 33.79  ? 478  PHE   A CA   1 
ATOM   3647 C  C    . PHE   A 1 499 ? 403.509 2.602   96.114  1.00 31.71  ? 478  PHE   A C    1 
ATOM   3648 O  O    . PHE   A 1 499 ? 402.947 1.845   96.912  1.00 32.86  ? 478  PHE   A O    1 
ATOM   3649 C  CB   . PHE   A 1 499 ? 402.284 2.658   93.955  1.00 30.01  ? 478  PHE   A CB   1 
ATOM   3650 C  CG   . PHE   A 1 499 ? 402.241 2.335   92.500  1.00 27.22  ? 478  PHE   A CG   1 
ATOM   3651 C  CD1  . PHE   A 1 499 ? 402.731 3.229   91.564  1.00 29.26  ? 478  PHE   A CD1  1 
ATOM   3652 C  CD2  . PHE   A 1 499 ? 401.705 1.139   92.064  1.00 26.78  ? 478  PHE   A CD2  1 
ATOM   3653 C  CE1  . PHE   A 1 499 ? 402.689 2.934   90.222  1.00 26.39  ? 478  PHE   A CE1  1 
ATOM   3654 C  CE2  . PHE   A 1 499 ? 401.660 0.838   90.723  1.00 30.09  ? 478  PHE   A CE2  1 
ATOM   3655 C  CZ   . PHE   A 1 499 ? 402.153 1.735   89.799  1.00 26.61  ? 478  PHE   A CZ   1 
ATOM   3656 N  N    . VAL   A 1 500 ? 404.071 3.753   96.465  1.00 35.27  ? 479  VAL   A N    1 
ATOM   3657 C  CA   . VAL   A 1 500 ? 403.924 4.312   97.804  1.00 38.19  ? 479  VAL   A CA   1 
ATOM   3658 C  C    . VAL   A 1 500 ? 403.414 5.738   97.652  1.00 36.55  ? 479  VAL   A C    1 
ATOM   3659 O  O    . VAL   A 1 500 ? 403.719 6.400   96.648  1.00 36.03  ? 479  VAL   A O    1 
ATOM   3660 C  CB   . VAL   A 1 500 ? 405.243 4.263   98.594  1.00 34.30  ? 479  VAL   A CB   1 
ATOM   3661 C  CG1  . VAL   A 1 500 ? 405.714 2.826   98.762  1.00 31.62  ? 479  VAL   A CG1  1 
ATOM   3662 C  CG2  . VAL   A 1 500 ? 406.316 5.114   97.918  1.00 29.04  ? 479  VAL   A CG2  1 
ATOM   3663 N  N    . PRO   A 1 501 ? 402.617 6.240   98.587  1.00 38.29  ? 480  PRO   A N    1 
ATOM   3664 C  CA   . PRO   A 1 501 ? 402.268 7.660   98.571  1.00 42.93  ? 480  PRO   A CA   1 
ATOM   3665 C  C    . PRO   A 1 501 ? 403.420 8.496   99.105  1.00 40.36  ? 480  PRO   A C    1 
ATOM   3666 O  O    . PRO   A 1 501 ? 404.274 8.024   99.856  1.00 41.99  ? 480  PRO   A O    1 
ATOM   3667 C  CB   . PRO   A 1 501 ? 401.054 7.734   99.503  1.00 41.38  ? 480  PRO   A CB   1 
ATOM   3668 C  CG   . PRO   A 1 501 ? 401.291 6.620   100.481 1.00 44.65  ? 480  PRO   A CG   1 
ATOM   3669 C  CD   . PRO   A 1 501 ? 401.956 5.518   99.690  1.00 39.54  ? 480  PRO   A CD   1 
ATOM   3670 N  N    . ILE   A 1 502 ? 403.442 9.758   98.689  1.00 39.92  ? 481  ILE   A N    1 
ATOM   3671 C  CA   . ILE   A 1 502 ? 404.367 10.744  99.239  1.00 43.33  ? 481  ILE   A CA   1 
ATOM   3672 C  C    . ILE   A 1 502 ? 403.656 11.436  100.399 1.00 46.81  ? 481  ILE   A C    1 
ATOM   3673 O  O    . ILE   A 1 502 ? 402.692 12.184  100.159 1.00 46.76  ? 481  ILE   A O    1 
ATOM   3674 C  CB   . ILE   A 1 502 ? 404.825 11.753  98.182  1.00 44.49  ? 481  ILE   A CB   1 
ATOM   3675 C  CG1  . ILE   A 1 502 ? 405.672 11.051  97.119  1.00 41.38  ? 481  ILE   A CG1  1 
ATOM   3676 C  CG2  . ILE   A 1 502 ? 405.627 12.865  98.835  1.00 43.50  ? 481  ILE   A CG2  1 
ATOM   3677 C  CD1  . ILE   A 1 502 ? 406.171 11.975  96.036  1.00 44.07  ? 481  ILE   A CD1  1 
ATOM   3678 N  N    . PRO   A 1 503 ? 404.067 11.202  101.643 1.00 47.64  ? 482  PRO   A N    1 
ATOM   3679 C  CA   . PRO   A 1 503 ? 403.339 11.771  102.782 1.00 45.77  ? 482  PRO   A CA   1 
ATOM   3680 C  C    . PRO   A 1 503 ? 403.127 13.269  102.623 1.00 53.23  ? 482  PRO   A C    1 
ATOM   3681 O  O    . PRO   A 1 503 ? 403.990 13.990  102.118 1.00 56.50  ? 482  PRO   A O    1 
ATOM   3682 C  CB   . PRO   A 1 503 ? 404.247 11.449  103.972 1.00 47.62  ? 482  PRO   A CB   1 
ATOM   3683 C  CG   . PRO   A 1 503 ? 404.980 10.214  103.550 1.00 44.47  ? 482  PRO   A CG   1 
ATOM   3684 C  CD   . PRO   A 1 503 ? 405.192 10.350  102.067 1.00 40.07  ? 482  PRO   A CD   1 
ATOM   3685 N  N    . GLY   A 1 504 ? 401.956 13.733  103.051 1.00 54.38  ? 483  GLY   A N    1 
ATOM   3686 C  CA   . GLY   A 1 504 ? 401.666 15.152  103.020 1.00 49.38  ? 483  GLY   A CA   1 
ATOM   3687 C  C    . GLY   A 1 504 ? 401.416 15.725  101.647 1.00 54.96  ? 483  GLY   A C    1 
ATOM   3688 O  O    . GLY   A 1 504 ? 401.473 16.946  101.477 1.00 59.35  ? 483  GLY   A O    1 
ATOM   3689 N  N    . THR   A 1 505 ? 401.142 14.881  100.654 1.00 53.82  ? 484  THR   A N    1 
ATOM   3690 C  CA   . THR   A 1 505 ? 400.871 15.337  99.299  1.00 54.47  ? 484  THR   A CA   1 
ATOM   3691 C  C    . THR   A 1 505 ? 399.780 14.469  98.688  1.00 54.10  ? 484  THR   A C    1 
ATOM   3692 O  O    . THR   A 1 505 ? 399.345 13.474  99.273  1.00 52.67  ? 484  THR   A O    1 
ATOM   3693 C  CB   . THR   A 1 505 ? 402.129 15.292  98.421  1.00 52.82  ? 484  THR   A CB   1 
ATOM   3694 O  OG1  . THR   A 1 505 ? 402.386 13.939  98.023  1.00 48.86  ? 484  THR   A OG1  1 
ATOM   3695 C  CG2  . THR   A 1 505 ? 403.334 15.825  99.180  1.00 52.41  ? 484  THR   A CG2  1 
ATOM   3696 N  N    . LYS   A 1 506 ? 399.335 14.864  97.495  1.00 55.27  ? 485  LYS   A N    1 
ATOM   3697 C  CA   . LYS   A 1 506 ? 398.470 14.033  96.668  1.00 49.39  ? 485  LYS   A CA   1 
ATOM   3698 C  C    . LYS   A 1 506 ? 399.257 13.230  95.641  1.00 51.48  ? 485  LYS   A C    1 
ATOM   3699 O  O    . LYS   A 1 506 ? 398.655 12.613  94.756  1.00 52.00  ? 485  LYS   A O    1 
ATOM   3700 C  CB   . LYS   A 1 506 ? 397.420 14.887  95.954  1.00 57.96  ? 485  LYS   A CB   1 
ATOM   3701 C  CG   . LYS   A 1 506 ? 396.830 16.008  96.787  1.00 71.99  ? 485  LYS   A CG   1 
ATOM   3702 C  CD   . LYS   A 1 506 ? 397.346 17.359  96.320  1.00 75.22  ? 485  LYS   A CD   1 
ATOM   3703 C  CE   . LYS   A 1 506 ? 396.614 18.501  97.007  1.00 77.29  ? 485  LYS   A CE   1 
ATOM   3704 N  NZ   . LYS   A 1 506 ? 397.128 19.828  96.573  1.00 79.05  ? 485  LYS   A NZ   1 
ATOM   3705 N  N    . LYS   A 1 507 ? 400.582 13.233  95.732  1.00 46.84  ? 486  LYS   A N    1 
ATOM   3706 C  CA   . LYS   A 1 507 ? 401.443 12.538  94.788  1.00 42.17  ? 486  LYS   A CA   1 
ATOM   3707 C  C    . LYS   A 1 507 ? 401.857 11.177  95.333  1.00 40.93  ? 486  LYS   A C    1 
ATOM   3708 O  O    . LYS   A 1 507 ? 401.730 10.887  96.525  1.00 43.20  ? 486  LYS   A O    1 
ATOM   3709 C  CB   . LYS   A 1 507 ? 402.692 13.367  94.474  1.00 47.03  ? 486  LYS   A CB   1 
ATOM   3710 C  CG   . LYS   A 1 507 ? 402.402 14.770  93.980  1.00 50.21  ? 486  LYS   A CG   1 
ATOM   3711 C  CD   . LYS   A 1 507 ? 403.686 15.549  93.751  1.00 62.56  ? 486  LYS   A CD   1 
ATOM   3712 C  CE   . LYS   A 1 507 ? 403.394 16.978  93.318  1.00 88.96  ? 486  LYS   A CE   1 
ATOM   3713 N  NZ   . LYS   A 1 507 ? 404.640 17.769  93.117  1.00 94.54  ? 486  LYS   A NZ   1 
ATOM   3714 N  N    . PHE   A 1 508 ? 402.368 10.344  94.432  1.00 42.33  ? 487  PHE   A N    1 
ATOM   3715 C  CA   . PHE   A 1 508 ? 402.832 9.011   94.776  1.00 36.52  ? 487  PHE   A CA   1 
ATOM   3716 C  C    . PHE   A 1 508 ? 404.154 8.756   94.071  1.00 35.61  ? 487  PHE   A C    1 
ATOM   3717 O  O    . PHE   A 1 508 ? 404.596 9.538   93.225  1.00 36.47  ? 487  PHE   A O    1 
ATOM   3718 C  CB   . PHE   A 1 508 ? 401.800 7.943   94.394  1.00 34.52  ? 487  PHE   A CB   1 
ATOM   3719 C  CG   . PHE   A 1 508 ? 401.561 7.834   92.913  1.00 30.76  ? 487  PHE   A CG   1 
ATOM   3720 C  CD1  . PHE   A 1 508 ? 402.341 6.997   92.132  1.00 34.75  ? 487  PHE   A CD1  1 
ATOM   3721 C  CD2  . PHE   A 1 508 ? 400.555 8.565   92.303  1.00 30.61  ? 487  PHE   A CD2  1 
ATOM   3722 C  CE1  . PHE   A 1 508 ? 402.127 6.891   90.771  1.00 32.72  ? 487  PHE   A CE1  1 
ATOM   3723 C  CE2  . PHE   A 1 508 ? 400.333 8.463   90.941  1.00 33.06  ? 487  PHE   A CE2  1 
ATOM   3724 C  CZ   . PHE   A 1 508 ? 401.121 7.624   90.175  1.00 35.61  ? 487  PHE   A CZ   1 
ATOM   3725 N  N    . LEU   A 1 509 ? 404.786 7.641   94.427  1.00 32.88  ? 488  LEU   A N    1 
ATOM   3726 C  CA   . LEU   A 1 509 ? 406.012 7.201   93.781  1.00 31.64  ? 488  LEU   A CA   1 
ATOM   3727 C  C    . LEU   A 1 509 ? 405.849 5.778   93.278  1.00 32.23  ? 488  LEU   A C    1 
ATOM   3728 O  O    . LEU   A 1 509 ? 405.180 4.958   93.913  1.00 27.92  ? 488  LEU   A O    1 
ATOM   3729 C  CB   . LEU   A 1 509 ? 407.208 7.264   94.733  1.00 33.06  ? 488  LEU   A CB   1 
ATOM   3730 C  CG   . LEU   A 1 509 ? 407.748 8.648   95.081  1.00 36.48  ? 488  LEU   A CG   1 
ATOM   3731 C  CD1  . LEU   A 1 509 ? 408.640 8.548   96.298  1.00 42.80  ? 488  LEU   A CD1  1 
ATOM   3732 C  CD2  . LEU   A 1 509 ? 408.510 9.241   93.906  1.00 37.55  ? 488  LEU   A CD2  1 
ATOM   3733 N  N    . LEU   A 1 510 ? 406.458 5.501   92.130  1.00 28.40  ? 489  LEU   A N    1 
ATOM   3734 C  CA   . LEU   A 1 510 ? 406.653 4.137   91.664  1.00 31.82  ? 489  LEU   A CA   1 
ATOM   3735 C  C    . LEU   A 1 510 ? 407.993 3.631   92.178  1.00 29.23  ? 489  LEU   A C    1 
ATOM   3736 O  O    . LEU   A 1 510 ? 409.025 4.281   91.980  1.00 30.09  ? 489  LEU   A O    1 
ATOM   3737 C  CB   . LEU   A 1 510 ? 406.619 4.072   90.137  1.00 29.16  ? 489  LEU   A CB   1 
ATOM   3738 C  CG   . LEU   A 1 510 ? 407.171 2.796   89.495  1.00 21.97  ? 489  LEU   A CG   1 
ATOM   3739 C  CD1  . LEU   A 1 510 ? 406.238 1.621   89.737  1.00 24.80  ? 489  LEU   A CD1  1 
ATOM   3740 C  CD2  . LEU   A 1 510 ? 407.403 2.998   88.008  1.00 23.32  ? 489  LEU   A CD2  1 
ATOM   3741 N  N    . LEU   A 1 511 ? 407.974 2.485   92.850  1.00 30.45  ? 490  LEU   A N    1 
ATOM   3742 C  CA   . LEU   A 1 511 ? 409.190 1.821   93.295  1.00 30.28  ? 490  LEU   A CA   1 
ATOM   3743 C  C    . LEU   A 1 511 ? 409.513 0.696   92.324  1.00 29.46  ? 490  LEU   A C    1 
ATOM   3744 O  O    . LEU   A 1 511 ? 408.656 -0.147  92.041  1.00 31.72  ? 490  LEU   A O    1 
ATOM   3745 C  CB   . LEU   A 1 511 ? 409.036 1.270   94.714  1.00 29.77  ? 490  LEU   A CB   1 
ATOM   3746 C  CG   . LEU   A 1 511 ? 408.621 2.260   95.802  1.00 33.03  ? 490  LEU   A CG   1 
ATOM   3747 C  CD1  . LEU   A 1 511 ? 408.632 1.593   97.171  1.00 32.38  ? 490  LEU   A CD1  1 
ATOM   3748 C  CD2  . LEU   A 1 511 ? 409.525 3.481   95.786  1.00 31.44  ? 490  LEU   A CD2  1 
ATOM   3749 N  N    . MET   A 1 512 ? 410.738 0.694   91.806  1.00 27.32  ? 491  MET   A N    1 
ATOM   3750 C  CA   . MET   A 1 512 ? 411.185 -0.316  90.857  1.00 27.85  ? 491  MET   A CA   1 
ATOM   3751 C  C    . MET   A 1 512 ? 412.371 -1.058  91.446  1.00 29.81  ? 491  MET   A C    1 
ATOM   3752 O  O    . MET   A 1 512 ? 413.285 -0.435  91.997  1.00 27.28  ? 491  MET   A O    1 
ATOM   3753 C  CB   . MET   A 1 512 ? 411.587 0.308   89.513  1.00 26.26  ? 491  MET   A CB   1 
ATOM   3754 C  CG   . MET   A 1 512 ? 410.452 0.882   88.677  1.00 30.40  ? 491  MET   A CG   1 
ATOM   3755 S  SD   . MET   A 1 512 ? 409.493 -0.360  87.777  1.00 38.18  ? 491  MET   A SD   1 
ATOM   3756 C  CE   . MET   A 1 512 ? 410.747 -1.164  86.774  1.00 25.66  ? 491  MET   A CE   1 
ATOM   3757 N  N    . ALA   A 1 513 ? 412.354 -2.383  91.343  1.00 28.80  ? 492  ALA   A N    1 
ATOM   3758 C  CA   . ALA   A 1 513 ? 413.577 -3.126  91.585  1.00 27.55  ? 492  ALA   A CA   1 
ATOM   3759 C  C    . ALA   A 1 513 ? 414.624 -2.682  90.573  1.00 27.74  ? 492  ALA   A C    1 
ATOM   3760 O  O    . ALA   A 1 513 ? 414.301 -2.305  89.444  1.00 29.76  ? 492  ALA   A O    1 
ATOM   3761 C  CB   . ALA   A 1 513 ? 413.327 -4.631  91.483  1.00 27.95  ? 492  ALA   A CB   1 
ATOM   3762 N  N    . SER   A 1 514 ? 415.888 -2.693  90.988  1.00 26.11  ? 493  SER   A N    1 
ATOM   3763 C  CA   . SER   A 1 514 ? 416.963 -2.257  90.100  1.00 30.39  ? 493  SER   A CA   1 
ATOM   3764 C  C    . SER   A 1 514 ? 418.219 -3.049  90.421  1.00 30.75  ? 493  SER   A C    1 
ATOM   3765 O  O    . SER   A 1 514 ? 418.784 -2.898  91.508  1.00 32.58  ? 493  SER   A O    1 
ATOM   3766 C  CB   . SER   A 1 514 ? 417.222 -0.760  90.236  1.00 28.30  ? 493  SER   A CB   1 
ATOM   3767 O  OG   . SER   A 1 514 ? 418.338 -0.380  89.448  1.00 29.31  ? 493  SER   A OG   1 
ATOM   3768 N  N    . THR   A 1 515 ? 418.667 -3.876  89.474  1.00 29.29  ? 494  THR   A N    1 
ATOM   3769 C  CA   . THR   A 1 515 ? 419.935 -4.563  89.678  1.00 35.16  ? 494  THR   A CA   1 
ATOM   3770 C  C    . THR   A 1 515 ? 421.116 -3.610  89.528  1.00 37.07  ? 494  THR   A C    1 
ATOM   3771 O  O    . THR   A 1 515 ? 422.132 -3.778  90.211  1.00 35.23  ? 494  THR   A O    1 
ATOM   3772 C  CB   . THR   A 1 515 ? 420.073 -5.751  88.719  1.00 31.53  ? 494  THR   A CB   1 
ATOM   3773 O  OG1  . THR   A 1 515 ? 420.409 -5.287  87.407  1.00 34.59  ? 494  THR   A OG1  1 
ATOM   3774 C  CG2  . THR   A 1 515 ? 418.772 -6.546  88.657  1.00 33.49  ? 494  THR   A CG2  1 
ATOM   3775 N  N    . SER   A 1 516 ? 421.006 -2.596  88.664  1.00 32.32  ? 495  SER   A N    1 
ATOM   3776 C  CA   . SER   A 1 516 ? 422.120 -1.664  88.507  1.00 34.56  ? 495  SER   A CA   1 
ATOM   3777 C  C    . SER   A 1 516 ? 422.330 -0.845  89.774  1.00 34.20  ? 495  SER   A C    1 
ATOM   3778 O  O    . SER   A 1 516 ? 423.472 -0.563  90.156  1.00 35.01  ? 495  SER   A O    1 
ATOM   3779 C  CB   . SER   A 1 516 ? 421.892 -0.746  87.308  1.00 33.74  ? 495  SER   A CB   1 
ATOM   3780 O  OG   . SER   A 1 516 ? 420.844 0.169   87.563  1.00 46.50  ? 495  SER   A OG   1 
ATOM   3781 N  N    . ALA   A 1 517 ? 421.241 -0.451  90.436  1.00 35.03  ? 496  ALA   A N    1 
ATOM   3782 C  CA   . ALA   A 1 517 ? 421.375 0.195   91.735  1.00 32.28  ? 496  ALA   A CA   1 
ATOM   3783 C  C    . ALA   A 1 517 ? 422.096 -0.704  92.728  1.00 40.12  ? 496  ALA   A C    1 
ATOM   3784 O  O    . ALA   A 1 517 ? 422.845 -0.214  93.581  1.00 37.68  ? 496  ALA   A O    1 
ATOM   3785 C  CB   . ALA   A 1 517 ? 420.001 0.589   92.275  1.00 33.42  ? 496  ALA   A CB   1 
ATOM   3786 N  N    . CYS   A 1 518 ? 421.891 -2.020  92.634  1.00 37.42  ? 497  CYS   A N    1 
ATOM   3787 C  CA   . CYS   A 1 518 ? 422.533 -2.915  93.589  1.00 35.26  ? 497  CYS   A CA   1 
ATOM   3788 C  C    . CYS   A 1 518 ? 424.024 -3.045  93.309  1.00 38.01  ? 497  CYS   A C    1 
ATOM   3789 O  O    . CYS   A 1 518 ? 424.834 -3.066  94.243  1.00 35.18  ? 497  CYS   A O    1 
ATOM   3790 C  CB   . CYS   A 1 518 ? 421.863 -4.288  93.575  1.00 32.83  ? 497  CYS   A CB   1 
ATOM   3791 S  SG   . CYS   A 1 518 ? 422.398 -5.342  94.945  1.00 39.72  ? 497  CYS   A SG   1 
ATOM   3792 N  N    . TYR   A 1 519 ? 424.410 -3.126  92.034  1.00 38.87  ? 498  TYR   A N    1 
ATOM   3793 C  CA   . TYR   A 1 519 ? 425.828 -3.228  91.706  1.00 41.40  ? 498  TYR   A CA   1 
ATOM   3794 C  C    . TYR   A 1 519 ? 426.562 -1.927  92.002  1.00 43.29  ? 498  TYR   A C    1 
ATOM   3795 O  O    . TYR   A 1 519 ? 427.709 -1.947  92.463  1.00 41.36  ? 498  TYR   A O    1 
ATOM   3796 C  CB   . TYR   A 1 519 ? 426.005 -3.637  90.243  1.00 37.71  ? 498  TYR   A CB   1 
ATOM   3797 C  CG   . TYR   A 1 519 ? 425.902 -5.130  90.040  1.00 39.90  ? 498  TYR   A CG   1 
ATOM   3798 C  CD1  . TYR   A 1 519 ? 424.680 -5.734  89.781  1.00 42.09  ? 498  TYR   A CD1  1 
ATOM   3799 C  CD2  . TYR   A 1 519 ? 427.027 -5.938  90.130  1.00 39.20  ? 498  TYR   A CD2  1 
ATOM   3800 C  CE1  . TYR   A 1 519 ? 424.583 -7.100  89.606  1.00 41.34  ? 498  TYR   A CE1  1 
ATOM   3801 C  CE2  . TYR   A 1 519 ? 426.940 -7.305  89.956  1.00 35.95  ? 498  TYR   A CE2  1 
ATOM   3802 C  CZ   . TYR   A 1 519 ? 425.715 -7.881  89.694  1.00 36.84  ? 498  TYR   A CZ   1 
ATOM   3803 O  OH   . TYR   A 1 519 ? 425.623 -9.242  89.520  1.00 43.67  ? 498  TYR   A OH   1 
ATOM   3804 N  N    . LYS   A 1 520 ? 425.921 -0.786  91.746  1.00 39.02  ? 499  LYS   A N    1 
ATOM   3805 C  CA   . LYS   A 1 520 ? 426.530 0.489   92.107  1.00 37.82  ? 499  LYS   A CA   1 
ATOM   3806 C  C    . LYS   A 1 520 ? 426.834 0.536   93.600  1.00 39.75  ? 499  LYS   A C    1 
ATOM   3807 O  O    . LYS   A 1 520 ? 427.948 0.882   94.011  1.00 43.46  ? 499  LYS   A O    1 
ATOM   3808 C  CB   . LYS   A 1 520 ? 425.611 1.641   91.699  1.00 43.30  ? 499  LYS   A CB   1 
ATOM   3809 C  CG   . LYS   A 1 520 ? 426.199 3.022   91.931  1.00 41.31  ? 499  LYS   A CG   1 
ATOM   3810 C  CD   . LYS   A 1 520 ? 427.490 3.215   91.153  1.00 44.73  ? 499  LYS   A CD   1 
ATOM   3811 C  CE   . LYS   A 1 520 ? 428.014 4.634   91.310  1.00 47.64  ? 499  LYS   A CE   1 
ATOM   3812 N  NZ   . LYS   A 1 520 ? 429.399 4.792   90.786  1.00 58.34  ? 499  LYS   A NZ   1 
ATOM   3813 N  N    . LEU   A 1 521 ? 425.853 0.166   94.428  1.00 43.03  ? 500  LEU   A N    1 
ATOM   3814 C  CA   . LEU   A 1 521 ? 426.054 0.175   95.874  1.00 42.64  ? 500  LEU   A CA   1 
ATOM   3815 C  C    . LEU   A 1 521 ? 427.158 -0.789  96.289  1.00 40.78  ? 500  LEU   A C    1 
ATOM   3816 O  O    . LEU   A 1 521 ? 427.988 -0.461  97.145  1.00 39.61  ? 500  LEU   A O    1 
ATOM   3817 C  CB   . LEU   A 1 521 ? 424.747 -0.176  96.586  1.00 41.03  ? 500  LEU   A CB   1 
ATOM   3818 C  CG   . LEU   A 1 521 ? 424.807 -0.314  98.110  1.00 37.93  ? 500  LEU   A CG   1 
ATOM   3819 C  CD1  . LEU   A 1 521 ? 425.146 1.018   98.754  1.00 37.55  ? 500  LEU   A CD1  1 
ATOM   3820 C  CD2  . LEU   A 1 521 ? 423.496 -0.855  98.657  1.00 42.38  ? 500  LEU   A CD2  1 
ATOM   3821 N  N    . PHE   A 1 522 ? 427.184 -1.986  95.699  1.00 36.65  ? 501  PHE   A N    1 
ATOM   3822 C  CA   . PHE   A 1 522 ? 428.175 -2.977  96.107  1.00 40.50  ? 501  PHE   A CA   1 
ATOM   3823 C  C    . PHE   A 1 522 ? 429.580 -2.565  95.688  1.00 43.26  ? 501  PHE   A C    1 
ATOM   3824 O  O    . PHE   A 1 522 ? 430.532 -2.712  96.463  1.00 44.29  ? 501  PHE   A O    1 
ATOM   3825 C  CB   . PHE   A 1 522 ? 427.817 -4.349  95.538  1.00 42.80  ? 501  PHE   A CB   1 
ATOM   3826 C  CG   . PHE   A 1 522 ? 426.733 -5.054  96.302  1.00 41.66  ? 501  PHE   A CG   1 
ATOM   3827 C  CD1  . PHE   A 1 522 ? 426.100 -4.430  97.366  1.00 43.25  ? 501  PHE   A CD1  1 
ATOM   3828 C  CD2  . PHE   A 1 522 ? 426.358 -6.345  95.969  1.00 42.90  ? 501  PHE   A CD2  1 
ATOM   3829 C  CE1  . PHE   A 1 522 ? 425.104 -5.075  98.076  1.00 45.67  ? 501  PHE   A CE1  1 
ATOM   3830 C  CE2  . PHE   A 1 522 ? 425.364 -6.998  96.675  1.00 45.32  ? 501  PHE   A CE2  1 
ATOM   3831 C  CZ   . PHE   A 1 522 ? 424.736 -6.361  97.731  1.00 47.94  ? 501  PHE   A CZ   1 
ATOM   3832 N  N    . ARG   A 1 523 ? 429.732 -2.050  94.465  1.00 41.84  ? 502  ARG   A N    1 
ATOM   3833 C  CA   . ARG   A 1 523 ? 431.036 -1.553  94.041  1.00 39.58  ? 502  ARG   A CA   1 
ATOM   3834 C  C    . ARG   A 1 523 ? 431.498 -0.401  94.920  1.00 43.36  ? 502  ARG   A C    1 
ATOM   3835 O  O    . ARG   A 1 523 ? 432.700 -0.244  95.164  1.00 44.91  ? 502  ARG   A O    1 
ATOM   3836 C  CB   . ARG   A 1 523 ? 430.984 -1.125  92.573  1.00 43.14  ? 502  ARG   A CB   1 
ATOM   3837 C  CG   . ARG   A 1 523 ? 430.604 -2.255  91.630  1.00 46.48  ? 502  ARG   A CG   1 
ATOM   3838 C  CD   . ARG   A 1 523 ? 430.792 -1.875  90.171  1.00 50.90  ? 502  ARG   A CD   1 
ATOM   3839 N  NE   . ARG   A 1 523 ? 430.593 -3.024  89.296  1.00 59.70  ? 502  ARG   A NE   1 
ATOM   3840 C  CZ   . ARG   A 1 523 ? 429.575 -3.171  88.459  1.00 54.99  ? 502  ARG   A CZ   1 
ATOM   3841 N  NH1  . ARG   A 1 523 ? 428.653 -2.231  88.316  1.00 49.61  ? 502  ARG   A NH1  1 
ATOM   3842 N  NH2  . ARG   A 1 523 ? 429.485 -4.286  87.738  1.00 48.50  ? 502  ARG   A NH2  1 
ATOM   3843 N  N    . GLU   A 1 524 ? 430.558 0.406   95.413  1.00 42.62  ? 503  GLU   A N    1 
ATOM   3844 C  CA   . GLU   A 1 524 ? 430.909 1.478   96.335  1.00 46.46  ? 503  GLU   A CA   1 
ATOM   3845 C  C    . GLU   A 1 524 ? 431.420 0.917   97.656  1.00 47.12  ? 503  GLU   A C    1 
ATOM   3846 O  O    . GLU   A 1 524 ? 432.486 1.313   98.141  1.00 49.59  ? 503  GLU   A O    1 
ATOM   3847 C  CB   . GLU   A 1 524 ? 429.699 2.383   96.563  1.00 49.67  ? 503  GLU   A CB   1 
ATOM   3848 C  CG   . GLU   A 1 524 ? 430.015 3.855   96.431  1.00 63.02  ? 503  GLU   A CG   1 
ATOM   3849 C  CD   . GLU   A 1 524 ? 430.611 4.197   95.078  1.00 59.06  ? 503  GLU   A CD   1 
ATOM   3850 O  OE1  . GLU   A 1 524 ? 430.138 3.651   94.058  1.00 57.16  ? 503  GLU   A OE1  1 
ATOM   3851 O  OE2  . GLU   A 1 524 ? 431.560 5.006   95.036  1.00 63.73  ? 503  GLU   A OE2  1 
ATOM   3852 N  N    . LYS   A 1 525 ? 430.669 -0.011  98.255  1.00 44.99  ? 504  LYS   A N    1 
ATOM   3853 C  CA   . LYS   A 1 525 ? 431.099 -0.596  99.521  1.00 48.42  ? 504  LYS   A CA   1 
ATOM   3854 C  C    . LYS   A 1 525 ? 432.406 -1.359  99.365  1.00 47.10  ? 504  LYS   A C    1 
ATOM   3855 O  O    . LYS   A 1 525 ? 433.227 -1.379  100.290 1.00 47.15  ? 504  LYS   A O    1 
ATOM   3856 C  CB   . LYS   A 1 525 ? 430.005 -1.508  100.077 1.00 48.04  ? 504  LYS   A CB   1 
ATOM   3857 C  CG   . LYS   A 1 525 ? 428.708 -0.781  100.406 1.00 50.58  ? 504  LYS   A CG   1 
ATOM   3858 C  CD   . LYS   A 1 525 ? 428.937 0.304   101.446 1.00 53.79  ? 504  LYS   A CD   1 
ATOM   3859 C  CE   . LYS   A 1 525 ? 427.711 1.184   101.613 1.00 55.16  ? 504  LYS   A CE   1 
ATOM   3860 N  NZ   . LYS   A 1 525 ? 427.969 2.297   102.566 1.00 59.04  ? 504  LYS   A NZ   1 
ATOM   3861 N  N    . GLN   A 1 526 ? 432.618 -1.988  98.208  1.00 45.10  ? 505  GLN   A N    1 
ATOM   3862 C  CA   . GLN   A 1 526 ? 433.895 -2.645  97.949  1.00 44.04  ? 505  GLN   A CA   1 
ATOM   3863 C  C    . GLN   A 1 526 ? 435.023 -1.626  97.851  1.00 47.06  ? 505  GLN   A C    1 
ATOM   3864 O  O    . GLN   A 1 526 ? 436.099 -1.826  98.423  1.00 49.39  ? 505  GLN   A O    1 
ATOM   3865 C  CB   . GLN   A 1 526 ? 433.806 -3.476  96.670  1.00 44.17  ? 505  GLN   A CB   1 
ATOM   3866 C  CG   . GLN   A 1 526 ? 435.078 -4.232  96.321  1.00 45.75  ? 505  GLN   A CG   1 
ATOM   3867 C  CD   . GLN   A 1 526 ? 435.059 -4.756  94.898  1.00 50.58  ? 505  GLN   A CD   1 
ATOM   3868 O  OE1  . GLN   A 1 526 ? 434.750 -4.021  93.961  1.00 46.29  ? 505  GLN   A OE1  1 
ATOM   3869 N  NE2  . GLN   A 1 526 ? 435.381 -6.033  94.729  1.00 48.49  ? 505  GLN   A NE2  1 
ATOM   3870 N  N    . LYS   A 1 527 ? 434.795 -0.528  97.127  1.00 42.51  ? 506  LYS   A N    1 
ATOM   3871 C  CA   . LYS   A 1 527 ? 435.798 0.528   97.069  1.00 47.04  ? 506  LYS   A CA   1 
ATOM   3872 C  C    . LYS   A 1 527 ? 436.090 1.075   98.460  1.00 53.71  ? 506  LYS   A C    1 
ATOM   3873 O  O    . LYS   A 1 527 ? 437.238 1.410   98.776  1.00 56.34  ? 506  LYS   A O    1 
ATOM   3874 C  CB   . LYS   A 1 527 ? 435.334 1.649   96.138  1.00 49.49  ? 506  LYS   A CB   1 
ATOM   3875 C  CG   . LYS   A 1 527 ? 436.448 2.592   95.718  1.00 55.89  ? 506  LYS   A CG   1 
ATOM   3876 C  CD   . LYS   A 1 527 ? 437.216 2.033   94.528  1.00 60.49  ? 506  LYS   A CD   1 
ATOM   3877 C  CE   . LYS   A 1 527 ? 438.664 2.507   94.505  1.00 66.49  ? 506  LYS   A CE   1 
ATOM   3878 N  NZ   . LYS   A 1 527 ? 439.521 1.741   95.456  1.00 77.43  ? 506  LYS   A NZ   1 
ATOM   3879 N  N    . ASP   A 1 528 ? 435.064 1.167   99.306  1.00 51.92  ? 507  ASP   A N    1 
ATOM   3880 C  CA   . ASP   A 1 528 ? 435.207 1.641   100.675 1.00 48.74  ? 507  ASP   A CA   1 
ATOM   3881 C  C    . ASP   A 1 528 ? 435.825 0.599   101.602 1.00 55.85  ? 507  ASP   A C    1 
ATOM   3882 O  O    . ASP   A 1 528 ? 435.895 0.832   102.814 1.00 56.21  ? 507  ASP   A O    1 
ATOM   3883 C  CB   . ASP   A 1 528 ? 433.844 2.083   101.217 1.00 56.00  ? 507  ASP   A CB   1 
ATOM   3884 C  CG   . ASP   A 1 528 ? 433.205 3.165   100.368 1.00 62.77  ? 507  ASP   A CG   1 
ATOM   3885 O  OD1  . ASP   A 1 528 ? 433.903 3.718   99.492  1.00 62.21  ? 507  ASP   A OD1  1 
ATOM   3886 O  OD2  . ASP   A 1 528 ? 432.007 3.459   100.568 1.00 62.32  ? 507  ASP   A OD2  1 
ATOM   3887 N  N    . GLY   A 1 529 ? 436.265 -0.538  101.069 1.00 54.06  ? 508  GLY   A N    1 
ATOM   3888 C  CA   . GLY   A 1 529 ? 436.954 -1.531  101.866 1.00 52.02  ? 508  GLY   A CA   1 
ATOM   3889 C  C    . GLY   A 1 529 ? 436.070 -2.528  102.578 1.00 53.14  ? 508  GLY   A C    1 
ATOM   3890 O  O    . GLY   A 1 529 ? 436.524 -3.151  103.545 1.00 48.57  ? 508  GLY   A O    1 
ATOM   3891 N  N    . HIS   A 1 530 ? 434.826 -2.710  102.130 1.00 50.28  ? 509  HIS   A N    1 
ATOM   3892 C  CA   . HIS   A 1 530 ? 433.896 -3.654  102.739 1.00 48.36  ? 509  HIS   A CA   1 
ATOM   3893 C  C    . HIS   A 1 530 ? 433.556 -4.814  101.809 1.00 44.62  ? 509  HIS   A C    1 
ATOM   3894 O  O    . HIS   A 1 530 ? 432.457 -5.374  101.883 1.00 45.79  ? 509  HIS   A O    1 
ATOM   3895 C  CB   . HIS   A 1 530 ? 432.618 -2.942  103.173 1.00 48.77  ? 509  HIS   A CB   1 
ATOM   3896 C  CG   . HIS   A 1 530 ? 432.853 -1.864  104.179 1.00 60.31  ? 509  HIS   A CG   1 
ATOM   3897 N  ND1  . HIS   A 1 530 ? 433.366 -2.120  105.432 1.00 63.78  ? 509  HIS   A ND1  1 
ATOM   3898 C  CD2  . HIS   A 1 530 ? 432.665 -0.525  104.115 1.00 59.53  ? 509  HIS   A CD2  1 
ATOM   3899 C  CE1  . HIS   A 1 530 ? 433.477 -0.986  106.100 1.00 65.05  ? 509  HIS   A CE1  1 
ATOM   3900 N  NE2  . HIS   A 1 530 ? 433.057 -0.003  105.323 1.00 66.73  ? 509  HIS   A NE2  1 
ATOM   3901 N  N    . GLY   A 1 531 ? 434.487 -5.185  100.930 1.00 47.17  ? 510  GLY   A N    1 
ATOM   3902 C  CA   . GLY   A 1 531 ? 434.222 -6.287  100.022 1.00 49.06  ? 510  GLY   A CA   1 
ATOM   3903 C  C    . GLY   A 1 531 ? 434.012 -7.609  100.736 1.00 50.00  ? 510  GLY   A C    1 
ATOM   3904 O  O    . GLY   A 1 531 ? 433.351 -8.509  100.208 1.00 49.81  ? 510  GLY   A O    1 
ATOM   3905 N  N    . GLU   A 1 532 ? 434.561 -7.748  101.940 1.00 53.51  ? 511  GLU   A N    1 
ATOM   3906 C  CA   . GLU   A 1 532 ? 434.430 -8.976  102.711 1.00 50.32  ? 511  GLU   A CA   1 
ATOM   3907 C  C    . GLU   A 1 532 ? 433.174 -9.014  103.571 1.00 54.10  ? 511  GLU   A C    1 
ATOM   3908 O  O    . GLU   A 1 532 ? 432.991 -9.973  104.326 1.00 53.55  ? 511  GLU   A O    1 
ATOM   3909 C  CB   . GLU   A 1 532 ? 435.663 -9.181  103.595 1.00 51.07  ? 511  GLU   A CB   1 
ATOM   3910 C  CG   . GLU   A 1 532 ? 436.411 -10.446 103.255 1.00 58.05  ? 511  GLU   A CG   1 
ATOM   3911 C  CD   . GLU   A 1 532 ? 436.545 -10.631 101.759 1.00 64.96  ? 511  GLU   A CD   1 
ATOM   3912 O  OE1  . GLU   A 1 532 ? 437.182 -9.775  101.110 1.00 69.92  ? 511  GLU   A OE1  1 
ATOM   3913 O  OE2  . GLU   A 1 532 ? 435.995 -11.619 101.229 1.00 65.95  ? 511  GLU   A OE2  1 
ATOM   3914 N  N    . ALA   A 1 533 ? 432.311 -8.005  103.483 1.00 53.26  ? 512  ALA   A N    1 
ATOM   3915 C  CA   . ALA   A 1 533 ? 431.042 -8.056  104.194 1.00 57.71  ? 512  ALA   A CA   1 
ATOM   3916 C  C    . ALA   A 1 533 ? 430.237 -9.265  103.736 1.00 59.72  ? 512  ALA   A C    1 
ATOM   3917 O  O    . ALA   A 1 533 ? 430.225 -9.614  102.552 1.00 55.02  ? 512  ALA   A O    1 
ATOM   3918 C  CB   . ALA   A 1 533 ? 430.247 -6.769  103.963 1.00 49.34  ? 512  ALA   A CB   1 
ATOM   3919 N  N    . ILE   A 1 534 ? 429.562 -9.910  104.686 1.00 62.89  ? 513  ILE   A N    1 
ATOM   3920 C  CA   . ILE   A 1 534 ? 428.841 -11.154 104.440 1.00 65.67  ? 513  ILE   A CA   1 
ATOM   3921 C  C    . ILE   A 1 534 ? 427.353 -10.865 104.313 1.00 66.88  ? 513  ILE   A C    1 
ATOM   3922 O  O    . ILE   A 1 534 ? 426.803 -10.018 105.029 1.00 66.23  ? 513  ILE   A O    1 
ATOM   3923 C  CB   . ILE   A 1 534 ? 429.112 -12.178 105.559 1.00 64.25  ? 513  ILE   A CB   1 
ATOM   3924 C  CG1  . ILE   A 1 534 ? 430.347 -13.013 105.230 1.00 66.69  ? 513  ILE   A CG1  1 
ATOM   3925 C  CG2  . ILE   A 1 534 ? 427.912 -13.092 105.755 1.00 70.38  ? 513  ILE   A CG2  1 
ATOM   3926 C  CD1  . ILE   A 1 534 ? 430.144 -13.940 104.052 1.00 74.51  ? 513  ILE   A CD1  1 
ATOM   3927 N  N    . MET   A 1 535 ? 426.700 -11.571 103.398 1.00 66.56  ? 514  MET   A N    1 
ATOM   3928 C  CA   . MET   A 1 535 ? 425.262 -11.479 103.202 1.00 59.86  ? 514  MET   A CA   1 
ATOM   3929 C  C    . MET   A 1 535 ? 424.564 -12.621 103.936 1.00 65.55  ? 514  MET   A C    1 
ATOM   3930 O  O    . MET   A 1 535 ? 425.135 -13.695 104.135 1.00 69.16  ? 514  MET   A O    1 
ATOM   3931 C  CB   . MET   A 1 535 ? 424.913 -11.523 101.712 1.00 59.19  ? 514  MET   A CB   1 
ATOM   3932 C  CG   . MET   A 1 535 ? 423.435 -11.367 101.427 1.00 66.48  ? 514  MET   A CG   1 
ATOM   3933 S  SD   . MET   A 1 535 ? 423.093 -10.047 100.252 1.00 65.24  ? 514  MET   A SD   1 
ATOM   3934 C  CE   . MET   A 1 535 ? 423.737 -10.774 98.750  1.00 63.11  ? 514  MET   A CE   1 
ATOM   3935 N  N    . PHE   A 1 536 ? 423.320 -12.376 104.343 1.00 66.55  ? 515  PHE   A N    1 
ATOM   3936 C  CA   . PHE   A 1 536 ? 422.458 -13.363 104.976 1.00 68.24  ? 515  PHE   A CA   1 
ATOM   3937 C  C    . PHE   A 1 536 ? 422.852 -13.649 106.419 1.00 74.91  ? 515  PHE   A C    1 
ATOM   3938 O  O    . PHE   A 1 536 ? 422.556 -14.734 106.943 1.00 77.36  ? 515  PHE   A O    1 
ATOM   3939 C  CB   . PHE   A 1 536 ? 422.433 -14.665 104.168 1.00 67.76  ? 515  PHE   A CB   1 
ATOM   3940 C  CG   . PHE   A 1 536 ? 422.035 -14.475 102.721 1.00 69.53  ? 515  PHE   A CG   1 
ATOM   3941 C  CD1  . PHE   A 1 536 ? 420.806 -13.920 102.396 1.00 61.42  ? 515  PHE   A CD1  1 
ATOM   3942 C  CD2  . PHE   A 1 536 ? 422.884 -14.851 101.690 1.00 65.24  ? 515  PHE   A CD2  1 
ATOM   3943 C  CE1  . PHE   A 1 536 ? 420.435 -13.739 101.075 1.00 57.23  ? 515  PHE   A CE1  1 
ATOM   3944 C  CE2  . PHE   A 1 536 ? 422.517 -14.673 100.366 1.00 59.56  ? 515  PHE   A CE2  1 
ATOM   3945 C  CZ   . PHE   A 1 536 ? 421.292 -14.118 100.059 1.00 53.51  ? 515  PHE   A CZ   1 
ATOM   3946 N  N    . LYS   A 1 537 ? 423.508 -12.700 107.084 1.00 78.24  ? 516  LYS   A N    1 
ATOM   3947 C  CA   . LYS   A 1 537 ? 423.856 -12.854 108.491 1.00 82.75  ? 516  LYS   A CA   1 
ATOM   3948 C  C    . LYS   A 1 537 ? 422.601 -13.063 109.329 1.00 83.75  ? 516  LYS   A C    1 
ATOM   3949 O  O    . LYS   A 1 537 ? 421.623 -12.320 109.203 1.00 80.67  ? 516  LYS   A O    1 
ATOM   3950 C  CB   . LYS   A 1 537 ? 424.617 -11.619 108.975 1.00 85.07  ? 516  LYS   A CB   1 
ATOM   3951 C  CG   . LYS   A 1 537 ? 425.898 -11.337 108.205 1.00 83.90  ? 516  LYS   A CG   1 
ATOM   3952 C  CD   . LYS   A 1 537 ? 426.372 -9.911  108.435 1.00 85.49  ? 516  LYS   A CD   1 
ATOM   3953 C  CE   . LYS   A 1 537 ? 426.568 -9.624  109.914 1.00 85.39  ? 516  LYS   A CE   1 
ATOM   3954 N  NZ   . LYS   A 1 537 ? 427.660 -10.447 110.500 1.00 85.04  ? 516  LYS   A NZ   1 
ATOM   3955 N  N    . GLY   A 1 538 ? 422.634 -14.071 110.195 1.00 81.50  ? 517  GLY   A N    1 
ATOM   3956 C  CA   . GLY   A 1 538 ? 421.473 -14.445 110.970 1.00 79.88  ? 517  GLY   A CA   1 
ATOM   3957 C  C    . GLY   A 1 538 ? 420.640 -15.551 110.363 1.00 83.25  ? 517  GLY   A C    1 
ATOM   3958 O  O    . GLY   A 1 538 ? 419.575 -15.873 110.909 1.00 77.30  ? 517  GLY   A O    1 
ATOM   3959 N  N    . LEU   A 1 539 ? 421.086 -16.135 109.253 1.00 80.80  ? 518  LEU   A N    1 
ATOM   3960 C  CA   . LEU   A 1 539 ? 420.423 -17.260 108.596 1.00 79.88  ? 518  LEU   A CA   1 
ATOM   3961 C  C    . LEU   A 1 539 ? 421.410 -18.424 108.580 1.00 80.11  ? 518  LEU   A C    1 
ATOM   3962 O  O    . LEU   A 1 539 ? 422.282 -18.494 107.708 1.00 83.81  ? 518  LEU   A O    1 
ATOM   3963 C  CB   . LEU   A 1 539 ? 419.977 -16.881 107.187 1.00 79.04  ? 518  LEU   A CB   1 
ATOM   3964 C  CG   . LEU   A 1 539 ? 419.169 -15.588 107.077 1.00 67.30  ? 518  LEU   A CG   1 
ATOM   3965 C  CD1  . LEU   A 1 539 ? 418.885 -15.256 105.621 1.00 65.41  ? 518  LEU   A CD1  1 
ATOM   3966 C  CD2  . LEU   A 1 539 ? 417.878 -15.703 107.872 1.00 70.18  ? 518  LEU   A CD2  1 
ATOM   3967 N  N    . GLY   A 1 540 ? 421.270 -19.339 109.544 1.00 75.30  ? 519  GLY   A N    1 
ATOM   3968 C  CA   . GLY   A 1 540 ? 422.247 -20.406 109.697 1.00 70.60  ? 519  GLY   A CA   1 
ATOM   3969 C  C    . GLY   A 1 540 ? 422.281 -21.387 108.541 1.00 73.77  ? 519  GLY   A C    1 
ATOM   3970 O  O    . GLY   A 1 540 ? 423.313 -22.020 108.293 1.00 67.96  ? 519  GLY   A O    1 
ATOM   3971 N  N    . GLY   A 1 541 ? 421.164 -21.538 107.828 1.00 77.05  ? 520  GLY   A N    1 
ATOM   3972 C  CA   . GLY   A 1 541 ? 421.122 -22.420 106.673 1.00 83.13  ? 520  GLY   A CA   1 
ATOM   3973 C  C    . GLY   A 1 541 ? 421.897 -21.920 105.473 1.00 82.20  ? 520  GLY   A C    1 
ATOM   3974 O  O    . GLY   A 1 541 ? 422.042 -22.664 104.497 1.00 82.42  ? 520  GLY   A O    1 
ATOM   3975 N  N    . MET   A 1 542 ? 422.390 -20.686 105.520 1.00 87.57  ? 521  MET   A N    1 
ATOM   3976 C  CA   . MET   A 1 542 ? 423.197 -20.137 104.441 1.00 88.43  ? 521  MET   A CA   1 
ATOM   3977 C  C    . MET   A 1 542 ? 424.577 -19.758 104.973 1.00 85.30  ? 521  MET   A C    1 
ATOM   3978 O  O    . MET   A 1 542 ? 425.479 -19.415 104.210 1.00 87.79  ? 521  MET   A O    1 
ATOM   3979 C  CB   . MET   A 1 542 ? 422.507 -18.922 103.811 1.00 85.47  ? 521  MET   A CB   1 
ATOM   3980 C  CG   . MET   A 1 542 ? 421.020 -19.131 103.536 1.00 89.79  ? 521  MET   A CG   1 
ATOM   3981 S  SD   . MET   A 1 542 ? 420.371 -18.145 102.169 1.00 96.76  ? 521  MET   A SD   1 
ATOM   3982 C  CE   . MET   A 1 542 ? 421.098 -18.982 100.760 1.00 83.11  ? 521  MET   A CE   1 
ATOM   3983 N  N    . LYS   A 1 545 ? 427.545 -20.904 102.884 1.00 76.89  ? 524  LYS   A N    1 
ATOM   3984 C  CA   . LYS   A 1 545 ? 427.776 -20.332 101.562 1.00 77.60  ? 524  LYS   A CA   1 
ATOM   3985 C  C    . LYS   A 1 545 ? 428.838 -19.235 101.613 1.00 73.47  ? 524  LYS   A C    1 
ATOM   3986 O  O    . LYS   A 1 545 ? 429.604 -19.062 100.665 1.00 78.60  ? 524  LYS   A O    1 
ATOM   3987 C  CB   . LYS   A 1 545 ? 426.473 -19.776 100.973 1.00 80.62  ? 524  LYS   A CB   1 
ATOM   3988 C  CG   . LYS   A 1 545 ? 425.454 -20.839 100.573 1.00 85.20  ? 524  LYS   A CG   1 
ATOM   3989 C  CD   . LYS   A 1 545 ? 424.895 -21.551 101.793 1.00 91.05  ? 524  LYS   A CD   1 
ATOM   3990 C  CE   . LYS   A 1 545 ? 424.218 -22.859 101.424 1.00 92.66  ? 524  LYS   A CE   1 
ATOM   3991 N  NZ   . LYS   A 1 545 ? 423.788 -23.598 102.643 1.00 85.70  ? 524  LYS   A NZ   1 
ATOM   3992 N  N    . ARG   A 1 546 ? 428.875 -18.496 102.721 1.00 74.11  ? 525  ARG   A N    1 
ATOM   3993 C  CA   . ARG   A 1 546 ? 429.849 -17.425 102.929 1.00 70.16  ? 525  ARG   A CA   1 
ATOM   3994 C  C    . ARG   A 1 546 ? 429.865 -16.461 101.741 1.00 72.40  ? 525  ARG   A C    1 
ATOM   3995 O  O    . ARG   A 1 546 ? 430.859 -16.318 101.027 1.00 71.80  ? 525  ARG   A O    1 
ATOM   3996 C  CB   . ARG   A 1 546 ? 431.242 -18.004 103.190 1.00 66.49  ? 525  ARG   A CB   1 
ATOM   3997 N  N    . ILE   A 1 547 ? 428.735 -15.787 101.545 1.00 72.22  ? 526  ILE   A N    1 
ATOM   3998 C  CA   . ILE   A 1 547 ? 428.541 -14.899 100.403 1.00 67.98  ? 526  ILE   A CA   1 
ATOM   3999 C  C    . ILE   A 1 547 ? 428.956 -13.486 100.796 1.00 62.76  ? 526  ILE   A C    1 
ATOM   4000 O  O    . ILE   A 1 547 ? 428.418 -12.913 101.750 1.00 61.45  ? 526  ILE   A O    1 
ATOM   4001 C  CB   . ILE   A 1 547 ? 427.085 -14.934 99.918  1.00 70.05  ? 526  ILE   A CB   1 
ATOM   4002 C  CG1  . ILE   A 1 547 ? 426.687 -16.366 99.549  1.00 71.46  ? 526  ILE   A CG1  1 
ATOM   4003 C  CG2  . ILE   A 1 547 ? 426.893 -13.994 98.734  1.00 58.11  ? 526  ILE   A CG2  1 
ATOM   4004 C  CD1  . ILE   A 1 547 ? 425.234 -16.519 99.156  1.00 77.94  ? 526  ILE   A CD1  1 
ATOM   4005 N  N    . THR   A 1 548 ? 429.904 -12.920 100.055 1.00 56.95  ? 527  THR   A N    1 
ATOM   4006 C  CA   . THR   A 1 548 ? 430.431 -11.590 100.319 1.00 56.44  ? 527  THR   A CA   1 
ATOM   4007 C  C    . THR   A 1 548 ? 430.193 -10.683 99.118  1.00 51.16  ? 527  THR   A C    1 
ATOM   4008 O  O    . THR   A 1 548 ? 429.788 -11.128 98.041  1.00 53.39  ? 527  THR   A O    1 
ATOM   4009 C  CB   . THR   A 1 548 ? 431.928 -11.643 100.641 1.00 54.69  ? 527  THR   A CB   1 
ATOM   4010 O  OG1  . THR   A 1 548 ? 432.642 -12.131 99.499  1.00 56.54  ? 527  THR   A OG1  1 
ATOM   4011 C  CG2  . THR   A 1 548 ? 432.185 -12.560 101.826 1.00 54.76  ? 527  THR   A CG2  1 
ATOM   4012 N  N    . ILE   A 1 549 ? 430.460 -9.390  99.317  1.00 50.60  ? 528  ILE   A N    1 
ATOM   4013 C  CA   . ILE   A 1 549 ? 430.366 -8.431  98.218  1.00 46.84  ? 528  ILE   A CA   1 
ATOM   4014 C  C    . ILE   A 1 549 ? 431.386 -8.764  97.137  1.00 49.29  ? 528  ILE   A C    1 
ATOM   4015 O  O    . ILE   A 1 549 ? 431.066 -8.791  95.942  1.00 45.87  ? 528  ILE   A O    1 
ATOM   4016 C  CB   . ILE   A 1 549 ? 430.554 -6.995  98.738  1.00 48.54  ? 528  ILE   A CB   1 
ATOM   4017 C  CG1  . ILE   A 1 549 ? 429.362 -6.569  99.597  1.00 48.34  ? 528  ILE   A CG1  1 
ATOM   4018 C  CG2  . ILE   A 1 549 ? 430.748 -6.031  97.578  1.00 41.43  ? 528  ILE   A CG2  1 
ATOM   4019 C  CD1  . ILE   A 1 549 ? 429.436 -5.131  100.055 1.00 45.14  ? 528  ILE   A CD1  1 
ATOM   4020 N  N    . ASN   A 1 550 ? 432.636 -9.009  97.542  1.00 48.06  ? 529  ASN   A N    1 
ATOM   4021 C  CA   . ASN   A 1 550 ? 433.672 -9.380  96.582  1.00 45.67  ? 529  ASN   A CA   1 
ATOM   4022 C  C    . ASN   A 1 550 ? 433.256 -10.593 95.763  1.00 46.93  ? 529  ASN   A C    1 
ATOM   4023 O  O    . ASN   A 1 550 ? 433.450 -10.625 94.543  1.00 45.37  ? 529  ASN   A O    1 
ATOM   4024 C  CB   . ASN   A 1 550 ? 434.989 -9.661  97.305  1.00 45.42  ? 529  ASN   A CB   1 
ATOM   4025 C  CG   . ASN   A 1 550 ? 435.615 -8.415  97.886  1.00 50.29  ? 529  ASN   A CG   1 
ATOM   4026 O  OD1  . ASN   A 1 550 ? 435.415 -7.312  97.382  1.00 53.10  ? 529  ASN   A OD1  1 
ATOM   4027 N  ND2  . ASN   A 1 550 ? 436.391 -8.587  98.950  1.00 54.10  ? 529  ASN   A ND2  1 
ATOM   4028 N  N    . LYS   A 1 551 ? 432.696 -11.609 96.423  1.00 48.14  ? 530  LYS   A N    1 
ATOM   4029 C  CA   . LYS   A 1 551 ? 432.268 -12.806 95.709  1.00 50.52  ? 530  LYS   A CA   1 
ATOM   4030 C  C    . LYS   A 1 551 ? 431.145 -12.498 94.728  1.00 50.11  ? 530  LYS   A C    1 
ATOM   4031 O  O    . LYS   A 1 551 ? 431.059 -13.124 93.665  1.00 51.03  ? 530  LYS   A O    1 
ATOM   4032 C  CB   . LYS   A 1 551 ? 431.842 -13.884 96.711  1.00 55.74  ? 530  LYS   A CB   1 
ATOM   4033 C  CG   . LYS   A 1 551 ? 433.000 -14.415 97.559  1.00 65.12  ? 530  LYS   A CG   1 
ATOM   4034 C  CD   . LYS   A 1 551 ? 432.547 -15.339 98.691  1.00 70.50  ? 530  LYS   A CD   1 
ATOM   4035 C  CE   . LYS   A 1 551 ? 432.424 -16.794 98.247  1.00 72.33  ? 530  LYS   A CE   1 
ATOM   4036 N  NZ   . LYS   A 1 551 ? 431.181 -17.057 97.471  1.00 71.72  ? 530  LYS   A NZ   1 
ATOM   4037 N  N    . ILE   A 1 552 ? 430.290 -11.526 95.051  1.00 51.05  ? 531  ILE   A N    1 
ATOM   4038 C  CA   . ILE   A 1 552 ? 429.192 -11.178 94.156  1.00 45.69  ? 531  ILE   A CA   1 
ATOM   4039 C  C    . ILE   A 1 552 ? 429.702 -10.389 92.957  1.00 48.29  ? 531  ILE   A C    1 
ATOM   4040 O  O    . ILE   A 1 552 ? 429.262 -10.604 91.822  1.00 46.22  ? 531  ILE   A O    1 
ATOM   4041 C  CB   . ILE   A 1 552 ? 428.108 -10.399 94.921  1.00 45.05  ? 531  ILE   A CB   1 
ATOM   4042 C  CG1  . ILE   A 1 552 ? 427.425 -11.304 95.946  1.00 45.84  ? 531  ILE   A CG1  1 
ATOM   4043 C  CG2  . ILE   A 1 552 ? 427.096 -9.811  93.954  1.00 42.46  ? 531  ILE   A CG2  1 
ATOM   4044 C  CD1  . ILE   A 1 552 ? 426.307 -10.624 96.700  1.00 46.45  ? 531  ILE   A CD1  1 
ATOM   4045 N  N    . LEU   A 1 553 ? 430.631 -9.459  93.187  1.00 43.60  ? 532  LEU   A N    1 
ATOM   4046 C  CA   . LEU   A 1 553 ? 431.101 -8.608  92.099  1.00 46.42  ? 532  LEU   A CA   1 
ATOM   4047 C  C    . LEU   A 1 553 ? 432.023 -9.361  91.148  1.00 48.05  ? 532  LEU   A C    1 
ATOM   4048 O  O    . LEU   A 1 553 ? 432.104 -9.015  89.965  1.00 48.66  ? 532  LEU   A O    1 
ATOM   4049 C  CB   . LEU   A 1 553 ? 431.805 -7.376  92.667  1.00 45.31  ? 532  LEU   A CB   1 
ATOM   4050 C  CG   . LEU   A 1 553 ? 430.909 -6.397  93.431  1.00 39.65  ? 532  LEU   A CG   1 
ATOM   4051 C  CD1  . LEU   A 1 553 ? 431.730 -5.272  94.036  1.00 43.20  ? 532  LEU   A CD1  1 
ATOM   4052 C  CD2  . LEU   A 1 553 ? 429.827 -5.836  92.520  1.00 43.46  ? 532  LEU   A CD2  1 
ATOM   4053 N  N    A SER   A 1 554 ? 432.721 -10.384 91.641  0.50 48.52  ? 533  SER   A N    1 
ATOM   4054 N  N    B SER   A 1 554 ? 432.718 -10.386 91.641  0.50 48.53  ? 533  SER   A N    1 
ATOM   4055 C  CA   A SER   A 1 554 ? 433.624 -11.165 90.806  0.50 50.62  ? 533  SER   A CA   1 
ATOM   4056 C  CA   B SER   A 1 554 ? 433.624 -11.170 90.812  0.50 50.61  ? 533  SER   A CA   1 
ATOM   4057 C  C    A SER   A 1 554 ? 432.902 -12.192 89.944  0.50 50.65  ? 533  SER   A C    1 
ATOM   4058 C  C    B SER   A 1 554 ? 432.905 -12.200 89.953  0.50 50.65  ? 533  SER   A C    1 
ATOM   4059 O  O    A SER   A 1 554 ? 433.526 -12.774 89.050  0.50 51.36  ? 533  SER   A O    1 
ATOM   4060 O  O    B SER   A 1 554 ? 433.536 -12.798 89.074  0.50 51.35  ? 533  SER   A O    1 
ATOM   4061 C  CB   A SER   A 1 554 ? 434.663 -11.876 91.677  0.50 47.66  ? 533  SER   A CB   1 
ATOM   4062 C  CB   B SER   A 1 554 ? 434.655 -11.879 91.692  0.50 47.63  ? 533  SER   A CB   1 
ATOM   4063 O  OG   A SER   A 1 554 ? 435.447 -10.944 92.400  0.50 46.98  ? 533  SER   A OG   1 
ATOM   4064 O  OG   B SER   A 1 554 ? 434.021 -12.785 92.577  0.50 47.71  ? 533  SER   A OG   1 
ATOM   4065 N  N    . ASN   A 1 555 ? 431.615 -12.426 90.184  1.00 49.74  ? 534  ASN   A N    1 
ATOM   4066 C  CA   . ASN   A 1 555 ? 430.854 -13.422 89.436  1.00 47.92  ? 534  ASN   A CA   1 
ATOM   4067 C  C    . ASN   A 1 555 ? 430.418 -12.803 88.114  1.00 52.55  ? 534  ASN   A C    1 
ATOM   4068 O  O    . ASN   A 1 555 ? 429.406 -12.101 88.044  1.00 48.78  ? 534  ASN   A O    1 
ATOM   4069 C  CB   . ASN   A 1 555 ? 429.666 -13.902 90.261  1.00 47.95  ? 534  ASN   A CB   1 
ATOM   4070 C  CG   . ASN   A 1 555 ? 429.016 -15.137 89.682  1.00 52.01  ? 534  ASN   A CG   1 
ATOM   4071 O  OD1  . ASN   A 1 555 ? 429.062 -15.369 88.475  1.00 52.98  ? 534  ASN   A OD1  1 
ATOM   4072 N  ND2  . ASN   A 1 555 ? 428.401 -15.939 90.543  1.00 63.18  ? 534  ASN   A ND2  1 
ATOM   4073 N  N    . GLU   A 1 556 ? 431.191 -13.066 87.057  1.00 47.78  ? 535  GLU   A N    1 
ATOM   4074 C  CA   . GLU   A 1 556 ? 430.905 -12.482 85.748  1.00 48.37  ? 535  GLU   A CA   1 
ATOM   4075 C  C    . GLU   A 1 556 ? 429.554 -12.946 85.220  1.00 43.53  ? 535  GLU   A C    1 
ATOM   4076 O  O    . GLU   A 1 556 ? 428.746 -12.138 84.745  1.00 48.39  ? 535  GLU   A O    1 
ATOM   4077 C  CB   . GLU   A 1 556 ? 432.016 -12.845 84.763  1.00 49.62  ? 535  GLU   A CB   1 
ATOM   4078 C  CG   . GLU   A 1 556 ? 433.410 -12.695 85.332  1.00 59.79  ? 535  GLU   A CG   1 
ATOM   4079 C  CD   . GLU   A 1 556 ? 434.439 -13.483 84.552  1.00 64.52  ? 535  GLU   A CD   1 
ATOM   4080 O  OE1  . GLU   A 1 556 ? 434.388 -13.456 83.304  1.00 63.39  ? 535  GLU   A OE1  1 
ATOM   4081 O  OE2  . GLU   A 1 556 ? 435.291 -14.140 85.187  1.00 62.74  ? 535  GLU   A OE2  1 
ATOM   4082 N  N    . SER   A 1 557 ? 429.300 -14.255 85.274  1.00 46.01  ? 536  SER   A N    1 
ATOM   4083 C  CA   . SER   A 1 557 ? 428.018 -14.784 84.821  1.00 49.75  ? 536  SER   A CA   1 
ATOM   4084 C  C    . SER   A 1 557 ? 426.854 -14.085 85.509  1.00 43.63  ? 536  SER   A C    1 
ATOM   4085 O  O    . SER   A 1 557 ? 425.853 -13.746 84.868  1.00 39.95  ? 536  SER   A O    1 
ATOM   4086 C  CB   . SER   A 1 557 ? 427.962 -16.291 85.071  1.00 49.62  ? 536  SER   A CB   1 
ATOM   4087 O  OG   . SER   A 1 557 ? 426.625 -16.761 85.076  1.00 59.48  ? 536  SER   A OG   1 
ATOM   4088 N  N    . LEU   A 1 558 ? 426.969 -13.858 86.820  1.00 47.27  ? 537  LEU   A N    1 
ATOM   4089 C  CA   . LEU   A 1 558 ? 425.898 -13.185 87.545  1.00 44.48  ? 537  LEU   A CA   1 
ATOM   4090 C  C    . LEU   A 1 558 ? 425.726 -11.749 87.064  1.00 42.86  ? 537  LEU   A C    1 
ATOM   4091 O  O    . LEU   A 1 558 ? 424.601 -11.240 86.995  1.00 44.26  ? 537  LEU   A O    1 
ATOM   4092 C  CB   . LEU   A 1 558 ? 426.181 -13.228 89.047  1.00 43.02  ? 537  LEU   A CB   1 
ATOM   4093 C  CG   . LEU   A 1 558 ? 425.080 -12.741 89.990  1.00 43.45  ? 537  LEU   A CG   1 
ATOM   4094 C  CD1  . LEU   A 1 558 ? 423.790 -13.525 89.774  1.00 36.28  ? 537  LEU   A CD1  1 
ATOM   4095 C  CD2  . LEU   A 1 558 ? 425.545 -12.837 91.439  1.00 37.98  ? 537  LEU   A CD2  1 
ATOM   4096 N  N    . VAL   A 1 559 ? 426.829 -11.082 86.718  1.00 42.75  ? 538  VAL   A N    1 
ATOM   4097 C  CA   . VAL   A 1 559 ? 426.739 -9.716  86.208  1.00 41.08  ? 538  VAL   A CA   1 
ATOM   4098 C  C    . VAL   A 1 559 ? 425.943 -9.684  84.912  1.00 41.90  ? 538  VAL   A C    1 
ATOM   4099 O  O    . VAL   A 1 559 ? 425.014 -8.884  84.751  1.00 39.24  ? 538  VAL   A O    1 
ATOM   4100 C  CB   . VAL   A 1 559 ? 428.140 -9.115  86.008  1.00 44.17  ? 538  VAL   A CB   1 
ATOM   4101 C  CG1  . VAL   A 1 559 ? 428.027 -7.795  85.263  1.00 41.76  ? 538  VAL   A CG1  1 
ATOM   4102 C  CG2  . VAL   A 1 559 ? 428.839 -8.926  87.344  1.00 48.65  ? 538  VAL   A CG2  1 
ATOM   4103 N  N    . GLN   A 1 560 ? 426.311 -10.538 83.956  1.00 42.87  ? 539  GLN   A N    1 
ATOM   4104 C  CA   . GLN   A 1 560 ? 425.596 -10.554 82.686  1.00 38.41  ? 539  GLN   A CA   1 
ATOM   4105 C  C    . GLN   A 1 560 ? 424.118 -10.841 82.897  1.00 39.67  ? 539  GLN   A C    1 
ATOM   4106 O  O    . GLN   A 1 560 ? 423.257 -10.193 82.289  1.00 36.58  ? 539  GLN   A O    1 
ATOM   4107 C  CB   . GLN   A 1 560 ? 426.222 -11.580 81.744  1.00 36.12  ? 539  GLN   A CB   1 
ATOM   4108 C  CG   . GLN   A 1 560 ? 427.647 -11.237 81.338  1.00 46.79  ? 539  GLN   A CG   1 
ATOM   4109 C  CD   . GLN   A 1 560 ? 427.758 -9.859  80.707  1.00 49.34  ? 539  GLN   A CD   1 
ATOM   4110 O  OE1  . GLN   A 1 560 ? 426.981 -9.505  79.818  1.00 51.97  ? 539  GLN   A OE1  1 
ATOM   4111 N  NE2  . GLN   A 1 560 ? 428.723 -9.073  81.170  1.00 52.64  ? 539  GLN   A NE2  1 
ATOM   4112 N  N    . GLU   A 1 561 ? 423.802 -11.800 83.770  1.00 39.16  ? 540  GLU   A N    1 
ATOM   4113 C  CA   . GLU   A 1 561 ? 422.406 -12.107 84.061  1.00 33.55  ? 540  GLU   A CA   1 
ATOM   4114 C  C    . GLU   A 1 561 ? 421.660 -10.866 84.533  1.00 34.88  ? 540  GLU   A C    1 
ATOM   4115 O  O    . GLU   A 1 561 ? 420.564 -10.562 84.048  1.00 34.54  ? 540  GLU   A O    1 
ATOM   4116 C  CB   . GLU   A 1 561 ? 422.321 -13.221 85.108  1.00 36.66  ? 540  GLU   A CB   1 
ATOM   4117 C  CG   . GLU   A 1 561 ? 422.940 -14.537 84.659  1.00 40.23  ? 540  GLU   A CG   1 
ATOM   4118 C  CD   . GLU   A 1 561 ? 422.919 -15.608 85.740  1.00 43.90  ? 540  GLU   A CD   1 
ATOM   4119 O  OE1  . GLU   A 1 561 ? 422.313 -15.377 86.808  1.00 45.99  ? 540  GLU   A OE1  1 
ATOM   4120 O  OE2  . GLU   A 1 561 ? 423.514 -16.685 85.519  1.00 50.97  ? 540  GLU   A OE2  1 
ATOM   4121 N  N    . ASN   A 1 562 ? 422.244 -10.127 85.477  1.00 32.68  ? 541  ASN   A N    1 
ATOM   4122 C  CA   . ASN   A 1 562 ? 421.537 -8.992  86.053  1.00 33.64  ? 541  ASN   A CA   1 
ATOM   4123 C  C    . ASN   A 1 562 ? 421.534 -7.776  85.141  1.00 33.29  ? 541  ASN   A C    1 
ATOM   4124 O  O    . ASN   A 1 562 ? 420.678 -6.899  85.308  1.00 31.72  ? 541  ASN   A O    1 
ATOM   4125 C  CB   . ASN   A 1 562 ? 422.131 -8.645  87.415  1.00 31.68  ? 541  ASN   A CB   1 
ATOM   4126 C  CG   . ASN   A 1 562 ? 421.682 -9.607  88.491  1.00 32.67  ? 541  ASN   A CG   1 
ATOM   4127 O  OD1  . ASN   A 1 562 ? 420.612 -9.441  89.077  1.00 35.05  ? 541  ASN   A OD1  1 
ATOM   4128 N  ND2  . ASN   A 1 562 ? 422.482 -10.636 88.740  1.00 36.10  ? 541  ASN   A ND2  1 
ATOM   4129 N  N    . LEU   A 1 563 ? 422.464 -7.699  84.186  1.00 36.15  ? 542  LEU   A N    1 
ATOM   4130 C  CA   . LEU   A 1 563 ? 422.345 -6.701  83.129  1.00 35.22  ? 542  LEU   A CA   1 
ATOM   4131 C  C    . LEU   A 1 563 ? 421.133 -6.984  82.253  1.00 36.09  ? 542  LEU   A C    1 
ATOM   4132 O  O    . LEU   A 1 563 ? 420.387 -6.065  81.895  1.00 35.87  ? 542  LEU   A O    1 
ATOM   4133 C  CB   . LEU   A 1 563 ? 423.617 -6.671  82.282  1.00 38.15  ? 542  LEU   A CB   1 
ATOM   4134 C  CG   . LEU   A 1 563 ? 424.851 -5.968  82.846  1.00 40.07  ? 542  LEU   A CG   1 
ATOM   4135 C  CD1  . LEU   A 1 563 ? 426.015 -6.115  81.883  1.00 42.04  ? 542  LEU   A CD1  1 
ATOM   4136 C  CD2  . LEU   A 1 563 ? 424.557 -4.502  83.103  1.00 41.72  ? 542  LEU   A CD2  1 
ATOM   4137 N  N    . TYR   A 1 564 ? 420.927 -8.253  81.895  1.00 33.74  ? 543  TYR   A N    1 
ATOM   4138 C  CA   . TYR   A 1 564 ? 419.745 -8.633  81.132  1.00 32.19  ? 543  TYR   A CA   1 
ATOM   4139 C  C    . TYR   A 1 564 ? 418.473 -8.360  81.924  1.00 30.66  ? 543  TYR   A C    1 
ATOM   4140 O  O    . TYR   A 1 564 ? 417.499 -7.814  81.393  1.00 31.94  ? 543  TYR   A O    1 
ATOM   4141 C  CB   . TYR   A 1 564 ? 419.834 -10.109 80.742  1.00 32.13  ? 543  TYR   A CB   1 
ATOM   4142 C  CG   . TYR   A 1 564 ? 418.536 -10.674 80.224  1.00 38.14  ? 543  TYR   A CG   1 
ATOM   4143 C  CD1  . TYR   A 1 564 ? 418.051 -10.312 78.975  1.00 38.22  ? 543  TYR   A CD1  1 
ATOM   4144 C  CD2  . TYR   A 1 564 ? 417.793 -11.571 80.982  1.00 32.62  ? 543  TYR   A CD2  1 
ATOM   4145 C  CE1  . TYR   A 1 564 ? 416.865 -10.823 78.496  1.00 40.07  ? 543  TYR   A CE1  1 
ATOM   4146 C  CE2  . TYR   A 1 564 ? 416.603 -12.088 80.510  1.00 35.62  ? 543  TYR   A CE2  1 
ATOM   4147 C  CZ   . TYR   A 1 564 ? 416.144 -11.710 79.264  1.00 42.67  ? 543  TYR   A CZ   1 
ATOM   4148 O  OH   . TYR   A 1 564 ? 414.959 -12.217 78.781  1.00 45.77  ? 543  TYR   A OH   1 
ATOM   4149 N  N    . PHE   A 1 565 ? 418.463 -8.737  83.204  1.00 33.07  ? 544  PHE   A N    1 
ATOM   4150 C  CA   . PHE   A 1 565 ? 417.292 -8.476  84.030  1.00 29.64  ? 544  PHE   A CA   1 
ATOM   4151 C  C    . PHE   A 1 565 ? 417.036 -6.983  84.181  1.00 29.82  ? 544  PHE   A C    1 
ATOM   4152 O  O    . PHE   A 1 565 ? 415.882 -6.567  84.327  1.00 29.48  ? 544  PHE   A O    1 
ATOM   4153 C  CB   . PHE   A 1 565 ? 417.456 -9.136  85.398  1.00 29.12  ? 544  PHE   A CB   1 
ATOM   4154 C  CG   . PHE   A 1 565 ? 417.547 -10.633 85.337  1.00 32.68  ? 544  PHE   A CG   1 
ATOM   4155 C  CD1  . PHE   A 1 565 ? 416.828 -11.346 84.389  1.00 35.88  ? 544  PHE   A CD1  1 
ATOM   4156 C  CD2  . PHE   A 1 565 ? 418.364 -11.327 86.216  1.00 32.36  ? 544  PHE   A CD2  1 
ATOM   4157 C  CE1  . PHE   A 1 565 ? 416.912 -12.724 84.324  1.00 37.82  ? 544  PHE   A CE1  1 
ATOM   4158 C  CE2  . PHE   A 1 565 ? 418.454 -12.708 86.156  1.00 33.98  ? 544  PHE   A CE2  1 
ATOM   4159 C  CZ   . PHE   A 1 565 ? 417.727 -13.408 85.208  1.00 36.48  ? 544  PHE   A CZ   1 
ATOM   4160 N  N    . GLN   A 1 566 ? 418.084 -6.159  84.147  1.00 28.50  ? 545  GLN   A N    1 
ATOM   4161 C  CA   . GLN   A 1 566 ? 417.842 -4.721  84.170  1.00 32.48  ? 545  GLN   A CA   1 
ATOM   4162 C  C    . GLN   A 1 566 ? 417.159 -4.266  82.886  1.00 29.58  ? 545  GLN   A C    1 
ATOM   4163 O  O    . GLN   A 1 566 ? 416.301 -3.376  82.917  1.00 30.91  ? 545  GLN   A O    1 
ATOM   4164 C  CB   . GLN   A 1 566 ? 419.145 -3.956  84.398  1.00 29.86  ? 545  GLN   A CB   1 
ATOM   4165 C  CG   . GLN   A 1 566 ? 418.935 -2.460  84.635  1.00 31.20  ? 545  GLN   A CG   1 
ATOM   4166 C  CD   . GLN   A 1 566 ? 418.143 -2.171  85.901  1.00 31.43  ? 545  GLN   A CD   1 
ATOM   4167 O  OE1  . GLN   A 1 566 ? 418.486 -2.647  86.983  1.00 35.15  ? 545  GLN   A OE1  1 
ATOM   4168 N  NE2  . GLN   A 1 566 ? 417.072 -1.393  85.768  1.00 25.50  ? 545  GLN   A NE2  1 
ATOM   4169 N  N    . ARG   A 1 567 ? 417.512 -4.875  81.749  1.00 32.94  ? 546  ARG   A N    1 
ATOM   4170 C  CA   . ARG   A 1 567 ? 416.806 -4.578  80.504  1.00 31.76  ? 546  ARG   A CA   1 
ATOM   4171 C  C    . ARG   A 1 567 ? 415.325 -4.918  80.623  1.00 29.90  ? 546  ARG   A C    1 
ATOM   4172 O  O    . ARG   A 1 567 ? 414.465 -4.164  80.150  1.00 30.84  ? 546  ARG   A O    1 
ATOM   4173 C  CB   . ARG   A 1 567 ? 417.434 -5.343  79.335  1.00 32.84  ? 546  ARG   A CB   1 
ATOM   4174 C  CG   . ARG   A 1 567 ? 418.851 -4.932  78.951  1.00 38.31  ? 546  ARG   A CG   1 
ATOM   4175 C  CD   . ARG   A 1 567 ? 418.876 -3.666  78.100  1.00 46.28  ? 546  ARG   A CD   1 
ATOM   4176 N  NE   . ARG   A 1 567 ? 417.902 -3.674  77.011  1.00 46.08  ? 546  ARG   A NE   1 
ATOM   4177 C  CZ   . ARG   A 1 567 ? 418.179 -3.971  75.747  1.00 47.99  ? 546  ARG   A CZ   1 
ATOM   4178 N  NH1  . ARG   A 1 567 ? 419.388 -4.358  75.375  1.00 45.88  ? 546  ARG   A NH1  1 
ATOM   4179 N  NH2  . ARG   A 1 567 ? 417.220 -3.867  74.831  1.00 46.47  ? 546  ARG   A NH2  1 
ATOM   4180 N  N    . CYS   A 1 568 ? 415.007 -6.057  81.247  1.00 30.80  ? 547  CYS   A N    1 
ATOM   4181 C  CA   . CYS   A 1 568 ? 413.612 -6.421  81.470  1.00 32.94  ? 547  CYS   A CA   1 
ATOM   4182 C  C    . CYS   A 1 568 ? 412.917 -5.406  82.367  1.00 27.64  ? 547  CYS   A C    1 
ATOM   4183 O  O    . CYS   A 1 568 ? 411.783 -4.999  82.094  1.00 26.84  ? 547  CYS   A O    1 
ATOM   4184 C  CB   . CYS   A 1 568 ? 413.523 -7.819  82.084  1.00 26.59  ? 547  CYS   A CB   1 
ATOM   4185 S  SG   . CYS   A 1 568 ? 414.242 -9.141  81.083  1.00 29.60  ? 547  CYS   A SG   1 
ATOM   4186 N  N    . LEU   A 1 569 ? 413.579 -4.994  83.450  1.00 26.08  ? 548  LEU   A N    1 
ATOM   4187 C  CA   . LEU   A 1 569 ? 412.999 -3.984  84.325  1.00 24.52  ? 548  LEU   A CA   1 
ATOM   4188 C  C    . LEU   A 1 569 ? 412.773 -2.679  83.579  1.00 24.88  ? 548  LEU   A C    1 
ATOM   4189 O  O    . LEU   A 1 569 ? 411.730 -2.032  83.738  1.00 25.38  ? 548  LEU   A O    1 
ATOM   4190 C  CB   . LEU   A 1 569 ? 413.909 -3.755  85.530  1.00 22.17  ? 548  LEU   A CB   1 
ATOM   4191 C  CG   . LEU   A 1 569 ? 414.051 -4.954  86.464  1.00 28.18  ? 548  LEU   A CG   1 
ATOM   4192 C  CD1  . LEU   A 1 569 ? 415.330 -4.860  87.282  1.00 22.62  ? 548  LEU   A CD1  1 
ATOM   4193 C  CD2  . LEU   A 1 569 ? 412.830 -5.030  87.359  1.00 26.44  ? 548  LEU   A CD2  1 
ATOM   4194 N  N    . ASP   A 1 570 ? 413.744 -2.276  82.759  1.00 28.47  ? 549  ASP   A N    1 
ATOM   4195 C  CA   . ASP   A 1 570 ? 413.637 -1.011  82.042  1.00 29.68  ? 549  ASP   A CA   1 
ATOM   4196 C  C    . ASP   A 1 570 ? 412.566 -1.065  80.966  1.00 28.73  ? 549  ASP   A C    1 
ATOM   4197 O  O    . ASP   A 1 570 ? 411.945 -0.041  80.657  1.00 24.78  ? 549  ASP   A O    1 
ATOM   4198 C  CB   . ASP   A 1 570 ? 414.983 -0.647  81.428  1.00 30.09  ? 549  ASP   A CB   1 
ATOM   4199 C  CG   . ASP   A 1 570 ? 416.024 -0.343  82.472  1.00 30.87  ? 549  ASP   A CG   1 
ATOM   4200 O  OD1  . ASP   A 1 570 ? 415.638 0.041   83.597  1.00 30.98  ? 549  ASP   A OD1  1 
ATOM   4201 O  OD2  . ASP   A 1 570 ? 417.227 -0.485  82.167  1.00 36.49  ? 549  ASP   A OD2  1 
ATOM   4202 N  N    . TRP   A 1 571 ? 412.353 -2.237  80.371  1.00 30.13  ? 550  TRP   A N    1 
ATOM   4203 C  CA   . TRP   A 1 571 ? 411.253 -2.389  79.429  1.00 25.94  ? 550  TRP   A CA   1 
ATOM   4204 C  C    . TRP   A 1 571 ? 409.920 -2.137  80.118  1.00 24.42  ? 550  TRP   A C    1 
ATOM   4205 O  O    . TRP   A 1 571 ? 409.033 -1.479  79.560  1.00 28.14  ? 550  TRP   A O    1 
ATOM   4206 C  CB   . TRP   A 1 571 ? 411.297 -3.784  78.802  1.00 29.16  ? 550  TRP   A CB   1 
ATOM   4207 C  CG   . TRP   A 1 571 ? 410.545 -3.877  77.518  1.00 37.58  ? 550  TRP   A CG   1 
ATOM   4208 C  CD1  . TRP   A 1 571 ? 411.027 -3.625  76.267  1.00 40.88  ? 550  TRP   A CD1  1 
ATOM   4209 C  CD2  . TRP   A 1 571 ? 409.170 -4.241  77.353  1.00 35.24  ? 550  TRP   A CD2  1 
ATOM   4210 N  NE1  . TRP   A 1 571 ? 410.036 -3.811  75.331  1.00 39.41  ? 550  TRP   A NE1  1 
ATOM   4211 C  CE2  . TRP   A 1 571 ? 408.887 -4.189  75.973  1.00 40.96  ? 550  TRP   A CE2  1 
ATOM   4212 C  CE3  . TRP   A 1 571 ? 408.150 -4.607  78.237  1.00 37.42  ? 550  TRP   A CE3  1 
ATOM   4213 C  CZ2  . TRP   A 1 571 ? 407.627 -4.490  75.457  1.00 40.91  ? 550  TRP   A CZ2  1 
ATOM   4214 C  CZ3  . TRP   A 1 571 ? 406.904 -4.914  77.720  1.00 40.19  ? 550  TRP   A CZ3  1 
ATOM   4215 C  CH2  . TRP   A 1 571 ? 406.650 -4.844  76.346  1.00 41.16  ? 550  TRP   A CH2  1 
ATOM   4216 N  N    . ASN   A 1 572 ? 409.770 -2.641  81.346  1.00 27.74  ? 551  ASN   A N    1 
ATOM   4217 C  CA   . ASN   A 1 572 ? 408.577 -2.352  82.134  1.00 23.89  ? 551  ASN   A CA   1 
ATOM   4218 C  C    . ASN   A 1 572 ? 408.528 -0.888  82.549  1.00 23.55  ? 551  ASN   A C    1 
ATOM   4219 O  O    . ASN   A 1 572 ? 407.460 -0.269  82.526  1.00 24.65  ? 551  ASN   A O    1 
ATOM   4220 C  CB   . ASN   A 1 572 ? 408.531 -3.255  83.365  1.00 21.55  ? 551  ASN   A CB   1 
ATOM   4221 C  CG   . ASN   A 1 572 ? 408.083 -4.659  83.036  1.00 24.09  ? 551  ASN   A CG   1 
ATOM   4222 O  OD1  . ASN   A 1 572 ? 406.904 -4.901  82.787  1.00 25.35  ? 551  ASN   A OD1  1 
ATOM   4223 N  ND2  . ASN   A 1 572 ? 409.025 -5.596  83.033  1.00 21.71  ? 551  ASN   A ND2  1 
ATOM   4224 N  N    . ARG   A 1 573 ? 409.671 -0.324  82.950  1.00 24.38  ? 552  ARG   A N    1 
ATOM   4225 C  CA   . ARG   A 1 573 ? 409.716 1.091   83.306  1.00 23.01  ? 552  ARG   A CA   1 
ATOM   4226 C  C    . ARG   A 1 573 ? 409.104 1.943   82.203  1.00 23.05  ? 552  ARG   A C    1 
ATOM   4227 O  O    . ARG   A 1 573 ? 408.308 2.850   82.472  1.00 26.21  ? 552  ARG   A O    1 
ATOM   4228 C  CB   . ARG   A 1 573 ? 411.163 1.507   83.575  1.00 23.79  ? 552  ARG   A CB   1 
ATOM   4229 C  CG   . ARG   A 1 573 ? 411.360 2.855   84.255  1.00 22.00  ? 552  ARG   A CG   1 
ATOM   4230 C  CD   . ARG   A 1 573 ? 412.818 3.273   84.114  1.00 26.62  ? 552  ARG   A CD   1 
ATOM   4231 N  NE   . ARG   A 1 573 ? 413.223 4.300   85.065  1.00 27.78  ? 552  ARG   A NE   1 
ATOM   4232 C  CZ   . ARG   A 1 573 ? 413.723 4.047   86.267  1.00 32.14  ? 552  ARG   A CZ   1 
ATOM   4233 N  NH1  . ARG   A 1 573 ? 413.865 2.807   86.709  1.00 32.47  ? 552  ARG   A NH1  1 
ATOM   4234 N  NH2  . ARG   A 1 573 ? 414.089 5.062   87.044  1.00 27.37  ? 552  ARG   A NH2  1 
ATOM   4235 N  N    . ASP   A 1 574 ? 409.446 1.642   80.947  1.00 25.09  ? 553  ASP   A N    1 
ATOM   4236 C  CA   . ASP   A 1 574 ? 408.970 2.438   79.820  1.00 24.65  ? 553  ASP   A CA   1 
ATOM   4237 C  C    . ASP   A 1 574 ? 407.461 2.305   79.634  1.00 25.07  ? 553  ASP   A C    1 
ATOM   4238 O  O    . ASP   A 1 574 ? 406.785 3.285   79.294  1.00 26.01  ? 553  ASP   A O    1 
ATOM   4239 C  CB   . ASP   A 1 574 ? 409.714 2.024   78.550  1.00 24.27  ? 553  ASP   A CB   1 
ATOM   4240 C  CG   . ASP   A 1 574 ? 411.209 2.309   78.624  1.00 32.23  ? 553  ASP   A CG   1 
ATOM   4241 O  OD1  . ASP   A 1 574 ? 411.642 3.022   79.556  1.00 32.36  ? 553  ASP   A OD1  1 
ATOM   4242 O  OD2  . ASP   A 1 574 ? 411.955 1.819   77.748  1.00 35.78  ? 553  ASP   A OD2  1 
ATOM   4243 N  N    . ILE   A 1 575 ? 406.913 1.102   79.839  1.00 21.69  ? 554  ILE   A N    1 
ATOM   4244 C  CA   . ILE   A 1 575 ? 405.464 0.920   79.759  1.00 26.31  ? 554  ILE   A CA   1 
ATOM   4245 C  C    . ILE   A 1 575 ? 404.769 1.699   80.867  1.00 27.59  ? 554  ILE   A C    1 
ATOM   4246 O  O    . ILE   A 1 575 ? 403.746 2.357   80.643  1.00 27.86  ? 554  ILE   A O    1 
ATOM   4247 C  CB   . ILE   A 1 575 ? 405.095 -0.572  79.837  1.00 24.82  ? 554  ILE   A CB   1 
ATOM   4248 C  CG1  . ILE   A 1 575 ? 405.696 -1.353  78.681  1.00 32.67  ? 554  ILE   A CG1  1 
ATOM   4249 C  CG2  . ILE   A 1 575 ? 403.584 -0.746  79.826  1.00 28.59  ? 554  ILE   A CG2  1 
ATOM   4250 C  CD1  . ILE   A 1 575 ? 405.131 -2.736  78.611  1.00 42.65  ? 554  ILE   A CD1  1 
ATOM   4251 N  N    . LEU   A 1 576 ? 405.292 1.601   82.089  1.00 22.62  ? 555  LEU   A N    1 
ATOM   4252 C  CA   . LEU   A 1 576 ? 404.640 2.257   83.217  1.00 22.46  ? 555  LEU   A CA   1 
ATOM   4253 C  C    . LEU   A 1 576 ? 404.626 3.767   83.042  1.00 25.49  ? 555  LEU   A C    1 
ATOM   4254 O  O    . LEU   A 1 576 ? 403.600 4.419   83.276  1.00 28.46  ? 555  LEU   A O    1 
ATOM   4255 C  CB   . LEU   A 1 576 ? 405.335 1.862   84.517  1.00 23.42  ? 555  LEU   A CB   1 
ATOM   4256 C  CG   . LEU   A 1 576 ? 405.030 0.417   84.907  1.00 21.62  ? 555  LEU   A CG   1 
ATOM   4257 C  CD1  . LEU   A 1 576 ? 406.121 -0.162  85.791  1.00 25.87  ? 555  LEU   A CD1  1 
ATOM   4258 C  CD2  . LEU   A 1 576 ? 403.674 0.352   85.597  1.00 23.17  ? 555  LEU   A CD2  1 
ATOM   4259 N  N    . LYS   A 1 577 ? 405.752 4.345   82.624  1.00 23.30  ? 556  LYS   A N    1 
ATOM   4260 C  CA   . LYS   A 1 577 ? 405.782 5.781   82.375  1.00 26.36  ? 556  LYS   A CA   1 
ATOM   4261 C  C    . LYS   A 1 577 ? 404.789 6.164   81.287  1.00 29.54  ? 556  LYS   A C    1 
ATOM   4262 O  O    . LYS   A 1 577 ? 404.063 7.158   81.416  1.00 34.72  ? 556  LYS   A O    1 
ATOM   4263 C  CB   . LYS   A 1 577 ? 407.195 6.222   81.995  1.00 28.10  ? 556  LYS   A CB   1 
ATOM   4264 C  CG   . LYS   A 1 577 ? 408.225 5.954   83.074  1.00 30.69  ? 556  LYS   A CG   1 
ATOM   4265 C  CD   . LYS   A 1 577 ? 409.424 6.879   82.954  1.00 35.59  ? 556  LYS   A CD   1 
ATOM   4266 C  CE   . LYS   A 1 577 ? 410.274 6.552   81.740  1.00 35.12  ? 556  LYS   A CE   1 
ATOM   4267 N  NZ   . LYS   A 1 577 ? 411.561 7.299   81.764  1.00 40.85  ? 556  LYS   A NZ   1 
ATOM   4268 N  N    . LYS   A 1 578 ? 404.732 5.376   80.212  1.00 28.20  ? 557  LYS   A N    1 
ATOM   4269 C  CA   . LYS   A 1 578 ? 403.833 5.690   79.107  1.00 29.36  ? 557  LYS   A CA   1 
ATOM   4270 C  C    . LYS   A 1 578 ? 402.374 5.557   79.522  1.00 32.10  ? 557  LYS   A C    1 
ATOM   4271 O  O    . LYS   A 1 578 ? 401.560 6.450   79.259  1.00 32.23  ? 557  LYS   A O    1 
ATOM   4272 C  CB   . LYS   A 1 578 ? 404.126 4.784   77.912  1.00 30.97  ? 557  LYS   A CB   1 
ATOM   4273 C  CG   . LYS   A 1 578 ? 403.065 4.883   76.830  1.00 32.87  ? 557  LYS   A CG   1 
ATOM   4274 C  CD   . LYS   A 1 578 ? 403.452 4.146   75.562  1.00 48.15  ? 557  LYS   A CD   1 
ATOM   4275 C  CE   . LYS   A 1 578 ? 403.102 2.670   75.630  1.00 54.62  ? 557  LYS   A CE   1 
ATOM   4276 N  NZ   . LYS   A 1 578 ? 403.121 2.055   74.272  1.00 71.95  ? 557  LYS   A NZ   1 
ATOM   4277 N  N    . GLU   A 1 579 ? 402.020 4.445   80.161  1.00 29.15  ? 558  GLU   A N    1 
ATOM   4278 C  CA   . GLU   A 1 579 ? 400.626 4.144   80.454  1.00 25.69  ? 558  GLU   A CA   1 
ATOM   4279 C  C    . GLU   A 1 579 ? 400.124 4.771   81.746  1.00 31.32  ? 558  GLU   A C    1 
ATOM   4280 O  O    . GLU   A 1 579 ? 398.907 4.810   81.960  1.00 31.70  ? 558  GLU   A O    1 
ATOM   4281 C  CB   . GLU   A 1 579 ? 400.414 2.627   80.512  1.00 25.95  ? 558  GLU   A CB   1 
ATOM   4282 C  CG   . GLU   A 1 579 ? 400.719 1.916   79.208  1.00 27.49  ? 558  GLU   A CG   1 
ATOM   4283 C  CD   . GLU   A 1 579 ? 399.735 2.269   78.109  1.00 32.65  ? 558  GLU   A CD   1 
ATOM   4284 O  OE1  . GLU   A 1 579 ? 398.568 2.583   78.431  1.00 35.19  ? 558  GLU   A OE1  1 
ATOM   4285 O  OE2  . GLU   A 1 579 ? 400.126 2.233   76.923  1.00 44.70  ? 558  GLU   A OE2  1 
ATOM   4286 N  N    . LEU   A 1 580 ? 401.013 5.253   82.611  1.00 29.81  ? 559  LEU   A N    1 
ATOM   4287 C  CA   . LEU   A 1 580 ? 400.604 5.884   83.858  1.00 26.32  ? 559  LEU   A CA   1 
ATOM   4288 C  C    . LEU   A 1 580 ? 400.950 7.363   83.922  1.00 27.99  ? 559  LEU   A C    1 
ATOM   4289 O  O    . LEU   A 1 580 ? 400.682 8.002   84.945  1.00 31.44  ? 559  LEU   A O    1 
ATOM   4290 C  CB   . LEU   A 1 580 ? 401.232 5.160   85.053  1.00 24.37  ? 559  LEU   A CB   1 
ATOM   4291 C  CG   . LEU   A 1 580 ? 400.887 3.678   85.199  1.00 24.24  ? 559  LEU   A CG   1 
ATOM   4292 C  CD1  . LEU   A 1 580 ? 401.501 3.128   86.473  1.00 22.49  ? 559  LEU   A CD1  1 
ATOM   4293 C  CD2  . LEU   A 1 580 ? 399.383 3.465   85.182  1.00 20.75  ? 559  LEU   A CD2  1 
ATOM   4294 N  N    . GLY   A 1 581 ? 401.535 7.923   82.868  1.00 26.53  ? 560  GLY   A N    1 
ATOM   4295 C  CA   . GLY   A 1 581 ? 401.861 9.338   82.854  1.00 26.34  ? 560  GLY   A CA   1 
ATOM   4296 C  C    . GLY   A 1 581 ? 402.978 9.722   83.801  1.00 33.04  ? 560  GLY   A C    1 
ATOM   4297 O  O    . GLY   A 1 581 ? 402.942 10.811  84.391  1.00 36.46  ? 560  GLY   A O    1 
ATOM   4298 N  N    . LEU   A 1 582 ? 403.973 8.859   83.957  1.00 33.03  ? 561  LEU   A N    1 
ATOM   4299 C  CA   . LEU   A 1 582 ? 405.042 9.059   84.921  1.00 32.18  ? 561  LEU   A CA   1 
ATOM   4300 C  C    . LEU   A 1 582 ? 406.274 9.645   84.249  1.00 35.84  ? 561  LEU   A C    1 
ATOM   4301 O  O    . LEU   A 1 582 ? 406.551 9.383   83.075  1.00 39.32  ? 561  LEU   A O    1 
ATOM   4302 C  CB   . LEU   A 1 582 ? 405.422 7.742   85.599  1.00 32.66  ? 561  LEU   A CB   1 
ATOM   4303 C  CG   . LEU   A 1 582 ? 404.338 6.956   86.333  1.00 32.67  ? 561  LEU   A CG   1 
ATOM   4304 C  CD1  . LEU   A 1 582 ? 404.905 5.648   86.855  1.00 31.60  ? 561  LEU   A CD1  1 
ATOM   4305 C  CD2  . LEU   A 1 582 ? 403.765 7.789   87.462  1.00 33.73  ? 561  LEU   A CD2  1 
ATOM   4306 N  N    . THR   A 1 583 ? 407.012 10.439  85.012  1.00 34.94  ? 562  THR   A N    1 
ATOM   4307 C  CA   . THR   A 1 583 ? 408.337 10.897  84.636  1.00 36.62  ? 562  THR   A CA   1 
ATOM   4308 C  C    . THR   A 1 583 ? 409.363 10.233  85.543  1.00 37.74  ? 562  THR   A C    1 
ATOM   4309 O  O    . THR   A 1 583 ? 409.021 9.553   86.514  1.00 34.26  ? 562  THR   A O    1 
ATOM   4310 C  CB   . THR   A 1 583 ? 408.436 12.425  84.728  1.00 39.07  ? 562  THR   A CB   1 
ATOM   4311 O  OG1  . THR   A 1 583 ? 408.445 12.822  86.104  1.00 39.32  ? 562  THR   A OG1  1 
ATOM   4312 C  CG2  . THR   A 1 583 ? 407.249 13.073  84.033  1.00 32.25  ? 562  THR   A CG2  1 
ATOM   4313 N  N    . GLU   A 1 584 ? 410.640 10.430  85.215  1.00 36.70  ? 563  GLU   A N    1 
ATOM   4314 C  CA   . GLU   A 1 584 ? 411.697 9.873   86.050  1.00 35.00  ? 563  GLU   A CA   1 
ATOM   4315 C  C    . GLU   A 1 584 ? 411.666 10.432  87.465  1.00 35.15  ? 563  GLU   A C    1 
ATOM   4316 O  O    . GLU   A 1 584 ? 412.242 9.823   88.374  1.00 35.09  ? 563  GLU   A O    1 
ATOM   4317 C  CB   . GLU   A 1 584 ? 413.059 10.128  85.410  1.00 32.97  ? 563  GLU   A CB   1 
ATOM   4318 C  CG   . GLU   A 1 584 ? 413.364 9.172   84.279  1.00 40.07  ? 563  GLU   A CG   1 
ATOM   4319 C  CD   . GLU   A 1 584 ? 413.340 7.726   84.734  1.00 37.56  ? 563  GLU   A CD   1 
ATOM   4320 O  OE1  . GLU   A 1 584 ? 413.846 7.441   85.840  1.00 37.73  ? 563  GLU   A OE1  1 
ATOM   4321 O  OE2  . GLU   A 1 584 ? 412.803 6.875   83.995  1.00 36.39  ? 563  GLU   A OE2  1 
ATOM   4322 N  N    . GLN   A 1 585 ? 411.001 11.568  87.675  1.00 35.79  ? 564  GLN   A N    1 
ATOM   4323 C  CA   . GLN   A 1 585 ? 410.890 12.147  89.007  1.00 38.06  ? 564  GLN   A CA   1 
ATOM   4324 C  C    . GLN   A 1 585 ? 409.946 11.369  89.914  1.00 37.31  ? 564  GLN   A C    1 
ATOM   4325 O  O    . GLN   A 1 585 ? 409.946 11.603  91.127  1.00 34.86  ? 564  GLN   A O    1 
ATOM   4326 C  CB   . GLN   A 1 585 ? 410.425 13.599  88.896  1.00 42.13  ? 564  GLN   A CB   1 
ATOM   4327 C  CG   . GLN   A 1 585 ? 411.366 14.472  88.080  1.00 51.32  ? 564  GLN   A CG   1 
ATOM   4328 C  CD   . GLN   A 1 585 ? 410.632 15.508  87.249  1.00 75.25  ? 564  GLN   A CD   1 
ATOM   4329 O  OE1  . GLN   A 1 585 ? 409.912 16.352  87.781  1.00 72.79  ? 564  GLN   A OE1  1 
ATOM   4330 N  NE2  . GLN   A 1 585 ? 410.807 15.442  85.933  1.00 75.25  ? 564  GLN   A NE2  1 
ATOM   4331 N  N    . ASP   A 1 586 ? 409.152 10.452  89.361  1.00 35.69  ? 565  ASP   A N    1 
ATOM   4332 C  CA   . ASP   A 1 586 ? 408.162 9.700   90.120  1.00 35.23  ? 565  ASP   A CA   1 
ATOM   4333 C  C    . ASP   A 1 586 ? 408.618 8.286   90.445  1.00 33.60  ? 565  ASP   A C    1 
ATOM   4334 O  O    . ASP   A 1 586 ? 407.813 7.486   90.931  1.00 33.68  ? 565  ASP   A O    1 
ATOM   4335 C  CB   . ASP   A 1 586 ? 406.843 9.633   89.350  1.00 35.98  ? 565  ASP   A CB   1 
ATOM   4336 C  CG   . ASP   A 1 586 ? 406.367 10.990  88.892  1.00 40.69  ? 565  ASP   A CG   1 
ATOM   4337 O  OD1  . ASP   A 1 586 ? 406.487 11.957  89.673  1.00 42.78  ? 565  ASP   A OD1  1 
ATOM   4338 O  OD2  . ASP   A 1 586 ? 405.876 11.088  87.749  1.00 42.28  ? 565  ASP   A OD2  1 
ATOM   4339 N  N    . ILE   A 1 587 ? 409.880 7.957   90.183  1.00 33.17  ? 566  ILE   A N    1 
ATOM   4340 C  CA   . ILE   A 1 587 ? 410.373 6.590   90.278  1.00 32.33  ? 566  ILE   A CA   1 
ATOM   4341 C  C    . ILE   A 1 587 ? 411.565 6.555   91.221  1.00 32.50  ? 566  ILE   A C    1 
ATOM   4342 O  O    . ILE   A 1 587 ? 412.493 7.361   91.090  1.00 35.64  ? 566  ILE   A O    1 
ATOM   4343 C  CB   . ILE   A 1 587 ? 410.762 6.036   88.896  1.00 28.72  ? 566  ILE   A CB   1 
ATOM   4344 C  CG1  . ILE   A 1 587 ? 409.616 6.248   87.904  1.00 29.40  ? 566  ILE   A CG1  1 
ATOM   4345 C  CG2  . ILE   A 1 587 ? 411.141 4.565   89.002  1.00 25.88  ? 566  ILE   A CG2  1 
ATOM   4346 C  CD1  . ILE   A 1 587 ? 409.909 5.732   86.515  1.00 32.23  ? 566  ILE   A CD1  1 
ATOM   4347 N  N    . ILE   A 1 588 ? 411.538 5.620   92.166  1.00 32.84  ? 567  ILE   A N    1 
ATOM   4348 C  CA   . ILE   A 1 588 ? 412.687 5.288   92.999  1.00 34.23  ? 567  ILE   A CA   1 
ATOM   4349 C  C    . ILE   A 1 588 ? 413.122 3.878   92.635  1.00 31.61  ? 567  ILE   A C    1 
ATOM   4350 O  O    . ILE   A 1 588 ? 412.283 2.975   92.519  1.00 31.66  ? 567  ILE   A O    1 
ATOM   4351 C  CB   . ILE   A 1 588 ? 412.359 5.391   94.499  1.00 36.87  ? 567  ILE   A CB   1 
ATOM   4352 C  CG1  . ILE   A 1 588 ? 411.919 6.809   94.857  1.00 34.60  ? 567  ILE   A CG1  1 
ATOM   4353 C  CG2  . ILE   A 1 588 ? 413.565 4.990   95.338  1.00 33.31  ? 567  ILE   A CG2  1 
ATOM   4354 C  CD1  . ILE   A 1 588 ? 412.991 7.835   94.629  1.00 31.76  ? 567  ILE   A CD1  1 
ATOM   4355 N  N    . ASP   A 1 589 ? 414.423 3.694   92.438  1.00 31.25  ? 568  ASP   A N    1 
ATOM   4356 C  CA   . ASP   A 1 589 ? 414.993 2.390   92.128  1.00 32.43  ? 568  ASP   A CA   1 
ATOM   4357 C  C    . ASP   A 1 589 ? 415.516 1.763   93.415  1.00 32.80  ? 568  ASP   A C    1 
ATOM   4358 O  O    . ASP   A 1 589 ? 416.430 2.303   94.048  1.00 37.01  ? 568  ASP   A O    1 
ATOM   4359 C  CB   . ASP   A 1 589 ? 416.108 2.515   91.091  1.00 28.86  ? 568  ASP   A CB   1 
ATOM   4360 C  CG   . ASP   A 1 589 ? 415.586 2.882   89.713  1.00 37.63  ? 568  ASP   A CG   1 
ATOM   4361 O  OD1  . ASP   A 1 589 ? 414.982 2.010   89.052  1.00 33.50  ? 568  ASP   A OD1  1 
ATOM   4362 O  OD2  . ASP   A 1 589 ? 415.764 4.047   89.295  1.00 43.25  ? 568  ASP   A OD2  1 
ATOM   4363 N  N    . LEU   A 1 590 ? 414.925 0.639   93.805  1.00 31.83  ? 569  LEU   A N    1 
ATOM   4364 C  CA   . LEU   A 1 590 ? 415.447 -0.029  94.985  1.00 32.84  ? 569  LEU   A CA   1 
ATOM   4365 C  C    . LEU   A 1 590 ? 416.408 -1.132  94.573  1.00 30.26  ? 569  LEU   A C    1 
ATOM   4366 O  O    . LEU   A 1 590 ? 416.125 -1.879  93.629  1.00 32.41  ? 569  LEU   A O    1 
ATOM   4367 C  CB   . LEU   A 1 590 ? 414.316 -0.629  95.822  1.00 34.61  ? 569  LEU   A CB   1 
ATOM   4368 C  CG   . LEU   A 1 590 ? 413.244 0.313   96.376  1.00 37.76  ? 569  LEU   A CG   1 
ATOM   4369 C  CD1  . LEU   A 1 590 ? 412.283 -0.457  97.269  1.00 35.57  ? 569  LEU   A CD1  1 
ATOM   4370 C  CD2  . LEU   A 1 590 ? 413.862 1.481   97.131  1.00 36.75  ? 569  LEU   A CD2  1 
ATOM   4371 N  N    . PRO   A 1 591 ? 417.552 -1.258  95.239  1.00 31.77  ? 570  PRO   A N    1 
ATOM   4372 C  CA   . PRO   A 1 591 ? 418.512 -2.293  94.844  1.00 33.37  ? 570  PRO   A CA   1 
ATOM   4373 C  C    . PRO   A 1 591 ? 417.878 -3.673  94.904  1.00 28.55  ? 570  PRO   A C    1 
ATOM   4374 O  O    . PRO   A 1 591 ? 417.138 -4.003  95.833  1.00 34.39  ? 570  PRO   A O    1 
ATOM   4375 C  CB   . PRO   A 1 591 ? 419.648 -2.140  95.863  1.00 30.85  ? 570  PRO   A CB   1 
ATOM   4376 C  CG   . PRO   A 1 591 ? 419.057 -1.375  97.001  1.00 35.23  ? 570  PRO   A CG   1 
ATOM   4377 C  CD   . PRO   A 1 591 ? 418.018 -0.481  96.400  1.00 36.92  ? 570  PRO   A CD   1 
ATOM   4378 N  N    . ALA   A 1 592 ? 418.160 -4.472  93.882  1.00 30.78  ? 571  ALA   A N    1 
ATOM   4379 C  CA   . ALA   A 1 592 ? 417.689 -5.844  93.825  1.00 28.00  ? 571  ALA   A CA   1 
ATOM   4380 C  C    . ALA   A 1 592 ? 418.715 -6.667  93.070  1.00 29.56  ? 571  ALA   A C    1 
ATOM   4381 O  O    . ALA   A 1 592 ? 419.556 -6.136  92.340  1.00 31.20  ? 571  ALA   A O    1 
ATOM   4382 C  CB   . ALA   A 1 592 ? 416.314 -5.957  93.159  1.00 26.06  ? 571  ALA   A CB   1 
ATOM   4383 N  N    . LEU   A 1 593 ? 418.637 -7.977  93.256  1.00 30.14  ? 572  LEU   A N    1 
ATOM   4384 C  CA   . LEU   A 1 593 ? 419.582 -8.885  92.634  1.00 31.42  ? 572  LEU   A CA   1 
ATOM   4385 C  C    . LEU   A 1 593 ? 418.851 -10.184 92.344  1.00 31.30  ? 572  LEU   A C    1 
ATOM   4386 O  O    . LEU   A 1 593 ? 418.040 -10.638 93.156  1.00 36.23  ? 572  LEU   A O    1 
ATOM   4387 C  CB   . LEU   A 1 593 ? 420.791 -9.121  93.543  1.00 32.46  ? 572  LEU   A CB   1 
ATOM   4388 C  CG   . LEU   A 1 593 ? 422.058 -9.666  92.893  1.00 38.22  ? 572  LEU   A CG   1 
ATOM   4389 C  CD1  . LEU   A 1 593 ? 422.528 -8.728  91.794  1.00 39.17  ? 572  LEU   A CD1  1 
ATOM   4390 C  CD2  . LEU   A 1 593 ? 423.138 -9.856  93.946  1.00 34.83  ? 572  LEU   A CD2  1 
ATOM   4391 N  N    . PHE   A 1 594 ? 419.124 -10.766 91.183  1.00 30.21  ? 573  PHE   A N    1 
ATOM   4392 C  CA   . PHE   A 1 594 ? 418.439 -11.973 90.755  1.00 32.68  ? 573  PHE   A CA   1 
ATOM   4393 C  C    . PHE   A 1 594 ? 419.458 -13.028 90.354  1.00 36.18  ? 573  PHE   A C    1 
ATOM   4394 O  O    . PHE   A 1 594 ? 420.604 -12.724 90.015  1.00 35.76  ? 573  PHE   A O    1 
ATOM   4395 C  CB   . PHE   A 1 594 ? 417.483 -11.693 89.583  1.00 32.39  ? 573  PHE   A CB   1 
ATOM   4396 C  CG   . PHE   A 1 594 ? 416.444 -10.644 89.880  1.00 31.77  ? 573  PHE   A CG   1 
ATOM   4397 C  CD1  . PHE   A 1 594 ? 415.222 -10.994 90.433  1.00 29.82  ? 573  PHE   A CD1  1 
ATOM   4398 C  CD2  . PHE   A 1 594 ? 416.690 -9.307  89.604  1.00 31.41  ? 573  PHE   A CD2  1 
ATOM   4399 C  CE1  . PHE   A 1 594 ? 414.266 -10.031 90.707  1.00 31.66  ? 573  PHE   A CE1  1 
ATOM   4400 C  CE2  . PHE   A 1 594 ? 415.737 -8.341  89.877  1.00 29.72  ? 573  PHE   A CE2  1 
ATOM   4401 C  CZ   . PHE   A 1 594 ? 414.525 -8.704  90.429  1.00 26.57  ? 573  PHE   A CZ   1 
ATOM   4402 N  N    . LYS   A 1 595 ? 419.025 -14.282 90.414  1.00 42.87  ? 574  LYS   A N    1 
ATOM   4403 C  CA   . LYS   A 1 595 ? 419.762 -15.401 89.851  1.00 41.25  ? 574  LYS   A CA   1 
ATOM   4404 C  C    . LYS   A 1 595 ? 418.933 -15.998 88.723  1.00 39.41  ? 574  LYS   A C    1 
ATOM   4405 O  O    . LYS   A 1 595 ? 417.708 -16.109 88.836  1.00 37.61  ? 574  LYS   A O    1 
ATOM   4406 C  CB   . LYS   A 1 595 ? 420.070 -16.464 90.910  1.00 38.58  ? 574  LYS   A CB   1 
ATOM   4407 N  N    . MET   A 1 596 ? 419.594 -16.359 87.630  1.00 39.70  ? 575  MET   A N    1 
ATOM   4408 C  CA   . MET   A 1 596 ? 418.907 -16.918 86.475  1.00 39.01  ? 575  MET   A CA   1 
ATOM   4409 C  C    . MET   A 1 596 ? 418.802 -18.431 86.611  1.00 47.46  ? 575  MET   A C    1 
ATOM   4410 O  O    . MET   A 1 596 ? 419.728 -19.089 87.095  1.00 51.79  ? 575  MET   A O    1 
ATOM   4411 C  CB   . MET   A 1 596 ? 419.642 -16.549 85.185  1.00 40.46  ? 575  MET   A CB   1 
ATOM   4412 C  CG   . MET   A 1 596 ? 418.962 -17.009 83.911  1.00 42.41  ? 575  MET   A CG   1 
ATOM   4413 S  SD   . MET   A 1 596 ? 419.855 -16.437 82.456  1.00 49.27  ? 575  MET   A SD   1 
ATOM   4414 C  CE   . MET   A 1 596 ? 419.395 -14.709 82.443  1.00 41.78  ? 575  MET   A CE   1 
ATOM   4415 N  N    . ASP   A 1 597 ? 417.664 -18.980 86.191  1.00 50.82  ? 576  ASP   A N    1 
ATOM   4416 C  CA   . ASP   A 1 597 ? 417.445 -20.417 86.222  1.00 46.98  ? 576  ASP   A CA   1 
ATOM   4417 C  C    . ASP   A 1 597 ? 417.582 -20.996 84.814  1.00 47.88  ? 576  ASP   A C    1 
ATOM   4418 O  O    . ASP   A 1 597 ? 417.916 -20.299 83.854  1.00 45.67  ? 576  ASP   A O    1 
ATOM   4419 C  CB   . ASP   A 1 597 ? 416.081 -20.744 86.843  1.00 50.15  ? 576  ASP   A CB   1 
ATOM   4420 C  CG   . ASP   A 1 597 ? 414.907 -20.245 86.011  1.00 54.02  ? 576  ASP   A CG   1 
ATOM   4421 O  OD1  . ASP   A 1 597 ? 415.078 -19.977 84.803  1.00 52.63  ? 576  ASP   A OD1  1 
ATOM   4422 O  OD2  . ASP   A 1 597 ? 413.798 -20.119 86.575  1.00 54.95  ? 576  ASP   A OD2  1 
ATOM   4423 N  N    . GLU   A 1 598 ? 417.308 -22.298 84.694  1.00 55.55  ? 577  GLU   A N    1 
ATOM   4424 C  CA   . GLU   A 1 598 ? 417.476 -22.989 83.418  1.00 51.56  ? 577  GLU   A CA   1 
ATOM   4425 C  C    . GLU   A 1 598 ? 416.612 -22.385 82.316  1.00 51.76  ? 577  GLU   A C    1 
ATOM   4426 O  O    . GLU   A 1 598 ? 416.993 -22.426 81.140  1.00 49.60  ? 577  GLU   A O    1 
ATOM   4427 C  CB   . GLU   A 1 598 ? 417.159 -24.477 83.578  1.00 64.67  ? 577  GLU   A CB   1 
ATOM   4428 C  CG   . GLU   A 1 598 ? 415.889 -24.768 84.370  1.00 68.00  ? 577  GLU   A CG   1 
ATOM   4429 C  CD   . GLU   A 1 598 ? 416.104 -24.682 85.871  1.00 78.16  ? 577  GLU   A CD   1 
ATOM   4430 O  OE1  . GLU   A 1 598 ? 417.274 -24.742 86.303  1.00 78.59  ? 577  GLU   A OE1  1 
ATOM   4431 O  OE2  . GLU   A 1 598 ? 415.108 -24.549 86.615  1.00 78.81  ? 577  GLU   A OE2  1 
ATOM   4432 N  N    . ASP   A 1 599 ? 415.446 -21.842 82.664  1.00 52.00  ? 578  ASP   A N    1 
ATOM   4433 C  CA   . ASP   A 1 599 ? 414.567 -21.211 81.686  1.00 49.91  ? 578  ASP   A CA   1 
ATOM   4434 C  C    . ASP   A 1 599 ? 414.955 -19.773 81.388  1.00 47.30  ? 578  ASP   A C    1 
ATOM   4435 O  O    . ASP   A 1 599 ? 414.214 -19.076 80.685  1.00 46.65  ? 578  ASP   A O    1 
ATOM   4436 C  CB   . ASP   A 1 599 ? 413.114 -21.254 82.166  1.00 48.69  ? 578  ASP   A CB   1 
ATOM   4437 C  CG   . ASP   A 1 599 ? 412.551 -22.656 82.192  1.00 56.86  ? 578  ASP   A CG   1 
ATOM   4438 O  OD1  . ASP   A 1 599 ? 413.023 -23.502 81.404  1.00 58.22  ? 578  ASP   A OD1  1 
ATOM   4439 O  OD2  . ASP   A 1 599 ? 411.633 -22.911 82.999  1.00 56.83  ? 578  ASP   A OD2  1 
ATOM   4440 N  N    . HIS   A 1 600 ? 416.090 -19.313 81.911  1.00 45.67  ? 579  HIS   A N    1 
ATOM   4441 C  CA   . HIS   A 1 600 ? 416.543 -17.941 81.722  1.00 47.47  ? 579  HIS   A CA   1 
ATOM   4442 C  C    . HIS   A 1 600 ? 415.629 -16.937 82.415  1.00 42.49  ? 579  HIS   A C    1 
ATOM   4443 O  O    . HIS   A 1 600 ? 415.515 -15.791 81.979  1.00 47.69  ? 579  HIS   A O    1 
ATOM   4444 C  CB   . HIS   A 1 600 ? 416.670 -17.602 80.236  1.00 45.89  ? 579  HIS   A CB   1 
ATOM   4445 C  CG   . HIS   A 1 600 ? 417.584 -18.519 79.486  1.00 52.28  ? 579  HIS   A CG   1 
ATOM   4446 N  ND1  . HIS   A 1 600 ? 418.956 -18.451 79.593  1.00 55.74  ? 579  HIS   A ND1  1 
ATOM   4447 C  CD2  . HIS   A 1 600 ? 417.323 -19.527 78.620  1.00 54.22  ? 579  HIS   A CD2  1 
ATOM   4448 C  CE1  . HIS   A 1 600 ? 419.501 -19.378 78.825  1.00 57.84  ? 579  HIS   A CE1  1 
ATOM   4449 N  NE2  . HIS   A 1 600 ? 418.532 -20.044 78.224  1.00 63.86  ? 579  HIS   A NE2  1 
ATOM   4450 N  N    . ARG   A 1 601 ? 414.970 -17.354 83.491  1.00 33.67  ? 580  ARG   A N    1 
ATOM   4451 C  CA   . ARG   A 1 601 ? 414.117 -16.474 84.272  1.00 37.53  ? 580  ARG   A CA   1 
ATOM   4452 C  C    . ARG   A 1 601 ? 414.758 -16.195 85.627  1.00 39.17  ? 580  ARG   A C    1 
ATOM   4453 O  O    . ARG   A 1 601 ? 415.583 -16.968 86.122  1.00 40.64  ? 580  ARG   A O    1 
ATOM   4454 C  CB   . ARG   A 1 601 ? 412.717 -17.076 84.442  1.00 35.67  ? 580  ARG   A CB   1 
ATOM   4455 C  CG   . ARG   A 1 601 ? 411.964 -17.247 83.124  1.00 40.28  ? 580  ARG   A CG   1 
ATOM   4456 C  CD   . ARG   A 1 601 ? 410.509 -17.615 83.363  1.00 38.04  ? 580  ARG   A CD   1 
ATOM   4457 N  NE   . ARG   A 1 601 ? 409.720 -17.676 82.137  1.00 38.64  ? 580  ARG   A NE   1 
ATOM   4458 C  CZ   . ARG   A 1 601 ? 409.368 -18.799 81.526  1.00 38.91  ? 580  ARG   A CZ   1 
ATOM   4459 N  NH1  . ARG   A 1 601 ? 409.767 -19.980 81.969  1.00 45.66  ? 580  ARG   A NH1  1 
ATOM   4460 N  NH2  . ARG   A 1 601 ? 408.590 -18.737 80.449  1.00 39.38  ? 580  ARG   A NH2  1 
ATOM   4461 N  N    . ALA   A 1 602 ? 414.374 -15.069 86.219  1.00 36.16  ? 581  ALA   A N    1 
ATOM   4462 C  CA   . ALA   A 1 602 ? 415.022 -14.550 87.415  1.00 33.03  ? 581  ALA   A CA   1 
ATOM   4463 C  C    . ALA   A 1 602 ? 414.276 -14.965 88.676  1.00 32.29  ? 581  ALA   A C    1 
ATOM   4464 O  O    . ALA   A 1 602 ? 413.043 -15.008 88.701  1.00 36.74  ? 581  ALA   A O    1 
ATOM   4465 C  CB   . ALA   A 1 602 ? 415.119 -13.024 87.359  1.00 26.88  ? 581  ALA   A CB   1 
ATOM   4466 N  N    . ARG   A 1 603 ? 415.034 -15.263 89.724  1.00 34.80  ? 582  ARG   A N    1 
ATOM   4467 C  CA   . ARG   A 1 603 ? 414.494 -15.413 91.066  1.00 38.04  ? 582  ARG   A CA   1 
ATOM   4468 C  C    . ARG   A 1 603 ? 415.344 -14.579 92.009  1.00 31.78  ? 582  ARG   A C    1 
ATOM   4469 O  O    . ARG   A 1 603 ? 416.564 -14.485 91.840  1.00 37.38  ? 582  ARG   A O    1 
ATOM   4470 C  CB   . ARG   A 1 603 ? 414.470 -16.880 91.509  1.00 38.83  ? 582  ARG   A CB   1 
ATOM   4471 C  CG   . ARG   A 1 603 ? 415.806 -17.575 91.357  1.00 52.32  ? 582  ARG   A CG   1 
ATOM   4472 C  CD   . ARG   A 1 603 ? 415.672 -19.085 91.366  1.00 61.61  ? 582  ARG   A CD   1 
ATOM   4473 N  NE   . ARG   A 1 603 ? 416.721 -19.706 90.565  1.00 64.04  ? 582  ARG   A NE   1 
ATOM   4474 C  CZ   . ARG   A 1 603 ? 417.976 -19.868 90.965  1.00 72.78  ? 582  ARG   A CZ   1 
ATOM   4475 N  NH1  . ARG   A 1 603 ? 418.379 -19.462 92.159  1.00 76.80  ? 582  ARG   A NH1  1 
ATOM   4476 N  NH2  . ARG   A 1 603 ? 418.849 -20.447 90.145  1.00 68.77  ? 582  ARG   A NH2  1 
ATOM   4477 N  N    . ALA   A 1 604 ? 414.690 -13.962 92.990  1.00 35.44  ? 583  ALA   A N    1 
ATOM   4478 C  CA   . ALA   A 1 604 ? 415.365 -13.039 93.892  1.00 32.47  ? 583  ALA   A CA   1 
ATOM   4479 C  C    . ALA   A 1 604 ? 416.586 -13.681 94.538  1.00 34.77  ? 583  ALA   A C    1 
ATOM   4480 O  O    . ALA   A 1 604 ? 416.514 -14.787 95.082  1.00 34.98  ? 583  ALA   A O    1 
ATOM   4481 C  CB   . ALA   A 1 604 ? 414.389 -12.560 94.967  1.00 34.91  ? 583  ALA   A CB   1 
ATOM   4482 N  N    . PHE   A 1 605 ? 417.715 -12.973 94.473  1.00 35.90  ? 584  PHE   A N    1 
ATOM   4483 C  CA   . PHE   A 1 605 ? 418.912 -13.404 95.187  1.00 35.98  ? 584  PHE   A CA   1 
ATOM   4484 C  C    . PHE   A 1 605 ? 418.765 -13.171 96.688  1.00 42.06  ? 584  PHE   A C    1 
ATOM   4485 O  O    . PHE   A 1 605 ? 419.146 -14.025 97.498  1.00 40.75  ? 584  PHE   A O    1 
ATOM   4486 C  CB   . PHE   A 1 605 ? 420.130 -12.665 94.632  1.00 39.24  ? 584  PHE   A CB   1 
ATOM   4487 C  CG   . PHE   A 1 605 ? 421.444 -13.178 95.139  1.00 43.09  ? 584  PHE   A CG   1 
ATOM   4488 C  CD1  . PHE   A 1 605 ? 421.858 -12.903 96.431  1.00 48.92  ? 584  PHE   A CD1  1 
ATOM   4489 C  CD2  . PHE   A 1 605 ? 422.277 -13.915 94.315  1.00 43.75  ? 584  PHE   A CD2  1 
ATOM   4490 C  CE1  . PHE   A 1 605 ? 423.070 -13.368 96.898  1.00 51.74  ? 584  PHE   A CE1  1 
ATOM   4491 C  CE2  . PHE   A 1 605 ? 423.492 -14.380 94.776  1.00 41.39  ? 584  PHE   A CE2  1 
ATOM   4492 C  CZ   . PHE   A 1 605 ? 423.890 -14.106 96.069  1.00 48.19  ? 584  PHE   A CZ   1 
ATOM   4493 N  N    . PHE   A 1 606 ? 418.226 -12.024 97.075  1.00 42.06  ? 585  PHE   A N    1 
ATOM   4494 C  CA   . PHE   A 1 606 ? 417.831 -11.730 98.442  1.00 42.80  ? 585  PHE   A CA   1 
ATOM   4495 C  C    . PHE   A 1 606 ? 416.422 -11.163 98.425  1.00 43.16  ? 585  PHE   A C    1 
ATOM   4496 O  O    . PHE   A 1 606 ? 415.932 -10.733 97.376  1.00 44.32  ? 585  PHE   A O    1 
ATOM   4497 C  CB   . PHE   A 1 606 ? 418.798 -10.746 99.123  1.00 45.06  ? 585  PHE   A CB   1 
ATOM   4498 C  CG   . PHE   A 1 606 ? 419.011 -9.463  98.364  1.00 40.71  ? 585  PHE   A CG   1 
ATOM   4499 C  CD1  . PHE   A 1 606 ? 418.117 -8.411  98.483  1.00 41.56  ? 585  PHE   A CD1  1 
ATOM   4500 C  CD2  . PHE   A 1 606 ? 420.123 -9.301  97.552  1.00 36.84  ? 585  PHE   A CD2  1 
ATOM   4501 C  CE1  . PHE   A 1 606 ? 418.318 -7.227  97.792  1.00 38.95  ? 585  PHE   A CE1  1 
ATOM   4502 C  CE2  . PHE   A 1 606 ? 420.332 -8.120  96.860  1.00 33.89  ? 585  PHE   A CE2  1 
ATOM   4503 C  CZ   . PHE   A 1 606 ? 419.428 -7.082  96.979  1.00 32.94  ? 585  PHE   A CZ   1 
ATOM   4504 N  N    . PRO   A 1 607 ? 415.740 -11.153 99.570  1.00 43.15  ? 586  PRO   A N    1 
ATOM   4505 C  CA   . PRO   A 1 607 ? 414.312 -10.809 99.580  1.00 43.80  ? 586  PRO   A CA   1 
ATOM   4506 C  C    . PRO   A 1 607 ? 414.019 -9.520  98.825  1.00 43.07  ? 586  PRO   A C    1 
ATOM   4507 O  O    . PRO   A 1 607 ? 414.695 -8.504  99.000  1.00 41.31  ? 586  PRO   A O    1 
ATOM   4508 C  CB   . PRO   A 1 607 ? 413.999 -10.674 101.073 1.00 41.85  ? 586  PRO   A CB   1 
ATOM   4509 C  CG   . PRO   A 1 607 ? 414.972 -11.589 101.731 1.00 46.00  ? 586  PRO   A CG   1 
ATOM   4510 C  CD   . PRO   A 1 607 ? 416.236 -11.485 100.917 1.00 45.42  ? 586  PRO   A CD   1 
ATOM   4511 N  N    . ASN   A 1 608 ? 412.999 -9.572  97.973  1.00 38.13  ? 587  ASN   A N    1 
ATOM   4512 C  CA   A ASN   A 1 608 ? 412.600 -8.417  97.174  0.50 39.29  ? 587  ASN   A CA   1 
ATOM   4513 C  CA   B ASN   A 1 608 ? 412.606 -8.415  97.177  0.50 39.30  ? 587  ASN   A CA   1 
ATOM   4514 C  C    . ASN   A 1 608 ? 411.995 -7.353  98.081  1.00 36.96  ? 587  ASN   A C    1 
ATOM   4515 O  O    . ASN   A 1 608 ? 410.883 -7.523  98.586  1.00 38.97  ? 587  ASN   A O    1 
ATOM   4516 C  CB   A ASN   A 1 608 ? 411.614 -8.843  96.090  0.50 38.48  ? 587  ASN   A CB   1 
ATOM   4517 C  CB   B ASN   A 1 608 ? 411.629 -8.835  96.084  0.50 38.80  ? 587  ASN   A CB   1 
ATOM   4518 C  CG   A ASN   A 1 608 ? 412.299 -9.492  94.902  0.50 36.69  ? 587  ASN   A CG   1 
ATOM   4519 C  CG   B ASN   A 1 608 ? 411.067 -7.656  95.327  0.50 38.41  ? 587  ASN   A CG   1 
ATOM   4520 O  OD1  A ASN   A 1 608 ? 413.410 -9.117  94.531  0.50 38.86  ? 587  ASN   A OD1  1 
ATOM   4521 O  OD1  B ASN   A 1 608 ? 411.806 -6.895  94.705  0.50 39.14  ? 587  ASN   A OD1  1 
ATOM   4522 N  ND2  A ASN   A 1 608 ? 411.639 -10.478 94.302  0.50 31.62  ? 587  ASN   A ND2  1 
ATOM   4523 N  ND2  B ASN   A 1 608 ? 409.751 -7.492  95.381  0.50 42.91  ? 587  ASN   A ND2  1 
ATOM   4524 N  N    . MET   A 1 609 ? 412.722 -6.249  98.278  1.00 39.00  ? 588  MET   A N    1 
ATOM   4525 C  CA   . MET   A 1 609 ? 412.259 -5.182  99.156  1.00 38.65  ? 588  MET   A CA   1 
ATOM   4526 C  C    . MET   A 1 609 ? 411.110 -4.387  98.560  1.00 36.99  ? 588  MET   A C    1 
ATOM   4527 O  O    . MET   A 1 609 ? 410.441 -3.653  99.294  1.00 37.78  ? 588  MET   A O    1 
ATOM   4528 C  CB   . MET   A 1 609 ? 413.414 -4.242  99.483  1.00 31.83  ? 588  MET   A CB   1 
ATOM   4529 C  CG   . MET   A 1 609 ? 414.481 -4.874  100.343 1.00 38.07  ? 588  MET   A CG   1 
ATOM   4530 S  SD   . MET   A 1 609 ? 415.747 -3.698  100.832 1.00 42.91  ? 588  MET   A SD   1 
ATOM   4531 C  CE   . MET   A 1 609 ? 416.779 -3.692  99.370  1.00 36.16  ? 588  MET   A CE   1 
ATOM   4532 N  N    . VAL   A 1 610 ? 410.866 -4.512  97.254  1.00 38.19  ? 589  VAL   A N    1 
ATOM   4533 C  CA   . VAL   A 1 610 ? 409.809 -3.734  96.619  1.00 39.80  ? 589  VAL   A CA   1 
ATOM   4534 C  C    . VAL   A 1 610 ? 408.435 -4.219  97.056  1.00 33.82  ? 589  VAL   A C    1 
ATOM   4535 O  O    . VAL   A 1 610 ? 407.467 -3.449  97.052  1.00 34.78  ? 589  VAL   A O    1 
ATOM   4536 C  CB   . VAL   A 1 610 ? 409.960 -3.794  95.090  1.00 35.73  ? 589  VAL   A CB   1 
ATOM   4537 C  CG1  . VAL   A 1 610 ? 409.086 -2.744  94.434  1.00 33.58  ? 589  VAL   A CG1  1 
ATOM   4538 C  CG2  . VAL   A 1 610 ? 411.414 -3.616  94.698  1.00 40.09  ? 589  VAL   A CG2  1 
ATOM   4539 N  N    . ASN   A 1 611 ? 408.317 -5.492  97.430  1.00 34.10  ? 590  ASN   A N    1 
ATOM   4540 C  CA   . ASN   A 1 611 ? 407.030 -6.071  97.810  1.00 40.69  ? 590  ASN   A CA   1 
ATOM   4541 C  C    . ASN   A 1 611 ? 406.818 -5.813  99.299  1.00 38.17  ? 590  ASN   A C    1 
ATOM   4542 O  O    . ASN   A 1 611 ? 407.080 -6.654  100.161 1.00 37.05  ? 590  ASN   A O    1 
ATOM   4543 C  CB   . ASN   A 1 611 ? 406.991 -7.554  97.466  1.00 42.90  ? 590  ASN   A CB   1 
ATOM   4544 C  CG   . ASN   A 1 611 ? 405.626 -8.170  97.687  1.00 46.29  ? 590  ASN   A CG   1 
ATOM   4545 O  OD1  . ASN   A 1 611 ? 404.642 -7.465  97.910  1.00 47.65  ? 590  ASN   A OD1  1 
ATOM   4546 N  ND2  . ASN   A 1 611 ? 405.560 -9.494  97.621  1.00 60.19  ? 590  ASN   A ND2  1 
ATOM   4547 N  N    . MET   A 1 612 ? 406.326 -4.615  99.597  1.00 35.72  ? 591  MET   A N    1 
ATOM   4548 C  CA   . MET   A 1 612 ? 406.250 -4.125  100.961 1.00 34.01  ? 591  MET   A CA   1 
ATOM   4549 C  C    . MET   A 1 612 ? 404.812 -3.809  101.349 1.00 36.06  ? 591  MET   A C    1 
ATOM   4550 O  O    . MET   A 1 612 ? 403.931 -3.647  100.499 1.00 35.71  ? 591  MET   A O    1 
ATOM   4551 C  CB   . MET   A 1 612 ? 407.124 -2.877  101.137 1.00 34.22  ? 591  MET   A CB   1 
ATOM   4552 C  CG   . MET   A 1 612 ? 406.790 -1.760  100.162 1.00 32.24  ? 591  MET   A CG   1 
ATOM   4553 S  SD   . MET   A 1 612 ? 407.837 -0.305  100.366 1.00 41.30  ? 591  MET   A SD   1 
ATOM   4554 C  CE   . MET   A 1 612 ? 409.433 -0.941  99.857  1.00 33.78  ? 591  MET   A CE   1 
ATOM   4555 N  N    . ILE   A 1 613 ? 404.593 -3.732  102.658 1.00 36.06  ? 592  ILE   A N    1 
ATOM   4556 C  CA   . ILE   A 1 613 ? 403.316 -3.326  103.234 1.00 35.37  ? 592  ILE   A CA   1 
ATOM   4557 C  C    . ILE   A 1 613 ? 403.295 -1.804  103.299 1.00 38.31  ? 592  ILE   A C    1 
ATOM   4558 O  O    . ILE   A 1 613 ? 404.150 -1.195  103.951 1.00 41.13  ? 592  ILE   A O    1 
ATOM   4559 C  CB   . ILE   A 1 613 ? 403.128 -3.932  104.633 1.00 39.23  ? 592  ILE   A CB   1 
ATOM   4560 C  CG1  . ILE   A 1 613 ? 403.504 -5.414  104.631 1.00 43.73  ? 592  ILE   A CG1  1 
ATOM   4561 C  CG2  . ILE   A 1 613 ? 401.702 -3.733  105.129 1.00 36.59  ? 592  ILE   A CG2  1 
ATOM   4562 C  CD1  . ILE   A 1 613 ? 403.483 -6.044  106.007 1.00 47.75  ? 592  ILE   A CD1  1 
ATOM   4563 N  N    . VAL   A 1 614 ? 402.321 -1.187  102.637 1.00 32.14  ? 593  VAL   A N    1 
ATOM   4564 C  CA   . VAL   A 1 614 ? 402.218 0.268   102.579 1.00 38.27  ? 593  VAL   A CA   1 
ATOM   4565 C  C    . VAL   A 1 614 ? 401.022 0.695   103.419 1.00 38.59  ? 593  VAL   A C    1 
ATOM   4566 O  O    . VAL   A 1 614 ? 399.866 0.476   103.034 1.00 36.25  ? 593  VAL   A O    1 
ATOM   4567 C  CB   . VAL   A 1 614 ? 402.100 0.777   101.138 1.00 34.01  ? 593  VAL   A CB   1 
ATOM   4568 C  CG1  . VAL   A 1 614 ? 402.130 2.296   101.113 1.00 35.99  ? 593  VAL   A CG1  1 
ATOM   4569 C  CG2  . VAL   A 1 614 ? 403.226 0.210   100.293 1.00 29.16  ? 593  VAL   A CG2  1 
ATOM   4570 N  N    . LEU   A 1 615 ? 401.298 1.317   104.563 1.00 35.62  ? 594  LEU   A N    1 
ATOM   4571 C  CA   . LEU   A 1 615 ? 400.283 1.825   105.486 1.00 40.22  ? 594  LEU   A CA   1 
ATOM   4572 C  C    . LEU   A 1 615 ? 400.476 3.335   105.599 1.00 42.07  ? 594  LEU   A C    1 
ATOM   4573 O  O    . LEU   A 1 615 ? 400.995 3.839   106.597 1.00 41.18  ? 594  LEU   A O    1 
ATOM   4574 C  CB   . LEU   A 1 615 ? 400.395 1.133   106.841 1.00 37.80  ? 594  LEU   A CB   1 
ATOM   4575 C  CG   . LEU   A 1 615 ? 400.259 -0.389  106.810 1.00 36.92  ? 594  LEU   A CG   1 
ATOM   4576 C  CD1  . LEU   A 1 615 ? 400.518 -0.972  108.187 1.00 39.22  ? 594  LEU   A CD1  1 
ATOM   4577 C  CD2  . LEU   A 1 615 ? 398.884 -0.792  106.301 1.00 36.02  ? 594  LEU   A CD2  1 
ATOM   4578 N  N    . ASP   A 1 616 ? 400.048 4.058   104.564 1.00 45.37  ? 595  ASP   A N    1 
ATOM   4579 C  CA   . ASP   A 1 616 ? 400.338 5.482   104.463 1.00 41.80  ? 595  ASP   A CA   1 
ATOM   4580 C  C    . ASP   A 1 616 ? 401.841 5.707   104.590 1.00 39.22  ? 595  ASP   A C    1 
ATOM   4581 O  O    . ASP   A 1 616 ? 402.619 5.116   103.836 1.00 44.11  ? 595  ASP   A O    1 
ATOM   4582 C  CB   . ASP   A 1 616 ? 399.558 6.272   105.516 1.00 40.26  ? 595  ASP   A CB   1 
ATOM   4583 C  CG   . ASP   A 1 616 ? 398.071 6.331   105.211 1.00 57.24  ? 595  ASP   A CG   1 
ATOM   4584 O  OD1  . ASP   A 1 616 ? 397.708 6.354   104.013 1.00 59.42  ? 595  ASP   A OD1  1 
ATOM   4585 O  OD2  . ASP   A 1 616 ? 397.265 6.351   106.165 1.00 58.74  ? 595  ASP   A OD2  1 
ATOM   4586 N  N    . LYS   A 1 617 ? 402.271 6.542   105.537 1.00 39.09  ? 596  LYS   A N    1 
ATOM   4587 C  CA   . LYS   A 1 617 ? 403.694 6.855   105.645 1.00 47.28  ? 596  LYS   A CA   1 
ATOM   4588 C  C    . LYS   A 1 617 ? 404.528 5.689   106.161 1.00 45.12  ? 596  LYS   A C    1 
ATOM   4589 O  O    . LYS   A 1 617 ? 405.760 5.766   106.111 1.00 43.49  ? 596  LYS   A O    1 
ATOM   4590 C  CB   . LYS   A 1 617 ? 403.905 8.072   106.552 1.00 47.00  ? 596  LYS   A CB   1 
ATOM   4591 C  CG   . LYS   A 1 617 ? 403.183 7.991   107.891 1.00 47.22  ? 596  LYS   A CG   1 
ATOM   4592 C  CD   . LYS   A 1 617 ? 404.136 8.181   109.065 1.00 56.94  ? 596  LYS   A CD   1 
ATOM   4593 C  CE   . LYS   A 1 617 ? 403.395 8.067   110.391 1.00 65.19  ? 596  LYS   A CE   1 
ATOM   4594 N  NZ   . LYS   A 1 617 ? 404.307 7.752   111.526 1.00 68.89  ? 596  LYS   A NZ   1 
ATOM   4595 N  N    . ASP   A 1 618 ? 403.900 4.621   106.642 1.00 41.94  ? 597  ASP   A N    1 
ATOM   4596 C  CA   . ASP   A 1 618 ? 404.603 3.522   107.289 1.00 44.46  ? 597  ASP   A CA   1 
ATOM   4597 C  C    . ASP   A 1 618 ? 404.742 2.361   106.314 1.00 42.50  ? 597  ASP   A C    1 
ATOM   4598 O  O    . ASP   A 1 618 ? 403.738 1.839   105.816 1.00 44.76  ? 597  ASP   A O    1 
ATOM   4599 C  CB   . ASP   A 1 618 ? 403.867 3.090   108.555 1.00 46.94  ? 597  ASP   A CB   1 
ATOM   4600 C  CG   . ASP   A 1 618 ? 404.043 4.077   109.688 1.00 56.38  ? 597  ASP   A CG   1 
ATOM   4601 O  OD1  . ASP   A 1 618 ? 405.135 4.092   110.296 1.00 60.26  ? 597  ASP   A OD1  1 
ATOM   4602 O  OD2  . ASP   A 1 618 ? 403.102 4.855   109.954 1.00 59.45  ? 597  ASP   A OD2  1 
ATOM   4603 N  N    . LEU   A 1 619 ? 405.981 1.961   106.050 1.00 40.48  ? 598  LEU   A N    1 
ATOM   4604 C  CA   . LEU   A 1 619 ? 406.290 0.906   105.097 1.00 40.18  ? 598  LEU   A CA   1 
ATOM   4605 C  C    . LEU   A 1 619 ? 406.879 -0.285  105.837 1.00 40.90  ? 598  LEU   A C    1 
ATOM   4606 O  O    . LEU   A 1 619 ? 407.826 -0.131  106.615 1.00 39.67  ? 598  LEU   A O    1 
ATOM   4607 C  CB   . LEU   A 1 619 ? 407.272 1.404   104.035 1.00 37.03  ? 598  LEU   A CB   1 
ATOM   4608 C  CG   . LEU   A 1 619 ? 406.916 2.729   103.361 1.00 34.93  ? 598  LEU   A CG   1 
ATOM   4609 C  CD1  . LEU   A 1 619 ? 408.047 3.176   102.455 1.00 33.25  ? 598  LEU   A CD1  1 
ATOM   4610 C  CD2  . LEU   A 1 619 ? 405.623 2.599   102.579 1.00 32.16  ? 598  LEU   A CD2  1 
ATOM   4611 N  N    . GLY   A 1 620 ? 406.306 -1.463  105.608 1.00 39.30  ? 599  GLY   A N    1 
ATOM   4612 C  CA   . GLY   A 1 620 ? 406.875 -2.693  106.120 1.00 39.48  ? 599  GLY   A CA   1 
ATOM   4613 C  C    . GLY   A 1 620 ? 407.641 -3.379  105.011 1.00 39.73  ? 599  GLY   A C    1 
ATOM   4614 O  O    . GLY   A 1 620 ? 407.038 -3.953  104.100 1.00 42.09  ? 599  GLY   A O    1 
ATOM   4615 N  N    . ILE   A 1 621 ? 408.962 -3.312  105.062 1.00 33.21  ? 600  ILE   A N    1 
ATOM   4616 C  CA   . ILE   A 1 621 ? 409.823 -3.683  103.941 1.00 41.89  ? 600  ILE   A CA   1 
ATOM   4617 C  C    . ILE   A 1 621 ? 410.477 -5.020  104.260 1.00 36.92  ? 600  ILE   A C    1 
ATOM   4618 O  O    . ILE   A 1 621 ? 411.075 -5.163  105.332 1.00 38.40  ? 600  ILE   A O    1 
ATOM   4619 C  CB   . ILE   A 1 621 ? 410.891 -2.608  103.661 1.00 40.85  ? 600  ILE   A CB   1 
ATOM   4620 C  CG1  . ILE   A 1 621 ? 410.228 -1.245  103.447 1.00 33.29  ? 600  ILE   A CG1  1 
ATOM   4621 C  CG2  . ILE   A 1 621 ? 411.740 -2.997  102.458 1.00 33.54  ? 600  ILE   A CG2  1 
ATOM   4622 C  CD1  . ILE   A 1 621 ? 411.211 -0.126  103.197 1.00 37.09  ? 600  ILE   A CD1  1 
ATOM   4623 N  N    . PRO   A 1 622 ? 410.392 -6.010  103.373 1.00 36.39  ? 601  PRO   A N    1 
ATOM   4624 C  CA   . PRO   A 1 622 ? 411.081 -7.281  103.617 1.00 39.39  ? 601  PRO   A CA   1 
ATOM   4625 C  C    . PRO   A 1 622 ? 412.545 -7.051  103.957 1.00 38.46  ? 601  PRO   A C    1 
ATOM   4626 O  O    . PRO   A 1 622 ? 413.257 -6.325  103.259 1.00 39.22  ? 601  PRO   A O    1 
ATOM   4627 C  CB   . PRO   A 1 622 ? 410.918 -8.030  102.290 1.00 37.24  ? 601  PRO   A CB   1 
ATOM   4628 C  CG   . PRO   A 1 622 ? 409.681 -7.461  101.692 1.00 35.31  ? 601  PRO   A CG   1 
ATOM   4629 C  CD   . PRO   A 1 622 ? 409.657 -6.012  102.097 1.00 36.45  ? 601  PRO   A CD   1 
ATOM   4630 N  N    . LYS   A 1 623 ? 412.990 -7.670  105.040 1.00 43.65  ? 602  LYS   A N    1 
ATOM   4631 C  CA   . LYS   A 1 623 ? 414.366 -7.507  105.496 1.00 46.55  ? 602  LYS   A CA   1 
ATOM   4632 C  C    . LYS   A 1 623 ? 415.319 -8.168  104.509 1.00 45.24  ? 602  LYS   A C    1 
ATOM   4633 O  O    . LYS   A 1 623 ? 415.210 -9.378  104.270 1.00 45.65  ? 602  LYS   A O    1 
ATOM   4634 C  CB   . LYS   A 1 623 ? 414.532 -8.101  106.891 1.00 49.13  ? 602  LYS   A CB   1 
ATOM   4635 C  CG   . LYS   A 1 623 ? 415.828 -7.715  107.586 1.00 49.96  ? 602  LYS   A CG   1 
ATOM   4636 C  CD   . LYS   A 1 623 ? 415.938 -8.371  108.956 1.00 51.49  ? 602  LYS   A CD   1 
ATOM   4637 C  CE   . LYS   A 1 623 ? 417.102 -7.801  109.752 1.00 62.06  ? 602  LYS   A CE   1 
ATOM   4638 N  NZ   . LYS   A 1 623 ? 416.904 -6.357  110.064 1.00 61.32  ? 602  LYS   A NZ   1 
ATOM   4639 N  N    . PRO   A 1 624 ? 416.269 -7.430  103.929 1.00 44.89  ? 603  PRO   A N    1 
ATOM   4640 C  CA   . PRO   A 1 624 ? 417.083 -7.981  102.836 1.00 46.60  ? 603  PRO   A CA   1 
ATOM   4641 C  C    . PRO   A 1 624 ? 418.147 -8.963  103.297 1.00 50.20  ? 603  PRO   A C    1 
ATOM   4642 O  O    . PRO   A 1 624 ? 418.528 -9.873  102.551 1.00 48.71  ? 603  PRO   A O    1 
ATOM   4643 C  CB   . PRO   A 1 624 ? 417.728 -6.729  102.236 1.00 47.55  ? 603  PRO   A CB   1 
ATOM   4644 C  CG   . PRO   A 1 624 ? 417.896 -5.830  103.426 1.00 44.45  ? 603  PRO   A CG   1 
ATOM   4645 C  CD   . PRO   A 1 624 ? 416.654 -6.046  104.258 1.00 43.23  ? 603  PRO   A CD   1 
ATOM   4646 N  N    . PHE   A 1 625 ? 418.651 -8.778  104.516 1.00 50.72  ? 604  PHE   A N    1 
ATOM   4647 C  CA   . PHE   A 1 625 ? 419.783 -9.557  105.008 1.00 52.17  ? 604  PHE   A CA   1 
ATOM   4648 C  C    . PHE   A 1 625 ? 421.012 -9.331  104.129 1.00 55.51  ? 604  PHE   A C    1 
ATOM   4649 O  O    . PHE   A 1 625 ? 421.674 -10.272 103.687 1.00 55.03  ? 604  PHE   A O    1 
ATOM   4650 C  CB   . PHE   A 1 625 ? 419.433 -11.043 105.093 1.00 57.37  ? 604  PHE   A CB   1 
ATOM   4651 C  CG   . PHE   A 1 625 ? 418.502 -11.377 106.215 1.00 56.93  ? 604  PHE   A CG   1 
ATOM   4652 C  CD1  . PHE   A 1 625 ? 418.984 -11.540 107.502 1.00 57.04  ? 604  PHE   A CD1  1 
ATOM   4653 C  CD2  . PHE   A 1 625 ? 417.144 -11.525 105.988 1.00 54.77  ? 604  PHE   A CD2  1 
ATOM   4654 C  CE1  . PHE   A 1 625 ? 418.132 -11.847 108.543 1.00 60.90  ? 604  PHE   A CE1  1 
ATOM   4655 C  CE2  . PHE   A 1 625 ? 416.285 -11.832 107.025 1.00 58.11  ? 604  PHE   A CE2  1 
ATOM   4656 C  CZ   . PHE   A 1 625 ? 416.780 -11.994 108.304 1.00 61.80  ? 604  PHE   A CZ   1 
ATOM   4657 N  N    . GLY   A 1 626 ? 421.313 -8.057  103.876 1.00 55.07  ? 605  GLY   A N    1 
ATOM   4658 C  CA   . GLY   A 1 626 ? 422.441 -7.698  103.052 1.00 54.60  ? 605  GLY   A CA   1 
ATOM   4659 C  C    . GLY   A 1 626 ? 423.732 -7.642  103.839 1.00 61.29  ? 605  GLY   A C    1 
ATOM   4660 O  O    . GLY   A 1 626 ? 423.787 -7.924  105.044 1.00 60.93  ? 605  GLY   A O    1 
ATOM   4661 N  N    . PRO   A 1 627 ? 424.809 -7.277  103.145 1.00 65.49  ? 606  PRO   A N    1 
ATOM   4662 C  CA   . PRO   A 1 627 ? 426.106 -7.142  103.820 1.00 61.76  ? 606  PRO   A CA   1 
ATOM   4663 C  C    . PRO   A 1 627 ? 426.029 -6.109  104.934 1.00 62.38  ? 606  PRO   A C    1 
ATOM   4664 O  O    . PRO   A 1 627 ? 425.487 -5.016  104.755 1.00 59.16  ? 606  PRO   A O    1 
ATOM   4665 C  CB   . PRO   A 1 627 ? 427.049 -6.699  102.694 1.00 55.96  ? 606  PRO   A CB   1 
ATOM   4666 C  CG   . PRO   A 1 627 ? 426.367 -7.115  101.428 1.00 51.32  ? 606  PRO   A CG   1 
ATOM   4667 C  CD   . PRO   A 1 627 ? 424.898 -6.991  101.704 1.00 55.70  ? 606  PRO   A CD   1 
ATOM   4668 N  N    . GLN   A 1 628 ? 426.575 -6.465  106.094 1.00 67.41  ? 607  GLN   A N    1 
ATOM   4669 C  CA   . GLN   A 1 628 ? 426.531 -5.603  107.267 1.00 70.25  ? 607  GLN   A CA   1 
ATOM   4670 C  C    . GLN   A 1 628 ? 427.768 -4.714  107.307 1.00 67.01  ? 607  GLN   A C    1 
ATOM   4671 O  O    . GLN   A 1 628 ? 428.898 -5.212  107.372 1.00 63.45  ? 607  GLN   A O    1 
ATOM   4672 C  CB   . GLN   A 1 628 ? 426.422 -6.430  108.547 1.00 71.40  ? 607  GLN   A CB   1 
ATOM   4673 C  CG   . GLN   A 1 628 ? 425.001 -6.843  108.891 1.00 75.18  ? 607  GLN   A CG   1 
ATOM   4674 C  CD   . GLN   A 1 628 ? 424.766 -6.920  110.386 1.00 75.47  ? 607  GLN   A CD   1 
ATOM   4675 O  OE1  . GLN   A 1 628 ? 425.710 -6.912  111.176 1.00 86.64  ? 607  GLN   A OE1  1 
ATOM   4676 N  NE2  . GLN   A 1 628 ? 423.500 -6.986  110.782 1.00 81.32  ? 607  GLN   A NE2  1 
ATOM   4677 N  N    . VAL   A 1 629 ? 427.548 -3.403  107.272 1.00 72.77  ? 608  VAL   A N    1 
ATOM   4678 C  CA   . VAL   A 1 629 ? 428.607 -2.406  107.371 1.00 73.15  ? 608  VAL   A CA   1 
ATOM   4679 C  C    . VAL   A 1 629 ? 428.364 -1.625  108.655 1.00 79.87  ? 608  VAL   A C    1 
ATOM   4680 O  O    . VAL   A 1 629 ? 427.398 -0.857  108.748 1.00 77.33  ? 608  VAL   A O    1 
ATOM   4681 C  CB   . VAL   A 1 629 ? 428.637 -1.469  106.156 1.00 73.35  ? 608  VAL   A CB   1 
ATOM   4682 C  CG1  . VAL   A 1 629 ? 430.009 -0.827  106.015 1.00 70.04  ? 608  VAL   A CG1  1 
ATOM   4683 C  CG2  . VAL   A 1 629 ? 428.237 -2.215  104.887 1.00 68.96  ? 608  VAL   A CG2  1 
ATOM   4684 N  N    . GLU   A 1 630 ? 429.233 -1.820  109.647 1.00 82.47  ? 609  GLU   A N    1 
ATOM   4685 C  CA   . GLU   A 1 630 ? 429.085 -1.180  110.954 1.00 87.26  ? 609  GLU   A CA   1 
ATOM   4686 C  C    . GLU   A 1 630 ? 427.825 -1.675  111.667 1.00 87.09  ? 609  GLU   A C    1 
ATOM   4687 O  O    . GLU   A 1 630 ? 427.001 -0.893  112.145 1.00 87.41  ? 609  GLU   A O    1 
ATOM   4688 C  CB   . GLU   A 1 630 ? 429.083 0.346   110.824 1.00 91.11  ? 609  GLU   A CB   1 
ATOM   4689 C  CG   . GLU   A 1 630 ? 430.455 0.955   110.561 1.00 98.37  ? 609  GLU   A CG   1 
ATOM   4690 C  CD   . GLU   A 1 630 ? 431.444 0.696   111.688 1.00 110.21 ? 609  GLU   A CD   1 
ATOM   4691 O  OE1  . GLU   A 1 630 ? 431.505 -0.446  112.188 1.00 107.33 ? 609  GLU   A OE1  1 
ATOM   4692 O  OE2  . GLU   A 1 630 ? 432.160 1.640   112.080 1.00 114.59 ? 609  GLU   A OE2  1 
ATOM   4693 N  N    . GLU   A 1 631 ? 427.685 -3.001  111.734 1.00 83.09  ? 610  GLU   A N    1 
ATOM   4694 C  CA   . GLU   A 1 631 ? 426.562 -3.650  112.413 1.00 80.67  ? 610  GLU   A CA   1 
ATOM   4695 C  C    . GLU   A 1 631 ? 425.214 -3.172  111.879 1.00 76.56  ? 610  GLU   A C    1 
ATOM   4696 O  O    . GLU   A 1 631 ? 424.216 -3.160  112.605 1.00 74.35  ? 610  GLU   A O    1 
ATOM   4697 C  CB   . GLU   A 1 631 ? 426.636 -3.448  113.931 1.00 88.89  ? 610  GLU   A CB   1 
ATOM   4698 C  CG   . GLU   A 1 631 ? 427.810 -4.152  114.603 1.00 93.85  ? 610  GLU   A CG   1 
ATOM   4699 C  CD   . GLU   A 1 631 ? 429.114 -3.389  114.464 1.00 105.51 ? 610  GLU   A CD   1 
ATOM   4700 O  OE1  . GLU   A 1 631 ? 429.121 -2.169  114.730 1.00 107.98 ? 610  GLU   A OE1  1 
ATOM   4701 O  OE2  . GLU   A 1 631 ? 430.132 -4.009  114.088 1.00 106.89 ? 610  GLU   A OE2  1 
ATOM   4702 N  N    . GLU   A 1 632 ? 425.171 -2.779  110.608 1.00 73.63  ? 611  GLU   A N    1 
ATOM   4703 C  CA   . GLU   A 1 632 ? 423.942 -2.324  109.970 1.00 71.53  ? 611  GLU   A CA   1 
ATOM   4704 C  C    . GLU   A 1 632 ? 423.926 -2.800  108.527 1.00 68.26  ? 611  GLU   A C    1 
ATOM   4705 O  O    . GLU   A 1 632 ? 424.917 -2.646  107.807 1.00 60.56  ? 611  GLU   A O    1 
ATOM   4706 C  CB   . GLU   A 1 632 ? 423.813 -0.795  110.019 1.00 71.76  ? 611  GLU   A CB   1 
ATOM   4707 C  CG   . GLU   A 1 632 ? 423.625 -0.210  111.415 1.00 79.77  ? 611  GLU   A CG   1 
ATOM   4708 C  CD   . GLU   A 1 632 ? 422.254 -0.497  112.003 1.00 75.71  ? 611  GLU   A CD   1 
ATOM   4709 O  OE1  . GLU   A 1 632 ? 421.471 -1.238  111.371 1.00 68.95  ? 611  GLU   A OE1  1 
ATOM   4710 O  OE2  . GLU   A 1 632 ? 421.958 0.024   113.100 1.00 74.50  ? 611  GLU   A OE2  1 
ATOM   4711 N  N    . CYS   A 1 633 ? 422.804 -3.378  108.110 1.00 57.04  ? 612  CYS   A N    1 
ATOM   4712 C  CA   . CYS   A 1 633 ? 422.662 -3.819  106.731 1.00 58.79  ? 612  CYS   A CA   1 
ATOM   4713 C  C    . CYS   A 1 633 ? 422.806 -2.633  105.784 1.00 52.09  ? 612  CYS   A C    1 
ATOM   4714 O  O    . CYS   A 1 633 ? 422.116 -1.621  105.931 1.00 48.63  ? 612  CYS   A O    1 
ATOM   4715 C  CB   . CYS   A 1 633 ? 421.305 -4.495  106.544 1.00 56.50  ? 612  CYS   A CB   1 
ATOM   4716 S  SG   . CYS   A 1 633 ? 420.928 -4.977  104.850 1.00 47.48  ? 612  CYS   A SG   1 
ATOM   4717 N  N    . CYS   A 1 634 ? 423.717 -2.752  104.812 1.00 54.06  ? 613  CYS   A N    1 
ATOM   4718 C  CA   . CYS   A 1 634 ? 423.931 -1.640  103.892 1.00 54.92  ? 613  CYS   A CA   1 
ATOM   4719 C  C    . CYS   A 1 634 ? 422.798 -1.505  102.884 1.00 48.02  ? 613  CYS   A C    1 
ATOM   4720 O  O    . CYS   A 1 634 ? 422.589 -0.412  102.347 1.00 47.25  ? 613  CYS   A O    1 
ATOM   4721 C  CB   . CYS   A 1 634 ? 425.279 -1.786  103.180 1.00 57.64  ? 613  CYS   A CB   1 
ATOM   4722 S  SG   . CYS   A 1 634 ? 425.367 -3.054  101.898 1.00 56.64  ? 613  CYS   A SG   1 
ATOM   4723 N  N    . LEU   A 1 635 ? 422.050 -2.580  102.627 1.00 42.81  ? 614  LEU   A N    1 
ATOM   4724 C  CA   . LEU   A 1 635 ? 420.830 -2.449  101.840 1.00 42.41  ? 614  LEU   A CA   1 
ATOM   4725 C  C    . LEU   A 1 635 ? 419.749 -1.716  102.627 1.00 44.48  ? 614  LEU   A C    1 
ATOM   4726 O  O    . LEU   A 1 635 ? 419.020 -0.887  102.068 1.00 42.39  ? 614  LEU   A O    1 
ATOM   4727 C  CB   . LEU   A 1 635 ? 420.341 -3.830  101.400 1.00 44.23  ? 614  LEU   A CB   1 
ATOM   4728 C  CG   . LEU   A 1 635 ? 421.268 -4.617  100.468 1.00 45.38  ? 614  LEU   A CG   1 
ATOM   4729 C  CD1  . LEU   A 1 635 ? 420.844 -6.076  100.389 1.00 43.83  ? 614  LEU   A CD1  1 
ATOM   4730 C  CD2  . LEU   A 1 635 ? 421.298 -3.990  99.081  1.00 39.09  ? 614  LEU   A CD2  1 
ATOM   4731 N  N    . GLU   A 1 636 ? 419.637 -2.001  103.928 1.00 44.58  ? 615  GLU   A N    1 
ATOM   4732 C  CA   . GLU   A 1 636 ? 418.660 -1.307  104.764 1.00 39.93  ? 615  GLU   A CA   1 
ATOM   4733 C  C    . GLU   A 1 636 ? 418.959 0.185   104.829 1.00 42.01  ? 615  GLU   A C    1 
ATOM   4734 O  O    . GLU   A 1 636 ? 418.068 1.020   104.633 1.00 39.20  ? 615  GLU   A O    1 
ATOM   4735 C  CB   . GLU   A 1 636 ? 418.644 -1.907  106.173 1.00 42.08  ? 615  GLU   A CB   1 
ATOM   4736 C  CG   . GLU   A 1 636 ? 417.724 -3.107  106.348 1.00 44.86  ? 615  GLU   A CG   1 
ATOM   4737 C  CD   . GLU   A 1 636 ? 417.667 -3.608  107.785 1.00 51.56  ? 615  GLU   A CD   1 
ATOM   4738 O  OE1  . GLU   A 1 636 ? 418.036 -2.849  108.708 1.00 48.48  ? 615  GLU   A OE1  1 
ATOM   4739 O  OE2  . GLU   A 1 636 ? 417.252 -4.767  107.991 1.00 50.70  ? 615  GLU   A OE2  1 
ATOM   4740 N  N    . MET   A 1 637 ? 420.214 0.538   105.120 1.00 37.76  ? 616  MET   A N    1 
ATOM   4741 C  CA   . MET   A 1 637 ? 420.582 1.946   105.201 1.00 45.82  ? 616  MET   A CA   1 
ATOM   4742 C  C    . MET   A 1 637 ? 420.389 2.651   103.867 1.00 44.48  ? 616  MET   A C    1 
ATOM   4743 O  O    . MET   A 1 637 ? 420.033 3.835   103.837 1.00 49.01  ? 616  MET   A O    1 
ATOM   4744 C  CB   . MET   A 1 637 ? 422.031 2.090   105.672 1.00 49.40  ? 616  MET   A CB   1 
ATOM   4745 C  CG   . MET   A 1 637 ? 422.298 1.564   107.077 1.00 62.20  ? 616  MET   A CG   1 
ATOM   4746 S  SD   . MET   A 1 637 ? 421.226 2.274   108.346 1.00 61.01  ? 616  MET   A SD   1 
ATOM   4747 C  CE   . MET   A 1 637 ? 419.991 0.988   108.521 1.00 59.18  ? 616  MET   A CE   1 
ATOM   4748 N  N    . HIS   A 1 638 ? 420.615 1.947   102.756 1.00 41.96  ? 617  HIS   A N    1 
ATOM   4749 C  CA   . HIS   A 1 638 ? 420.425 2.561   101.447 1.00 40.91  ? 617  HIS   A CA   1 
ATOM   4750 C  C    . HIS   A 1 638 ? 418.949 2.826   101.178 1.00 40.08  ? 617  HIS   A C    1 
ATOM   4751 O  O    . HIS   A 1 638 ? 418.574 3.922   100.746 1.00 40.31  ? 617  HIS   A O    1 
ATOM   4752 C  CB   . HIS   A 1 638 ? 421.024 1.670   100.359 1.00 40.99  ? 617  HIS   A CB   1 
ATOM   4753 C  CG   . HIS   A 1 638 ? 420.898 2.235   98.978  1.00 43.36  ? 617  HIS   A CG   1 
ATOM   4754 N  ND1  . HIS   A 1 638 ? 421.796 3.144   98.459  1.00 42.90  ? 617  HIS   A ND1  1 
ATOM   4755 C  CD2  . HIS   A 1 638 ? 419.979 2.018   98.008  1.00 43.92  ? 617  HIS   A CD2  1 
ATOM   4756 C  CE1  . HIS   A 1 638 ? 421.435 3.461   97.228  1.00 44.02  ? 617  HIS   A CE1  1 
ATOM   4757 N  NE2  . HIS   A 1 638 ? 420.335 2.793   96.931  1.00 43.15  ? 617  HIS   A NE2  1 
ATOM   4758 N  N    . VAL   A 1 639 ? 418.095 1.833   101.431 1.00 37.49  ? 618  VAL   A N    1 
ATOM   4759 C  CA   . VAL   A 1 639 ? 416.660 2.024   101.239 1.00 37.29  ? 618  VAL   A CA   1 
ATOM   4760 C  C    . VAL   A 1 639 ? 416.149 3.147   102.133 1.00 42.76  ? 618  VAL   A C    1 
ATOM   4761 O  O    . VAL   A 1 639 ? 415.316 3.961   101.716 1.00 38.67  ? 618  VAL   A O    1 
ATOM   4762 C  CB   . VAL   A 1 639 ? 415.908 0.702   101.486 1.00 33.66  ? 618  VAL   A CB   1 
ATOM   4763 C  CG1  . VAL   A 1 639 ? 414.405 0.935   101.518 1.00 29.63  ? 618  VAL   A CG1  1 
ATOM   4764 C  CG2  . VAL   A 1 639 ? 416.267 -0.311  100.410 1.00 33.64  ? 618  VAL   A CG2  1 
ATOM   4765 N  N    . ARG   A 1 640 ? 416.643 3.218   103.373 1.00 39.42  ? 619  ARG   A N    1 
ATOM   4766 C  CA   . ARG   A 1 640 ? 416.247 4.315   104.250 1.00 39.59  ? 619  ARG   A CA   1 
ATOM   4767 C  C    . ARG   A 1 640 ? 416.676 5.658   103.672 1.00 39.04  ? 619  ARG   A C    1 
ATOM   4768 O  O    . ARG   A 1 640 ? 415.915 6.633   103.714 1.00 40.40  ? 619  ARG   A O    1 
ATOM   4769 C  CB   . ARG   A 1 640 ? 416.837 4.125   105.648 1.00 43.07  ? 619  ARG   A CB   1 
ATOM   4770 C  CG   . ARG   A 1 640 ? 416.206 3.006   106.466 1.00 46.39  ? 619  ARG   A CG   1 
ATOM   4771 C  CD   . ARG   A 1 640 ? 416.540 3.173   107.946 1.00 50.95  ? 619  ARG   A CD   1 
ATOM   4772 N  NE   . ARG   A 1 640 ? 416.135 2.028   108.754 1.00 56.54  ? 619  ARG   A NE   1 
ATOM   4773 C  CZ   . ARG   A 1 640 ? 414.940 1.880   109.309 1.00 54.85  ? 619  ARG   A CZ   1 
ATOM   4774 N  NH1  . ARG   A 1 640 ? 413.982 2.777   109.141 1.00 51.69  ? 619  ARG   A NH1  1 
ATOM   4775 N  NH2  . ARG   A 1 640 ? 414.698 0.802   110.051 1.00 54.15  ? 619  ARG   A NH2  1 
ATOM   4776 N  N    . GLY   A 1 641 ? 417.894 5.730   103.131 1.00 41.48  ? 620  GLY   A N    1 
ATOM   4777 C  CA   . GLY   A 1 641 ? 418.349 6.968   102.523 1.00 40.96  ? 620  GLY   A CA   1 
ATOM   4778 C  C    . GLY   A 1 641 ? 417.513 7.387   101.330 1.00 39.26  ? 620  GLY   A C    1 
ATOM   4779 O  O    . GLY   A 1 641 ? 417.413 8.578   101.025 1.00 46.50  ? 620  GLY   A O    1 
ATOM   4780 N  N    . LEU   A 1 642 ? 416.901 6.422   100.642 1.00 36.13  ? 621  LEU   A N    1 
ATOM   4781 C  CA   . LEU   A 1 642 ? 416.072 6.749   99.488  1.00 36.46  ? 621  LEU   A CA   1 
ATOM   4782 C  C    . LEU   A 1 642 ? 414.674 7.196   99.899  1.00 42.87  ? 621  LEU   A C    1 
ATOM   4783 O  O    . LEU   A 1 642 ? 414.109 8.111   99.291  1.00 38.52  ? 621  LEU   A O    1 
ATOM   4784 C  CB   . LEU   A 1 642 ? 415.974 5.545   98.551  1.00 40.34  ? 621  LEU   A CB   1 
ATOM   4785 C  CG   . LEU   A 1 642 ? 417.245 5.070   97.855  1.00 38.51  ? 621  LEU   A CG   1 
ATOM   4786 C  CD1  . LEU   A 1 642 ? 416.987 3.730   97.191  1.00 37.58  ? 621  LEU   A CD1  1 
ATOM   4787 C  CD2  . LEU   A 1 642 ? 417.709 6.094   96.834  1.00 38.40  ? 621  LEU   A CD2  1 
ATOM   4788 N  N    . LEU   A 1 643 ? 414.100 6.568   100.923 1.00 42.75  ? 622  LEU   A N    1 
ATOM   4789 C  CA   . LEU   A 1 643 ? 412.691 6.763   101.239 1.00 42.26  ? 622  LEU   A CA   1 
ATOM   4790 C  C    . LEU   A 1 643 ? 412.441 7.719   102.395 1.00 38.86  ? 622  LEU   A C    1 
ATOM   4791 O  O    . LEU   A 1 643 ? 411.449 8.454   102.367 1.00 41.94  ? 622  LEU   A O    1 
ATOM   4792 C  CB   . LEU   A 1 643 ? 412.036 5.415   101.556 1.00 37.26  ? 622  LEU   A CB   1 
ATOM   4793 C  CG   . LEU   A 1 643 ? 412.095 4.425   100.395 1.00 37.55  ? 622  LEU   A CG   1 
ATOM   4794 C  CD1  . LEU   A 1 643 ? 411.462 3.103   100.781 1.00 41.69  ? 622  LEU   A CD1  1 
ATOM   4795 C  CD2  . LEU   A 1 643 ? 411.410 5.016   99.175  1.00 37.23  ? 622  LEU   A CD2  1 
ATOM   4796 N  N    . GLU   A 1 644 ? 413.303 7.737   103.404 1.00 41.23  ? 623  GLU   A N    1 
ATOM   4797 C  CA   . GLU   A 1 644 ? 413.016 8.503   104.610 1.00 42.92  ? 623  GLU   A CA   1 
ATOM   4798 C  C    . GLU   A 1 644 ? 412.995 10.008  104.357 1.00 48.11  ? 623  GLU   A C    1 
ATOM   4799 O  O    . GLU   A 1 644 ? 412.163 10.713  104.942 1.00 50.15  ? 623  GLU   A O    1 
ATOM   4800 C  CB   . GLU   A 1 644 ? 414.023 8.155   105.706 1.00 42.39  ? 623  GLU   A CB   1 
ATOM   4801 C  CG   . GLU   A 1 644 ? 413.900 6.715   106.167 1.00 48.04  ? 623  GLU   A CG   1 
ATOM   4802 C  CD   . GLU   A 1 644 ? 414.660 6.430   107.443 1.00 54.16  ? 623  GLU   A CD   1 
ATOM   4803 O  OE1  . GLU   A 1 644 ? 415.731 7.037   107.661 1.00 53.93  ? 623  GLU   A OE1  1 
ATOM   4804 O  OE2  . GLU   A 1 644 ? 414.176 5.593   108.235 1.00 57.27  ? 623  GLU   A OE2  1 
ATOM   4805 N  N    . PRO   A 1 645 ? 413.878 10.547  103.512 1.00 43.80  ? 624  PRO   A N    1 
ATOM   4806 C  CA   . PRO   A 1 645 ? 413.813 11.991  103.236 1.00 44.57  ? 624  PRO   A CA   1 
ATOM   4807 C  C    . PRO   A 1 645 ? 412.463 12.440  102.706 1.00 45.33  ? 624  PRO   A C    1 
ATOM   4808 O  O    . PRO   A 1 645 ? 412.154 13.637  102.770 1.00 47.60  ? 624  PRO   A O    1 
ATOM   4809 C  CB   . PRO   A 1 645 ? 414.928 12.198  102.203 1.00 46.38  ? 624  PRO   A CB   1 
ATOM   4810 C  CG   . PRO   A 1 645 ? 415.899 11.096  102.498 1.00 44.83  ? 624  PRO   A CG   1 
ATOM   4811 C  CD   . PRO   A 1 645 ? 415.032 9.920   102.844 1.00 41.08  ? 624  PRO   A CD   1 
ATOM   4812 N  N    . LEU   A 1 646 ? 411.643 11.520  102.206 1.00 44.28  ? 625  LEU   A N    1 
ATOM   4813 C  CA   . LEU   A 1 646 ? 410.321 11.835  101.687 1.00 40.53  ? 625  LEU   A CA   1 
ATOM   4814 C  C    . LEU   A 1 646 ? 409.230 11.741  102.745 1.00 40.29  ? 625  LEU   A C    1 
ATOM   4815 O  O    . LEU   A 1 646 ? 408.045 11.796  102.402 1.00 52.12  ? 625  LEU   A O    1 
ATOM   4816 C  CB   . LEU   A 1 646 ? 409.985 10.903  100.523 1.00 46.91  ? 625  LEU   A CB   1 
ATOM   4817 C  CG   . LEU   A 1 646 ? 410.939 10.977  99.335  1.00 45.83  ? 625  LEU   A CG   1 
ATOM   4818 C  CD1  . LEU   A 1 646 ? 410.678 9.832   98.378  1.00 44.99  ? 625  LEU   A CD1  1 
ATOM   4819 C  CD2  . LEU   A 1 646 ? 410.773 12.315  98.641  1.00 48.65  ? 625  LEU   A CD2  1 
ATOM   4820 N  N    . GLY   A 1 647 ? 409.596 11.598  104.015 1.00 42.06  ? 626  GLY   A N    1 
ATOM   4821 C  CA   . GLY   A 1 647 ? 408.612 11.407  105.059 1.00 46.17  ? 626  GLY   A CA   1 
ATOM   4822 C  C    . GLY   A 1 647 ? 408.113 9.990   105.211 1.00 44.95  ? 626  GLY   A C    1 
ATOM   4823 O  O    . GLY   A 1 647 ? 407.175 9.759   105.982 1.00 49.22  ? 626  GLY   A O    1 
ATOM   4824 N  N    . LEU   A 1 648 ? 408.700 9.034   104.500 1.00 46.00  ? 627  LEU   A N    1 
ATOM   4825 C  CA   . LEU   A 1 648 ? 408.321 7.637   104.632 1.00 45.49  ? 627  LEU   A CA   1 
ATOM   4826 C  C    . LEU   A 1 648 ? 409.120 6.995   105.758 1.00 48.81  ? 627  LEU   A C    1 
ATOM   4827 O  O    . LEU   A 1 648 ? 410.328 7.216   105.883 1.00 49.70  ? 627  LEU   A O    1 
ATOM   4828 C  CB   . LEU   A 1 648 ? 408.554 6.892   103.316 1.00 39.95  ? 627  LEU   A CB   1 
ATOM   4829 C  CG   . LEU   A 1 648 ? 407.688 7.344   102.136 1.00 38.08  ? 627  LEU   A CG   1 
ATOM   4830 C  CD1  . LEU   A 1 648 ? 408.283 6.860   100.826 1.00 41.93  ? 627  LEU   A CD1  1 
ATOM   4831 C  CD2  . LEU   A 1 648 ? 406.264 6.835   102.297 1.00 34.32  ? 627  LEU   A CD2  1 
ATOM   4832 N  N    . GLU   A 1 649 ? 408.437 6.213   106.588 1.00 47.53  ? 628  GLU   A N    1 
ATOM   4833 C  CA   . GLU   A 1 649 ? 409.052 5.549   107.730 1.00 47.84  ? 628  GLU   A CA   1 
ATOM   4834 C  C    . GLU   A 1 649 ? 409.188 4.065   107.418 1.00 42.52  ? 628  GLU   A C    1 
ATOM   4835 O  O    . GLU   A 1 649 ? 408.198 3.401   107.092 1.00 43.13  ? 628  GLU   A O    1 
ATOM   4836 C  CB   . GLU   A 1 649 ? 408.234 5.779   109.001 1.00 49.72  ? 628  GLU   A CB   1 
ATOM   4837 C  CG   . GLU   A 1 649 ? 408.045 7.257   109.333 1.00 57.86  ? 628  GLU   A CG   1 
ATOM   4838 C  CD   . GLU   A 1 649 ? 407.389 7.496   110.682 1.00 75.09  ? 628  GLU   A CD   1 
ATOM   4839 O  OE1  . GLU   A 1 649 ? 407.084 6.512   111.389 1.00 78.11  ? 628  GLU   A OE1  1 
ATOM   4840 O  OE2  . GLU   A 1 649 ? 407.182 8.676   111.037 1.00 77.74  ? 628  GLU   A OE2  1 
ATOM   4841 N  N    . CYS   A 1 650 ? 410.411 3.553   107.519 1.00 42.30  ? 629  CYS   A N    1 
ATOM   4842 C  CA   . CYS   A 1 650 ? 410.744 2.207   107.075 1.00 41.93  ? 629  CYS   A CA   1 
ATOM   4843 C  C    . CYS   A 1 650 ? 410.855 1.275   108.275 1.00 43.90  ? 629  CYS   A C    1 
ATOM   4844 O  O    . CYS   A 1 650 ? 411.627 1.536   109.202 1.00 43.58  ? 629  CYS   A O    1 
ATOM   4845 C  CB   . CYS   A 1 650 ? 412.051 2.214   106.282 1.00 44.86  ? 629  CYS   A CB   1 
ATOM   4846 S  SG   . CYS   A 1 650 ? 412.010 3.252   104.803 1.00 49.87  ? 629  CYS   A SG   1 
ATOM   4847 N  N    . THR   A 1 651 ? 410.079 0.197   108.256 1.00 44.92  ? 630  THR   A N    1 
ATOM   4848 C  CA   . THR   A 1 651 ? 410.236 -0.908  109.190 1.00 45.73  ? 630  THR   A CA   1 
ATOM   4849 C  C    . THR   A 1 651 ? 410.543 -2.156  108.379 1.00 42.32  ? 630  THR   A C    1 
ATOM   4850 O  O    . THR   A 1 651 ? 409.801 -2.494  107.454 1.00 44.24  ? 630  THR   A O    1 
ATOM   4851 C  CB   . THR   A 1 651 ? 408.980 -1.124  110.043 1.00 47.23  ? 630  THR   A CB   1 
ATOM   4852 O  OG1  . THR   A 1 651 ? 408.670 0.076   110.761 1.00 51.62  ? 630  THR   A OG1  1 
ATOM   4853 C  CG2  . THR   A 1 651 ? 409.202 -2.251  111.039 1.00 41.98  ? 630  THR   A CG2  1 
ATOM   4854 N  N    . PHE   A 1 652 ? 411.645 -2.817  108.699 1.00 40.78  ? 631  PHE   A N    1 
ATOM   4855 C  CA   . PHE   A 1 652 ? 412.085 -3.985  107.950 1.00 43.08  ? 631  PHE   A CA   1 
ATOM   4856 C  C    . PHE   A 1 652 ? 411.564 -5.235  108.644 1.00 40.90  ? 631  PHE   A C    1 
ATOM   4857 O  O    . PHE   A 1 652 ? 411.862 -5.468  109.820 1.00 50.58  ? 631  PHE   A O    1 
ATOM   4858 C  CB   . PHE   A 1 652 ? 413.606 -4.003  107.813 1.00 40.80  ? 631  PHE   A CB   1 
ATOM   4859 C  CG   . PHE   A 1 652 ? 414.132 -2.896  106.946 1.00 39.83  ? 631  PHE   A CG   1 
ATOM   4860 C  CD1  . PHE   A 1 652 ? 414.093 -3.005  105.567 1.00 37.87  ? 631  PHE   A CD1  1 
ATOM   4861 C  CD2  . PHE   A 1 652 ? 414.638 -1.736  107.508 1.00 41.05  ? 631  PHE   A CD2  1 
ATOM   4862 C  CE1  . PHE   A 1 652 ? 414.563 -1.987  104.764 1.00 36.84  ? 631  PHE   A CE1  1 
ATOM   4863 C  CE2  . PHE   A 1 652 ? 415.110 -0.715  106.709 1.00 41.84  ? 631  PHE   A CE2  1 
ATOM   4864 C  CZ   . PHE   A 1 652 ? 415.073 -0.840  105.337 1.00 37.41  ? 631  PHE   A CZ   1 
ATOM   4865 N  N    . ILE   A 1 653 ? 410.769 -6.020  107.921 1.00 48.30  ? 632  ILE   A N    1 
ATOM   4866 C  CA   . ILE   A 1 653 ? 410.091 -7.181  108.484 1.00 48.15  ? 632  ILE   A CA   1 
ATOM   4867 C  C    . ILE   A 1 653 ? 410.831 -8.439  108.060 1.00 51.72  ? 632  ILE   A C    1 
ATOM   4868 O  O    . ILE   A 1 653 ? 411.118 -8.635  106.871 1.00 52.03  ? 632  ILE   A O    1 
ATOM   4869 C  CB   . ILE   A 1 653 ? 408.619 -7.237  108.047 1.00 44.70  ? 632  ILE   A CB   1 
ATOM   4870 C  CG1  . ILE   A 1 653 ? 407.958 -5.869  108.222 1.00 46.17  ? 632  ILE   A CG1  1 
ATOM   4871 C  CG2  . ILE   A 1 653 ? 407.877 -8.295  108.851 1.00 45.04  ? 632  ILE   A CG2  1 
ATOM   4872 C  CD1  . ILE   A 1 653 ? 408.060 -5.316  109.621 1.00 45.72  ? 632  ILE   A CD1  1 
ATOM   4873 N  N    . ASP   A 1 654 ? 411.130 -9.294  109.032 1.00 58.12  ? 633  ASP   A N    1 
ATOM   4874 C  CA   . ASP   A 1 654 ? 411.838 -10.545 108.799 1.00 62.76  ? 633  ASP   A CA   1 
ATOM   4875 C  C    . ASP   A 1 654 ? 410.810 -11.660 108.634 1.00 68.62  ? 633  ASP   A C    1 
ATOM   4876 O  O    . ASP   A 1 654 ? 410.156 -12.059 109.604 1.00 69.98  ? 633  ASP   A O    1 
ATOM   4877 C  CB   . ASP   A 1 654 ? 412.786 -10.827 109.961 1.00 62.95  ? 633  ASP   A CB   1 
ATOM   4878 C  CG   . ASP   A 1 654 ? 413.649 -12.046 109.733 1.00 75.97  ? 633  ASP   A CG   1 
ATOM   4879 O  OD1  . ASP   A 1 654 ? 413.431 -12.755 108.728 1.00 80.41  ? 633  ASP   A OD1  1 
ATOM   4880 O  OD2  . ASP   A 1 654 ? 414.551 -12.289 110.561 1.00 81.66  ? 633  ASP   A OD2  1 
ATOM   4881 N  N    . ASP   A 1 655 ? 410.664 -12.165 107.406 1.00 76.89  ? 634  ASP   A N    1 
ATOM   4882 C  CA   . ASP   A 1 655 ? 409.705 -13.224 107.109 1.00 78.84  ? 634  ASP   A CA   1 
ATOM   4883 C  C    . ASP   A 1 655 ? 410.386 -14.512 106.656 1.00 85.36  ? 634  ASP   A C    1 
ATOM   4884 O  O    . ASP   A 1 655 ? 409.764 -15.324 105.963 1.00 89.04  ? 634  ASP   A O    1 
ATOM   4885 C  CB   . ASP   A 1 655 ? 408.701 -12.758 106.051 1.00 80.06  ? 634  ASP   A CB   1 
ATOM   4886 C  CG   . ASP   A 1 655 ? 409.374 -12.282 104.776 1.00 83.35  ? 634  ASP   A CG   1 
ATOM   4887 O  OD1  . ASP   A 1 655 ? 410.015 -13.111 104.095 1.00 95.58  ? 634  ASP   A OD1  1 
ATOM   4888 O  OD2  . ASP   A 1 655 ? 409.257 -11.081 104.451 1.00 73.03  ? 634  ASP   A OD2  1 
ATOM   4889 N  N    . ILE   A 1 656 ? 411.645 -14.728 107.042 1.00 84.55  ? 635  ILE   A N    1 
ATOM   4890 C  CA   . ILE   A 1 656 ? 412.404 -15.873 106.549 1.00 90.75  ? 635  ILE   A CA   1 
ATOM   4891 C  C    . ILE   A 1 656 ? 413.282 -16.471 107.644 1.00 92.13  ? 635  ILE   A C    1 
ATOM   4892 O  O    . ILE   A 1 656 ? 413.733 -17.617 107.529 1.00 98.93  ? 635  ILE   A O    1 
ATOM   4893 C  CB   . ILE   A 1 656 ? 413.255 -15.479 105.327 1.00 88.82  ? 635  ILE   A CB   1 
ATOM   4894 C  CG1  . ILE   A 1 656 ? 414.300 -14.433 105.719 1.00 80.88  ? 635  ILE   A CG1  1 
ATOM   4895 C  CG2  . ILE   A 1 656 ? 412.372 -14.956 104.201 1.00 77.61  ? 635  ILE   A CG2  1 
ATOM   4896 C  CD1  . ILE   A 1 656 ? 415.148 -13.956 104.563 1.00 66.92  ? 635  ILE   A CD1  1 
ATOM   4897 N  N    . SER   A 1 657 ? 413.533 -15.708 108.713 1.00 87.74  ? 636  SER   A N    1 
ATOM   4898 C  CA   . SER   A 1 657 ? 414.420 -16.189 109.771 1.00 92.17  ? 636  SER   A CA   1 
ATOM   4899 C  C    . SER   A 1 657 ? 413.898 -17.466 110.423 1.00 95.55  ? 636  SER   A C    1 
ATOM   4900 O  O    . SER   A 1 657 ? 414.693 -18.306 110.861 1.00 91.08  ? 636  SER   A O    1 
ATOM   4901 C  CB   . SER   A 1 657 ? 414.625 -15.104 110.830 1.00 85.77  ? 636  SER   A CB   1 
ATOM   4902 O  OG   . SER   A 1 657 ? 415.670 -14.218 110.464 1.00 79.97  ? 636  SER   A OG   1 
ATOM   4903 N  N    . ALA   A 1 658 ? 412.574 -17.629 110.506 1.00 97.65  ? 637  ALA   A N    1 
ATOM   4904 C  CA   . ALA   A 1 658 ? 412.008 -18.852 111.063 1.00 96.24  ? 637  ALA   A CA   1 
ATOM   4905 C  C    . ALA   A 1 658 ? 412.312 -20.072 110.203 1.00 100.53 ? 637  ALA   A C    1 
ATOM   4906 O  O    . ALA   A 1 658 ? 412.183 -21.203 110.685 1.00 99.74  ? 637  ALA   A O    1 
ATOM   4907 C  CB   . ALA   A 1 658 ? 410.496 -18.702 111.241 1.00 77.90  ? 637  ALA   A CB   1 
ATOM   4908 N  N    . TYR   A 1 659 ? 412.711 -19.867 108.947 1.00 107.02 ? 638  TYR   A N    1 
ATOM   4909 C  CA   . TYR   A 1 659 ? 413.059 -20.958 108.048 1.00 105.53 ? 638  TYR   A CA   1 
ATOM   4910 C  C    . TYR   A 1 659 ? 414.558 -21.212 107.968 1.00 108.23 ? 638  TYR   A C    1 
ATOM   4911 O  O    . TYR   A 1 659 ? 414.965 -22.274 107.483 1.00 106.26 ? 638  TYR   A O    1 
ATOM   4912 C  CB   . TYR   A 1 659 ? 412.512 -20.676 106.644 1.00 105.45 ? 638  TYR   A CB   1 
ATOM   4913 C  CG   . TYR   A 1 659 ? 411.026 -20.402 106.629 1.00 107.59 ? 638  TYR   A CG   1 
ATOM   4914 C  CD1  . TYR   A 1 659 ? 410.531 -19.130 106.888 1.00 110.07 ? 638  TYR   A CD1  1 
ATOM   4915 C  CD2  . TYR   A 1 659 ? 410.117 -21.417 106.366 1.00 109.72 ? 638  TYR   A CD2  1 
ATOM   4916 C  CE1  . TYR   A 1 659 ? 409.172 -18.877 106.882 1.00 110.53 ? 638  TYR   A CE1  1 
ATOM   4917 C  CE2  . TYR   A 1 659 ? 408.757 -21.173 106.356 1.00 114.41 ? 638  TYR   A CE2  1 
ATOM   4918 C  CZ   . TYR   A 1 659 ? 408.290 -19.902 106.616 1.00 113.96 ? 638  TYR   A CZ   1 
ATOM   4919 O  OH   . TYR   A 1 659 ? 406.936 -19.657 106.607 1.00 111.74 ? 638  TYR   A OH   1 
ATOM   4920 N  N    . HIS   A 1 660 ? 415.379 -20.267 108.422 1.00 96.66  ? 639  HIS   A N    1 
ATOM   4921 C  CA   . HIS   A 1 660 ? 416.830 -20.370 108.565 1.00 89.42  ? 639  HIS   A CA   1 
ATOM   4922 C  C    . HIS   A 1 660 ? 417.575 -20.169 107.248 1.00 90.21  ? 639  HIS   A C    1 
ATOM   4923 O  O    . HIS   A 1 660 ? 418.807 -20.290 107.237 1.00 77.90  ? 639  HIS   A O    1 
ATOM   4924 C  CB   . HIS   A 1 660 ? 417.271 -21.714 109.169 1.00 88.20  ? 639  HIS   A CB   1 
ATOM   4925 C  CG   . HIS   A 1 660 ? 416.531 -22.094 110.415 1.00 95.43  ? 639  HIS   A CG   1 
ATOM   4926 N  ND1  . HIS   A 1 660 ? 416.661 -21.404 111.601 1.00 90.28  ? 639  HIS   A ND1  1 
ATOM   4927 C  CD2  . HIS   A 1 660 ? 415.661 -23.102 110.661 1.00 94.47  ? 639  HIS   A CD2  1 
ATOM   4928 C  CE1  . HIS   A 1 660 ? 415.898 -21.966 112.522 1.00 92.51  ? 639  HIS   A CE1  1 
ATOM   4929 N  NE2  . HIS   A 1 660 ? 415.281 -22.999 111.977 1.00 95.59  ? 639  HIS   A NE2  1 
ATOM   4930 N  N    . LYS   A 1 661 ? 416.888 -19.874 106.147 1.00 96.45  ? 640  LYS   A N    1 
ATOM   4931 C  CA   . LYS   A 1 661 ? 417.551 -19.681 104.863 1.00 96.03  ? 640  LYS   A CA   1 
ATOM   4932 C  C    . LYS   A 1 661 ? 416.547 -19.117 103.869 1.00 98.27  ? 640  LYS   A C    1 
ATOM   4933 O  O    . LYS   A 1 661 ? 415.332 -19.197 104.071 1.00 98.15  ? 640  LYS   A O    1 
ATOM   4934 C  CB   . LYS   A 1 661 ? 418.160 -20.985 104.332 1.00 94.86  ? 640  LYS   A CB   1 
ATOM   4935 C  CG   . LYS   A 1 661 ? 417.162 -22.116 104.114 1.00 96.11  ? 640  LYS   A CG   1 
ATOM   4936 C  CD   . LYS   A 1 661 ? 417.863 -23.375 103.619 1.00 94.73  ? 640  LYS   A CD   1 
ATOM   4937 C  CE   . LYS   A 1 661 ? 416.903 -24.551 103.510 1.00 99.75  ? 640  LYS   A CE   1 
ATOM   4938 N  NZ   . LYS   A 1 661 ? 416.402 -24.999 104.840 1.00 92.44  ? 640  LYS   A NZ   1 
ATOM   4939 N  N    . PHE   A 1 662 ? 417.077 -18.550 102.787 1.00 93.39  ? 641  PHE   A N    1 
ATOM   4940 C  CA   . PHE   A 1 662 ? 416.280 -17.923 101.740 1.00 88.83  ? 641  PHE   A CA   1 
ATOM   4941 C  C    . PHE   A 1 662 ? 416.643 -18.556 100.405 1.00 92.04  ? 641  PHE   A C    1 
ATOM   4942 O  O    . PHE   A 1 662 ? 417.797 -18.477 99.970  1.00 95.70  ? 641  PHE   A O    1 
ATOM   4943 C  CB   . PHE   A 1 662 ? 416.514 -16.410 101.712 1.00 81.27  ? 641  PHE   A CB   1 
ATOM   4944 C  CG   . PHE   A 1 662 ? 415.743 -15.691 100.643 1.00 75.39  ? 641  PHE   A CG   1 
ATOM   4945 C  CD1  . PHE   A 1 662 ? 414.378 -15.481 100.774 1.00 66.56  ? 641  PHE   A CD1  1 
ATOM   4946 C  CD2  . PHE   A 1 662 ? 416.385 -15.207 99.514  1.00 59.85  ? 641  PHE   A CD2  1 
ATOM   4947 C  CE1  . PHE   A 1 662 ? 413.667 -14.814 99.795  1.00 68.68  ? 641  PHE   A CE1  1 
ATOM   4948 C  CE2  . PHE   A 1 662 ? 415.680 -14.539 98.531  1.00 56.45  ? 641  PHE   A CE2  1 
ATOM   4949 C  CZ   . PHE   A 1 662 ? 414.318 -14.341 98.671  1.00 60.87  ? 641  PHE   A CZ   1 
ATOM   4950 N  N    . LEU   A 1 663 ? 415.661 -19.194 99.765  1.00 93.40  ? 642  LEU   A N    1 
ATOM   4951 C  CA   . LEU   A 1 663 ? 415.829 -19.784 98.443  1.00 94.42  ? 642  LEU   A CA   1 
ATOM   4952 C  C    . LEU   A 1 663 ? 415.031 -19.038 97.378  1.00 89.12  ? 642  LEU   A C    1 
ATOM   4953 O  O    . LEU   A 1 663 ? 414.702 -19.612 96.335  1.00 88.97  ? 642  LEU   A O    1 
ATOM   4954 C  CB   . LEU   A 1 663 ? 415.428 -21.260 98.460  1.00 100.75 ? 642  LEU   A CB   1 
ATOM   4955 C  CG   . LEU   A 1 663 ? 416.101 -22.169 99.492  1.00 100.72 ? 642  LEU   A CG   1 
ATOM   4956 C  CD1  . LEU   A 1 663 ? 415.357 -22.134 100.821 1.00 100.10 ? 642  LEU   A CD1  1 
ATOM   4957 C  CD2  . LEU   A 1 663 ? 416.216 -23.593 98.966  1.00 99.89  ? 642  LEU   A CD2  1 
ATOM   4958 N  N    . GLY   A 1 664 ? 414.712 -17.768 97.624  1.00 89.19  ? 643  GLY   A N    1 
ATOM   4959 C  CA   . GLY   A 1 664 ? 413.897 -16.980 96.726  1.00 79.91  ? 643  GLY   A CA   1 
ATOM   4960 C  C    . GLY   A 1 664 ? 412.426 -16.938 97.088  1.00 89.86  ? 643  GLY   A C    1 
ATOM   4961 O  O    . GLY   A 1 664 ? 411.674 -16.176 96.465  1.00 90.44  ? 643  GLY   A O    1 
ATOM   4962 N  N    . GLU   A 1 665 ? 411.993 -17.720 98.074  1.00 107.29 ? 644  GLU   A N    1 
ATOM   4963 C  CA   . GLU   A 1 665 ? 410.583 -17.815 98.422  1.00 114.73 ? 644  GLU   A CA   1 
ATOM   4964 C  C    . GLU   A 1 665 ? 410.288 -17.033 99.697  1.00 111.68 ? 644  GLU   A C    1 
ATOM   4965 O  O    . GLU   A 1 665 ? 411.040 -17.102 100.669 1.00 107.74 ? 644  GLU   A O    1 
ATOM   4966 C  CB   . GLU   A 1 665 ? 410.166 -19.280 98.595  1.00 114.42 ? 644  GLU   A CB   1 
ATOM   4967 C  CG   . GLU   A 1 665 ? 408.659 -19.506 98.527  1.00 119.23 ? 644  GLU   A CG   1 
ATOM   4968 C  CD   . GLU   A 1 665 ? 408.297 -20.946 98.219  1.00 119.12 ? 644  GLU   A CD   1 
ATOM   4969 O  OE1  . GLU   A 1 665 ? 409.166 -21.687 97.711  1.00 121.37 ? 644  GLU   A OE1  1 
ATOM   4970 O  OE2  . GLU   A 1 665 ? 407.142 -21.339 98.482  1.00 116.69 ? 644  GLU   A OE2  1 
ATOM   4971 N  N    . VAL   A 1 666 ? 409.198 -16.277 99.673  1.00 104.35 ? 645  VAL   A N    1 
ATOM   4972 C  CA   . VAL   A 1 666 ? 408.557 -15.753 100.869 1.00 102.39 ? 645  VAL   A CA   1 
ATOM   4973 C  C    . VAL   A 1 666 ? 407.442 -16.717 101.234 1.00 103.34 ? 645  VAL   A C    1 
ATOM   4974 O  O    . VAL   A 1 666 ? 406.652 -17.118 100.371 1.00 101.61 ? 645  VAL   A O    1 
ATOM   4975 C  CB   . VAL   A 1 666 ? 408.006 -14.335 100.639 1.00 98.15  ? 645  VAL   A CB   1 
ATOM   4976 C  CG1  . VAL   A 1 666 ? 407.810 -13.621 101.986 1.00 88.06  ? 645  VAL   A CG1  1 
ATOM   4977 C  CG2  . VAL   A 1 666 ? 408.898 -13.540 99.714  1.00 97.77  ? 645  VAL   A CG2  1 
ATOM   4978 N  N    . HIS   A 1 667 ? 407.385 -17.102 102.500 1.00 99.16  ? 646  HIS   A N    1 
ATOM   4979 C  CA   . HIS   A 1 667 ? 406.346 -18.002 102.961 1.00 94.25  ? 646  HIS   A CA   1 
ATOM   4980 C  C    . HIS   A 1 667 ? 405.261 -17.287 103.757 1.00 89.29  ? 646  HIS   A C    1 
ATOM   4981 O  O    . HIS   A 1 667 ? 404.254 -17.910 104.112 1.00 92.31  ? 646  HIS   A O    1 
ATOM   4982 C  CB   . HIS   A 1 667 ? 406.960 -19.136 103.786 1.00 99.52  ? 646  HIS   A CB   1 
ATOM   4983 C  CG   . HIS   A 1 667 ? 408.004 -19.922 103.049 1.00 104.46 ? 646  HIS   A CG   1 
ATOM   4984 N  ND1  . HIS   A 1 667 ? 409.348 -19.853 103.353 1.00 109.92 ? 646  HIS   A ND1  1 
ATOM   4985 C  CD2  . HIS   A 1 667 ? 407.898 -20.783 102.011 1.00 101.92 ? 646  HIS   A CD2  1 
ATOM   4986 C  CE1  . HIS   A 1 667 ? 410.023 -20.645 102.537 1.00 109.39 ? 646  HIS   A CE1  1 
ATOM   4987 N  NE2  . HIS   A 1 667 ? 409.166 -21.220 101.713 1.00 106.41 ? 646  HIS   A NE2  1 
ATOM   4988 N  N    . CYS   A 1 668 ? 405.429 -15.997 104.023 1.00 90.03  ? 647  CYS   A N    1 
ATOM   4989 C  CA   . CYS   A 1 668 ? 404.449 -15.190 104.733 1.00 77.29  ? 647  CYS   A CA   1 
ATOM   4990 C  C    . CYS   A 1 668 ? 403.790 -14.196 103.788 1.00 77.11  ? 647  CYS   A C    1 
ATOM   4991 O  O    . CYS   A 1 668 ? 404.417 -13.681 102.858 1.00 83.88  ? 647  CYS   A O    1 
ATOM   4992 C  CB   . CYS   A 1 668 ? 405.093 -14.423 105.893 1.00 62.38  ? 647  CYS   A CB   1 
ATOM   4993 S  SG   . CYS   A 1 668 ? 405.624 -15.454 107.266 1.00 81.99  ? 647  CYS   A SG   1 
ATOM   4994 N  N    . GLY   A 1 669 ? 402.514 -13.918 104.051 1.00 71.69  ? 648  GLY   A N    1 
ATOM   4995 C  CA   . GLY   A 1 669 ? 401.772 -12.968 103.260 1.00 67.08  ? 648  GLY   A CA   1 
ATOM   4996 C  C    . GLY   A 1 669 ? 401.045 -11.969 104.138 1.00 56.40  ? 648  GLY   A C    1 
ATOM   4997 O  O    . GLY   A 1 669 ? 400.766 -12.213 105.312 1.00 53.48  ? 648  GLY   A O    1 
ATOM   4998 N  N    . THR   A 1 670 ? 400.749 -10.821 103.538 1.00 57.10  ? 649  THR   A N    1 
ATOM   4999 C  CA   . THR   A 1 670 ? 399.902 -9.816  104.156 1.00 48.66  ? 649  THR   A CA   1 
ATOM   5000 C  C    . THR   A 1 670 ? 399.021 -9.205  103.081 1.00 48.28  ? 649  THR   A C    1 
ATOM   5001 O  O    . THR   A 1 670 ? 399.386 -9.168  101.903 1.00 47.13  ? 649  THR   A O    1 
ATOM   5002 C  CB   . THR   A 1 670 ? 400.712 -8.715  104.850 1.00 44.22  ? 649  THR   A CB   1 
ATOM   5003 O  OG1  . THR   A 1 670 ? 401.500 -8.018  103.878 1.00 50.35  ? 649  THR   A OG1  1 
ATOM   5004 C  CG2  . THR   A 1 670 ? 401.627 -9.317  105.900 1.00 46.04  ? 649  THR   A CG2  1 
ATOM   5005 N  N    . ASN   A 1 671 ? 397.850 -8.738  103.498 1.00 45.44  ? 650  ASN   A N    1 
ATOM   5006 C  CA   . ASN   A 1 671 ? 396.930 -8.064  102.599 1.00 44.07  ? 650  ASN   A CA   1 
ATOM   5007 C  C    . ASN   A 1 671 ? 396.216 -6.984  103.395 1.00 44.06  ? 650  ASN   A C    1 
ATOM   5008 O  O    . ASN   A 1 671 ? 395.848 -7.202  104.552 1.00 49.15  ? 650  ASN   A O    1 
ATOM   5009 C  CB   . ASN   A 1 671 ? 395.929 -9.044  101.978 1.00 44.67  ? 650  ASN   A CB   1 
ATOM   5010 C  CG   . ASN   A 1 671 ? 395.734 -8.812  100.495 1.00 51.44  ? 650  ASN   A CG   1 
ATOM   5011 O  OD1  . ASN   A 1 671 ? 395.844 -7.685  100.013 1.00 46.04  ? 650  ASN   A OD1  1 
ATOM   5012 N  ND2  . ASN   A 1 671 ? 395.450 -9.881  99.760  1.00 52.66  ? 650  ASN   A ND2  1 
ATOM   5013 N  N    . VAL   A 1 672 ? 396.041 -5.821  102.778 1.00 40.25  ? 651  VAL   A N    1 
ATOM   5014 C  CA   . VAL   A 1 672 ? 395.484 -4.650  103.443 1.00 37.85  ? 651  VAL   A CA   1 
ATOM   5015 C  C    . VAL   A 1 672 ? 394.120 -4.351  102.842 1.00 42.17  ? 651  VAL   A C    1 
ATOM   5016 O  O    . VAL   A 1 672 ? 393.984 -4.235  101.619 1.00 40.75  ? 651  VAL   A O    1 
ATOM   5017 C  CB   . VAL   A 1 672 ? 396.413 -3.431  103.312 1.00 36.41  ? 651  VAL   A CB   1 
ATOM   5018 C  CG1  . VAL   A 1 672 ? 395.846 -2.248  104.084 1.00 34.87  ? 651  VAL   A CG1  1 
ATOM   5019 C  CG2  . VAL   A 1 672 ? 397.810 -3.771  103.797 1.00 35.47  ? 651  VAL   A CG2  1 
ATOM   5020 N  N    . ARG   A 1 673 ? 393.114 -4.228  103.699 1.00 38.93  ? 652  ARG   A N    1 
ATOM   5021 C  CA   . ARG   A 1 673 ? 391.811 -3.737  103.282 1.00 37.03  ? 652  ARG   A CA   1 
ATOM   5022 C  C    . ARG   A 1 673 ? 391.810 -2.224  103.449 1.00 40.95  ? 652  ARG   A C    1 
ATOM   5023 O  O    . ARG   A 1 673 ? 392.083 -1.714  104.541 1.00 42.44  ? 652  ARG   A O    1 
ATOM   5024 C  CB   . ARG   A 1 673 ? 390.695 -4.391  104.094 1.00 46.38  ? 652  ARG   A CB   1 
ATOM   5025 C  CG   . ARG   A 1 673 ? 389.348 -4.358  103.405 1.00 49.74  ? 652  ARG   A CG   1 
ATOM   5026 C  CD   . ARG   A 1 673 ? 388.550 -3.144  103.816 1.00 49.04  ? 652  ARG   A CD   1 
ATOM   5027 N  NE   . ARG   A 1 673 ? 387.663 -3.430  104.936 1.00 51.39  ? 652  ARG   A NE   1 
ATOM   5028 C  CZ   . ARG   A 1 673 ? 386.772 -2.574  105.415 1.00 58.88  ? 652  ARG   A CZ   1 
ATOM   5029 N  NH1  . ARG   A 1 673 ? 386.641 -1.358  104.909 1.00 62.15  ? 652  ARG   A NH1  1 
ATOM   5030 N  NH2  . ARG   A 1 673 ? 385.989 -2.948  106.425 1.00 55.67  ? 652  ARG   A NH2  1 
ATOM   5031 N  N    . ARG   A 1 674 ? 391.531 -1.509  102.368 1.00 36.97  ? 653  ARG   A N    1 
ATOM   5032 C  CA   . ARG   A 1 674 ? 391.670 -0.064  102.357 1.00 38.56  ? 653  ARG   A CA   1 
ATOM   5033 C  C    . ARG   A 1 674 ? 390.313 0.605   102.197 1.00 36.96  ? 653  ARG   A C    1 
ATOM   5034 O  O    . ARG   A 1 674 ? 389.340 -0.006  101.746 1.00 36.37  ? 653  ARG   A O    1 
ATOM   5035 C  CB   . ARG   A 1 674 ? 392.620 0.372   101.237 1.00 30.78  ? 653  ARG   A CB   1 
ATOM   5036 C  CG   . ARG   A 1 674 ? 393.955 -0.343  101.313 1.00 34.08  ? 653  ARG   A CG   1 
ATOM   5037 C  CD   . ARG   A 1 674 ? 394.956 0.169   100.300 1.00 33.80  ? 653  ARG   A CD   1 
ATOM   5038 N  NE   . ARG   A 1 674 ? 396.230 -0.527  100.443 1.00 36.87  ? 653  ARG   A NE   1 
ATOM   5039 C  CZ   . ARG   A 1 674 ? 397.207 -0.143  101.254 1.00 35.00  ? 653  ARG   A CZ   1 
ATOM   5040 N  NH1  . ARG   A 1 674 ? 397.108 0.957   101.983 1.00 33.69  ? 653  ARG   A NH1  1 
ATOM   5041 N  NH2  . ARG   A 1 674 ? 398.308 -0.883  101.340 1.00 40.29  ? 653  ARG   A NH2  1 
ATOM   5042 N  N    . LYS   A 1 675 ? 390.256 1.867   102.602 1.00 38.86  ? 654  LYS   A N    1 
ATOM   5043 C  CA   . LYS   A 1 675 ? 389.083 2.672   102.313 1.00 40.69  ? 654  LYS   A CA   1 
ATOM   5044 C  C    . LYS   A 1 675 ? 388.905 2.784   100.802 1.00 40.89  ? 654  LYS   A C    1 
ATOM   5045 O  O    . LYS   A 1 675 ? 389.892 2.917   100.069 1.00 41.79  ? 654  LYS   A O    1 
ATOM   5046 C  CB   . LYS   A 1 675 ? 389.223 4.065   102.922 1.00 38.72  ? 654  LYS   A CB   1 
ATOM   5047 C  CG   . LYS   A 1 675 ? 389.210 4.100   104.434 1.00 44.56  ? 654  LYS   A CG   1 
ATOM   5048 C  CD   . LYS   A 1 675 ? 388.651 5.426   104.907 1.00 49.06  ? 654  LYS   A CD   1 
ATOM   5049 C  CE   . LYS   A 1 675 ? 389.443 5.984   106.073 1.00 58.97  ? 654  LYS   A CE   1 
ATOM   5050 N  NZ   . LYS   A 1 675 ? 389.835 7.400   105.829 1.00 64.39  ? 654  LYS   A NZ   1 
ATOM   5051 N  N    . PRO   A 1 676 ? 387.676 2.728   100.298 1.00 35.63  ? 655  PRO   A N    1 
ATOM   5052 C  CA   . PRO   A 1 676 ? 387.467 2.921   98.860  1.00 34.07  ? 655  PRO   A CA   1 
ATOM   5053 C  C    . PRO   A 1 676 ? 387.832 4.333   98.426  1.00 37.03  ? 655  PRO   A C    1 
ATOM   5054 O  O    . PRO   A 1 676 ? 387.969 5.254   99.235  1.00 37.33  ? 655  PRO   A O    1 
ATOM   5055 C  CB   . PRO   A 1 676 ? 385.967 2.654   98.676  1.00 32.04  ? 655  PRO   A CB   1 
ATOM   5056 C  CG   . PRO   A 1 676 ? 385.372 2.817   100.037 1.00 40.26  ? 655  PRO   A CG   1 
ATOM   5057 C  CD   . PRO   A 1 676 ? 386.432 2.369   100.996 1.00 37.42  ? 655  PRO   A CD   1 
ATOM   5058 N  N    . PHE   A 1 677 ? 388.009 4.489   97.117  1.00 37.88  ? 656  PHE   A N    1 
ATOM   5059 C  CA   . PHE   A 1 677 ? 388.163 5.822   96.555  1.00 38.16  ? 656  PHE   A CA   1 
ATOM   5060 C  C    . PHE   A 1 677 ? 386.979 6.693   96.954  1.00 39.69  ? 656  PHE   A C    1 
ATOM   5061 O  O    . PHE   A 1 677 ? 385.844 6.222   97.073  1.00 39.34  ? 656  PHE   A O    1 
ATOM   5062 C  CB   . PHE   A 1 677 ? 388.255 5.763   95.029  1.00 38.87  ? 656  PHE   A CB   1 
ATOM   5063 C  CG   . PHE   A 1 677 ? 389.523 5.151   94.508  1.00 34.93  ? 656  PHE   A CG   1 
ATOM   5064 C  CD1  . PHE   A 1 677 ? 390.680 5.906   94.406  1.00 38.43  ? 656  PHE   A CD1  1 
ATOM   5065 C  CD2  . PHE   A 1 677 ? 389.551 3.830   94.086  1.00 33.28  ? 656  PHE   A CD2  1 
ATOM   5066 C  CE1  . PHE   A 1 677 ? 391.848 5.353   93.912  1.00 34.38  ? 656  PHE   A CE1  1 
ATOM   5067 C  CE2  . PHE   A 1 677 ? 390.716 3.271   93.591  1.00 35.40  ? 656  PHE   A CE2  1 
ATOM   5068 C  CZ   . PHE   A 1 677 ? 391.863 4.034   93.503  1.00 33.79  ? 656  PHE   A CZ   1 
ATOM   5069 N  N    . THR   A 1 678 ? 387.242 7.983   97.165  1.00 41.12  ? 657  THR   A N    1 
ATOM   5070 C  CA   . THR   A 1 678 ? 386.125 8.900   97.349  1.00 43.44  ? 657  THR   A CA   1 
ATOM   5071 C  C    . THR   A 1 678 ? 385.436 9.182   96.019  1.00 41.38  ? 657  THR   A C    1 
ATOM   5072 O  O    . THR   A 1 678 ? 384.229 9.446   95.985  1.00 38.97  ? 657  THR   A O    1 
ATOM   5073 C  CB   . THR   A 1 678 ? 386.598 10.194  98.009  1.00 41.72  ? 657  THR   A CB   1 
ATOM   5074 O  OG1  . THR   A 1 678 ? 387.431 10.923  97.101  1.00 55.54  ? 657  THR   A OG1  1 
ATOM   5075 C  CG2  . THR   A 1 678 ? 387.392 9.878   99.264  1.00 39.43  ? 657  THR   A CG2  1 
ATOM   5076 N  N    . PHE   A 1 679 ? 386.181 9.108   94.920  1.00 37.59  ? 658  PHE   A N    1 
ATOM   5077 C  CA   . PHE   A 1 679 ? 385.608 9.247   93.587  1.00 39.27  ? 658  PHE   A CA   1 
ATOM   5078 C  C    . PHE   A 1 679 ? 384.666 8.078   93.306  1.00 35.66  ? 658  PHE   A C    1 
ATOM   5079 O  O    . PHE   A 1 679 ? 385.067 6.915   93.411  1.00 35.76  ? 658  PHE   A O    1 
ATOM   5080 C  CB   . PHE   A 1 679 ? 386.732 9.303   92.554  1.00 36.54  ? 658  PHE   A CB   1 
ATOM   5081 C  CG   . PHE   A 1 679 ? 386.268 9.602   91.162  1.00 34.37  ? 658  PHE   A CG   1 
ATOM   5082 C  CD1  . PHE   A 1 679 ? 385.839 8.583   90.329  1.00 34.79  ? 658  PHE   A CD1  1 
ATOM   5083 C  CD2  . PHE   A 1 679 ? 386.267 10.901  90.683  1.00 34.52  ? 658  PHE   A CD2  1 
ATOM   5084 C  CE1  . PHE   A 1 679 ? 385.409 8.855   89.045  1.00 38.49  ? 658  PHE   A CE1  1 
ATOM   5085 C  CE2  . PHE   A 1 679 ? 385.839 11.179  89.398  1.00 34.69  ? 658  PHE   A CE2  1 
ATOM   5086 C  CZ   . PHE   A 1 679 ? 385.410 10.155  88.578  1.00 36.97  ? 658  PHE   A CZ   1 
ATOM   5087 N  N    . LYS   A 1 680 ? 383.414 8.380   92.961  1.00 35.42  ? 659  LYS   A N    1 
ATOM   5088 C  CA   . LYS   A 1 680 ? 382.448 7.335   92.639  1.00 32.85  ? 659  LYS   A CA   1 
ATOM   5089 C  C    . LYS   A 1 680 ? 382.705 6.815   91.232  1.00 29.38  ? 659  LYS   A C    1 
ATOM   5090 O  O    . LYS   A 1 680 ? 382.860 7.599   90.291  1.00 33.74  ? 659  LYS   A O    1 
ATOM   5091 C  CB   . LYS   A 1 680 ? 381.020 7.864   92.750  1.00 33.04  ? 659  LYS   A CB   1 
ATOM   5092 C  CG   . LYS   A 1 680 ? 380.750 8.641   94.020  1.00 35.76  ? 659  LYS   A CG   1 
ATOM   5093 C  CD   . LYS   A 1 680 ? 381.033 7.807   95.255  1.00 35.96  ? 659  LYS   A CD   1 
ATOM   5094 C  CE   . LYS   A 1 680 ? 380.663 8.570   96.512  1.00 41.51  ? 659  LYS   A CE   1 
ATOM   5095 N  NZ   . LYS   A 1 680 ? 380.908 7.774   97.742  1.00 52.38  ? 659  LYS   A NZ   1 
ATOM   5096 N  N    . TRP   A 1 681 ? 382.743 5.489   91.083  1.00 32.66  ? 660  TRP   A N    1 
ATOM   5097 C  CA   . TRP   A 1 681 ? 383.136 4.922   89.796  1.00 25.22  ? 660  TRP   A CA   1 
ATOM   5098 C  C    . TRP   A 1 681 ? 382.207 5.364   88.676  1.00 28.82  ? 660  TRP   A C    1 
ATOM   5099 O  O    . TRP   A 1 681 ? 382.654 5.553   87.539  1.00 29.05  ? 660  TRP   A O    1 
ATOM   5100 C  CB   . TRP   A 1 681 ? 383.185 3.395   89.873  1.00 27.01  ? 660  TRP   A CB   1 
ATOM   5101 C  CG   . TRP   A 1 681 ? 381.876 2.737   90.204  1.00 30.57  ? 660  TRP   A CG   1 
ATOM   5102 C  CD1  . TRP   A 1 681 ? 381.432 2.381   91.445  1.00 27.53  ? 660  TRP   A CD1  1 
ATOM   5103 C  CD2  . TRP   A 1 681 ? 380.846 2.342   89.282  1.00 23.88  ? 660  TRP   A CD2  1 
ATOM   5104 N  NE1  . TRP   A 1 681 ? 380.193 1.795   91.355  1.00 30.09  ? 660  TRP   A NE1  1 
ATOM   5105 C  CE2  . TRP   A 1 681 ? 379.811 1.759   90.040  1.00 26.12  ? 660  TRP   A CE2  1 
ATOM   5106 C  CE3  . TRP   A 1 681 ? 380.698 2.427   87.893  1.00 26.78  ? 660  TRP   A CE3  1 
ATOM   5107 C  CZ2  . TRP   A 1 681 ? 378.642 1.263   89.456  1.00 28.11  ? 660  TRP   A CZ2  1 
ATOM   5108 C  CZ3  . TRP   A 1 681 ? 379.536 1.933   87.315  1.00 24.98  ? 660  TRP   A CZ3  1 
ATOM   5109 C  CH2  . TRP   A 1 681 ? 378.525 1.359   88.096  1.00 26.58  ? 660  TRP   A CH2  1 
ATOM   5110 N  N    . TRP   A 1 682 ? 380.921 5.549   88.972  1.00 28.35  ? 661  TRP   A N    1 
ATOM   5111 C  CA   . TRP   A 1 682 ? 379.977 5.896   87.919  1.00 30.80  ? 661  TRP   A CA   1 
ATOM   5112 C  C    . TRP   A 1 682 ? 380.158 7.317   87.399  1.00 32.32  ? 661  TRP   A C    1 
ATOM   5113 O  O    . TRP   A 1 682 ? 379.541 7.667   86.388  1.00 35.99  ? 661  TRP   A O    1 
ATOM   5114 C  CB   . TRP   A 1 682 ? 378.541 5.690   88.405  1.00 29.07  ? 661  TRP   A CB   1 
ATOM   5115 C  CG   . TRP   A 1 682 ? 378.190 6.402   89.678  1.00 30.05  ? 661  TRP   A CG   1 
ATOM   5116 C  CD1  . TRP   A 1 682 ? 377.727 7.679   89.801  1.00 30.85  ? 661  TRP   A CD1  1 
ATOM   5117 C  CD2  . TRP   A 1 682 ? 378.239 5.863   91.008  1.00 30.83  ? 661  TRP   A CD2  1 
ATOM   5118 N  NE1  . TRP   A 1 682 ? 377.496 7.975   91.125  1.00 34.75  ? 661  TRP   A NE1  1 
ATOM   5119 C  CE2  . TRP   A 1 682 ? 377.803 6.877   91.886  1.00 37.69  ? 661  TRP   A CE2  1 
ATOM   5120 C  CE3  . TRP   A 1 682 ? 378.616 4.626   91.542  1.00 32.35  ? 661  TRP   A CE3  1 
ATOM   5121 C  CZ2  . TRP   A 1 682 ? 377.732 6.691   93.267  1.00 33.13  ? 661  TRP   A CZ2  1 
ATOM   5122 C  CZ3  . TRP   A 1 682 ? 378.546 4.444   92.916  1.00 31.61  ? 661  TRP   A CZ3  1 
ATOM   5123 C  CH2  . TRP   A 1 682 ? 378.107 5.471   93.761  1.00 35.18  ? 661  TRP   A CH2  1 
ATOM   5124 N  N    . HIS   A 1 683 ? 380.983 8.136   88.052  1.00 35.80  ? 662  HIS   A N    1 
ATOM   5125 C  CA   . HIS   A 1 683 ? 381.303 9.459   87.529  1.00 34.35  ? 662  HIS   A CA   1 
ATOM   5126 C  C    . HIS   A 1 683 ? 382.392 9.421   86.467  1.00 39.51  ? 662  HIS   A C    1 
ATOM   5127 O  O    . HIS   A 1 683 ? 382.667 10.449  85.841  1.00 43.78  ? 662  HIS   A O    1 
ATOM   5128 C  CB   . HIS   A 1 683 ? 381.726 10.383  88.670  1.00 37.55  ? 662  HIS   A CB   1 
ATOM   5129 C  CG   . HIS   A 1 683 ? 380.592 10.809  89.549  1.00 34.51  ? 662  HIS   A CG   1 
ATOM   5130 N  ND1  . HIS   A 1 683 ? 380.784 11.352  90.801  1.00 36.18  ? 662  HIS   A ND1  1 
ATOM   5131 C  CD2  . HIS   A 1 683 ? 379.253 10.781  89.352  1.00 39.35  ? 662  HIS   A CD2  1 
ATOM   5132 C  CE1  . HIS   A 1 683 ? 379.611 11.637  91.340  1.00 41.36  ? 662  HIS   A CE1  1 
ATOM   5133 N  NE2  . HIS   A 1 683 ? 378.666 11.300  90.481  1.00 37.10  ? 662  HIS   A NE2  1 
ATOM   5134 N  N    . MET   A 1 684 ? 383.009 8.266   86.257  1.00 39.30  ? 663  MET   A N    1 
ATOM   5135 C  CA   . MET   A 1 684 ? 384.035 8.095   85.245  1.00 38.76  ? 663  MET   A CA   1 
ATOM   5136 C  C    . MET   A 1 684 ? 383.414 8.091   83.848  1.00 43.72  ? 663  MET   A C    1 
ATOM   5137 O  O    . MET   A 1 684 ? 382.200 7.947   83.682  1.00 43.64  ? 663  MET   A O    1 
ATOM   5138 C  CB   . MET   A 1 684 ? 384.782 6.790   85.513  1.00 36.57  ? 663  MET   A CB   1 
ATOM   5139 C  CG   . MET   A 1 684 ? 385.878 6.450   84.549  1.00 48.58  ? 663  MET   A CG   1 
ATOM   5140 S  SD   . MET   A 1 684 ? 386.862 5.098   85.211  1.00 44.25  ? 663  MET   A SD   1 
ATOM   5141 C  CE   . MET   A 1 684 ? 388.116 4.973   83.948  1.00 40.26  ? 663  MET   A CE   1 
ATOM   5142 N  N    . VAL   A 1 685 ? 384.262 8.255   82.835  1.00 48.41  ? 664  VAL   A N    1 
ATOM   5143 C  CA   . VAL   A 1 685 ? 383.834 8.057   81.449  1.00 50.24  ? 664  VAL   A CA   1 
ATOM   5144 C  C    . VAL   A 1 685 ? 384.810 7.123   80.739  1.00 53.32  ? 664  VAL   A C    1 
ATOM   5145 O  O    . VAL   A 1 685 ? 385.764 7.596   80.105  1.00 56.74  ? 664  VAL   A O    1 
ATOM   5146 C  CB   . VAL   A 1 685 ? 383.716 9.388   80.691  1.00 50.06  ? 664  VAL   A CB   1 
ATOM   5147 C  CG1  . VAL   A 1 685 ? 382.901 9.185   79.421  1.00 47.21  ? 664  VAL   A CG1  1 
ATOM   5148 C  CG2  . VAL   A 1 685 ? 383.095 10.458  81.570  1.00 50.18  ? 664  VAL   A CG2  1 
ATOM   5149 N  N    . PRO   A 1 686 ? 384.610 5.807   80.799  1.00 51.91  ? 665  PRO   A N    1 
ATOM   5150 C  CA   . PRO   A 1 686 ? 385.547 4.889   80.142  1.00 50.99  ? 665  PRO   A CA   1 
ATOM   5151 C  C    . PRO   A 1 686 ? 385.487 5.020   78.628  1.00 57.85  ? 665  PRO   A C    1 
ATOM   5152 O  O    . PRO   A 1 686 ? 384.490 5.458   78.050  1.00 60.49  ? 665  PRO   A O    1 
ATOM   5153 C  CB   . PRO   A 1 686 ? 385.073 3.501   80.595  1.00 45.60  ? 665  PRO   A CB   1 
ATOM   5154 C  CG   . PRO   A 1 686 ? 384.148 3.750   81.755  1.00 41.71  ? 665  PRO   A CG   1 
ATOM   5155 C  CD   . PRO   A 1 686 ? 383.527 5.086   81.485  1.00 44.47  ? 665  PRO   A CD   1 
ATOM   5156 N  N    . SER   A 1 687 ? 386.582 4.623   77.984  1.00 56.88  ? 666  SER   A N    1 
ATOM   5157 C  CA   . SER   A 1 687 ? 386.634 4.624   76.530  1.00 62.63  ? 666  SER   A CA   1 
ATOM   5158 C  C    . SER   A 1 687 ? 385.736 3.530   75.957  1.00 69.38  ? 666  SER   A C    1 
ATOM   5159 O  O    . SER   A 1 687 ? 385.515 2.487   76.577  1.00 70.88  ? 666  SER   A O    1 
ATOM   5160 C  CB   . SER   A 1 687 ? 388.072 4.430   76.049  1.00 63.94  ? 666  SER   A CB   1 
ATOM   5161 O  OG   . SER   A 1 687 ? 388.901 5.498   76.478  1.00 72.70  ? 666  SER   A OG   1 
ATOM   5162 N  N    . ARG   A 1 688 ? 385.218 3.781   74.756  1.00 76.93  ? 667  ARG   A N    1 
ATOM   5163 C  CA   . ARG   A 1 688 ? 384.316 2.843   74.088  1.00 72.44  ? 667  ARG   A CA   1 
ATOM   5164 C  C    . ARG   A 1 688 ? 385.079 1.748   73.347  1.00 72.28  ? 667  ARG   A C    1 
ATOM   5165 O  O    . ARG   A 1 688 ? 386.239 1.925   72.974  1.00 78.89  ? 667  ARG   A O    1 
ATOM   5166 C  CB   . ARG   A 1 688 ? 383.400 3.585   73.111  1.00 63.95  ? 667  ARG   A CB   1 
HETATM 5167 CA CA   . CA    B 2 .   ? 374.890 -6.788  103.498 1.00 56.46  2 701  CA    A CA   1 
HETATM 5168 CA CA   . CA    C 2 .   ? 373.574 -9.499  101.328 1.00 43.41  2 702  CA    A CA   1 
HETATM 5169 CA CA   . CA    D 2 .   ? 369.640 -14.995 98.637  1.00 64.02  2 703  CA    A CA   1 
HETATM 5170 CA CA   . CA    E 2 .   ? 366.891 9.171   92.988  1.00 60.22  2 704  CA    A CA   1 
HETATM 5171 C  C4   . A1A8O F 3 .   ? 388.495 -14.434 88.770  1.00 36.58  ? 705  A1A8O A C4   1 
HETATM 5172 C  C6   . A1A8O F 3 .   ? 387.986 -14.199 86.432  1.00 36.65  ? 705  A1A8O A C6   1 
HETATM 5173 C  C13  . A1A8O F 3 .   ? 383.146 -13.925 89.565  1.00 38.70  ? 705  A1A8O A C13  1 
HETATM 5174 C  C20  . A1A8O F 3 .   ? 379.248 -15.421 93.189  1.00 47.84  ? 705  A1A8O A C20  1 
HETATM 5175 C  C21  . A1A8O F 3 .   ? 378.389 -14.215 93.260  1.00 48.26  ? 705  A1A8O A C21  1 
HETATM 5176 C  C8   . A1A8O F 3 .   ? 386.262 -14.676 87.856  1.00 35.75  ? 705  A1A8O A C8   1 
HETATM 5177 C  C16  . A1A8O F 3 .   ? 380.091 -13.790 90.048  1.00 39.94  ? 705  A1A8O A C16  1 
HETATM 5178 O  O17  . A1A8O F 3 .   ? 379.966 -12.660 89.617  1.00 39.37  ? 705  A1A8O A O17  1 
HETATM 5179 C  C19  . A1A8O F 3 .   ? 379.693 -15.527 91.745  1.00 46.63  ? 705  A1A8O A C19  1 
HETATM 5180 C  C26  . A1A8O F 3 .   ? 390.784 -14.029 89.697  1.00 39.66  ? 705  A1A8O A C26  1 
HETATM 5181 C  C1   . A1A8O F 3 .   ? 387.605 -14.997 91.363  1.00 39.81  ? 705  A1A8O A C1   1 
HETATM 5182 C  C10  . A1A8O F 3 .   ? 383.980 -14.953 86.995  1.00 38.34  ? 705  A1A8O A C10  1 
HETATM 5183 C  C11  . A1A8O F 3 .   ? 382.645 -15.374 87.576  1.00 43.98  ? 705  A1A8O A C11  1 
HETATM 5184 C  C12  . A1A8O F 3 .   ? 382.088 -14.318 88.541  1.00 42.94  ? 705  A1A8O A C12  1 
HETATM 5185 C  C14  . A1A8O F 3 .   ? 384.428 -13.546 88.844  1.00 39.59  ? 705  A1A8O A C14  1 
HETATM 5186 C  C15  . A1A8O F 3 .   ? 380.862 -14.850 89.263  1.00 48.69  ? 705  A1A8O A C15  1 
HETATM 5187 C  C2   . A1A8O F 3 .   ? 386.717 -15.027 90.333  1.00 37.30  ? 705  A1A8O A C2   1 
HETATM 5188 C  C22  . A1A8O F 3 .   ? 378.878 -13.279 92.172  1.00 45.06  ? 705  A1A8O A C22  1 
HETATM 5189 C  C24  . A1A8O F 3 .   ? 389.400 -14.394 89.873  1.00 38.40  ? 705  A1A8O A C24  1 
HETATM 5190 C  C25  . A1A8O F 3 .   ? 388.931 -14.676 91.136  1.00 37.95  ? 705  A1A8O A C25  1 
HETATM 5191 C  C27  . A1A8O F 3 .   ? 391.143 -12.741 89.340  1.00 34.49  ? 705  A1A8O A C27  1 
HETATM 5192 C  C28  . A1A8O F 3 .   ? 392.483 -12.433 89.197  1.00 31.90  ? 705  A1A8O A C28  1 
HETATM 5193 C  C29  . A1A8O F 3 .   ? 393.407 -13.430 89.419  1.00 36.34  ? 705  A1A8O A C29  1 
HETATM 5194 C  C3   . A1A8O F 3 .   ? 387.128 -14.733 89.008  1.00 41.60  ? 705  A1A8O A C3   1 
HETATM 5195 C  C30  . A1A8O F 3 .   ? 392.993 -14.689 89.769  1.00 38.55  ? 705  A1A8O A C30  1 
HETATM 5196 C  C5   . A1A8O F 3 .   ? 388.902 -14.169 87.438  1.00 36.76  ? 705  A1A8O A C5   1 
HETATM 5197 N  N18  . A1A8O F 3 .   ? 379.574 -14.159 91.231  1.00 41.57  ? 705  A1A8O A N18  1 
HETATM 5198 N  N23  . A1A8O F 3 .   ? 379.872 -15.278 88.419  1.00 42.13  ? 705  A1A8O A N23  1 
HETATM 5199 N  N31  . A1A8O F 3 .   ? 391.698 -14.993 89.907  1.00 40.24  ? 705  A1A8O A N31  1 
HETATM 5200 N  N7   . A1A8O F 3 .   ? 386.680 -14.442 86.608  1.00 34.14  ? 705  A1A8O A N7   1 
HETATM 5201 N  N9   . A1A8O F 3 .   ? 384.922 -14.688 88.079  1.00 35.29  ? 705  A1A8O A N9   1 
HETATM 5202 CL CL1  . A1A8O F 3 .   ? 395.101 -13.067 89.244  1.00 42.34  ? 705  A1A8O A CL1  1 
HETATM 5203 CL CL2  . A1A8O F 3 .   ? 389.972 -11.491 89.071  1.00 36.43  ? 705  A1A8O A CL2  1 
HETATM 5204 H  H1   . A1A8O F 3 .   ? 388.266 -14.022 85.394  1.00 44.60  ? 705  A1A8O A H1   1 
HETATM 5205 H  H2   . A1A8O F 3 .   ? 382.815 -13.088 90.178  1.00 47.06  ? 705  A1A8O A H2   1 
HETATM 5206 H  H3   . A1A8O F 3 .   ? 383.349 -14.738 90.261  1.00 47.06  ? 705  A1A8O A H3   1 
HETATM 5207 H  H4   . A1A8O F 3 .   ? 378.716 -16.317 93.508  1.00 58.03  ? 705  A1A8O A H4   1 
HETATM 5208 H  H5   . A1A8O F 3 .   ? 380.100 -15.353 93.864  1.00 58.03  ? 705  A1A8O A H5   1 
HETATM 5209 H  H6   . A1A8O F 3 .   ? 377.337 -14.463 93.129  1.00 58.53  ? 705  A1A8O A H6   1 
HETATM 5210 H  H7   . A1A8O F 3 .   ? 378.438 -13.744 94.241  1.00 58.53  ? 705  A1A8O A H7   1 
HETATM 5211 H  H8   . A1A8O F 3 .   ? 379.078 -16.220 91.174  1.00 56.57  ? 705  A1A8O A H8   1 
HETATM 5212 H  H9   . A1A8O F 3 .   ? 380.714 -15.896 91.655  1.00 56.57  ? 705  A1A8O A H9   1 
HETATM 5213 H  H10  . A1A8O F 3 .   ? 387.274 -15.226 92.375  1.00 48.39  ? 705  A1A8O A H10  1 
HETATM 5214 H  H11  . A1A8O F 3 .   ? 383.836 -14.081 86.358  1.00 46.62  ? 705  A1A8O A H11  1 
HETATM 5215 H  H12  . A1A8O F 3 .   ? 384.341 -15.730 86.323  1.00 46.62  ? 705  A1A8O A H12  1 
HETATM 5216 H  H13  . A1A8O F 3 .   ? 381.963 -15.564 86.749  1.00 53.40  ? 705  A1A8O A H13  1 
HETATM 5217 H  H14  . A1A8O F 3 .   ? 382.780 -16.336 88.068  1.00 53.40  ? 705  A1A8O A H14  1 
HETATM 5218 H  H15  . A1A8O F 3 .   ? 381.826 -13.440 87.953  1.00 52.15  ? 705  A1A8O A H15  1 
HETATM 5219 H  H16  . A1A8O F 3 .   ? 385.186 -13.211 89.550  1.00 48.12  ? 705  A1A8O A H16  1 
HETATM 5220 H  H17  . A1A8O F 3 .   ? 384.267 -12.695 88.185  1.00 48.12  ? 705  A1A8O A H17  1 
HETATM 5221 H  H18  . A1A8O F 3 .   ? 381.233 -15.667 89.879  1.00 59.04  ? 705  A1A8O A H18  1 
HETATM 5222 H  H19  . A1A8O F 3 .   ? 385.671 -15.278 90.505  1.00 45.38  ? 705  A1A8O A H19  1 
HETATM 5223 H  H20  . A1A8O F 3 .   ? 379.551 -12.510 92.545  1.00 54.70  ? 705  A1A8O A H20  1 
HETATM 5224 H  H21  . A1A8O F 3 .   ? 378.067 -12.750 91.672  1.00 54.70  ? 705  A1A8O A H21  1 
HETATM 5225 H  H22  . A1A8O F 3 .   ? 389.615 -14.647 91.983  1.00 46.15  ? 705  A1A8O A H22  1 
HETATM 5226 H  H23  . A1A8O F 3 .   ? 392.802 -11.430 88.916  1.00 38.90  ? 705  A1A8O A H23  1 
HETATM 5227 H  H24  . A1A8O F 3 .   ? 393.696 -15.500 89.951  1.00 46.88  ? 705  A1A8O A H24  1 
HETATM 5228 H  H25  . A1A8O F 3 .   ? 389.944 -13.941 87.219  1.00 44.73  ? 705  A1A8O A H25  1 
HETATM 5229 H  H27  . A1A8O F 3 .   ? 380.087 -15.184 87.431  1.00 51.17  ? 705  A1A8O A H27  1 
HETATM 5230 H  H23B . A1A8O F 3 .   ? 379.044 -15.637 88.884  1.00 51.17  ? 705  A1A8O A H23B 1 
HETATM 5231 O  O    . HOH   G 4 .   ? 346.590 1.454   91.217  1.00 44.77  ? 801  HOH   A O    1 
HETATM 5232 O  O    . HOH   G 4 .   ? 385.127 -14.534 84.081  1.00 39.28  ? 802  HOH   A O    1 
HETATM 5233 O  O    . HOH   G 4 .   ? 392.325 -4.553  95.738  1.00 38.43  ? 803  HOH   A O    1 
HETATM 5234 O  O    . HOH   G 4 .   ? 331.091 -3.660  71.381  1.00 63.56  ? 804  HOH   A O    1 
HETATM 5235 O  O    . HOH   G 4 .   ? 370.223 7.302   81.178  1.00 36.81  ? 805  HOH   A O    1 
HETATM 5236 O  O    . HOH   G 4 .   ? 385.914 -13.829 81.628  1.00 44.69  ? 806  HOH   A O    1 
HETATM 5237 O  O    . HOH   G 4 .   ? 437.608 -14.497 84.961  1.00 57.78  ? 807  HOH   A O    1 
HETATM 5238 O  O    . HOH   G 4 .   ? 394.760 -4.237  96.339  1.00 46.71  ? 808  HOH   A O    1 
HETATM 5239 O  O    . HOH   G 4 .   ? 400.970 5.475   109.129 1.00 49.06  ? 809  HOH   A O    1 
HETATM 5240 O  O    . HOH   G 4 .   ? 398.919 -2.521  94.378  1.00 45.29  ? 810  HOH   A O    1 
HETATM 5241 O  O    . HOH   G 4 .   ? 369.142 -14.672 96.359  1.00 52.90  ? 811  HOH   A O    1 
HETATM 5242 O  O    . HOH   G 4 .   ? 344.373 15.653  72.059  1.00 47.40  ? 812  HOH   A O    1 
HETATM 5243 O  O    . HOH   G 4 .   ? 394.171 -6.879  98.474  1.00 47.32  ? 813  HOH   A O    1 
HETATM 5244 O  O    . HOH   G 4 .   ? 358.674 -9.207  111.170 1.00 47.63  ? 814  HOH   A O    1 
HETATM 5245 O  O    . HOH   G 4 .   ? 342.406 13.793  81.788  1.00 44.98  ? 815  HOH   A O    1 
HETATM 5246 O  O    . HOH   G 4 .   ? 364.256 6.331   79.932  1.00 37.28  ? 816  HOH   A O    1 
HETATM 5247 O  O    . HOH   G 4 .   ? 326.304 15.401  56.605  1.00 54.61  ? 817  HOH   A O    1 
HETATM 5248 O  O    . HOH   G 4 .   ? 412.083 5.008   109.375 1.00 51.08  ? 818  HOH   A O    1 
HETATM 5249 O  O    . HOH   G 4 .   ? 402.877 -14.421 74.989  1.00 45.65  ? 819  HOH   A O    1 
HETATM 5250 O  O    . HOH   G 4 .   ? 347.612 -7.341  87.013  1.00 39.46  ? 820  HOH   A O    1 
HETATM 5251 O  O    . HOH   G 4 .   ? 420.241 -3.096  109.775 1.00 51.02  ? 821  HOH   A O    1 
HETATM 5252 O  O    . HOH   G 4 .   ? 403.702 -3.350  98.063  1.00 43.91  ? 822  HOH   A O    1 
HETATM 5253 O  O    . HOH   G 4 .   ? 363.228 -15.481 100.110 1.00 50.61  ? 823  HOH   A O    1 
HETATM 5254 O  O    . HOH   G 4 .   ? 411.178 5.440   79.303  1.00 39.37  ? 824  HOH   A O    1 
HETATM 5255 O  O    . HOH   G 4 .   ? 410.875 0.424   76.010  1.00 32.91  ? 825  HOH   A O    1 
HETATM 5256 O  O    . HOH   G 4 .   ? 379.121 -2.669  85.207  1.00 28.43  ? 826  HOH   A O    1 
HETATM 5257 O  O    . HOH   G 4 .   ? 427.923 -10.490 89.735  1.00 47.72  ? 827  HOH   A O    1 
HETATM 5258 O  O    . HOH   G 4 .   ? 330.960 18.013  67.154  1.00 43.80  ? 828  HOH   A O    1 
HETATM 5259 O  O    . HOH   G 4 .   ? 344.259 3.767   59.108  1.00 44.33  ? 829  HOH   A O    1 
HETATM 5260 O  O    . HOH   G 4 .   ? 435.181 -8.900  93.837  1.00 47.27  ? 830  HOH   A O    1 
HETATM 5261 O  O    . HOH   G 4 .   ? 365.589 -8.434  81.020  1.00 31.45  ? 831  HOH   A O    1 
HETATM 5262 O  O    . HOH   G 4 .   ? 380.387 -6.477  108.881 1.00 55.29  ? 832  HOH   A O    1 
HETATM 5263 O  O    . HOH   G 4 .   ? 350.864 11.020  63.919  1.00 45.31  ? 833  HOH   A O    1 
HETATM 5264 O  O    . HOH   G 4 .   ? 380.505 -12.365 85.860  1.00 36.32  ? 834  HOH   A O    1 
HETATM 5265 O  O    . HOH   G 4 .   ? 399.087 -0.011  94.359  1.00 27.26  ? 835  HOH   A O    1 
HETATM 5266 O  O    . HOH   G 4 .   ? 405.340 -5.268  94.901  1.00 36.13  ? 836  HOH   A O    1 
HETATM 5267 O  O    . HOH   G 4 .   ? 336.528 4.300   62.481  1.00 52.49  ? 837  HOH   A O    1 
HETATM 5268 O  O    . HOH   G 4 .   ? 391.126 -3.044  99.871  1.00 32.20  ? 838  HOH   A O    1 
HETATM 5269 O  O    . HOH   G 4 .   ? 378.099 4.241   98.291  1.00 48.52  ? 839  HOH   A O    1 
HETATM 5270 O  O    . HOH   G 4 .   ? 381.646 -1.082  92.366  1.00 26.15  ? 840  HOH   A O    1 
HETATM 5271 O  O    . HOH   G 4 .   ? 388.329 -3.820  100.190 1.00 32.56  ? 841  HOH   A O    1 
HETATM 5272 O  O    . HOH   G 4 .   ? 398.938 11.913  92.318  1.00 46.36  ? 842  HOH   A O    1 
HETATM 5273 O  O    . HOH   G 4 .   ? 396.005 1.874   77.486  1.00 46.96  ? 843  HOH   A O    1 
HETATM 5274 O  O    . HOH   G 4 .   ? 325.656 21.438  63.566  1.00 44.42  ? 844  HOH   A O    1 
HETATM 5275 O  O    . HOH   G 4 .   ? 342.961 5.092   65.046  1.00 41.47  ? 845  HOH   A O    1 
HETATM 5276 O  O    . HOH   G 4 .   ? 372.431 -11.469 80.317  1.00 43.49  ? 846  HOH   A O    1 
HETATM 5277 O  O    . HOH   G 4 .   ? 385.089 4.684   94.866  1.00 43.46  ? 847  HOH   A O    1 
HETATM 5278 O  O    . HOH   G 4 .   ? 425.330 -0.600  88.398  1.00 45.16  ? 848  HOH   A O    1 
HETATM 5279 O  O    . HOH   G 4 .   ? 388.343 -2.657  88.142  1.00 23.70  ? 849  HOH   A O    1 
HETATM 5280 O  O    . HOH   G 4 .   ? 356.032 7.525   88.918  1.00 37.21  ? 850  HOH   A O    1 
HETATM 5281 O  O    . HOH   G 4 .   ? 354.141 8.303   86.497  1.00 50.60  ? 851  HOH   A O    1 
HETATM 5282 O  O    . HOH   G 4 .   ? 435.331 -8.734  91.098  1.00 53.35  ? 852  HOH   A O    1 
HETATM 5283 O  O    . HOH   G 4 .   ? 398.165 3.490   102.297 1.00 37.02  ? 853  HOH   A O    1 
HETATM 5284 O  O    . HOH   G 4 .   ? 424.514 1.279   102.582 1.00 47.51  ? 854  HOH   A O    1 
HETATM 5285 O  O    . HOH   G 4 .   ? 342.419 19.190  73.689  1.00 52.50  ? 855  HOH   A O    1 
HETATM 5286 O  O    . HOH   G 4 .   ? 391.316 -9.365  77.483  1.00 50.17  ? 856  HOH   A O    1 
HETATM 5287 O  O    . HOH   G 4 .   ? 419.038 2.068   89.069  1.00 39.78  ? 857  HOH   A O    1 
HETATM 5288 O  O    . HOH   G 4 .   ? 328.079 13.566  68.675  1.00 50.40  ? 858  HOH   A O    1 
HETATM 5289 O  O    . HOH   G 4 .   ? 341.586 7.950   59.264  1.00 48.53  ? 859  HOH   A O    1 
HETATM 5290 O  O    . HOH   G 4 .   ? 336.225 12.570  81.836  1.00 51.34  ? 860  HOH   A O    1 
HETATM 5291 O  O    . HOH   G 4 .   ? 434.588 -1.460  93.732  1.00 43.79  ? 861  HOH   A O    1 
HETATM 5292 O  O    . HOH   G 4 .   ? 343.159 -1.407  75.011  1.00 43.82  ? 862  HOH   A O    1 
HETATM 5293 O  O    . HOH   G 4 .   ? 327.737 16.334  69.043  1.00 56.85  ? 863  HOH   A O    1 
HETATM 5294 O  O    . HOH   G 4 .   ? 378.744 -1.280  79.051  1.00 50.47  ? 864  HOH   A O    1 
HETATM 5295 O  O    . HOH   G 4 .   ? 354.442 1.444   75.421  1.00 31.98  ? 865  HOH   A O    1 
HETATM 5296 O  O    . HOH   G 4 .   ? 397.075 10.142  92.069  1.00 39.30  ? 866  HOH   A O    1 
HETATM 5297 O  O    . HOH   G 4 .   ? 321.895 12.003  59.274  1.00 49.91  ? 867  HOH   A O    1 
HETATM 5298 O  O    . HOH   G 4 .   ? 372.933 -5.422  104.478 1.00 46.05  ? 868  HOH   A O    1 
HETATM 5299 O  O    . HOH   G 4 .   ? 394.806 -18.541 90.214  1.00 46.41  ? 869  HOH   A O    1 
HETATM 5300 O  O    . HOH   G 4 .   ? 329.435 3.143   63.066  1.00 51.98  ? 870  HOH   A O    1 
HETATM 5301 O  O    . HOH   G 4 .   ? 378.493 -5.020  92.161  1.00 28.81  ? 871  HOH   A O    1 
HETATM 5302 O  O    . HOH   G 4 .   ? 415.405 9.553   97.558  1.00 46.45  ? 872  HOH   A O    1 
HETATM 5303 O  O    . HOH   G 4 .   ? 351.009 -13.346 90.373  1.00 46.10  ? 873  HOH   A O    1 
HETATM 5304 O  O    . HOH   G 4 .   ? 368.020 3.261   85.191  1.00 28.92  ? 874  HOH   A O    1 
HETATM 5305 O  O    . HOH   G 4 .   ? 404.015 12.315  86.392  1.00 42.39  ? 875  HOH   A O    1 
HETATM 5306 O  O    . HOH   G 4 .   ? 390.444 9.666   92.302  1.00 35.61  ? 876  HOH   A O    1 
HETATM 5307 O  O    . HOH   G 4 .   ? 395.976 -2.960  99.524  1.00 43.33  ? 877  HOH   A O    1 
HETATM 5308 O  O    . HOH   G 4 .   ? 416.549 6.454   89.952  1.00 50.65  ? 878  HOH   A O    1 
HETATM 5309 O  O    . HOH   G 4 .   ? 352.464 -11.437 74.989  1.00 46.08  ? 879  HOH   A O    1 
HETATM 5310 O  O    . HOH   G 4 .   ? 330.527 8.969   86.150  1.00 57.04  ? 880  HOH   A O    1 
HETATM 5311 O  O    . HOH   G 4 .   ? 417.330 -0.408  109.338 1.00 53.89  ? 881  HOH   A O    1 
HETATM 5312 O  O    . HOH   G 4 .   ? 339.311 8.803   60.868  1.00 37.04  ? 882  HOH   A O    1 
HETATM 5313 O  O    . HOH   G 4 .   ? 390.462 4.455   86.553  1.00 28.68  ? 883  HOH   A O    1 
HETATM 5314 O  O    . HOH   G 4 .   ? 388.029 0.589   80.289  1.00 38.11  ? 884  HOH   A O    1 
HETATM 5315 O  O    . HOH   G 4 .   ? 365.919 11.063  93.435  1.00 40.28  ? 885  HOH   A O    1 
HETATM 5316 O  O    . HOH   G 4 .   ? 397.077 -7.538  93.873  1.00 41.91  ? 886  HOH   A O    1 
HETATM 5317 O  O    . HOH   G 4 .   ? 428.737 0.370   88.692  1.00 47.61  ? 887  HOH   A O    1 
HETATM 5318 O  O    . HOH   G 4 .   ? 396.778 -2.786  96.403  1.00 42.86  ? 888  HOH   A O    1 
HETATM 5319 O  O    . HOH   G 4 .   ? 377.374 -12.398 75.352  1.00 52.98  ? 889  HOH   A O    1 
HETATM 5320 O  O    . HOH   G 4 .   ? 364.870 -7.597  78.674  1.00 33.27  ? 890  HOH   A O    1 
HETATM 5321 O  O    . HOH   G 4 .   ? 393.003 -1.153  79.137  1.00 38.70  ? 891  HOH   A O    1 
HETATM 5322 O  O    . HOH   G 4 .   ? 406.986 -10.207 70.484  1.00 42.47  ? 892  HOH   A O    1 
HETATM 5323 O  O    . HOH   G 4 .   ? 369.770 -12.719 98.586  1.00 47.71  ? 893  HOH   A O    1 
HETATM 5324 O  O    . HOH   G 4 .   ? 408.036 5.392   78.290  1.00 36.65  ? 894  HOH   A O    1 
HETATM 5325 O  O    . HOH   G 4 .   ? 399.235 -11.640 81.244  1.00 35.41  ? 895  HOH   A O    1 
HETATM 5326 O  O    . HOH   G 4 .   ? 405.861 11.714  92.392  1.00 38.16  ? 896  HOH   A O    1 
HETATM 5327 O  O    . HOH   G 4 .   ? 354.989 10.930  69.313  1.00 61.26  ? 897  HOH   A O    1 
HETATM 5328 O  O    . HOH   G 4 .   ? 395.583 6.703   77.841  1.00 53.24  ? 898  HOH   A O    1 
HETATM 5329 O  O    . HOH   G 4 .   ? 387.144 -1.030  100.647 1.00 37.21  ? 899  HOH   A O    1 
HETATM 5330 O  O    . HOH   G 4 .   ? 370.879 3.824   93.955  1.00 35.94  ? 900  HOH   A O    1 
HETATM 5331 O  O    . HOH   G 4 .   ? 331.497 18.724  70.269  1.00 57.60  ? 901  HOH   A O    1 
HETATM 5332 O  O    . HOH   G 4 .   ? 414.047 0.167   77.645  1.00 33.87  ? 902  HOH   A O    1 
HETATM 5333 O  O    . HOH   G 4 .   ? 391.035 -18.280 80.043  1.00 45.61  ? 903  HOH   A O    1 
HETATM 5334 O  O    . HOH   G 4 .   ? 415.136 -0.323  87.764  1.00 26.53  ? 904  HOH   A O    1 
HETATM 5335 O  O    . HOH   G 4 .   ? 403.672 -12.608 94.708  1.00 54.62  ? 905  HOH   A O    1 
HETATM 5336 O  O    . HOH   G 4 .   ? 391.634 15.381  81.938  1.00 64.09  ? 906  HOH   A O    1 
HETATM 5337 O  O    . HOH   G 4 .   ? 367.235 -21.873 94.869  1.00 63.44  ? 907  HOH   A O    1 
HETATM 5338 O  O    . HOH   G 4 .   ? 347.669 3.999   76.106  1.00 32.92  ? 908  HOH   A O    1 
HETATM 5339 O  O    . HOH   G 4 .   ? 383.159 6.078   97.425  1.00 46.04  ? 909  HOH   A O    1 
HETATM 5340 O  O    . HOH   G 4 .   ? 401.644 -8.122  96.062  1.00 55.15  ? 910  HOH   A O    1 
HETATM 5341 O  O    . HOH   G 4 .   ? 397.035 -9.302  97.179  1.00 49.09  ? 911  HOH   A O    1 
HETATM 5342 O  O    . HOH   G 4 .   ? 406.607 14.445  88.642  1.00 51.60  ? 912  HOH   A O    1 
HETATM 5343 O  O    . HOH   G 4 .   ? 344.922 -13.109 74.283  1.00 52.71  ? 913  HOH   A O    1 
HETATM 5344 O  O    . HOH   G 4 .   ? 353.851 6.818   80.420  1.00 40.73  ? 914  HOH   A O    1 
HETATM 5345 O  O    . HOH   G 4 .   ? 377.175 -15.237 88.380  1.00 40.35  ? 915  HOH   A O    1 
HETATM 5346 O  O    . HOH   G 4 .   ? 317.276 16.934  60.177  1.00 45.40  ? 916  HOH   A O    1 
HETATM 5347 O  O    . HOH   G 4 .   ? 402.981 -9.946  101.537 1.00 59.16  ? 917  HOH   A O    1 
HETATM 5348 O  O    . HOH   G 4 .   ? 385.459 0.512   78.776  1.00 49.28  ? 918  HOH   A O    1 
HETATM 5349 O  O    . HOH   G 4 .   ? 339.433 -0.905  68.004  1.00 46.74  ? 919  HOH   A O    1 
HETATM 5350 O  O    . HOH   G 4 .   ? 433.725 4.354   96.869  1.00 53.19  ? 920  HOH   A O    1 
HETATM 5351 O  O    . HOH   G 4 .   ? 427.595 -20.377 105.599 1.00 56.18  ? 921  HOH   A O    1 
HETATM 5352 O  O    . HOH   G 4 .   ? 418.849 -6.866  106.430 1.00 47.32  ? 922  HOH   A O    1 
HETATM 5353 O  O    . HOH   G 4 .   ? 350.002 2.531   75.765  1.00 30.80  ? 923  HOH   A O    1 
HETATM 5354 O  O    . HOH   G 4 .   ? 373.825 -16.506 88.555  1.00 46.06  ? 924  HOH   A O    1 
HETATM 5355 O  O    . HOH   G 4 .   ? 371.679 -16.119 80.768  1.00 50.71  ? 925  HOH   A O    1 
HETATM 5356 O  O    . HOH   G 4 .   ? 399.962 -7.454  94.203  1.00 47.60  ? 926  HOH   A O    1 
HETATM 5357 O  O    . HOH   G 4 .   ? 348.818 11.378  78.983  1.00 48.72  ? 927  HOH   A O    1 
HETATM 5358 O  O    . HOH   G 4 .   ? 381.705 -4.755  80.688  1.00 34.28  ? 928  HOH   A O    1 
HETATM 5359 O  O    . HOH   G 4 .   ? 367.302 -14.655 90.492  1.00 37.26  ? 929  HOH   A O    1 
HETATM 5360 O  O    . HOH   G 4 .   ? 436.802 -3.970  100.156 1.00 47.11  ? 930  HOH   A O    1 
HETATM 5361 O  O    . HOH   G 4 .   ? 386.171 -8.329  78.705  1.00 34.83  ? 931  HOH   A O    1 
HETATM 5362 O  O    . HOH   G 4 .   ? 371.090 4.104   91.656  1.00 33.78  ? 932  HOH   A O    1 
HETATM 5363 O  O    . HOH   G 4 .   ? 360.861 3.343   80.285  1.00 34.30  ? 933  HOH   A O    1 
HETATM 5364 O  O    . HOH   G 4 .   ? 360.902 7.664   81.989  1.00 38.84  ? 934  HOH   A O    1 
HETATM 5365 O  O    . HOH   G 4 .   ? 411.192 -20.663 84.490  1.00 46.82  ? 935  HOH   A O    1 
HETATM 5366 O  O    . HOH   G 4 .   ? 361.655 -13.204 108.103 1.00 63.56  ? 936  HOH   A O    1 
HETATM 5367 O  O    . HOH   G 4 .   ? 435.959 -12.918 87.809  1.00 54.91  ? 937  HOH   A O    1 
HETATM 5368 O  O    . HOH   G 4 .   ? 355.180 5.760   82.666  1.00 42.76  ? 938  HOH   A O    1 
HETATM 5369 O  O    . HOH   G 4 .   ? 390.773 -8.795  114.914 1.00 60.39  ? 939  HOH   A O    1 
HETATM 5370 O  O    . HOH   G 4 .   ? 406.024 -11.788 95.306  1.00 60.08  ? 940  HOH   A O    1 
HETATM 5371 O  O    . HOH   G 4 .   ? 416.057 -8.575  95.680  1.00 34.63  ? 941  HOH   A O    1 
HETATM 5372 O  O    . HOH   G 4 .   ? 352.961 7.294   93.783  1.00 46.87  ? 942  HOH   A O    1 
HETATM 5373 O  O    . HOH   G 4 .   ? 415.044 -2.427  78.095  1.00 33.85  ? 943  HOH   A O    1 
HETATM 5374 O  O    . HOH   G 4 .   ? 422.581 -4.075  86.214  1.00 36.76  ? 944  HOH   A O    1 
HETATM 5375 O  O    . HOH   G 4 .   ? 376.117 2.279   79.731  1.00 36.34  ? 945  HOH   A O    1 
HETATM 5376 O  O    . HOH   G 4 .   ? 410.731 9.727   107.088 1.00 53.58  ? 946  HOH   A O    1 
HETATM 5377 O  O    . HOH   G 4 .   ? 382.935 11.376  92.537  1.00 40.80  ? 947  HOH   A O    1 
HETATM 5378 O  O    . HOH   G 4 .   ? 372.066 -3.037  94.857  1.00 35.09  ? 948  HOH   A O    1 
HETATM 5379 O  O    . HOH   G 4 .   ? 337.809 0.943   79.571  1.00 43.39  ? 949  HOH   A O    1 
HETATM 5380 O  O    . HOH   G 4 .   ? 335.828 5.894   82.621  1.00 47.93  ? 950  HOH   A O    1 
HETATM 5381 O  O    . HOH   G 4 .   ? 366.837 2.048   92.150  1.00 27.50  ? 951  HOH   A O    1 
HETATM 5382 O  O    . HOH   G 4 .   ? 377.231 -14.182 107.975 1.00 56.04  ? 952  HOH   A O    1 
HETATM 5383 O  O    . HOH   G 4 .   ? 333.744 2.353   68.114  1.00 45.11  ? 953  HOH   A O    1 
HETATM 5384 O  O    . HOH   G 4 .   ? 344.803 13.081  60.137  1.00 46.82  ? 954  HOH   A O    1 
HETATM 5385 O  O    . HOH   G 4 .   ? 371.394 -7.493  79.247  1.00 39.91  ? 955  HOH   A O    1 
HETATM 5386 O  O    . HOH   G 4 .   ? 351.375 -0.235  92.400  1.00 42.60  ? 956  HOH   A O    1 
HETATM 5387 O  O    . HOH   G 4 .   ? 362.548 6.724   88.293  1.00 34.81  ? 957  HOH   A O    1 
HETATM 5388 O  O    . HOH   G 4 .   ? 410.730 -15.389 90.279  1.00 31.23  ? 958  HOH   A O    1 
HETATM 5389 O  O    . HOH   G 4 .   ? 349.671 -0.398  72.299  1.00 40.94  ? 959  HOH   A O    1 
HETATM 5390 O  O    . HOH   G 4 .   ? 405.324 9.957   80.626  1.00 40.47  ? 960  HOH   A O    1 
HETATM 5391 O  O    . HOH   G 4 .   ? 388.833 -2.679  85.321  1.00 27.78  ? 961  HOH   A O    1 
HETATM 5392 O  O    . HOH   G 4 .   ? 403.989 -21.379 85.806  1.00 38.88  ? 962  HOH   A O    1 
HETATM 5393 O  O    . HOH   G 4 .   ? 407.199 2.179   109.412 1.00 49.64  ? 963  HOH   A O    1 
HETATM 5394 O  O    . HOH   G 4 .   ? 381.763 -6.863  79.103  1.00 34.09  ? 964  HOH   A O    1 
HETATM 5395 O  O    . HOH   G 4 .   ? 402.481 9.013   78.561  1.00 49.65  ? 965  HOH   A O    1 
HETATM 5396 O  O    . HOH   G 4 .   ? 408.820 -14.929 77.936  1.00 35.77  ? 966  HOH   A O    1 
HETATM 5397 O  O    . HOH   G 4 .   ? 366.587 -19.177 84.374  1.00 52.20  ? 967  HOH   A O    1 
HETATM 5398 O  O    . HOH   G 4 .   ? 399.683 10.731  98.722  1.00 50.34  ? 968  HOH   A O    1 
HETATM 5399 O  O    . HOH   G 4 .   ? 422.444 -18.140 87.685  1.00 53.14  ? 969  HOH   A O    1 
HETATM 5400 O  O    . HOH   G 4 .   ? 361.445 12.745  88.288  1.00 51.86  ? 970  HOH   A O    1 
HETATM 5401 O  O    . HOH   G 4 .   ? 394.020 -4.342  98.795  1.00 43.17  ? 971  HOH   A O    1 
HETATM 5402 O  O    . HOH   G 4 .   ? 375.033 -11.557 78.567  1.00 48.54  ? 972  HOH   A O    1 
HETATM 5403 O  O    . HOH   G 4 .   ? 368.578 -9.451  77.466  1.00 39.35  ? 973  HOH   A O    1 
HETATM 5404 O  O    . HOH   G 4 .   ? 346.985 11.770  65.078  1.00 43.97  ? 974  HOH   A O    1 
HETATM 5405 O  O    . HOH   G 4 .   ? 351.566 6.265   83.372  1.00 32.52  ? 975  HOH   A O    1 
HETATM 5406 O  O    . HOH   G 4 .   ? 339.049 18.808  74.069  1.00 42.60  ? 976  HOH   A O    1 
HETATM 5407 O  O    . HOH   G 4 .   ? 392.374 -20.054 99.196  1.00 43.17  ? 977  HOH   A O    1 
HETATM 5408 O  O    . HOH   G 4 .   ? 436.396 -6.061  103.289 1.00 48.36  ? 978  HOH   A O    1 
HETATM 5409 O  O    . HOH   G 4 .   ? 400.908 -2.856  77.613  1.00 37.09  ? 979  HOH   A O    1 
HETATM 5410 O  O    . HOH   G 4 .   ? 396.101 -16.434 78.062  1.00 47.94  ? 980  HOH   A O    1 
HETATM 5411 O  O    . HOH   G 4 .   ? 383.427 4.161   93.630  1.00 43.38  ? 981  HOH   A O    1 
HETATM 5412 O  O    . HOH   G 4 .   ? 413.654 -14.384 80.351  1.00 39.13  ? 982  HOH   A O    1 
HETATM 5413 O  O    . HOH   G 4 .   ? 372.196 -6.645  95.535  1.00 32.53  ? 983  HOH   A O    1 
HETATM 5414 O  O    . HOH   G 4 .   ? 341.914 -0.235  67.533  1.00 39.74  ? 984  HOH   A O    1 
HETATM 5415 O  O    . HOH   G 4 .   ? 367.624 -1.064  99.704  1.00 39.72  ? 985  HOH   A O    1 
HETATM 5416 O  O    . HOH   G 4 .   ? 352.776 -14.516 88.375  1.00 43.72  ? 986  HOH   A O    1 
HETATM 5417 O  O    . HOH   G 4 .   ? 416.241 -3.705  110.876 1.00 47.56  ? 987  HOH   A O    1 
HETATM 5418 O  O    . HOH   G 4 .   ? 373.190 -18.870 99.755  1.00 58.03  ? 988  HOH   A O    1 
HETATM 5419 O  O    . HOH   G 4 .   ? 366.975 -20.784 96.567  1.00 57.64  ? 989  HOH   A O    1 
HETATM 5420 O  O    . HOH   G 4 .   ? 367.382 -13.816 76.465  1.00 36.28  ? 990  HOH   A O    1 
HETATM 5421 O  O    . HOH   G 4 .   ? 336.868 11.547  59.119  1.00 42.84  ? 991  HOH   A O    1 
HETATM 5422 O  O    . HOH   G 4 .   ? 318.262 13.402  59.737  1.00 46.63  ? 992  HOH   A O    1 
HETATM 5423 O  O    . HOH   G 4 .   ? 360.563 12.530  91.733  1.00 46.25  ? 993  HOH   A O    1 
HETATM 5424 O  O    . HOH   G 4 .   ? 368.119 -14.769 93.175  1.00 38.54  ? 994  HOH   A O    1 
HETATM 5425 O  O    . HOH   G 4 .   ? 413.625 0.121   85.651  1.00 27.17  ? 995  HOH   A O    1 
HETATM 5426 O  O    . HOH   G 4 .   ? 400.235 10.706  85.838  1.00 39.45  ? 996  HOH   A O    1 
HETATM 5427 O  O    . HOH   G 4 .   ? 377.936 6.830   78.678  1.00 31.87  ? 997  HOH   A O    1 
HETATM 5428 O  O    . HOH   G 4 .   ? 378.333 -14.270 81.922  1.00 53.63  ? 998  HOH   A O    1 
HETATM 5429 O  O    . HOH   G 4 .   ? 318.625 8.953   61.519  1.00 50.46  ? 999  HOH   A O    1 
HETATM 5430 O  O    . HOH   G 4 .   ? 357.190 -15.145 89.794  1.00 43.77  ? 1000 HOH   A O    1 
HETATM 5431 O  O    . HOH   G 4 .   ? 368.711 -6.265  79.092  1.00 42.07  ? 1001 HOH   A O    1 
HETATM 5432 O  O    . HOH   G 4 .   ? 407.086 -20.805 79.100  1.00 44.81  ? 1002 HOH   A O    1 
HETATM 5433 O  O    . HOH   G 4 .   ? 408.389 -12.592 76.611  1.00 35.98  ? 1003 HOH   A O    1 
HETATM 5434 O  O    . HOH   G 4 .   ? 355.845 8.114   81.337  1.00 53.40  ? 1004 HOH   A O    1 
HETATM 5435 O  O    . HOH   G 4 .   ? 351.646 -9.090  92.964  1.00 46.57  ? 1005 HOH   A O    1 
HETATM 5436 O  O    . HOH   G 4 .   ? 415.205 -6.054  96.504  1.00 32.61  ? 1006 HOH   A O    1 
HETATM 5437 O  O    . HOH   G 4 .   ? 356.335 -5.948  75.664  1.00 44.44  ? 1007 HOH   A O    1 
HETATM 5438 O  O    . HOH   G 4 .   ? 409.271 -9.925  98.830  1.00 45.44  ? 1008 HOH   A O    1 
HETATM 5439 O  O    . HOH   G 4 .   ? 346.449 10.946  87.586  1.00 42.81  ? 1009 HOH   A O    1 
HETATM 5440 O  O    . HOH   G 4 .   ? 408.656 -0.930  76.729  1.00 36.66  ? 1010 HOH   A O    1 
HETATM 5441 O  O    . HOH   G 4 .   ? 400.171 -19.005 79.357  1.00 41.01  ? 1011 HOH   A O    1 
HETATM 5442 O  O    . HOH   G 4 .   ? 398.339 -7.487  98.524  1.00 54.92  ? 1012 HOH   A O    1 
HETATM 5443 O  O    . HOH   G 4 .   ? 394.448 -5.071  115.981 1.00 56.70  ? 1013 HOH   A O    1 
HETATM 5444 O  O    . HOH   G 4 .   ? 335.342 -1.108  61.853  1.00 52.96  ? 1014 HOH   A O    1 
HETATM 5445 O  O    . HOH   G 4 .   ? 363.082 5.400   97.571  1.00 46.32  ? 1015 HOH   A O    1 
HETATM 5446 O  O    . HOH   G 4 .   ? 365.917 -2.814  77.330  1.00 45.50  ? 1016 HOH   A O    1 
HETATM 5447 O  O    . HOH   G 4 .   ? 397.646 -5.363  100.110 1.00 48.12  ? 1017 HOH   A O    1 
HETATM 5448 O  O    . HOH   G 4 .   ? 432.913 -11.192 82.132  1.00 52.62  ? 1018 HOH   A O    1 
HETATM 5449 O  O    . HOH   G 4 .   ? 334.129 21.895  76.481  1.00 48.44  ? 1019 HOH   A O    1 
HETATM 5450 O  O    . HOH   G 4 .   ? 337.273 11.378  88.837  1.00 56.65  ? 1020 HOH   A O    1 
HETATM 5451 O  O    . HOH   G 4 .   ? 333.117 22.051  68.317  1.00 57.33  ? 1021 HOH   A O    1 
HETATM 5452 O  O    . HOH   G 4 .   ? 339.543 11.473  87.151  1.00 49.57  ? 1022 HOH   A O    1 
HETATM 5453 O  O    . HOH   G 4 .   ? 394.123 -18.971 112.867 1.00 66.10  ? 1023 HOH   A O    1 
HETATM 5454 O  O    . HOH   G 4 .   ? 336.334 3.489   85.955  1.00 50.04  ? 1024 HOH   A O    1 
HETATM 5455 O  O    . HOH   G 4 .   ? 386.558 -14.847 79.025  1.00 45.70  ? 1025 HOH   A O    1 
HETATM 5456 O  O    . HOH   G 4 .   ? 338.056 19.042  78.275  1.00 47.43  ? 1026 HOH   A O    1 
HETATM 5457 O  O    . HOH   G 4 .   ? 388.638 -2.066  79.993  1.00 41.32  ? 1027 HOH   A O    1 
HETATM 5458 O  O    . HOH   G 4 .   ? 413.668 -10.609 76.603  1.00 49.36  ? 1028 HOH   A O    1 
HETATM 5459 O  O    . HOH   G 4 .   ? 386.451 9.821   78.204  1.00 56.45  ? 1029 HOH   A O    1 
HETATM 5460 O  O    . HOH   G 4 .   ? 416.082 6.212   92.457  1.00 42.02  ? 1030 HOH   A O    1 
HETATM 5461 O  O    . HOH   G 4 .   ? 393.956 -18.685 78.460  1.00 51.96  ? 1031 HOH   A O    1 
HETATM 5462 O  O    . HOH   G 4 .   ? 389.188 12.293  81.700  1.00 52.83  ? 1032 HOH   A O    1 
HETATM 5463 O  O    . HOH   G 4 .   ? 375.774 9.979   94.777  1.00 50.42  ? 1033 HOH   A O    1 
HETATM 5464 O  O    . HOH   G 4 .   ? 375.889 -7.870  77.607  1.00 44.05  ? 1034 HOH   A O    1 
HETATM 5465 O  O    . HOH   G 4 .   ? 382.852 -5.245  106.659 1.00 57.19  ? 1035 HOH   A O    1 
HETATM 5466 O  O    . HOH   G 4 .   ? 396.802 8.312   111.837 1.00 58.62  ? 1036 HOH   A O    1 
HETATM 5467 O  O    . HOH   G 4 .   ? 382.639 0.182   99.182  1.00 40.15  ? 1037 HOH   A O    1 
HETATM 5468 O  O    . HOH   G 4 .   ? 414.579 7.798   88.920  1.00 46.69  ? 1038 HOH   A O    1 
HETATM 5469 O  O    . HOH   G 4 .   ? 404.835 -20.601 77.806  1.00 52.92  ? 1039 HOH   A O    1 
HETATM 5470 O  O    . HOH   G 4 .   ? 423.017 2.793   94.034  1.00 42.28  ? 1040 HOH   A O    1 
HETATM 5471 O  O    . HOH   G 4 .   ? 345.190 -11.109 86.103  1.00 49.26  ? 1041 HOH   A O    1 
HETATM 5472 O  O    . HOH   G 4 .   ? 403.252 -5.297  96.275  1.00 49.39  ? 1042 HOH   A O    1 
HETATM 5473 O  O    . HOH   G 4 .   ? 381.535 -17.119 94.917  1.00 50.97  ? 1043 HOH   A O    1 
HETATM 5474 O  O    . HOH   G 4 .   ? 393.777 -8.563  77.308  1.00 45.84  ? 1044 HOH   A O    1 
HETATM 5475 O  O    . HOH   G 4 .   ? 358.904 -18.090 83.927  1.00 45.90  ? 1045 HOH   A O    1 
HETATM 5476 O  O    . HOH   G 4 .   ? 354.789 -2.521  98.496  1.00 47.78  ? 1046 HOH   A O    1 
HETATM 5477 O  O    . HOH   G 4 .   ? 375.604 11.293  90.696  1.00 41.41  ? 1047 HOH   A O    1 
HETATM 5478 O  O    . HOH   G 4 .   ? 398.473 -3.303  77.661  1.00 36.00  ? 1048 HOH   A O    1 
HETATM 5479 O  O    . HOH   G 4 .   ? 404.200 -8.072  102.399 1.00 49.41  ? 1049 HOH   A O    1 
HETATM 5480 O  O    . HOH   G 4 .   ? 375.864 10.066  92.725  1.00 40.50  ? 1050 HOH   A O    1 
HETATM 5481 O  O    . HOH   G 4 .   ? 375.361 -15.960 92.408  1.00 50.70  ? 1051 HOH   A O    1 
HETATM 5482 O  O    . HOH   G 4 .   ? 370.377 -15.926 100.842 1.00 49.50  ? 1052 HOH   A O    1 
HETATM 5483 O  O    . HOH   G 4 .   ? 389.224 9.545   94.684  1.00 39.69  ? 1053 HOH   A O    1 
HETATM 5484 O  O    . HOH   G 4 .   ? 337.881 -0.228  62.516  1.00 52.66  ? 1054 HOH   A O    1 
HETATM 5485 O  O    . HOH   G 4 .   ? 398.912 11.705  86.939  1.00 41.06  ? 1055 HOH   A O    1 
HETATM 5486 O  O    . HOH   G 4 .   ? 325.120 16.390  68.268  1.00 55.43  ? 1056 HOH   A O    1 
HETATM 5487 O  O    . HOH   G 4 .   ? 412.789 -17.573 78.383  1.00 53.63  ? 1057 HOH   A O    1 
HETATM 5488 O  O    . HOH   G 4 .   ? 400.486 -3.043  100.886 1.00 34.46  ? 1058 HOH   A O    1 
HETATM 5489 O  O    . HOH   G 4 .   ? 369.482 1.754   92.654  1.00 43.30  ? 1059 HOH   A O    1 
HETATM 5490 O  O    . HOH   G 4 .   ? 432.962 -9.538  87.027  1.00 53.13  ? 1060 HOH   A O    1 
HETATM 5491 O  O    . HOH   G 4 .   ? 357.853 12.624  86.505  1.00 48.76  ? 1061 HOH   A O    1 
HETATM 5492 O  O    . HOH   G 4 .   ? 351.079 6.212   92.645  1.00 51.06  ? 1062 HOH   A O    1 
HETATM 5493 O  O    . HOH   G 4 .   ? 381.602 -2.612  84.136  1.00 37.27  ? 1063 HOH   A O    1 
HETATM 5494 O  O    . HOH   G 4 .   ? 391.052 2.797   110.968 1.00 59.62  ? 1064 HOH   A O    1 
HETATM 5495 O  O    . HOH   G 4 .   ? 425.995 -16.734 102.692 1.00 66.13  ? 1065 HOH   A O    1 
HETATM 5496 O  O    . HOH   G 4 .   ? 411.086 -14.397 79.074  1.00 49.69  ? 1066 HOH   A O    1 
HETATM 5497 O  O    . HOH   G 4 .   ? 421.078 -3.032  81.555  1.00 42.62  ? 1067 HOH   A O    1 
HETATM 5498 O  O    . HOH   G 4 .   ? 348.061 -7.132  68.774  1.00 42.67  ? 1068 HOH   A O    1 
HETATM 5499 O  O    . HOH   G 4 .   ? 357.228 6.059   81.503  1.00 37.72  ? 1069 HOH   A O    1 
HETATM 5500 O  O    . HOH   G 4 .   ? 354.079 -2.026  74.153  1.00 38.48  ? 1070 HOH   A O    1 
HETATM 5501 O  O    . HOH   G 4 .   ? 415.289 6.055   111.136 1.00 55.60  ? 1071 HOH   A O    1 
HETATM 5502 O  O    . HOH   G 4 .   ? 419.457 10.689  102.137 1.00 55.67  ? 1072 HOH   A O    1 
HETATM 5503 O  O    . HOH   G 4 .   ? 411.533 -12.358 98.160  1.00 46.41  ? 1073 HOH   A O    1 
HETATM 5504 O  O    . HOH   G 4 .   ? 373.055 8.370   99.105  1.00 53.76  ? 1074 HOH   A O    1 
HETATM 5505 O  O    . HOH   G 4 .   ? 420.759 -5.506  110.183 1.00 57.71  ? 1075 HOH   A O    1 
HETATM 5506 O  O    . HOH   G 4 .   ? 386.853 9.630   84.069  1.00 48.61  ? 1076 HOH   A O    1 
HETATM 5507 O  O    . HOH   G 4 .   ? 388.570 12.412  94.527  1.00 47.21  ? 1077 HOH   A O    1 
HETATM 5508 O  O    . HOH   G 4 .   ? 412.731 -11.221 105.079 1.00 57.08  ? 1078 HOH   A O    1 
HETATM 5509 O  O    . HOH   G 4 .   ? 354.165 8.460   90.268  1.00 50.10  ? 1079 HOH   A O    1 
HETATM 5510 O  O    . HOH   G 4 .   ? 435.153 -6.034  91.481  1.00 50.09  ? 1080 HOH   A O    1 
HETATM 5511 O  O    . HOH   G 4 .   ? 399.370 6.350   76.579  1.00 51.55  ? 1081 HOH   A O    1 
HETATM 5512 O  O    . HOH   G 4 .   ? 413.562 -1.988  111.200 1.00 40.90  ? 1082 HOH   A O    1 
HETATM 5513 O  O    . HOH   G 4 .   ? 401.542 -0.669  76.744  1.00 43.14  ? 1083 HOH   A O    1 
HETATM 5514 O  O    . HOH   G 4 .   ? 418.522 -0.201  112.213 1.00 58.24  ? 1084 HOH   A O    1 
HETATM 5515 O  O    . HOH   G 4 .   ? 398.326 -20.631 89.907  1.00 50.68  ? 1085 HOH   A O    1 
HETATM 5516 O  O    . HOH   G 4 .   ? 377.296 1.222   102.773 1.00 56.11  ? 1086 HOH   A O    1 
HETATM 5517 O  O    . HOH   G 4 .   ? 399.055 -8.780  96.042  1.00 55.67  ? 1087 HOH   A O    1 
HETATM 5518 O  O    . HOH   G 4 .   ? 420.398 6.403   99.653  1.00 49.14  ? 1088 HOH   A O    1 
HETATM 5519 O  O    . HOH   G 4 .   ? 394.167 -11.511 115.207 1.00 46.24  ? 1089 HOH   A O    1 
HETATM 5520 O  O    . HOH   G 4 .   ? 365.713 11.687  77.577  1.00 59.65  ? 1090 HOH   A O    1 
HETATM 5521 O  O    . HOH   G 4 .   ? 389.999 7.579   100.351 1.00 47.50  ? 1091 HOH   A O    1 
HETATM 5522 O  O    . HOH   G 4 .   ? 355.110 -7.947  76.938  1.00 43.80  ? 1092 HOH   A O    1 
HETATM 5523 O  O    . HOH   G 4 .   ? 419.567 -10.298 110.802 1.00 61.19  ? 1093 HOH   A O    1 
HETATM 5524 O  O    . HOH   G 4 .   ? 355.168 -0.094  99.121  1.00 53.37  ? 1094 HOH   A O    1 
HETATM 5525 O  O    . HOH   G 4 .   ? 372.137 2.424   77.623  1.00 38.69  ? 1095 HOH   A O    1 
HETATM 5526 O  O    . HOH   G 4 .   ? 420.575 -17.005 97.068  1.00 48.25  ? 1096 HOH   A O    1 
HETATM 5527 O  O    . HOH   G 4 .   ? 350.109 -1.619  97.143  1.00 52.33  ? 1097 HOH   A O    1 
HETATM 5528 O  O    . HOH   G 4 .   ? 399.955 -19.273 91.072  1.00 46.68  ? 1098 HOH   A O    1 
HETATM 5529 O  O    . HOH   G 4 .   ? 388.508 7.963   102.782 1.00 49.90  ? 1099 HOH   A O    1 
HETATM 5530 O  O    . HOH   G 4 .   ? 390.368 9.103   96.517  1.00 44.81  ? 1100 HOH   A O    1 
HETATM 5531 O  O    . HOH   G 4 .   ? 375.677 -13.784 79.225  1.00 48.61  ? 1101 HOH   A O    1 
HETATM 5532 O  O    . HOH   G 4 .   ? 330.481 11.705  81.286  1.00 55.72  ? 1102 HOH   A O    1 
HETATM 5533 O  O    . HOH   G 4 .   ? 328.319 4.578   71.349  1.00 46.94  ? 1103 HOH   A O    1 
HETATM 5534 O  O    . HOH   G 4 .   ? 347.069 -1.141  71.114  1.00 43.42  ? 1104 HOH   A O    1 
HETATM 5535 O  O    . HOH   G 4 .   ? 368.006 1.416   97.226  1.00 35.30  ? 1105 HOH   A O    1 
HETATM 5536 O  O    . HOH   G 4 .   ? 351.507 -12.875 93.572  1.00 51.01  ? 1106 HOH   A O    1 
HETATM 5537 O  O    . HOH   G 4 .   ? 324.993 0.052   65.667  1.00 64.20  ? 1107 HOH   A O    1 
HETATM 5538 O  O    . HOH   G 4 .   ? 379.852 -17.223 85.546  1.00 50.31  ? 1108 HOH   A O    1 
HETATM 5539 O  O    . HOH   G 4 .   ? 403.252 10.726  90.053  1.00 43.93  ? 1109 HOH   A O    1 
HETATM 5540 O  O    . HOH   G 4 .   ? 427.870 -16.095 94.003  1.00 54.21  ? 1110 HOH   A O    1 
HETATM 5541 O  O    . HOH   G 4 .   ? 418.474 4.950   92.982  1.00 46.52  ? 1111 HOH   A O    1 
HETATM 5542 O  O    . HOH   G 4 .   ? 408.586 -10.958 96.122  1.00 47.91  ? 1112 HOH   A O    1 
HETATM 5543 O  O    . HOH   G 4 .   ? 406.197 -21.001 89.291  1.00 48.69  ? 1113 HOH   A O    1 
HETATM 5544 O  O    . HOH   G 4 .   ? 382.276 -3.056  106.055 1.00 50.87  ? 1114 HOH   A O    1 
HETATM 5545 O  O    . HOH   G 4 .   ? 367.903 -21.937 98.821  1.00 63.50  ? 1115 HOH   A O    1 
HETATM 5546 O  O    . HOH   G 4 .   ? 342.731 7.571   90.936  1.00 48.22  ? 1116 HOH   A O    1 
HETATM 5547 O  O    . HOH   G 4 .   ? 402.361 11.855  91.182  1.00 34.59  ? 1117 HOH   A O    1 
HETATM 5548 O  O    . HOH   G 4 .   ? 370.060 -18.474 81.421  1.00 51.16  ? 1118 HOH   A O    1 
HETATM 5549 O  O    . HOH   G 4 .   ? 400.012 -5.458  101.821 1.00 46.62  ? 1119 HOH   A O    1 
HETATM 5550 O  O    . HOH   G 4 .   ? 403.574 -6.961  76.632  1.00 31.15  ? 1120 HOH   A O    1 
HETATM 5551 O  O    . HOH   G 4 .   ? 323.360 15.120  68.181  1.00 48.14  ? 1121 HOH   A O    1 
HETATM 5552 O  O    . HOH   G 4 .   ? 336.762 3.965   50.842  1.00 47.22  ? 1122 HOH   A O    1 
HETATM 5553 O  O    . HOH   G 4 .   ? 382.891 13.859  89.242  1.00 42.96  ? 1123 HOH   A O    1 
HETATM 5554 O  O    . HOH   G 4 .   ? 384.345 -0.626  100.878 1.00 45.91  ? 1124 HOH   A O    1 
HETATM 5555 O  O    . HOH   G 4 .   ? 417.681 6.457   87.334  1.00 56.24  ? 1125 HOH   A O    1 
HETATM 5556 O  O    . HOH   G 4 .   ? 368.669 14.825  92.881  1.00 51.91  ? 1126 HOH   A O    1 
HETATM 5557 O  O    . HOH   G 4 .   ? 422.035 -6.974  78.622  1.00 50.72  ? 1127 HOH   A O    1 
HETATM 5558 O  O    . HOH   G 4 .   ? 404.068 12.770  81.468  1.00 51.93  ? 1128 HOH   A O    1 
HETATM 5559 O  O    . HOH   G 4 .   ? 354.824 8.540   68.021  1.00 52.51  ? 1129 HOH   A O    1 
HETATM 5560 O  O    . HOH   G 4 .   ? 337.718 19.930  76.292  1.00 54.37  ? 1130 HOH   A O    1 
HETATM 5561 O  O    . HOH   G 4 .   ? 334.313 3.793   81.259  1.00 49.39  ? 1131 HOH   A O    1 
HETATM 5562 O  O    . HOH   G 4 .   ? 391.541 2.853   78.213  1.00 46.86  ? 1132 HOH   A O    1 
HETATM 5563 O  O    . HOH   G 4 .   ? 363.538 12.483  87.146  1.00 49.49  ? 1133 HOH   A O    1 
HETATM 5564 O  O    . HOH   G 4 .   ? 348.915 15.263  72.594  1.00 52.03  ? 1134 HOH   A O    1 
HETATM 5565 O  O    . HOH   G 4 .   ? 376.598 -15.641 83.472  1.00 52.43  ? 1135 HOH   A O    1 
HETATM 5566 O  O    . HOH   G 4 .   ? 353.479 14.018  66.163  1.00 50.66  ? 1136 HOH   A O    1 
HETATM 5567 O  O    . HOH   G 4 .   ? 405.086 17.513  103.082 1.00 51.87  ? 1137 HOH   A O    1 
HETATM 5568 O  O    . HOH   G 4 .   ? 368.021 2.662   95.932  1.00 38.85  ? 1138 HOH   A O    1 
HETATM 5569 O  O    . HOH   G 4 .   ? 363.946 -20.481 83.287  1.00 48.92  ? 1139 HOH   A O    1 
HETATM 5570 O  O    . HOH   G 4 .   ? 361.455 5.791   79.735  1.00 37.38  ? 1140 HOH   A O    1 
HETATM 5571 O  O    . HOH   G 4 .   ? 357.370 -17.966 85.560  1.00 47.61  ? 1141 HOH   A O    1 
HETATM 5572 O  O    . HOH   G 4 .   ? 391.244 -26.573 94.591  1.00 59.52  ? 1142 HOH   A O    1 
HETATM 5573 O  O    . HOH   G 4 .   ? 394.616 -6.819  78.722  1.00 44.41  ? 1143 HOH   A O    1 
HETATM 5574 O  O    . HOH   G 4 .   ? 370.416 -17.270 78.235  1.00 45.55  ? 1144 HOH   A O    1 
HETATM 5575 O  O    . HOH   G 4 .   ? 344.528 -7.164  87.991  1.00 53.85  ? 1145 HOH   A O    1 
HETATM 5576 O  O    . HOH   G 4 .   ? 341.681 11.782  51.173  1.00 59.04  ? 1146 HOH   A O    1 
HETATM 5577 O  O    . HOH   G 4 .   ? 352.365 -10.398 94.382  1.00 45.93  ? 1147 HOH   A O    1 
HETATM 5578 O  O    . HOH   G 4 .   ? 390.941 8.799   98.547  1.00 48.18  ? 1148 HOH   A O    1 
HETATM 5579 O  O    . HOH   G 4 .   ? 438.655 -3.126  94.550  1.00 56.61  ? 1149 HOH   A O    1 
HETATM 5580 O  O    . HOH   G 4 .   ? 403.810 4.080   117.937 1.00 60.66  ? 1150 HOH   A O    1 
HETATM 5581 O  O    . HOH   G 4 .   ? 356.783 -5.073  73.415  1.00 41.70  ? 1151 HOH   A O    1 
HETATM 5582 O  O    . HOH   G 4 .   ? 369.077 -19.879 85.049  1.00 50.31  ? 1152 HOH   A O    1 
HETATM 5583 O  O    . HOH   G 4 .   ? 399.869 -5.945  95.820  1.00 51.94  ? 1153 HOH   A O    1 
HETATM 5584 O  O    . HOH   G 4 .   ? 409.730 -15.057 66.460  1.00 48.66  ? 1154 HOH   A O    1 
HETATM 5585 O  O    . HOH   G 4 .   ? 402.843 -16.169 67.995  1.00 46.57  ? 1155 HOH   A O    1 
HETATM 5586 O  O    . HOH   G 4 .   ? 384.962 -4.265  77.584  1.00 50.55  ? 1156 HOH   A O    1 
HETATM 5587 O  O    . HOH   G 4 .   ? 392.990 11.893  88.861  1.00 48.74  ? 1157 HOH   A O    1 
HETATM 5588 O  O    . HOH   G 4 .   ? 384.256 -6.552  78.197  1.00 42.33  ? 1158 HOH   A O    1 
HETATM 5589 O  O    . HOH   G 4 .   ? 386.737 11.351  85.685  1.00 48.55  ? 1159 HOH   A O    1 
HETATM 5590 O  O    . HOH   G 4 .   ? 405.949 -8.536  104.054 1.00 51.50  ? 1160 HOH   A O    1 
HETATM 5591 O  O    . HOH   G 4 .   ? 367.397 -6.969  77.204  1.00 43.41  ? 1161 HOH   A O    1 
HETATM 5592 O  O    . HOH   G 4 .   ? 326.300 24.126  63.744  1.00 46.76  ? 1162 HOH   A O    1 
HETATM 5593 O  O    . HOH   G 4 .   ? 326.489 16.367  54.103  1.00 58.07  ? 1163 HOH   A O    1 
HETATM 5594 O  O    . HOH   G 4 .   ? 390.896 -2.462  78.585  1.00 44.04  ? 1164 HOH   A O    1 
HETATM 5595 O  O    . HOH   G 4 .   ? 369.419 -22.244 96.468  1.00 65.77  ? 1165 HOH   A O    1 
HETATM 5596 O  O    . HOH   G 4 .   ? 422.177 -2.222  84.225  1.00 42.89  ? 1166 HOH   A O    1 
HETATM 5597 O  O    . HOH   G 4 .   ? 352.788 -8.009  94.154  1.00 41.86  ? 1167 HOH   A O    1 
HETATM 5598 O  O    . HOH   G 4 .   ? 345.948 -16.801 77.657  1.00 57.06  ? 1168 HOH   A O    1 
HETATM 5599 O  O    . HOH   G 4 .   ? 402.295 -21.267 78.818  1.00 50.80  ? 1169 HOH   A O    1 
HETATM 5600 O  O    . HOH   G 4 .   ? 392.159 11.414  92.280  1.00 43.31  ? 1170 HOH   A O    1 
HETATM 5601 O  O    . HOH   G 4 .   ? 422.346 -13.234 79.039  1.00 48.78  ? 1171 HOH   A O    1 
HETATM 5602 O  O    . HOH   G 4 .   ? 330.021 20.511  56.330  1.00 60.02  ? 1172 HOH   A O    1 
HETATM 5603 O  O    . HOH   G 4 .   ? 422.707 -12.019 114.555 1.00 53.58  ? 1173 HOH   A O    1 
HETATM 5604 O  O    . HOH   G 4 .   ? 390.120 12.337  90.872  1.00 49.00  ? 1174 HOH   A O    1 
HETATM 5605 O  O    . HOH   G 4 .   ? 416.878 15.272  103.019 1.00 55.76  ? 1175 HOH   A O    1 
HETATM 5606 O  O    . HOH   G 4 .   ? 393.867 -27.211 101.913 1.00 56.56  ? 1176 HOH   A O    1 
HETATM 5607 O  O    . HOH   G 4 .   ? 381.855 8.183   71.276  1.00 58.12  ? 1177 HOH   A O    1 
HETATM 5608 O  O    . HOH   G 4 .   ? 395.409 -26.029 103.652 1.00 59.93  ? 1178 HOH   A 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   . MET   A 22  ? 0.9095 1.1270 1.1588 -0.1408 -0.0804 -0.1673 1   MET   A N   
2    C  CA  . MET   A 22  ? 0.8737 1.0886 1.1320 -0.1361 -0.0610 -0.1559 1   MET   A CA  
3    C  C   . MET   A 22  ? 0.9858 1.2506 1.2827 -0.1577 -0.0555 -0.1278 1   MET   A C   
4    O  O   . MET   A 22  ? 1.1052 1.3513 1.4186 -0.1882 -0.0635 -0.1141 1   MET   A O   
5    C  CB  . MET   A 22  ? 0.8463 0.9881 1.0832 -0.1394 -0.0634 -0.1641 1   MET   A CB  
6    N  N   . LEU   A 23  ? 0.7095 1.0369 1.0189 -0.1393 -0.0412 -0.1166 2   LEU   A N   
7    C  CA  . LEU   A 23  ? 0.6938 1.0811 1.0382 -0.1505 -0.0324 -0.0867 2   LEU   A CA  
8    C  C   . LEU   A 23  ? 0.7091 1.1358 1.0457 -0.1163 -0.0094 -0.0785 2   LEU   A C   
9    O  O   . LEU   A 23  ? 0.6904 1.1456 1.0413 -0.1175 0.0053  -0.0566 2   LEU   A O   
10   C  CB  . LEU   A 23  ? 0.6068 1.0380 0.9767 -0.1640 -0.0467 -0.0774 2   LEU   A CB  
11   N  N   . ARG   A 24  ? 0.5467 0.9714 0.8566 -0.0839 -0.0069 -0.0945 3   ARG   A N   
12   C  CA  . ARG   A 24  ? 0.4663 0.9078 0.7580 -0.0483 0.0091  -0.0906 3   ARG   A CA  
13   C  C   . ARG   A 24  ? 0.3758 0.7723 0.6508 -0.0389 0.0152  -0.1022 3   ARG   A C   
14   O  O   . ARG   A 24  ? 0.4168 0.7660 0.6809 -0.0411 0.0076  -0.1216 3   ARG   A O   
15   C  CB  . ARG   A 24  ? 0.4492 0.8935 0.7172 -0.0193 0.0064  -0.1013 3   ARG   A CB  
16   C  CG  . ARG   A 24  ? 0.5192 0.9907 0.7977 -0.0283 -0.0056 -0.1022 3   ARG   A CG  
17   C  CD  . ARG   A 24  ? 0.5151 0.9847 0.7654 0.0048  -0.0054 -0.1112 3   ARG   A CD  
18   N  NE  . ARG   A 24  ? 0.6166 1.1112 0.8715 0.0016  -0.0169 -0.1154 3   ARG   A NE  
19   C  CZ  . ARG   A 24  ? 0.5691 1.0764 0.8048 0.0285  -0.0172 -0.1170 3   ARG   A CZ  
20   N  NH1 . ARG   A 24  ? 0.5513 1.0405 0.7606 0.0589  -0.0088 -0.1149 3   ARG   A NH1 
21   N  NH2 . ARG   A 24  ? 0.3442 0.8795 0.5854 0.0250  -0.0284 -0.1208 3   ARG   A NH2 
22   N  N   . GLU   A 25  ? 0.3342 0.7477 0.6059 -0.0249 0.0289  -0.0896 4   GLU   A N   
23   C  CA  . GLU   A 25  ? 0.3793 0.7417 0.6258 -0.0115 0.0321  -0.0976 4   GLU   A CA  
24   C  C   . GLU   A 25  ? 0.2973 0.6481 0.5143 0.0259  0.0319  -0.1110 4   GLU   A C   
25   O  O   . GLU   A 25  ? 0.3160 0.6933 0.5178 0.0486  0.0359  -0.1027 4   GLU   A O   
26   C  CB  . GLU   A 25  ? 0.3508 0.7230 0.5972 -0.0143 0.0440  -0.0758 4   GLU   A CB  
27   C  CG  . GLU   A 25  ? 0.3932 0.7025 0.6132 -0.0072 0.0422  -0.0829 4   GLU   A CG  
28   C  CD  . GLU   A 25  ? 0.5096 0.8224 0.7275 -0.0119 0.0529  -0.0595 4   GLU   A CD  
29   O  OE1 . GLU   A 25  ? 0.4371 0.8010 0.6528 0.0037  0.0660  -0.0409 4   GLU   A OE1 
30   O  OE2 . GLU   A 25  ? 0.5903 0.8555 0.8057 -0.0273 0.0490  -0.0582 4   GLU   A OE2 
31   N  N   . ARG   A 26  ? 0.3099 0.6033 0.5091 0.0303  0.0241  -0.1261 5   ARG   A N   
32   C  CA  . ARG   A 26  ? 0.2693 0.5347 0.4411 0.0572  0.0183  -0.1367 5   ARG   A CA  
33   C  C   . ARG   A 26  ? 0.3111 0.5345 0.4674 0.0632  0.0146  -0.1423 5   ARG   A C   
34   O  O   . ARG   A 26  ? 0.3480 0.5466 0.5123 0.0449  0.0133  -0.1414 5   ARG   A O   
35   C  CB  . ARG   A 26  ? 0.2962 0.5394 0.4668 0.0529  0.0094  -0.1445 5   ARG   A CB  
36   C  CG  . ARG   A 26  ? 0.3496 0.5520 0.4957 0.0698  0.0002  -0.1486 5   ARG   A CG  
37   C  CD  . ARG   A 26  ? 0.3584 0.5500 0.5096 0.0640  -0.0043 -0.1508 5   ARG   A CD  
38   N  NE  . ARG   A 26  ? 0.3350 0.4866 0.4769 0.0711  -0.0124 -0.1520 5   ARG   A NE  
39   C  CZ  . ARG   A 26  ? 0.3870 0.5249 0.5395 0.0637  -0.0138 -0.1515 5   ARG   A CZ  
40   N  NH1 . ARG   A 26  ? 0.2839 0.4391 0.4467 0.0526  -0.0087 -0.1515 5   ARG   A NH1 
41   N  NH2 . ARG   A 26  ? 0.3836 0.4900 0.5368 0.0690  -0.0213 -0.1517 5   ARG   A NH2 
42   N  N   . THR   A 27  ? 0.2902 0.4971 0.4158 0.0878  0.0094  -0.1445 6   THR   A N   
43   C  CA  . THR   A 27  ? 0.3083 0.4784 0.4162 0.0948  0.0011  -0.1506 6   THR   A CA  
44   C  C   . THR   A 27  ? 0.3576 0.4823 0.4651 0.0871  -0.0148 -0.1578 6   THR   A C   
45   O  O   . THR   A 27  ? 0.4043 0.5127 0.4996 0.0957  -0.0238 -0.1596 6   THR   A O   
46   C  CB  . THR   A 27  ? 0.3658 0.5355 0.4363 0.1232  -0.0017 -0.1493 6   THR   A CB  
47   O  OG1 . THR   A 27  ? 0.3855 0.6080 0.4589 0.1308  0.0164  -0.1353 6   THR   A OG1 
48   C  CG2 . THR   A 27  ? 0.3764 0.5075 0.4271 0.1291  -0.0156 -0.1574 6   THR   A CG2 
49   N  N   . VAL   A 28  ? 0.3641 0.4721 0.4872 0.0723  -0.0174 -0.1593 7   VAL   A N   
50   C  CA  . VAL   A 28  ? 0.3756 0.4535 0.5059 0.0645  -0.0309 -0.1610 7   VAL   A CA  
51   C  C   . VAL   A 28  ? 0.4190 0.4815 0.5463 0.0652  -0.0395 -0.1633 7   VAL   A C   
52   O  O   . VAL   A 28  ? 0.5375 0.6070 0.6758 0.0588  -0.0313 -0.1612 7   VAL   A O   
53   C  CB  . VAL   A 28  ? 0.3938 0.4777 0.5497 0.0482  -0.0246 -0.1574 7   VAL   A CB  
54   C  CG1 . VAL   A 28  ? 0.3737 0.4390 0.5456 0.0420  -0.0345 -0.1569 7   VAL   A CG1 
55   C  CG2 . VAL   A 28  ? 0.3817 0.4793 0.5370 0.0507  -0.0205 -0.1566 7   VAL   A CG2 
56   N  N   . ARG   A 29  ? 0.4141 0.4531 0.5252 0.0740  -0.0578 -0.1684 8   ARG   A N   
57   C  CA  . ARG   A 29  ? 0.4891 0.5159 0.5955 0.0766  -0.0710 -0.1727 8   ARG   A CA  
58   C  C   . ARG   A 29  ? 0.5281 0.5448 0.6656 0.0598  -0.0837 -0.1710 8   ARG   A C   
59   O  O   . ARG   A 29  ? 0.4879 0.4932 0.6392 0.0510  -0.0909 -0.1679 8   ARG   A O   
60   C  CB  . ARG   A 29  ? 0.5218 0.5294 0.5911 0.0964  -0.0881 -0.1804 8   ARG   A CB  
61   C  CG  . ARG   A 29  ? 0.5087 0.5336 0.5462 0.1184  -0.0750 -0.1803 8   ARG   A CG  
62   C  CD  . ARG   A 29  ? 0.4583 0.4642 0.4541 0.1428  -0.0925 -0.1885 8   ARG   A CD  
63   N  NE  . ARG   A 29  ? 0.5274 0.5590 0.4934 0.1675  -0.0773 -0.1847 8   ARG   A NE  
64   C  CZ  . ARG   A 29  ? 0.5668 0.6280 0.5177 0.1822  -0.0629 -0.1788 8   ARG   A CZ  
65   N  NH1 . ARG   A 29  ? 0.5842 0.6461 0.5407 0.1776  -0.0634 -0.1790 8   ARG   A NH1 
66   N  NH2 . ARG   A 29  ? 0.4567 0.5512 0.3870 0.2035  -0.0467 -0.1697 8   ARG   A NH2 
67   N  N   . LEU   A 30  ? 0.4524 0.4761 0.6020 0.0565  -0.0861 -0.1707 9   LEU   A N   
68   C  CA  . LEU   A 30  ? 0.4307 0.4558 0.6110 0.0425  -0.1013 -0.1652 9   LEU   A CA  
69   C  C   . LEU   A 30  ? 0.4868 0.4870 0.6544 0.0444  -0.1300 -0.1720 9   LEU   A C   
70   O  O   . LEU   A 30  ? 0.5030 0.4899 0.6332 0.0624  -0.1381 -0.1818 9   LEU   A O   
71   C  CB  . LEU   A 30  ? 0.4014 0.4470 0.5928 0.0437  -0.0946 -0.1560 9   LEU   A CB  
72   C  CG  . LEU   A 30  ? 0.4008 0.4595 0.5969 0.0435  -0.0678 -0.1471 9   LEU   A CG  
73   C  CD1 . LEU   A 30  ? 0.4382 0.5084 0.6424 0.0488  -0.0639 -0.1382 9   LEU   A CD1 
74   C  CD2 . LEU   A 30  ? 0.3870 0.4541 0.6055 0.0328  -0.0589 -0.1421 9   LEU   A CD2 
75   N  N   . GLN   A 31  ? 0.5438 0.5387 0.7395 0.0266  -0.1428 -0.1618 10  GLN   A N   
76   C  CA  . GLN   A 31  ? 0.5921 0.5562 0.7759 0.0236  -0.1694 -0.1638 10  GLN   A CA  
77   C  C   . GLN   A 31  ? 0.6116 0.5902 0.8171 0.0132  -0.1871 -0.1590 10  GLN   A C   
78   O  O   . GLN   A 31  ? 0.5545 0.5688 0.8006 -0.0007 -0.1795 -0.1440 10  GLN   A O   
79   C  CB  . GLN   A 31  ? 0.6087 0.5526 0.8079 0.0076  -0.1744 -0.1535 10  GLN   A CB  
80   C  CG  . GLN   A 31  ? 0.7982 0.7015 0.9844 0.0020  -0.2042 -0.1564 10  GLN   A CG  
81   C  CD  . GLN   A 31  ? 0.8000 0.6798 1.0028 -0.0151 -0.2099 -0.1442 10  GLN   A CD  
82   O  OE1 . GLN   A 31  ? 0.8419 0.7283 1.0514 -0.0142 -0.1918 -0.1387 10  GLN   A OE1 
83   N  NE2 . GLN   A 31  ? 0.7272 0.5783 0.9375 -0.0315 -0.2368 -0.1397 10  GLN   A NE2 
84   N  N   . TYR   A 32  ? 0.6109 0.5662 0.7878 0.0228  -0.2103 -0.1710 11  TYR   A N   
85   C  CA  . TYR   A 32  ? 0.6551 0.6243 0.8463 0.0156  -0.2307 -0.1692 11  TYR   A CA  
86   C  C   . TYR   A 32  ? 0.6820 0.6769 0.9275 -0.0153 -0.2344 -0.1467 11  TYR   A C   
87   O  O   . TYR   A 32  ? 0.6352 0.6076 0.8918 -0.0339 -0.2485 -0.1399 11  TYR   A O   
88   C  CB  . TYR   A 32  ? 0.7079 0.6381 0.8605 0.0267  -0.2595 -0.1855 11  TYR   A CB  
89   C  CG  . TYR   A 32  ? 0.6957 0.6409 0.8514 0.0263  -0.2818 -0.1890 11  TYR   A CG  
90   C  CD1 . TYR   A 32  ? 0.6867 0.6652 0.8364 0.0431  -0.2739 -0.1911 11  TYR   A CD1 
91   C  CD2 . TYR   A 32  ? 0.7613 0.6870 0.9243 0.0099  -0.3128 -0.1905 11  TYR   A CD2 
92   C  CE1 . TYR   A 32  ? 0.6632 0.6591 0.8135 0.0456  -0.2950 -0.1933 11  TYR   A CE1 
93   C  CE2 . TYR   A 32  ? 0.7403 0.6841 0.9062 0.0093  -0.3348 -0.1942 11  TYR   A CE2 
94   C  CZ  . TYR   A 32  ? 0.7561 0.7367 0.9150 0.0283  -0.3251 -0.1952 11  TYR   A CZ  
95   O  OH  . TYR   A 32  ? 0.8307 0.8332 0.9910 0.0302  -0.3473 -0.1977 11  TYR   A OH  
96   N  N   . GLY   A 33  ? 0.6276 0.6724 0.9069 -0.0187 -0.2214 -0.1331 12  GLY   A N   
97   C  CA  . GLY   A 33  ? 0.5976 0.6838 0.9297 -0.0433 -0.2206 -0.1071 12  GLY   A CA  
98   C  C   . GLY   A 33  ? 0.7290 0.8232 1.0863 -0.0568 -0.2011 -0.0895 12  GLY   A C   
99   O  O   . GLY   A 33  ? 0.7682 0.9128 1.1616 -0.0611 -0.1827 -0.0684 12  GLY   A O   
100  N  N   . SER   A 34  ? 0.8093 0.8570 1.1450 -0.0588 -0.2039 -0.0971 13  SER   A N   
101  C  CA  . SER   A 34  ? 0.7638 0.8169 1.1221 -0.0708 -0.1885 -0.0798 13  SER   A CA  
102  C  C   . SER   A 34  ? 0.7325 0.8115 1.0906 -0.0547 -0.1572 -0.0805 13  SER   A C   
103  O  O   . SER   A 34  ? 0.6887 0.7718 1.0260 -0.0353 -0.1487 -0.0962 13  SER   A O   
104  C  CB  . SER   A 34  ? 0.7627 0.7566 1.0946 -0.0730 -0.2025 -0.0891 13  SER   A CB  
105  O  OG  . SER   A 34  ? 0.8170 0.8154 1.1758 -0.0879 -0.1928 -0.0685 13  SER   A OG  
106  N  N   . ARG   A 35  ? 0.7600 0.8570 1.1424 -0.0628 -0.1409 -0.0625 14  ARG   A N   
107  C  CA  . ARG   A 35  ? 0.6737 0.7930 1.0550 -0.0477 -0.1124 -0.0638 14  ARG   A CA  
108  C  C   . ARG   A 35  ? 0.6448 0.7275 1.0043 -0.0440 -0.1106 -0.0764 14  ARG   A C   
109  O  O   . ARG   A 35  ? 0.6780 0.7343 1.0432 -0.0572 -0.1234 -0.0682 14  ARG   A O   
110  C  CB  . ARG   A 35  ? 0.6333 0.8078 1.0525 -0.0520 -0.0923 -0.0342 14  ARG   A CB  
111  C  CG  . ARG   A 35  ? 0.7717 0.9441 1.2130 -0.0692 -0.0924 -0.0125 14  ARG   A CG  
112  C  CD  . ARG   A 35  ? 0.8309 1.0651 1.3087 -0.0735 -0.0741 0.0225  14  ARG   A CD  
113  N  NE  . ARG   A 35  ? 0.8450 1.1065 1.3187 -0.0548 -0.0448 0.0296  14  ARG   A NE  
114  C  CZ  . ARG   A 35  ? 0.7954 1.1103 1.2861 -0.0483 -0.0232 0.0576  14  ARG   A CZ  
115  N  NH1 . ARG   A 35  ? 0.6834 1.0346 1.2038 -0.0614 -0.0263 0.0830  14  ARG   A NH1 
116  N  NH2 . ARG   A 35  ? 0.7260 1.0579 1.1988 -0.0257 0.0018  0.0585  14  ARG   A NH2 
117  N  N   . VAL   A 36  ? 0.5252 0.6057 0.8572 -0.0254 -0.0945 -0.0944 15  VAL   A N   
118  C  CA  . VAL   A 36  ? 0.4788 0.5321 0.7797 -0.0163 -0.0877 -0.1046 15  VAL   A CA  
119  C  C   . VAL   A 36  ? 0.4391 0.5217 0.7438 -0.0103 -0.0610 -0.0932 15  VAL   A C   
120  O  O   . VAL   A 36  ? 0.4330 0.5413 0.7363 -0.0015 -0.0446 -0.0941 15  VAL   A O   
121  C  CB  . VAL   A 36  ? 0.4882 0.5216 0.7477 0.0010  -0.0875 -0.1286 15  VAL   A CB  
122  C  CG1 . VAL   A 36  ? 0.5157 0.5379 0.7497 0.0124  -0.0771 -0.1355 15  VAL   A CG1 
123  C  CG2 . VAL   A 36  ? 0.4518 0.4538 0.6939 0.0028  -0.1134 -0.1398 15  VAL   A CG2 
124  N  N   . GLU   A 37  ? 0.4599 0.5341 0.7651 -0.0126 -0.0587 -0.0833 16  GLU   A N   
125  C  CA  . GLU   A 37  ? 0.4176 0.5175 0.7186 -0.0033 -0.0364 -0.0745 16  GLU   A CA  
126  C  C   . GLU   A 37  ? 0.4697 0.5490 0.7373 0.0090  -0.0345 -0.0897 16  GLU   A C   
127  O  O   . GLU   A 37  ? 0.5266 0.5724 0.7841 0.0089  -0.0485 -0.0921 16  GLU   A O   
128  C  CB  . GLU   A 37  ? 0.4502 0.5695 0.7816 -0.0135 -0.0325 -0.0434 16  GLU   A CB  
129  C  CG  . GLU   A 37  ? 0.5722 0.7221 0.9459 -0.0280 -0.0366 -0.0234 16  GLU   A CG  
130  C  CD  . GLU   A 37  ? 0.6137 0.7916 1.0245 -0.0412 -0.0313 0.0146  16  GLU   A CD  
131  O  OE1 . GLU   A 37  ? 0.7084 0.8836 1.1063 -0.0344 -0.0202 0.0255  16  GLU   A OE1 
132  O  OE2 . GLU   A 37  ? 0.6409 0.8482 1.0957 -0.0585 -0.0383 0.0365  16  GLU   A OE2 
133  N  N   . ALA   A 38  ? 0.3820 0.4803 0.6322 0.0205  -0.0196 -0.1003 17  ALA   A N   
134  C  CA  . ALA   A 38  ? 0.2890 0.3807 0.5134 0.0312  -0.0185 -0.1142 17  ALA   A CA  
135  C  C   . ALA   A 38  ? 0.3553 0.4745 0.5713 0.0392  -0.0044 -0.1142 17  ALA   A C   
136  O  O   . ALA   A 38  ? 0.3437 0.4804 0.5630 0.0399  0.0046  -0.1138 17  ALA   A O   
137  C  CB  . ALA   A 38  ? 0.3128 0.3980 0.5230 0.0337  -0.0218 -0.1324 17  ALA   A CB  
138  N  N   . VAL   A 39  ? 0.3681 0.4895 0.5696 0.0486  -0.0046 -0.1160 18  VAL   A N   
139  C  CA  . VAL   A 39  ? 0.3609 0.5092 0.5498 0.0569  0.0033  -0.1218 18  VAL   A CA  
140  C  C   . VAL   A 39  ? 0.2997 0.4540 0.4793 0.0523  0.0010  -0.1393 18  VAL   A C   
141  O  O   . VAL   A 39  ? 0.3828 0.5304 0.5585 0.0521  -0.0042 -0.1435 18  VAL   A O   
142  C  CB  . VAL   A 39  ? 0.3974 0.5507 0.5750 0.0699  0.0026  -0.1137 18  VAL   A CB  
143  C  CG1 . VAL   A 39  ? 0.3456 0.5304 0.5088 0.0785  0.0050  -0.1250 18  VAL   A CG1 
144  C  CG2 . VAL   A 39  ? 0.4034 0.5536 0.5892 0.0712  0.0073  -0.0890 18  VAL   A CG2 
145  N  N   . TYR   A 40  ? 0.2960 0.4590 0.4679 0.0479  0.0036  -0.1457 19  TYR   A N   
146  C  CA  . TYR   A 40  ? 0.3351 0.5038 0.5054 0.0385  -0.0002 -0.1596 19  TYR   A CA  
147  C  C   . TYR   A 40  ? 0.2756 0.4722 0.4399 0.0428  -0.0036 -0.1694 19  TYR   A C   
148  O  O   . TYR   A 40  ? 0.3125 0.5143 0.4654 0.0509  -0.0028 -0.1729 19  TYR   A O   
149  C  CB  . TYR   A 40  ? 0.3272 0.4800 0.4993 0.0319  0.0015  -0.1660 19  TYR   A CB  
150  C  CG  . TYR   A 40  ? 0.3858 0.5367 0.5603 0.0196  -0.0025 -0.1801 19  TYR   A CG  
151  C  CD1 . TYR   A 40  ? 0.4568 0.6169 0.6237 0.0143  -0.0100 -0.1918 19  TYR   A CD1 
152  C  CD2 . TYR   A 40  ? 0.3882 0.5245 0.5696 0.0102  -0.0018 -0.1770 19  TYR   A CD2 
153  C  CE1 . TYR   A 40  ? 0.4376 0.5901 0.6090 -0.0048 -0.0180 -0.1986 19  TYR   A CE1 
154  C  CE2 . TYR   A 40  ? 0.3831 0.5139 0.5668 -0.0059 -0.0059 -0.1808 19  TYR   A CE2 
155  C  CZ  . TYR   A 40  ? 0.3957 0.5331 0.5768 -0.0159 -0.0146 -0.1908 19  TYR   A CZ  
156  O  OH  . TYR   A 40  ? 0.4107 0.5393 0.5991 -0.0378 -0.0218 -0.1915 19  TYR   A OH  
157  N  N   . VAL   A 41  ? 0.3033 0.5236 0.4742 0.0402  -0.0076 -0.1730 20  VAL   A N   
158  C  CA  . VAL   A 41  ? 0.3043 0.5597 0.4740 0.0417  -0.0147 -0.1808 20  VAL   A CA  
159  C  C   . VAL   A 41  ? 0.3129 0.5712 0.4903 0.0195  -0.0236 -0.1925 20  VAL   A C   
160  O  O   . VAL   A 41  ? 0.3595 0.6194 0.5525 0.0047  -0.0227 -0.1887 20  VAL   A O   
161  C  CB  . VAL   A 41  ? 0.2913 0.5706 0.4592 0.0511  -0.0157 -0.1709 20  VAL   A CB  
162  C  CG1 . VAL   A 41  ? 0.2278 0.5510 0.3965 0.0538  -0.0247 -0.1775 20  VAL   A CG1 
163  C  CG2 . VAL   A 41  ? 0.3260 0.5794 0.4783 0.0683  -0.0115 -0.1560 20  VAL   A CG2 
164  N  N   . LEU   A 42  ? 0.2848 0.5407 0.4487 0.0177  -0.0336 -0.2060 21  LEU   A N   
165  C  CA  . LEU   A 42  ? 0.3290 0.5761 0.4975 -0.0058 -0.0478 -0.2186 21  LEU   A CA  
166  C  C   . LEU   A 42  ? 0.3377 0.6204 0.5280 -0.0220 -0.0515 -0.2067 21  LEU   A C   
167  O  O   . LEU   A 42  ? 0.2998 0.6247 0.4951 -0.0104 -0.0501 -0.2002 21  LEU   A O   
168  C  CB  . LEU   A 42  ? 0.3282 0.5615 0.4689 0.0018  -0.0599 -0.2336 21  LEU   A CB  
169  C  CG  . LEU   A 42  ? 0.4272 0.6285 0.5395 0.0242  -0.0519 -0.2390 21  LEU   A CG  
170  C  CD1 . LEU   A 42  ? 0.4183 0.6083 0.4977 0.0367  -0.0644 -0.2519 21  LEU   A CD1 
171  C  CD2 . LEU   A 42  ? 0.4394 0.5976 0.5546 0.0169  -0.0442 -0.2330 21  LEU   A CD2 
172  N  N   . GLY   A 43  ? 0.3243 0.5897 0.5258 -0.0477 -0.0563 -0.2007 22  GLY   A N   
173  C  CA  . GLY   A 43  ? 0.3703 0.6740 0.5977 -0.0655 -0.0575 -0.1834 22  GLY   A CA  
174  C  C   . GLY   A 43  ? 0.3371 0.6519 0.5788 -0.0637 -0.0411 -0.1669 22  GLY   A C   
175  O  O   . GLY   A 43  ? 0.3459 0.6968 0.6103 -0.0767 -0.0392 -0.1487 22  GLY   A O   
176  N  N   . THR   A 44  ? 0.3597 0.6486 0.5899 -0.0466 -0.0300 -0.1715 23  THR   A N   
177  C  CA  . THR   A 44  ? 0.3226 0.6142 0.5602 -0.0419 -0.0172 -0.1597 23  THR   A CA  
178  C  C   . THR   A 44  ? 0.4037 0.6472 0.6380 -0.0505 -0.0162 -0.1655 23  THR   A C   
179  O  O   . THR   A 44  ? 0.4258 0.6301 0.6459 -0.0541 -0.0236 -0.1778 23  THR   A O   
180  C  CB  . THR   A 44  ? 0.3539 0.6517 0.5773 -0.0114 -0.0086 -0.1584 23  THR   A CB  
181  O  OG1 . THR   A 44  ? 0.3750 0.6327 0.5871 -0.0018 -0.0075 -0.1679 23  THR   A OG1 
182  C  CG2 . THR   A 44  ? 0.3192 0.6448 0.5345 0.0021  -0.0127 -0.1583 23  THR   A CG2 
183  N  N   . TYR   A 45  ? 0.3731 0.6126 0.6086 -0.0473 -0.0058 -0.1527 24  TYR   A N   
184  C  CA  . TYR   A 45  ? 0.3988 0.5886 0.6204 -0.0449 -0.0027 -0.1534 24  TYR   A CA  
185  C  C   . TYR   A 45  ? 0.3450 0.5386 0.5579 -0.0249 0.0065  -0.1455 24  TYR   A C   
186  O  O   . TYR   A 45  ? 0.3216 0.5522 0.5371 -0.0141 0.0115  -0.1384 24  TYR   A O   
187  C  CB  . TYR   A 45  ? 0.4432 0.6083 0.6718 -0.0693 -0.0059 -0.1463 24  TYR   A CB  
188  C  CG  . TYR   A 45  ? 0.4537 0.6533 0.7011 -0.0824 0.0014  -0.1236 24  TYR   A CG  
189  C  CD1 . TYR   A 45  ? 0.4635 0.7070 0.7384 -0.1055 -0.0033 -0.1142 24  TYR   A CD1 
190  C  CD2 . TYR   A 45  ? 0.5149 0.7092 0.7536 -0.0713 0.0129  -0.1094 24  TYR   A CD2 
191  C  CE1 . TYR   A 45  ? 0.4996 0.7860 0.7966 -0.1174 0.0063  -0.0872 24  TYR   A CE1 
192  C  CE2 . TYR   A 45  ? 0.5160 0.7484 0.7691 -0.0794 0.0227  -0.0847 24  TYR   A CE2 
193  C  CZ  . TYR   A 45  ? 0.5592 0.8400 0.8433 -0.1027 0.0210  -0.0717 24  TYR   A CZ  
194  O  OH  . TYR   A 45  ? 0.6166 0.9463 0.9197 -0.1105 0.0337  -0.0411 24  TYR   A OH  
195  N  N   . LEU   A 46  ? 0.3575 0.5135 0.5580 -0.0170 0.0070  -0.1481 25  LEU   A N   
196  C  CA  . LEU   A 46  ? 0.3925 0.5441 0.5817 0.0012  0.0095  -0.1451 25  LEU   A CA  
197  C  C   . LEU   A 46  ? 0.3820 0.5251 0.5665 -0.0012 0.0141  -0.1334 25  LEU   A C   
198  O  O   . LEU   A 46  ? 0.4227 0.5416 0.6094 -0.0142 0.0140  -0.1297 25  LEU   A O   
199  C  CB  . LEU   A 46  ? 0.3478 0.4723 0.5316 0.0107  0.0043  -0.1527 25  LEU   A CB  
200  C  CG  . LEU   A 46  ? 0.3483 0.4765 0.5359 0.0118  0.0019  -0.1595 25  LEU   A CG  
201  C  CD1 . LEU   A 46  ? 0.3522 0.4628 0.5401 0.0191  -0.0011 -0.1582 25  LEU   A CD1 
202  C  CD2 . LEU   A 46  ? 0.3343 0.4898 0.5214 0.0193  0.0015  -0.1601 25  LEU   A CD2 
203  N  N   . TRP   A 47  ? 0.3531 0.5135 0.5262 0.0147  0.0176  -0.1276 26  TRP   A N   
204  C  CA  . TRP   A 47  ? 0.3645 0.5131 0.5237 0.0224  0.0202  -0.1186 26  TRP   A CA  
205  C  C   . TRP   A 47  ? 0.3346 0.4599 0.4779 0.0406  0.0092  -0.1311 26  TRP   A C   
206  O  O   . TRP   A 47  ? 0.3680 0.4970 0.5034 0.0540  0.0029  -0.1410 26  TRP   A O   
207  C  CB  . TRP   A 47  ? 0.3962 0.5839 0.5490 0.0310  0.0312  -0.1023 26  TRP   A CB  
208  C  CG  . TRP   A 47  ? 0.4485 0.6449 0.5728 0.0631  0.0289  -0.1085 26  TRP   A CG  
209  C  CD1 . TRP   A 47  ? 0.4383 0.6599 0.5529 0.0831  0.0291  -0.1152 26  TRP   A CD1 
210  C  CD2 . TRP   A 47  ? 0.4731 0.6496 0.5695 0.0825  0.0235  -0.1105 26  TRP   A CD2 
211  N  NE1 . TRP   A 47  ? 0.4880 0.6993 0.5667 0.1146  0.0230  -0.1236 26  TRP   A NE1 
212  C  CE2 . TRP   A 47  ? 0.4789 0.6643 0.5465 0.1134  0.0184  -0.1215 26  TRP   A CE2 
213  C  CE3 . TRP   A 47  ? 0.5427 0.6935 0.6328 0.0795  0.0205  -0.1052 26  TRP   A CE3 
214  C  CZ2 . TRP   A 47  ? 0.5233 0.6907 0.5547 0.1393  0.0078  -0.1299 26  TRP   A CZ2 
215  C  CZ3 . TRP   A 47  ? 0.6028 0.7436 0.6611 0.1045  0.0115  -0.1108 26  TRP   A CZ3 
216  C  CH2 . TRP   A 47  ? 0.5639 0.7120 0.5927 0.1331  0.0040  -0.1242 26  TRP   A CH2 
217  N  N   . THR   A 48  ? 0.3463 0.4459 0.4866 0.0401  0.0047  -0.1302 27  THR   A N   
218  C  CA  . THR   A 48  ? 0.4028 0.4842 0.5389 0.0498  -0.0093 -0.1403 27  THR   A CA  
219  C  C   . THR   A 48  ? 0.3743 0.4494 0.4907 0.0639  -0.0148 -0.1366 27  THR   A C   
220  O  O   . THR   A 48  ? 0.4215 0.4905 0.5366 0.0615  -0.0090 -0.1254 27  THR   A O   
221  C  CB  . THR   A 48  ? 0.3667 0.4346 0.5223 0.0393  -0.0115 -0.1421 27  THR   A CB  
222  O  OG1 . THR   A 48  ? 0.4494 0.5248 0.6168 0.0302  -0.0068 -0.1459 27  THR   A OG1 
223  C  CG2 . THR   A 48  ? 0.4010 0.4617 0.5627 0.0446  -0.0264 -0.1470 27  THR   A CG2 
224  N  N   . ASP   A 49  ? 0.3760 0.4482 0.4729 0.0807  -0.0280 -0.1469 28  ASP   A N   
225  C  CA  . ASP   A 49  ? 0.4570 0.5217 0.5308 0.0970  -0.0397 -0.1485 28  ASP   A CA  
226  C  C   . ASP   A 49  ? 0.4725 0.5232 0.5651 0.0890  -0.0556 -0.1520 28  ASP   A C   
227  O  O   . ASP   A 49  ? 0.4506 0.4929 0.5602 0.0807  -0.0692 -0.1609 28  ASP   A O   
228  C  CB  . ASP   A 49  ? 0.4786 0.5388 0.5195 0.1201  -0.0531 -0.1631 28  ASP   A CB  
229  C  CG  . ASP   A 49  ? 0.5181 0.5643 0.5318 0.1377  -0.0742 -0.1719 28  ASP   A CG  
230  O  OD1 . ASP   A 49  ? 0.6030 0.6517 0.6230 0.1344  -0.0748 -0.1626 28  ASP   A OD1 
231  O  OD2 . ASP   A 49  ? 0.6466 0.6768 0.6291 0.1575  -0.0926 -0.1897 28  ASP   A OD2 
232  N  N   . VAL   A 50  ? 0.4298 0.4812 0.5213 0.0921  -0.0533 -0.1417 29  VAL   A N   
233  C  CA  . VAL   A 50  ? 0.5034 0.5533 0.6119 0.0905  -0.0692 -0.1428 29  VAL   A CA  
234  C  C   . VAL   A 50  ? 0.4677 0.5168 0.5516 0.1081  -0.0903 -0.1489 29  VAL   A C   
235  O  O   . VAL   A 50  ? 0.5082 0.5621 0.6092 0.1055  -0.1104 -0.1519 29  VAL   A O   
236  C  CB  . VAL   A 50  ? 0.4714 0.5220 0.5949 0.0872  -0.0555 -0.1286 29  VAL   A CB  
237  C  CG1 . VAL   A 50  ? 0.3974 0.4447 0.5397 0.0722  -0.0396 -0.1271 29  VAL   A CG1 
238  C  CG2 . VAL   A 50  ? 0.4280 0.4724 0.5246 0.0996  -0.0448 -0.1151 29  VAL   A CG2 
239  N  N   . TYR   A 51  ? 0.4707 0.5193 0.5151 0.1271  -0.0873 -0.1500 30  TYR   A N   
240  C  CA  . TYR   A 51  ? 0.5431 0.5916 0.5539 0.1499  -0.1063 -0.1557 30  TYR   A CA  
241  C  C   . TYR   A 51  ? 0.6321 0.6643 0.6313 0.1541  -0.1396 -0.1809 30  TYR   A C   
242  O  O   . TYR   A 51  ? 0.5867 0.6167 0.5804 0.1599  -0.1675 -0.1897 30  TYR   A O   
243  C  CB  . TYR   A 51  ? 0.5849 0.6435 0.5541 0.1725  -0.0877 -0.1443 30  TYR   A CB  
244  C  CG  . TYR   A 51  ? 0.6079 0.6689 0.5311 0.2033  -0.1052 -0.1501 30  TYR   A CG  
245  C  CD1 . TYR   A 51  ? 0.6438 0.7112 0.5615 0.2123  -0.1083 -0.1370 30  TYR   A CD1 
246  C  CD2 . TYR   A 51  ? 0.6294 0.6848 0.5091 0.2280  -0.1195 -0.1697 30  TYR   A CD2 
247  C  CE1 . TYR   A 51  ? 0.6637 0.7361 0.5353 0.2432  -0.1258 -0.1425 30  TYR   A CE1 
248  C  CE2 . TYR   A 51  ? 0.6071 0.6635 0.4368 0.2606  -0.1377 -0.1780 30  TYR   A CE2 
249  C  CZ  . TYR   A 51  ? 0.6205 0.6876 0.4471 0.2672  -0.1410 -0.1640 30  TYR   A CZ  
250  O  OH  . TYR   A 51  ? 0.8062 0.8769 0.5794 0.3023  -0.1606 -0.1725 30  TYR   A OH  
251  N  N   A SER   A 52  ? 0.5678 0.5856 0.5625 0.1513  -0.1400 -0.1928 31  SER   A N   
252  N  N   B SER   A 52  ? 0.5677 0.5855 0.5625 0.1513  -0.1400 -0.1928 31  SER   A N   
253  C  CA  A SER   A 52  ? 0.5967 0.5853 0.5750 0.1560  -0.1737 -0.2164 31  SER   A CA  
254  C  CA  B SER   A 52  ? 0.5967 0.5852 0.5752 0.1559  -0.1736 -0.2163 31  SER   A CA  
255  C  C   A SER   A 52  ? 0.6066 0.5885 0.6336 0.1262  -0.1946 -0.2138 31  SER   A C   
256  C  C   B SER   A 52  ? 0.6066 0.5884 0.6336 0.1262  -0.1946 -0.2138 31  SER   A C   
257  O  O   A SER   A 52  ? 0.6621 0.6231 0.6854 0.1242  -0.2198 -0.2185 31  SER   A O   
258  O  O   B SER   A 52  ? 0.6621 0.6231 0.6854 0.1242  -0.2198 -0.2185 31  SER   A O   
259  C  CB  A SER   A 52  ? 0.6266 0.6050 0.5943 0.1593  -0.1614 -0.2139 31  SER   A CB  
260  C  CB  B SER   A 52  ? 0.6265 0.6047 0.5944 0.1591  -0.1614 -0.2139 31  SER   A CB  
261  O  OG  A SER   A 52  ? 0.5902 0.5866 0.5181 0.1867  -0.1410 -0.2102 31  SER   A OG  
262  O  OG  B SER   A 52  ? 0.6547 0.6359 0.6638 0.1333  -0.1477 -0.2058 31  SER   A OG  
263  N  N   . ALA   A 53  ? 0.5216 0.5230 0.5953 0.1034  -0.1803 -0.2014 32  ALA   A N   
264  C  CA  . ALA   A 53  ? 0.5273 0.5358 0.6508 0.0770  -0.1952 -0.1933 32  ALA   A CA  
265  C  C   . ALA   A 53  ? 0.5296 0.5663 0.6715 0.0773  -0.2103 -0.1878 32  ALA   A C   
266  O  O   . ALA   A 53  ? 0.5447 0.5932 0.7251 0.0569  -0.2207 -0.1759 32  ALA   A O   
267  C  CB  . ALA   A 53  ? 0.5636 0.5885 0.7273 0.0583  -0.1710 -0.1792 32  ALA   A CB  
268  N  N   . ALA   A 54  ? 0.5780 0.6250 0.6892 0.1005  -0.1999 -0.1844 33  ALA   A N   
269  C  CA  . ALA   A 54  ? 0.5163 0.5909 0.6405 0.1063  -0.2114 -0.1757 33  ALA   A CA  
270  C  C   . ALA   A 54  ? 0.5368 0.6027 0.6552 0.1034  -0.2511 -0.1893 33  ALA   A C   
271  O  O   . ALA   A 54  ? 0.5911 0.6220 0.6651 0.1153  -0.2620 -0.2052 33  ALA   A O   
272  C  CB  . ALA   A 54  ? 0.4660 0.5447 0.5505 0.1340  -0.1912 -0.1665 33  ALA   A CB  
273  N  N   . PRO   A 55  ? 0.5780 0.6717 0.7369 0.0876  -0.2629 -0.1765 34  PRO   A N   
274  C  CA  . PRO   A 55  ? 0.5605 0.6446 0.7116 0.0813  -0.2937 -0.1833 34  PRO   A CA  
275  C  C   . PRO   A 55  ? 0.5407 0.6182 0.6355 0.1153  -0.3048 -0.1967 34  PRO   A C   
276  O  O   . PRO   A 55  ? 0.5687 0.6640 0.6418 0.1414  -0.2890 -0.1915 34  PRO   A O   
277  C  CB  . PRO   A 55  ? 0.5443 0.6794 0.7535 0.0610  -0.2985 -0.1614 34  PRO   A CB  
278  C  CG  . PRO   A 55  ? 0.4898 0.6502 0.7382 0.0534  -0.2683 -0.1437 34  PRO   A CG  
279  C  CD  . PRO   A 55  ? 0.4770 0.6169 0.6893 0.0779  -0.2478 -0.1541 34  PRO   A CD  
280  N  N   . ALA   A 56  ? 0.5784 0.6288 0.6470 0.1169  -0.3319 -0.2120 35  ALA   A N   
281  C  CA  . ALA   A 56  ? 0.6276 0.6744 0.6406 0.1514  -0.3428 -0.2239 35  ALA   A CA  
282  C  C   . ALA   A 56  ? 0.6293 0.7257 0.6575 0.1607  -0.3423 -0.2078 35  ALA   A C   
283  O  O   . ALA   A 56  ? 0.6145 0.7467 0.6982 0.1368  -0.3482 -0.1923 35  ALA   A O   
284  C  CB  . ALA   A 56  ? 0.7029 0.7155 0.6933 0.1498  -0.3765 -0.2431 35  ALA   A CB  
285  N  N   . GLY   A 57  ? 0.6342 0.7365 0.6118 0.1983  -0.3324 -0.2072 36  GLY   A N   
286  C  CA  . GLY   A 57  ? 0.6287 0.7718 0.6109 0.2148  -0.3292 -0.1889 36  GLY   A CA  
287  C  C   . GLY   A 57  ? 0.5779 0.7480 0.5942 0.2153  -0.3006 -0.1642 36  GLY   A C   
288  O  O   . GLY   A 57  ? 0.6452 0.8377 0.6513 0.2393  -0.2900 -0.1459 36  GLY   A O   
289  N  N   . ALA   A 58  ? 0.5690 0.7337 0.6236 0.1921  -0.2866 -0.1621 37  ALA   A N   
290  C  CA  . ALA   A 58  ? 0.5499 0.7335 0.6355 0.1953  -0.2576 -0.1408 37  ALA   A CA  
291  C  C   . ALA   A 58  ? 0.5967 0.7575 0.6312 0.2216  -0.2239 -0.1267 37  ALA   A C   
292  O  O   . ALA   A 58  ? 0.6115 0.7472 0.5996 0.2317  -0.2179 -0.1349 37  ALA   A O   
293  C  CB  . ALA   A 58  ? 0.5118 0.6823 0.6345 0.1643  -0.2413 -0.1423 37  ALA   A CB  
294  N  N   . GLN   A 59  ? 0.5551 0.7250 0.5989 0.2337  -0.2016 -0.1032 38  GLN   A N   
295  C  CA  . GLN   A 59  ? 0.5968 0.7437 0.5956 0.2572  -0.1743 -0.0840 38  GLN   A CA  
296  C  C   . GLN   A 59  ? 0.6171 0.7355 0.6271 0.2450  -0.1369 -0.0688 38  GLN   A C   
297  O  O   . GLN   A 59  ? 0.6216 0.7136 0.5991 0.2492  -0.1145 -0.0570 38  GLN   A O   
298  C  CB  . GLN   A 59  ? 0.6498 0.8172 0.6358 0.2876  -0.1828 -0.0677 38  GLN   A CB  
299  C  CG  . GLN   A 59  ? 0.8323 0.9793 0.7593 0.3169  -0.1664 -0.0484 38  GLN   A CG  
300  C  CD  . GLN   A 59  ? 0.9263 1.0823 0.8045 0.3354  -0.1883 -0.0623 38  GLN   A CD  
301  O  OE1 . GLN   A 59  ? 0.8935 1.0543 0.7757 0.3225  -0.2125 -0.0903 38  GLN   A OE1 
302  N  NE2 . GLN   A 59  ? 0.9866 1.1411 0.8139 0.3685  -0.1806 -0.0424 38  GLN   A NE2 
303  N  N   . THR   A 60  ? 0.6016 0.7271 0.6562 0.2303  -0.1308 -0.0679 39  THR   A N   
304  C  CA  . THR   A 60  ? 0.5760 0.6703 0.6367 0.2216  -0.1007 -0.0576 39  THR   A CA  
305  C  C   . THR   A 60  ? 0.5298 0.6343 0.6328 0.1963  -0.0992 -0.0700 39  THR   A C   
306  O  O   . THR   A 60  ? 0.4840 0.6218 0.6180 0.1856  -0.1200 -0.0806 39  THR   A O   
307  C  CB  . THR   A 60  ? 0.5473 0.6316 0.6036 0.2453  -0.0904 -0.0385 39  THR   A CB  
308  O  OG1 . THR   A 60  ? 0.5453 0.6742 0.6382 0.2538  -0.1058 -0.0403 39  THR   A OG1 
309  C  CG2 . THR   A 60  ? 0.5695 0.6417 0.5815 0.2717  -0.0909 -0.0217 39  THR   A CG2 
310  N  N   . PHE   A 61  ? 0.4666 0.5414 0.5709 0.1857  -0.0758 -0.0672 40  PHE   A N   
311  C  CA  . PHE   A 61  ? 0.4651 0.5492 0.6037 0.1668  -0.0709 -0.0761 40  PHE   A CA  
312  C  C   . PHE   A 61  ? 0.4867 0.5414 0.6217 0.1724  -0.0499 -0.0697 40  PHE   A C   
313  O  O   . PHE   A 61  ? 0.5574 0.5703 0.6628 0.1784  -0.0380 -0.0612 40  PHE   A O   
314  C  CB  . PHE   A 61  ? 0.4290 0.5050 0.5673 0.1431  -0.0703 -0.0893 40  PHE   A CB  
315  C  CG  . PHE   A 61  ? 0.4431 0.4839 0.5567 0.1363  -0.0503 -0.0858 40  PHE   A CG  
316  C  CD1 . PHE   A 61  ? 0.4814 0.5105 0.5621 0.1437  -0.0470 -0.0778 40  PHE   A CD1 
317  C  CD2 . PHE   A 61  ? 0.4243 0.4487 0.5489 0.1225  -0.0357 -0.0886 40  PHE   A CD2 
318  C  CE1 . PHE   A 61  ? 0.4660 0.4724 0.5330 0.1333  -0.0287 -0.0691 40  PHE   A CE1 
319  C  CE2 . PHE   A 61  ? 0.4395 0.4360 0.5478 0.1116  -0.0214 -0.0844 40  PHE   A CE2 
320  C  CZ  . PHE   A 61  ? 0.4315 0.4215 0.5150 0.1148  -0.0175 -0.0729 40  PHE   A CZ  
321  N  N   . SER   A 62  ? 0.4475 0.5233 0.6115 0.1711  -0.0467 -0.0730 41  SER   A N   
322  C  CA  . SER   A 62  ? 0.4571 0.5046 0.6145 0.1771  -0.0296 -0.0740 41  SER   A CA  
323  C  C   . SER   A 62  ? 0.4147 0.4759 0.5935 0.1558  -0.0252 -0.0847 41  SER   A C   
324  O  O   . SER   A 62  ? 0.3430 0.4323 0.5430 0.1373  -0.0351 -0.0888 41  SER   A O   
325  C  CB  . SER   A 62  ? 0.4401 0.5052 0.6035 0.2090  -0.0273 -0.0654 41  SER   A CB  
326  O  OG  . SER   A 62  ? 0.4338 0.5672 0.6402 0.2089  -0.0363 -0.0616 41  SER   A OG  
327  N  N   . LEU   A 63  ? 0.4493 0.4863 0.6186 0.1603  -0.0122 -0.0898 42  LEU   A N   
328  C  CA  . LEU   A 63  ? 0.4597 0.5094 0.6440 0.1426  -0.0076 -0.0989 42  LEU   A CA  
329  C  C   . LEU   A 63  ? 0.4152 0.4572 0.5911 0.1614  0.0040  -0.1031 42  LEU   A C   
330  O  O   . LEU   A 63  ? 0.5642 0.5666 0.7094 0.1803  0.0086  -0.1023 42  LEU   A O   
331  C  CB  . LEU   A 63  ? 0.4225 0.4413 0.5921 0.1176  -0.0066 -0.1074 42  LEU   A CB  
332  C  CG  . LEU   A 63  ? 0.5224 0.4853 0.6614 0.1155  -0.0001 -0.1103 42  LEU   A CG  
333  C  CD1 . LEU   A 63  ? 0.4824 0.4276 0.6142 0.1160  0.0056  -0.1227 42  LEU   A CD1 
334  C  CD2 . LEU   A 63  ? 0.4363 0.3887 0.5687 0.0931  -0.0010 -0.1082 42  LEU   A CD2 
335  N  N   . LYS   A 64  ? 0.4102 0.4854 0.6035 0.1529  0.0087  -0.1025 43  LYS   A N   
336  C  CA  . LYS   A 64  ? 0.5022 0.5702 0.6755 0.1645  0.0207  -0.1036 43  LYS   A CA  
337  C  C   . LYS   A 64  ? 0.4205 0.4807 0.5908 0.1425  0.0214  -0.1142 43  LYS   A C   
338  O  O   . LYS   A 64  ? 0.4246 0.4994 0.6170 0.1202  0.0151  -0.1161 43  LYS   A O   
339  C  CB  . LYS   A 64  ? 0.4727 0.6000 0.6711 0.1805  0.0284  -0.0857 43  LYS   A CB  
340  C  CG  . LYS   A 64  ? 0.4753 0.6328 0.6921 0.1967  0.0245  -0.0710 43  LYS   A CG  
341  C  CD  . LYS   A 64  ? 0.6637 0.7784 0.8424 0.2238  0.0290  -0.0741 43  LYS   A CD  
342  C  CE  . LYS   A 64  ? 0.7362 0.8995 0.9319 0.2468  0.0322  -0.0572 43  LYS   A CE  
343  N  NZ  . LYS   A 64  ? 0.7488 0.9703 0.9914 0.2365  0.0208  -0.0417 43  LYS   A NZ  
344  N  N   . HIS   A 65  ? 0.4496 0.4855 0.5900 0.1505  0.0278  -0.1217 44  HIS   A N   
345  C  CA  . HIS   A 65  ? 0.4412 0.4782 0.5785 0.1335  0.0276  -0.1300 44  HIS   A CA  
346  C  C   . HIS   A 65  ? 0.4954 0.5235 0.6031 0.1522  0.0350  -0.1344 44  HIS   A C   
347  O  O   . HIS   A 65  ? 0.5285 0.5319 0.6112 0.1740  0.0380  -0.1365 44  HIS   A O   
348  C  CB  . HIS   A 65  ? 0.4639 0.4626 0.5919 0.1089  0.0187  -0.1426 44  HIS   A CB  
349  C  CG  . HIS   A 65  ? 0.5457 0.4854 0.6391 0.1120  0.0147  -0.1522 44  HIS   A CG  
350  N  ND1 . HIS   A 65  ? 0.5145 0.4255 0.5776 0.1156  0.0128  -0.1635 44  HIS   A ND1 
351  C  CD2 . HIS   A 65  ? 0.5199 0.4193 0.6039 0.1109  0.0106  -0.1514 44  HIS   A CD2 
352  C  CE1 . HIS   A 65  ? 0.6006 0.4533 0.6385 0.1135  0.0062  -0.1698 44  HIS   A CE1 
353  N  NE2 . HIS   A 65  ? 0.5499 0.3937 0.6002 0.1108  0.0058  -0.1612 44  HIS   A NE2 
354  N  N   . SER   A 66  ? 0.4930 0.5409 0.6025 0.1450  0.0371  -0.1364 45  SER   A N   
355  C  CA  . SER   A 66  ? 0.5067 0.5534 0.5882 0.1640  0.0433  -0.1408 45  SER   A CA  
356  C  C   . SER   A 66  ? 0.5483 0.5365 0.5901 0.1592  0.0318  -0.1632 45  SER   A C   
357  O  O   . SER   A 66  ? 0.5463 0.5003 0.5878 0.1375  0.0210  -0.1715 45  SER   A O   
358  C  CB  . SER   A 66  ? 0.4646 0.5579 0.5635 0.1604  0.0503  -0.1309 45  SER   A CB  
359  O  OG  . SER   A 66  ? 0.4732 0.5655 0.5871 0.1337  0.0418  -0.1362 45  SER   A OG  
360  N  N   . GLU   A 67  ? 0.6176 0.5976 0.6276 0.1785  0.0329  -0.1719 46  GLU   A N   
361  C  CA  . GLU   A 67  ? 0.6584 0.5785 0.6294 0.1766  0.0188  -0.1936 46  GLU   A CA  
362  C  C   . GLU   A 67  ? 0.6502 0.5574 0.6249 0.1461  0.0054  -0.2048 46  GLU   A C   
363  O  O   . GLU   A 67  ? 0.7202 0.5782 0.6828 0.1277  -0.0082 -0.2160 46  GLU   A O   
364  C  CB  . GLU   A 67  ? 0.6982 0.6175 0.6327 0.2073  0.0196  -0.2020 46  GLU   A CB  
365  C  CG  . GLU   A 67  ? 0.8815 0.7889 0.7987 0.2376  0.0246  -0.1987 46  GLU   A CG  
366  C  CD  . GLU   A 67  ? 0.9805 0.8192 0.8818 0.2295  0.0127  -0.2097 46  GLU   A CD  
367  O  OE1 . GLU   A 67  ? 1.0466 0.8359 0.9319 0.2078  -0.0029 -0.2262 46  GLU   A OE1 
368  O  OE2 . GLU   A 67  ? 1.0247 0.8605 0.9312 0.2439  0.0183  -0.1999 46  GLU   A OE2 
369  N  N   . HIS   A 68  ? 0.6232 0.5763 0.6171 0.1394  0.0089  -0.1999 47  HIS   A N   
370  C  CA  . HIS   A 68  ? 0.6084 0.5606 0.6071 0.1153  -0.0038 -0.2106 47  HIS   A CA  
371  C  C   . HIS   A 68  ? 0.5586 0.5249 0.5957 0.0868  -0.0053 -0.2031 47  HIS   A C   
372  O  O   . HIS   A 68  ? 0.5430 0.5246 0.5933 0.0682  -0.0123 -0.2079 47  HIS   A O   
373  C  CB  . HIS   A 68  ? 0.5756 0.5690 0.5702 0.1273  0.0002  -0.2102 47  HIS   A CB  
374  C  CG  . HIS   A 68  ? 0.6838 0.6677 0.6377 0.1569  0.0004  -0.2183 47  HIS   A CG  
375  N  ND1 . HIS   A 68  ? 0.7623 0.7896 0.7118 0.1827  0.0151  -0.2049 47  HIS   A ND1 
376  C  CD2 . HIS   A 68  ? 0.6775 0.6135 0.5931 0.1652  -0.0132 -0.2374 47  HIS   A CD2 
377  C  CE1 . HIS   A 68  ? 0.8041 0.8148 0.7123 0.2088  0.0107  -0.2162 47  HIS   A CE1 
378  N  NE2 . HIS   A 68  ? 0.8204 0.7731 0.7066 0.1993  -0.0075 -0.2378 47  HIS   A NE2 
379  N  N   . VAL   A 69  ? 0.5623 0.5271 0.6169 0.0854  0.0010  -0.1916 48  VAL   A N   
380  C  CA  . VAL   A 69  ? 0.5668 0.5399 0.6519 0.0617  -0.0007 -0.1854 48  VAL   A CA  
381  C  C   . VAL   A 69  ? 0.5485 0.4742 0.6234 0.0537  -0.0065 -0.1870 48  VAL   A C   
382  O  O   . VAL   A 69  ? 0.6047 0.5100 0.6676 0.0711  -0.0024 -0.1828 48  VAL   A O   
383  C  CB  . VAL   A 69  ? 0.4837 0.4944 0.5973 0.0659  0.0090  -0.1703 48  VAL   A CB  
384  C  CG1 . VAL   A 69  ? 0.3892 0.4039 0.5258 0.0458  0.0063  -0.1664 48  VAL   A CG1 
385  C  CG2 . VAL   A 69  ? 0.4444 0.4948 0.5673 0.0723  0.0149  -0.1649 48  VAL   A CG2 
386  N  N   . TRP   A 70  ? 0.5559 0.4657 0.6367 0.0282  -0.0157 -0.1913 49  TRP   A N   
387  C  CA  . TRP   A 70  ? 0.5397 0.4075 0.6188 0.0148  -0.0204 -0.1879 49  TRP   A CA  
388  C  C   . TRP   A 70  ? 0.5321 0.4255 0.6409 0.0090  -0.0118 -0.1764 49  TRP   A C   
389  O  O   . TRP   A 70  ? 0.5189 0.4549 0.6506 0.0002  -0.0079 -0.1743 49  TRP   A O   
390  C  CB  . TRP   A 70  ? 0.6086 0.4533 0.6874 -0.0149 -0.0345 -0.1931 49  TRP   A CB  
391  C  CG  . TRP   A 70  ? 0.7056 0.5197 0.7512 -0.0116 -0.0472 -0.2077 49  TRP   A CG  
392  C  CD1 . TRP   A 70  ? 0.7049 0.5478 0.7464 -0.0083 -0.0515 -0.2178 49  TRP   A CD1 
393  C  CD2 . TRP   A 70  ? 0.8892 0.6352 0.8988 -0.0101 -0.0574 -0.2155 49  TRP   A CD2 
394  N  NE1 . TRP   A 70  ? 0.8692 0.6683 0.8738 -0.0044 -0.0646 -0.2327 49  TRP   A NE1 
395  C  CE2 . TRP   A 70  ? 0.9100 0.6483 0.8947 -0.0060 -0.0680 -0.2323 49  TRP   A CE2 
396  C  CE3 . TRP   A 70  ? 0.9605 0.6495 0.9559 -0.0101 -0.0581 -0.2104 49  TRP   A CE3 
397  C  CZ2 . TRP   A 70  ? 0.9746 0.6519 0.9226 -0.0026 -0.0795 -0.2466 49  TRP   A CZ2 
398  C  CZ3 . TRP   A 70  ? 1.0156 0.6426 0.9759 -0.0068 -0.0683 -0.2228 49  TRP   A CZ3 
399  C  CH2 . TRP   A 70  ? 1.0253 0.6477 0.9633 -0.0033 -0.0792 -0.2420 49  TRP   A CH2 
400  N  N   . VAL   A 71  ? 0.5459 0.4107 0.6503 0.0176  -0.0092 -0.1698 50  VAL   A N   
401  C  CA  . VAL   A 71  ? 0.5252 0.4144 0.6472 0.0173  -0.0021 -0.1547 50  VAL   A CA  
402  C  C   . VAL   A 71  ? 0.5445 0.3960 0.6588 0.0066  -0.0033 -0.1401 50  VAL   A C   
403  O  O   . VAL   A 71  ? 0.6135 0.4128 0.7072 0.0163  -0.0075 -0.1415 50  VAL   A O   
404  C  CB  . VAL   A 71  ? 0.5284 0.4388 0.6531 0.0438  0.0029  -0.1515 50  VAL   A CB  
405  C  CG1 . VAL   A 71  ? 0.4634 0.3959 0.5985 0.0433  0.0047  -0.1364 50  VAL   A CG1 
406  C  CG2 . VAL   A 71  ? 0.4946 0.4451 0.6288 0.0497  0.0051  -0.1561 50  VAL   A CG2 
407  N  N   . GLU   A 72  ? 0.5428 0.4203 0.6711 -0.0102 0.0009  -0.1243 51  GLU   A N   
408  C  CA  . GLU   A 72  ? 0.5520 0.4062 0.6758 -0.0199 0.0035  -0.1025 51  GLU   A CA  
409  C  C   . GLU   A 72  ? 0.5478 0.4371 0.6717 -0.0046 0.0115  -0.0882 51  GLU   A C   
410  O  O   . GLU   A 72  ? 0.4826 0.4184 0.6165 -0.0014 0.0139  -0.0922 51  GLU   A O   
411  C  CB  . GLU   A 72  ? 0.5398 0.4013 0.6800 -0.0537 0.0023  -0.0910 51  GLU   A CB  
412  C  CG  . GLU   A 72  ? 0.6157 0.4406 0.7560 -0.0738 -0.0118 -0.1064 51  GLU   A CG  
413  C  CD  . GLU   A 72  ? 0.6520 0.5097 0.8203 -0.1090 -0.0147 -0.0960 51  GLU   A CD  
414  O  OE1 . GLU   A 72  ? 0.5959 0.5089 0.7793 -0.1091 -0.0125 -0.1043 51  GLU   A OE1 
415  O  OE2 . GLU   A 72  ? 0.6432 0.4741 0.8204 -0.1365 -0.0194 -0.0766 51  GLU   A OE2 
416  N  N   . VAL   A 73  ? 0.5374 0.3998 0.6458 0.0075  0.0133  -0.0731 52  VAL   A N   
417  C  CA  . VAL   A 73  ? 0.5425 0.4344 0.6449 0.0207  0.0189  -0.0570 52  VAL   A CA  
418  C  C   . VAL   A 73  ? 0.5473 0.4460 0.6522 0.0013  0.0277  -0.0311 52  VAL   A C   
419  O  O   . VAL   A 73  ? 0.5816 0.4390 0.6861 -0.0167 0.0277  -0.0166 52  VAL   A O   
420  C  CB  . VAL   A 73  ? 0.6338 0.5020 0.7176 0.0472  0.0163  -0.0512 52  VAL   A CB  
421  C  CG1 . VAL   A 73  ? 0.5159 0.4167 0.5889 0.0631  0.0185  -0.0376 52  VAL   A CG1 
422  C  CG2 . VAL   A 73  ? 0.6144 0.4869 0.7031 0.0651  0.0094  -0.0718 52  VAL   A CG2 
423  N  N   . VAL   A 74  ? 0.5830 0.5338 0.6905 0.0053  0.0345  -0.0243 53  VAL   A N   
424  C  CA  . VAL   A 74  ? 0.5639 0.5421 0.6777 -0.0094 0.0465  0.0036  53  VAL   A CA  
425  C  C   . VAL   A 74  ? 0.5977 0.5975 0.6864 0.0174  0.0541  0.0214  53  VAL   A C   
426  O  O   . VAL   A 74  ? 0.5809 0.6103 0.6561 0.0416  0.0502  0.0058  53  VAL   A O   
427  C  CB  . VAL   A 74  ? 0.5498 0.5794 0.6847 -0.0213 0.0497  -0.0036 53  VAL   A CB  
428  C  CG1 . VAL   A 74  ? 0.5936 0.6656 0.7399 -0.0345 0.0645  0.0300  53  VAL   A CG1 
429  C  CG2 . VAL   A 74  ? 0.5117 0.5214 0.6668 -0.0441 0.0396  -0.0235 53  VAL   A CG2 
430  N  N   . ARG   A 75  ? 0.6814 0.6630 0.7612 0.0133  0.0628  0.0541  54  ARG   A N   
431  C  CA  . ARG   A 75  ? 0.6944 0.6892 0.7434 0.0426  0.0692  0.0734  54  ARG   A CA  
432  C  C   . ARG   A 75  ? 0.7945 0.8276 0.8452 0.0345  0.0888  0.1142  54  ARG   A C   
433  O  O   . ARG   A 75  ? 0.9398 0.9470 0.9878 0.0241  0.0969  0.1492  54  ARG   A O   
434  C  CB  . ARG   A 75  ? 0.7218 0.6588 0.7524 0.0543  0.0625  0.0793  54  ARG   A CB  
435  N  N   . ASP   A 76  ? 0.7679 0.8644 0.8217 0.0422  0.0970  0.1122  55  ASP   A N   
436  C  CA  . ASP   A 76  ? 0.7585 0.9114 0.8177 0.0387  0.1188  0.1523  55  ASP   A CA  
437  C  C   . ASP   A 76  ? 0.7502 0.9106 0.8583 -0.0089 0.1235  0.1706  55  ASP   A C   
438  O  O   . ASP   A 76  ? 0.8320 1.0017 0.9571 -0.0318 0.1369  0.2153  55  ASP   A O   
439  C  CB  . ASP   A 76  ? 0.8364 0.9815 0.8682 0.0540  0.1309  0.1921  55  ASP   A CB  
440  N  N   . GLY   A 77  ? 0.7416 0.8996 0.8734 -0.0251 0.1110  0.1379  56  GLY   A N   
441  C  CA  . GLY   A 77  ? 0.7316 0.9022 0.9091 -0.0687 0.1099  0.1482  56  GLY   A CA  
442  C  C   . GLY   A 77  ? 0.8071 0.8985 0.9992 -0.1041 0.0935  0.1437  56  GLY   A C   
443  O  O   . GLY   A 77  ? 0.7710 0.8627 0.9977 -0.1400 0.0842  0.1397  56  GLY   A O   
444  N  N   . GLU   A 78  ? 0.8646 0.8876 1.0285 -0.0921 0.0878  0.1429  57  GLU   A N   
445  C  CA  . GLU   A 78  ? 0.8471 0.7842 1.0138 -0.1167 0.0713  0.1369  57  GLU   A CA  
446  C  C   . GLU   A 78  ? 0.6871 0.5855 0.8364 -0.0967 0.0551  0.0882  57  GLU   A C   
447  O  O   . GLU   A 78  ? 0.6984 0.5937 0.8202 -0.0603 0.0556  0.0742  57  GLU   A O   
448  C  CB  . GLU   A 78  ? 0.7720 0.6564 0.9164 -0.1118 0.0762  0.1702  57  GLU   A CB  
449  N  N   . ALA   A 79  ? 0.6805 0.5542 0.8468 -0.1202 0.0401  0.0645  58  ALA   A N   
450  C  CA  . ALA   A 79  ? 0.6680 0.5183 0.8212 -0.1019 0.0275  0.0218  58  ALA   A CA  
451  C  C   . ALA   A 79  ? 0.7451 0.5059 0.8757 -0.0984 0.0139  0.0110  58  ALA   A C   
452  O  O   . ALA   A 79  ? 0.8649 0.5711 0.9982 -0.1255 0.0057  0.0265  58  ALA   A O   
453  C  CB  . ALA   A 79  ? 0.6350 0.5177 0.8129 -0.1214 0.0196  0.0003  58  ALA   A CB  
454  N  N   . GLU   A 80  ? 0.7617 0.5075 0.8702 -0.0644 0.0106  -0.0146 59  GLU   A N   
455  C  CA  . GLU   A 80  ? 0.7486 0.4171 0.8303 -0.0491 -0.0006 -0.0283 59  GLU   A CA  
456  C  C   . GLU   A 80  ? 0.7386 0.4140 0.8154 -0.0311 -0.0076 -0.0652 59  GLU   A C   
457  O  O   . GLU   A 80  ? 0.7327 0.4620 0.8153 -0.0105 -0.0009 -0.0746 59  GLU   A O   
458  C  CB  . GLU   A 80  ? 0.7372 0.3866 0.7943 -0.0165 0.0059  -0.0128 59  GLU   A CB  
459  C  CG  . GLU   A 80  ? 1.0390 0.6081 1.0651 0.0056  -0.0045 -0.0240 59  GLU   A CG  
460  C  CD  . GLU   A 80  ? 1.1893 0.7411 1.1920 0.0379  0.0013  -0.0039 59  GLU   A CD  
461  O  OE1 . GLU   A 80  ? 1.0476 0.6614 1.0551 0.0584  0.0096  0.0004  59  GLU   A OE1 
462  O  OE2 . GLU   A 80  ? 1.4011 0.8738 1.3787 0.0433  -0.0047 0.0073  59  GLU   A OE2 
463  N  N   . GLU   A 81  ? 0.7736 0.3926 0.8378 -0.0385 -0.0224 -0.0849 60  GLU   A N   
464  C  CA  . GLU   A 81  ? 0.7176 0.3426 0.7714 -0.0176 -0.0277 -0.1176 60  GLU   A CA  
465  C  C   . GLU   A 81  ? 0.7204 0.3325 0.7501 0.0275  -0.0228 -0.1234 60  GLU   A C   
466  O  O   . GLU   A 81  ? 0.8472 0.3971 0.8509 0.0431  -0.0266 -0.1169 60  GLU   A O   
467  C  CB  . GLU   A 81  ? 0.7136 0.2806 0.7514 -0.0345 -0.0466 -0.1375 60  GLU   A CB  
468  C  CG  . GLU   A 81  ? 0.8326 0.4389 0.8597 -0.0242 -0.0471 -0.1607 60  GLU   A CG  
469  C  CD  . GLU   A 81  ? 1.0504 0.6199 1.0562 -0.0439 -0.0617 -0.1734 60  GLU   A CD  
470  O  OE1 . GLU   A 81  ? 1.0732 0.5773 1.0527 -0.0402 -0.0676 -0.1760 60  GLU   A OE1 
471  O  OE2 . GLU   A 81  ? 1.0662 0.6743 1.0850 -0.0619 -0.0678 -0.1814 60  GLU   A OE2 
472  N  N   . VAL   A 82  ? 0.6443 0.3169 0.6847 0.0485  -0.0149 -0.1333 61  VAL   A N   
473  C  CA  . VAL   A 82  ? 0.6620 0.3470 0.6922 0.0886  -0.0091 -0.1336 61  VAL   A CA  
474  C  C   . VAL   A 82  ? 0.7079 0.3995 0.7190 0.1085  -0.0072 -0.1492 61  VAL   A C   
475  O  O   . VAL   A 82  ? 0.6314 0.3495 0.6478 0.0955  -0.0081 -0.1597 61  VAL   A O   
476  C  CB  . VAL   A 82  ? 0.6326 0.3934 0.6909 0.0920  -0.0006 -0.1223 61  VAL   A CB  
477  C  CG1 . VAL   A 82  ? 0.7359 0.5158 0.7911 0.1290  0.0024  -0.1185 61  VAL   A CG1 
478  C  CG2 . VAL   A 82  ? 0.6927 0.4615 0.7591 0.0715  0.0019  -0.1015 61  VAL   A CG2 
479  N  N   . ALA   A 83  ? 0.7618 0.4389 0.7525 0.1401  -0.0026 -0.1461 62  ALA   A N   
480  C  CA  . ALA   A 83  ? 0.7032 0.3983 0.6802 0.1617  0.0022  -0.1556 62  ALA   A CA  
481  C  C   . ALA   A 83  ? 0.7323 0.5080 0.7373 0.1697  0.0115  -0.1511 62  ALA   A C   
482  O  O   . ALA   A 83  ? 0.6840 0.5007 0.7190 0.1621  0.0128  -0.1419 62  ALA   A O   
483  C  CB  . ALA   A 83  ? 0.7379 0.4063 0.6926 0.1948  0.0032  -0.1521 62  ALA   A CB  
484  N  N   . THR   A 84  ? 0.7813 0.5792 0.7772 0.1854  0.0164  -0.1573 63  THR   A N   
485  C  CA  . THR   A 84  ? 0.6415 0.5128 0.6654 0.1908  0.0254  -0.1494 63  THR   A CA  
486  C  C   . THR   A 84  ? 0.6759 0.5943 0.7256 0.2099  0.0317  -0.1317 63  THR   A C   
487  O  O   . THR   A 84  ? 0.6518 0.6214 0.7380 0.1997  0.0328  -0.1212 63  THR   A O   
488  C  CB  . THR   A 84  ? 0.6569 0.5395 0.6617 0.2061  0.0295  -0.1575 63  THR   A CB  
489  O  OG1 . THR   A 84  ? 0.7070 0.5610 0.6811 0.2356  0.0290  -0.1616 63  THR   A OG1 
490  C  CG2 . THR   A 84  ? 0.6443 0.4951 0.6305 0.1845  0.0205  -0.1742 63  THR   A CG2 
491  N  N   . ASN   A 85  ? 0.8392 0.7427 0.8713 0.2373  0.0331  -0.1285 64  ASN   A N   
492  C  CA  . ASN   A 85  ? 0.8463 0.8012 0.9019 0.2580  0.0373  -0.1108 64  ASN   A CA  
493  C  C   . ASN   A 85  ? 0.8329 0.7435 0.8703 0.2704  0.0311  -0.1077 64  ASN   A C   
494  O  O   . ASN   A 85  ? 0.9716 0.8628 0.9829 0.2983  0.0316  -0.1072 64  ASN   A O   
495  C  CB  . ASN   A 85  ? 0.7639 0.7594 0.8147 0.2852  0.0460  -0.1058 64  ASN   A CB  
496  C  CG  . ASN   A 85  ? 0.8603 0.9353 0.9534 0.2937  0.0510  -0.0835 64  ASN   A CG  
497  O  OD1 . ASN   A 85  ? 0.8211 0.9505 0.9548 0.2753  0.0536  -0.0732 64  ASN   A OD1 
498  N  ND2 . ASN   A 85  ? 0.9322 1.0139 1.0170 0.3203  0.0507  -0.0749 64  ASN   A ND2 
499  N  N   . GLY   A 86  ? 0.9901 0.8845 1.0378 0.2522  0.0249  -0.1044 65  GLY   A N   
500  C  CA  . GLY   A 86  ? 0.9954 0.8520 1.0277 0.2634  0.0193  -0.0966 65  GLY   A CA  
501  C  C   . GLY   A 86  ? 0.9710 0.8860 1.0352 0.2684  0.0163  -0.0807 65  GLY   A C   
502  O  O   . GLY   A 86  ? 0.9519 0.9201 1.0508 0.2520  0.0146  -0.0790 65  GLY   A O   
503  N  N   . LYS   A 87  ? 0.7797 0.6843 0.8310 0.2911  0.0132  -0.0692 66  LYS   A N   
504  C  CA  . LYS   A 87  ? 0.6583 0.6162 0.7349 0.2979  0.0065  -0.0543 66  LYS   A CA  
505  C  C   . LYS   A 87  ? 0.6518 0.5737 0.7146 0.2909  -0.0011 -0.0491 66  LYS   A C   
506  O  O   . LYS   A 87  ? 0.6689 0.6223 0.7393 0.3024  -0.0089 -0.0366 66  LYS   A O   
507  C  CB  . LYS   A 87  ? 0.5990 0.5805 0.6701 0.3305  0.0074  -0.0425 66  LYS   A CB  
508  C  CG  . LYS   A 87  ? 0.5843 0.6213 0.6740 0.3413  0.0153  -0.0416 66  LYS   A CG  
509  C  CD  . LYS   A 87  ? 0.6179 0.6693 0.6926 0.3778  0.0171  -0.0311 66  LYS   A CD  
510  C  CE  . LYS   A 87  ? 0.6291 0.7559 0.7303 0.3890  0.0250  -0.0236 66  LYS   A CE  
511  N  NZ  . LYS   A 87  ? 0.6501 0.8600 0.8115 0.3668  0.0187  -0.0109 66  LYS   A NZ  
512  N  N   . GLN   A 88  ? 0.6512 0.5104 0.6928 0.2728  0.0003  -0.0569 67  GLN   A N   
513  C  CA  . GLN   A 88  ? 0.6497 0.4721 0.6737 0.2683  -0.0041 -0.0465 67  GLN   A CA  
514  C  C   . GLN   A 88  ? 0.6207 0.5065 0.6733 0.2455  -0.0105 -0.0445 67  GLN   A C   
515  O  O   . GLN   A 88  ? 0.5616 0.4876 0.6425 0.2250  -0.0117 -0.0566 67  GLN   A O   
516  C  CB  . GLN   A 88  ? 0.7411 0.4909 0.7435 0.2401  -0.0006 -0.0500 67  GLN   A CB  
517  C  CG  . GLN   A 88  ? 0.8156 0.5438 0.8066 0.2205  0.0000  -0.0301 67  GLN   A CG  
518  C  CD  . GLN   A 88  ? 0.9780 0.6340 0.9523 0.1926  0.0023  -0.0266 67  GLN   A CD  
519  O  OE1 . GLN   A 88  ? 1.0687 0.6960 1.0429 0.1807  0.0003  -0.0451 67  GLN   A OE1 
520  N  NE2 . GLN   A 88  ? 1.0362 0.6652 0.9971 0.1815  0.0053  -0.0011 67  GLN   A NE2 
521  N  N   . ARG   A 89  ? 0.6109 0.5010 0.6512 0.2521  -0.0158 -0.0293 68  ARG   A N   
522  C  CA  . ARG   A 89  ? 0.5575 0.4960 0.6118 0.2368  -0.0252 -0.0297 68  ARG   A CA  
523  C  C   . ARG   A 89  ? 0.6118 0.5181 0.6403 0.2207  -0.0194 -0.0186 68  ARG   A C   
524  O  O   . ARG   A 89  ? 0.6351 0.4909 0.6356 0.2282  -0.0117 -0.0011 68  ARG   A O   
525  C  CB  . ARG   A 89  ? 0.5193 0.5062 0.5802 0.2629  -0.0399 -0.0222 68  ARG   A CB  
526  C  CG  . ARG   A 89  ? 0.5672 0.6160 0.6703 0.2679  -0.0490 -0.0305 68  ARG   A CG  
527  C  CD  . ARG   A 89  ? 0.5083 0.6069 0.6212 0.2951  -0.0653 -0.0203 68  ARG   A CD  
528  N  NE  . ARG   A 89  ? 0.5954 0.6685 0.6845 0.3236  -0.0555 -0.0057 68  ARG   A NE  
529  C  CZ  . ARG   A 89  ? 0.5915 0.7023 0.6846 0.3429  -0.0645 0.0057  68  ARG   A CZ  
530  N  NH1 . ARG   A 89  ? 0.5840 0.7599 0.7060 0.3360  -0.0854 0.0046  68  ARG   A NH1 
531  N  NH2 . ARG   A 89  ? 0.5876 0.6674 0.6543 0.3686  -0.0547 0.0171  68  ARG   A NH2 
532  N  N   . TRP   A 90  ? 0.5561 0.4924 0.5941 0.1996  -0.0228 -0.0267 69  TRP   A N   
533  C  CA  . TRP   A 90  ? 0.5752 0.5016 0.5914 0.1890  -0.0161 -0.0146 69  TRP   A CA  
534  C  C   . TRP   A 90  ? 0.6145 0.5857 0.6229 0.2000  -0.0301 -0.0186 69  TRP   A C   
535  O  O   . TRP   A 90  ? 0.5723 0.5789 0.6018 0.1991  -0.0463 -0.0370 69  TRP   A O   
536  C  CB  . TRP   A 90  ? 0.5668 0.4853 0.5948 0.1574  -0.0062 -0.0219 69  TRP   A CB  
537  C  CG  . TRP   A 90  ? 0.6914 0.5628 0.7237 0.1436  0.0025  -0.0221 69  TRP   A CG  
538  C  CD1 . TRP   A 90  ? 0.7057 0.5299 0.7245 0.1301  0.0119  -0.0043 69  TRP   A CD1 
539  C  CD2 . TRP   A 90  ? 0.6757 0.5408 0.7250 0.1423  0.0002  -0.0410 69  TRP   A CD2 
540  N  NE1 . TRP   A 90  ? 0.7311 0.5130 0.7547 0.1200  0.0116  -0.0156 69  TRP   A NE1 
541  C  CE2 . TRP   A 90  ? 0.7320 0.5400 0.7711 0.1306  0.0059  -0.0387 69  TRP   A CE2 
542  C  CE3 . TRP   A 90  ? 0.5726 0.4761 0.6448 0.1497  -0.0067 -0.0577 69  TRP   A CE3 
543  C  CZ2 . TRP   A 90  ? 0.7233 0.5100 0.7662 0.1319  0.0045  -0.0568 69  TRP   A CZ2 
544  C  CZ3 . TRP   A 90  ? 0.6344 0.5246 0.7146 0.1507  -0.0037 -0.0701 69  TRP   A CZ3 
545  C  CH2 . TRP   A 90  ? 0.6947 0.5263 0.7565 0.1446  0.0016  -0.0717 69  TRP   A CH2 
546  N  N   . LEU   A 91  ? 0.6676 0.6353 0.6437 0.2105  -0.0249 -0.0004 70  LEU   A N   
547  C  CA  . LEU   A 91  ? 0.6080 0.6128 0.5651 0.2250  -0.0391 -0.0071 70  LEU   A CA  
548  C  C   . LEU   A 91  ? 0.5940 0.6170 0.5616 0.2062  -0.0417 -0.0277 70  LEU   A C   
549  O  O   . LEU   A 91  ? 0.6376 0.6502 0.6103 0.1870  -0.0242 -0.0226 70  LEU   A O   
550  C  CB  . LEU   A 91  ? 0.6644 0.6641 0.5793 0.2443  -0.0286 0.0204  70  LEU   A CB  
551  C  CG  . LEU   A 91  ? 0.7786 0.7720 0.6713 0.2752  -0.0348 0.0383  70  LEU   A CG  
552  C  CD1 . LEU   A 91  ? 0.8704 0.8340 0.7855 0.2750  -0.0333 0.0406  70  LEU   A CD1 
553  C  CD2 . LEU   A 91  ? 0.9789 0.9579 0.8319 0.2887  -0.0168 0.0742  70  LEU   A CD2 
554  N  N   . LEU   A 92  ? 0.6465 0.6954 0.6186 0.2113  -0.0659 -0.0506 71  LEU   A N   
555  C  CA  . LEU   A 92  ? 0.5658 0.6241 0.5402 0.1994  -0.0720 -0.0711 71  LEU   A CA  
556  C  C   . LEU   A 92  ? 0.5810 0.6459 0.5127 0.2151  -0.0622 -0.0634 71  LEU   A C   
557  O  O   . LEU   A 92  ? 0.5821 0.6570 0.4764 0.2424  -0.0702 -0.0576 71  LEU   A O   
558  C  CB  . LEU   A 92  ? 0.4748 0.5493 0.4610 0.2006  -0.1050 -0.0958 71  LEU   A CB  
559  C  CG  . LEU   A 92  ? 0.4528 0.5336 0.4901 0.1786  -0.1128 -0.1042 71  LEU   A CG  
560  C  CD1 . LEU   A 92  ? 0.4991 0.6021 0.5517 0.1804  -0.1481 -0.1181 71  LEU   A CD1 
561  C  CD2 . LEU   A 92  ? 0.5305 0.6016 0.5848 0.1559  -0.1037 -0.1148 71  LEU   A CD2 
562  N  N   . SER   A 93  ? 0.6061 0.6717 0.5427 0.2007  -0.0445 -0.0620 72  SER   A N   
563  C  CA  . SER   A 93  ? 0.6084 0.6922 0.5095 0.2172  -0.0311 -0.0516 72  SER   A CA  
564  C  C   . SER   A 93  ? 0.6136 0.7064 0.5269 0.2045  -0.0255 -0.0656 72  SER   A C   
565  O  O   . SER   A 93  ? 0.6188 0.7014 0.5707 0.1765  -0.0198 -0.0692 72  SER   A O   
566  C  CB  . SER   A 93  ? 0.6456 0.7298 0.5404 0.2152  -0.0029 -0.0126 72  SER   A CB  
567  O  OG  . SER   A 93  ? 0.7058 0.8195 0.5821 0.2228  0.0162  0.0023  72  SER   A OG  
568  N  N   . PRO   A 94  ? 0.6565 0.7684 0.5339 0.2289  -0.0274 -0.0741 73  PRO   A N   
569  C  CA  . PRO   A 94  ? 0.6664 0.7899 0.5534 0.2219  -0.0193 -0.0838 73  PRO   A CA  
570  C  C   . PRO   A 94  ? 0.6281 0.7698 0.5461 0.1974  0.0109  -0.0560 73  PRO   A C   
571  O  O   . PRO   A 94  ? 0.6237 0.7710 0.5673 0.1803  0.0153  -0.0641 73  PRO   A O   
572  C  CB  . PRO   A 94  ? 0.6032 0.7462 0.4345 0.2634  -0.0235 -0.0927 73  PRO   A CB  
573  C  CG  . PRO   A 94  ? 0.6396 0.7910 0.4343 0.2886  -0.0230 -0.0759 73  PRO   A CG  
574  C  CD  . PRO   A 94  ? 0.6531 0.7771 0.4749 0.2689  -0.0380 -0.0769 73  PRO   A CD  
575  N  N   . SER   A 95  ? 0.6040 0.7530 0.5213 0.1937  0.0295  -0.0225 74  SER   A N   
576  C  CA  . SER   A 95  ? 0.6313 0.7941 0.5803 0.1655  0.0539  0.0068  74  SER   A CA  
577  C  C   . SER   A 95  ? 0.6247 0.7469 0.6115 0.1308  0.0511  0.0076  74  SER   A C   
578  O  O   . SER   A 95  ? 0.5861 0.7077 0.5988 0.1033  0.0655  0.0297  74  SER   A O   
579  C  CB  . SER   A 95  ? 0.6225 0.8126 0.5515 0.1774  0.0758  0.0483  74  SER   A CB  
580  O  OG  . SER   A 95  ? 0.6205 0.7785 0.5360 0.1821  0.0716  0.0618  74  SER   A OG  
581  N  N   . THR   A 96  ? 0.6550 0.7449 0.6448 0.1324  0.0317  -0.0154 75  THR   A N   
582  C  CA  . THR   A 96  ? 0.5948 0.6492 0.6147 0.1080  0.0284  -0.0202 75  THR   A CA  
583  C  C   . THR   A 96  ? 0.5391 0.5947 0.5802 0.0987  0.0166  -0.0500 75  THR   A C   
584  O  O   . THR   A 96  ? 0.5155 0.5744 0.5494 0.1128  -0.0003 -0.0703 75  THR   A O   
585  C  CB  . THR   A 96  ? 0.6231 0.6490 0.6327 0.1209  0.0190  -0.0174 75  THR   A CB  
586  O  OG1 . THR   A 96  ? 0.6639 0.6847 0.6513 0.1304  0.0310  0.0143  75  THR   A OG1 
587  C  CG2 . THR   A 96  ? 0.5305 0.5212 0.5652 0.1036  0.0165  -0.0243 75  THR   A CG2 
588  N  N   . THR   A 97  ? 0.5593 0.5422 0.6534 0.0766  -0.1016 -0.0114 76  THR   A N   
589  C  CA  . THR   A 97  ? 0.5677 0.5559 0.6626 0.0720  -0.0893 -0.0280 76  THR   A CA  
590  C  C   . THR   A 97  ? 0.4761 0.4576 0.5920 0.0743  -0.0922 -0.0386 76  THR   A C   
591  O  O   . THR   A 97  ? 0.4662 0.4364 0.5971 0.0800  -0.1051 -0.0351 76  THR   A O   
592  C  CB  . THR   A 97  ? 0.5187 0.5055 0.5969 0.0641  -0.0763 -0.0203 76  THR   A CB  
593  O  OG1 . THR   A 97  ? 0.5391 0.5121 0.6222 0.0613  -0.0775 -0.0062 76  THR   A OG1 
594  C  CG2 . THR   A 97  ? 0.5403 0.5368 0.5972 0.0648  -0.0749 -0.0118 76  THR   A CG2 
595  N  N   . LEU   A 98  ? 0.4298 0.4195 0.5475 0.0707  -0.0813 -0.0517 77  LEU   A N   
596  C  CA  . LEU   A 98  ? 0.4426 0.4312 0.5763 0.0736  -0.0820 -0.0629 77  LEU   A CA  
597  C  C   . LEU   A 98  ? 0.4478 0.4293 0.5745 0.0662  -0.0717 -0.0579 77  LEU   A C   
598  O  O   . LEU   A 98  ? 0.4205 0.4048 0.5315 0.0586  -0.0604 -0.0521 77  LEU   A O   
599  C  CB  . LEU   A 98  ? 0.3798 0.3913 0.5233 0.0768  -0.0779 -0.0817 77  LEU   A CB  
600  C  CG  . LEU   A 98  ? 0.3614 0.3861 0.5109 0.0821  -0.0850 -0.0879 77  LEU   A CG  
601  C  CD1 . LEU   A 98  ? 0.3707 0.4229 0.5324 0.0835  -0.0792 -0.1039 77  LEU   A CD1 
602  C  CD2 . LEU   A 98  ? 0.4417 0.4553 0.6031 0.0925  -0.1021 -0.0866 77  LEU   A CD2 
603  N  N   . ARG   A 99  ? 0.4288 0.4004 0.5686 0.0695  -0.0775 -0.0611 78  ARG   A N   
604  C  CA  . ARG   A 99  ? 0.4121 0.3810 0.5496 0.0646  -0.0689 -0.0621 78  ARG   A CA  
605  C  C   . ARG   A 99  ? 0.4407 0.4257 0.5905 0.0715  -0.0682 -0.0829 78  ARG   A C   
606  O  O   . ARG   A 99  ? 0.4974 0.4820 0.6642 0.0821  -0.0810 -0.0944 78  ARG   A O   
607  C  CB  . ARG   A 99  ? 0.5442 0.4910 0.6881 0.0627  -0.0773 -0.0489 78  ARG   A CB  
608  C  CG  . ARG   A 99  ? 0.5762 0.5203 0.7160 0.0565  -0.0682 -0.0477 78  ARG   A CG  
609  C  CD  . ARG   A 99  ? 0.6785 0.6040 0.8206 0.0504  -0.0731 -0.0276 78  ARG   A CD  
610  N  NE  . ARG   A 99  ? 0.7164 0.6245 0.8826 0.0555  -0.0919 -0.0275 78  ARG   A NE  
611  C  CZ  . ARG   A 99  ? 0.7830 0.6772 0.9587 0.0545  -0.1047 -0.0092 78  ARG   A CZ  
612  N  NH1 . ARG   A 99  ? 0.8051 0.7045 0.9654 0.0497  -0.0997 0.0102  78  ARG   A NH1 
613  N  NH2 . ARG   A 99  ? 0.7608 0.6366 0.9631 0.0590  -0.1241 -0.0103 78  ARG   A NH2 
614  N  N   . VAL   A 100 ? 0.4009 0.4024 0.5429 0.0665  -0.0540 -0.0877 79  VAL   A N   
615  C  CA  . VAL   A 100 ? 0.4208 0.4474 0.5716 0.0726  -0.0503 -0.1050 79  VAL   A CA  
616  C  C   . VAL   A 100 ? 0.4102 0.4371 0.5582 0.0705  -0.0442 -0.1070 79  VAL   A C   
617  O  O   . VAL   A 100 ? 0.4284 0.4509 0.5633 0.0603  -0.0334 -0.0959 79  VAL   A O   
618  C  CB  . VAL   A 100 ? 0.4106 0.4626 0.5579 0.0679  -0.0396 -0.1065 79  VAL   A CB  
619  C  CG1 . VAL   A 100 ? 0.3579 0.4420 0.5134 0.0726  -0.0333 -0.1197 79  VAL   A CG1 
620  C  CG2 . VAL   A 100 ? 0.3330 0.3876 0.4857 0.0715  -0.0474 -0.1077 79  VAL   A CG2 
621  N  N   . THR   A 101 ? 0.4330 0.4661 0.5937 0.0815  -0.0522 -0.1226 80  THR   A N   
622  C  CA  A THR   A 101 ? 0.4558 0.4904 0.6150 0.0817  -0.0490 -0.1271 80  THR   A CA  
623  C  CA  B THR   A 101 ? 0.4562 0.4907 0.6157 0.0818  -0.0492 -0.1272 80  THR   A CA  
624  C  C   . THR   A 101 ? 0.4085 0.4764 0.5756 0.0941  -0.0486 -0.1484 80  THR   A C   
625  O  O   . THR   A 101 ? 0.4201 0.5014 0.5997 0.1062  -0.0573 -0.1629 80  THR   A O   
626  C  CB  A THR   A 101 ? 0.4194 0.4230 0.5877 0.0833  -0.0632 -0.1243 80  THR   A CB  
627  C  CB  B THR   A 101 ? 0.4381 0.4415 0.6070 0.0838  -0.0637 -0.1248 80  THR   A CB  
628  O  OG1 A THR   A 101 ? 0.4627 0.4693 0.6303 0.0839  -0.0608 -0.1305 80  THR   A OG1 
629  O  OG1 B THR   A 101 ? 0.5071 0.5072 0.6958 0.0979  -0.0818 -0.1406 80  THR   A OG1 
630  C  CG2 A THR   A 101 ? 0.5078 0.5041 0.6968 0.0971  -0.0829 -0.1382 80  THR   A CG2 
631  C  CG2 B THR   A 101 ? 0.4609 0.4383 0.6229 0.0728  -0.0643 -0.1018 80  THR   A CG2 
632  N  N   . MET   A 102 ? 0.4207 0.5049 0.5802 0.0918  -0.0384 -0.1499 81  MET   A N   
633  C  CA  . MET   A 102 ? 0.4158 0.5369 0.5798 0.1041  -0.0368 -0.1688 81  MET   A CA  
634  C  C   . MET   A 102 ? 0.4212 0.5358 0.5824 0.1061  -0.0389 -0.1738 81  MET   A C   
635  O  O   . MET   A 102 ? 0.4758 0.5661 0.6285 0.0940  -0.0348 -0.1583 81  MET   A O   
636  C  CB  . MET   A 102 ? 0.4078 0.5684 0.5645 0.0985  -0.0195 -0.1628 81  MET   A CB  
637  C  CG  . MET   A 102 ? 0.4209 0.5884 0.5819 0.0944  -0.0174 -0.1567 81  MET   A CG  
638  S  SD  . MET   A 102 ? 0.3559 0.5714 0.5158 0.0864  0.0004  -0.1476 81  MET   A SD  
639  C  CE  . MET   A 102 ? 0.2933 0.5619 0.4610 0.1056  0.0003  -0.1696 81  MET   A CE  
640  N  N   . SER   A 103 ? 0.4611 0.5993 0.6296 0.1221  -0.0461 -0.1963 82  SER   A N   
641  C  CA  . SER   A 103 ? 0.5170 0.6514 0.6816 0.1235  -0.0502 -0.2016 82  SER   A CA  
642  C  C   . SER   A 103 ? 0.5135 0.6930 0.6662 0.1279  -0.0415 -0.2083 82  SER   A C   
643  O  O   . SER   A 103 ? 0.5813 0.7622 0.7288 0.1289  -0.0430 -0.2117 82  SER   A O   
644  C  CB  . SER   A 103 ? 0.4744 0.5830 0.6531 0.1307  -0.0741 -0.2137 82  SER   A CB  
645  O  OG  . SER   A 103 ? 0.5643 0.6951 0.7483 0.1422  -0.0844 -0.2302 82  SER   A OG  
646  N  N   . GLN   A 104 ? 0.4659 0.6829 0.6146 0.1302  -0.0333 -0.2088 83  GLN   A N   
647  C  CA  . GLN   A 104 ? 0.4184 0.6812 0.5552 0.1331  -0.0244 -0.2102 83  GLN   A CA  
648  C  C   . GLN   A 104 ? 0.4041 0.6926 0.5352 0.1217  -0.0042 -0.1905 83  GLN   A C   
649  O  O   . GLN   A 104 ? 0.3779 0.6617 0.5169 0.1169  -0.0005 -0.1837 83  GLN   A O   
650  C  CB  . GLN   A 104 ? 0.4079 0.6979 0.5472 0.1474  -0.0364 -0.2294 83  GLN   A CB  
651  N  N   . ALA   A 105 ? 0.3864 0.7019 0.5057 0.1169  0.0075  -0.1802 84  ALA   A N   
652  C  CA  . ALA   A 105 ? 0.4034 0.7440 0.5202 0.1043  0.0247  -0.1583 84  ALA   A CA  
653  C  C   . ALA   A 105 ? 0.3678 0.7461 0.4880 0.1083  0.0260  -0.1594 84  ALA   A C   
654  O  O   . ALA   A 105 ? 0.3796 0.7773 0.4976 0.1219  0.0164  -0.1765 84  ALA   A O   
655  C  CB  . ALA   A 105 ? 0.3541 0.7119 0.4582 0.0979  0.0346  -0.1447 84  ALA   A CB  
656  N  N   . SER   A 106 ? 0.3128 0.7023 0.4401 0.0962  0.0368  -0.1415 85  SER   A N   
657  C  CA  . SER   A 106 ? 0.4080 0.8349 0.5406 0.0979  0.0394  -0.1392 85  SER   A CA  
658  C  C   . SER   A 106 ? 0.4420 0.9122 0.5636 0.0987  0.0458  -0.1307 85  SER   A C   
659  O  O   . SER   A 106 ? 0.4466 0.9180 0.5590 0.0924  0.0519  -0.1185 85  SER   A O   
660  C  CB  . SER   A 106 ? 0.3106 0.7375 0.4572 0.0830  0.0477  -0.1209 85  SER   A CB  
661  O  OG  . SER   A 106 ? 0.3624 0.7510 0.5180 0.0819  0.0418  -0.1273 85  SER   A OG  
662  N  N   . THR   A 107 ? 0.4651 0.9726 0.5879 0.1072  0.0438  -0.1372 86  THR   A N   
663  C  CA  . THR   A 107 ? 0.4635 1.0192 0.5778 0.1076  0.0503  -0.1263 86  THR   A CA  
664  C  C   . THR   A 107 ? 0.4494 1.0339 0.5760 0.0972  0.0594  -0.1070 86  THR   A C   
665  O  O   . THR   A 107 ? 0.4763 1.0400 0.6177 0.0867  0.0618  -0.0990 86  THR   A O   
666  C  CB  . THR   A 107 ? 0.4934 1.0768 0.5978 0.1281  0.0391  -0.1511 86  THR   A CB  
667  O  OG1 . THR   A 107 ? 0.4545 1.0456 0.5677 0.1380  0.0316  -0.1676 86  THR   A OG1 
668  C  CG2 . THR   A 107 ? 0.4377 0.9898 0.5348 0.1375  0.0274  -0.1709 86  THR   A CG2 
669  N  N   . GLU   A 108 ? 0.5519 1.1862 0.6737 0.1001  0.0634  -0.0990 87  GLU   A N   
670  C  CA  . GLU   A 108 ? 0.6266 1.2912 0.7624 0.0907  0.0708  -0.0807 87  GLU   A CA  
671  C  C   . GLU   A 108 ? 0.6130 1.2862 0.7579 0.1016  0.0642  -0.0998 87  GLU   A C   
672  O  O   . GLU   A 108 ? 0.6544 1.3359 0.8164 0.0921  0.0686  -0.0875 87  GLU   A O   
673  C  CB  . GLU   A 108 ? 0.6684 1.3861 0.7967 0.0901  0.0770  -0.0637 87  GLU   A CB  
674  C  CG  . GLU   A 108 ? 0.6838 1.3945 0.8084 0.0752  0.0842  -0.0373 87  GLU   A CG  
675  C  CD  . GLU   A 108 ? 0.7127 1.3968 0.8569 0.0529  0.0906  -0.0123 87  GLU   A CD  
676  O  OE1 . GLU   A 108 ? 0.7361 1.4430 0.8967 0.0443  0.0943  0.0028  87  GLU   A OE1 
677  O  OE2 . GLU   A 108 ? 0.6341 1.2753 0.7785 0.0442  0.0909  -0.0085 87  GLU   A OE2 
678  N  N   . ALA   A 109 ? 0.7113 1.3820 0.8470 0.1212  0.0524  -0.1297 88  ALA   A N   
679  C  CA  . ALA   A 109 ? 0.6919 1.3669 0.8356 0.1334  0.0436  -0.1504 88  ALA   A CA  
680  C  C   . ALA   A 109 ? 0.6523 1.2738 0.8064 0.1323  0.0359  -0.1614 88  ALA   A C   
681  O  O   . ALA   A 109 ? 0.5971 1.2136 0.7574 0.1439  0.0255  -0.1811 88  ALA   A O   
682  C  CB  . ALA   A 109 ? 0.5791 1.2793 0.7100 0.1557  0.0316  -0.1781 88  ALA   A CB  
683  N  N   . SER   A 110 ? 0.5894 1.1723 0.7456 0.1192  0.0399  -0.1489 89  SER   A N   
684  C  CA  . SER   A 110 ? 0.6183 1.1527 0.7832 0.1184  0.0322  -0.1579 89  SER   A CA  
685  C  C   . SER   A 110 ? 0.5840 1.1182 0.7677 0.1078  0.0360  -0.1461 89  SER   A C   
686  O  O   . SER   A 110 ? 0.5935 1.1493 0.7855 0.0931  0.0469  -0.1231 89  SER   A O   
687  C  CB  . SER   A 110 ? 0.4538 0.9505 0.6129 0.1098  0.0345  -0.1504 89  SER   A CB  
688  O  OG  . SER   A 110 ? 0.4606 0.9475 0.6061 0.1214  0.0265  -0.1664 89  SER   A OG  
689  N  N   . SER   A 111 ? 0.5196 1.0285 0.7117 0.1153  0.0249  -0.1618 90  SER   A N   
690  C  CA  . SER   A 111 ? 0.4991 0.9984 0.7092 0.1063  0.0248  -0.1539 90  SER   A CA  
691  C  C   . SER   A 111 ? 0.4570 0.9058 0.6693 0.1096  0.0137  -0.1647 90  SER   A C   
692  O  O   . SER   A 111 ? 0.5185 0.9530 0.7381 0.1185  0.0021  -0.1780 90  SER   A O   
693  C  CB  . SER   A 111 ? 0.4750 1.0053 0.6955 0.1135  0.0217  -0.1607 90  SER   A CB  
694  O  OG  . SER   A 111 ? 0.5142 1.0930 0.7348 0.1087  0.0327  -0.1470 90  SER   A OG  
695  N  N   . ASP   A 112 ? 0.3763 0.7980 0.5819 0.1026  0.0168  -0.1580 91  ASP   A N   
696  C  CA  . ASP   A 112 ? 0.3842 0.7582 0.5904 0.1057  0.0067  -0.1661 91  ASP   A CA  
697  C  C   . ASP   A 112 ? 0.3553 0.7133 0.5739 0.0953  0.0054  -0.1567 91  ASP   A C   
698  O  O   . ASP   A 112 ? 0.4166 0.7681 0.6325 0.0772  0.0137  -0.1370 91  ASP   A O   
699  C  CB  . ASP   A 112 ? 0.4422 0.7952 0.6368 0.1010  0.0112  -0.1610 91  ASP   A CB  
700  C  CG  . ASP   A 112 ? 0.4163 0.7859 0.5965 0.1090  0.0117  -0.1681 91  ASP   A CG  
701  O  OD1 . ASP   A 112 ? 0.4834 0.8579 0.6618 0.1233  0.0007  -0.1860 91  ASP   A OD1 
702  O  OD2 . ASP   A 112 ? 0.5429 0.9213 0.7141 0.1010  0.0219  -0.1561 91  ASP   A OD2 
703  N  N   . LYS   A 113 ? 0.3537 0.6940 0.5792 0.1040  -0.0075 -0.1675 92  LYS   A N   
704  C  CA  . LYS   A 113 ? 0.3918 0.7115 0.6209 0.0929  -0.0111 -0.1568 92  LYS   A CA  
705  C  C   . LYS   A 113 ? 0.3818 0.6586 0.6078 0.1009  -0.0269 -0.1645 92  LYS   A C   
706  O  O   . LYS   A 113 ? 0.3754 0.6462 0.6044 0.1169  -0.0371 -0.1803 92  LYS   A O   
707  C  CB  . LYS   A 113 ? 0.3411 0.7067 0.5898 0.0925  -0.0082 -0.1569 92  LYS   A CB  
708  C  CG  . LYS   A 113 ? 0.4369 0.8291 0.6908 0.1106  -0.0142 -0.1748 92  LYS   A CG  
709  C  CD  . LYS   A 113 ? 0.5112 0.9457 0.7780 0.1063  -0.0090 -0.1691 92  LYS   A CD  
710  C  CE  . LYS   A 113 ? 0.5610 1.0288 0.8298 0.0910  0.0069  -0.1494 92  LYS   A CE  
711  N  NZ  . LYS   A 113 ? 0.6332 1.1449 0.9149 0.0879  0.0118  -0.1423 92  LYS   A NZ  
712  N  N   . VAL   A 114 ? 0.4635 0.7113 0.6845 0.0897  -0.0298 -0.1525 93  VAL   A N   
713  C  CA  . VAL   A 114 ? 0.3976 0.6128 0.6172 0.0954  -0.0442 -0.1551 93  VAL   A CA  
714  C  C   . VAL   A 114 ? 0.4219 0.6467 0.6496 0.0893  -0.0462 -0.1506 93  VAL   A C   
715  O  O   . VAL   A 114 ? 0.4354 0.6635 0.6611 0.0747  -0.0384 -0.1390 93  VAL   A O   
716  C  CB  . VAL   A 114 ? 0.4188 0.5877 0.6202 0.0888  -0.0466 -0.1440 93  VAL   A CB  
717  C  CG1 . VAL   A 114 ? 0.3592 0.4999 0.5605 0.0957  -0.0620 -0.1441 93  VAL   A CG1 
718  C  CG2 . VAL   A 114 ? 0.3656 0.5272 0.5610 0.0921  -0.0437 -0.1470 93  VAL   A CG2 
719  N  N   . THR   A 115 ? 0.3138 0.5425 0.5525 0.1008  -0.0582 -0.1604 94  THR   A N   
720  C  CA  . THR   A 115 ? 0.3452 0.5861 0.5940 0.0971  -0.0622 -0.1586 94  THR   A CA  
721  C  C   . THR   A 115 ? 0.3765 0.5847 0.6194 0.1027  -0.0772 -0.1580 94  THR   A C   
722  O  O   . THR   A 115 ? 0.4053 0.6017 0.6512 0.1165  -0.0882 -0.1660 94  THR   A O   
723  C  CB  . THR   A 115 ? 0.3707 0.6598 0.6423 0.1062  -0.0619 -0.1706 94  THR   A CB  
724  O  OG1 . THR   A 115 ? 0.4168 0.7427 0.6943 0.0984  -0.0469 -0.1662 94  THR   A OG1 
725  C  CG2 . THR   A 115 ? 0.5053 0.8042 0.7894 0.1038  -0.0691 -0.1700 94  THR   A CG2 
726  N  N   . VAL   A 116 ? 0.3788 0.5736 0.6143 0.0928  -0.0788 -0.1485 95  VAL   A N   
727  C  CA  . VAL   A 116 ? 0.4037 0.5734 0.6315 0.0975  -0.0922 -0.1454 95  VAL   A CA  
728  C  C   . VAL   A 116 ? 0.4285 0.6198 0.6710 0.0989  -0.0991 -0.1507 95  VAL   A C   
729  O  O   . VAL   A 116 ? 0.3899 0.5981 0.6388 0.0879  -0.0934 -0.1485 95  VAL   A O   
730  C  CB  . VAL   A 116 ? 0.3479 0.4873 0.5528 0.0877  -0.0898 -0.1319 95  VAL   A CB  
731  C  CG1 . VAL   A 116 ? 0.3715 0.4939 0.5678 0.0928  -0.1030 -0.1274 95  VAL   A CG1 
732  C  CG2 . VAL   A 116 ? 0.3441 0.4628 0.5367 0.0868  -0.0842 -0.1262 95  VAL   A CG2 
733  N  N   . ASN   A 117 ? 0.3700 0.5606 0.6204 0.1122  -0.1127 -0.1573 96  ASN   A N   
734  C  CA  . ASN   A 117 ? 0.3589 0.5665 0.6219 0.1151  -0.1219 -0.1620 96  ASN   A CA  
735  C  C   . ASN   A 117 ? 0.3354 0.5152 0.5818 0.1162  -0.1334 -0.1537 96  ASN   A C   
736  O  O   . ASN   A 117 ? 0.3628 0.5149 0.5956 0.1211  -0.1387 -0.1462 96  ASN   A O   
737  C  CB  . ASN   A 117 ? 0.4083 0.6389 0.6930 0.1311  -0.1303 -0.1760 96  ASN   A CB  
738  C  CG  . ASN   A 117 ? 0.4073 0.6793 0.7102 0.1312  -0.1189 -0.1852 96  ASN   A CG  
739  O  OD1 . ASN   A 117 ? 0.5744 0.8611 0.8881 0.1452  -0.1211 -0.1974 96  ASN   A OD1 
740  N  ND2 . ASN   A 117 ? 0.4644 0.7573 0.7720 0.1161  -0.1075 -0.1790 96  ASN   A ND2 
741  N  N   . TYR   A 118 ? 0.3472 0.5370 0.5962 0.1116  -0.1378 -0.1542 97  TYR   A N   
742  C  CA  . TYR   A 118 ? 0.3991 0.5701 0.6310 0.1133  -0.1485 -0.1476 97  TYR   A CA  
743  C  C   . TYR   A 118 ? 0.3988 0.5849 0.6449 0.1234  -0.1633 -0.1548 97  TYR   A C   
744  O  O   . TYR   A 118 ? 0.4252 0.6398 0.6932 0.1218  -0.1634 -0.1644 97  TYR   A O   
745  C  CB  . TYR   A 118 ? 0.3836 0.5513 0.6037 0.1007  -0.1436 -0.1443 97  TYR   A CB  
746  C  CG  . TYR   A 118 ? 0.3930 0.5444 0.5978 0.0914  -0.1302 -0.1367 97  TYR   A CG  
747  C  CD1 . TYR   A 118 ? 0.3972 0.5231 0.5783 0.0939  -0.1297 -0.1259 97  TYR   A CD1 
748  C  CD2 . TYR   A 118 ? 0.4005 0.5641 0.6160 0.0799  -0.1184 -0.1385 97  TYR   A CD2 
749  C  CE1 . TYR   A 118 ? 0.3796 0.4923 0.5478 0.0859  -0.1177 -0.1194 97  TYR   A CE1 
750  C  CE2 . TYR   A 118 ? 0.3884 0.5371 0.5904 0.0721  -0.1070 -0.1315 97  TYR   A CE2 
751  C  CZ  . TYR   A 118 ? 0.3773 0.5005 0.5555 0.0755  -0.1067 -0.1231 97  TYR   A CZ  
752  O  OH  . TYR   A 118 ? 0.4151 0.5251 0.5809 0.0682  -0.0956 -0.1166 97  TYR   A OH  
753  N  N   . TYR   A 119 ? 0.4874 0.6561 0.7223 0.1333  -0.1761 -0.1483 98  TYR   A N   
754  C  CA  . TYR   A 119 ? 0.4787 0.6585 0.7250 0.1444  -0.1920 -0.1533 98  TYR   A CA  
755  C  C   . TYR   A 119 ? 0.5473 0.7172 0.7724 0.1449  -0.2014 -0.1448 98  TYR   A C   
756  O  O   . TYR   A 119 ? 0.4791 0.6284 0.6799 0.1427  -0.1990 -0.1315 98  TYR   A O   
757  C  CB  . TYR   A 119 ? 0.3878 0.5581 0.6440 0.1588  -0.2023 -0.1530 98  TYR   A CB  
758  C  CG  . TYR   A 119 ? 0.3810 0.5596 0.6543 0.1616  -0.1944 -0.1630 98  TYR   A CG  
759  C  CD1 . TYR   A 119 ? 0.3545 0.5139 0.6174 0.1569  -0.1849 -0.1569 98  TYR   A CD1 
760  C  CD2 . TYR   A 119 ? 0.3922 0.6013 0.6921 0.1700  -0.1968 -0.1793 98  TYR   A CD2 
761  C  CE1 . TYR   A 119 ? 0.3825 0.5520 0.6597 0.1611  -0.1787 -0.1678 98  TYR   A CE1 
762  C  CE2 . TYR   A 119 ? 0.3881 0.6062 0.6968 0.1724  -0.1873 -0.1885 98  TYR   A CE2 
763  C  CZ  . TYR   A 119 ? 0.4291 0.6308 0.7306 0.1706  -0.1810 -0.1847 98  TYR   A CZ  
764  O  OH  . TYR   A 119 ? 0.4904 0.7021 0.7976 0.1736  -0.1722 -0.1951 98  TYR   A OH  
765  N  N   . ASP   A 120 ? 0.5561 0.7444 0.7906 0.1486  -0.2121 -0.1528 99  ASP   A N   
766  C  CA  . ASP   A 120 ? 0.6266 0.8102 0.8420 0.1537  -0.2245 -0.1465 99  ASP   A CA  
767  C  C   . ASP   A 120 ? 0.6496 0.8253 0.8661 0.1680  -0.2391 -0.1379 99  ASP   A C   
768  O  O   . ASP   A 120 ? 0.6830 0.8558 0.9175 0.1743  -0.2409 -0.1400 99  ASP   A O   
769  C  CB  . ASP   A 120 ? 0.6051 0.8111 0.8304 0.1512  -0.2315 -0.1596 99  ASP   A CB  
770  C  CG  . ASP   A 120 ? 0.7418 0.9725 1.0002 0.1557  -0.2376 -0.1720 99  ASP   A CG  
771  O  OD1 . ASP   A 120 ? 0.8245 1.0534 1.0879 0.1676  -0.2465 -0.1699 99  ASP   A OD1 
772  O  OD2 . ASP   A 120 ? 0.7911 1.0423 1.0702 0.1464  -0.2326 -0.1824 99  ASP   A OD2 
773  N  N   . GLU   A 121 ? 0.7398 0.9130 0.9374 0.1741  -0.2507 -0.1282 100 GLU   A N   
774  C  CA  . GLU   A 121 ? 0.8021 0.9673 1.0011 0.1870  -0.2662 -0.1161 100 GLU   A CA  
775  C  C   . GLU   A 121 ? 0.8012 0.9777 1.0257 0.1936  -0.2732 -0.1285 100 GLU   A C   
776  O  O   . GLU   A 121 ? 0.8475 1.0108 1.0787 0.2011  -0.2805 -0.1208 100 GLU   A O   
777  C  CB  . GLU   A 121 ? 0.7316 0.8988 0.9038 0.1918  -0.2762 -0.1023 100 GLU   A CB  
778  N  N   . GLU   A 122 ? 0.9802 1.1792 1.2187 0.1890  -0.2693 -0.1462 101 GLU   A N   
779  C  CA  . GLU   A 122 ? 0.9780 1.1912 1.2369 0.1938  -0.2738 -0.1571 101 GLU   A CA  
780  C  C   . GLU   A 122 ? 1.0214 1.2317 1.3005 0.1978  -0.2689 -0.1630 101 GLU   A C   
781  O  O   . GLU   A 122 ? 1.1335 1.3264 1.4133 0.2068  -0.2771 -0.1557 101 GLU   A O   
782  C  CB  . GLU   A 122 ? 0.9214 1.1603 1.1923 0.1855  -0.2697 -0.1723 101 GLU   A CB  
783  C  CG  . GLU   A 122 ? 1.1601 1.4158 1.4455 0.1906  -0.2780 -0.1805 101 GLU   A CG  
784  C  CD  . GLU   A 122 ? 1.3178 1.5898 1.6035 0.1836  -0.2811 -0.1885 101 GLU   A CD  
785  O  OE1 . GLU   A 122 ? 1.3845 1.6497 1.6510 0.1789  -0.2817 -0.1856 101 GLU   A OE1 
786  O  OE2 . GLU   A 122 ? 1.3150 1.6067 1.6207 0.1831  -0.2836 -0.1982 101 GLU   A OE2 
787  N  N   . GLY   A 123 ? 0.8491 1.0772 1.1447 0.1913  -0.2561 -0.1759 102 GLY   A N   
788  C  CA  . GLY   A 123 ? 0.6701 0.9041 0.9838 0.1964  -0.2509 -0.1855 102 GLY   A CA  
789  C  C   . GLY   A 123 ? 0.5824 0.8041 0.8941 0.1940  -0.2407 -0.1841 102 GLY   A C   
790  O  O   . GLY   A 123 ? 0.5298 0.7373 0.8274 0.1879  -0.2371 -0.1745 102 GLY   A O   
791  N  N   . SER   A 124 ? 0.5204 0.7496 0.8461 0.1998  -0.2363 -0.1951 103 SER   A N   
792  C  CA  . SER   A 124 ? 0.4266 0.6463 0.7517 0.1995  -0.2275 -0.1972 103 SER   A CA  
793  C  C   . SER   A 124 ? 0.3863 0.6375 0.7207 0.1913  -0.2100 -0.2065 103 SER   A C   
794  O  O   . SER   A 124 ? 0.4259 0.6760 0.7605 0.1921  -0.2016 -0.2108 103 SER   A O   
795  C  CB  . SER   A 124 ? 0.4399 0.6459 0.7723 0.2121  -0.2358 -0.2044 103 SER   A CB  
796  O  OG  . SER   A 124 ? 0.5677 0.7432 0.8938 0.2179  -0.2523 -0.1920 103 SER   A OG  
797  N  N   . ILE   A 125 ? 0.4440 0.7236 0.7868 0.1830  -0.2048 -0.2085 104 ILE   A N   
798  C  CA  . ILE   A 125 ? 0.3945 0.7057 0.7480 0.1723  -0.1883 -0.2120 104 ILE   A CA  
799  C  C   . ILE   A 125 ? 0.3740 0.6762 0.7184 0.1588  -0.1833 -0.2023 104 ILE   A C   
800  O  O   . ILE   A 125 ? 0.4190 0.7126 0.7572 0.1545  -0.1918 -0.1974 104 ILE   A O   
801  C  CB  . ILE   A 125 ? 0.4523 0.8007 0.8249 0.1690  -0.1863 -0.2176 104 ILE   A CB  
802  C  CG1 . ILE   A 125 ? 0.3826 0.7416 0.7639 0.1838  -0.1916 -0.2287 104 ILE   A CG1 
803  C  CG2 . ILE   A 125 ? 0.3301 0.7119 0.7153 0.1553  -0.1696 -0.2158 104 ILE   A CG2 
804  C  CD1 . ILE   A 125 ? 0.3701 0.7316 0.7499 0.1922  -0.1847 -0.2370 104 ILE   A CD1 
805  N  N   . PRO   A 126 ? 0.3491 0.6530 0.6913 0.1526  -0.1707 -0.2004 105 PRO   A N   
806  C  CA  . PRO   A 126 ? 0.3353 0.6256 0.6662 0.1398  -0.1661 -0.1910 105 PRO   A CA  
807  C  C   . PRO   A 126 ? 0.3875 0.6940 0.7267 0.1260  -0.1655 -0.1892 105 PRO   A C   
808  O  O   . PRO   A 126 ? 0.4547 0.7950 0.8169 0.1228  -0.1632 -0.1941 105 PRO   A O   
809  C  CB  . PRO   A 126 ? 0.3531 0.6490 0.6827 0.1346  -0.1496 -0.1900 105 PRO   A CB  
810  C  CG  . PRO   A 126 ? 0.4146 0.7423 0.7610 0.1432  -0.1452 -0.2007 105 PRO   A CG  
811  C  CD  . PRO   A 126 ? 0.3918 0.7094 0.7384 0.1569  -0.1595 -0.2068 105 PRO   A CD  
812  N  N   . ILE   A 127 ? 0.3233 0.6024 0.6410 0.1173  -0.1671 -0.1811 106 ILE   A N   
813  C  CA  . ILE   A 127 ? 0.4328 0.7209 0.7580 0.1047  -0.1695 -0.1812 106 ILE   A CA  
814  C  C   . ILE   A 127 ? 0.4695 0.7558 0.7944 0.0877  -0.1557 -0.1747 106 ILE   A C   
815  O  O   . ILE   A 127 ? 0.4594 0.7595 0.8014 0.0755  -0.1572 -0.1751 106 ILE   A O   
816  C  CB  . ILE   A 127 ? 0.5296 0.7939 0.8333 0.1083  -0.1832 -0.1799 106 ILE   A CB  
817  C  CG1 . ILE   A 127 ? 0.4630 0.6932 0.7340 0.1061  -0.1773 -0.1702 106 ILE   A CG1 
818  C  CG2 . ILE   A 127 ? 0.5432 0.8091 0.8475 0.1250  -0.1978 -0.1835 106 ILE   A CG2 
819  C  CD1 . ILE   A 127 ? 0.5531 0.7666 0.8004 0.1107  -0.1892 -0.1682 106 ILE   A CD1 
820  N  N   . ASP   A 128 ? 0.4175 0.6866 0.7256 0.0865  -0.1440 -0.1684 107 ASP   A N   
821  C  CA  . ASP   A 128 ? 0.4439 0.7132 0.7531 0.0715  -0.1306 -0.1615 107 ASP   A CA  
822  C  C   . ASP   A 128 ? 0.3936 0.6556 0.6911 0.0754  -0.1185 -0.1579 107 ASP   A C   
823  O  O   . ASP   A 128 ? 0.3614 0.6157 0.6516 0.0892  -0.1222 -0.1615 107 ASP   A O   
824  C  CB  . ASP   A 128 ? 0.4737 0.7156 0.7653 0.0628  -0.1339 -0.1577 107 ASP   A CB  
825  C  CG  . ASP   A 128 ? 0.5515 0.7976 0.8542 0.0459  -0.1245 -0.1516 107 ASP   A CG  
826  O  OD1 . ASP   A 128 ? 0.4728 0.7460 0.7964 0.0398  -0.1147 -0.1478 107 ASP   A OD1 
827  O  OD2 . ASP   A 128 ? 0.6655 0.8897 0.9565 0.0395  -0.1277 -0.1505 107 ASP   A OD2 
828  N  N   . GLN   A 129 ? 0.4175 0.6815 0.7150 0.0635  -0.1055 -0.1509 108 GLN   A N   
829  C  CA  . GLN   A 129 ? 0.3698 0.6333 0.6595 0.0668  -0.0939 -0.1488 108 GLN   A CA  
830  C  C   . GLN   A 129 ? 0.3922 0.6406 0.6708 0.0531  -0.0832 -0.1386 108 GLN   A C   
831  O  O   . GLN   A 129 ? 0.4981 0.7597 0.7913 0.0395  -0.0799 -0.1331 108 GLN   A O   
832  C  CB  . GLN   A 129 ? 0.3868 0.6947 0.7008 0.0710  -0.0877 -0.1540 108 GLN   A CB  
833  C  CG  . GLN   A 129 ? 0.4918 0.8041 0.7986 0.0786  -0.0783 -0.1564 108 GLN   A CG  
834  C  CD  . GLN   A 129 ? 0.6026 0.9643 0.9321 0.0876  -0.0742 -0.1652 108 GLN   A CD  
835  O  OE1 . GLN   A 129 ? 0.5952 0.9734 0.9382 0.0995  -0.0837 -0.1758 108 GLN   A OE1 
836  N  NE2 . GLN   A 129 ? 0.5433 0.9322 0.8772 0.0828  -0.0603 -0.1608 108 GLN   A NE2 
837  N  N   . ALA   A 130 ? 0.4267 0.6470 0.6818 0.0566  -0.0792 -0.1353 109 ALA   A N   
838  C  CA  . ALA   A 130 ? 0.4181 0.6241 0.6615 0.0459  -0.0688 -0.1264 109 ALA   A CA  
839  C  C   . ALA   A 130 ? 0.3958 0.6100 0.6367 0.0501  -0.0584 -0.1261 109 ALA   A C   
840  O  O   . ALA   A 130 ? 0.3946 0.6031 0.6303 0.0630  -0.0622 -0.1325 109 ALA   A O   
841  C  CB  . ALA   A 130 ? 0.4112 0.5795 0.6287 0.0459  -0.0728 -0.1225 109 ALA   A CB  
842  N  N   . GLY   A 131 ? 0.4190 0.6464 0.6647 0.0396  -0.0468 -0.1189 110 GLY   A N   
843  C  CA  . GLY   A 131 ? 0.4166 0.6595 0.6613 0.0440  -0.0369 -0.1197 110 GLY   A CA  
844  C  C   . GLY   A 131 ? 0.4191 0.6434 0.6487 0.0353  -0.0276 -0.1101 110 GLY   A C   
845  O  O   . GLY   A 131 ? 0.4551 0.6694 0.6844 0.0225  -0.0256 -0.1008 110 GLY   A O   
846  N  N   . LEU   A 132 ? 0.3447 0.5642 0.5636 0.0433  -0.0236 -0.1135 111 LEU   A N   
847  C  CA  . LEU   A 132 ? 0.3797 0.5880 0.5859 0.0370  -0.0142 -0.1056 111 LEU   A CA  
848  C  C   . LEU   A 132 ? 0.3768 0.6215 0.5909 0.0418  -0.0056 -0.1089 111 LEU   A C   
849  O  O   . LEU   A 132 ? 0.3927 0.6480 0.6087 0.0564  -0.0094 -0.1220 111 LEU   A O   
850  C  CB  . LEU   A 132 ? 0.3929 0.5621 0.5786 0.0422  -0.0184 -0.1063 111 LEU   A CB  
851  C  CG  . LEU   A 132 ? 0.4451 0.6001 0.6171 0.0367  -0.0099 -0.0990 111 LEU   A CG  
852  C  CD1 . LEU   A 132 ? 0.4672 0.6171 0.6378 0.0223  -0.0043 -0.0875 111 LEU   A CD1 
853  C  CD2 . LEU   A 132 ? 0.3973 0.5178 0.5535 0.0421  -0.0155 -0.0988 111 LEU   A CD2 
854  N  N   . PHE   A 133 ? 0.3500 0.6157 0.5697 0.0305  0.0048  -0.0974 112 PHE   A N   
855  C  CA  . PHE   A 133 ? 0.3513 0.6580 0.5766 0.0345  0.0144  -0.0979 112 PHE   A CA  
856  C  C   . PHE   A 133 ? 0.3362 0.6271 0.5455 0.0302  0.0216  -0.0907 112 PHE   A C   
857  O  O   . PHE   A 133 ? 0.3577 0.6279 0.5629 0.0166  0.0244  -0.0771 112 PHE   A O   
858  C  CB  . PHE   A 133 ? 0.3766 0.7292 0.6243 0.0248  0.0209  -0.0868 112 PHE   A CB  
859  C  CG  . PHE   A 133 ? 0.4984 0.8705 0.7644 0.0287  0.0138  -0.0938 112 PHE   A CG  
860  C  CD1 . PHE   A 133 ? 0.5406 0.9477 0.8141 0.0453  0.0126  -0.1088 112 PHE   A CD1 
861  C  CD2 . PHE   A 133 ? 0.6033 0.9590 0.8794 0.0173  0.0069  -0.0872 112 PHE   A CD2 
862  C  CE1 . PHE   A 133 ? 0.5908 1.0169 0.8820 0.0496  0.0056  -0.1156 112 PHE   A CE1 
863  C  CE2 . PHE   A 133 ? 0.6100 0.9842 0.9036 0.0210  -0.0004 -0.0940 112 PHE   A CE2 
864  C  CZ  . PHE   A 133 ? 0.6150 1.0247 0.9163 0.0369  -0.0006 -0.1073 112 PHE   A CZ  
865  N  N   . LEU   A 134 ? 0.3242 0.6244 0.5256 0.0428  0.0232  -0.1013 113 LEU   A N   
866  C  CA  . LEU   A 134 ? 0.3463 0.6248 0.5311 0.0416  0.0269  -0.0983 113 LEU   A CA  
867  C  C   . LEU   A 134 ? 0.3012 0.6220 0.4869 0.0445  0.0369  -0.0967 113 LEU   A C   
868  O  O   . LEU   A 134 ? 0.3162 0.6791 0.5104 0.0566  0.0379  -0.1077 113 LEU   A O   
869  C  CB  . LEU   A 134 ? 0.3846 0.6297 0.5591 0.0540  0.0167  -0.1124 113 LEU   A CB  
870  C  CG  . LEU   A 134 ? 0.4159 0.6192 0.5860 0.0511  0.0072  -0.1105 113 LEU   A CG  
871  C  CD1 . LEU   A 134 ? 0.3835 0.5590 0.5482 0.0626  -0.0036 -0.1209 113 LEU   A CD1 
872  C  CD2 . LEU   A 134 ? 0.3122 0.4893 0.4719 0.0362  0.0118  -0.0948 113 LEU   A CD2 
873  N  N   . THR   A 135 ? 0.2948 0.6069 0.4714 0.0345  0.0442  -0.0831 114 THR   A N   
874  C  CA  . THR   A 135 ? 0.3285 0.6747 0.5009 0.0381  0.0529  -0.0810 114 THR   A CA  
875  C  C   . THR   A 135 ? 0.3035 0.6133 0.4583 0.0405  0.0507  -0.0848 114 THR   A C   
876  O  O   . THR   A 135 ? 0.2779 0.5546 0.4256 0.0285  0.0521  -0.0720 114 THR   A O   
877  C  CB  . THR   A 135 ? 0.2848 0.6598 0.4661 0.0225  0.0634  -0.0573 114 THR   A CB  
878  O  OG1 . THR   A 135 ? 0.3314 0.7373 0.5329 0.0180  0.0641  -0.0518 114 THR   A OG1 
879  C  CG2 . THR   A 135 ? 0.3080 0.7223 0.4824 0.0277  0.0719  -0.0538 114 THR   A CG2 
880  N  N   . ALA   A 136 ? 0.2998 0.6156 0.4495 0.0568  0.0457  -0.1037 115 ALA   A N   
881  C  CA  . ALA   A 136 ? 0.2723 0.5550 0.4092 0.0596  0.0416  -0.1086 115 ALA   A CA  
882  C  C   . ALA   A 136 ? 0.3463 0.6556 0.4755 0.0590  0.0506  -0.1025 115 ALA   A C   
883  O  O   . ALA   A 136 ? 0.3459 0.7002 0.4760 0.0676  0.0540  -0.1076 115 ALA   A O   
884  C  CB  . ALA   A 136 ? 0.3410 0.6122 0.4802 0.0771  0.0282  -0.1322 115 ALA   A CB  
885  N  N   A ILE   A 137 ? 0.3145 0.5947 0.4340 0.0483  0.0536  -0.0898 116 ILE   A N   
886  N  N   B ILE   A 137 ? 0.3227 0.6020 0.4419 0.0489  0.0532  -0.0906 116 ILE   A N   
887  C  CA  A ILE   A 137 ? 0.3105 0.6102 0.4215 0.0478  0.0606  -0.0836 116 ILE   A CA  
888  C  CA  B ILE   A 137 ? 0.3149 0.6139 0.4260 0.0468  0.0610  -0.0823 116 ILE   A CA  
889  C  C   A ILE   A 137 ? 0.3492 0.6097 0.4501 0.0496  0.0545  -0.0894 116 ILE   A C   
890  C  C   B ILE   A 137 ? 0.3494 0.6097 0.4498 0.0476  0.0559  -0.0863 116 ILE   A C   
891  O  O   A ILE   A 137 ? 0.3612 0.5787 0.4614 0.0457  0.0480  -0.0895 116 ILE   A O   
892  O  O   B ILE   A 137 ? 0.3670 0.5836 0.4656 0.0411  0.0512  -0.0828 116 ILE   A O   
893  C  CB  A ILE   A 137 ? 0.3302 0.6400 0.4428 0.0310  0.0712  -0.0575 116 ILE   A CB  
894  C  CB  B ILE   A 137 ? 0.3290 0.6378 0.4435 0.0296  0.0712  -0.0563 116 ILE   A CB  
895  C  CG1 A ILE   A 137 ? 0.3132 0.5724 0.4238 0.0176  0.0689  -0.0462 116 ILE   A CG1 
896  C  CG1 B ILE   A 137 ? 0.3513 0.7032 0.4804 0.0277  0.0758  -0.0501 116 ILE   A CG1 
897  C  CG2 A ILE   A 137 ? 0.3509 0.7031 0.4779 0.0274  0.0767  -0.0489 116 ILE   A CG2 
898  C  CG2 B ILE   A 137 ? 0.3698 0.6953 0.4758 0.0271  0.0782  -0.0454 116 ILE   A CG2 
899  C  CD1 A ILE   A 137 ? 0.3315 0.5941 0.4471 0.0019  0.0756  -0.0227 116 ILE   A CD1 
900  C  CD1 B ILE   A 137 ? 0.3434 0.6977 0.4828 0.0089  0.0818  -0.0240 116 ILE   A CD1 
901  N  N   . GLU   A 138 ? 0.3355 0.6150 0.4293 0.0560  0.0564  -0.0936 117 GLU   A N   
902  C  CA  . GLU   A 138 ? 0.3409 0.5892 0.4269 0.0566  0.0513  -0.0971 117 GLU   A CA  
903  C  C   . GLU   A 138 ? 0.3574 0.6051 0.4354 0.0442  0.0611  -0.0763 117 GLU   A C   
904  O  O   . GLU   A 138 ? 0.3566 0.6438 0.4329 0.0433  0.0695  -0.0673 117 GLU   A O   
905  C  CB  . GLU   A 138 ? 0.3750 0.6427 0.4604 0.0744  0.0432  -0.1204 117 GLU   A CB  
906  C  CG  . GLU   A 138 ? 0.4823 0.7177 0.5639 0.0752  0.0353  -0.1256 117 GLU   A CG  
907  C  CD  . GLU   A 138 ? 0.5810 0.8345 0.6653 0.0938  0.0240  -0.1516 117 GLU   A CD  
908  O  OE1 . GLU   A 138 ? 0.6508 0.9255 0.7372 0.1034  0.0172  -0.1634 117 GLU   A OE1 
909  O  OE2 . GLU   A 138 ? 0.6951 0.9337 0.7769 0.0951  0.0183  -0.1558 117 GLU   A OE2 
910  N  N   . ILE   A 139 ? 0.3024 0.5082 0.3766 0.0348  0.0597  -0.0676 118 ILE   A N   
911  C  CA  . ILE   A 139 ? 0.2832 0.4821 0.3511 0.0243  0.0666  -0.0498 118 ILE   A CA  
912  C  C   . ILE   A 139 ? 0.3982 0.5661 0.4604 0.0255  0.0612  -0.0544 118 ILE   A C   
913  O  O   . ILE   A 139 ? 0.4650 0.6012 0.5296 0.0254  0.0544  -0.0595 118 ILE   A O   
914  C  CB  . ILE   A 139 ? 0.3357 0.5165 0.4074 0.0104  0.0708  -0.0323 118 ILE   A CB  
915  C  CG1 . ILE   A 139 ? 0.3798 0.5897 0.4616 0.0078  0.0744  -0.0272 118 ILE   A CG1 
916  C  CG2 . ILE   A 139 ? 0.3924 0.5674 0.4601 0.0011  0.0762  -0.0150 118 ILE   A CG2 
917  C  CD1 . ILE   A 139 ? 0.3450 0.5354 0.4340 -0.0053 0.0752  -0.0127 118 ILE   A CD1 
918  N  N   . SER   A 140 ? 0.3764 0.5559 0.4322 0.0264  0.0640  -0.0509 119 SER   A N   
919  C  CA  . SER   A 140 ? 0.3408 0.4961 0.3935 0.0279  0.0584  -0.0557 119 SER   A CA  
920  C  C   . SER   A 140 ? 0.3405 0.5081 0.3858 0.0246  0.0643  -0.0443 119 SER   A C   
921  O  O   . SER   A 140 ? 0.3315 0.5356 0.3731 0.0310  0.0669  -0.0467 119 SER   A O   
922  C  CB  . SER   A 140 ? 0.3071 0.4673 0.3642 0.0415  0.0471  -0.0783 119 SER   A CB  
923  O  OG  . SER   A 140 ? 0.3990 0.5322 0.4581 0.0410  0.0397  -0.0816 119 SER   A OG  
924  N  N   . LEU   A 141 ? 0.4008 0.5412 0.4441 0.0157  0.0664  -0.0320 120 LEU   A N   
925  C  CA  . LEU   A 141 ? 0.3933 0.5397 0.4308 0.0128  0.0703  -0.0214 120 LEU   A CA  
926  C  C   . LEU   A 141 ? 0.3605 0.4969 0.3971 0.0188  0.0631  -0.0329 120 LEU   A C   
927  O  O   . LEU   A 141 ? 0.3668 0.4730 0.4071 0.0159  0.0589  -0.0341 120 LEU   A O   
928  C  CB  . LEU   A 141 ? 0.3371 0.4602 0.3752 0.0018  0.0748  -0.0041 120 LEU   A CB  
929  C  CG  . LEU   A 141 ? 0.3579 0.4872 0.3925 -0.0021 0.0787  0.0101  120 LEU   A CG  
930  C  CD1 . LEU   A 141 ? 0.3048 0.4725 0.3390 -0.0022 0.0836  0.0200  120 LEU   A CD1 
931  C  CD2 . LEU   A 141 ? 0.3395 0.4409 0.3771 -0.0106 0.0800  0.0223  120 LEU   A CD2 
932  N  N   . ASP   A 142 ? 0.3622 0.5266 0.3950 0.0274  0.0611  -0.0411 121 ASP   A N   
933  C  CA  . ASP   A 142 ? 0.3707 0.5295 0.4059 0.0350  0.0510  -0.0567 121 ASP   A CA  
934  C  C   . ASP   A 142 ? 0.3482 0.5115 0.3777 0.0335  0.0527  -0.0488 121 ASP   A C   
935  O  O   . ASP   A 142 ? 0.3948 0.5837 0.4163 0.0328  0.0600  -0.0375 121 ASP   A O   
936  C  CB  . ASP   A 142 ? 0.3835 0.5714 0.4199 0.0496  0.0437  -0.0786 121 ASP   A CB  
937  C  CG  . ASP   A 142 ? 0.3932 0.5715 0.4385 0.0530  0.0382  -0.0901 121 ASP   A CG  
938  O  OD1 . ASP   A 142 ? 0.3811 0.5267 0.4318 0.0441  0.0383  -0.0821 121 ASP   A OD1 
939  O  OD2 . ASP   A 142 ? 0.3581 0.5636 0.4047 0.0657  0.0334  -0.1076 121 ASP   A OD2 
940  N  N   . VAL   A 143 ? 0.3181 0.4578 0.3536 0.0325  0.0455  -0.0532 122 VAL   A N   
941  C  CA  . VAL   A 143 ? 0.3259 0.4690 0.3584 0.0323  0.0448  -0.0489 122 VAL   A CA  
942  C  C   . VAL   A 143 ? 0.2917 0.4285 0.3341 0.0391  0.0308  -0.0674 122 VAL   A C   
943  O  O   . VAL   A 143 ? 0.3441 0.4686 0.3975 0.0424  0.0214  -0.0808 122 VAL   A O   
944  C  CB  . VAL   A 143 ? 0.3268 0.4455 0.3594 0.0213  0.0513  -0.0302 122 VAL   A CB  
945  C  CG1 . VAL   A 143 ? 0.2552 0.3801 0.2811 0.0153  0.0619  -0.0131 122 VAL   A CG1 
946  C  CG2 . VAL   A 143 ? 0.3104 0.3972 0.3528 0.0159  0.0479  -0.0305 122 VAL   A CG2 
947  N  N   . ASP   A 144 ? 0.3540 0.4989 0.3948 0.0413  0.0278  -0.0678 123 ASP   A N   
948  C  CA  . ASP   A 144 ? 0.3787 0.5197 0.4315 0.0477  0.0124  -0.0858 123 ASP   A CA  
949  C  C   . ASP   A 144 ? 0.3870 0.4942 0.4544 0.0373  0.0089  -0.0771 123 ASP   A C   
950  O  O   . ASP   A 144 ? 0.3917 0.4962 0.4633 0.0349  0.0063  -0.0732 123 ASP   A O   
951  C  CB  . ASP   A 144 ? 0.4082 0.5789 0.4523 0.0561  0.0099  -0.0916 123 ASP   A CB  
952  C  CG  . ASP   A 144 ? 0.4525 0.6172 0.5111 0.0618  -0.0074 -0.1099 123 ASP   A CG  
953  O  OD1 . ASP   A 144 ? 0.4392 0.5905 0.5134 0.0659  -0.0209 -0.1271 123 ASP   A OD1 
954  O  OD2 . ASP   A 144 ? 0.4011 0.5738 0.4576 0.0623  -0.0091 -0.1070 123 ASP   A OD2 
955  N  N   . ALA   A 145 ? 0.3653 0.4496 0.4410 0.0314  0.0089  -0.0731 124 ALA   A N   
956  C  CA  . ALA   A 145 ? 0.3909 0.4487 0.4798 0.0212  0.0075  -0.0613 124 ALA   A CA  
957  C  C   . ALA   A 145 ? 0.3708 0.4189 0.4818 0.0221  -0.0097 -0.0717 124 ALA   A C   
958  O  O   . ALA   A 145 ? 0.4134 0.4477 0.5367 0.0135  -0.0109 -0.0597 124 ALA   A O   
959  C  CB  . ALA   A 145 ? 0.3472 0.3876 0.4379 0.0157  0.0116  -0.0536 124 ALA   A CB  
960  N  N   . ASP   A 146 ? 0.3612 0.4179 0.4793 0.0326  -0.0239 -0.0940 125 ASP   A N   
961  C  CA  . ASP   A 146 ? 0.4201 0.4664 0.5629 0.0341  -0.0438 -0.1063 125 ASP   A CA  
962  C  C   . ASP   A 146 ? 0.4066 0.4704 0.5477 0.0391  -0.0485 -0.1140 125 ASP   A C   
963  O  O   . ASP   A 146 ? 0.4669 0.5242 0.6298 0.0410  -0.0668 -0.1264 125 ASP   A O   
964  C  CB  . ASP   A 146 ? 0.3922 0.4357 0.5480 0.0446  -0.0610 -0.1299 125 ASP   A CB  
965  C  CG  . ASP   A 146 ? 0.4181 0.4936 0.5559 0.0608  -0.0603 -0.1507 125 ASP   A CG  
966  O  OD1 . ASP   A 146 ? 0.4100 0.5101 0.5298 0.0641  -0.0512 -0.1483 125 ASP   A OD1 
967  O  OD2 . ASP   A 146 ? 0.4494 0.5281 0.5916 0.0709  -0.0692 -0.1686 125 ASP   A OD2 
968  N  N   . ARG   A 147 ? 0.4391 0.5248 0.5564 0.0413  -0.0339 -0.1068 126 ARG   A N   
969  C  CA  . ARG   A 147 ? 0.4453 0.5448 0.5598 0.0427  -0.0350 -0.1058 126 ARG   A CA  
970  C  C   . ARG   A 147 ? 0.4422 0.5606 0.5619 0.0568  -0.0526 -0.1327 126 ARG   A C   
971  O  O   . ARG   A 147 ? 0.5322 0.6498 0.6653 0.0569  -0.0641 -0.1382 126 ARG   A O   
972  C  CB  . ARG   A 147 ? 0.3671 0.4461 0.4997 0.0302  -0.0364 -0.0904 126 ARG   A CB  
973  C  CG  . ARG   A 147 ? 0.3810 0.4465 0.5069 0.0190  -0.0194 -0.0662 126 ARG   A CG  
974  C  CD  . ARG   A 147 ? 0.3348 0.3832 0.4818 0.0076  -0.0219 -0.0520 126 ARG   A CD  
975  N  NE  . ARG   A 147 ? 0.2933 0.3334 0.4316 0.0000  -0.0062 -0.0321 126 ARG   A NE  
976  C  CZ  . ARG   A 147 ? 0.3342 0.3648 0.4862 -0.0093 -0.0041 -0.0163 126 ARG   A CZ  
977  N  NH1 . ARG   A 147 ? 0.3439 0.3710 0.5219 -0.0146 -0.0163 -0.0147 126 ARG   A NH1 
978  N  NH2 . ARG   A 147 ? 0.3415 0.3687 0.4823 -0.0132 0.0099  -0.0018 126 ARG   A NH2 
979  N  N   . ASP   A 148 ? 0.4315 0.5696 0.5408 0.0699  -0.0554 -0.1508 127 ASP   A N   
980  C  CA  . ASP   A 148 ? 0.4561 0.6199 0.5657 0.0870  -0.0713 -0.1791 127 ASP   A CA  
981  C  C   . ASP   A 148 ? 0.5170 0.7250 0.5969 0.0981  -0.0593 -0.1798 127 ASP   A C   
982  O  O   . ASP   A 148 ? 0.5314 0.7700 0.6062 0.1151  -0.0704 -0.2040 127 ASP   A O   
983  C  CB  . ASP   A 148 ? 0.4851 0.6405 0.6122 0.0970  -0.0900 -0.2055 127 ASP   A CB  
984  C  CG  . ASP   A 148 ? 0.4700 0.6341 0.5839 0.1009  -0.0792 -0.2051 127 ASP   A CG  
985  O  OD1 . ASP   A 148 ? 0.5390 0.7105 0.6333 0.0930  -0.0576 -0.1820 127 ASP   A OD1 
986  O  OD2 . ASP   A 148 ? 0.5015 0.6649 0.6266 0.1121  -0.0936 -0.2284 127 ASP   A OD2 
987  N  N   . GLY   A 149 ? 0.5059 0.7196 0.5675 0.0892  -0.0380 -0.1535 128 GLY   A N   
988  C  CA  . GLY   A 149 ? 0.4415 0.6974 0.4780 0.0970  -0.0263 -0.1478 128 GLY   A CA  
989  C  C   . GLY   A 149 ? 0.4840 0.7671 0.5101 0.1070  -0.0222 -0.1572 128 GLY   A C   
990  O  O   . GLY   A 149 ? 0.5099 0.8365 0.5168 0.1154  -0.0142 -0.1540 128 GLY   A O   
991  N  N   . VAL   A 150 ? 0.4669 0.7286 0.5057 0.1067  -0.0275 -0.1676 129 VAL   A N   
992  C  CA  . VAL   A 150 ? 0.4488 0.7345 0.4800 0.1155  -0.0231 -0.1759 129 VAL   A CA  
993  C  C   . VAL   A 150 ? 0.4885 0.7409 0.5267 0.1015  -0.0143 -0.1597 129 VAL   A C   
994  O  O   . VAL   A 150 ? 0.4727 0.6836 0.5282 0.0922  -0.0211 -0.1578 129 VAL   A O   
995  C  CB  . VAL   A 150 ? 0.5262 0.8255 0.5673 0.1351  -0.0432 -0.2133 129 VAL   A CB  
996  C  CG1 . VAL   A 150 ? 0.5154 0.8376 0.5509 0.1434  -0.0383 -0.2203 129 VAL   A CG1 
997  C  CG2 . VAL   A 150 ? 0.5932 0.9316 0.6250 0.1516  -0.0523 -0.2318 129 VAL   A CG2 
998  N  N   . VAL   A 151 ? 0.4749 0.7482 0.5006 0.0999  0.0004  -0.1472 130 VAL   A N   
999  C  CA  . VAL   A 151 ? 0.4383 0.6835 0.4683 0.0862  0.0100  -0.1297 130 VAL   A CA  
1000 C  C   . VAL   A 151 ? 0.3656 0.6018 0.4077 0.0937  -0.0002 -0.1499 130 VAL   A C   
1001 O  O   . VAL   A 151 ? 0.3978 0.6652 0.4343 0.1037  0.0022  -0.1594 130 VAL   A O   
1002 C  CB  . VAL   A 151 ? 0.3606 0.6295 0.3763 0.0797  0.0281  -0.1062 130 VAL   A CB  
1003 C  CG1 . VAL   A 151 ? 0.3570 0.5946 0.3784 0.0661  0.0357  -0.0905 130 VAL   A CG1 
1004 C  CG2 . VAL   A 151 ? 0.3845 0.6625 0.3905 0.0739  0.0353  -0.0870 130 VAL   A CG2 
1005 N  N   . GLU   A 152 ? 0.3806 0.5755 0.4407 0.0886  -0.0119 -0.1551 131 GLU   A N   
1006 C  CA  . GLU   A 152 ? 0.3953 0.5760 0.4700 0.0945  -0.0235 -0.1718 131 GLU   A CA  
1007 C  C   . GLU   A 152 ? 0.4033 0.5795 0.4733 0.0868  -0.0105 -0.1568 131 GLU   A C   
1008 O  O   . GLU   A 152 ? 0.3911 0.5670 0.4499 0.0750  0.0055  -0.1330 131 GLU   A O   
1009 C  CB  . GLU   A 152 ? 0.3738 0.5117 0.4717 0.0886  -0.0396 -0.1753 131 GLU   A CB  
1010 C  CG  . GLU   A 152 ? 0.4330 0.5377 0.5335 0.0694  -0.0300 -0.1473 131 GLU   A CG  
1011 C  CD  . GLU   A 152 ? 0.4479 0.5520 0.5429 0.0617  -0.0239 -0.1333 131 GLU   A CD  
1012 O  OE1 . GLU   A 152 ? 0.4390 0.5719 0.5225 0.0694  -0.0222 -0.1397 131 GLU   A OE1 
1013 O  OE2 . GLU   A 152 ? 0.3900 0.4678 0.4923 0.0487  -0.0211 -0.1157 131 GLU   A OE2 
1014 N  N   . LYS   A 153 ? 0.4173 0.5891 0.4976 0.0943  -0.0194 -0.1719 132 LYS   A N   
1015 C  CA  . LYS   A 153 ? 0.4331 0.6046 0.5103 0.0894  -0.0093 -0.1616 132 LYS   A CA  
1016 C  C   . LYS   A 153 ? 0.4543 0.5806 0.5410 0.0747  -0.0096 -0.1452 132 LYS   A C   
1017 O  O   . LYS   A 153 ? 0.4534 0.5525 0.5577 0.0758  -0.0247 -0.1538 132 LYS   A O   
1018 C  CB  . LYS   A 153 ? 0.4561 0.6484 0.5395 0.1059  -0.0185 -0.1859 132 LYS   A CB  
1019 C  CG  . LYS   A 153 ? 0.5080 0.7544 0.5772 0.1186  -0.0137 -0.1950 132 LYS   A CG  
1020 C  CD  . LYS   A 153 ? 0.6773 0.9389 0.7525 0.1309  -0.0281 -0.2138 132 LYS   A CD  
1021 C  CE  . LYS   A 153 ? 0.7199 1.0346 0.7796 0.1389  -0.0242 -0.2142 132 LYS   A CE  
1022 N  NZ  . LYS   A 153 ? 0.7240 1.0609 0.7729 0.1307  -0.0058 -0.1929 132 LYS   A NZ  
1023 N  N   . ASN   A 154 ? 0.4033 0.5235 0.4797 0.0613  0.0060  -0.1214 133 ASN   A N   
1024 C  CA  . ASN   A 154 ? 0.4183 0.5049 0.4993 0.0492  0.0084  -0.1056 133 ASN   A CA  
1025 C  C   . ASN   A 154 ? 0.4267 0.4822 0.5228 0.0450  -0.0037 -0.1050 133 ASN   A C   
1026 O  O   . ASN   A 154 ? 0.5237 0.5578 0.6336 0.0444  -0.0137 -0.1070 133 ASN   A O   
1027 C  CB  . ASN   A 154 ? 0.4777 0.5636 0.5626 0.0519  0.0072  -0.1100 133 ASN   A CB  
1028 C  CG  . ASN   A 154 ? 0.3889 0.4460 0.4755 0.0404  0.0108  -0.0932 133 ASN   A CG  
1029 O  OD1 . ASN   A 154 ? 0.4178 0.4646 0.4972 0.0303  0.0197  -0.0762 133 ASN   A OD1 
1030 N  ND2 . ASN   A 154 ? 0.4489 0.4946 0.5448 0.0433  0.0030  -0.0986 133 ASN   A ND2 
1031 N  N   . ASN   A 155 ? 0.4135 0.4678 0.5083 0.0415  -0.0030 -0.1000 134 ASN   A N   
1032 C  CA  . ASN   A 155 ? 0.4462 0.4742 0.5566 0.0350  -0.0124 -0.0943 134 ASN   A CA  
1033 C  C   . ASN   A 155 ? 0.4318 0.4381 0.5432 0.0238  -0.0062 -0.0746 134 ASN   A C   
1034 O  O   . ASN   A 155 ? 0.4059 0.4156 0.5023 0.0178  0.0085  -0.0606 134 ASN   A O   
1035 C  CB  . ASN   A 155 ? 0.4136 0.4475 0.5205 0.0319  -0.0094 -0.0890 134 ASN   A CB  
1036 C  CG  . ASN   A 155 ? 0.4387 0.4508 0.5655 0.0255  -0.0206 -0.0839 134 ASN   A CG  
1037 O  OD1 . ASN   A 155 ? 0.4451 0.4369 0.5822 0.0173  -0.0221 -0.0711 134 ASN   A OD1 
1038 N  ND2 . ASN   A 155 ? 0.3495 0.3684 0.4828 0.0289  -0.0288 -0.0929 134 ASN   A ND2 
1039 N  N   . PRO   A 156 ? 0.4391 0.4243 0.5683 0.0213  -0.0180 -0.0729 135 PRO   A N   
1040 C  CA  . PRO   A 156 ? 0.3944 0.3648 0.5221 0.0123  -0.0118 -0.0540 135 PRO   A CA  
1041 C  C   . PRO   A 156 ? 0.4633 0.4312 0.5848 0.0027  -0.0012 -0.0346 135 PRO   A C   
1042 O  O   . PRO   A 156 ? 0.5078 0.4728 0.6196 -0.0021 0.0085  -0.0211 135 PRO   A O   
1043 C  CB  . PRO   A 156 ? 0.4549 0.4057 0.6068 0.0120  -0.0295 -0.0549 135 PRO   A CB  
1044 C  CG  . PRO   A 156 ? 0.4350 0.3850 0.6044 0.0176  -0.0454 -0.0710 135 PRO   A CG  
1045 C  CD  . PRO   A 156 ? 0.4514 0.4263 0.6041 0.0275  -0.0390 -0.0883 135 PRO   A CD  
1046 N  N   . LYS   A 157 ? 0.4186 0.3895 0.5454 0.0011  -0.0033 -0.0343 136 LYS   A N   
1047 C  CA  . LYS   A 157 ? 0.4248 0.3966 0.5470 -0.0065 0.0064  -0.0174 136 LYS   A CA  
1048 C  C   . LYS   A 157 ? 0.4036 0.3900 0.5065 -0.0044 0.0192  -0.0181 136 LYS   A C   
1049 O  O   . LYS   A 157 ? 0.3897 0.3791 0.4906 -0.0081 0.0248  -0.0087 136 LYS   A O   
1050 C  CB  . LYS   A 157 ? 0.4573 0.4234 0.6010 -0.0109 -0.0046 -0.0134 136 LYS   A CB  
1051 C  CG  . LYS   A 157 ? 0.4825 0.4326 0.6498 -0.0153 -0.0185 -0.0072 136 LYS   A CG  
1052 C  CD  . LYS   A 157 ? 0.6586 0.6041 0.8512 -0.0221 -0.0296 0.0006  136 LYS   A CD  
1053 C  CE  . LYS   A 157 ? 0.7742 0.7055 0.9915 -0.0299 -0.0409 0.0164  136 LYS   A CE  
1054 N  NZ  . LYS   A 157 ? 0.8298 0.7662 1.0339 -0.0353 -0.0268 0.0379  136 LYS   A NZ  
1055 N  N   . LYS   A 158 ? 0.3864 0.3836 0.4768 0.0013  0.0234  -0.0276 137 LYS   A N   
1056 C  CA  . LYS   A 158 ? 0.3776 0.3900 0.4533 0.0028  0.0333  -0.0264 137 LYS   A CA  
1057 C  C   . LYS   A 158 ? 0.3969 0.4052 0.4620 -0.0025 0.0451  -0.0119 137 LYS   A C   
1058 O  O   . LYS   A 158 ? 0.3773 0.3939 0.4341 -0.0026 0.0516  -0.0076 137 LYS   A O   
1059 C  CB  . LYS   A 158 ? 0.3408 0.3704 0.4090 0.0095  0.0343  -0.0375 137 LYS   A CB  
1060 C  CG  . LYS   A 158 ? 0.3433 0.3704 0.4066 0.0082  0.0393  -0.0348 137 LYS   A CG  
1061 C  CD  . LYS   A 158 ? 0.3669 0.4162 0.4262 0.0152  0.0397  -0.0455 137 LYS   A CD  
1062 C  CE  . LYS   A 158 ? 0.3589 0.4086 0.4144 0.0127  0.0455  -0.0411 137 LYS   A CE  
1063 N  NZ  . LYS   A 158 ? 0.3683 0.4436 0.4232 0.0201  0.0449  -0.0520 137 LYS   A NZ  
1064 N  N   . ALA   A 159 ? 0.4089 0.4055 0.4746 -0.0059 0.0468  -0.0050 138 ALA   A N   
1065 C  CA  . ALA   A 159 ? 0.3589 0.3524 0.4153 -0.0086 0.0559  0.0051  138 ALA   A CA  
1066 C  C   . ALA   A 159 ? 0.3766 0.3672 0.4368 -0.0113 0.0574  0.0150  138 ALA   A C   
1067 O  O   . ALA   A 159 ? 0.4377 0.4276 0.4909 -0.0115 0.0637  0.0215  138 ALA   A O   
1068 C  CB  . ALA   A 159 ? 0.3164 0.3038 0.3690 -0.0088 0.0569  0.0055  138 ALA   A CB  
1069 N  N   . SER   A 160 ? 0.3927 0.3838 0.4655 -0.0130 0.0510  0.0157  139 SER   A N   
1070 C  CA  . SER   A 160 ? 0.4693 0.4629 0.5486 -0.0162 0.0527  0.0267  139 SER   A CA  
1071 C  C   . SER   A 160 ? 0.3742 0.3735 0.4616 -0.0162 0.0485  0.0236  139 SER   A C   
1072 O  O   . SER   A 160 ? 0.4059 0.4068 0.4951 -0.0133 0.0424  0.0123  139 SER   A O   
1073 C  CB  . SER   A 160 ? 0.4702 0.4596 0.5626 -0.0206 0.0473  0.0359  139 SER   A CB  
1074 O  OG  . SER   A 160 ? 0.5460 0.5294 0.6562 -0.0224 0.0347  0.0308  139 SER   A OG  
1075 N  N   . TRP   A 161 ? 0.4571 0.4625 0.5494 -0.0184 0.0515  0.0331  140 TRP   A N   
1076 C  CA  . TRP   A 161 ? 0.3675 0.3795 0.4685 -0.0186 0.0474  0.0311  140 TRP   A CA  
1077 C  C   . TRP   A 161 ? 0.3852 0.4017 0.5048 -0.0245 0.0442  0.0431  140 TRP   A C   
1078 O  O   . TRP   A 161 ? 0.3975 0.4220 0.5146 -0.0254 0.0523  0.0547  140 TRP   A O   
1079 C  CB  . TRP   A 161 ? 0.3513 0.3705 0.4390 -0.0144 0.0553  0.0309  140 TRP   A CB  
1080 C  CG  . TRP   A 161 ? 0.3695 0.3957 0.4611 -0.0124 0.0498  0.0244  140 TRP   A CG  
1081 C  CD1 . TRP   A 161 ? 0.3560 0.3867 0.4389 -0.0080 0.0478  0.0148  140 TRP   A CD1 
1082 C  CD2 . TRP   A 161 ? 0.3735 0.4067 0.4792 -0.0143 0.0450  0.0273  140 TRP   A CD2 
1083 N  NE1 . TRP   A 161 ? 0.3425 0.3825 0.4313 -0.0060 0.0418  0.0105  140 TRP   A NE1 
1084 C  CE2 . TRP   A 161 ? 0.3517 0.3917 0.4553 -0.0101 0.0395  0.0174  140 TRP   A CE2 
1085 C  CE3 . TRP   A 161 ? 0.3388 0.3765 0.4594 -0.0191 0.0449  0.0381  140 TRP   A CE3 
1086 C  CZ2 . TRP   A 161 ? 0.3166 0.3647 0.4325 -0.0103 0.0328  0.0163  140 TRP   A CZ2 
1087 C  CZ3 . TRP   A 161 ? 0.3490 0.3951 0.4839 -0.0204 0.0387  0.0384  140 TRP   A CZ3 
1088 C  CH2 . TRP   A 161 ? 0.3532 0.4029 0.4857 -0.0160 0.0322  0.0266  140 TRP   A CH2 
1089 N  N   . THR   A 162 ? 0.3714 0.3848 0.5113 -0.0280 0.0316  0.0403  141 THR   A N   
1090 C  CA  . THR   A 162 ? 0.4470 0.4646 0.6106 -0.0358 0.0261  0.0540  141 THR   A CA  
1091 C  C   . THR   A 162 ? 0.4118 0.4339 0.5917 -0.0368 0.0166  0.0486  141 THR   A C   
1092 O  O   . THR   A 162 ? 0.3558 0.3731 0.5350 -0.0320 0.0079  0.0317  141 THR   A O   
1093 C  CB  . THR   A 162 ? 0.4282 0.4344 0.6096 -0.0415 0.0156  0.0593  141 THR   A CB  
1094 O  OG1 . THR   A 162 ? 0.3837 0.3769 0.5715 -0.0379 0.0020  0.0411  141 THR   A OG1 
1095 C  CG2 . THR   A 162 ? 0.3848 0.3894 0.5503 -0.0404 0.0249  0.0663  141 THR   A CG2 
1096 N  N   . TRP   A 163 ? 0.3872 0.4218 0.5817 -0.0424 0.0183  0.0627  142 TRP   A N   
1097 C  CA  . TRP   A 163 ? 0.3941 0.4353 0.6066 -0.0442 0.0092  0.0595  142 TRP   A CA  
1098 C  C   . TRP   A 163 ? 0.3454 0.3761 0.5903 -0.0514 -0.0104 0.0585  142 TRP   A C   
1099 O  O   . TRP   A 163 ? 0.3790 0.3999 0.6364 -0.0571 -0.0157 0.0670  142 TRP   A O   
1100 C  CB  . TRP   A 163 ? 0.4163 0.4777 0.6351 -0.0475 0.0181  0.0759  142 TRP   A CB  
1101 C  CG  . TRP   A 163 ? 0.4072 0.4780 0.5992 -0.0390 0.0336  0.0742  142 TRP   A CG  
1102 C  CD1 . TRP   A 163 ? 0.3560 0.4303 0.5296 -0.0354 0.0466  0.0801  142 TRP   A CD1 
1103 C  CD2 . TRP   A 163 ? 0.3144 0.3915 0.4970 -0.0324 0.0356  0.0658  142 TRP   A CD2 
1104 N  NE1 . TRP   A 163 ? 0.3688 0.4490 0.5244 -0.0270 0.0554  0.0749  142 TRP   A NE1 
1105 C  CE2 . TRP   A 163 ? 0.3610 0.4428 0.5217 -0.0255 0.0492  0.0675  142 TRP   A CE2 
1106 C  CE3 . TRP   A 163 ? 0.3055 0.3851 0.4970 -0.0311 0.0260  0.0565  142 TRP   A CE3 
1107 C  CZ2 . TRP   A 163 ? 0.3476 0.4344 0.4968 -0.0182 0.0530  0.0623  142 TRP   A CZ2 
1108 C  CZ3 . TRP   A 163 ? 0.2799 0.3673 0.4572 -0.0237 0.0311  0.0520  142 TRP   A CZ3 
1109 C  CH2 . TRP   A 163 ? 0.3238 0.4138 0.4810 -0.0177 0.0444  0.0559  142 TRP   A CH2 
1110 N  N   . GLY   A 164 ? 0.3674 0.3997 0.6275 -0.0507 -0.0228 0.0480  143 GLY   A N   
1111 C  CA  . GLY   A 164 ? 0.4212 0.4443 0.7183 -0.0580 -0.0441 0.0471  143 GLY   A CA  
1112 C  C   . GLY   A 164 ? 0.4451 0.4539 0.7445 -0.0497 -0.0614 0.0200  143 GLY   A C   
1113 O  O   . GLY   A 164 ? 0.4137 0.4210 0.6853 -0.0391 -0.0556 0.0042  143 GLY   A O   
1114 N  N   . PRO   A 165 ? 0.4490 0.4493 0.7840 -0.0541 -0.0843 0.0140  144 PRO   A N   
1115 C  CA  . PRO   A 165 ? 0.4827 0.4708 0.8228 -0.0440 -0.1038 -0.0152 144 PRO   A CA  
1116 C  C   . PRO   A 165 ? 0.5717 0.5442 0.9046 -0.0400 -0.1057 -0.0214 144 PRO   A C   
1117 O  O   . PRO   A 165 ? 0.5836 0.5541 0.9041 -0.0269 -0.1127 -0.0473 144 PRO   A O   
1118 C  CB  . PRO   A 165 ? 0.5075 0.4869 0.8948 -0.0520 -0.1299 -0.0161 144 PRO   A CB  
1119 C  CG  . PRO   A 165 ? 0.4673 0.4614 0.8684 -0.0651 -0.1206 0.0113  144 PRO   A CG  
1120 C  CD  . PRO   A 165 ? 0.4404 0.4430 0.8152 -0.0683 -0.0946 0.0335  144 PRO   A CD  
1121 N  N   . GLU   A 166 ? 0.5917 0.5563 0.9317 -0.0500 -0.0996 0.0018  145 GLU   A N   
1122 C  CA  . GLU   A 166 ? 0.6320 0.5829 0.9640 -0.0465 -0.0999 -0.0016 145 GLU   A CA  
1123 C  C   . GLU   A 166 ? 0.5756 0.5365 0.8667 -0.0419 -0.0744 0.0038  145 GLU   A C   
1124 O  O   . GLU   A 166 ? 0.6590 0.6109 0.9412 -0.0394 -0.0723 0.0029  145 GLU   A O   
1125 C  CB  . GLU   A 166 ? 0.6630 0.5992 1.0286 -0.0598 -0.1109 0.0212  145 GLU   A CB  
1126 C  CG  . GLU   A 166 ? 0.7876 0.7149 1.1937 -0.0646 -0.1355 0.0216  145 GLU   A CG  
1127 C  CD  . GLU   A 166 ? 0.9977 0.9121 1.4129 -0.0508 -0.1582 -0.0127 145 GLU   A CD  
1128 O  OE1 . GLU   A 166 ? 1.0485 0.9554 1.4494 -0.0406 -0.1598 -0.0319 145 GLU   A OE1 
1129 O  OE2 . GLU   A 166 ? 0.9741 0.8883 1.4097 -0.0487 -0.1742 -0.0211 145 GLU   A OE2 
1130 N  N   . GLY   A 167 ? 0.4302 0.4087 0.6986 -0.0406 -0.0567 0.0090  146 GLY   A N   
1131 C  CA  . GLY   A 167 ? 0.4106 0.3967 0.6445 -0.0365 -0.0353 0.0134  146 GLY   A CA  
1132 C  C   . GLY   A 167 ? 0.4247 0.4135 0.6342 -0.0241 -0.0329 -0.0088 146 GLY   A C   
1133 O  O   . GLY   A 167 ? 0.4466 0.4370 0.6614 -0.0166 -0.0458 -0.0290 146 GLY   A O   
1134 N  N   . GLN   A 168 ? 0.3826 0.3747 0.5657 -0.0214 -0.0167 -0.0047 147 GLN   A N   
1135 C  CA  . GLN   A 168 ? 0.3875 0.3863 0.5484 -0.0113 -0.0124 -0.0210 147 GLN   A CA  
1136 C  C   . GLN   A 168 ? 0.3814 0.3882 0.5166 -0.0110 0.0068  -0.0112 147 GLN   A C   
1137 O  O   . GLN   A 168 ? 0.3690 0.3739 0.5023 -0.0168 0.0160  0.0050  147 GLN   A O   
1138 C  CB  . GLN   A 168 ? 0.4425 0.4315 0.6070 -0.0072 -0.0206 -0.0319 147 GLN   A CB  
1139 C  CG  . GLN   A 168 ? 0.4630 0.4435 0.6536 -0.0042 -0.0429 -0.0473 147 GLN   A CG  
1140 C  CD  . GLN   A 168 ? 0.5102 0.4858 0.7009 0.0043  -0.0511 -0.0639 147 GLN   A CD  
1141 O  OE1 . GLN   A 168 ? 0.5313 0.5223 0.7048 0.0151  -0.0481 -0.0804 147 GLN   A OE1 
1142 N  NE2 . GLN   A 168 ? 0.6192 0.5759 0.8297 -0.0005 -0.0614 -0.0580 147 GLN   A NE2 
1143 N  N   . GLY   A 169 ? 0.3812 0.3989 0.4981 -0.0036 0.0116  -0.0213 148 GLY   A N   
1144 C  CA  . GLY   A 169 ? 0.3693 0.3937 0.4654 -0.0032 0.0267  -0.0129 148 GLY   A CA  
1145 C  C   . GLY   A 169 ? 0.3319 0.3736 0.4176 0.0025  0.0282  -0.0184 148 GLY   A C   
1146 O  O   . GLY   A 169 ? 0.3739 0.4216 0.4675 0.0037  0.0218  -0.0217 148 GLY   A O   
1147 N  N   . ALA   A 170 ? 0.3785 0.4301 0.4479 0.0058  0.0361  -0.0180 149 ALA   A N   
1148 C  CA  . ALA   A 170 ? 0.4006 0.4734 0.4601 0.0115  0.0370  -0.0211 149 ALA   A CA  
1149 C  C   . ALA   A 170 ? 0.3931 0.4670 0.4496 0.0090  0.0423  -0.0087 149 ALA   A C   
1150 O  O   . ALA   A 170 ? 0.3701 0.4312 0.4271 0.0039  0.0488  0.0027  149 ALA   A O   
1151 C  CB  . ALA   A 170 ? 0.3162 0.4026 0.3624 0.0141  0.0439  -0.0201 149 ALA   A CB  
1152 N  N   . ILE   A 171 ? 0.3359 0.4274 0.3893 0.0140  0.0386  -0.0123 150 ILE   A N   
1153 C  CA  . ILE   A 171 ? 0.3003 0.3946 0.3527 0.0130  0.0414  -0.0020 150 ILE   A CA  
1154 C  C   . ILE   A 171 ? 0.3327 0.4445 0.3707 0.0161  0.0471  0.0063  150 ILE   A C   
1155 O  O   . ILE   A 171 ? 0.3510 0.4833 0.3809 0.0213  0.0460  0.0007  150 ILE   A O   
1156 C  CB  . ILE   A 171 ? 0.3219 0.4218 0.3855 0.0155  0.0310  -0.0103 150 ILE   A CB  
1157 C  CG1 . ILE   A 171 ? 0.2837 0.3664 0.3662 0.0102  0.0246  -0.0138 150 ILE   A CG1 
1158 C  CG2 . ILE   A 171 ? 0.3596 0.4645 0.4220 0.0154  0.0339  0.0004  150 ILE   A CG2 
1159 C  CD1 . ILE   A 171 ? 0.3458 0.4331 0.4449 0.0115  0.0112  -0.0234 150 ILE   A CD1 
1160 N  N   . LEU   A 172 ? 0.3495 0.4553 0.3859 0.0134  0.0524  0.0205  151 LEU   A N   
1161 C  CA  . LEU   A 172 ? 0.3135 0.4308 0.3406 0.0140  0.0571  0.0336  151 LEU   A CA  
1162 C  C   . LEU   A 172 ? 0.3043 0.4262 0.3327 0.0160  0.0551  0.0415  151 LEU   A C   
1163 O  O   . LEU   A 172 ? 0.3226 0.4300 0.3593 0.0147  0.0546  0.0423  151 LEU   A O   
1164 C  CB  . LEU   A 172 ? 0.2765 0.3767 0.3038 0.0084  0.0636  0.0439  151 LEU   A CB  
1165 C  CG  . LEU   A 172 ? 0.3620 0.4694 0.3853 0.0064  0.0669  0.0602  151 LEU   A CG  
1166 C  CD1 . LEU   A 172 ? 0.2991 0.4354 0.3146 0.0085  0.0677  0.0606  151 LEU   A CD1 
1167 C  CD2 . LEU   A 172 ? 0.2871 0.3720 0.3153 0.0011  0.0701  0.0659  151 LEU   A CD2 
1168 N  N   . LEU   A 173 ? 0.3229 0.4679 0.3433 0.0199  0.0540  0.0478  152 LEU   A N   
1169 C  CA  . LEU   A 173 ? 0.3045 0.4555 0.3256 0.0225  0.0514  0.0568  152 LEU   A CA  
1170 C  C   . LEU   A 173 ? 0.3083 0.4493 0.3305 0.0189  0.0553  0.0765  152 LEU   A C   
1171 O  O   . LEU   A 173 ? 0.3460 0.4875 0.3656 0.0151  0.0591  0.0857  152 LEU   A O   
1172 C  CB  . LEU   A 173 ? 0.3761 0.5602 0.3880 0.0297  0.0467  0.0544  152 LEU   A CB  
1173 C  CG  . LEU   A 173 ? 0.4082 0.6055 0.4210 0.0360  0.0385  0.0326  152 LEU   A CG  
1174 C  CD1 . LEU   A 173 ? 0.4076 0.6420 0.4087 0.0451  0.0338  0.0315  152 LEU   A CD1 
1175 C  CD2 . LEU   A 173 ? 0.3309 0.5101 0.3581 0.0343  0.0331  0.0253  152 LEU   A CD2 
1176 N  N   . VAL   A 174 ? 0.3252 0.4570 0.3536 0.0204  0.0529  0.0826  153 VAL   A N   
1177 C  CA  . VAL   A 174 ? 0.3707 0.4956 0.4023 0.0191  0.0526  0.1012  153 VAL   A CA  
1178 C  C   . VAL   A 174 ? 0.3571 0.5108 0.3809 0.0216  0.0502  0.1142  153 VAL   A C   
1179 O  O   . VAL   A 174 ? 0.3527 0.5237 0.3729 0.0273  0.0460  0.1103  153 VAL   A O   
1180 C  CB  . VAL   A 174 ? 0.3644 0.4720 0.4062 0.0221  0.0497  0.1016  153 VAL   A CB  
1181 C  CG1 . VAL   A 174 ? 0.3499 0.4485 0.3978 0.0219  0.0464  0.1199  153 VAL   A CG1 
1182 C  CG2 . VAL   A 174 ? 0.3655 0.4522 0.4135 0.0208  0.0530  0.0898  153 VAL   A CG2 
1183 N  N   . ASN   A 175 ? 0.3186 0.4802 0.3406 0.0172  0.0524  0.1306  154 ASN   A N   
1184 C  CA  . ASN   A 175 ? 0.3368 0.5331 0.3505 0.0190  0.0514  0.1464  154 ASN   A CA  
1185 C  C   . ASN   A 175 ? 0.3733 0.5655 0.3940 0.0196  0.0458  0.1664  154 ASN   A C   
1186 O  O   . ASN   A 175 ? 0.4252 0.6167 0.4528 0.0143  0.0444  0.1900  154 ASN   A O   
1187 C  CB  . ASN   A 175 ? 0.4088 0.6193 0.4204 0.0130  0.0564  0.1585  154 ASN   A CB  
1188 C  CG  . ASN   A 175 ? 0.4347 0.6923 0.4347 0.0164  0.0574  0.1717  154 ASN   A CG  
1189 O  OD1 . ASN   A 175 ? 0.3657 0.6457 0.3565 0.0245  0.0539  0.1676  154 ASN   A OD1 
1190 N  ND2 . ASN   A 175 ? 0.3864 0.6627 0.3869 0.0106  0.0620  0.1877  154 ASN   A ND2 
1191 N  N   . CYS   A 176 ? 0.3604 0.5498 0.3817 0.0261  0.0413  0.1572  155 CYS   A N   
1192 C  CA  . CYS   A 176 ? 0.4366 0.6174 0.4669 0.0283  0.0348  0.1721  155 CYS   A CA  
1193 C  C   . CYS   A 176 ? 0.4084 0.6232 0.4294 0.0344  0.0304  0.1817  155 CYS   A C   
1194 O  O   . CYS   A 176 ? 0.4415 0.6512 0.4691 0.0383  0.0239  0.1901  155 CYS   A O   
1195 C  CB  . CYS   A 176 ? 0.3904 0.5438 0.4309 0.0318  0.0326  0.1566  155 CYS   A CB  
1196 S  SG  . CYS   A 176 ? 0.3988 0.5636 0.4343 0.0372  0.0329  0.1300  155 CYS   A SG  
1197 N  N   . ASP   A 177 ? 0.4248 0.6760 0.4305 0.0369  0.0330  0.1797  156 ASP   A N   
1198 C  CA  . ASP   A 177 ? 0.4836 0.7728 0.4788 0.0432  0.0289  0.1924  156 ASP   A CA  
1199 C  C   . ASP   A 177 ? 0.5445 0.8491 0.5412 0.0370  0.0301  0.2262  156 ASP   A C   
1200 O  O   . ASP   A 177 ? 0.4645 0.7429 0.4748 0.0278  0.0316  0.2391  156 ASP   A O   
1201 C  CB  . ASP   A 177 ? 0.4803 0.8052 0.4588 0.0515  0.0292  0.1710  156 ASP   A CB  
1202 C  CG  . ASP   A 177 ? 0.4513 0.7938 0.4215 0.0492  0.0364  0.1670  156 ASP   A CG  
1203 O  OD1 . ASP   A 177 ? 0.4558 0.7731 0.4349 0.0402  0.0417  0.1722  156 ASP   A OD1 
1204 O  OD2 . ASP   A 177 ? 0.4430 0.8263 0.3980 0.0577  0.0360  0.1572  156 ASP   A OD2 
1205 N  N   . ARG   A 178 ? 0.5827 0.9318 0.5670 0.0419  0.0286  0.2421  157 ARG   A N   
1206 C  CA  . ARG   A 178 ? 0.6344 0.9980 0.6290 0.0347  0.0282  0.2686  157 ARG   A CA  
1207 C  C   . ARG   A 178 ? 0.5936 1.0115 0.5751 0.0406  0.0311  0.2649  157 ARG   A C   
1208 O  O   . ARG   A 178 ? 0.5867 1.0353 0.5572 0.0504  0.0275  0.2622  157 ARG   A O   
1209 C  CB  . ARG   A 178 ? 0.6442 0.9945 0.6531 0.0333  0.0194  0.2903  157 ARG   A CB  
1210 C  CG  . ARG   A 178 ? 0.7326 1.0832 0.7615 0.0225  0.0171  0.3158  157 ARG   A CG  
1211 C  CD  . ARG   A 178 ? 0.8251 1.1539 0.8707 0.0209  0.0068  0.3345  157 ARG   A CD  
1212 N  NE  . ARG   A 178 ? 0.8561 1.2159 0.8901 0.0302  0.0034  0.3378  157 ARG   A NE  
1213 C  CZ  . ARG   A 178 ? 0.8947 1.2409 0.9387 0.0322  -0.0059 0.3503  157 ARG   A CZ  
1214 N  NH1 . ARG   A 178 ? 0.8775 1.1789 0.9439 0.0266  -0.0136 0.3593  157 ARG   A NH1 
1215 N  NH2 . ARG   A 178 ? 0.9308 1.3091 0.9627 0.0410  -0.0084 0.3519  157 ARG   A NH2 
1216 N  N   . GLU   A 179 ? 0.5418 0.9729 0.5261 0.0358  0.0367  0.2643  158 GLU   A N   
1217 C  CA  . GLU   A 179 ? 0.5824 1.0674 0.5564 0.0432  0.0392  0.2592  158 GLU   A CA  
1218 C  C   . GLU   A 179 ? 0.7121 1.2296 0.6958 0.0412  0.0367  0.2866  158 GLU   A C   
1219 O  O   . GLU   A 179 ? 0.7237 1.2907 0.6970 0.0512  0.0369  0.2833  158 GLU   A O   
1220 C  CB  . GLU   A 179 ? 0.4980 0.9873 0.4730 0.0398  0.0450  0.2494  158 GLU   A CB  
1221 C  CG  . GLU   A 179 ? 0.5311 0.9868 0.4994 0.0400  0.0482  0.2244  158 GLU   A CG  
1222 C  CD  . GLU   A 179 ? 0.5434 1.0123 0.4926 0.0535  0.0465  0.1964  158 GLU   A CD  
1223 O  OE1 . GLU   A 179 ? 0.5957 1.1049 0.5351 0.0645  0.0427  0.1919  158 GLU   A OE1 
1224 O  OE2 . GLU   A 179 ? 0.5249 0.9653 0.4704 0.0534  0.0482  0.1783  158 GLU   A OE2 
1225 N  N   . THR   A 180 ? 0.7452 1.2373 0.7501 0.0289  0.0335  0.3129  159 THR   A N   
1226 C  CA  . THR   A 180 ? 0.7950 1.3162 0.8127 0.0251  0.0303  0.3418  159 THR   A CA  
1227 C  C   . THR   A 180 ? 0.7834 1.2704 0.8145 0.0202  0.0222  0.3593  159 THR   A C   
1228 O  O   . THR   A 180 ? 0.8033 1.2392 0.8477 0.0126  0.0187  0.3600  159 THR   A O   
1229 C  CB  . THR   A 180 ? 0.8554 1.3864 0.8913 0.0140  0.0321  0.3600  159 THR   A CB  
1230 O  OG1 . THR   A 180 ? 0.8850 1.3618 0.9365 0.0028  0.0299  0.3610  159 THR   A OG1 
1231 C  CG2 . THR   A 180 ? 0.8349 1.4068 0.8579 0.0209  0.0390  0.3440  159 THR   A CG2 
1232 N  N   . PRO   A 181 ? 0.8551 1.3690 0.8844 0.0250  0.0184  0.3728  160 PRO   A N   
1233 C  CA  . PRO   A 181 ? 0.8963 1.3771 0.9379 0.0220  0.0093  0.3875  160 PRO   A CA  
1234 C  C   . PRO   A 181 ? 0.8763 1.3356 0.9478 0.0078  0.0030  0.4161  160 PRO   A C   
1235 O  O   . PRO   A 181 ? 0.8464 1.2691 0.9318 0.0050  -0.0062 0.4255  160 PRO   A O   
1236 C  CB  . PRO   A 181 ? 0.8979 1.4214 0.9264 0.0324  0.0077  0.3921  160 PRO   A CB  
1237 C  CG  . PRO   A 181 ? 0.8266 1.4093 0.8498 0.0347  0.0147  0.3966  160 PRO   A CG  
1238 C  CD  . PRO   A 181 ? 0.8681 1.4455 0.8850 0.0342  0.0216  0.3753  160 PRO   A CD  
1239 N  N   . TRP   A 182 ? 0.9155 1.3975 0.9989 -0.0005 0.0062  0.4297  161 TRP   A N   
1240 C  CA  . TRP   A 182 ? 0.9306 1.3956 1.0454 -0.0145 -0.0015 0.4577  161 TRP   A CA  
1241 C  C   . TRP   A 182 ? 0.9325 1.3304 1.0631 -0.0206 -0.0092 0.4509  161 TRP   A C   
1242 O  O   . TRP   A 182 ? 0.9819 1.3511 1.1319 -0.0248 -0.0204 0.4654  161 TRP   A O   
1243 C  CB  . TRP   A 182 ? 0.7989 1.2970 0.9232 -0.0218 0.0033  0.4685  161 TRP   A CB  
1244 N  N   . LEU   A 183 ? 0.9488 1.3219 1.0720 -0.0202 -0.0041 0.4279  162 LEU   A N   
1245 C  CA  . LEU   A 183 ? 0.8580 1.1708 0.9950 -0.0239 -0.0110 0.4186  162 LEU   A CA  
1246 C  C   . LEU   A 183 ? 0.8877 1.1762 1.0111 -0.0129 -0.0131 0.4019  162 LEU   A C   
1247 O  O   . LEU   A 183 ? 0.9512 1.2662 1.0499 -0.0028 -0.0064 0.3892  162 LEU   A O   
1248 C  CB  . LEU   A 183 ? 0.8864 1.1831 1.0215 -0.0276 -0.0048 0.4015  162 LEU   A CB  
1249 C  CG  . LEU   A 183 ? 0.9177 1.2348 1.0235 -0.0188 0.0076  0.3767  162 LEU   A CG  
1250 C  CD1 . LEU   A 183 ? 0.9917 1.2777 1.0846 -0.0102 0.0078  0.3553  162 LEU   A CD1 
1251 C  CD2 . LEU   A 183 ? 0.8750 1.1911 0.9825 -0.0247 0.0134  0.3682  162 LEU   A CD2 
1252 N  N   . PRO   A 184 ? 0.8986 1.1383 1.0391 -0.0136 -0.0235 0.4005  163 PRO   A N   
1253 C  CA  . PRO   A 184 ? 0.9258 1.1467 1.0578 -0.0022 -0.0276 0.3888  163 PRO   A CA  
1254 C  C   . PRO   A 184 ? 0.8867 1.0859 1.0050 0.0052  -0.0219 0.3616  163 PRO   A C   
1255 O  O   . PRO   A 184 ? 0.9216 1.1240 1.0262 0.0162  -0.0215 0.3503  163 PRO   A O   
1256 C  CB  . PRO   A 184 ? 0.9321 1.1132 1.0925 -0.0054 -0.0431 0.4002  163 PRO   A CB  
1257 C  CG  . PRO   A 184 ? 0.9154 1.0753 1.0964 -0.0169 -0.0457 0.4032  163 PRO   A CG  
1258 C  CD  . PRO   A 184 ? 0.8305 1.0343 1.0017 -0.0238 -0.0343 0.4110  163 PRO   A CD  
1259 N  N   . LYS   A 185 ? 0.8965 1.0753 1.0200 -0.0006 -0.0181 0.3517  164 LYS   A N   
1260 C  CA  . LYS   A 185 ? 0.8001 0.9548 0.9151 0.0053  -0.0133 0.3282  164 LYS   A CA  
1261 C  C   . LYS   A 185 ? 0.7359 0.9209 0.8268 0.0062  0.0006  0.3152  164 LYS   A C   
1262 O  O   . LYS   A 185 ? 0.7505 0.9712 0.8339 0.0020  0.0060  0.3220  164 LYS   A O   
1263 C  CB  . LYS   A 185 ? 0.8128 0.9233 0.9492 -0.0002 -0.0190 0.3227  164 LYS   A CB  
1264 C  CG  . LYS   A 185 ? 0.8627 0.9426 1.0249 -0.0002 -0.0349 0.3322  164 LYS   A CG  
1265 C  CD  . LYS   A 185 ? 0.9667 1.0049 1.1498 -0.0038 -0.0423 0.3224  164 LYS   A CD  
1266 C  CE  . LYS   A 185 ? 1.0520 1.0597 1.2610 -0.0016 -0.0601 0.3278  164 LYS   A CE  
1267 N  NZ  . LYS   A 185 ? 1.0031 1.0049 1.2080 0.0124  -0.0645 0.3209  164 LYS   A NZ  
1268 N  N   . GLU   A 186 ? 0.6498 0.8212 0.7301 0.0127  0.0056  0.2955  165 GLU   A N   
1269 C  CA  . GLU   A 186 ? 0.6051 0.8010 0.6640 0.0144  0.0172  0.2766  165 GLU   A CA  
1270 C  C   . GLU   A 186 ? 0.5745 0.7749 0.6358 0.0045  0.0233  0.2796  165 GLU   A C   
1271 O  O   . GLU   A 186 ? 0.6138 0.7921 0.6949 -0.0039 0.0181  0.2894  165 GLU   A O   
1272 C  CB  . GLU   A 186 ? 0.6047 0.7776 0.6606 0.0206  0.0199  0.2419  165 GLU   A CB  
1273 C  CG  . GLU   A 186 ? 0.6368 0.7689 0.7069 0.0167  0.0198  0.2311  165 GLU   A CG  
1274 C  CD  . GLU   A 186 ? 0.7598 0.8599 0.8514 0.0178  0.0086  0.2419  165 GLU   A CD  
1275 O  OE1 . GLU   A 186 ? 0.7084 0.8132 0.8037 0.0236  0.0013  0.2516  165 GLU   A OE1 
1276 O  OE2 . GLU   A 186 ? 0.8130 0.8833 0.9187 0.0140  0.0058  0.2394  165 GLU   A OE2 
1277 N  N   . ASP   A 187 ? 0.5174 0.7467 0.5599 0.0065  0.0327  0.2662  166 ASP   A N   
1278 C  CA  . ASP   A 187 ? 0.5031 0.7440 0.5477 -0.0008 0.0375  0.2655  166 ASP   A CA  
1279 C  C   . ASP   A 187 ? 0.5256 0.7264 0.5836 -0.0079 0.0381  0.2591  166 ASP   A C   
1280 O  O   . ASP   A 187 ? 0.5330 0.7299 0.6042 -0.0163 0.0362  0.2674  166 ASP   A O   
1281 C  CB  . ASP   A 187 ? 0.4910 0.7684 0.5137 0.0057  0.0457  0.2476  166 ASP   A CB  
1282 C  CG  . ASP   A 187 ? 0.5336 0.8555 0.5432 0.0141  0.0440  0.2514  166 ASP   A CG  
1283 O  OD1 . ASP   A 187 ? 0.6334 0.9667 0.6526 0.0118  0.0386  0.2728  166 ASP   A OD1 
1284 O  OD2 . ASP   A 187 ? 0.5069 0.8530 0.4978 0.0235  0.0473  0.2318  166 ASP   A OD2 
1285 N  N   . CYS   A 188 ? 0.5484 0.7205 0.6047 -0.0039 0.0395  0.2404  167 CYS   A N   
1286 C  CA  . CYS   A 188 ? 0.5466 0.6843 0.6135 -0.0085 0.0401  0.2283  167 CYS   A CA  
1287 C  C   . CYS   A 188 ? 0.5399 0.6430 0.6304 -0.0131 0.0299  0.2427  167 CYS   A C   
1288 O  O   . CYS   A 188 ? 0.5625 0.6375 0.6632 -0.0163 0.0285  0.2330  167 CYS   A O   
1289 C  CB  . CYS   A 188 ? 0.4528 0.5731 0.5121 -0.0014 0.0432  0.1968  167 CYS   A CB  
1290 S  SG  . CYS   A 188 ? 0.5340 0.6407 0.5966 0.0081  0.0367  0.1898  167 CYS   A SG  
1291 N  N   . ARG   A 189 ? 0.5751 0.6793 0.6758 -0.0127 0.0210  0.2628  168 ARG   A N   
1292 C  CA  . ARG   A 189 ? 0.6278 0.6969 0.7539 -0.0154 0.0079  0.2701  168 ARG   A CA  
1293 C  C   . ARG   A 189 ? 0.6000 0.6673 0.7417 -0.0268 0.0038  0.2788  168 ARG   A C   
1294 O  O   . ARG   A 189 ? 0.6275 0.6619 0.7908 -0.0295 -0.0070 0.2782  168 ARG   A O   
1295 C  CB  . ARG   A 189 ? 0.6570 0.7285 0.7910 -0.0115 -0.0020 0.2849  168 ARG   A CB  
1296 C  CG  . ARG   A 189 ? 0.7111 0.7414 0.8703 -0.0095 -0.0170 0.2848  168 ARG   A CG  
1297 C  CD  . ARG   A 189 ? 0.8479 0.8499 1.0065 0.0022  -0.0172 0.2636  168 ARG   A CD  
1298 N  NE  . ARG   A 189 ? 0.8879 0.9008 1.0367 0.0131  -0.0170 0.2563  168 ARG   A NE  
1299 C  CZ  . ARG   A 189 ? 0.9113 0.9083 1.0753 0.0204  -0.0296 0.2620  168 ARG   A CZ  
1300 N  NH1 . ARG   A 189 ? 0.8822 0.8508 1.0708 0.0182  -0.0440 0.2688  168 ARG   A NH1 
1301 N  NH2 . ARG   A 189 ? 0.9899 1.0013 1.1441 0.0300  -0.0283 0.2549  168 ARG   A NH2 
1302 N  N   . ASP   A 190 ? 0.5699 0.6731 0.7026 -0.0321 0.0111  0.2855  169 ASP   A N   
1303 C  CA  . ASP   A 190 ? 0.5896 0.6974 0.7380 -0.0424 0.0078  0.2958  169 ASP   A CA  
1304 C  C   . ASP   A 190 ? 0.6237 0.7422 0.7594 -0.0441 0.0185  0.2815  169 ASP   A C   
1305 O  O   . ASP   A 190 ? 0.5662 0.6860 0.6825 -0.0379 0.0277  0.2633  169 ASP   A O   
1306 C  CB  . ASP   A 190 ? 0.5656 0.7104 0.7200 -0.0466 0.0052  0.3203  169 ASP   A CB  
1307 C  CG  . ASP   A 190 ? 0.5936 0.7857 0.7227 -0.0407 0.0164  0.3189  169 ASP   A CG  
1308 O  OD1 . ASP   A 190 ? 0.5550 0.7546 0.6645 -0.0361 0.0263  0.2996  169 ASP   A OD1 
1309 O  OD2 . ASP   A 190 ? 0.5982 0.8209 0.7280 -0.0400 0.0143  0.3364  169 ASP   A OD2 
1310 N  N   . GLU   A 191 ? 0.5949 0.7211 0.7435 -0.0527 0.0163  0.2901  170 GLU   A N   
1311 C  CA  . GLU   A 191 ? 0.5070 0.6476 0.6459 -0.0547 0.0252  0.2793  170 GLU   A CA  
1312 C  C   . GLU   A 191 ? 0.5393 0.7294 0.6722 -0.0559 0.0299  0.2925  170 GLU   A C   
1313 O  O   . GLU   A 191 ? 0.5451 0.7495 0.6835 -0.0611 0.0316  0.2956  170 GLU   A O   
1314 C  CB  . GLU   A 191 ? 0.5713 0.6827 0.7299 -0.0623 0.0187  0.2767  170 GLU   A CB  
1315 C  CG  . GLU   A 191 ? 0.5747 0.6394 0.7391 -0.0591 0.0135  0.2605  170 GLU   A CG  
1316 C  CD  . GLU   A 191 ? 0.6764 0.7161 0.8600 -0.0582 -0.0003 0.2697  170 GLU   A CD  
1317 O  OE1 . GLU   A 191 ? 0.7507 0.7778 0.9596 -0.0651 -0.0128 0.2806  170 GLU   A OE1 
1318 O  OE2 . GLU   A 191 ? 0.6646 0.6977 0.8391 -0.0503 0.0004  0.2657  170 GLU   A OE2 
1319 N  N   . LYS   A 192 ? 0.5356 0.7543 0.6579 -0.0502 0.0316  0.3003  171 LYS   A N   
1320 C  CA  . LYS   A 192 ? 0.5610 0.8313 0.6772 -0.0489 0.0353  0.3127  171 LYS   A CA  
1321 C  C   . LYS   A 192 ? 0.5684 0.8669 0.6568 -0.0369 0.0436  0.2968  171 LYS   A C   
1322 O  O   . LYS   A 192 ? 0.5581 0.8393 0.6357 -0.0307 0.0443  0.2850  171 LYS   A O   
1323 C  CB  . LYS   A 192 ? 0.5409 0.8271 0.6756 -0.0536 0.0267  0.3417  171 LYS   A CB  
1324 C  CG  . LYS   A 192 ? 0.6446 0.9299 0.8079 -0.0656 0.0190  0.3627  171 LYS   A CG  
1325 C  CD  . LYS   A 192 ? 0.6738 0.9045 0.8575 -0.0721 0.0096  0.3582  171 LYS   A CD  
1326 C  CE  . LYS   A 192 ? 0.7345 0.9649 0.9467 -0.0838 0.0015  0.3753  171 LYS   A CE  
1327 N  NZ  . LYS   A 192 ? 0.7867 1.0472 1.0194 -0.0900 -0.0059 0.4071  171 LYS   A NZ  
1328 N  N   . VAL   A 193 ? 0.5572 0.9006 0.6353 -0.0329 0.0489  0.2959  172 VAL   A N   
1329 C  CA  . VAL   A 193 ? 0.5089 0.8895 0.5641 -0.0204 0.0538  0.2834  172 VAL   A CA  
1330 C  C   . VAL   A 193 ? 0.5810 1.0137 0.6400 -0.0191 0.0523  0.3045  172 VAL   A C   
1331 O  O   . VAL   A 193 ? 0.6523 1.1095 0.7197 -0.0231 0.0533  0.3144  172 VAL   A O   
1332 C  CB  . VAL   A 193 ? 0.5253 0.9135 0.5633 -0.0136 0.0608  0.2562  172 VAL   A CB  
1333 C  CG1 . VAL   A 193 ? 0.4756 0.9098 0.4936 0.0003  0.0630  0.2440  172 VAL   A CG1 
1334 C  CG2 . VAL   A 193 ? 0.4669 0.8087 0.5007 -0.0140 0.0627  0.2361  172 VAL   A CG2 
1335 N  N   . TYR   A 194 ? 0.5296 0.9815 0.5837 -0.0133 0.0499  0.3125  173 TYR   A N   
1336 C  CA  . TYR   A 194 ? 0.5962 1.1006 0.6551 -0.0117 0.0485  0.3342  173 TYR   A CA  
1337 C  C   . TYR   A 194 ? 0.6321 1.1887 0.6689 0.0034  0.0530  0.3184  173 TYR   A C   
1338 O  O   . TYR   A 194 ? 0.7965 1.4046 0.8361 0.0061  0.0538  0.3311  173 TYR   A O   
1339 C  CB  . TYR   A 194 ? 0.6879 1.1851 0.7584 -0.0150 0.0419  0.3560  173 TYR   A CB  
1340 C  CG  . TYR   A 194 ? 0.7109 1.1598 0.8071 -0.0287 0.0346  0.3722  173 TYR   A CG  
1341 C  CD1 . TYR   A 194 ? 0.6804 1.1377 0.8015 -0.0401 0.0300  0.3970  173 TYR   A CD1 
1342 C  CD2 . TYR   A 194 ? 0.6697 1.0665 0.7669 -0.0295 0.0309  0.3622  173 TYR   A CD2 
1343 C  CE1 . TYR   A 194 ? 0.6795 1.0925 0.8265 -0.0517 0.0210  0.4094  173 TYR   A CE1 
1344 C  CE2 . TYR   A 194 ? 0.6680 1.0215 0.7900 -0.0400 0.0223  0.3740  173 TYR   A CE2 
1345 C  CZ  . TYR   A 194 ? 0.7600 1.1208 0.9070 -0.0510 0.0168  0.3966  173 TYR   A CZ  
1346 O  OH  . TYR   A 194 ? 0.7779 1.0958 0.9516 -0.0607 0.0061  0.4061  173 TYR   A OH  
1347 N  N   . SER   A 195 ? 0.5877 1.1345 0.6044 0.0139  0.0549  0.2907  174 SER   A N   
1348 C  CA  . SER   A 195 ? 0.5974 1.1908 0.5946 0.0300  0.0565  0.2711  174 SER   A CA  
1349 C  C   . SER   A 195 ? 0.5758 1.1560 0.5598 0.0361  0.0595  0.2386  174 SER   A C   
1350 O  O   . SER   A 195 ? 0.5637 1.0956 0.5467 0.0316  0.0604  0.2263  174 SER   A O   
1351 C  CB  . SER   A 195 ? 0.6122 1.2119 0.5987 0.0388  0.0534  0.2667  174 SER   A CB  
1352 O  OG  . SER   A 195 ? 0.7785 1.4286 0.7490 0.0553  0.0532  0.2485  174 SER   A OG  
1353 N  N   . LYS   A 196 ? 0.4734 1.0983 0.4488 0.0470  0.0606  0.2248  175 LYS   A N   
1354 C  CA  . LYS   A 196 ? 0.5577 1.1724 0.5219 0.0542  0.0618  0.1924  175 LYS   A CA  
1355 C  C   . LYS   A 196 ? 0.5365 1.1376 0.4865 0.0647  0.0587  0.1655  175 LYS   A C   
1356 O  O   . LYS   A 196 ? 0.5217 1.1005 0.4659 0.0680  0.0588  0.1395  175 LYS   A O   
1357 C  CB  . LYS   A 196 ? 0.5499 1.2176 0.5099 0.0651  0.0617  0.1831  175 LYS   A CB  
1358 C  CG  . LYS   A 196 ? 0.5020 1.2216 0.4501 0.0838  0.0573  0.1679  175 LYS   A CG  
1359 C  CD  . LYS   A 196 ? 0.4678 1.2384 0.4132 0.0959  0.0563  0.1554  175 LYS   A CD  
1360 C  CE  . LYS   A 196 ? 0.7089 1.5274 0.6432 0.1176  0.0502  0.1314  175 LYS   A CE  
1361 N  NZ  . LYS   A 196 ? 0.5651 1.4235 0.5004 0.1214  0.0497  0.1519  175 LYS   A NZ  
1362 N  N   . GLU   A 197 ? 0.5444 1.1594 0.4900 0.0699  0.0554  0.1714  176 GLU   A N   
1363 C  CA  . GLU   A 197 ? 0.5160 1.1134 0.4503 0.0777  0.0517  0.1488  176 GLU   A CA  
1364 C  C   . GLU   A 197 ? 0.5190 1.0566 0.4580 0.0660  0.0541  0.1501  176 GLU   A C   
1365 O  O   . GLU   A 197 ? 0.4715 0.9901 0.4029 0.0712  0.0522  0.1272  176 GLU   A O   
1366 C  CB  . GLU   A 197 ? 0.6703 1.2948 0.6004 0.0847  0.0476  0.1582  176 GLU   A CB  
1367 C  CG  . GLU   A 197 ? 0.7744 1.4014 0.6910 0.0985  0.0413  0.1287  176 GLU   A CG  
1368 C  CD  . GLU   A 197 ? 0.8909 1.5433 0.8004 0.1134  0.0371  0.0939  176 GLU   A CD  
1369 O  OE1 . GLU   A 197 ? 0.8594 1.5474 0.7716 0.1175  0.0386  0.0957  176 GLU   A OE1 
1370 O  OE2 . GLU   A 197 ? 0.9330 1.5700 0.8361 0.1213  0.0309  0.0643  176 GLU   A OE2 
1371 N  N   . ASP   A 198 ? 0.5076 1.0172 0.4611 0.0509  0.0575  0.1757  177 ASP   A N   
1372 C  CA  . ASP   A 198 ? 0.4807 0.9358 0.4414 0.0407  0.0597  0.1764  177 ASP   A CA  
1373 C  C   . ASP   A 198 ? 0.4803 0.9166 0.4379 0.0414  0.0632  0.1514  177 ASP   A C   
1374 O  O   . ASP   A 198 ? 0.4223 0.8228 0.3814 0.0384  0.0650  0.1417  177 ASP   A O   
1375 C  CB  . ASP   A 198 ? 0.4652 0.8972 0.4449 0.0260  0.0601  0.2055  177 ASP   A CB  
1376 C  CG  . ASP   A 198 ? 0.4959 0.8757 0.4850 0.0178  0.0595  0.2100  177 ASP   A CG  
1377 O  OD1 . ASP   A 198 ? 0.4536 0.8199 0.4341 0.0233  0.0595  0.1959  177 ASP   A OD1 
1378 O  OD2 . ASP   A 198 ? 0.4595 0.8135 0.4658 0.0067  0.0583  0.2270  177 ASP   A OD2 
1379 N  N   . LEU   A 199 ? 0.4304 0.8925 0.3853 0.0458  0.0641  0.1412  178 LEU   A N   
1380 C  CA  . LEU   A 199 ? 0.3720 0.8170 0.3261 0.0466  0.0666  0.1181  178 LEU   A CA  
1381 C  C   . LEU   A 199 ? 0.3826 0.8260 0.3268 0.0581  0.0633  0.0873  178 LEU   A C   
1382 O  O   . LEU   A 199 ? 0.4404 0.8577 0.3879 0.0568  0.0652  0.0699  178 LEU   A O   
1383 C  CB  . LEU   A 199 ? 0.3849 0.8621 0.3389 0.0503  0.0669  0.1146  178 LEU   A CB  
1384 C  CG  . LEU   A 199 ? 0.4753 0.9602 0.4415 0.0393  0.0694  0.1443  178 LEU   A CG  
1385 C  CD1 . LEU   A 199 ? 0.4480 0.9673 0.4138 0.0439  0.0701  0.1390  178 LEU   A CD1 
1386 C  CD2 . LEU   A 199 ? 0.4372 0.8720 0.4171 0.0238  0.0724  0.1574  178 LEU   A CD2 
1387 N  N   . LYS   A 200 ? 0.4629 0.9349 0.3972 0.0696  0.0574  0.0796  179 LYS   A N   
1388 C  CA  . LYS   A 200 ? 0.4156 0.8861 0.3430 0.0810  0.0516  0.0485  179 LYS   A CA  
1389 C  C   . LYS   A 200 ? 0.4749 0.8898 0.4154 0.0715  0.0494  0.0470  179 LYS   A C   
1390 O  O   . LYS   A 200 ? 0.4012 0.7925 0.3488 0.0749  0.0415  0.0211  179 LYS   A O   
1391 C  CB  . LYS   A 200 ? 0.4468 0.9561 0.3637 0.0947  0.0430  0.0415  179 LYS   A CB  
1392 N  N   . ASP   A 201 ? 0.4178 0.8094 0.3651 0.0597  0.0541  0.0741  180 ASP   A N   
1393 C  CA  . ASP   A 201 ? 0.4070 0.7473 0.3682 0.0514  0.0518  0.0734  180 ASP   A CA  
1394 C  C   . ASP   A 201 ? 0.4114 0.7149 0.3832 0.0423  0.0562  0.0696  180 ASP   A C   
1395 O  O   . ASP   A 201 ? 0.4225 0.6878 0.4049 0.0376  0.0541  0.0636  180 ASP   A O   
1396 C  CB  . ASP   A 201 ? 0.4175 0.7483 0.3828 0.0448  0.0532  0.1015  180 ASP   A CB  
1397 C  CG  . ASP   A 201 ? 0.3873 0.7467 0.3440 0.0533  0.0474  0.1053  180 ASP   A CG  
1398 O  OD1 . ASP   A 201 ? 0.4208 0.7952 0.3720 0.0636  0.0403  0.0816  180 ASP   A OD1 
1399 O  OD2 . ASP   A 201 ? 0.4544 0.8205 0.4116 0.0498  0.0483  0.1321  180 ASP   A OD2 
1400 N  N   . MET   A 202 ? 0.3502 0.6673 0.3197 0.0401  0.0622  0.0736  181 MET   A N   
1401 C  CA  . MET   A 202 ? 0.3408 0.6254 0.3199 0.0312  0.0664  0.0735  181 MET   A CA  
1402 C  C   . MET   A 202 ? 0.3330 0.6133 0.3127 0.0365  0.0633  0.0462  181 MET   A C   
1403 O  O   . MET   A 202 ? 0.4101 0.7188 0.3827 0.0477  0.0584  0.0284  181 MET   A O   
1404 C  CB  . MET   A 202 ? 0.3365 0.6364 0.3169 0.0239  0.0738  0.0968  181 MET   A CB  
1405 C  CG  . MET   A 202 ? 0.2863 0.5865 0.2708 0.0174  0.0745  0.1263  181 MET   A CG  
1406 S  SD  . MET   A 202 ? 0.3974 0.7014 0.3927 0.0068  0.0754  0.1507  181 MET   A SD  
1407 C  CE  . MET   A 202 ? 0.4044 0.7111 0.4062 0.0034  0.0701  0.1789  181 MET   A CE  
1408 N  N   . SER   A 203 ? 0.3435 0.5878 0.3328 0.0294  0.0648  0.0424  182 SER   A N   
1409 C  CA  . SER   A 203 ? 0.4049 0.6409 0.3975 0.0329  0.0614  0.0203  182 SER   A CA  
1410 C  C   . SER   A 203 ? 0.3558 0.6100 0.3458 0.0324  0.0671  0.0229  182 SER   A C   
1411 O  O   . SER   A 203 ? 0.3492 0.6015 0.3414 0.0238  0.0741  0.0431  182 SER   A O   
1412 C  CB  . SER   A 203 ? 0.3256 0.5176 0.3294 0.0259  0.0599  0.0165  182 SER   A CB  
1413 O  OG  . SER   A 203 ? 0.3604 0.5397 0.3685 0.0260  0.0552  0.0155  182 SER   A OG  
1414 N  N   . GLN   A 204 ? 0.4083 0.6810 0.3961 0.0419  0.0629  0.0019  183 GLN   A N   
1415 C  CA  . GLN   A 204 ? 0.3741 0.6691 0.3602 0.0434  0.0679  0.0018  183 GLN   A CA  
1416 C  C   . GLN   A 204 ? 0.3757 0.6354 0.3717 0.0366  0.0683  -0.0030 183 GLN   A C   
1417 O  O   . GLN   A 204 ? 0.3596 0.5892 0.3625 0.0372  0.0613  -0.0174 183 GLN   A O   
1418 C  CB  . GLN   A 204 ? 0.3537 0.6889 0.3328 0.0596  0.0624  -0.0209 183 GLN   A CB  
1419 C  CG  . GLN   A 204 ? 0.4129 0.7943 0.3794 0.0674  0.0633  -0.0139 183 GLN   A CG  
1420 C  CD  . GLN   A 204 ? 0.4953 0.9087 0.4561 0.0844  0.0526  -0.0397 183 GLN   A CD  
1421 O  OE1 . GLN   A 204 ? 0.4624 0.8777 0.4273 0.0900  0.0485  -0.0565 183 GLN   A OE1 
1422 N  NE2 . GLN   A 204 ? 0.5386 0.9778 0.4910 0.0936  0.0465  -0.0439 183 GLN   A NE2 
1423 N  N   . MET   A 205 ? 0.3839 0.6491 0.3819 0.0298  0.0758  0.0110  184 MET   A N   
1424 C  CA  . MET   A 205 ? 0.3516 0.5895 0.3579 0.0240  0.0765  0.0078  184 MET   A CA  
1425 C  C   . MET   A 205 ? 0.3668 0.6384 0.3729 0.0268  0.0810  0.0081  184 MET   A C   
1426 O  O   . MET   A 205 ? 0.4277 0.7242 0.4329 0.0220  0.0871  0.0278  184 MET   A O   
1427 C  CB  . MET   A 205 ? 0.3220 0.5264 0.3343 0.0111  0.0802  0.0264  184 MET   A CB  
1428 C  CG  . MET   A 205 ? 0.3602 0.5381 0.3798 0.0057  0.0806  0.0234  184 MET   A CG  
1429 S  SD  . MET   A 205 ? 0.3854 0.5289 0.4117 -0.0063 0.0828  0.0417  184 MET   A SD  
1430 C  CE  . MET   A 205 ? 0.3528 0.5247 0.3828 -0.0126 0.0876  0.0660  184 MET   A CE  
1431 N  N   . ILE   A 206 ? 0.3367 0.6088 0.3453 0.0344  0.0763  -0.0128 185 ILE   A N   
1432 C  CA  . ILE   A 206 ? 0.3316 0.6413 0.3403 0.0404  0.0795  -0.0172 185 ILE   A CA  
1433 C  C   . ILE   A 206 ? 0.3315 0.6165 0.3498 0.0332  0.0805  -0.0165 185 ILE   A C   
1434 O  O   . ILE   A 206 ? 0.3804 0.6298 0.4034 0.0336  0.0738  -0.0296 185 ILE   A O   
1435 C  CB  . ILE   A 206 ? 0.3419 0.6731 0.3465 0.0576  0.0697  -0.0448 185 ILE   A CB  
1436 C  CG1 . ILE   A 206 ? 0.3876 0.7367 0.3827 0.0648  0.0653  -0.0477 185 ILE   A CG1 
1437 C  CG2 . ILE   A 206 ? 0.4010 0.7620 0.4046 0.0625  0.0683  -0.0468 185 ILE   A CG2 
1438 C  CD1 . ILE   A 206 ? 0.3736 0.7437 0.3660 0.0824  0.0526  -0.0761 185 ILE   A CD1 
1439 N  N   . LEU   A 207 ? 0.3889 0.6906 0.4111 0.0260  0.0870  0.0003  186 LEU   A N   
1440 C  CA  . LEU   A 207 ? 0.3883 0.6799 0.4202 0.0214  0.0886  -0.0008 186 LEU   A CA  
1441 C  C   . LEU   A 207 ? 0.3105 0.6293 0.3416 0.0335  0.0842  -0.0183 186 LEU   A C   
1442 O  O   . LEU   A 207 ? 0.3334 0.6838 0.3617 0.0350  0.0847  -0.0105 186 LEU   A O   
1443 C  CB  . LEU   A 207 ? 0.3531 0.6415 0.3929 0.0067  0.0936  0.0252  186 LEU   A CB  
1444 C  CG  . LEU   A 207 ? 0.3137 0.5942 0.3653 0.0013  0.0948  0.0248  186 LEU   A CG  
1445 C  CD1 . LEU   A 207 ? 0.2696 0.4999 0.3209 0.0009  0.0882  0.0115  186 LEU   A CD1 
1446 C  CD2 . LEU   A 207 ? 0.3154 0.5919 0.3779 -0.0133 0.0970  0.0497  186 LEU   A CD2 
1447 N  N   . ARG   A 208 ? 0.3111 0.6177 0.3459 0.0427  0.0783  -0.0420 187 ARG   A N   
1448 C  CA  . ARG   A 208 ? 0.3405 0.6669 0.3762 0.0556  0.0710  -0.0615 187 ARG   A CA  
1449 C  C   . ARG   A 208 ? 0.3678 0.6886 0.4139 0.0515  0.0731  -0.0606 187 ARG   A C   
1450 O  O   . ARG   A 208 ? 0.3507 0.6332 0.4028 0.0445  0.0716  -0.0598 187 ARG   A O   
1451 C  CB  . ARG   A 208 ? 0.3663 0.6796 0.4031 0.0695  0.0590  -0.0895 187 ARG   A CB  
1452 C  CG  . ARG   A 208 ? 0.3577 0.6793 0.3858 0.0752  0.0549  -0.0940 187 ARG   A CG  
1453 C  CD  . ARG   A 208 ? 0.4212 0.7365 0.4537 0.0906  0.0388  -0.1240 187 ARG   A CD  
1454 N  NE  . ARG   A 208 ? 0.4294 0.7623 0.4538 0.0983  0.0329  -0.1309 187 ARG   A NE  
1455 C  CZ  . ARG   A 208 ? 0.4667 0.7801 0.4927 0.0981  0.0296  -0.1354 187 ARG   A CZ  
1456 N  NH1 . ARG   A 208 ? 0.3826 0.6487 0.4171 0.0863  0.0285  -0.1276 187 ARG   A NH1 
1457 N  NH2 . ARG   A 208 ? 0.4791 0.8128 0.4977 0.1061  0.0233  -0.1425 187 ARG   A NH2 
1458 N  N   . THR   A 209 ? 0.3503 0.7016 0.3969 0.0543  0.0734  -0.0585 188 THR   A N   
1459 C  CA  . THR   A 209 ? 0.3534 0.7048 0.4108 0.0506  0.0752  -0.0570 188 THR   A CA  
1460 C  C   . THR   A 209 ? 0.3785 0.7596 0.4355 0.0641  0.0686  -0.0732 188 THR   A C   
1461 O  O   . THR   A 209 ? 0.3579 0.7691 0.4059 0.0728  0.0653  -0.0776 188 THR   A O   
1462 C  CB  . THR   A 209 ? 0.3774 0.7357 0.4408 0.0343  0.0844  -0.0287 188 THR   A CB  
1463 O  OG1 . THR   A 209 ? 0.4220 0.8174 0.4802 0.0350  0.0862  -0.0168 188 THR   A OG1 
1464 C  CG2 . THR   A 209 ? 0.3926 0.7223 0.4564 0.0214  0.0890  -0.0126 188 THR   A CG2 
1465 N  N   A LYS   A 210 ? 0.3882 0.7621 0.4553 0.0663  0.0657  -0.0826 189 LYS   A N   
1466 N  N   B LYS   A 210 ? 0.3882 0.7623 0.4553 0.0662  0.0658  -0.0824 189 LYS   A N   
1467 C  CA  A LYS   A 210 ? 0.3744 0.7760 0.4432 0.0780  0.0596  -0.0966 189 LYS   A CA  
1468 C  CA  B LYS   A 210 ? 0.3732 0.7751 0.4419 0.0781  0.0596  -0.0966 189 LYS   A CA  
1469 C  C   A LYS   A 210 ? 0.3574 0.7587 0.4389 0.0708  0.0637  -0.0891 189 LYS   A C   
1470 C  C   B LYS   A 210 ? 0.3567 0.7581 0.4382 0.0712  0.0634  -0.0898 189 LYS   A C   
1471 O  O   A LYS   A 210 ? 0.3649 0.7348 0.4552 0.0653  0.0638  -0.0898 189 LYS   A O   
1472 O  O   B LYS   A 210 ? 0.3530 0.7227 0.4432 0.0664  0.0629  -0.0917 189 LYS   A O   
1473 C  CB  A LYS   A 210 ? 0.3854 0.7733 0.4548 0.0945  0.0445  -0.1265 189 LYS   A CB  
1474 C  CB  B LYS   A 210 ? 0.3858 0.7742 0.4548 0.0946  0.0445  -0.1265 189 LYS   A CB  
1475 N  N   . GLY   A 211 ? 0.3562 0.7947 0.4394 0.0709  0.0668  -0.0818 190 GLY   A N   
1476 C  CA  . GLY   A 211 ? 0.3511 0.7942 0.4481 0.0640  0.0703  -0.0741 190 GLY   A CA  
1477 C  C   . GLY   A 211 ? 0.3622 0.8517 0.4604 0.0636  0.0743  -0.0631 190 GLY   A C   
1478 O  O   . GLY   A 211 ? 0.3438 0.8651 0.4307 0.0715  0.0733  -0.0645 190 GLY   A O   
1479 N  N   . PRO   A 212 ? 0.3995 0.8959 0.5124 0.0545  0.0782  -0.0518 191 PRO   A N   
1480 C  CA  . PRO   A 212 ? 0.4324 0.9742 0.5494 0.0539  0.0817  -0.0409 191 PRO   A CA  
1481 C  C   . PRO   A 212 ? 0.3497 0.9093 0.4656 0.0408  0.0892  -0.0117 191 PRO   A C   
1482 O  O   . PRO   A 212 ? 0.3268 0.8635 0.4380 0.0331  0.0913  -0.0013 191 PRO   A O   
1483 C  CB  . PRO   A 212 ? 0.3912 0.9269 0.5277 0.0468  0.0822  -0.0381 191 PRO   A CB  
1484 C  CG  . PRO   A 212 ? 0.3781 0.8686 0.5217 0.0359  0.0825  -0.0342 191 PRO   A CG  
1485 C  CD  . PRO   A 212 ? 0.3443 0.8091 0.4722 0.0447  0.0786  -0.0491 191 PRO   A CD  
1486 N  N   . ASP   A 213 ? 0.3787 0.9808 0.5000 0.0386  0.0925  0.0021  192 ASP   A N   
1487 C  CA  . ASP   A 213 ? 0.4454 1.0704 0.5664 0.0279  0.0976  0.0305  192 ASP   A CA  
1488 C  C   . ASP   A 213 ? 0.4386 1.0271 0.5727 0.0077  0.1004  0.0532  192 ASP   A C   
1489 O  O   . ASP   A 213 ? 0.4810 1.0675 0.6106 0.0006  0.1020  0.0712  192 ASP   A O   
1490 C  CB  . ASP   A 213 ? 0.4610 1.1364 0.5902 0.0271  0.1002  0.0436  192 ASP   A CB  
1491 C  CG  . ASP   A 213 ? 0.6564 1.3745 0.7712 0.0480  0.0966  0.0223  192 ASP   A CG  
1492 O  OD1 . ASP   A 213 ? 0.6605 1.3770 0.7576 0.0617  0.0918  0.0040  192 ASP   A OD1 
1493 O  OD2 . ASP   A 213 ? 0.7501 1.5042 0.8724 0.0512  0.0975  0.0231  192 ASP   A OD2 
1494 N  N   . ARG   A 214 ? 0.4296 0.9900 0.5806 -0.0012 0.0997  0.0522  193 ARG   A N   
1495 C  CA  . ARG   A 214 ? 0.4631 0.9900 0.6291 -0.0201 0.0999  0.0716  193 ARG   A CA  
1496 C  C   . ARG   A 214 ? 0.4183 0.9041 0.5895 -0.0206 0.0968  0.0553  193 ARG   A C   
1497 O  O   . ARG   A 214 ? 0.3537 0.8408 0.5238 -0.0093 0.0944  0.0336  193 ARG   A O   
1498 C  CB  . ARG   A 214 ? 0.4716 1.0158 0.6607 -0.0349 0.1002  0.0951  193 ARG   A CB  
1499 C  CG  . ARG   A 214 ? 0.5859 1.1805 0.7718 -0.0327 0.1031  0.1110  193 ARG   A CG  
1500 C  CD  . ARG   A 214 ? 0.6635 1.2799 0.8740 -0.0449 0.1029  0.1302  193 ARG   A CD  
1501 N  NE  . ARG   A 214 ? 0.7000 1.3735 0.9052 -0.0355 0.1061  0.1328  193 ARG   A NE  
1502 C  CZ  . ARG   A 214 ? 0.7372 1.4475 0.9340 -0.0343 0.1081  0.1508  193 ARG   A CZ  
1503 N  NH1 . ARG   A 214 ? 0.7320 1.4271 0.9255 -0.0421 0.1071  0.1685  193 ARG   A NH1 
1504 N  NH2 . ARG   A 214 ? 0.8291 1.5949 1.0209 -0.0243 0.1105  0.1510  193 ARG   A NH2 
1505 N  N   . LEU   A 215 ? 0.4120 0.8620 0.5887 -0.0332 0.0957  0.0661  194 LEU   A N   
1506 C  CA  . LEU   A 215 ? 0.3717 0.7880 0.5581 -0.0374 0.0920  0.0565  194 LEU   A CA  
1507 C  C   . LEU   A 215 ? 0.4101 0.8332 0.6215 -0.0475 0.0886  0.0637  194 LEU   A C   
1508 O  O   . LEU   A 215 ? 0.4023 0.8407 0.6270 -0.0583 0.0886  0.0841  194 LEU   A O   
1509 C  CB  . LEU   A 215 ? 0.3554 0.7339 0.5414 -0.0481 0.0905  0.0667  194 LEU   A CB  
1510 C  CG  . LEU   A 215 ? 0.3985 0.7653 0.5618 -0.0393 0.0931  0.0591  194 LEU   A CG  
1511 C  CD1 . LEU   A 215 ? 0.3726 0.7054 0.5380 -0.0512 0.0914  0.0735  194 LEU   A CD1 
1512 C  CD2 . LEU   A 215 ? 0.3284 0.6863 0.4812 -0.0253 0.0921  0.0324  194 LEU   A CD2 
1513 N  N   . PRO   A 216 ? 0.3799 0.7933 0.5993 -0.0442 0.0846  0.0475  195 PRO   A N   
1514 C  CA  . PRO   A 216 ? 0.3489 0.7661 0.5941 -0.0549 0.0794  0.0539  195 PRO   A CA  
1515 C  C   . PRO   A 216 ? 0.3743 0.7664 0.6366 -0.0744 0.0744  0.0757  195 PRO   A C   
1516 O  O   . PRO   A 216 ? 0.3645 0.7292 0.6188 -0.0788 0.0739  0.0818  195 PRO   A O   
1517 C  CB  . PRO   A 216 ? 0.3893 0.7792 0.6298 -0.0462 0.0723  0.0299  195 PRO   A CB  
1518 C  CG  . PRO   A 216 ? 0.3833 0.7696 0.5981 -0.0281 0.0749  0.0100  195 PRO   A CG  
1519 C  CD  . PRO   A 216 ? 0.3594 0.7516 0.5638 -0.0309 0.0821  0.0224  195 PRO   A CD  
1520 N  N   . ALA   A 217 ? 0.3312 0.7310 0.6181 -0.0855 0.0690  0.0863  196 ALA   A N   
1521 C  CA  . ALA   A 217 ? 0.2734 0.6447 0.5792 -0.1030 0.0602  0.1039  196 ALA   A CA  
1522 C  C   . ALA   A 217 ? 0.3853 0.7111 0.6914 -0.1058 0.0522  0.0953  196 ALA   A C   
1523 O  O   . ALA   A 217 ? 0.3362 0.6378 0.6272 -0.0946 0.0479  0.0716  196 ALA   A O   
1524 C  CB  . ALA   A 217 ? 0.3073 0.6908 0.6413 -0.1129 0.0530  0.1110  196 ALA   A CB  
1525 N  N   . GLY   A 218 ? 0.3016 0.5964 0.6080 -0.1141 0.0477  0.1072  197 GLY   A N   
1526 C  CA  . GLY   A 218 ? 0.2800 0.5208 0.5802 -0.1136 0.0375  0.0956  197 GLY   A CA  
1527 C  C   . GLY   A 218 ? 0.3715 0.5882 0.6373 -0.1009 0.0431  0.0826  197 GLY   A C   
1528 O  O   . GLY   A 218 ? 0.4328 0.6059 0.6858 -0.0960 0.0357  0.0680  197 GLY   A O   
1529 N  N   . TYR   A 219 ? 0.3500 0.5958 0.6010 -0.0949 0.0553  0.0870  198 TYR   A N   
1530 C  CA  . TYR   A 219 ? 0.3235 0.5484 0.5450 -0.0838 0.0598  0.0757  198 TYR   A CA  
1531 C  C   . TYR   A 219 ? 0.3301 0.5722 0.5513 -0.0888 0.0665  0.0955  198 TYR   A C   
1532 O  O   . TYR   A 219 ? 0.3311 0.6075 0.5620 -0.0939 0.0701  0.1121  198 TYR   A O   
1533 C  CB  . TYR   A 219 ? 0.3424 0.5815 0.5428 -0.0677 0.0657  0.0554  198 TYR   A CB  
1534 C  CG  . TYR   A 219 ? 0.3477 0.5664 0.5449 -0.0609 0.0586  0.0357  198 TYR   A CG  
1535 C  CD1 . TYR   A 219 ? 0.3717 0.5474 0.5511 -0.0544 0.0532  0.0212  198 TYR   A CD1 
1536 C  CD2 . TYR   A 219 ? 0.3352 0.5810 0.5474 -0.0607 0.0574  0.0330  198 TYR   A CD2 
1537 C  CE1 . TYR   A 219 ? 0.3817 0.5419 0.5575 -0.0481 0.0466  0.0057  198 TYR   A CE1 
1538 C  CE2 . TYR   A 219 ? 0.4124 0.6403 0.6215 -0.0541 0.0502  0.0159  198 TYR   A CE2 
1539 C  CZ  . TYR   A 219 ? 0.4138 0.5988 0.6043 -0.0479 0.0447  0.0030  198 TYR   A CZ  
1540 O  OH  . TYR   A 219 ? 0.4620 0.6325 0.6492 -0.0413 0.0373  -0.0116 198 TYR   A OH  
1541 N  N   . GLU   A 220 ? 0.3694 0.5810 0.5723 -0.0842 0.0662  0.0905  199 GLU   A N   
1542 C  CA  . GLU   A 220 ? 0.3737 0.6000 0.5711 -0.0858 0.0725  0.1059  199 GLU   A CA  
1543 C  C   . GLU   A 220 ? 0.3106 0.5092 0.4809 -0.0743 0.0740  0.0897  199 GLU   A C   
1544 O  O   . GLU   A 220 ? 0.3603 0.5210 0.5213 -0.0695 0.0683  0.0734  199 GLU   A O   
1545 C  CB  . GLU   A 220 ? 0.4077 0.6170 0.6216 -0.0984 0.0645  0.1262  199 GLU   A CB  
1546 C  CG  . GLU   A 220 ? 0.4507 0.6121 0.6706 -0.1020 0.0552  0.1227  199 GLU   A CG  
1547 C  CD  . GLU   A 220 ? 0.5089 0.6529 0.7446 -0.1114 0.0445  0.1397  199 GLU   A CD  
1548 O  OE1 . GLU   A 220 ? 0.4325 0.6022 0.6747 -0.1158 0.0451  0.1564  199 GLU   A OE1 
1549 O  OE2 . GLU   A 220 ? 0.6595 0.7647 0.9019 -0.1130 0.0347  0.1357  199 GLU   A OE2 
1550 N  N   . ILE   A 221 ? 0.3712 0.5919 0.5295 -0.0699 0.0814  0.0952  200 ILE   A N   
1551 C  CA  . ILE   A 221 ? 0.3551 0.5548 0.4907 -0.0599 0.0827  0.0821  200 ILE   A CA  
1552 C  C   . ILE   A 221 ? 0.3333 0.5173 0.4714 -0.0666 0.0811  0.0982  200 ILE   A C   
1553 O  O   . ILE   A 221 ? 0.3540 0.5586 0.4990 -0.0723 0.0818  0.1167  200 ILE   A O   
1554 C  CB  . ILE   A 221 ? 0.3034 0.5381 0.4239 -0.0478 0.0898  0.0724  200 ILE   A CB  
1555 C  CG1 . ILE   A 221 ? 0.3276 0.5735 0.4472 -0.0394 0.0892  0.0538  200 ILE   A CG1 
1556 C  CG2 . ILE   A 221 ? 0.2895 0.5024 0.3910 -0.0396 0.0895  0.0613  200 ILE   A CG2 
1557 C  CD1 . ILE   A 221 ? 0.3394 0.6243 0.4487 -0.0260 0.0938  0.0420  200 ILE   A CD1 
1558 N  N   . VAL   A 222 ? 0.3759 0.5191 0.5044 -0.0633 0.0764  0.0881  201 VAL   A N   
1559 C  CA  . VAL   A 222 ? 0.4063 0.5288 0.5388 -0.0682 0.0727  0.1002  201 VAL   A CA  
1560 C  C   . VAL   A 222 ? 0.3666 0.4743 0.4784 -0.0585 0.0750  0.0886  201 VAL   A C   
1561 O  O   . VAL   A 222 ? 0.3872 0.4763 0.4866 -0.0509 0.0743  0.0700  201 VAL   A O   
1562 C  CB  . VAL   A 222 ? 0.3413 0.4279 0.4891 -0.0742 0.0619  0.0998  201 VAL   A CB  
1563 C  CG1 . VAL   A 222 ? 0.3821 0.4471 0.5359 -0.0774 0.0563  0.1104  201 VAL   A CG1 
1564 C  CG2 . VAL   A 222 ? 0.3256 0.4263 0.4979 -0.0850 0.0577  0.1114  201 VAL   A CG2 
1565 N  N   . LEU   A 223 ? 0.3880 0.5058 0.4974 -0.0593 0.0774  0.1012  202 LEU   A N   
1566 C  CA  . LEU   A 223 ? 0.3429 0.4440 0.4374 -0.0521 0.0778  0.0935  202 LEU   A CA  
1567 C  C   . LEU   A 223 ? 0.3569 0.4245 0.4599 -0.0558 0.0705  0.0987  202 LEU   A C   
1568 O  O   . LEU   A 223 ? 0.4187 0.4849 0.5399 -0.0646 0.0654  0.1159  202 LEU   A O   
1569 C  CB  . LEU   A 223 ? 0.3804 0.5124 0.4671 -0.0494 0.0833  0.1027  202 LEU   A CB  
1570 C  CG  . LEU   A 223 ? 0.4113 0.5780 0.4863 -0.0411 0.0892  0.0922  202 LEU   A CG  
1571 C  CD1 . LEU   A 223 ? 0.4170 0.6175 0.4870 -0.0394 0.0914  0.1040  202 LEU   A CD1 
1572 C  CD2 . LEU   A 223 ? 0.3455 0.4947 0.4060 -0.0310 0.0880  0.0697  202 LEU   A CD2 
1573 N  N   . TYR   A 224 ? 0.3054 0.3476 0.3975 -0.0486 0.0688  0.0843  203 TYR   A N   
1574 C  CA  . TYR   A 224 ? 0.3601 0.3736 0.4600 -0.0492 0.0613  0.0860  203 TYR   A CA  
1575 C  C   . TYR   A 224 ? 0.3532 0.3535 0.4387 -0.0403 0.0628  0.0753  203 TYR   A C   
1576 O  O   . TYR   A 224 ? 0.3503 0.3577 0.4217 -0.0347 0.0682  0.0649  203 TYR   A O   
1577 C  CB  . TYR   A 224 ? 0.3885 0.3810 0.4988 -0.0509 0.0535  0.0780  203 TYR   A CB  
1578 C  CG  . TYR   A 224 ? 0.3656 0.3496 0.4620 -0.0434 0.0553  0.0583  203 TYR   A CG  
1579 C  CD1 . TYR   A 224 ? 0.3633 0.3621 0.4556 -0.0436 0.0593  0.0530  203 TYR   A CD1 
1580 C  CD2 . TYR   A 224 ? 0.4052 0.3688 0.4935 -0.0355 0.0525  0.0462  203 TYR   A CD2 
1581 C  CE1 . TYR   A 224 ? 0.3845 0.3750 0.4657 -0.0371 0.0597  0.0376  203 TYR   A CE1 
1582 C  CE2 . TYR   A 224 ? 0.4728 0.4323 0.5490 -0.0292 0.0541  0.0320  203 TYR   A CE2 
1583 C  CZ  . TYR   A 224 ? 0.4550 0.4264 0.5280 -0.0305 0.0573  0.0286  203 TYR   A CZ  
1584 O  OH  . TYR   A 224 ? 0.5090 0.4757 0.5714 -0.0246 0.0578  0.0170  203 TYR   A OH  
1585 N  N   . ILE   A 225 ? 0.3966 0.3784 0.4889 -0.0392 0.0567  0.0786  204 ILE   A N   
1586 C  CA  . ILE   A 225 ? 0.3700 0.3400 0.4526 -0.0307 0.0570  0.0697  204 ILE   A CA  
1587 C  C   . ILE   A 225 ? 0.4041 0.3487 0.4953 -0.0267 0.0478  0.0621  204 ILE   A C   
1588 O  O   . ILE   A 225 ? 0.3828 0.3168 0.4904 -0.0316 0.0392  0.0663  204 ILE   A O   
1589 C  CB  . ILE   A 225 ? 0.3012 0.2806 0.3830 -0.0303 0.0585  0.0813  204 ILE   A CB  
1590 C  CG1 . ILE   A 225 ? 0.3605 0.3342 0.4610 -0.0368 0.0506  0.0988  204 ILE   A CG1 
1591 C  CG2 . ILE   A 225 ? 0.3767 0.3839 0.4485 -0.0314 0.0663  0.0850  204 ILE   A CG2 
1592 C  CD1 . ILE   A 225 ? 0.3499 0.3317 0.4506 -0.0361 0.0505  0.1119  204 ILE   A CD1 
1593 N  N   . SER   A 226 ? 0.3824 0.3195 0.4640 -0.0173 0.0486  0.0504  205 SER   A N   
1594 C  CA  . SER   A 226 ? 0.3926 0.3104 0.4810 -0.0100 0.0395  0.0405  205 SER   A CA  
1595 C  C   . SER   A 226 ? 0.4182 0.3257 0.5216 -0.0104 0.0312  0.0503  205 SER   A C   
1596 O  O   . SER   A 226 ? 0.4809 0.3984 0.5841 -0.0140 0.0348  0.0637  205 SER   A O   
1597 C  CB  . SER   A 226 ? 0.3918 0.3119 0.4655 0.0011  0.0439  0.0267  205 SER   A CB  
1598 O  OG  . SER   A 226 ? 0.4320 0.3594 0.5016 0.0039  0.0482  0.0316  205 SER   A OG  
1599 N  N   . MET   A 227 ? 0.4408 0.3279 0.5581 -0.0057 0.0184  0.0426  206 MET   A N   
1600 C  CA  . MET   A 227 ? 0.4685 0.3420 0.6024 -0.0037 0.0078  0.0494  206 MET   A CA  
1601 C  C   . MET   A 227 ? 0.4853 0.3665 0.6074 0.0052  0.0137  0.0472  206 MET   A C   
1602 O  O   . MET   A 227 ? 0.4554 0.3366 0.5852 0.0031  0.0112  0.0608  206 MET   A O   
1603 C  CB  . MET   A 227 ? 0.4488 0.2979 0.5994 0.0036  -0.0091 0.0350  206 MET   A CB  
1604 C  CG  . MET   A 227 ? 0.4876 0.3184 0.6582 0.0084  -0.0235 0.0383  206 MET   A CG  
1605 S  SD  . MET   A 227 ? 0.6914 0.5134 0.8918 -0.0091 -0.0339 0.0690  206 MET   A SD  
1606 C  CE  . MET   A 227 ? 0.6885 0.4876 0.9094 0.0008  -0.0512 0.0689  206 MET   A CE  
1607 N  N   . SER   A 228 ? 0.5029 0.3930 0.6076 0.0147  0.0214  0.0318  207 SER   A N   
1608 C  CA  . SER   A 228 ? 0.4967 0.3968 0.5929 0.0229  0.0268  0.0296  207 SER   A CA  
1609 C  C   . SER   A 228 ? 0.4416 0.3569 0.5323 0.0147  0.0353  0.0457  207 SER   A C   
1610 O  O   . SER   A 228 ? 0.4593 0.3768 0.5534 0.0176  0.0339  0.0519  207 SER   A O   
1611 C  CB  . SER   A 228 ? 0.5007 0.4131 0.5808 0.0319  0.0345  0.0146  207 SER   A CB  
1612 O  OG  . SER   A 228 ? 0.6186 0.5441 0.6930 0.0384  0.0401  0.0144  207 SER   A OG  
1613 N  N   . ASP   A 229 ? 0.4578 0.3851 0.5403 0.0059  0.0432  0.0510  208 ASP   A N   
1614 C  CA  . ASP   A 229 ? 0.4485 0.3934 0.5250 0.0002  0.0502  0.0626  208 ASP   A CA  
1615 C  C   . ASP   A 229 ? 0.3952 0.3418 0.4828 -0.0074 0.0456  0.0810  208 ASP   A C   
1616 O  O   . ASP   A 229 ? 0.4165 0.3816 0.4985 -0.0108 0.0506  0.0909  208 ASP   A O   
1617 C  CB  . ASP   A 229 ? 0.3392 0.2973 0.4045 -0.0044 0.0584  0.0593  208 ASP   A CB  
1618 C  CG  . ASP   A 229 ? 0.4989 0.4613 0.5537 0.0013  0.0638  0.0472  208 ASP   A CG  
1619 O  OD1 . ASP   A 229 ? 0.5583 0.5214 0.6125 0.0080  0.0639  0.0440  208 ASP   A OD1 
1620 O  OD2 . ASP   A 229 ? 0.4629 0.4296 0.5116 -0.0010 0.0675  0.0423  208 ASP   A OD2 
1621 N  N   . SER   A 230 ? 0.3907 0.3202 0.4953 -0.0100 0.0353  0.0865  209 SER   A N   
1622 C  CA  . SER   A 230 ? 0.4520 0.3859 0.5703 -0.0197 0.0307  0.1086  209 SER   A CA  
1623 C  C   . SER   A 230 ? 0.4821 0.4202 0.6038 -0.0176 0.0279  0.1216  209 SER   A C   
1624 O  O   . SER   A 230 ? 0.4948 0.4472 0.6223 -0.0254 0.0276  0.1429  209 SER   A O   
1625 C  CB  . SER   A 230 ? 0.4397 0.3520 0.5804 -0.0243 0.0179  0.1121  209 SER   A CB  
1626 O  OG  . SER   A 230 ? 0.5148 0.4023 0.6676 -0.0154 0.0055  0.1030  209 SER   A OG  
1627 N  N   . ASP   A 231 ? 0.4415 0.3712 0.5600 -0.0070 0.0260  0.1105  210 ASP   A N   
1628 C  CA  . ASP   A 231 ? 0.4477 0.3841 0.5675 -0.0039 0.0241  0.1212  210 ASP   A CA  
1629 C  C   . ASP   A 231 ? 0.4346 0.3927 0.5352 0.0002  0.0352  0.1145  210 ASP   A C   
1630 O  O   . ASP   A 231 ? 0.3770 0.3408 0.4771 0.0051  0.0338  0.1183  210 ASP   A O   
1631 C  CB  . ASP   A 231 ? 0.4887 0.4020 0.6227 0.0059  0.0121  0.1146  210 ASP   A CB  
1632 C  CG  . ASP   A 231 ? 0.5607 0.4676 0.6867 0.0176  0.0143  0.0893  210 ASP   A CG  
1633 O  OD1 . ASP   A 231 ? 0.5688 0.4887 0.6787 0.0170  0.0255  0.0797  210 ASP   A OD1 
1634 O  OD2 . ASP   A 231 ? 0.6991 0.5899 0.8360 0.0281  0.0043  0.0793  210 ASP   A OD2 
1635 N  N   . LYS   A 232 ? 0.3915 0.3609 0.4786 -0.0018 0.0445  0.1046  211 LYS   A N   
1636 C  CA  . LYS   A 232 ? 0.3639 0.3515 0.4367 0.0011  0.0526  0.0970  211 LYS   A CA  
1637 C  C   . LYS   A 232 ? 0.4273 0.4387 0.4914 -0.0046 0.0578  0.1042  211 LYS   A C   
1638 O  O   . LYS   A 232 ? 0.3727 0.4006 0.4286 -0.0017 0.0608  0.1011  211 LYS   A O   
1639 C  CB  . LYS   A 232 ? 0.3704 0.3533 0.4363 0.0046  0.0574  0.0794  211 LYS   A CB  
1640 C  CG  . LYS   A 232 ? 0.3504 0.3164 0.4220 0.0124  0.0532  0.0692  211 LYS   A CG  
1641 C  CD  . LYS   A 232 ? 0.3848 0.3511 0.4613 0.0203  0.0497  0.0697  211 LYS   A CD  
1642 C  CE  . LYS   A 232 ? 0.4163 0.3752 0.4952 0.0311  0.0478  0.0553  211 LYS   A CE  
1643 N  NZ  . LYS   A 232 ? 0.4888 0.4292 0.5744 0.0329  0.0409  0.0488  211 LYS   A NZ  
1644 N  N   . VAL   A 233 ? 0.4124 0.4285 0.4794 -0.0117 0.0583  0.1126  212 VAL   A N   
1645 C  CA  . VAL   A 233 ? 0.4013 0.4451 0.4597 -0.0151 0.0636  0.1171  212 VAL   A CA  
1646 C  C   . VAL   A 233 ? 0.4211 0.4769 0.4884 -0.0225 0.0614  0.1392  212 VAL   A C   
1647 O  O   . VAL   A 233 ? 0.4355 0.4729 0.5180 -0.0273 0.0553  0.1487  212 VAL   A O   
1648 C  CB  . VAL   A 233 ? 0.3977 0.4435 0.4495 -0.0159 0.0686  0.1026  212 VAL   A CB  
1649 C  CG1 . VAL   A 233 ? 0.3691 0.4043 0.4151 -0.0102 0.0700  0.0849  212 VAL   A CG1 
1650 C  CG2 . VAL   A 233 ? 0.4253 0.4563 0.4867 -0.0215 0.0666  0.1051  212 VAL   A CG2 
1651 N  N   . GLY   A 234 ? 0.4081 0.4972 0.4672 -0.0229 0.0655  0.1475  213 GLY   A N   
1652 C  CA  . GLY   A 234 ? 0.3713 0.4831 0.4369 -0.0306 0.0664  0.1685  213 GLY   A CA  
1653 C  C   . GLY   A 234 ? 0.4177 0.5606 0.4712 -0.0288 0.0739  0.1597  213 GLY   A C   
1654 O  O   . GLY   A 234 ? 0.4120 0.5689 0.4512 -0.0207 0.0766  0.1440  213 GLY   A O   
1655 N  N   . VAL   A 235 ? 0.3599 0.5094 0.4199 -0.0346 0.0734  0.1639  214 VAL   A N   
1656 C  CA  . VAL   A 235 ? 0.3767 0.5538 0.4272 -0.0317 0.0786  0.1531  214 VAL   A CA  
1657 C  C   . VAL   A 235 ? 0.4068 0.6143 0.4609 -0.0346 0.0764  0.1691  214 VAL   A C   
1658 O  O   . VAL   A 235 ? 0.4017 0.5999 0.4720 -0.0432 0.0715  0.1848  214 VAL   A O   
1659 C  CB  . VAL   A 235 ? 0.3822 0.5415 0.4374 -0.0346 0.0810  0.1409  214 VAL   A CB  
1660 C  CG1 . VAL   A 235 ? 0.3286 0.5177 0.3761 -0.0308 0.0851  0.1304  214 VAL   A CG1 
1661 C  CG2 . VAL   A 235 ? 0.3423 0.4716 0.3927 -0.0296 0.0807  0.1218  214 VAL   A CG2 
1662 N  N   . PHE   A 236 ? 0.4375 0.6830 0.4783 -0.0268 0.0791  0.1648  215 PHE   A N   
1663 C  CA  . PHE   A 236 ? 0.4435 0.7256 0.4866 -0.0274 0.0775  0.1808  215 PHE   A CA  
1664 C  C   . PHE   A 236 ? 0.3959 0.7110 0.4303 -0.0210 0.0814  0.1679  215 PHE   A C   
1665 O  O   . PHE   A 236 ? 0.4214 0.7369 0.4446 -0.0130 0.0843  0.1448  215 PHE   A O   
1666 C  CB  . PHE   A 236 ? 0.4044 0.7092 0.4409 -0.0220 0.0751  0.1910  215 PHE   A CB  
1667 C  CG  . PHE   A 236 ? 0.4598 0.7374 0.5078 -0.0281 0.0697  0.2076  215 PHE   A CG  
1668 C  CD1 . PHE   A 236 ? 0.4454 0.6930 0.4898 -0.0258 0.0696  0.1981  215 PHE   A CD1 
1669 C  CD2 . PHE   A 236 ? 0.4764 0.7599 0.5412 -0.0357 0.0640  0.2329  215 PHE   A CD2 
1670 C  CE1 . PHE   A 236 ? 0.5126 0.7356 0.5686 -0.0298 0.0637  0.2122  215 PHE   A CE1 
1671 C  CE2 . PHE   A 236 ? 0.5078 0.7651 0.5855 -0.0403 0.0572  0.2469  215 PHE   A CE2 
1672 C  CZ  . PHE   A 236 ? 0.5024 0.7289 0.5751 -0.0368 0.0569  0.2358  215 PHE   A CZ  
1673 N  N   . TYR   A 237 ? 0.4673 0.8115 0.5090 -0.0241 0.0804  0.1836  216 TYR   A N   
1674 C  CA  . TYR   A 237 ? 0.4882 0.8701 0.5239 -0.0177 0.0831  0.1753  216 TYR   A CA  
1675 C  C   . TYR   A 237 ? 0.5137 0.9443 0.5476 -0.0136 0.0813  0.1920  216 TYR   A C   
1676 O  O   . TYR   A 237 ? 0.5356 0.9688 0.5824 -0.0217 0.0779  0.2177  216 TYR   A O   
1677 C  CB  . TYR   A 237 ? 0.4425 0.8144 0.4921 -0.0266 0.0841  0.1792  216 TYR   A CB  
1678 C  CG  . TYR   A 237 ? 0.5355 0.9469 0.5816 -0.0207 0.0866  0.1729  216 TYR   A CG  
1679 C  CD1 . TYR   A 237 ? 0.5456 0.9571 0.5820 -0.0119 0.0893  0.1462  216 TYR   A CD1 
1680 C  CD2 . TYR   A 237 ? 0.5338 0.9833 0.5883 -0.0236 0.0854  0.1941  216 TYR   A CD2 
1681 C  CE1 . TYR   A 237 ? 0.5927 1.0404 0.6268 -0.0053 0.0905  0.1392  216 TYR   A CE1 
1682 C  CE2 . TYR   A 237 ? 0.5219 1.0104 0.5735 -0.0174 0.0876  0.1885  216 TYR   A CE2 
1683 C  CZ  . TYR   A 237 ? 0.5997 1.0865 0.6406 -0.0079 0.0900  0.1601  216 TYR   A CZ  
1684 O  OH  . TYR   A 237 ? 0.6517 1.1775 0.6902 -0.0006 0.0911  0.1532  216 TYR   A OH  
1685 N  N   . VAL   A 238 ? 0.5334 1.0038 0.5529 -0.0003 0.0822  0.1772  217 VAL   A N   
1686 C  CA  . VAL   A 238 ? 0.5640 1.0883 0.5807 0.0060  0.0804  0.1910  217 VAL   A CA  
1687 C  C   . VAL   A 238 ? 0.5680 1.1252 0.5935 0.0035  0.0817  0.2017  217 VAL   A C   
1688 O  O   . VAL   A 238 ? 0.5522 1.1183 0.5723 0.0096  0.0837  0.1827  217 VAL   A O   
1689 C  CB  . VAL   A 238 ? 0.6238 1.1783 0.6215 0.0236  0.0789  0.1679  217 VAL   A CB  
1690 C  CG1 . VAL   A 238 ? 0.6357 1.2527 0.6312 0.0316  0.0769  0.1811  217 VAL   A CG1 
1691 C  CG2 . VAL   A 238 ? 0.5481 1.0733 0.5387 0.0255  0.0773  0.1598  217 VAL   A CG2 
1692 N  N   A GLU   A 239 ? 0.5976 1.1739 0.6381 -0.0055 0.0800  0.2328  218 GLU   A N   
1693 N  N   B GLU   A 239 ? 0.5976 1.1737 0.6382 -0.0055 0.0800  0.2327  218 GLU   A N   
1694 C  CA  A GLU   A 239 ? 0.6399 1.2532 0.6912 -0.0089 0.0807  0.2482  218 GLU   A CA  
1695 C  CA  B GLU   A 239 ? 0.6401 1.2533 0.6911 -0.0087 0.0808  0.2477  218 GLU   A CA  
1696 C  C   A GLU   A 239 ? 0.6475 1.3287 0.6922 0.0022  0.0799  0.2571  218 GLU   A C   
1697 C  C   B GLU   A 239 ? 0.6475 1.3286 0.6922 0.0022  0.0799  0.2570  218 GLU   A C   
1698 O  O   A GLU   A 239 ? 0.6229 1.3198 0.6656 0.0051  0.0775  0.2682  218 GLU   A O   
1699 O  O   B GLU   A 239 ? 0.6229 1.3195 0.6660 0.0048  0.0775  0.2685  218 GLU   A O   
1700 C  CB  A GLU   A 239 ? 0.6253 1.2182 0.7019 -0.0267 0.0777  0.2785  218 GLU   A CB  
1701 C  CB  B GLU   A 239 ? 0.6255 1.2182 0.7018 -0.0266 0.0779  0.2775  218 GLU   A CB  
1702 C  CG  A GLU   A 239 ? 0.5975 1.2357 0.6885 -0.0314 0.0774  0.3015  218 GLU   A CG  
1703 C  CG  B GLU   A 239 ? 0.5717 1.1182 0.6578 -0.0361 0.0788  0.2689  218 GLU   A CG  
1704 C  CD  A GLU   A 239 ? 0.6056 1.2806 0.7097 -0.0354 0.0732  0.3352  218 GLU   A CD  
1705 C  CD  B GLU   A 239 ? 0.5719 1.1199 0.6841 -0.0507 0.0752  0.2964  218 GLU   A CD  
1706 O  OE1 A GLU   A 239 ? 0.5823 1.2286 0.6958 -0.0424 0.0687  0.3482  218 GLU   A OE1 
1707 O  OE1 B GLU   A 239 ? 0.5784 1.1434 0.7053 -0.0570 0.0703  0.3249  218 GLU   A OE1 
1708 O  OE2 A GLU   A 239 ? 0.5453 1.2800 0.6511 -0.0311 0.0740  0.3490  218 GLU   A OE2 
1709 O  OE2 B GLU   A 239 ? 0.5875 1.1211 0.7074 -0.0559 0.0765  0.2901  218 GLU   A OE2 
1710 N  N   . ASN   A 240 ? 0.6680 1.3917 0.7099 0.0091  0.0816  0.2519  219 ASN   A N   
1711 C  CA  . ASN   A 240 ? 0.6063 1.4018 0.6427 0.0212  0.0807  0.2591  219 ASN   A CA  
1712 C  C   . ASN   A 240 ? 0.7361 1.5483 0.7541 0.0374  0.0783  0.2396  219 ASN   A C   
1713 O  O   . ASN   A 240 ? 0.7041 1.5488 0.7234 0.0401  0.0764  0.2569  219 ASN   A O   
1714 C  CB  . ASN   A 240 ? 0.6329 1.4585 0.6889 0.0101  0.0791  0.3005  219 ASN   A CB  
1715 C  CG  . ASN   A 240 ? 0.6529 1.5603 0.7060 0.0219  0.0787  0.3113  219 ASN   A CG  
1716 O  OD1 . ASN   A 240 ? 0.6977 1.6406 0.7404 0.0342  0.0801  0.2931  219 ASN   A OD1 
1717 N  ND2 . ASN   A 240 ? 0.6618 1.6016 0.7253 0.0186  0.0764  0.3412  219 ASN   A ND2 
1718 N  N   . PRO   A 241 ? 0.7560 1.5476 0.7584 0.0486  0.0777  0.2034  220 PRO   A N   
1719 C  CA  . PRO   A 241 ? 0.8174 1.6218 0.8046 0.0639  0.0739  0.1832  220 PRO   A CA  
1720 C  C   . PRO   A 241 ? 0.8163 1.6965 0.7968 0.0812  0.0707  0.1811  220 PRO   A C   
1721 O  O   . PRO   A 241 ? 0.7985 1.6993 0.7715 0.0916  0.0673  0.1758  220 PRO   A O   
1722 C  CB  . PRO   A 241 ? 0.8146 1.5801 0.7914 0.0709  0.0726  0.1457  220 PRO   A CB  
1723 C  CG  . PRO   A 241 ? 0.7803 1.5018 0.7676 0.0560  0.0771  0.1504  220 PRO   A CG  
1724 C  CD  . PRO   A 241 ? 0.6597 1.4161 0.6599 0.0480  0.0795  0.1797  220 PRO   A CD  
1725 N  N   . PHE   A 242 ? 0.8736 1.7985 0.8574 0.0853  0.0715  0.1851  221 PHE   A N   
1726 C  CA  . PHE   A 242 ? 0.8211 1.8227 0.7983 0.1043  0.0679  0.1790  221 PHE   A CA  
1727 C  C   . PHE   A 242 ? 0.8267 1.8827 0.8136 0.1009  0.0692  0.2165  221 PHE   A C   
1728 O  O   . PHE   A 242 ? 0.8436 1.9705 0.8264 0.1170  0.0666  0.2148  221 PHE   A O   
1729 C  CB  . PHE   A 242 ? 0.8343 1.8631 0.8102 0.1120  0.0676  0.1641  221 PHE   A CB  
1730 C  CG  . PHE   A 242 ? 0.9509 1.9321 0.9193 0.1168  0.0652  0.1270  221 PHE   A CG  
1731 C  CD1 . PHE   A 242 ? 1.0340 1.9513 1.0091 0.1000  0.0699  0.1296  221 PHE   A CD1 
1732 C  CD2 . PHE   A 242 ? 0.8693 1.8715 0.8264 0.1386  0.0572  0.0896  221 PHE   A CD2 
1733 C  CE1 . PHE   A 242 ? 1.0134 1.8900 0.9836 0.1043  0.0678  0.0973  221 PHE   A CE1 
1734 C  CE2 . PHE   A 242 ? 0.9729 1.9315 0.9265 0.1426  0.0536  0.0569  221 PHE   A CE2 
1735 C  CZ  . PHE   A 242 ? 1.0773 1.9738 1.0371 0.1252  0.0595  0.0617  221 PHE   A CZ  
1736 N  N   . PHE   A 243 ? 0.6896 1.7165 0.6912 0.0811  0.0722  0.2499  222 PHE   A N   
1737 C  CA  . PHE   A 243 ? 0.6269 1.7010 0.6409 0.0766  0.0723  0.2874  222 PHE   A CA  
1738 C  C   . PHE   A 243 ? 0.6435 1.6745 0.6634 0.0654  0.0716  0.3028  222 PHE   A C   
1739 O  O   . PHE   A 243 ? 0.6269 1.6345 0.6336 0.0736  0.0698  0.2804  222 PHE   A O   
1740 C  CB  . PHE   A 243 ? 0.5894 1.6840 0.6225 0.0627  0.0747  0.3203  222 PHE   A CB  
1741 C  CG  . PHE   A 243 ? 0.6148 1.7693 0.6431 0.0750  0.0753  0.3114  222 PHE   A CG  
1742 C  CD1 . PHE   A 243 ? 0.5574 1.7976 0.5856 0.0880  0.0741  0.3242  222 PHE   A CD1 
1743 C  CD2 . PHE   A 243 ? 0.6765 1.8043 0.7011 0.0743  0.0769  0.2905  222 PHE   A CD2 
1744 C  CE1 . PHE   A 243 ? 0.5712 1.8697 0.5950 0.1005  0.0741  0.3156  222 PHE   A CE1 
1745 C  CE2 . PHE   A 243 ? 0.5317 1.7153 0.5521 0.0863  0.0770  0.2818  222 PHE   A CE2 
1746 C  CZ  . PHE   A 243 ? 0.5584 1.8278 0.5781 0.0997  0.0754  0.2941  222 PHE   A CZ  
1747 N  N   . GLY   A 244 ? 0.6312 1.6523 0.6722 0.0472  0.0719  0.3407  223 GLY   A N   
1748 C  CA  . GLY   A 244 ? 0.6573 1.6301 0.7067 0.0352  0.0701  0.3550  223 GLY   A CA  
1749 C  C   . GLY   A 244 ? 0.6602 1.5504 0.7083 0.0252  0.0706  0.3375  223 GLY   A C   
1750 O  O   . GLY   A 244 ? 0.6139 1.4752 0.6750 0.0123  0.0713  0.3456  223 GLY   A O   
1751 N  N   . GLN   A 245 ? 0.6181 1.4722 0.6517 0.0312  0.0700  0.3140  224 GLN   A N   
1752 C  CA  . GLN   A 245 ? 0.6796 1.4634 0.7086 0.0255  0.0710  0.2922  224 GLN   A CA  
1753 C  C   . GLN   A 245 ? 0.7076 1.4368 0.7546 0.0073  0.0690  0.3136  224 GLN   A C   
1754 O  O   . GLN   A 245 ? 0.7006 1.4329 0.7567 0.0029  0.0659  0.3353  224 GLN   A O   
1755 C  CB  . GLN   A 245 ? 0.6358 1.4056 0.6438 0.0393  0.0702  0.2593  224 GLN   A CB  
1756 C  CG  . GLN   A 245 ? 0.7027 1.4806 0.6959 0.0524  0.0709  0.2243  224 GLN   A CG  
1757 C  CD  . GLN   A 245 ? 0.6468 1.4144 0.6226 0.0665  0.0680  0.1923  224 GLN   A CD  
1758 O  OE1 . GLN   A 245 ? 0.5960 1.3348 0.5698 0.0636  0.0669  0.1940  224 GLN   A OE1 
1759 N  NE2 . GLN   A 245 ? 0.6054 1.3975 0.5701 0.0822  0.0655  0.1624  224 GLN   A NE2 
1760 N  N   . ARG   A 246 ? 0.6334 1.3133 0.6866 -0.0025 0.0702  0.3060  225 ARG   A N   
1761 C  CA  . ARG   A 246 ? 0.6503 1.2737 0.7206 -0.0179 0.0670  0.3195  225 ARG   A CA  
1762 C  C   . ARG   A 246 ? 0.6303 1.1973 0.6914 -0.0181 0.0693  0.2912  225 ARG   A C   
1763 O  O   . ARG   A 246 ? 0.5911 1.1615 0.6401 -0.0113 0.0733  0.2677  225 ARG   A O   
1764 C  CB  . ARG   A 246 ? 0.6307 1.2575 0.7270 -0.0323 0.0642  0.3476  225 ARG   A CB  
1765 C  CG  . ARG   A 246 ? 0.7245 1.4099 0.8339 -0.0336 0.0615  0.3800  225 ARG   A CG  
1766 C  CD  . ARG   A 246 ? 0.7381 1.4254 0.8509 -0.0334 0.0574  0.3951  225 ARG   A CD  
1767 N  NE  . ARG   A 246 ? 0.8578 1.5965 0.9889 -0.0377 0.0539  0.4309  225 ARG   A NE  
1768 C  CZ  . ARG   A 246 ? 0.8407 1.6419 0.9626 -0.0265 0.0559  0.4372  225 ARG   A CZ  
1769 N  NH1 . ARG   A 246 ? 0.8262 1.6464 0.9209 -0.0096 0.0604  0.4088  225 ARG   A NH1 
1770 N  NH2 . ARG   A 246 ? 0.8036 1.6508 0.9456 -0.0322 0.0526  0.4731  225 ARG   A NH2 
1771 N  N   . TYR   A 247 ? 0.6513 1.1683 0.7195 -0.0256 0.0663  0.2939  226 TYR   A N   
1772 C  CA  . TYR   A 247 ? 0.5933 1.0600 0.6526 -0.0249 0.0683  0.2687  226 TYR   A CA  
1773 C  C   . TYR   A 247 ? 0.4743 0.8921 0.5541 -0.0389 0.0645  0.2784  226 TYR   A C   
1774 O  O   . TYR   A 247 ? 0.5288 0.9300 0.6240 -0.0460 0.0582  0.2977  226 TYR   A O   
1775 C  CB  . TYR   A 247 ? 0.5368 0.9941 0.5822 -0.0169 0.0677  0.2583  226 TYR   A CB  
1776 C  CG  . TYR   A 247 ? 0.5824 1.0936 0.6132 -0.0039 0.0683  0.2559  226 TYR   A CG  
1777 C  CD1 . TYR   A 247 ? 0.5790 1.1129 0.5912 0.0094  0.0712  0.2288  226 TYR   A CD1 
1778 C  CD2 . TYR   A 247 ? 0.5951 1.1363 0.6328 -0.0043 0.0649  0.2802  226 TYR   A CD2 
1779 C  CE1 . TYR   A 247 ? 0.6031 1.1883 0.6034 0.0230  0.0700  0.2241  226 TYR   A CE1 
1780 C  CE2 . TYR   A 247 ? 0.5880 1.1822 0.6130 0.0086  0.0651  0.2774  226 TYR   A CE2 
1781 C  CZ  . TYR   A 247 ? 0.6410 1.2573 0.6472 0.0227  0.0675  0.2484  226 TYR   A CZ  
1782 O  OH  . TYR   A 247 ? 0.6387 1.3094 0.6337 0.0371  0.0662  0.2431  226 TYR   A OH  
1783 N  N   A ILE   A 248 ? 0.4331 0.8283 0.5140 -0.0419 0.0672  0.2638  227 ILE   A N   
1784 N  N   B ILE   A 248 ? 0.4348 0.8302 0.5158 -0.0420 0.0672  0.2640  227 ILE   A N   
1785 C  CA  A ILE   A 248 ? 0.4680 0.8232 0.5697 -0.0543 0.0627  0.2713  227 ILE   A CA  
1786 C  CA  B ILE   A 248 ? 0.4654 0.8207 0.5673 -0.0543 0.0626  0.2716  227 ILE   A CA  
1787 C  C   A ILE   A 248 ? 0.4837 0.7892 0.5804 -0.0537 0.0630  0.2517  227 ILE   A C   
1788 C  C   B ILE   A 248 ? 0.4827 0.7883 0.5794 -0.0537 0.0630  0.2518  227 ILE   A C   
1789 O  O   A ILE   A 248 ? 0.4389 0.7399 0.5189 -0.0465 0.0691  0.2279  227 ILE   A O   
1790 O  O   B ILE   A 248 ? 0.4626 0.7639 0.5426 -0.0465 0.0691  0.2280  227 ILE   A O   
1791 C  CB  A ILE   A 248 ? 0.4776 0.8452 0.5869 -0.0587 0.0648  0.2710  227 ILE   A CB  
1792 C  CB  B ILE   A 248 ? 0.4760 0.8435 0.5859 -0.0590 0.0646  0.2718  227 ILE   A CB  
1793 C  CG1 A ILE   A 248 ? 0.4635 0.8765 0.5861 -0.0627 0.0623  0.2979  227 ILE   A CG1 
1794 C  CG1 B ILE   A 248 ? 0.4620 0.7933 0.5977 -0.0721 0.0572  0.2834  227 ILE   A CG1 
1795 C  CG2 A ILE   A 248 ? 0.4568 0.7777 0.5831 -0.0687 0.0606  0.2686  227 ILE   A CG2 
1796 C  CG2 B ILE   A 248 ? 0.4884 0.8528 0.5806 -0.0512 0.0719  0.2426  227 ILE   A CG2 
1797 C  CD1 A ILE   A 248 ? 0.4993 0.9670 0.6049 -0.0511 0.0664  0.2985  227 ILE   A CD1 
1798 C  CD1 B ILE   A 248 ? 0.4883 0.8194 0.6463 -0.0802 0.0476  0.3121  227 ILE   A CD1 
1799 N  N   . HIS   A 249 ? 0.4476 0.7171 0.5605 -0.0607 0.0556  0.2618  228 HIS   A N   
1800 C  CA  . HIS   A 249 ? 0.4320 0.6554 0.5436 -0.0603 0.0546  0.2458  228 HIS   A CA  
1801 C  C   . HIS   A 249 ? 0.4837 0.6830 0.6062 -0.0666 0.0536  0.2376  228 HIS   A C   
1802 O  O   . HIS   A 249 ? 0.5410 0.7302 0.6857 -0.0755 0.0457  0.2517  228 HIS   A O   
1803 C  CB  . HIS   A 249 ? 0.5031 0.7013 0.6286 -0.0633 0.0454  0.2593  228 HIS   A CB  
1804 C  CG  . HIS   A 249 ? 0.4962 0.6491 0.6226 -0.0618 0.0430  0.2446  228 HIS   A CG  
1805 N  ND1 . HIS   A 249 ? 0.4700 0.5865 0.6169 -0.0680 0.0340  0.2452  228 HIS   A ND1 
1806 C  CD2 . HIS   A 249 ? 0.4406 0.5812 0.5515 -0.0541 0.0476  0.2292  228 HIS   A CD2 
1807 C  CE1 . HIS   A 249 ? 0.4922 0.5767 0.6351 -0.0632 0.0336  0.2303  228 HIS   A CE1 
1808 N  NE2 . HIS   A 249 ? 0.4507 0.5495 0.5723 -0.0554 0.0422  0.2217  228 HIS   A NE2 
1809 N  N   . ILE   A 250 ? 0.4532 0.6444 0.5619 -0.0619 0.0606  0.2151  229 ILE   A N   
1810 C  CA  . ILE   A 250 ? 0.4308 0.6058 0.5481 -0.0669 0.0605  0.2066  229 ILE   A CA  
1811 C  C   . ILE   A 250 ? 0.4471 0.5795 0.5665 -0.0666 0.0586  0.1919  229 ILE   A C   
1812 O  O   . ILE   A 250 ? 0.3944 0.5078 0.5260 -0.0717 0.0553  0.1875  229 ILE   A O   
1813 C  CB  . ILE   A 250 ? 0.4799 0.6844 0.5840 -0.0622 0.0692  0.1936  229 ILE   A CB  
1814 C  CG1 . ILE   A 250 ? 0.4233 0.6271 0.5065 -0.0519 0.0760  0.1718  229 ILE   A CG1 
1815 C  CG2 . ILE   A 250 ? 0.4954 0.7456 0.5985 -0.0612 0.0704  0.2081  229 ILE   A CG2 
1816 C  CD1 . ILE   A 250 ? 0.4597 0.6721 0.5362 -0.0481 0.0817  0.1533  229 ILE   A CD1 
1817 N  N   . LEU   A 251 ? 0.4713 0.5903 0.5800 -0.0603 0.0604  0.1841  230 LEU   A N   
1818 C  CA  . LEU   A 251 ? 0.4248 0.5064 0.5366 -0.0587 0.0585  0.1719  230 LEU   A CA  
1819 C  C   . LEU   A 251 ? 0.4150 0.4833 0.5250 -0.0542 0.0556  0.1756  230 LEU   A C   
1820 O  O   . LEU   A 251 ? 0.3691 0.4601 0.4677 -0.0500 0.0590  0.1804  230 LEU   A O   
1821 C  CB  . LEU   A 251 ? 0.4193 0.5018 0.5172 -0.0533 0.0676  0.1516  230 LEU   A CB  
1822 C  CG  . LEU   A 251 ? 0.4213 0.5125 0.5211 -0.0561 0.0706  0.1441  230 LEU   A CG  
1823 C  CD1 . LEU   A 251 ? 0.3046 0.3925 0.3873 -0.0472 0.0755  0.1193  230 LEU   A CD1 
1824 C  CD2 . LEU   A 251 ? 0.3765 0.4411 0.4963 -0.0635 0.0624  0.1471  230 LEU   A CD2 
1825 N  N   . GLY   A 252 ? 0.4014 0.4337 0.5237 -0.0539 0.0487  0.1724  231 GLY   A N   
1826 C  CA  . GLY   A 252 ? 0.4297 0.4466 0.5516 -0.0477 0.0439  0.1725  231 GLY   A CA  
1827 C  C   . GLY   A 252 ? 0.4876 0.4735 0.6339 -0.0506 0.0297  0.1809  231 GLY   A C   
1828 O  O   . GLY   A 252 ? 0.4691 0.4340 0.6280 -0.0531 0.0231  0.1733  231 GLY   A O   
1829 N  N   . ARG   A 253 ? 0.4653 0.4484 0.6182 -0.0490 0.0228  0.1932  232 ARG   A N   
1830 C  CA  . ARG   A 253 ? 0.4464 0.3987 0.6225 -0.0487 0.0064  0.1958  232 ARG   A CA  
1831 C  C   . ARG   A 253 ? 0.5053 0.4549 0.7007 -0.0582 -0.0027 0.2022  232 ARG   A C   
1832 O  O   . ARG   A 253 ? 0.5394 0.5153 0.7389 -0.0659 -0.0021 0.2199  232 ARG   A O   
1833 C  CB  . ARG   A 253 ? 0.5661 0.5237 0.7468 -0.0467 0.0005  0.2111  232 ARG   A CB  
1834 C  CG  . ARG   A 253 ? 0.4926 0.4515 0.6575 -0.0366 0.0074  0.2054  232 ARG   A CG  
1835 C  CD  . ARG   A 253 ? 0.5032 0.4579 0.6775 -0.0329 -0.0024 0.2176  232 ARG   A CD  
1836 N  NE  . ARG   A 253 ? 0.4975 0.4569 0.6555 -0.0218 0.0034  0.2072  232 ARG   A NE  
1837 C  CZ  . ARG   A 253 ? 0.5413 0.5308 0.6836 -0.0208 0.0112  0.2159  232 ARG   A CZ  
1838 N  NH1 . ARG   A 253 ? 0.5096 0.5296 0.6485 -0.0290 0.0151  0.2357  232 ARG   A NH1 
1839 N  NH2 . ARG   A 253 ? 0.4530 0.4457 0.5825 -0.0104 0.0144  0.2012  232 ARG   A NH2 
1840 N  N   . ARG   A 254 ? 0.5035 0.4234 0.7113 -0.0566 -0.0116 0.1871  233 ARG   A N   
1841 C  CA  . ARG   A 254 ? 0.5694 0.4823 0.7992 -0.0646 -0.0231 0.1908  233 ARG   A CA  
1842 C  C   . ARG   A 254 ? 0.5604 0.5008 0.7842 -0.0732 -0.0133 0.1966  233 ARG   A C   
1843 O  O   . ARG   A 254 ? 0.6057 0.5498 0.8486 -0.0814 -0.0213 0.2062  233 ARG   A O   
1844 C  CB  . ARG   A 254 ? 0.5228 0.4353 0.7759 -0.0695 -0.0372 0.2101  233 ARG   A CB  
1845 C  CG  . ARG   A 254 ? 0.5936 0.4741 0.8593 -0.0606 -0.0518 0.2009  233 ARG   A CG  
1846 C  CD  . ARG   A 254 ? 0.7353 0.6173 1.0253 -0.0660 -0.0657 0.2217  233 ARG   A CD  
1847 N  NE  . ARG   A 254 ? 0.7755 0.6886 1.0544 -0.0692 -0.0560 0.2435  233 ARG   A NE  
1848 C  CZ  . ARG   A 254 ? 0.7869 0.7017 1.0508 -0.0612 -0.0508 0.2427  233 ARG   A CZ  
1849 N  NH1 . ARG   A 254 ? 0.7458 0.6339 1.0039 -0.0492 -0.0533 0.2220  233 ARG   A NH1 
1850 N  NH2 . ARG   A 254 ? 0.6896 0.6360 0.9443 -0.0642 -0.0432 0.2624  233 ARG   A NH2 
1851 N  N   . LYS   A 255 ? 0.4925 0.4534 0.6919 -0.0709 0.0032  0.1907  234 LYS   A N   
1852 C  CA  . LYS   A 255 ? 0.4692 0.4550 0.6615 -0.0762 0.0124  0.1908  234 LYS   A CA  
1853 C  C   . LYS   A 255 ? 0.4531 0.4320 0.6286 -0.0705 0.0224  0.1699  234 LYS   A C   
1854 O  O   . LYS   A 255 ? 0.4399 0.4344 0.5951 -0.0651 0.0343  0.1654  234 LYS   A O   
1855 C  CB  . LYS   A 255 ? 0.5029 0.5309 0.6833 -0.0783 0.0219  0.2061  234 LYS   A CB  
1856 C  CG  . LYS   A 255 ? 0.4874 0.5285 0.6862 -0.0847 0.0129  0.2301  234 LYS   A CG  
1857 C  CD  . LYS   A 255 ? 0.5756 0.6619 0.7603 -0.0840 0.0226  0.2432  234 LYS   A CD  
1858 C  CE  . LYS   A 255 ? 0.6046 0.7048 0.8066 -0.0888 0.0138  0.2688  234 LYS   A CE  
1859 N  NZ  . LYS   A 255 ? 0.6080 0.6856 0.8144 -0.0850 0.0064  0.2713  234 LYS   A NZ  
1860 N  N   . LEU   A 256 ? 0.4639 0.4206 0.6493 -0.0711 0.0167  0.1569  235 LEU   A N   
1861 C  CA  . LEU   A 256 ? 0.4397 0.3896 0.6060 -0.0622 0.0238  0.1321  235 LEU   A CA  
1862 C  C   . LEU   A 256 ? 0.3815 0.3559 0.5373 -0.0653 0.0341  0.1286  235 LEU   A C   
1863 O  O   . LEU   A 256 ? 0.3595 0.3366 0.4944 -0.0572 0.0418  0.1103  235 LEU   A O   
1864 C  CB  . LEU   A 256 ? 0.4021 0.3189 0.5780 -0.0568 0.0114  0.1135  235 LEU   A CB  
1865 C  CG  . LEU   A 256 ? 0.4685 0.3600 0.6543 -0.0499 -0.0003 0.1107  235 LEU   A CG  
1866 C  CD1 . LEU   A 256 ? 0.5305 0.3957 0.7194 -0.0397 -0.0111 0.0857  235 LEU   A CD1 
1867 C  CD2 . LEU   A 256 ? 0.4123 0.3135 0.5780 -0.0418 0.0090  0.1095  235 LEU   A CD2 
1868 N  N   . TYR   A 257 ? 0.3873 0.3809 0.5589 -0.0766 0.0339  0.1465  236 TYR   A N   
1869 C  CA  . TYR   A 257 ? 0.4188 0.4376 0.5825 -0.0781 0.0428  0.1420  236 TYR   A CA  
1870 C  C   . TYR   A 257 ? 0.3997 0.4540 0.5651 -0.0834 0.0452  0.1594  236 TYR   A C   
1871 O  O   . TYR   A 257 ? 0.4053 0.4610 0.5822 -0.0875 0.0379  0.1756  236 TYR   A O   
1872 C  CB  . TYR   A 257 ? 0.4119 0.4133 0.5864 -0.0801 0.0357  0.1296  236 TYR   A CB  
1873 C  CG  . TYR   A 257 ? 0.4515 0.4466 0.6544 -0.0905 0.0228  0.1436  236 TYR   A CG  
1874 C  CD1 . TYR   A 257 ? 0.4538 0.4780 0.6641 -0.0977 0.0246  0.1558  236 TYR   A CD1 
1875 C  CD2 . TYR   A 257 ? 0.4836 0.4448 0.7032 -0.0900 0.0073  0.1405  236 TYR   A CD2 
1876 C  CE1 . TYR   A 257 ? 0.4745 0.4941 0.7095 -0.1056 0.0119  0.1674  236 TYR   A CE1 
1877 C  CE2 . TYR   A 257 ? 0.4976 0.4533 0.7419 -0.0971 -0.0067 0.1498  236 TYR   A CE2 
1878 C  CZ  . TYR   A 257 ? 0.5247 0.5094 0.7774 -0.1057 -0.0041 0.1646  236 TYR   A CZ  
1879 O  OH  . TYR   A 257 ? 0.5366 0.5166 0.8168 -0.1132 -0.0184 0.1758  236 TYR   A OH  
1880 N  N   . HIS   A 258 ? 0.3820 0.4661 0.5366 -0.0819 0.0548  0.1550  237 HIS   A N   
1881 C  CA  . HIS   A 258 ? 0.3632 0.4850 0.5179 -0.0843 0.0577  0.1686  237 HIS   A CA  
1882 C  C   . HIS   A 258 ? 0.3627 0.5072 0.5156 -0.0840 0.0637  0.1604  237 HIS   A C   
1883 O  O   . HIS   A 258 ? 0.3743 0.5255 0.5121 -0.0765 0.0715  0.1439  237 HIS   A O   
1884 C  CB  . HIS   A 258 ? 0.3996 0.5450 0.5358 -0.0771 0.0641  0.1716  237 HIS   A CB  
1885 C  CG  . HIS   A 258 ? 0.4630 0.6488 0.5998 -0.0781 0.0659  0.1864  237 HIS   A CG  
1886 N  ND1 . HIS   A 258 ? 0.4150 0.6368 0.5374 -0.0711 0.0742  0.1784  237 HIS   A ND1 
1887 C  CD2 . HIS   A 258 ? 0.3789 0.5766 0.5310 -0.0847 0.0596  0.2091  237 HIS   A CD2 
1888 C  CE1 . HIS   A 258 ? 0.4067 0.6624 0.5338 -0.0728 0.0735  0.1955  237 HIS   A CE1 
1889 N  NE2 . HIS   A 258 ? 0.4963 0.7387 0.6417 -0.0817 0.0651  0.2157  237 HIS   A NE2 
1890 N  N   . VAL   A 259 ? 0.3995 0.5567 0.5696 -0.0917 0.0594  0.1721  238 VAL   A N   
1891 C  CA  . VAL   A 259 ? 0.3986 0.5813 0.5696 -0.0914 0.0646  0.1661  238 VAL   A CA  
1892 C  C   . VAL   A 259 ? 0.3533 0.5791 0.5072 -0.0833 0.0736  0.1664  238 VAL   A C   
1893 O  O   . VAL   A 259 ? 0.3497 0.5983 0.5053 -0.0846 0.0727  0.1836  238 VAL   A O   
1894 C  CB  . VAL   A 259 ? 0.4026 0.5869 0.5991 -0.1022 0.0565  0.1798  238 VAL   A CB  
1895 C  CG1 . VAL   A 259 ? 0.3593 0.5734 0.5571 -0.1014 0.0622  0.1739  238 VAL   A CG1 
1896 C  CG2 . VAL   A 259 ? 0.4108 0.5510 0.6248 -0.1082 0.0447  0.1757  238 VAL   A CG2 
1897 N  N   . VAL   A 260 ? 0.3773 0.6153 0.5163 -0.0739 0.0810  0.1470  239 VAL   A N   
1898 C  CA  . VAL   A 260 ? 0.3254 0.6023 0.4479 -0.0632 0.0873  0.1416  239 VAL   A CA  
1899 C  C   . VAL   A 260 ? 0.3988 0.7112 0.5299 -0.0644 0.0885  0.1475  239 VAL   A C   
1900 O  O   . VAL   A 260 ? 0.4705 0.7793 0.6128 -0.0678 0.0881  0.1417  239 VAL   A O   
1901 C  CB  . VAL   A 260 ? 0.4098 0.6834 0.5154 -0.0513 0.0920  0.1166  239 VAL   A CB  
1902 C  CG1 . VAL   A 260 ? 0.4623 0.7757 0.5534 -0.0387 0.0954  0.1074  239 VAL   A CG1 
1903 C  CG2 . VAL   A 260 ? 0.3421 0.5852 0.4393 -0.0500 0.0912  0.1129  239 VAL   A CG2 
1904 N  N   . LYS   A 261 ? 0.4164 0.7659 0.5427 -0.0611 0.0898  0.1595  240 LYS   A N   
1905 C  CA  . LYS   A 261 ? 0.4253 0.8164 0.5558 -0.0590 0.0920  0.1632  240 LYS   A CA  
1906 C  C   . LYS   A 261 ? 0.4486 0.8564 0.5636 -0.0443 0.0965  0.1365  240 LYS   A C   
1907 O  O   . LYS   A 261 ? 0.5356 0.9545 0.6323 -0.0323 0.0978  0.1242  240 LYS   A O   
1908 C  CB  . LYS   A 261 ? 0.3415 0.7714 0.4706 -0.0585 0.0915  0.1844  240 LYS   A CB  
1909 N  N   . TYR   A 262 ? 0.4119 0.8211 0.5360 -0.0448 0.0972  0.1269  241 TYR   A N   
1910 C  CA  . TYR   A 262 ? 0.4727 0.8933 0.5856 -0.0304 0.0993  0.1004  241 TYR   A CA  
1911 C  C   . TYR   A 262 ? 0.5216 0.9932 0.6266 -0.0196 0.1004  0.0984  241 TYR   A C   
1912 O  O   . TYR   A 262 ? 0.4773 0.9773 0.5930 -0.0256 0.1011  0.1162  241 TYR   A O   
1913 C  CB  . TYR   A 262 ? 0.4185 0.8226 0.5453 -0.0342 0.0986  0.0908  241 TYR   A CB  
1914 C  CG  . TYR   A 262 ? 0.4039 0.8242 0.5233 -0.0191 0.0989  0.0652  241 TYR   A CG  
1915 C  CD1 . TYR   A 262 ? 0.4417 0.8413 0.5500 -0.0086 0.0974  0.0424  241 TYR   A CD1 
1916 C  CD2 . TYR   A 262 ? 0.4039 0.8600 0.5288 -0.0148 0.0993  0.0639  241 TYR   A CD2 
1917 C  CE1 . TYR   A 262 ? 0.4231 0.8340 0.5270 0.0060  0.0946  0.0182  241 TYR   A CE1 
1918 C  CE2 . TYR   A 262 ? 0.4148 0.8838 0.5338 0.0002  0.0975  0.0392  241 TYR   A CE2 
1919 C  CZ  . TYR   A 262 ? 0.4282 0.8728 0.5371 0.0107  0.0943  0.0161  241 TYR   A CZ  
1920 O  OH  . TYR   A 262 ? 0.3731 0.8267 0.4784 0.0261  0.0896  -0.0091 241 TYR   A OH  
1921 N  N   . THR   A 263 ? 0.4415 0.9257 0.5289 -0.0033 0.0996  0.0765  242 THR   A N   
1922 C  CA  . THR   A 263 ? 0.4764 1.0091 0.5546 0.0104  0.0986  0.0683  242 THR   A CA  
1923 C  C   . THR   A 263 ? 0.4740 1.0054 0.5496 0.0235  0.0957  0.0387  242 THR   A C   
1924 O  O   . THR   A 263 ? 0.4923 0.9912 0.5636 0.0286  0.0930  0.0196  242 THR   A O   
1925 C  CB  . THR   A 263 ? 0.5347 1.0875 0.5957 0.0204  0.0965  0.0659  242 THR   A CB  
1926 O  OG1 . THR   A 263 ? 0.6505 1.2105 0.7154 0.0091  0.0982  0.0953  242 THR   A OG1 
1927 C  CG2 . THR   A 263 ? 0.4995 1.1033 0.5504 0.0373  0.0935  0.0520  242 THR   A CG2 
1928 N  N   . GLY   A 264 ? 0.4305 0.9977 0.5100 0.0291  0.0955  0.0355  243 GLY   A N   
1929 C  CA  . GLY   A 264 ? 0.3962 0.9633 0.4757 0.0418  0.0913  0.0084  243 GLY   A CA  
1930 C  C   . GLY   A 264 ? 0.4066 0.9825 0.4700 0.0613  0.0837  -0.0191 243 GLY   A C   
1931 O  O   . GLY   A 264 ? 0.4832 1.0698 0.5345 0.0658  0.0821  -0.0179 243 GLY   A O   
1932 N  N   . GLY   A 265 ? 0.4037 0.9746 0.4688 0.0733  0.0771  -0.0450 244 GLY   A N   
1933 C  CA  . GLY   A 265 ? 0.3979 0.9726 0.4521 0.0920  0.0664  -0.0737 244 GLY   A CA  
1934 C  C   . GLY   A 265 ? 0.3892 0.9253 0.4379 0.0910  0.0637  -0.0795 244 GLY   A C   
1935 O  O   . GLY   A 265 ? 0.4405 0.9399 0.4946 0.0778  0.0692  -0.0672 244 GLY   A O   
1936 N  N   . SER   A 266 ? 0.3838 0.9307 0.4227 0.1059  0.0540  -0.0994 245 SER   A N   
1937 C  CA  . SER   A 266 ? 0.4007 0.9172 0.4346 0.1064  0.0503  -0.1059 245 SER   A CA  
1938 C  C   . SER   A 266 ? 0.4545 0.9849 0.4803 0.0971  0.0586  -0.0812 245 SER   A C   
1939 O  O   . SER   A 266 ? 0.5081 1.0818 0.5255 0.1039  0.0575  -0.0775 245 SER   A O   
1940 C  CB  . SER   A 266 ? 0.4530 0.9764 0.4833 0.1258  0.0344  -0.1371 245 SER   A CB  
1941 O  OG  . SER   A 266 ? 0.5934 1.0722 0.6330 0.1286  0.0254  -0.1558 245 SER   A OG  
1942 N  N   . ALA   A 267 ? 0.4036 0.8991 0.4325 0.0823  0.0660  -0.0641 246 ALA   A N   
1943 C  CA  . ALA   A 267 ? 0.3080 0.8106 0.3316 0.0722  0.0728  -0.0392 246 ALA   A CA  
1944 C  C   . ALA   A 267 ? 0.4265 0.8909 0.4472 0.0686  0.0723  -0.0414 246 ALA   A C   
1945 O  O   . ALA   A 267 ? 0.4629 0.8892 0.4898 0.0660  0.0714  -0.0507 246 ALA   A O   
1946 C  CB  . ALA   A 267 ? 0.3648 0.8670 0.3983 0.0547  0.0824  -0.0095 246 ALA   A CB  
1947 N  N   . GLU   A 268 ? 0.4089 0.8867 0.4206 0.0691  0.0725  -0.0325 247 GLU   A N   
1948 C  CA  . GLU   A 268 ? 0.3707 0.8173 0.3795 0.0643  0.0732  -0.0298 247 GLU   A CA  
1949 C  C   . GLU   A 268 ? 0.4446 0.8969 0.4526 0.0514  0.0802  0.0012  247 GLU   A C   
1950 O  O   . GLU   A 268 ? 0.4699 0.9612 0.4735 0.0539  0.0803  0.0129  247 GLU   A O   
1951 C  CB  . GLU   A 268 ? 0.3735 0.8281 0.3737 0.0796  0.0634  -0.0531 247 GLU   A CB  
1952 C  CG  . GLU   A 268 ? 0.4399 0.8845 0.4447 0.0928  0.0526  -0.0848 247 GLU   A CG  
1953 C  CD  . GLU   A 268 ? 0.5550 0.9949 0.5567 0.1052  0.0408  -0.1078 247 GLU   A CD  
1954 O  OE1 . GLU   A 268 ? 0.5219 0.9714 0.5157 0.1046  0.0421  -0.0996 247 GLU   A OE1 
1955 O  OE2 . GLU   A 268 ? 0.5766 1.0024 0.5858 0.1156  0.0287  -0.1340 247 GLU   A OE2 
1956 N  N   . LEU   A 269 ? 0.3391 0.7539 0.3528 0.0381  0.0849  0.0146  248 LEU   A N   
1957 C  CA  . LEU   A 269 ? 0.3620 0.7734 0.3770 0.0265  0.0886  0.0418  248 LEU   A CA  
1958 C  C   . LEU   A 269 ? 0.2971 0.6887 0.3049 0.0284  0.0869  0.0373  248 LEU   A C   
1959 O  O   . LEU   A 269 ? 0.3577 0.7149 0.3680 0.0266  0.0872  0.0274  248 LEU   A O   
1960 C  CB  . LEU   A 269 ? 0.3156 0.7002 0.3448 0.0101  0.0929  0.0608  248 LEU   A CB  
1961 C  CG  . LEU   A 269 ? 0.3968 0.8046 0.4352 0.0067  0.0944  0.0688  248 LEU   A CG  
1962 C  CD1 . LEU   A 269 ? 0.4016 0.7786 0.4560 -0.0079 0.0965  0.0808  248 LEU   A CD1 
1963 C  CD2 . LEU   A 269 ? 0.3971 0.8457 0.4345 0.0062  0.0942  0.0888  248 LEU   A CD2 
1964 N  N   . LEU   A 270 ? 0.3887 0.8053 0.3884 0.0327  0.0850  0.0449  249 LEU   A N   
1965 C  CA  . LEU   A 270 ? 0.3504 0.7554 0.3429 0.0359  0.0828  0.0407  249 LEU   A CA  
1966 C  C   . LEU   A 270 ? 0.3503 0.7324 0.3485 0.0220  0.0862  0.0669  249 LEU   A C   
1967 O  O   . LEU   A 270 ? 0.3971 0.7960 0.3993 0.0158  0.0869  0.0899  249 LEU   A O   
1968 C  CB  . LEU   A 270 ? 0.3053 0.7525 0.2865 0.0497  0.0774  0.0330  249 LEU   A CB  
1969 C  CG  . LEU   A 270 ? 0.3694 0.8113 0.3432 0.0538  0.0744  0.0297  249 LEU   A CG  
1970 C  CD1 . LEU   A 270 ? 0.4159 0.8235 0.3911 0.0570  0.0720  0.0069  249 LEU   A CD1 
1971 C  CD2 . LEU   A 270 ? 0.3320 0.8208 0.2957 0.0686  0.0678  0.0211  249 LEU   A CD2 
1972 N  N   . PHE   A 271 ? 0.3208 0.6656 0.3211 0.0177  0.0872  0.0634  250 PHE   A N   
1973 C  CA  . PHE   A 271 ? 0.3473 0.6677 0.3531 0.0068  0.0883  0.0844  250 PHE   A CA  
1974 C  C   . PHE   A 271 ? 0.3528 0.6694 0.3506 0.0126  0.0864  0.0786  250 PHE   A C   
1975 O  O   . PHE   A 271 ? 0.3658 0.6836 0.3576 0.0222  0.0847  0.0560  250 PHE   A O   
1976 C  CB  . PHE   A 271 ? 0.2804 0.5603 0.2978 -0.0038 0.0906  0.0878  250 PHE   A CB  
1977 C  CG  . PHE   A 271 ? 0.3667 0.6493 0.3938 -0.0101 0.0918  0.0936  250 PHE   A CG  
1978 C  CD1 . PHE   A 271 ? 0.3369 0.6251 0.3738 -0.0193 0.0905  0.1166  250 PHE   A CD1 
1979 C  CD2 . PHE   A 271 ? 0.3541 0.6356 0.3822 -0.0065 0.0932  0.0762  250 PHE   A CD2 
1980 C  CE1 . PHE   A 271 ? 0.3451 0.6380 0.3928 -0.0253 0.0910  0.1222  250 PHE   A CE1 
1981 C  CE2 . PHE   A 271 ? 0.3514 0.6378 0.3891 -0.0120 0.0942  0.0816  250 PHE   A CE2 
1982 C  CZ  . PHE   A 271 ? 0.3853 0.6777 0.4328 -0.0217 0.0933  0.1046  250 PHE   A CZ  
1983 N  N   . PHE   A 272 ? 0.3460 0.6582 0.3456 0.0071  0.0856  0.0988  251 PHE   A N   
1984 C  CA  . PHE   A 272 ? 0.2909 0.5980 0.2847 0.0112  0.0840  0.0970  251 PHE   A CA  
1985 C  C   . PHE   A 272 ? 0.3640 0.6305 0.3679 0.0012  0.0849  0.1093  251 PHE   A C   
1986 O  O   . PHE   A 272 ? 0.3624 0.6157 0.3769 -0.0083 0.0837  0.1285  251 PHE   A O   
1987 C  CB  . PHE   A 272 ? 0.2842 0.6258 0.2712 0.0159  0.0808  0.1092  251 PHE   A CB  
1988 C  CG  . PHE   A 272 ? 0.3741 0.7592 0.3507 0.0285  0.0785  0.0946  251 PHE   A CG  
1989 C  CD1 . PHE   A 272 ? 0.3993 0.8105 0.3786 0.0278  0.0791  0.1019  251 PHE   A CD1 
1990 C  CD2 . PHE   A 272 ? 0.4223 0.8233 0.3879 0.0418  0.0745  0.0722  251 PHE   A CD2 
1991 C  CE1 . PHE   A 272 ? 0.3567 0.8103 0.3273 0.0409  0.0760  0.0876  251 PHE   A CE1 
1992 C  CE2 . PHE   A 272 ? 0.3466 0.7873 0.3041 0.0552  0.0698  0.0558  251 PHE   A CE2 
1993 C  CZ  . PHE   A 272 ? 0.4329 0.9006 0.3926 0.0550  0.0708  0.0637  251 PHE   A CZ  
1994 N  N   . VAL   A 273 ? 0.3000 0.5404 0.3029 0.0044  0.0824  0.0942  252 VAL   A N   
1995 C  CA  . VAL   A 273 ? 0.2828 0.4795 0.2948 -0.0019 0.0802  0.0978  252 VAL   A CA  
1996 C  C   . VAL   A 273 ? 0.3347 0.5278 0.3443 0.0016  0.0763  0.1007  252 VAL   A C   
1997 O  O   . VAL   A 273 ? 0.3602 0.5656 0.3626 0.0097  0.0734  0.0862  252 VAL   A O   
1998 C  CB  . VAL   A 273 ? 0.2875 0.4545 0.3020 -0.0013 0.0789  0.0775  252 VAL   A CB  
1999 C  CG1 . VAL   A 273 ? 0.3158 0.4445 0.3387 -0.0064 0.0775  0.0812  252 VAL   A CG1 
2000 C  CG2 . VAL   A 273 ? 0.3011 0.4763 0.3167 -0.0026 0.0818  0.0718  252 VAL   A CG2 
2001 N  N   . GLU   A 274 ? 0.3035 0.4794 0.3213 -0.0038 0.0748  0.1184  253 GLU   A N   
2002 C  CA  . GLU   A 274 ? 0.3365 0.5057 0.3544 -0.0003 0.0706  0.1215  253 GLU   A CA  
2003 C  C   . GLU   A 274 ? 0.4100 0.5393 0.4376 -0.0023 0.0681  0.1170  253 GLU   A C   
2004 O  O   . GLU   A 274 ? 0.3632 0.4714 0.3996 -0.0078 0.0681  0.1219  253 GLU   A O   
2005 C  CB  . GLU   A 274 ? 0.3331 0.5219 0.3528 -0.0024 0.0691  0.1473  253 GLU   A CB  
2006 C  CG  . GLU   A 274 ? 0.4063 0.5784 0.4411 -0.0122 0.0678  0.1685  253 GLU   A CG  
2007 C  CD  . GLU   A 274 ? 0.4870 0.6739 0.5278 -0.0152 0.0639  0.1966  253 GLU   A CD  
2008 O  OE1 . GLU   A 274 ? 0.4247 0.6399 0.4550 -0.0090 0.0634  0.1999  253 GLU   A OE1 
2009 O  OE2 . GLU   A 274 ? 0.5058 0.6729 0.5635 -0.0226 0.0579  0.2105  253 GLU   A OE2 
2010 N  N   . GLY   A 275 ? 0.3484 0.4702 0.3748 0.0030  0.0654  0.1068  254 GLY   A N   
2011 C  CA  . GLY   A 275 ? 0.3036 0.3959 0.3387 0.0033  0.0634  0.1042  254 GLY   A CA  
2012 C  C   . GLY   A 275 ? 0.3684 0.4552 0.4111 0.0034  0.0587  0.1212  254 GLY   A C   
2013 O  O   . GLY   A 275 ? 0.3491 0.4560 0.3886 0.0053  0.0566  0.1324  254 GLY   A O   
2014 N  N   . LEU   A 276 ? 0.3689 0.4286 0.4223 0.0025  0.0559  0.1227  255 LEU   A N   
2015 C  CA  . LEU   A 276 ? 0.4016 0.4502 0.4663 0.0036  0.0488  0.1369  255 LEU   A CA  
2016 C  C   . LEU   A 276 ? 0.4289 0.4617 0.4990 0.0114  0.0454  0.1266  255 LEU   A C   
2017 O  O   . LEU   A 276 ? 0.4260 0.4501 0.5060 0.0147  0.0382  0.1361  255 LEU   A O   
2018 C  CB  . LEU   A 276 ? 0.3719 0.4021 0.4496 -0.0026 0.0444  0.1476  255 LEU   A CB  
2019 C  CG  . LEU   A 276 ? 0.3703 0.4153 0.4469 -0.0114 0.0479  0.1583  255 LEU   A CG  
2020 C  CD1 . LEU   A 276 ? 0.4069 0.4308 0.5025 -0.0180 0.0404  0.1706  255 LEU   A CD1 
2021 C  CD2 . LEU   A 276 ? 0.3625 0.4422 0.4315 -0.0129 0.0502  0.1745  255 LEU   A CD2 
2022 N  N   . CYS   A 277 ? 0.3500 0.3807 0.4154 0.0148  0.0500  0.1088  256 CYS   A N   
2023 C  CA  . CYS   A 277 ? 0.3517 0.3703 0.4236 0.0223  0.0481  0.0993  256 CYS   A CA  
2024 C  C   . CYS   A 277 ? 0.3164 0.3474 0.3829 0.0244  0.0535  0.0867  256 CYS   A C   
2025 O  O   . CYS   A 277 ? 0.3196 0.3542 0.3801 0.0202  0.0583  0.0796  256 CYS   A O   
2026 C  CB  . CYS   A 277 ? 0.3825 0.3793 0.4607 0.0236  0.0463  0.0927  256 CYS   A CB  
2027 S  SG  . CYS   A 277 ? 0.5493 0.5365 0.6353 0.0360  0.0434  0.0793  256 CYS   A SG  
2028 N  N   . PHE   A 278 ? 0.3262 0.3639 0.3974 0.0305  0.0515  0.0848  257 PHE   A N   
2029 C  CA  . PHE   A 278 ? 0.3061 0.3555 0.3775 0.0314  0.0552  0.0750  257 PHE   A CA  
2030 C  C   . PHE   A 278 ? 0.3385 0.3804 0.4128 0.0338  0.0593  0.0662  257 PHE   A C   
2031 O  O   . PHE   A 278 ? 0.3163 0.3446 0.3931 0.0382  0.0576  0.0648  257 PHE   A O   
2032 C  CB  . PHE   A 278 ? 0.2564 0.3181 0.3341 0.0369  0.0516  0.0765  257 PHE   A CB  
2033 C  CG  . PHE   A 278 ? 0.3541 0.4311 0.4272 0.0350  0.0482  0.0817  257 PHE   A CG  
2034 C  CD1 . PHE   A 278 ? 0.2797 0.3705 0.3508 0.0317  0.0487  0.0744  257 PHE   A CD1 
2035 C  CD2 . PHE   A 278 ? 0.3525 0.4313 0.4245 0.0372  0.0430  0.0938  257 PHE   A CD2 
2036 C  CE1 . PHE   A 278 ? 0.2912 0.3988 0.3571 0.0322  0.0442  0.0759  257 PHE   A CE1 
2037 C  CE2 . PHE   A 278 ? 0.3651 0.4633 0.4308 0.0369  0.0399  0.0985  257 PHE   A CE2 
2038 C  CZ  . PHE   A 278 ? 0.3501 0.4636 0.4117 0.0353  0.0406  0.0879  257 PHE   A CZ  
2039 N  N   . PRO   A 279 ? 0.2980 0.3499 0.3731 0.0313  0.0636  0.0605  258 PRO   A N   
2040 C  CA  . PRO   A 279 ? 0.3240 0.3772 0.4023 0.0349  0.0679  0.0548  258 PRO   A CA  
2041 C  C   . PRO   A 279 ? 0.3258 0.3837 0.4115 0.0455  0.0661  0.0533  258 PRO   A C   
2042 O  O   . PRO   A 279 ? 0.3172 0.3829 0.4085 0.0483  0.0626  0.0567  258 PRO   A O   
2043 C  CB  . PRO   A 279 ? 0.2852 0.3526 0.3680 0.0291  0.0707  0.0541  258 PRO   A CB  
2044 C  CG  . PRO   A 279 ? 0.2969 0.3630 0.3757 0.0223  0.0674  0.0547  258 PRO   A CG  
2045 C  CD  . PRO   A 279 ? 0.2802 0.3439 0.3549 0.0254  0.0633  0.0592  258 PRO   A CD  
2046 N  N   . ASP   A 280 ? 0.3305 0.3853 0.4162 0.0527  0.0678  0.0469  259 ASP   A N   
2047 C  CA  A ASP   A 280 ? 0.3871 0.4470 0.4799 0.0657  0.0650  0.0420  259 ASP   A CA  
2048 C  CA  B ASP   A 280 ? 0.3932 0.4545 0.4862 0.0656  0.0653  0.0421  259 ASP   A CA  
2049 C  C   . ASP   A 280 ? 0.3613 0.4311 0.4522 0.0733  0.0699  0.0330  259 ASP   A C   
2050 O  O   . ASP   A 280 ? 0.3728 0.4450 0.4572 0.0672  0.0753  0.0330  259 ASP   A O   
2051 C  CB  A ASP   A 280 ? 0.4156 0.4539 0.5113 0.0706  0.0556  0.0426  259 ASP   A CB  
2052 C  CB  B ASP   A 280 ? 0.4127 0.4541 0.5093 0.0710  0.0558  0.0431  259 ASP   A CB  
2053 C  CG  A ASP   A 280 ? 0.3811 0.4246 0.4873 0.0828  0.0497  0.0404  259 ASP   A CG  
2054 C  CG  B ASP   A 280 ? 0.4311 0.4512 0.5253 0.0730  0.0518  0.0376  259 ASP   A CG  
2055 O  OD1 A ASP   A 280 ? 0.3777 0.4415 0.4880 0.0916  0.0535  0.0334  259 ASP   A OD1 
2056 O  OD1 B ASP   A 280 ? 0.4469 0.4655 0.5332 0.0672  0.0569  0.0350  259 ASP   A OD1 
2057 O  OD2 A ASP   A 280 ? 0.3878 0.4171 0.4992 0.0837  0.0410  0.0468  259 ASP   A OD2 
2058 O  OD2 B ASP   A 280 ? 0.4924 0.4965 0.5946 0.0803  0.0421  0.0358  259 ASP   A OD2 
2059 N  N   . GLU   A 281 ? 0.4027 0.4801 0.4992 0.0879  0.0672  0.0247  260 GLU   A N   
2060 C  CA  . GLU   A 281 ? 0.4678 0.5570 0.5608 0.0986  0.0703  0.0136  260 GLU   A CA  
2061 C  C   . GLU   A 281 ? 0.4825 0.5475 0.5674 0.0963  0.0668  0.0082  260 GLU   A C   
2062 O  O   . GLU   A 281 ? 0.5590 0.5976 0.6473 0.0967  0.0573  0.0067  260 GLU   A O   
2063 C  CB  . GLU   A 281 ? 0.4211 0.5199 0.5221 0.1177  0.0650  0.0020  260 GLU   A CB  
2064 C  CG  . GLU   A 281 ? 0.4849 0.6026 0.5812 0.1325  0.0676  -0.0123 260 GLU   A CG  
2065 C  CD  . GLU   A 281 ? 0.5872 0.7463 0.6820 0.1317  0.0804  -0.0063 260 GLU   A CD  
2066 O  OE1 . GLU   A 281 ? 0.6014 0.7723 0.7026 0.1203  0.0853  0.0076  260 GLU   A OE1 
2067 O  OE2 . GLU   A 281 ? 0.7103 0.8920 0.7988 0.1424  0.0847  -0.0149 260 GLU   A OE2 
2068 N  N   . GLY   A 282 ? 0.4689 0.5433 0.5451 0.0929  0.0736  0.0072  261 GLY   A N   
2069 C  CA  . GLY   A 282 ? 0.4915 0.5457 0.5605 0.0911  0.0702  0.0013  261 GLY   A CA  
2070 C  C   . GLY   A 282 ? 0.5321 0.5644 0.5985 0.0750  0.0692  0.0109  261 GLY   A C   
2071 O  O   . GLY   A 282 ? 0.5650 0.5813 0.6272 0.0726  0.0661  0.0069  261 GLY   A O   
2072 N  N   . PHE   A 283 ? 0.4508 0.4844 0.5199 0.0650  0.0711  0.0223  262 PHE   A N   
2073 C  CA  . PHE   A 283 ? 0.3677 0.3895 0.4330 0.0513  0.0715  0.0302  262 PHE   A CA  
2074 C  C   . PHE   A 283 ? 0.3773 0.4154 0.4429 0.0432  0.0773  0.0371  262 PHE   A C   
2075 O  O   . PHE   A 283 ? 0.3711 0.4183 0.4427 0.0429  0.0765  0.0415  262 PHE   A O   
2076 C  CB  . PHE   A 283 ? 0.4170 0.4229 0.4866 0.0481  0.0645  0.0365  262 PHE   A CB  
2077 C  CG  . PHE   A 283 ? 0.3723 0.3750 0.4373 0.0358  0.0660  0.0445  262 PHE   A CG  
2078 C  CD1 . PHE   A 283 ? 0.4151 0.4121 0.4741 0.0299  0.0684  0.0424  262 PHE   A CD1 
2079 C  CD2 . PHE   A 283 ? 0.3238 0.3321 0.3901 0.0316  0.0646  0.0530  262 PHE   A CD2 
2080 C  CE1 . PHE   A 283 ? 0.3800 0.3777 0.4352 0.0207  0.0695  0.0479  262 PHE   A CE1 
2081 C  CE2 . PHE   A 283 ? 0.3280 0.3387 0.3891 0.0229  0.0657  0.0581  262 PHE   A CE2 
2082 C  CZ  . PHE   A 283 ? 0.3244 0.3302 0.3804 0.0178  0.0683  0.0551  262 PHE   A CZ  
2083 N  N   . SER   A 284 ? 0.3703 0.4110 0.4313 0.0367  0.0814  0.0378  263 SER   A N   
2084 C  CA  . SER   A 284 ? 0.3375 0.3920 0.4030 0.0294  0.0845  0.0437  263 SER   A CA  
2085 C  C   . SER   A 284 ? 0.3605 0.4095 0.4277 0.0211  0.0810  0.0469  263 SER   A C   
2086 O  O   . SER   A 284 ? 0.3920 0.4508 0.4666 0.0158  0.0804  0.0501  263 SER   A O   
2087 C  CB  . SER   A 284 ? 0.3639 0.4214 0.4259 0.0257  0.0881  0.0444  263 SER   A CB  
2088 O  OG  . SER   A 284 ? 0.4240 0.4639 0.4791 0.0208  0.0859  0.0417  263 SER   A OG  
2089 N  N   . GLY   A 285 ? 0.3107 0.3465 0.3725 0.0201  0.0777  0.0463  264 GLY   A N   
2090 C  CA  . GLY   A 285 ? 0.2930 0.3289 0.3535 0.0142  0.0749  0.0480  264 GLY   A CA  
2091 C  C   . GLY   A 285 ? 0.3080 0.3371 0.3628 0.0088  0.0752  0.0455  264 GLY   A C   
2092 O  O   . GLY   A 285 ? 0.3682 0.4003 0.4206 0.0059  0.0728  0.0453  264 GLY   A O   
2093 N  N   . LEU   A 286 ? 0.3668 0.3898 0.4191 0.0086  0.0779  0.0431  265 LEU   A N   
2094 C  CA  . LEU   A 286 ? 0.2736 0.2907 0.3217 0.0041  0.0779  0.0403  265 LEU   A CA  
2095 C  C   . LEU   A 286 ? 0.3027 0.3094 0.3458 0.0044  0.0775  0.0402  265 LEU   A C   
2096 O  O   . LEU   A 286 ? 0.3542 0.3536 0.3972 0.0087  0.0773  0.0393  265 LEU   A O   
2097 C  CB  . LEU   A 286 ? 0.3019 0.3196 0.3510 0.0032  0.0800  0.0394  265 LEU   A CB  
2098 C  CG  . LEU   A 286 ? 0.3715 0.3994 0.4306 0.0000  0.0788  0.0426  265 LEU   A CG  
2099 C  CD1 . LEU   A 286 ? 0.2816 0.3129 0.3426 -0.0012 0.0811  0.0462  265 LEU   A CD1 
2100 C  CD2 . LEU   A 286 ? 0.2985 0.3254 0.3616 -0.0043 0.0732  0.0391  265 LEU   A CD2 
2101 N  N   . VAL   A 287 ? 0.3162 0.3240 0.3569 0.0004  0.0764  0.0407  266 VAL   A N   
2102 C  CA  . VAL   A 287 ? 0.3397 0.3409 0.3792 -0.0015 0.0756  0.0433  266 VAL   A CA  
2103 C  C   . VAL   A 287 ? 0.3449 0.3482 0.3816 -0.0052 0.0763  0.0393  266 VAL   A C   
2104 O  O   . VAL   A 287 ? 0.4191 0.4312 0.4551 -0.0058 0.0759  0.0353  266 VAL   A O   
2105 C  CB  . VAL   A 287 ? 0.3523 0.3594 0.3936 -0.0027 0.0737  0.0523  266 VAL   A CB  
2106 C  CG1 . VAL   A 287 ? 0.3671 0.3698 0.4127 0.0018  0.0715  0.0561  266 VAL   A CG1 
2107 C  CG2 . VAL   A 287 ? 0.3295 0.3548 0.3673 -0.0037 0.0740  0.0524  266 VAL   A CG2 
2108 N  N   . SER   A 288 ? 0.3378 0.3328 0.3750 -0.0068 0.0759  0.0390  267 SER   A N   
2109 C  CA  . SER   A 288 ? 0.3485 0.3453 0.3842 -0.0096 0.0763  0.0349  267 SER   A CA  
2110 C  C   . SER   A 288 ? 0.3192 0.3214 0.3582 -0.0137 0.0757  0.0411  267 SER   A C   
2111 O  O   . SER   A 288 ? 0.3850 0.3797 0.4296 -0.0154 0.0733  0.0479  267 SER   A O   
2112 C  CB  . SER   A 288 ? 0.3645 0.3500 0.3987 -0.0080 0.0759  0.0293  267 SER   A CB  
2113 O  OG  . SER   A 288 ? 0.5476 0.5343 0.5800 -0.0056 0.0771  0.0266  267 SER   A OG  
2114 N  N   . ILE   A 289 ? 0.3490 0.3656 0.3865 -0.0152 0.0768  0.0392  268 ILE   A N   
2115 C  CA  . ILE   A 289 ? 0.3295 0.3573 0.3712 -0.0195 0.0773  0.0458  268 ILE   A CA  
2116 C  C   . ILE   A 289 ? 0.3496 0.3779 0.3913 -0.0197 0.0772  0.0373  268 ILE   A C   
2117 O  O   . ILE   A 289 ? 0.3562 0.3858 0.3939 -0.0159 0.0768  0.0273  268 ILE   A O   
2118 C  CB  . ILE   A 289 ? 0.3575 0.4117 0.3974 -0.0193 0.0792  0.0522  268 ILE   A CB  
2119 C  CG1 . ILE   A 289 ? 0.3678 0.4212 0.4069 -0.0181 0.0785  0.0599  268 ILE   A CG1 
2120 C  CG2 . ILE   A 289 ? 0.3424 0.4133 0.3889 -0.0248 0.0805  0.0636  268 ILE   A CG2 
2121 C  CD1 . ILE   A 289 ? 0.3878 0.4700 0.4235 -0.0168 0.0799  0.0672  268 ILE   A CD1 
2122 N  N   . HIS   A 290 ? 0.3322 0.3585 0.3807 -0.0242 0.0762  0.0417  269 HIS   A N   
2123 C  CA  . HIS   A 290 ? 0.3188 0.3441 0.3685 -0.0243 0.0753  0.0340  269 HIS   A CA  
2124 C  C   . HIS   A 290 ? 0.3276 0.3754 0.3842 -0.0284 0.0767  0.0401  269 HIS   A C   
2125 O  O   . HIS   A 290 ? 0.3532 0.4125 0.4167 -0.0335 0.0775  0.0538  269 HIS   A O   
2126 C  CB  . HIS   A 290 ? 0.3991 0.4021 0.4518 -0.0252 0.0714  0.0313  269 HIS   A CB  
2127 C  CG  . HIS   A 290 ? 0.3595 0.3465 0.4063 -0.0205 0.0706  0.0273  269 HIS   A CG  
2128 N  ND1 . HIS   A 290 ? 0.3125 0.2958 0.3517 -0.0160 0.0715  0.0198  269 HIS   A ND1 
2129 C  CD2 . HIS   A 290 ? 0.3047 0.2812 0.3535 -0.0192 0.0686  0.0307  269 HIS   A CD2 
2130 C  CE1 . HIS   A 290 ? 0.3507 0.3254 0.3867 -0.0124 0.0715  0.0195  269 HIS   A CE1 
2131 N  NE2 . HIS   A 290 ? 0.3436 0.3137 0.3848 -0.0134 0.0696  0.0244  269 HIS   A NE2 
2132 N  N   . VAL   A 291 ? 0.3626 0.4188 0.4187 -0.0260 0.0768  0.0310  270 VAL   A N   
2133 C  CA  . VAL   A 291 ? 0.3588 0.4367 0.4233 -0.0295 0.0779  0.0353  270 VAL   A CA  
2134 C  C   . VAL   A 291 ? 0.3880 0.4521 0.4562 -0.0298 0.0743  0.0272  270 VAL   A C   
2135 O  O   . VAL   A 291 ? 0.3699 0.4216 0.4311 -0.0242 0.0723  0.0153  270 VAL   A O   
2136 C  CB  . VAL   A 291 ? 0.2990 0.4096 0.3597 -0.0236 0.0812  0.0302  270 VAL   A CB  
2137 C  CG1 . VAL   A 291 ? 0.2989 0.4022 0.3540 -0.0153 0.0779  0.0119  270 VAL   A CG1 
2138 C  CG2 . VAL   A 291 ? 0.3091 0.4502 0.3799 -0.0277 0.0839  0.0388  270 VAL   A CG2 
2139 N  N   . SER   A 292 ? 0.3451 0.4116 0.4258 -0.0368 0.0723  0.0348  271 SER   A N   
2140 C  CA  . SER   A 292 ? 0.3428 0.3988 0.4281 -0.0371 0.0679  0.0272  271 SER   A CA  
2141 C  C   . SER   A 292 ? 0.3289 0.4119 0.4271 -0.0414 0.0689  0.0320  271 SER   A C   
2142 O  O   . SER   A 292 ? 0.3353 0.4383 0.4444 -0.0483 0.0712  0.0471  271 SER   A O   
2143 C  CB  . SER   A 292 ? 0.4020 0.4311 0.4929 -0.0407 0.0615  0.0284  271 SER   A CB  
2144 O  OG  . SER   A 292 ? 0.4691 0.4769 0.5469 -0.0339 0.0602  0.0188  271 SER   A OG  
2145 N  N   . LEU   A 293 ? 0.3399 0.4255 0.4377 -0.0372 0.0670  0.0208  272 LEU   A N   
2146 C  CA  . LEU   A 293 ? 0.3321 0.4390 0.4447 -0.0415 0.0662  0.0240  272 LEU   A CA  
2147 C  C   . LEU   A 293 ? 0.2992 0.3831 0.4223 -0.0476 0.0584  0.0247  272 LEU   A C   
2148 O  O   . LEU   A 293 ? 0.3277 0.3878 0.4424 -0.0425 0.0537  0.0130  272 LEU   A O   
2149 C  CB  . LEU   A 293 ? 0.2753 0.3971 0.3837 -0.0325 0.0666  0.0100  272 LEU   A CB  
2150 C  CG  . LEU   A 293 ? 0.2969 0.4439 0.4205 -0.0348 0.0658  0.0107  272 LEU   A CG  
2151 C  CD1 . LEU   A 293 ? 0.2851 0.4754 0.4190 -0.0388 0.0726  0.0240  272 LEU   A CD1 
2152 C  CD2 . LEU   A 293 ? 0.3404 0.4896 0.4589 -0.0241 0.0629  -0.0066 272 LEU   A CD2 
2153 N  N   . LEU   A 294 ? 0.2895 0.3815 0.4323 -0.0583 0.0560  0.0391  273 LEU   A N   
2154 C  CA  . LEU   A 294 ? 0.3595 0.4291 0.5166 -0.0644 0.0457  0.0393  273 LEU   A CA  
2155 C  C   . LEU   A 294 ? 0.3789 0.4668 0.5543 -0.0694 0.0423  0.0403  273 LEU   A C   
2156 O  O   . LEU   A 294 ? 0.3596 0.4826 0.5456 -0.0738 0.0481  0.0511  273 LEU   A O   
2157 C  CB  . LEU   A 294 ? 0.3664 0.4267 0.5388 -0.0739 0.0414  0.0553  273 LEU   A CB  
2158 C  CG  . LEU   A 294 ? 0.3747 0.4175 0.5331 -0.0697 0.0436  0.0561  273 LEU   A CG  
2159 C  CD1 . LEU   A 294 ? 0.4498 0.4815 0.6284 -0.0792 0.0361  0.0720  273 LEU   A CD1 
2160 C  CD2 . LEU   A 294 ? 0.3280 0.3428 0.4679 -0.0592 0.0406  0.0372  273 LEU   A CD2 
2161 N  N   . GLU   A 295 ? 0.4176 0.4851 0.5968 -0.0682 0.0328  0.0290  274 GLU   A N   
2162 C  CA  . GLU   A 295 ? 0.4669 0.5487 0.6653 -0.0732 0.0275  0.0287  274 GLU   A CA  
2163 C  C   . GLU   A 295 ? 0.4728 0.5390 0.6972 -0.0840 0.0147  0.0356  274 GLU   A C   
2164 O  O   . GLU   A 295 ? 0.4049 0.4389 0.6252 -0.0808 0.0056  0.0264  274 GLU   A O   
2165 C  CB  . GLU   A 295 ? 0.4239 0.4976 0.6090 -0.0628 0.0244  0.0096  274 GLU   A CB  
2166 C  CG  . GLU   A 295 ? 0.4651 0.5544 0.6708 -0.0673 0.0181  0.0083  274 GLU   A CG  
2167 C  CD  . GLU   A 295 ? 0.5426 0.6261 0.7350 -0.0565 0.0148  -0.0092 274 GLU   A CD  
2168 O  OE1 . GLU   A 295 ? 0.5258 0.6016 0.6949 -0.0460 0.0196  -0.0174 274 GLU   A OE1 
2169 O  OE2 . GLU   A 295 ? 0.6258 0.7128 0.8330 -0.0588 0.0063  -0.0136 274 GLU   A OE2 
2170 N  N   . TYR   A 296 ? 0.4314 0.5223 0.6840 -0.0962 0.0130  0.0515  275 TYR   A N   
2171 C  CA  . TYR   A 296 ? 0.4636 0.5414 0.7483 -0.1085 -0.0017 0.0598  275 TYR   A CA  
2172 C  C   . TYR   A 296 ? 0.5339 0.5993 0.8243 -0.1049 -0.0134 0.0416  275 TYR   A C   
2173 O  O   . TYR   A 296 ? 0.5094 0.5993 0.8040 -0.1045 -0.0105 0.0392  275 TYR   A O   
2174 C  CB  . TYR   A 296 ? 0.4950 0.6089 0.8105 -0.1241 0.0010  0.0870  275 TYR   A CB  
2175 C  CG  . TYR   A 296 ? 0.5170 0.6234 0.8712 -0.1381 -0.0154 0.0968  275 TYR   A CG  
2176 C  CD1 . TYR   A 296 ? 0.5195 0.6411 0.8908 -0.1414 -0.0209 0.0923  275 TYR   A CD1 
2177 C  CD2 . TYR   A 296 ? 0.5265 0.6073 0.8891 -0.1425 -0.0261 0.1066  275 TYR   A CD2 
2178 C  CE1 . TYR   A 296 ? 0.5372 0.6479 0.9327 -0.1494 -0.0362 0.0976  275 TYR   A CE1 
2179 C  CE2 . TYR   A 296 ? 0.5401 0.6099 0.9285 -0.1498 -0.0421 0.1119  275 TYR   A CE2 
2180 C  CZ  . TYR   A 296 ? 0.4884 0.5729 0.8930 -0.1535 -0.0470 0.1076  275 TYR   A CZ  
2181 O  OH  . TYR   A 296 ? 0.6606 0.7340 1.0926 -0.1606 -0.0636 0.1131  275 TYR   A OH  
2182 N  N   . MET   A 297 ? 0.5616 0.5908 0.8512 -0.1009 -0.0272 0.0275  276 MET   A N   
2183 C  CA  . MET   A 297 ? 0.5563 0.5727 0.8493 -0.0958 -0.0402 0.0084  276 MET   A CA  
2184 C  C   . MET   A 297 ? 0.6048 0.6192 0.9402 -0.1097 -0.0573 0.0156  276 MET   A C   
2185 O  O   . MET   A 297 ? 0.6172 0.6440 0.9667 -0.1120 -0.0634 0.0107  276 MET   A O   
2186 C  CB  . MET   A 297 ? 0.6158 0.5999 0.8839 -0.0814 -0.0464 -0.0129 276 MET   A CB  
2187 C  CG  . MET   A 297 ? 0.5489 0.5351 0.7785 -0.0686 -0.0312 -0.0191 276 MET   A CG  
2188 S  SD  . MET   A 297 ? 0.6461 0.6504 0.8585 -0.0598 -0.0255 -0.0301 276 MET   A SD  
2189 C  CE  . MET   A 297 ? 0.6244 0.6370 0.8064 -0.0521 -0.0072 -0.0260 276 MET   A CE  
2190 N  N   . ALA   A 298 ? 0.6377 0.6360 0.9961 -0.1192 -0.0667 0.0278  277 ALA   A N   
2191 C  CA  . ALA   A 298 ? 0.5832 0.5766 0.9776 -0.1303 -0.0836 0.0367  277 ALA   A CA  
2192 C  C   . ALA   A 298 ? 0.6759 0.6470 1.0752 -0.1313 -0.0903 0.0473  277 ALA   A C   
2193 O  O   . ALA   A 298 ? 0.6723 0.6295 1.0531 -0.1251 -0.0847 0.0443  277 ALA   A O   
2194 C  CB  . ALA   A 298 ? 0.5159 0.4903 0.9168 -0.1234 -0.1020 0.0119  277 ALA   A CB  
2195 N  N   . GLN   A 299 ? 0.6524 0.6211 1.0789 -0.1391 -0.1031 0.0603  278 GLN   A N   
2196 C  CA  . GLN   A 299 ? 0.7482 0.6943 1.1859 -0.1391 -0.1142 0.0687  278 GLN   A CA  
2197 C  C   . GLN   A 299 ? 0.7669 0.6759 1.1973 -0.1245 -0.1301 0.0398  278 GLN   A C   
2198 O  O   . GLN   A 299 ? 0.7541 0.6535 1.1857 -0.1174 -0.1414 0.0173  278 GLN   A O   
2199 C  CB  . GLN   A 299 ? 0.8813 0.8337 1.3544 -0.1505 -0.1266 0.0888  278 GLN   A CB  
2200 N  N   . ASP   A 300 ? 0.7774 0.6687 1.1988 -0.1184 -0.1308 0.0395  279 ASP   A N   
2201 C  CA  . ASP   A 300 ? 0.7963 0.6574 1.2082 -0.1025 -0.1440 0.0132  279 ASP   A CA  
2202 C  C   . ASP   A 300 ? 0.7710 0.6295 1.1470 -0.0903 -0.1324 -0.0088 279 ASP   A C   
2203 O  O   . ASP   A 300 ? 0.8201 0.6592 1.1815 -0.0753 -0.1393 -0.0299 279 ASP   A O   
2204 C  CB  . ASP   A 300 ? 0.8560 0.7015 1.2887 -0.0962 -0.1678 -0.0053 279 ASP   A CB  
2205 C  CG  . ASP   A 300 ? 0.8846 0.7335 1.3568 -0.1094 -0.1806 0.0167  279 ASP   A CG  
2206 O  OD1 . ASP   A 300 ? 0.9542 0.8061 1.4391 -0.1179 -0.1785 0.0414  279 ASP   A OD1 
2207 O  OD2 . ASP   A 300 ? 0.8787 0.7284 1.3698 -0.1110 -0.1931 0.0100  279 ASP   A OD2 
2208 N  N   . ILE   A 301 ? 0.6986 0.5783 1.0609 -0.0951 -0.1157 -0.0047 280 ILE   A N   
2209 C  CA  . ILE   A 301 ? 0.6578 0.5357 0.9886 -0.0844 -0.1045 -0.0226 280 ILE   A CA  
2210 C  C   . ILE   A 301 ? 0.7002 0.5898 1.0115 -0.0861 -0.0841 -0.0050 280 ILE   A C   
2211 O  O   . ILE   A 301 ? 0.6927 0.6024 1.0188 -0.1003 -0.0755 0.0207  280 ILE   A O   
2212 C  CB  . ILE   A 301 ? 0.6467 0.5457 0.9641 -0.0820 -0.0971 -0.0303 280 ILE   A CB  
2213 C  CG1 . ILE   A 301 ? 0.6223 0.5121 0.9629 -0.0821 -0.1185 -0.0463 280 ILE   A CG1 
2214 C  CG2 . ILE   A 301 ? 0.6283 0.5305 0.9000 -0.0643 -0.0835 -0.0464 280 ILE   A CG2 
2215 C  CD1 . ILE   A 301 ? 0.6358 0.5041 0.9585 -0.0627 -0.1315 -0.0762 280 ILE   A CD1 
2216 N  N   . PRO   A 302 ? 0.7157 0.5977 0.9937 -0.0713 -0.0758 -0.0175 281 PRO   A N   
2217 C  CA  . PRO   A 302 ? 0.6526 0.5481 0.9103 -0.0718 -0.0564 -0.0025 281 PRO   A CA  
2218 C  C   . PRO   A 302 ? 0.5899 0.5147 0.8304 -0.0734 -0.0388 0.0038  281 PRO   A C   
2219 O  O   . PRO   A 302 ? 0.6241 0.5551 0.8543 -0.0677 -0.0386 -0.0094 281 PRO   A O   
2220 C  CB  . PRO   A 302 ? 0.7208 0.6012 0.9496 -0.0546 -0.0545 -0.0207 281 PRO   A CB  
2221 C  CG  . PRO   A 302 ? 0.6707 0.5436 0.8917 -0.0429 -0.0650 -0.0457 281 PRO   A CG  
2222 C  CD  . PRO   A 302 ? 0.7009 0.5657 0.9587 -0.0529 -0.0838 -0.0456 281 PRO   A CD  
2223 N  N   . LEU   A 303 ? 0.6179 0.5621 0.8561 -0.0803 -0.0251 0.0234  282 LEU   A N   
2224 C  CA  . LEU   A 303 ? 0.5670 0.5399 0.7894 -0.0795 -0.0095 0.0269  282 LEU   A CA  
2225 C  C   . LEU   A 303 ? 0.5194 0.4869 0.7068 -0.0646 -0.0013 0.0103  282 LEU   A C   
2226 O  O   . LEU   A 303 ? 0.5081 0.4606 0.6807 -0.0575 0.0001  0.0056  282 LEU   A O   
2227 C  CB  . LEU   A 303 ? 0.5602 0.5580 0.7873 -0.0880 0.0020  0.0497  282 LEU   A CB  
2228 C  CG  . LEU   A 303 ? 0.5402 0.5538 0.8030 -0.1045 -0.0036 0.0726  282 LEU   A CG  
2229 C  CD1 . LEU   A 303 ? 0.6248 0.6103 0.9104 -0.1107 -0.0186 0.0798  282 LEU   A CD1 
2230 C  CD2 . LEU   A 303 ? 0.4635 0.5155 0.7245 -0.1098 0.0112  0.0932  282 LEU   A CD2 
2231 N  N   . THR   A 304 ? 0.4379 0.6324 0.6645 -0.1294 0.0511  -0.0062 283 THR   A N   
2232 C  CA  . THR   A 304 ? 0.4491 0.6235 0.6551 -0.1082 0.0532  -0.0219 283 THR   A CA  
2233 C  C   . THR   A 304 ? 0.4013 0.5892 0.5947 -0.0994 0.0660  -0.0222 283 THR   A C   
2234 O  O   . THR   A 304 ? 0.3552 0.5846 0.5587 -0.1005 0.0735  -0.0219 283 THR   A O   
2235 C  CB  . THR   A 304 ? 0.4490 0.6355 0.6618 -0.0982 0.0481  -0.0357 283 THR   A CB  
2236 O  OG1 . THR   A 304 ? 0.5644 0.7377 0.7881 -0.1053 0.0351  -0.0373 283 THR   A OG1 
2237 C  CG2 . THR   A 304 ? 0.3562 0.5219 0.5485 -0.0790 0.0479  -0.0471 283 THR   A CG2 
2238 N  N   . PRO   A 305 ? 0.3971 0.5549 0.5696 -0.0901 0.0681  -0.0242 284 PRO   A N   
2239 C  CA  . PRO   A 305 ? 0.3730 0.5409 0.5345 -0.0800 0.0776  -0.0272 284 PRO   A CA  
2240 C  C   . PRO   A 305 ? 0.3529 0.5262 0.5136 -0.0637 0.0746  -0.0418 284 PRO   A C   
2241 O  O   . PRO   A 305 ? 0.4559 0.6009 0.6042 -0.0547 0.0686  -0.0466 284 PRO   A O   
2242 C  CB  . PRO   A 305 ? 0.3405 0.4722 0.4823 -0.0774 0.0783  -0.0233 284 PRO   A CB  
2243 C  CG  . PRO   A 305 ? 0.3988 0.5045 0.5423 -0.0850 0.0690  -0.0200 284 PRO   A CG  
2244 C  CD  . PRO   A 305 ? 0.3587 0.4757 0.5177 -0.0877 0.0611  -0.0253 284 PRO   A CD  
2245 N  N   . ILE   A 306 ? 0.3400 0.5522 0.5150 -0.0596 0.0772  -0.0489 285 ILE   A N   
2246 C  CA  . ILE   A 306 ? 0.3681 0.5836 0.5460 -0.0427 0.0706  -0.0641 285 ILE   A CA  
2247 C  C   . ILE   A 306 ? 0.3692 0.5795 0.5375 -0.0293 0.0720  -0.0710 285 ILE   A C   
2248 O  O   . ILE   A 306 ? 0.3572 0.5577 0.5263 -0.0150 0.0624  -0.0817 285 ILE   A O   
2249 C  CB  . ILE   A 306 ? 0.3842 0.6452 0.5852 -0.0415 0.0695  -0.0729 285 ILE   A CB  
2250 C  CG1 . ILE   A 306 ? 0.2557 0.5645 0.4651 -0.0412 0.0798  -0.0756 285 ILE   A CG1 
2251 C  CG2 . ILE   A 306 ? 0.3658 0.6334 0.5790 -0.0577 0.0672  -0.0642 285 ILE   A CG2 
2252 C  CD1 . ILE   A 306 ? 0.3311 0.6852 0.5584 -0.0394 0.0780  -0.0821 285 ILE   A CD1 
2253 N  N   . PHE   A 307 ? 0.3660 0.5809 0.5264 -0.0336 0.0815  -0.0646 286 PHE   A N   
2254 C  CA  . PHE   A 307 ? 0.3329 0.5396 0.4838 -0.0219 0.0818  -0.0709 286 PHE   A CA  
2255 C  C   . PHE   A 307 ? 0.3191 0.5146 0.4559 -0.0313 0.0911  -0.0580 286 PHE   A C   
2256 O  O   . PHE   A 307 ? 0.2861 0.5033 0.4265 -0.0442 0.0991  -0.0479 286 PHE   A O   
2257 C  CB  . PHE   A 307 ? 0.2922 0.5416 0.4569 -0.0094 0.0823  -0.0874 286 PHE   A CB  
2258 C  CG  . PHE   A 307 ? 0.3052 0.5478 0.4620 0.0024  0.0813  -0.0954 286 PHE   A CG  
2259 C  CD1 . PHE   A 307 ? 0.3963 0.6104 0.5529 0.0171  0.0671  -0.1057 286 PHE   A CD1 
2260 C  CD2 . PHE   A 307 ? 0.3562 0.6105 0.5014 -0.0020 0.0894  -0.0879 286 PHE   A CD2 
2261 C  CE1 . PHE   A 307 ? 0.4040 0.6091 0.5560 0.0272  0.0633  -0.1132 286 PHE   A CE1 
2262 C  CE2 . PHE   A 307 ? 0.3237 0.5697 0.4612 0.0088  0.0865  -0.0957 286 PHE   A CE2 
2263 C  CZ  . PHE   A 307 ? 0.3407 0.5676 0.4861 0.0240  0.0753  -0.1117 286 PHE   A CZ  
2264 N  N   . THR   A 308 ? 0.3349 0.4979 0.4568 -0.0258 0.0887  -0.0569 287 THR   A N   
2265 C  CA  . THR   A 308 ? 0.3454 0.4955 0.4537 -0.0325 0.0960  -0.0462 287 THR   A CA  
2266 C  C   . THR   A 308 ? 0.3685 0.5104 0.4695 -0.0213 0.0943  -0.0529 287 THR   A C   
2267 O  O   . THR   A 308 ? 0.3605 0.4790 0.4588 -0.0130 0.0847  -0.0575 287 THR   A O   
2268 C  CB  . THR   A 308 ? 0.3126 0.4276 0.4097 -0.0401 0.0940  -0.0357 287 THR   A CB  
2269 O  OG1 . THR   A 308 ? 0.3477 0.4684 0.4539 -0.0502 0.0928  -0.0311 287 THR   A OG1 
2270 C  CG2 . THR   A 308 ? 0.2994 0.4013 0.3841 -0.0451 0.1000  -0.0265 287 THR   A CG2 
2271 N  N   . ASP   A 309 ? 0.3941 0.5560 0.4926 -0.0222 0.1022  -0.0524 288 ASP   A N   
2272 C  CA  . ASP   A 309 ? 0.3601 0.5133 0.4511 -0.0131 0.1006  -0.0581 288 ASP   A CA  
2273 C  C   . ASP   A 309 ? 0.3259 0.4581 0.3997 -0.0214 0.1042  -0.0417 288 ASP   A C   
2274 O  O   . ASP   A 309 ? 0.3658 0.5018 0.4353 -0.0305 0.1059  -0.0276 288 ASP   A O   
2275 C  CB  . ASP   A 309 ? 0.3840 0.5695 0.4791 -0.0024 0.0977  -0.0691 288 ASP   A CB  
2276 C  CG  . ASP   A 309 ? 0.3477 0.5262 0.4450 0.0122  0.0906  -0.0854 288 ASP   A CG  
2277 O  OD1 . ASP   A 309 ? 0.3879 0.5310 0.4843 0.0146  0.0823  -0.0851 288 ASP   A OD1 
2278 O  OD2 . ASP   A 309 ? 0.2990 0.4981 0.3948 0.0203  0.0874  -0.0933 288 ASP   A OD2 
2279 N  N   . THR   A 310 ? 0.3303 0.4403 0.3971 -0.0178 0.1036  -0.0436 289 THR   A N   
2280 C  CA  . THR   A 310 ? 0.3755 0.4639 0.4270 -0.0234 0.1041  -0.0299 289 THR   A CA  
2281 C  C   . THR   A 310 ? 0.3677 0.4551 0.4142 -0.0167 0.1034  -0.0346 289 THR   A C   
2282 O  O   . THR   A 310 ? 0.3226 0.4064 0.3759 -0.0080 0.0987  -0.0471 289 THR   A O   
2283 C  CB  . THR   A 310 ? 0.3332 0.3925 0.3793 -0.0278 0.1036  -0.0244 289 THR   A CB  
2284 O  OG1 . THR   A 310 ? 0.3636 0.4230 0.4132 -0.0344 0.1035  -0.0203 289 THR   A OG1 
2285 C  CG2 . THR   A 310 ? 0.3501 0.3915 0.3824 -0.0295 0.1012  -0.0151 289 THR   A CG2 
2286 N  N   . VAL   A 311 ? 0.3508 0.4387 0.3869 -0.0194 0.1032  -0.0241 290 VAL   A N   
2287 C  CA  . VAL   A 311 ? 0.2974 0.3816 0.3273 -0.0147 0.1024  -0.0265 290 VAL   A CA  
2288 C  C   . VAL   A 311 ? 0.4073 0.4704 0.4267 -0.0206 0.1002  -0.0137 290 VAL   A C   
2289 O  O   . VAL   A 311 ? 0.3652 0.4255 0.3826 -0.0267 0.0987  -0.0038 290 VAL   A O   
2290 C  CB  . VAL   A 311 ? 0.3200 0.4319 0.3492 -0.0094 0.1037  -0.0286 290 VAL   A CB  
2291 C  CG1 . VAL   A 311 ? 0.3140 0.4502 0.3545 -0.0007 0.1024  -0.0459 290 VAL   A CG1 
2292 C  CG2 . VAL   A 311 ? 0.2965 0.4166 0.3223 -0.0169 0.1062  -0.0113 290 VAL   A CG2 
2293 N  N   . ILE   A 312 ? 0.3503 0.3996 0.3656 -0.0184 0.0994  -0.0158 291 ILE   A N   
2294 C  CA  . ILE   A 312 ? 0.3850 0.4187 0.3919 -0.0216 0.0961  -0.0067 291 ILE   A CA  
2295 C  C   . ILE   A 312 ? 0.3660 0.4073 0.3689 -0.0188 0.0960  -0.0069 291 ILE   A C   
2296 O  O   . ILE   A 312 ? 0.3878 0.4379 0.3936 -0.0133 0.0985  -0.0169 291 ILE   A O   
2297 C  CB  . ILE   A 312 ? 0.3861 0.4000 0.3918 -0.0229 0.0952  -0.0059 291 ILE   A CB  
2298 C  CG1 . ILE   A 312 ? 0.4345 0.4435 0.4417 -0.0257 0.0946  -0.0040 291 ILE   A CG1 
2299 C  CG2 . ILE   A 312 ? 0.4749 0.4807 0.4736 -0.0235 0.0916  0.0000  291 ILE   A CG2 
2300 C  CD1 . ILE   A 312 ? 0.6487 0.6465 0.6520 -0.0274 0.0928  0.0000  291 ILE   A CD1 
2301 N  N   . PHE   A 313 ? 0.3689 0.4081 0.3665 -0.0216 0.0932  0.0017  292 PHE   A N   
2302 C  CA  . PHE   A 313 ? 0.3440 0.3883 0.3370 -0.0196 0.0928  0.0030  292 PHE   A CA  
2303 C  C   . PHE   A 313 ? 0.3184 0.3446 0.3080 -0.0211 0.0897  0.0063  292 PHE   A C   
2304 O  O   . PHE   A 313 ? 0.3285 0.3446 0.3180 -0.0234 0.0878  0.0097  292 PHE   A O   
2305 C  CB  . PHE   A 313 ? 0.3355 0.3990 0.3271 -0.0218 0.0934  0.0117  292 PHE   A CB  
2306 C  CG  . PHE   A 313 ? 0.3442 0.4320 0.3388 -0.0170 0.0985  0.0108  292 PHE   A CG  
2307 C  CD1 . PHE   A 313 ? 0.3626 0.4601 0.3542 -0.0088 0.1029  0.0035  292 PHE   A CD1 
2308 C  CD2 . PHE   A 313 ? 0.3236 0.4191 0.3240 -0.0201 0.1010  0.0160  292 PHE   A CD2 
2309 C  CE1 . PHE   A 313 ? 0.3515 0.4648 0.3447 -0.0067 0.1086  -0.0036 292 PHE   A CE1 
2310 C  CE2 . PHE   A 313 ? 0.3093 0.4195 0.3125 -0.0170 0.1087  0.0122  292 PHE   A CE2 
2311 C  CZ  . PHE   A 313 ? 0.2992 0.4211 0.2982 -0.0117 0.1110  0.0004  292 PHE   A CZ  
2312 N  N   . ARG   A 314 ? 0.3466 0.3710 0.3339 -0.0188 0.0899  0.0041  293 ARG   A N   
2313 C  CA  . ARG   A 314 ? 0.3251 0.3406 0.3096 -0.0196 0.0873  0.0080  293 ARG   A CA  
2314 C  C   . ARG   A 314 ? 0.3517 0.3764 0.3325 -0.0195 0.0874  0.0116  293 ARG   A C   
2315 O  O   . ARG   A 314 ? 0.3423 0.3794 0.3215 -0.0171 0.0896  0.0087  293 ARG   A O   
2316 C  CB  . ARG   A 314 ? 0.3440 0.3518 0.3295 -0.0194 0.0880  0.0058  293 ARG   A CB  
2317 C  CG  . ARG   A 314 ? 0.3567 0.3625 0.3400 -0.0198 0.0854  0.0099  293 ARG   A CG  
2318 C  CD  . ARG   A 314 ? 0.3639 0.3670 0.3495 -0.0222 0.0857  0.0112  293 ARG   A CD  
2319 N  NE  . ARG   A 314 ? 0.4389 0.4413 0.4266 -0.0252 0.0840  0.0145  293 ARG   A NE  
2320 C  CZ  . ARG   A 314 ? 0.3931 0.4022 0.3793 -0.0247 0.0817  0.0168  293 ARG   A CZ  
2321 N  NH1 . ARG   A 314 ? 0.3787 0.3904 0.3625 -0.0214 0.0819  0.0152  293 ARG   A NH1 
2322 N  NH2 . ARG   A 314 ? 0.3931 0.4073 0.3804 -0.0278 0.0806  0.0205  293 ARG   A NH2 
2323 N  N   . ILE   A 315 ? 0.3735 0.3926 0.3528 -0.0219 0.0863  0.0172  294 ILE   A N   
2324 C  CA  . ILE   A 315 ? 0.3449 0.3697 0.3204 -0.0234 0.0870  0.0225  294 ILE   A CA  
2325 C  C   . ILE   A 315 ? 0.2915 0.3141 0.2649 -0.0201 0.0868  0.0195  294 ILE   A C   
2326 O  O   . ILE   A 315 ? 0.3078 0.3213 0.2829 -0.0186 0.0859  0.0171  294 ILE   A O   
2327 C  CB  . ILE   A 315 ? 0.3518 0.3651 0.3273 -0.0277 0.0880  0.0296  294 ILE   A CB  
2328 C  CG1 . ILE   A 315 ? 0.3915 0.4107 0.3700 -0.0337 0.0881  0.0354  294 ILE   A CG1 
2329 C  CG2 . ILE   A 315 ? 0.3547 0.3672 0.3256 -0.0296 0.0890  0.0367  294 ILE   A CG2 
2330 C  CD1 . ILE   A 315 ? 0.4832 0.4875 0.4635 -0.0405 0.0886  0.0453  294 ILE   A CD1 
2331 N  N   . ALA   A 316 ? 0.3480 0.3831 0.3177 -0.0192 0.0881  0.0198  295 ALA   A N   
2332 C  CA  . ALA   A 316 ? 0.3268 0.3609 0.2949 -0.0163 0.0886  0.0161  295 ALA   A CA  
2333 C  C   . ALA   A 316 ? 0.3160 0.3407 0.2829 -0.0168 0.0883  0.0203  295 ALA   A C   
2334 O  O   . ALA   A 316 ? 0.3727 0.3946 0.3366 -0.0192 0.0893  0.0269  295 ALA   A O   
2335 C  CB  . ALA   A 316 ? 0.3125 0.3648 0.2755 -0.0138 0.0911  0.0140  295 ALA   A CB  
2336 N  N   . PRO   A 317 ? 0.2887 0.3092 0.2581 -0.0151 0.0880  0.0174  296 PRO   A N   
2337 C  CA  . PRO   A 317 ? 0.3487 0.3652 0.3177 -0.0138 0.0893  0.0195  296 PRO   A CA  
2338 C  C   . PRO   A 317 ? 0.3282 0.3487 0.2919 -0.0125 0.0913  0.0221  296 PRO   A C   
2339 O  O   . PRO   A 317 ? 0.3485 0.3777 0.3088 -0.0125 0.0915  0.0204  296 PRO   A O   
2340 C  CB  . PRO   A 317 ? 0.2838 0.3037 0.2581 -0.0139 0.0883  0.0167  296 PRO   A CB  
2341 C  CG  . PRO   A 317 ? 0.3176 0.3387 0.2934 -0.0158 0.0882  0.0146  296 PRO   A CG  
2342 C  CD  . PRO   A 317 ? 0.2684 0.2883 0.2419 -0.0153 0.0881  0.0132  296 PRO   A CD  
2343 N  N   . TRP   A 318 ? 0.3089 0.3234 0.2712 -0.0100 0.0944  0.0256  297 TRP   A N   
2344 C  CA  . TRP   A 318 ? 0.3543 0.3713 0.3111 -0.0074 0.0967  0.0295  297 TRP   A CA  
2345 C  C   . TRP   A 318 ? 0.3154 0.3410 0.2766 -0.0051 0.0968  0.0236  297 TRP   A C   
2346 O  O   . TRP   A 318 ? 0.3425 0.3712 0.3108 -0.0039 0.0972  0.0202  297 TRP   A O   
2347 C  CB  . TRP   A 318 ? 0.3697 0.3750 0.3265 -0.0037 0.0950  0.0361  297 TRP   A CB  
2348 C  CG  . TRP   A 318 ? 0.3857 0.3935 0.3394 -0.0006 0.0887  0.0405  297 TRP   A CG  
2349 C  CD1 . TRP   A 318 ? 0.4019 0.4145 0.3467 -0.0044 0.0867  0.0504  297 TRP   A CD1 
2350 C  CD2 . TRP   A 318 ? 0.3824 0.3922 0.3422 0.0069  0.0831  0.0356  297 TRP   A CD2 
2351 N  NE1 . TRP   A 318 ? 0.4427 0.4567 0.3867 0.0002  0.0795  0.0528  297 TRP   A NE1 
2352 C  CE2 . TRP   A 318 ? 0.4465 0.4579 0.4006 0.0076  0.0770  0.0430  297 TRP   A CE2 
2353 C  CE3 . TRP   A 318 ? 0.3907 0.4064 0.3603 0.0133  0.0828  0.0255  297 TRP   A CE3 
2354 C  CZ2 . TRP   A 318 ? 0.4725 0.4866 0.4313 0.0151  0.0697  0.0400  297 TRP   A CZ2 
2355 C  CZ3 . TRP   A 318 ? 0.4589 0.4815 0.4338 0.0209  0.0764  0.0217  297 TRP   A CZ3 
2356 C  CH2 . TRP   A 318 ? 0.4466 0.4662 0.4167 0.0220  0.0696  0.0286  297 TRP   A CH2 
2357 N  N   . ILE   A 319 ? 0.3127 0.3459 0.2702 -0.0049 0.0969  0.0224  298 ILE   A N   
2358 C  CA  . ILE   A 319 ? 0.3202 0.3609 0.2840 -0.0047 0.0956  0.0176  298 ILE   A CA  
2359 C  C   . ILE   A 319 ? 0.3565 0.4034 0.3186 -0.0003 0.0907  0.0181  298 ILE   A C   
2360 O  O   . ILE   A 319 ? 0.3801 0.4288 0.3327 0.0015  0.0890  0.0210  298 ILE   A O   
2361 C  CB  . ILE   A 319 ? 0.3257 0.3682 0.2915 -0.0074 0.0936  0.0116  298 ILE   A CB  
2362 C  CG1 . ILE   A 319 ? 0.3221 0.3578 0.2902 -0.0110 0.0962  0.0112  298 ILE   A CG1 
2363 C  CG2 . ILE   A 319 ? 0.3139 0.3611 0.2907 -0.0099 0.0873  0.0086  298 ILE   A CG2 
2364 C  CD1 . ILE   A 319 ? 0.3055 0.3410 0.2758 -0.0109 0.0927  0.0032  298 ILE   A CD1 
2365 N  N   . MET   A 320 ? 0.3962 0.4505 0.3674 0.0010  0.0883  0.0162  299 MET   A N   
2366 C  CA  . MET   A 320 ? 0.3684 0.4304 0.3405 0.0056  0.0826  0.0155  299 MET   A CA  
2367 C  C   . MET   A 320 ? 0.3466 0.4167 0.3232 0.0026  0.0780  0.0107  299 MET   A C   
2368 O  O   . MET   A 320 ? 0.3585 0.4288 0.3429 -0.0035 0.0774  0.0086  299 MET   A O   
2369 C  CB  . MET   A 320 ? 0.3365 0.4071 0.3182 0.0100  0.0816  0.0140  299 MET   A CB  
2370 C  CG  . MET   A 320 ? 0.4410 0.5015 0.4209 0.0163  0.0809  0.0152  299 MET   A CG  
2371 S  SD  . MET   A 320 ? 0.5590 0.6366 0.5524 0.0257  0.0779  0.0069  299 MET   A SD  
2372 C  CE  . MET   A 320 ? 0.4160 0.5101 0.4146 0.0276  0.0725  0.0055  299 MET   A CE  
2373 N  N   . THR   A 321 ? 0.3396 0.4155 0.3126 0.0069  0.0724  0.0093  300 THR   A N   
2374 C  CA  . THR   A 321 ? 0.3333 0.4159 0.3100 0.0058  0.0655  0.0025  300 THR   A CA  
2375 C  C   . THR   A 321 ? 0.3758 0.4700 0.3643 0.0060  0.0599  0.0016  300 THR   A C   
2376 O  O   . THR   A 321 ? 0.3666 0.4658 0.3517 0.0122  0.0580  0.0035  300 THR   A O   
2377 C  CB  . THR   A 321 ? 0.3637 0.4500 0.3260 0.0108  0.0629  -0.0002 300 THR   A CB  
2378 O  OG1 . THR   A 321 ? 0.4107 0.4989 0.3642 0.0152  0.0627  0.0079  300 THR   A OG1 
2379 C  CG2 . THR   A 321 ? 0.3491 0.4320 0.3026 0.0098  0.0681  -0.0013 300 THR   A CG2 
2380 N  N   . PRO   A 322 ? 0.3555 0.4552 0.3592 -0.0014 0.0556  0.0001  301 PRO   A N   
2381 C  CA  . PRO   A 322 ? 0.3332 0.4493 0.3502 -0.0031 0.0500  0.0002  301 PRO   A CA  
2382 C  C   . PRO   A 322 ? 0.3914 0.5099 0.4062 0.0014  0.0403  -0.0067 301 PRO   A C   
2383 O  O   . PRO   A 322 ? 0.3833 0.4941 0.3880 0.0050  0.0369  -0.0131 301 PRO   A O   
2384 C  CB  . PRO   A 322 ? 0.3245 0.4456 0.3590 -0.0160 0.0468  0.0043  301 PRO   A CB  
2385 C  CG  . PRO   A 322 ? 0.3488 0.4503 0.3792 -0.0187 0.0448  0.0017  301 PRO   A CG  
2386 C  CD  . PRO   A 322 ? 0.3588 0.4505 0.3701 -0.0099 0.0542  0.0001  301 PRO   A CD  
2387 N  N   . ASN   A 323 ? 0.4455 0.5798 0.4706 0.0019  0.0355  -0.0065 302 ASN   A N   
2388 C  CA  . ASN   A 323 ? 0.4200 0.5599 0.4438 0.0070  0.0256  -0.0131 302 ASN   A CA  
2389 C  C   . ASN   A 323 ? 0.4554 0.5903 0.4872 0.0020  0.0140  -0.0214 302 ASN   A C   
2390 O  O   . ASN   A 323 ? 0.4269 0.5655 0.4546 0.0080  0.0050  -0.0302 302 ASN   A O   
2391 C  CB  . ASN   A 323 ? 0.4241 0.5841 0.4610 0.0079  0.0224  -0.0114 302 ASN   A CB  
2392 C  CG  . ASN   A 323 ? 0.4461 0.6105 0.4771 0.0170  0.0290  -0.0078 302 ASN   A CG  
2393 O  OD1 . ASN   A 323 ? 0.5286 0.6784 0.5431 0.0236  0.0326  -0.0056 302 ASN   A OD1 
2394 N  ND2 . ASN   A 323 ? 0.5025 0.6890 0.5487 0.0176  0.0290  -0.0075 302 ASN   A ND2 
2395 N  N   . ILE   A 324 ? 0.3834 0.5102 0.4279 -0.0083 0.0115  -0.0195 303 ILE   A N   
2396 C  CA  . ILE   A 324 ? 0.4339 0.5511 0.4896 -0.0119 -0.0041 -0.0291 303 ILE   A CA  
2397 C  C   . ILE   A 324 ? 0.4852 0.5908 0.5254 -0.0021 -0.0053 -0.0418 303 ILE   A C   
2398 O  O   . ILE   A 324 ? 0.5114 0.6104 0.5596 -0.0002 -0.0204 -0.0555 303 ILE   A O   
2399 C  CB  . ILE   A 324 ? 0.4003 0.5112 0.4779 -0.0278 -0.0106 -0.0202 303 ILE   A CB  
2400 C  CG1 . ILE   A 324 ? 0.3707 0.4716 0.4409 -0.0302 0.0008  -0.0132 303 ILE   A CG1 
2401 C  CG2 . ILE   A 324 ? 0.3628 0.4955 0.4581 -0.0391 -0.0109 -0.0076 303 ILE   A CG2 
2402 C  CD1 . ILE   A 324 ? 0.4478 0.5271 0.5171 -0.0278 -0.0075 -0.0232 303 ILE   A CD1 
2403 N  N   . LEU   A 325 ? 0.4588 0.5643 0.4785 0.0044  0.0088  -0.0387 304 LEU   A N   
2404 C  CA  . LEU   A 325 ? 0.4208 0.5241 0.4264 0.0129  0.0090  -0.0500 304 LEU   A CA  
2405 C  C   . LEU   A 325 ? 0.4813 0.6013 0.4719 0.0238  0.0054  -0.0592 304 LEU   A C   
2406 O  O   . LEU   A 325 ? 0.4679 0.5971 0.4509 0.0256  0.0094  -0.0508 304 LEU   A O   
2407 C  CB  . LEU   A 325 ? 0.3873 0.4863 0.3792 0.0129  0.0244  -0.0408 304 LEU   A CB  
2408 C  CG  . LEU   A 325 ? 0.4000 0.4844 0.4041 0.0038  0.0269  -0.0347 304 LEU   A CG  
2409 C  CD1 . LEU   A 325 ? 0.3635 0.4445 0.3547 0.0040  0.0417  -0.0260 304 LEU   A CD1 
2410 C  CD2 . LEU   A 325 ? 0.4481 0.5224 0.4637 0.0038  0.0135  -0.0480 304 LEU   A CD2 
2411 N  N   . PRO   A 326 ? 0.4862 0.6128 0.4727 0.0320  -0.0032 -0.0771 305 PRO   A N   
2412 C  CA  . PRO   A 326 ? 0.4627 0.6118 0.4348 0.0426  -0.0081 -0.0874 305 PRO   A CA  
2413 C  C   . PRO   A 326 ? 0.4862 0.6497 0.4346 0.0445  0.0060  -0.0722 305 PRO   A C   
2414 O  O   . PRO   A 326 ? 0.4878 0.6500 0.4262 0.0425  0.0177  -0.0635 305 PRO   A O   
2415 C  CB  . PRO   A 326 ? 0.4863 0.6442 0.4572 0.0526  -0.0171 -0.1110 305 PRO   A CB  
2416 C  CG  . PRO   A 326 ? 0.5693 0.7011 0.5624 0.0462  -0.0244 -0.1146 305 PRO   A CG  
2417 C  CD  . PRO   A 326 ? 0.4924 0.6092 0.4870 0.0337  -0.0096 -0.0903 305 PRO   A CD  
2418 N  N   . PRO   A 327 ? 0.4851 0.6612 0.4255 0.0474  0.0034  -0.0672 306 PRO   A N   
2419 C  CA  . PRO   A 327 ? 0.5013 0.6881 0.4212 0.0478  0.0127  -0.0497 306 PRO   A CA  
2420 C  C   . PRO   A 327 ? 0.5301 0.7459 0.4285 0.0540  0.0146  -0.0548 306 PRO   A C   
2421 O  O   . PRO   A 327 ? 0.5317 0.7682 0.4272 0.0626  0.0056  -0.0743 306 PRO   A O   
2422 C  CB  . PRO   A 327 ? 0.4440 0.6347 0.3657 0.0496  0.0055  -0.0445 306 PRO   A CB  
2423 C  CG  . PRO   A 327 ? 0.4311 0.6276 0.3653 0.0536  -0.0083 -0.0650 306 PRO   A CG  
2424 C  CD  . PRO   A 327 ? 0.4802 0.6596 0.4323 0.0493  -0.0100 -0.0754 306 PRO   A CD  
2425 N  N   . VAL   A 328 ? 0.5135 0.7338 0.3977 0.0496  0.0255  -0.0375 307 VAL   A N   
2426 C  CA  . VAL   A 328 ? 0.5717 0.8276 0.4344 0.0525  0.0292  -0.0362 307 VAL   A CA  
2427 C  C   . VAL   A 328 ? 0.5320 0.8051 0.3774 0.0507  0.0272  -0.0165 307 VAL   A C   
2428 O  O   . VAL   A 328 ? 0.6663 0.9750 0.4969 0.0567  0.0223  -0.0225 307 VAL   A O   
2429 C  CB  . VAL   A 328 ? 0.5919 0.8467 0.4512 0.0466  0.0410  -0.0277 307 VAL   A CB  
2430 C  CG1 . VAL   A 328 ? 0.6201 0.9109 0.4626 0.0449  0.0443  -0.0182 307 VAL   A CG1 
2431 C  CG2 . VAL   A 328 ? 0.5802 0.8255 0.4542 0.0507  0.0404  -0.0500 307 VAL   A CG2 
2432 N  N   . SER   A 329 ? 0.6048 0.8537 0.4528 0.0432  0.0290  0.0066  308 SER   A N   
2433 C  CA  . SER   A 329 ? 0.6450 0.9035 0.4795 0.0406  0.0238  0.0285  308 SER   A CA  
2434 C  C   . SER   A 329 ? 0.5580 0.7798 0.4069 0.0383  0.0195  0.0407  308 SER   A C   
2435 O  O   . SER   A 329 ? 0.4852 0.6796 0.3487 0.0354  0.0247  0.0400  308 SER   A O   
2436 C  CB  . SER   A 329 ? 0.7413 1.0222 0.5577 0.0321  0.0295  0.0502  308 SER   A CB  
2437 O  OG  . SER   A 329 ? 0.6596 0.9206 0.4839 0.0252  0.0387  0.0556  308 SER   A OG  
2438 N  N   . VAL   A 330 ? 0.5914 0.8161 0.4364 0.0408  0.0091  0.0503  309 VAL   A N   
2439 C  CA  . VAL   A 330 ? 0.5761 0.7719 0.4359 0.0423  0.0020  0.0579  309 VAL   A CA  
2440 C  C   . VAL   A 330 ? 0.6166 0.8036 0.4680 0.0364  -0.0044 0.0862  309 VAL   A C   
2441 O  O   . VAL   A 330 ? 0.5737 0.7832 0.4074 0.0336  -0.0105 0.1014  309 VAL   A O   
2442 C  CB  . VAL   A 330 ? 0.5460 0.7490 0.4120 0.0505  -0.0082 0.0465  309 VAL   A CB  
2443 C  CG1 . VAL   A 330 ? 0.5858 0.7641 0.4702 0.0541  -0.0149 0.0502  309 VAL   A CG1 
2444 C  CG2 . VAL   A 330 ? 0.5025 0.7153 0.3771 0.0542  -0.0055 0.0204  309 VAL   A CG2 
2445 N  N   . PHE   A 331 ? 0.6020 0.7578 0.4670 0.0343  -0.0048 0.0937  310 PHE   A N   
2446 C  CA  . PHE   A 331 ? 0.6367 0.7752 0.5001 0.0292  -0.0158 0.1196  310 PHE   A CA  
2447 C  C   . PHE   A 331 ? 0.6148 0.7339 0.4926 0.0387  -0.0308 0.1187  310 PHE   A C   
2448 O  O   . PHE   A 331 ? 0.6389 0.7462 0.5350 0.0469  -0.0287 0.1000  310 PHE   A O   
2449 C  CB  . PHE   A 331 ? 0.6799 0.7954 0.5510 0.0224  -0.0102 0.1263  310 PHE   A CB  
2450 C  CG  . PHE   A 331 ? 0.7797 0.8892 0.6429 0.0108  -0.0194 0.1569  310 PHE   A CG  
2451 C  CD1 . PHE   A 331 ? 0.8949 0.9789 0.7663 0.0118  -0.0393 0.1740  310 PHE   A CD1 
2452 C  CD2 . PHE   A 331 ? 0.8066 0.9370 0.6561 -0.0015 -0.0099 0.1691  310 PHE   A CD2 
2453 C  CE1 . PHE   A 331 ? 0.9080 0.9837 0.7748 -0.0015 -0.0513 0.2056  310 PHE   A CE1 
2454 C  CE2 . PHE   A 331 ? 0.9589 1.0870 0.8028 -0.0154 -0.0193 0.2009  310 PHE   A CE2 
2455 C  CZ  . PHE   A 331 ? 0.9227 1.0214 0.7756 -0.0165 -0.0408 0.2207  310 PHE   A CZ  
2456 N  N   . VAL   A 332 ? 0.6026 0.7222 0.4728 0.0375  -0.0468 0.1392  311 VAL   A N   
2457 C  CA  . VAL   A 332 ? 0.6831 0.7879 0.5664 0.0481  -0.0639 0.1381  311 VAL   A CA  
2458 C  C   . VAL   A 332 ? 0.6848 0.7623 0.5717 0.0441  -0.0835 0.1647  311 VAL   A C   
2459 O  O   . VAL   A 332 ? 0.6854 0.7714 0.5559 0.0314  -0.0889 0.1919  311 VAL   A O   
2460 C  CB  . VAL   A 332 ? 0.6826 0.8152 0.5548 0.0528  -0.0693 0.1348  311 VAL   A CB  
2461 C  CG1 . VAL   A 332 ? 0.6298 0.7473 0.5144 0.0630  -0.0901 0.1388  311 VAL   A CG1 
2462 C  CG2 . VAL   A 332 ? 0.6634 0.8156 0.5394 0.0582  -0.0553 0.1061  311 VAL   A CG2 
2463 N  N   . CYS   A 333 ? 0.7224 0.7695 0.6322 0.0547  -0.0955 0.1568  312 CYS   A N   
2464 C  CA  . CYS   A 333 ? 0.7564 0.7717 0.6759 0.0548  -0.1207 0.1778  312 CYS   A CA  
2465 C  C   . CYS   A 333 ? 0.7797 0.7887 0.7129 0.0708  -0.1398 0.1695  312 CYS   A C   
2466 O  O   . CYS   A 333 ? 0.7415 0.7588 0.6886 0.0848  -0.1333 0.1414  312 CYS   A O   
2467 C  CB  . CYS   A 333 ? 0.8571 0.8397 0.7951 0.0562  -0.1232 0.1728  312 CYS   A CB  
2468 S  SG  . CYS   A 333 ? 0.9116 0.8804 0.8800 0.0798  -0.1272 0.1368  312 CYS   A SG  
2469 N  N   . CYS   A 334 ? 0.7990 0.7959 0.7289 0.0680  -0.1641 0.1953  313 CYS   A N   
2470 C  CA  . CYS   A 334 ? 0.8208 0.8087 0.7650 0.0838  -0.1866 0.1899  313 CYS   A CA  
2471 C  C   . CYS   A 334 ? 0.9139 0.8822 0.8528 0.0749  -0.2156 0.2272  313 CYS   A C   
2472 O  O   . CYS   A 334 ? 0.9791 0.9429 0.9051 0.0558  -0.2169 0.2566  313 CYS   A O   
2473 C  CB  . CYS   A 334 ? 0.7783 0.8027 0.7145 0.0910  -0.1755 0.1723  313 CYS   A CB  
2474 S  SG  . CYS   A 334 ? 0.8443 0.9070 0.7448 0.0753  -0.1692 0.1954  313 CYS   A SG  
2475 N  N   . MET   A 335 ? 0.9262 0.8845 0.8765 0.0880  -0.2399 0.2273  314 MET   A N   
2476 C  CA  . MET   A 335 ? 0.9912 0.9322 0.9380 0.0794  -0.2628 0.2565  314 MET   A CA  
2477 C  C   . MET   A 335 ? 0.9670 0.9464 0.8836 0.0678  -0.2552 0.2742  314 MET   A C   
2478 O  O   . MET   A 335 ? 0.8870 0.9040 0.7898 0.0717  -0.2416 0.2632  314 MET   A O   
2479 C  CB  . MET   A 335 ? 1.0061 0.9192 0.9807 0.0990  -0.2883 0.2427  314 MET   A CB  
2480 C  CG  . MET   A 335 ? 1.0563 0.9307 1.0603 0.1082  -0.2981 0.2262  314 MET   A CG  
2481 S  SD  . MET   A 335 ? 1.5415 1.3946 1.5389 0.0824  -0.2918 0.2505  314 MET   A SD  
2482 C  CE  . MET   A 335 ? 1.0870 0.9340 1.0730 0.0613  -0.3083 0.2885  314 MET   A CE  
2483 N  N   . LYS   A 336 ? 0.9547 0.9264 0.8630 0.0529  -0.2650 0.3006  315 LYS   A N   
2484 C  CA  . LYS   A 336 ? 0.9837 0.9942 0.8622 0.0391  -0.2560 0.3182  315 LYS   A CA  
2485 C  C   . LYS   A 336 ? 0.9925 1.0225 0.8649 0.0532  -0.2649 0.3098  315 LYS   A C   
2486 O  O   . LYS   A 336 ? 1.0159 1.0865 0.8628 0.0467  -0.2534 0.3135  315 LYS   A O   
2487 C  CB  . LYS   A 336 ? 1.0836 1.0821 0.9599 0.0181  -0.2663 0.3501  315 LYS   A CB  
2488 C  CG  . LYS   A 336 ? 1.1795 1.1505 1.0705 0.0055  -0.2648 0.3575  315 LYS   A CG  
2489 C  CD  . LYS   A 336 ? 1.2898 1.2378 1.1919 -0.0119 -0.2856 0.3866  315 LYS   A CD  
2490 C  CE  . LYS   A 336 ? 1.2668 1.1829 1.1892 -0.0221 -0.2889 0.3898  315 LYS   A CE  
2491 N  NZ  . LYS   A 336 ? 1.1996 1.0912 1.1378 -0.0399 -0.3138 0.4175  315 LYS   A NZ  
2492 N  N   . ASP   A 337 ? 0.9821 0.9873 0.8791 0.0730  -0.2848 0.2957  316 ASP   A N   
2493 C  CA  . ASP   A 337 ? 0.9302 0.9528 0.8256 0.0872  -0.2954 0.2871  316 ASP   A CA  
2494 C  C   . ASP   A 337 ? 0.8941 0.9347 0.8018 0.1063  -0.2894 0.2548  316 ASP   A C   
2495 O  O   . ASP   A 337 ? 0.9646 1.0184 0.8782 0.1204  -0.2997 0.2428  316 ASP   A O   
2496 C  CB  . ASP   A 337 ? 0.8684 0.8567 0.7849 0.0952  -0.3235 0.2945  316 ASP   A CB  
2497 C  CG  . ASP   A 337 ? 0.8430 0.7950 0.7965 0.1125  -0.3351 0.2717  316 ASP   A CG  
2498 O  OD1 . ASP   A 337 ? 0.8853 0.8291 0.8467 0.1125  -0.3230 0.2593  316 ASP   A OD1 
2499 O  OD2 . ASP   A 337 ? 0.8392 0.7727 0.8140 0.1265  -0.3563 0.2643  316 ASP   A OD2 
2500 N  N   . ASN   A 338 ? 0.8678 0.9111 0.7814 0.1061  -0.2736 0.2407  317 ASN   A N   
2501 C  CA  . ASN   A 338 ? 0.8559 0.9205 0.7808 0.1198  -0.2529 0.2003  317 ASN   A CA  
2502 C  C   . ASN   A 338 ? 0.8400 0.9504 0.7380 0.1116  -0.2325 0.1964  317 ASN   A C   
2503 O  O   . ASN   A 338 ? 0.8493 0.9772 0.7369 0.1036  -0.2070 0.1857  317 ASN   A O   
2504 C  CB  . ASN   A 338 ? 0.8002 0.8500 0.7409 0.1213  -0.2348 0.1798  317 ASN   A CB  
2505 C  CG  . ASN   A 338 ? 0.8661 0.9278 0.8303 0.1385  -0.2246 0.1412  317 ASN   A CG  
2506 O  OD1 . ASN   A 338 ? 0.9631 1.0522 0.9273 0.1452  -0.2222 0.1274  317 ASN   A OD1 
2507 N  ND2 . ASN   A 338 ? 0.8765 0.9210 0.8614 0.1453  -0.2193 0.1242  317 ASN   A ND2 
2508 N  N   . TYR   A 339 ? 0.8240 0.9541 0.7117 0.1153  -0.2465 0.2038  318 TYR   A N   
2509 C  CA  . TYR   A 339 ? 0.8184 0.9935 0.6786 0.1084  -0.2328 0.2023  318 TYR   A CA  
2510 C  C   . TYR   A 339 ? 0.7770 0.9740 0.6470 0.1172  -0.2131 0.1634  318 TYR   A C   
2511 O  O   . TYR   A 339 ? 0.7734 0.9966 0.6279 0.1101  -0.1930 0.1532  318 TYR   A O   
2512 C  CB  . TYR   A 339 ? 0.9264 1.1157 0.7727 0.1097  -0.2554 0.2219  318 TYR   A CB  
2513 C  CG  . TYR   A 339 ? 0.9142 1.0751 0.7493 0.0964  -0.2673 0.2535  318 TYR   A CG  
2514 C  CD1 . TYR   A 339 ? 0.9703 1.1288 0.7912 0.0778  -0.2529 0.2705  318 TYR   A CD1 
2515 C  CD2 . TYR   A 339 ? 0.8785 1.0188 0.7200 0.1030  -0.2917 0.2655  318 TYR   A CD2 
2516 C  CE1 . TYR   A 339 ? 0.9393 1.0780 0.7544 0.0640  -0.2627 0.2999  318 TYR   A CE1 
2517 C  CE2 . TYR   A 339 ? 0.9041 1.0228 0.7389 0.0900  -0.3015 0.2953  318 TYR   A CE2 
2518 C  CZ  . TYR   A 339 ? 0.9630 1.0817 0.7854 0.0695  -0.2871 0.3130  318 TYR   A CZ  
2519 O  OH  . TYR   A 339 ? 1.0132 1.1145 0.8331 0.0539  -0.2976 0.3439  318 TYR   A OH  
2520 N  N   . LEU   A 340 ? 0.7655 0.9542 0.6630 0.1326  -0.2202 0.1414  319 LEU   A N   
2521 C  CA  . LEU   A 340 ? 0.7938 1.0041 0.7039 0.1381  -0.2038 0.1082  319 LEU   A CA  
2522 C  C   . LEU   A 340 ? 0.7486 0.9549 0.6617 0.1302  -0.1792 0.0959  319 LEU   A C   
2523 O  O   . LEU   A 340 ? 0.7447 0.9732 0.6516 0.1255  -0.1633 0.0801  319 LEU   A O   
2524 C  CB  . LEU   A 340 ? 0.7435 0.9489 0.6858 0.1545  -0.2152 0.0892  319 LEU   A CB  
2525 C  CG  . LEU   A 340 ? 0.8695 1.0816 0.8137 0.1651  -0.2401 0.0955  319 LEU   A CG  
2526 C  CD1 . LEU   A 340 ? 0.9383 1.1460 0.9180 0.1827  -0.2507 0.0750  319 LEU   A CD1 
2527 C  CD2 . LEU   A 340 ? 0.9056 1.1539 0.8322 0.1622  -0.2370 0.0892  319 LEU   A CD2 
2528 N  N   . PHE   A 341 ? 0.7427 0.9194 0.6667 0.1292  -0.1780 0.1023  320 PHE   A N   
2529 C  CA  . PHE   A 341 ? 0.6829 0.8548 0.6094 0.1217  -0.1559 0.0924  320 PHE   A CA  
2530 C  C   . PHE   A 341 ? 0.6765 0.8631 0.5743 0.1074  -0.1426 0.1033  320 PHE   A C   
2531 O  O   . PHE   A 341 ? 0.5599 0.7617 0.4555 0.1032  -0.1248 0.0865  320 PHE   A O   
2532 C  CB  . PHE   A 341 ? 0.6641 0.8018 0.6056 0.1240  -0.1605 0.0986  320 PHE   A CB  
2533 C  CG  . PHE   A 341 ? 0.6471 0.7788 0.5900 0.1160  -0.1392 0.0908  320 PHE   A CG  
2534 C  CD1 . PHE   A 341 ? 0.5386 0.6804 0.5000 0.1201  -0.1249 0.0656  320 PHE   A CD1 
2535 C  CD2 . PHE   A 341 ? 0.6248 0.7433 0.5513 0.1034  -0.1342 0.1105  320 PHE   A CD2 
2536 C  CE1 . PHE   A 341 ? 0.5431 0.6794 0.5054 0.1126  -0.1067 0.0599  320 PHE   A CE1 
2537 C  CE2 . PHE   A 341 ? 0.6435 0.7567 0.5719 0.0968  -0.1155 0.1029  320 PHE   A CE2 
2538 C  CZ  . PHE   A 341 ? 0.5627 0.6835 0.5085 0.1018  -0.1021 0.0774  320 PHE   A CZ  
2539 N  N   . LEU   A 342 ? 0.6787 0.8636 0.5557 0.0997  -0.1524 0.1319  321 LEU   A N   
2540 C  CA  . LEU   A 342 ? 0.6760 0.8839 0.5255 0.0867  -0.1400 0.1428  321 LEU   A CA  
2541 C  C   . LEU   A 342 ? 0.6740 0.9210 0.5105 0.0894  -0.1333 0.1243  321 LEU   A C   
2542 O  O   . LEU   A 342 ? 0.6464 0.9108 0.4751 0.0853  -0.1166 0.1102  321 LEU   A O   
2543 C  CB  . LEU   A 342 ? 0.7090 0.9158 0.5394 0.0765  -0.1545 0.1805  321 LEU   A CB  
2544 C  CG  . LEU   A 342 ? 0.7347 0.9065 0.5733 0.0680  -0.1571 0.2001  321 LEU   A CG  
2545 C  CD1 . LEU   A 342 ? 0.8348 1.0002 0.6610 0.0572  -0.1786 0.2409  321 LEU   A CD1 
2546 C  CD2 . LEU   A 342 ? 0.7476 0.9294 0.5779 0.0580  -0.1333 0.1940  321 LEU   A CD2 
2547 N  N   . LYS   A 343 ? 0.6300 0.8907 0.4656 0.0974  -0.1481 0.1225  322 LYS   A N   
2548 C  CA  . LYS   A 343 ? 0.6913 0.9891 0.5156 0.1012  -0.1454 0.1036  322 LYS   A CA  
2549 C  C   . LYS   A 343 ? 0.6407 0.9383 0.4840 0.1045  -0.1315 0.0708  322 LYS   A C   
2550 O  O   . LYS   A 343 ? 0.6668 0.9865 0.4999 0.1024  -0.1216 0.0556  322 LYS   A O   
2551 C  CB  . LYS   A 343 ? 0.7076 1.0154 0.5329 0.1103  -0.1653 0.1059  322 LYS   A CB  
2552 C  CG  . LYS   A 343 ? 0.7726 1.1214 0.5829 0.1144  -0.1667 0.0892  322 LYS   A CG  
2553 C  CD  . LYS   A 343 ? 0.9325 1.2893 0.7457 0.1236  -0.1874 0.0918  322 LYS   A CD  
2554 C  CE  . LYS   A 343 ? 0.9163 1.2486 0.7650 0.1329  -0.1926 0.0758  322 LYS   A CE  
2555 N  NZ  . LYS   A 343 ? 0.9571 1.2927 0.8109 0.1425  -0.2149 0.0822  322 LYS   A NZ  
2556 N  N   . GLU   A 344 ? 0.6148 0.8896 0.4871 0.1097  -0.1322 0.0598  323 GLU   A N   
2557 C  CA  . GLU   A 344 ? 0.6040 0.8811 0.4967 0.1104  -0.1216 0.0329  323 GLU   A CA  
2558 C  C   . GLU   A 344 ? 0.5885 0.8558 0.4797 0.1019  -0.1037 0.0294  323 GLU   A C   
2559 O  O   . GLU   A 344 ? 0.5703 0.8465 0.4674 0.0997  -0.0960 0.0100  323 GLU   A O   
2560 C  CB  . GLU   A 344 ? 0.5509 0.8157 0.4744 0.1173  -0.1268 0.0245  323 GLU   A CB  
2561 C  CG  . GLU   A 344 ? 0.6832 0.9618 0.6125 0.1269  -0.1447 0.0224  323 GLU   A CG  
2562 C  CD  . GLU   A 344 ? 0.6577 0.9258 0.6152 0.1361  -0.1525 0.0188  323 GLU   A CD  
2563 O  OE1 . GLU   A 344 ? 0.6106 0.8618 0.5820 0.1355  -0.1441 0.0180  323 GLU   A OE1 
2564 O  OE2 . GLU   A 344 ? 0.7388 1.0187 0.7049 0.1451  -0.1675 0.0154  323 GLU   A OE2 
2565 N  N   . VAL   A 345 ? 0.5766 0.8243 0.4617 0.0969  -0.0990 0.0479  324 VAL   A N   
2566 C  CA  . VAL   A 345 ? 0.5614 0.8022 0.4428 0.0888  -0.0826 0.0456  324 VAL   A CA  
2567 C  C   . VAL   A 345 ? 0.5544 0.8224 0.4104 0.0848  -0.0777 0.0450  324 VAL   A C   
2568 O  O   . VAL   A 345 ? 0.5475 0.8209 0.4039 0.0820  -0.0665 0.0299  324 VAL   A O   
2569 C  CB  . VAL   A 345 ? 0.5576 0.7708 0.4409 0.0846  -0.0806 0.0649  324 VAL   A CB  
2570 C  CG1 . VAL   A 345 ? 0.5478 0.7579 0.4239 0.0757  -0.0643 0.0648  324 VAL   A CG1 
2571 C  CG2 . VAL   A 345 ? 0.5045 0.6966 0.4156 0.0913  -0.0838 0.0574  324 VAL   A CG2 
2572 N  N   . LYS   A 346 ? 0.6056 0.8941 0.4393 0.0849  -0.0871 0.0608  325 LYS   A N   
2573 C  CA  . LYS   A 346 ? 0.5734 0.8994 0.3821 0.0832  -0.0831 0.0574  325 LYS   A CA  
2574 C  C   . LYS   A 346 ? 0.6244 0.9704 0.4388 0.0914  -0.0850 0.0256  325 LYS   A C   
2575 O  O   . LYS   A 346 ? 0.6612 1.0231 0.4710 0.0919  -0.0773 0.0077  325 LYS   A O   
2576 C  CB  . LYS   A 346 ? 0.5806 0.9302 0.3643 0.0807  -0.0941 0.0836  325 LYS   A CB  
2577 N  N   . ASN   A 347 ? 0.6265 0.9714 0.4533 0.0984  -0.0974 0.0173  326 ASN   A N   
2578 C  CA  . ASN   A 347 ? 0.6596 1.0184 0.4976 0.1049  -0.1024 -0.0127 326 ASN   A CA  
2579 C  C   . ASN   A 347 ? 0.7189 1.0585 0.5787 0.1014  -0.0928 -0.0312 326 ASN   A C   
2580 O  O   . ASN   A 347 ? 0.7299 1.0823 0.5907 0.1039  -0.0934 -0.0539 326 ASN   A O   
2581 C  CB  . ASN   A 347 ? 0.6672 1.0229 0.5213 0.1108  -0.1166 -0.0160 326 ASN   A CB  
2582 C  CG  . ASN   A 347 ? 0.8226 1.2025 0.6550 0.1158  -0.1298 -0.0028 326 ASN   A CG  
2583 O  OD1 . ASN   A 347 ? 0.8518 1.2591 0.6558 0.1149  -0.1290 0.0054  326 ASN   A OD1 
2584 N  ND2 . ASN   A 347 ? 0.8746 1.2486 0.7206 0.1211  -0.1426 -0.0004 326 ASN   A ND2 
2585 N  N   . LEU   A 348 ? 0.6389 0.9482 0.5173 0.0961  -0.0857 -0.0223 327 LEU   A N   
2586 C  CA  . LEU   A 348 ? 0.5991 0.8913 0.4983 0.0910  -0.0772 -0.0358 327 LEU   A CA  
2587 C  C   . LEU   A 348 ? 0.6339 0.9302 0.5193 0.0881  -0.0670 -0.0404 327 LEU   A C   
2588 O  O   . LEU   A 348 ? 0.6630 0.9606 0.5581 0.0883  -0.0678 -0.0609 327 LEU   A O   
2589 C  CB  . LEU   A 348 ? 0.6138 0.8803 0.5315 0.0868  -0.0708 -0.0240 327 LEU   A CB  
2590 C  CG  . LEU   A 348 ? 0.6161 0.8667 0.5541 0.0797  -0.0610 -0.0325 327 LEU   A CG  
2591 C  CD1 . LEU   A 348 ? 0.5590 0.8156 0.5214 0.0780  -0.0689 -0.0499 327 LEU   A CD1 
2592 C  CD2 . LEU   A 348 ? 0.5046 0.7363 0.4530 0.0774  -0.0534 -0.0193 327 LEU   A CD2 
2593 N  N   . VAL   A 349 ? 0.6214 0.9202 0.4860 0.0851  -0.0593 -0.0211 328 VAL   A N   
2594 C  CA  . VAL   A 349 ? 0.6247 0.9319 0.4769 0.0823  -0.0489 -0.0245 328 VAL   A CA  
2595 C  C   . VAL   A 349 ? 0.6878 1.0320 0.5248 0.0899  -0.0542 -0.0443 328 VAL   A C   
2596 O  O   . VAL   A 349 ? 0.6648 1.0177 0.4998 0.0913  -0.0488 -0.0591 328 VAL   A O   
2597 C  CB  . VAL   A 349 ? 0.5745 0.8795 0.4096 0.0754  -0.0409 0.0033  328 VAL   A CB  
2598 C  CG1 . VAL   A 349 ? 0.6418 0.9676 0.4616 0.0731  -0.0308 -0.0003 328 VAL   A CG1 
2599 C  CG2 . VAL   A 349 ? 0.5587 0.8258 0.4115 0.0699  -0.0358 0.0159  328 VAL   A CG2 
2600 N  N   . GLU   A 350 ? 0.6899 1.0583 0.5168 0.0965  -0.0660 -0.0469 329 GLU   A N   
2601 C  CA  . GLU   A 350 ? 0.7390 1.1474 0.5515 0.1062  -0.0729 -0.0694 329 GLU   A CA  
2602 C  C   . GLU   A 350 ? 0.7508 1.1512 0.5866 0.1128  -0.0832 -0.1031 329 GLU   A C   
2603 O  O   . GLU   A 350 ? 0.8010 1.2266 0.6322 0.1218  -0.0882 -0.1277 329 GLU   A O   
2604 C  CB  . GLU   A 350 ? 0.7343 1.1704 0.5297 0.1100  -0.0819 -0.0592 329 GLU   A CB  
2605 C  CG  . GLU   A 350 ? 0.8397 1.2904 0.6156 0.1016  -0.0723 -0.0290 329 GLU   A CG  
2606 C  CD  . GLU   A 350 ? 0.9389 1.4068 0.7037 0.1021  -0.0812 -0.0142 329 GLU   A CD  
2607 O  OE1 . GLU   A 350 ? 0.9703 1.4459 0.7410 0.1110  -0.0928 -0.0326 329 GLU   A OE1 
2608 O  OE2 . GLU   A 350 ? 1.1132 1.5853 0.8649 0.0925  -0.0780 0.0163  329 GLU   A OE2 
2609 N  N   . LYS   A 351 ? 0.7527 1.1190 0.6168 0.1080  -0.0871 -0.1041 330 LYS   A N   
2610 C  CA  . LYS   A 351 ? 0.6878 1.0404 0.5781 0.1094  -0.0970 -0.1307 330 LYS   A CA  
2611 C  C   . LYS   A 351 ? 0.6952 1.0345 0.5917 0.1068  -0.0892 -0.1393 330 LYS   A C   
2612 O  O   . LYS   A 351 ? 0.7399 1.0704 0.6557 0.1093  -0.1005 -0.1632 330 LYS   A O   
2613 C  CB  . LYS   A 351 ? 0.6183 0.9437 0.5379 0.1016  -0.1016 -0.1246 330 LYS   A CB  
2614 C  CG  . LYS   A 351 ? 0.5809 0.9190 0.4997 0.1054  -0.1118 -0.1198 330 LYS   A CG  
2615 C  CD  . LYS   A 351 ? 0.6595 0.9768 0.6065 0.0973  -0.1125 -0.1103 330 LYS   A CD  
2616 C  CE  . LYS   A 351 ? 0.7177 1.0488 0.6634 0.1024  -0.1220 -0.1041 330 LYS   A CE  
2617 N  NZ  . LYS   A 351 ? 0.6966 1.0148 0.6681 0.0963  -0.1208 -0.0939 330 LYS   A NZ  
2618 N  N   . THR   A 352 ? 0.6600 0.9962 0.5422 0.1016  -0.0726 -0.1203 331 THR   A N   
2619 C  CA  . THR   A 352 ? 0.7158 1.0389 0.6034 0.0985  -0.0638 -0.1252 331 THR   A CA  
2620 C  C   . THR   A 352 ? 0.7317 1.0899 0.5919 0.1047  -0.0562 -0.1276 331 THR   A C   
2621 O  O   . THR   A 352 ? 0.7930 1.1873 0.6298 0.1099  -0.0574 -0.1232 331 THR   A O   
2622 C  CB  . THR   A 352 ? 0.6931 0.9834 0.5905 0.0861  -0.0505 -0.1013 331 THR   A CB  
2623 O  OG1 . THR   A 352 ? 0.6748 0.9743 0.5495 0.0831  -0.0383 -0.0773 331 THR   A OG1 
2624 C  CG2 . THR   A 352 ? 0.5983 0.8692 0.5164 0.0807  -0.0559 -0.0936 331 THR   A CG2 
2625 N  N   . ASN   A 353 ? 0.6808 1.0320 0.5447 0.1034  -0.0485 -0.1334 332 ASN   A N   
2626 C  CA  . ASN   A 353 ? 0.7589 1.1444 0.6032 0.1078  -0.0394 -0.1352 332 ASN   A CA  
2627 C  C   . ASN   A 353 ? 0.7712 1.1531 0.6016 0.0958  -0.0220 -0.1023 332 ASN   A C   
2628 O  O   . ASN   A 353 ? 0.7969 1.1939 0.6258 0.0936  -0.0125 -0.0970 332 ASN   A O   
2629 C  CB  . ASN   A 353 ? 0.8768 1.2557 0.7393 0.1142  -0.0432 -0.1615 332 ASN   A CB  
2630 C  CG  . ASN   A 353 ? 0.9458 1.2778 0.8300 0.1062  -0.0444 -0.1615 332 ASN   A CG  
2631 O  OD1 . ASN   A 353 ? 0.8993 1.2073 0.8068 0.1062  -0.0590 -0.1741 332 ASN   A OD1 
2632 N  ND2 . ASN   A 353 ? 0.9233 1.2398 0.8057 0.0968  -0.0290 -0.1426 332 ASN   A ND2 
2633 N  N   . CYS   A 354 ? 0.6684 1.0222 0.5016 0.0863  -0.0191 -0.0775 333 CYS   A N   
2634 C  CA  . CYS   A 354 ? 0.6764 1.0155 0.5037 0.0749  -0.0061 -0.0485 333 CYS   A CA  
2635 C  C   . CYS   A 354 ? 0.6447 1.0138 0.4465 0.0711  -0.0043 -0.0236 333 CYS   A C   
2636 O  O   . CYS   A 354 ? 0.6384 1.0268 0.4332 0.0751  -0.0131 -0.0226 333 CYS   A O   
2637 C  CB  . CYS   A 354 ? 0.6226 0.9171 0.4698 0.0680  -0.0059 -0.0357 333 CYS   A CB  
2638 S  SG  . CYS   A 354 ? 0.7207 0.9854 0.5988 0.0689  -0.0110 -0.0588 333 CYS   A SG  
2639 N  N   . GLU   A 355 ? 0.6666 1.0305 0.4657 0.0605  0.0060  -0.0014 334 GLU   A N   
2640 C  CA  . GLU   A 355 ? 0.6835 1.0571 0.4721 0.0509  0.0057  0.0292  334 GLU   A CA  
2641 C  C   . GLU   A 355 ? 0.6404 0.9839 0.4264 0.0469  -0.0001 0.0523  334 GLU   A C   
2642 O  O   . GLU   A 355 ? 0.6404 0.9438 0.4471 0.0469  0.0016  0.0466  334 GLU   A O   
2643 C  CB  . GLU   A 355 ? 0.8120 1.1915 0.6028 0.0402  0.0156  0.0429  334 GLU   A CB  
2644 C  CG  . GLU   A 355 ? 0.9610 1.3452 0.7441 0.0270  0.0133  0.0771  334 GLU   A CG  
2645 C  CD  . GLU   A 355 ? 1.0365 1.4067 0.8256 0.0144  0.0207  0.0943  334 GLU   A CD  
2646 O  OE1 . GLU   A 355 ? 1.0310 1.3749 0.8287 0.0153  0.0270  0.0856  334 GLU   A OE1 
2647 O  OE2 . GLU   A 355 ? 1.0851 1.4716 0.8713 0.0030  0.0195  0.1166  334 GLU   A OE2 
2648 N  N   . LEU   A 356 ? 0.6764 1.0266 0.4540 0.0420  -0.0083 0.0757  335 LEU   A N   
2649 C  CA  . LEU   A 356 ? 0.6247 0.9422 0.4069 0.0386  -0.0178 0.0989  335 LEU   A CA  
2650 C  C   . LEU   A 356 ? 0.6787 0.9910 0.4557 0.0240  -0.0186 0.1322  335 LEU   A C   
2651 O  O   . LEU   A 356 ? 0.6896 1.0286 0.4598 0.0167  -0.0181 0.1413  335 LEU   A O   
2652 C  CB  . LEU   A 356 ? 0.5705 0.8939 0.3506 0.0460  -0.0322 0.0984  335 LEU   A CB  
2653 C  CG  . LEU   A 356 ? 0.5453 0.8310 0.3385 0.0453  -0.0449 0.1166  335 LEU   A CG  
2654 C  CD1 . LEU   A 356 ? 0.5991 0.8433 0.4192 0.0487  -0.0405 0.1028  335 LEU   A CD1 
2655 C  CD2 . LEU   A 356 ? 0.5345 0.8322 0.3249 0.0537  -0.0590 0.1133  335 LEU   A CD2 
2656 N  N   . LYS   A 357 ? 0.6892 0.9631 0.4772 0.0194  -0.0205 0.1468  336 LYS   A N   
2657 C  CA  . LYS   A 357 ? 0.6544 0.9130 0.4435 0.0051  -0.0257 0.1780  336 LYS   A CA  
2658 C  C   . LYS   A 357 ? 0.6844 0.9027 0.4856 0.0078  -0.0436 0.1936  336 LYS   A C   
2659 O  O   . LYS   A 357 ? 0.6752 0.8601 0.4974 0.0168  -0.0426 0.1748  336 LYS   A O   
2660 C  CB  . LYS   A 357 ? 0.7346 0.9821 0.5315 -0.0027 -0.0128 0.1766  336 LYS   A CB  
2661 C  CG  . LYS   A 357 ? 0.8411 1.0707 0.6442 -0.0184 -0.0192 0.2049  336 LYS   A CG  
2662 C  CD  . LYS   A 357 ? 0.7959 1.0586 0.5910 -0.0285 -0.0223 0.2192  336 LYS   A CD  
2663 C  CE  . LYS   A 357 ? 0.8034 1.0497 0.6072 -0.0453 -0.0307 0.2481  336 LYS   A CE  
2664 N  NZ  . LYS   A 357 ? 0.7781 1.0589 0.5753 -0.0560 -0.0362 0.2666  336 LYS   A NZ  
2665 N  N   . VAL   A 358 ? 0.7362 0.9520 0.5330 0.0004  -0.0594 0.2203  337 VAL   A N   
2666 C  CA  . VAL   A 358 ? 0.7722 0.9520 0.5814 0.0053  -0.0818 0.2351  337 VAL   A CA  
2667 C  C   . VAL   A 358 ? 0.8279 0.9737 0.6483 -0.0082 -0.0925 0.2603  337 VAL   A C   
2668 O  O   . VAL   A 358 ? 0.8415 1.0024 0.6561 -0.0237 -0.0871 0.2736  337 VAL   A O   
2669 C  CB  . VAL   A 358 ? 0.7514 0.9471 0.5519 0.0097  -0.0953 0.2401  337 VAL   A CB  
2670 C  CG1 . VAL   A 358 ? 0.7956 0.9512 0.6123 0.0148  -0.1213 0.2556  337 VAL   A CG1 
2671 C  CG2 . VAL   A 358 ? 0.6685 0.8909 0.4644 0.0242  -0.0868 0.2093  337 VAL   A CG2 
2672 N  N   . CYS   A 359 ? 1.0011 1.1030 0.8417 -0.0009 -0.1091 0.2639  338 CYS   A N   
2673 C  CA  . CYS   A 359 ? 1.0629 1.1249 0.9192 -0.0103 -0.1254 0.2834  338 CYS   A CA  
2674 C  C   . CYS   A 359 ? 1.0375 1.0670 0.9093 0.0008  -0.1533 0.2883  338 CYS   A C   
2675 O  O   . CYS   A 359 ? 1.0346 1.0547 0.9187 0.0195  -0.1576 0.2667  338 CYS   A O   
2676 C  CB  . CYS   A 359 ? 1.0708 1.1058 0.9423 -0.0100 -0.1199 0.2761  338 CYS   A CB  
2677 S  SG  . CYS   A 359 ? 1.2368 1.2225 1.1313 -0.0203 -0.1408 0.2937  338 CYS   A SG  
2678 N  N   . PHE   A 360 ? 1.0442 1.0587 0.9196 -0.0100 -0.1697 0.3100  339 PHE   A N   
2679 C  CA  . PHE   A 360 ? 1.0934 1.0769 0.9846 0.0005  -0.1973 0.3138  339 PHE   A CA  
2680 C  C   . PHE   A 360 ? 1.1128 1.0459 1.0319 0.0006  -0.2167 0.3165  339 PHE   A C   
2681 O  O   . PHE   A 360 ? 1.1580 1.0603 1.0990 0.0198  -0.2321 0.2986  339 PHE   A O   
2682 C  CB  . PHE   A 360 ? 1.1039 1.1072 0.9810 -0.0104 -0.2054 0.3357  339 PHE   A CB  
2683 C  CG  . PHE   A 360 ? 1.1211 1.1704 0.9743 -0.0054 -0.1925 0.3276  339 PHE   A CG  
2684 C  CD1 . PHE   A 360 ? 1.1029 1.1580 0.9580 0.0147  -0.1913 0.3038  339 PHE   A CD1 
2685 C  CD2 . PHE   A 360 ? 1.1440 1.2345 0.9758 -0.0205 -0.1826 0.3422  339 PHE   A CD2 
2686 C  CE1 . PHE   A 360 ? 1.0276 1.1256 0.8630 0.0191  -0.1810 0.2940  339 PHE   A CE1 
2687 C  CE2 . PHE   A 360 ? 1.0268 1.1599 0.8382 -0.0144 -0.1720 0.3306  339 PHE   A CE2 
2688 C  CZ  . PHE   A 360 ? 0.9503 1.0853 0.7631 0.0052  -0.1715 0.3061  339 PHE   A CZ  
2689 N  N   . ASP   A 367 ? 1.0127 0.8586 1.0941 0.1505  -0.2249 0.0807  346 ASP   A N   
2690 C  CA  . ASP   A 367 ? 1.1046 0.9771 1.1718 0.1479  -0.2184 0.0884  346 ASP   A CA  
2691 C  C   . ASP   A 367 ? 1.1380 1.0515 1.1849 0.1367  -0.1807 0.0822  346 ASP   A C   
2692 O  O   . ASP   A 367 ? 1.1034 1.0326 1.1281 0.1223  -0.1706 0.1008  346 ASP   A O   
2693 C  CB  . ASP   A 367 ? 1.0084 0.8900 1.0976 0.1736  -0.2354 0.0638  346 ASP   A CB  
2694 N  N   . ARG   A 368 ? 1.1981 1.1301 1.2535 0.1440  -0.1620 0.0553  347 ARG   A N   
2695 C  CA  . ARG   A 368 ? 1.1713 1.1354 1.2112 0.1323  -0.1294 0.0499  347 ARG   A CA  
2696 C  C   . ARG   A 368 ? 1.0595 1.0115 1.0889 0.1172  -0.1157 0.0593  347 ARG   A C   
2697 O  O   . ARG   A 368 ? 1.0000 0.9738 1.0226 0.1108  -0.0913 0.0498  347 ARG   A O   
2698 C  CB  . ARG   A 368 ? 1.1000 1.0976 1.1553 0.1464  -0.1170 0.0186  347 ARG   A CB  
2699 C  CG  . ARG   A 368 ? 1.2102 1.2368 1.2686 0.1532  -0.1175 0.0111  347 ARG   A CG  
2700 C  CD  . ARG   A 368 ? 1.1965 1.2618 1.2509 0.1458  -0.0911 -0.0003 347 ARG   A CD  
2701 N  NE  . ARG   A 368 ? 1.2425 1.3419 1.3182 0.1607  -0.0908 -0.0243 347 ARG   A NE  
2702 C  CZ  . ARG   A 368 ? 1.2237 1.3433 1.3141 0.1683  -0.0828 -0.0438 347 ARG   A CZ  
2703 N  NH1 . ARG   A 368 ? 1.1860 1.2920 1.2722 0.1630  -0.0745 -0.0433 347 ARG   A NH1 
2704 N  NH2 . ARG   A 368 ? 1.1750 1.3340 1.2848 0.1814  -0.0831 -0.0641 347 ARG   A NH2 
2705 N  N   . TRP   A 369 ? 0.8975 0.8150 0.9269 0.1103  -0.1326 0.0793  348 TRP   A N   
2706 C  CA  . TRP   A 369 ? 0.7961 0.7014 0.8197 0.0973  -0.1224 0.0869  348 TRP   A CA  
2707 C  C   . TRP   A 369 ? 0.7846 0.7163 0.7852 0.0804  -0.0939 0.0941  348 TRP   A C   
2708 O  O   . TRP   A 369 ? 0.7648 0.6990 0.7629 0.0743  -0.0779 0.0884  348 TRP   A O   
2709 C  CB  . TRP   A 369 ? 0.8299 0.6973 0.8555 0.0875  -0.1468 0.1146  348 TRP   A CB  
2710 C  CG  . TRP   A 369 ? 0.8440 0.7150 0.8516 0.0725  -0.1533 0.1468  348 TRP   A CG  
2711 C  CD1 . TRP   A 369 ? 0.8969 0.7583 0.9082 0.0775  -0.1770 0.1591  348 TRP   A CD1 
2712 C  CD2 . TRP   A 369 ? 0.8242 0.7144 0.8071 0.0506  -0.1362 0.1701  348 TRP   A CD2 
2713 N  NE1 . TRP   A 369 ? 0.9670 0.8420 0.9557 0.0590  -0.1753 0.1904  348 TRP   A NE1 
2714 C  CE2 . TRP   A 369 ? 0.9077 0.8029 0.8787 0.0429  -0.1500 0.1965  348 TRP   A CE2 
2715 C  CE3 . TRP   A 369 ? 0.7582 0.6650 0.7282 0.0379  -0.1115 0.1703  348 TRP   A CE3 
2716 C  CZ2 . TRP   A 369 ? 0.9159 0.8373 0.8620 0.0232  -0.1386 0.2218  348 TRP   A CZ2 
2717 C  CZ3 . TRP   A 369 ? 0.8713 0.8016 0.8184 0.0197  -0.1011 0.1937  348 TRP   A CZ3 
2718 C  CH2 . TRP   A 369 ? 0.9201 0.8602 0.8551 0.0126  -0.1141 0.2187  348 TRP   A CH2 
2719 N  N   . ILE   A 370 ? 0.8119 0.7641 0.7962 0.0740  -0.0886 0.1047  349 ILE   A N   
2720 C  CA  . ILE   A 370 ? 0.8463 0.8246 0.8109 0.0611  -0.0647 0.1072  349 ILE   A CA  
2721 C  C   . ILE   A 370 ? 0.8097 0.8094 0.7797 0.0669  -0.0452 0.0813  349 ILE   A C   
2722 O  O   . ILE   A 370 ? 0.7264 0.7425 0.6847 0.0575  -0.0271 0.0797  349 ILE   A O   
2723 C  CB  . ILE   A 370 ? 0.8103 0.8088 0.7568 0.0551  -0.0661 0.1216  349 ILE   A CB  
2724 C  CG1 . ILE   A 370 ? 0.7810 0.8038 0.7071 0.0416  -0.0461 0.1265  349 ILE   A CG1 
2725 C  CG2 . ILE   A 370 ? 0.8092 0.8256 0.7621 0.0678  -0.0666 0.1035  349 ILE   A CG2 
2726 C  CD1 . ILE   A 370 ? 0.8797 0.8920 0.8004 0.0284  -0.0421 0.1422  349 ILE   A CD1 
2727 N  N   . GLN   A 371 ? 0.8145 0.8170 0.8033 0.0817  -0.0499 0.0614  350 GLN   A N   
2728 C  CA  . GLN   A 371 ? 0.8025 0.8286 0.7989 0.0851  -0.0332 0.0403  350 GLN   A CA  
2729 C  C   . GLN   A 371 ? 0.7846 0.8055 0.7971 0.0938  -0.0329 0.0249  350 GLN   A C   
2730 O  O   . GLN   A 371 ? 0.7430 0.7799 0.7565 0.0899  -0.0164 0.0150  350 GLN   A O   
2731 C  CB  . GLN   A 371 ? 0.8245 0.8751 0.8289 0.0938  -0.0355 0.0286  350 GLN   A CB  
2732 C  CG  . GLN   A 371 ? 0.8751 0.9544 0.8890 0.0939  -0.0199 0.0111  350 GLN   A CG  
2733 C  CD  . GLN   A 371 ? 0.9884 1.0934 1.0168 0.1042  -0.0254 -0.0014 350 GLN   A CD  
2734 O  OE1 . GLN   A 371 ? 0.9805 1.0880 1.0248 0.1193  -0.0372 -0.0120 350 GLN   A OE1 
2735 N  NE2 . GLN   A 371 ? 0.9544 1.0798 0.9793 0.0969  -0.0185 -0.0017 350 GLN   A NE2 
2736 N  N   . ASP   A 372 ? 0.6218 0.6216 0.6477 0.1058  -0.0524 0.0221  351 ASP   A N   
2737 C  CA  . ASP   A 372 ? 0.5973 0.5945 0.6390 0.1168  -0.0546 0.0038  351 ASP   A CA  
2738 C  C   . ASP   A 372 ? 0.6028 0.5690 0.6416 0.1094  -0.0586 0.0138  351 ASP   A C   
2739 O  O   . ASP   A 372 ? 0.5095 0.4781 0.5564 0.1144  -0.0540 -0.0009 351 ASP   A O   
2740 C  CB  . ASP   A 372 ? 0.6433 0.6387 0.7065 0.1389  -0.0767 -0.0128 351 ASP   A CB  
2741 C  CG  . ASP   A 372 ? 0.7370 0.7716 0.8082 0.1483  -0.0712 -0.0283 351 ASP   A CG  
2742 O  OD1 . ASP   A 372 ? 0.7381 0.7953 0.7979 0.1360  -0.0535 -0.0225 351 ASP   A OD1 
2743 O  OD2 . ASP   A 372 ? 0.7771 0.8210 0.8679 0.1685  -0.0862 -0.0472 351 ASP   A OD2 
2744 N  N   . GLU   A 373 ? 0.5717 0.5126 0.5996 0.0970  -0.0674 0.0391  352 GLU   A N   
2745 C  CA  . GLU   A 373 ? 0.5687 0.4818 0.5955 0.0875  -0.0726 0.0516  352 GLU   A CA  
2746 C  C   . GLU   A 373 ? 0.5032 0.4252 0.5100 0.0674  -0.0520 0.0674  352 GLU   A C   
2747 O  O   . GLU   A 373 ? 0.5153 0.4226 0.5221 0.0594  -0.0506 0.0733  352 GLU   A O   
2748 C  CB  . GLU   A 373 ? 0.6266 0.5047 0.6597 0.0862  -0.1016 0.0718  352 GLU   A CB  
2749 C  CG  . GLU   A 373 ? 0.6787 0.5416 0.7355 0.1084  -0.1276 0.0544  352 GLU   A CG  
2750 C  CD  . GLU   A 373 ? 0.7332 0.5545 0.7996 0.1059  -0.1609 0.0760  352 GLU   A CD  
2751 O  OE1 . GLU   A 373 ? 0.8288 0.6324 0.8862 0.0859  -0.1634 0.1038  352 GLU   A OE1 
2752 O  OE2 . GLU   A 373 ? 0.7447 0.5526 0.8291 0.1236  -0.1858 0.0659  352 GLU   A OE2 
2753 N  N   . ILE   A 374 ? 0.5616 0.5084 0.5531 0.0604  -0.0374 0.0722  353 ILE   A N   
2754 C  CA  . ILE   A 374 ? 0.6047 0.5640 0.5780 0.0442  -0.0202 0.0842  353 ILE   A CA  
2755 C  C   . ILE   A 374 ? 0.5657 0.5522 0.5353 0.0453  -0.0001 0.0672  353 ILE   A C   
2756 O  O   . ILE   A 374 ? 0.5181 0.5194 0.4940 0.0543  0.0000  0.0544  353 ILE   A O   
2757 C  CB  . ILE   A 374 ? 0.5739 0.5383 0.5316 0.0340  -0.0261 0.1080  353 ILE   A CB  
2758 C  CG1 . ILE   A 374 ? 0.6053 0.5504 0.5604 0.0208  -0.0367 0.1331  353 ILE   A CG1 
2759 C  CG2 . ILE   A 374 ? 0.7000 0.6953 0.6407 0.0271  -0.0073 0.1060  353 ILE   A CG2 
2760 C  CD1 . ILE   A 374 ? 0.6615 0.5707 0.6365 0.0275  -0.0596 0.1343  353 ILE   A CD1 
2761 N  N   . GLU   A 375 ? 0.4825 0.4759 0.4438 0.0355  0.0152  0.0680  354 GLU   A N   
2762 C  CA  . GLU   A 375 ? 0.4512 0.4657 0.4104 0.0344  0.0311  0.0546  354 GLU   A CA  
2763 C  C   . GLU   A 375 ? 0.4471 0.4695 0.3922 0.0229  0.0419  0.0619  354 GLU   A C   
2764 O  O   . GLU   A 375 ? 0.4349 0.4474 0.3775 0.0163  0.0442  0.0695  354 GLU   A O   
2765 C  CB  . GLU   A 375 ? 0.4791 0.4947 0.4512 0.0395  0.0369  0.0392  354 GLU   A CB  
2766 C  CG  . GLU   A 375 ? 0.4574 0.4933 0.4300 0.0358  0.0504  0.0294  354 GLU   A CG  
2767 C  CD  . GLU   A 375 ? 0.5416 0.5961 0.5189 0.0397  0.0484  0.0232  354 GLU   A CD  
2768 O  OE1 . GLU   A 375 ? 0.6200 0.6757 0.6046 0.0491  0.0383  0.0205  354 GLU   A OE1 
2769 O  OE2 . GLU   A 375 ? 0.6446 0.7118 0.6198 0.0337  0.0549  0.0204  354 GLU   A OE2 
2770 N  N   . PHE   A 376 ? 0.4658 0.5074 0.4032 0.0214  0.0472  0.0578  355 PHE   A N   
2771 C  CA  . PHE   A 376 ? 0.4889 0.5435 0.4144 0.0140  0.0560  0.0595  355 PHE   A CA  
2772 C  C   . PHE   A 376 ? 0.4307 0.4873 0.3628 0.0130  0.0659  0.0458  355 PHE   A C   
2773 O  O   . PHE   A 376 ? 0.4745 0.5376 0.4143 0.0159  0.0664  0.0346  355 PHE   A O   
2774 C  CB  . PHE   A 376 ? 0.4844 0.5600 0.3990 0.0151  0.0535  0.0592  355 PHE   A CB  
2775 C  CG  . PHE   A 376 ? 0.5574 0.6352 0.4624 0.0138  0.0436  0.0767  355 PHE   A CG  
2776 C  CD1 . PHE   A 376 ? 0.6711 0.7324 0.5765 0.0085  0.0375  0.0943  355 PHE   A CD1 
2777 C  CD2 . PHE   A 376 ? 0.6480 0.7438 0.5447 0.0171  0.0382  0.0766  355 PHE   A CD2 
2778 C  CE1 . PHE   A 376 ? 0.6605 0.7223 0.5587 0.0051  0.0254  0.1143  355 PHE   A CE1 
2779 C  CE2 . PHE   A 376 ? 0.7048 0.8039 0.5921 0.0147  0.0277  0.0954  355 PHE   A CE2 
2780 C  CZ  . PHE   A 376 ? 0.6469 0.7285 0.5352 0.0080  0.0210  0.1157  355 PHE   A CZ  
2781 N  N   . GLY   A 377 ? 0.4218 0.4728 0.3524 0.0077  0.0722  0.0483  356 GLY   A N   
2782 C  CA  . GLY   A 377 ? 0.3997 0.4530 0.3349 0.0058  0.0799  0.0375  356 GLY   A CA  
2783 C  C   . GLY   A 377 ? 0.3903 0.4555 0.3157 0.0018  0.0847  0.0378  356 GLY   A C   
2784 O  O   . GLY   A 377 ? 0.3943 0.4745 0.3085 0.0012  0.0828  0.0438  356 GLY   A O   
2785 N  N   . TYR   A 378 ? 0.3531 0.4160 0.2826 -0.0004 0.0903  0.0312  357 TYR   A N   
2786 C  CA  . TYR   A 378 ? 0.4152 0.4929 0.3373 -0.0024 0.0944  0.0293  357 TYR   A CA  
2787 C  C   . TYR   A 378 ? 0.3931 0.4585 0.3234 -0.0069 0.0966  0.0249  357 TYR   A C   
2788 O  O   . TYR   A 378 ? 0.3391 0.3911 0.2787 -0.0068 0.0965  0.0236  357 TYR   A O   
2789 C  CB  . TYR   A 378 ? 0.3642 0.4595 0.2846 0.0030  0.0915  0.0148  357 TYR   A CB  
2790 C  CG  . TYR   A 378 ? 0.3778 0.4621 0.3116 0.0047  0.0884  0.0015  357 TYR   A CG  
2791 C  CD1 . TYR   A 378 ? 0.3694 0.4451 0.3123 0.0050  0.0831  -0.0003 357 TYR   A CD1 
2792 C  CD2 . TYR   A 378 ? 0.3774 0.4613 0.3161 0.0050  0.0893  -0.0077 357 TYR   A CD2 
2793 C  CE1 . TYR   A 378 ? 0.4015 0.4688 0.3580 0.0032  0.0784  -0.0078 357 TYR   A CE1 
2794 C  CE2 . TYR   A 378 ? 0.4102 0.4814 0.3626 0.0047  0.0832  -0.0164 357 TYR   A CE2 
2795 C  CZ  . TYR   A 378 ? 0.4038 0.4669 0.3650 0.0026  0.0776  -0.0149 357 TYR   A CZ  
2796 O  OH  . TYR   A 378 ? 0.4458 0.4982 0.4221 -0.0010 0.0698  -0.0190 357 TYR   A OH  
2797 N  N   . ILE   A 379 ? 0.4195 0.4910 0.3464 -0.0100 0.0977  0.0227  358 ILE   A N   
2798 C  CA  . ILE   A 379 ? 0.3658 0.4338 0.3003 -0.0135 0.0979  0.0165  358 ILE   A CA  
2799 C  C   . ILE   A 379 ? 0.4048 0.4832 0.3375 -0.0043 0.1007  0.0065  358 ILE   A C   
2800 O  O   . ILE   A 379 ? 0.4180 0.5173 0.3440 -0.0012 0.0982  0.0037  358 ILE   A O   
2801 C  CB  . ILE   A 379 ? 0.3561 0.4198 0.2902 -0.0215 0.0967  0.0264  358 ILE   A CB  
2802 C  CG1 . ILE   A 379 ? 0.3220 0.3931 0.2458 -0.0211 0.1005  0.0352  358 ILE   A CG1 
2803 C  CG2 . ILE   A 379 ? 0.3244 0.3748 0.2627 -0.0216 0.0939  0.0381  358 ILE   A CG2 
2804 C  CD1 . ILE   A 379 ? 0.3456 0.4117 0.2696 -0.0292 0.1002  0.0476  358 ILE   A CD1 
2805 N  N   . GLU   A 380 ? 0.3965 0.4722 0.3373 0.0000  0.1008  -0.0001 359 GLU   A N   
2806 C  CA  . GLU   A 380 ? 0.3893 0.4835 0.3318 0.0057  0.0981  -0.0168 359 GLU   A CA  
2807 C  C   . GLU   A 380 ? 0.4465 0.5362 0.3964 0.0062  0.0988  -0.0197 359 GLU   A C   
2808 O  O   . GLU   A 380 ? 0.3828 0.4581 0.3397 0.0025  0.0982  -0.0154 359 GLU   A O   
2809 C  CB  . GLU   A 380 ? 0.4224 0.5237 0.3700 0.0112  0.0929  -0.0344 359 GLU   A CB  
2810 C  CG  . GLU   A 380 ? 0.4524 0.5722 0.4046 0.0221  0.0853  -0.0567 359 GLU   A CG  
2811 C  CD  . GLU   A 380 ? 0.5788 0.6866 0.5424 0.0281  0.0701  -0.0715 359 GLU   A CD  
2812 O  OE1 . GLU   A 380 ? 0.6118 0.6964 0.5815 0.0215  0.0665  -0.0622 359 GLU   A OE1 
2813 O  OE2 . GLU   A 380 ? 0.6101 0.7340 0.5779 0.0398  0.0604  -0.0934 359 GLU   A OE2 
2814 N  N   . ALA   A 381 ? 0.3416 0.6733 0.3959 0.0835  0.0885  -0.0430 360 ALA   A N   
2815 C  CA  . ALA   A 381 ? 0.2805 0.6270 0.3538 0.0918  0.0861  -0.0501 360 ALA   A CA  
2816 C  C   . ALA   A 381 ? 0.3489 0.7046 0.4242 0.1100  0.0830  -0.0691 360 ALA   A C   
2817 O  O   . ALA   A 381 ? 0.3539 0.7089 0.4153 0.1136  0.0837  -0.0759 360 ALA   A O   
2818 C  CB  . ALA   A 381 ? 0.2825 0.6597 0.3647 0.0807  0.0931  -0.0416 360 ALA   A CB  
2819 N  N   . PRO   A 382 ? 0.3498 0.7140 0.4429 0.1222  0.0788  -0.0787 361 PRO   A N   
2820 C  CA  . PRO   A 382 ? 0.3279 0.6996 0.4250 0.1400  0.0752  -0.0985 361 PRO   A CA  
2821 C  C   . PRO   A 382 ? 0.3980 0.8064 0.4863 0.1397  0.0830  -0.1048 361 PRO   A C   
2822 O  O   . PRO   A 382 ? 0.4450 0.8579 0.5287 0.1515  0.0806  -0.1213 361 PRO   A O   
2823 C  CB  . PRO   A 382 ? 0.3821 0.7591 0.5026 0.1510  0.0699  -0.1035 361 PRO   A CB  
2824 C  CG  . PRO   A 382 ? 0.3003 0.6617 0.4265 0.1408  0.0676  -0.0873 361 PRO   A CG  
2825 C  CD  . PRO   A 382 ? 0.3813 0.7482 0.4926 0.1211  0.0759  -0.0728 361 PRO   A CD  
2826 N  N   . HIS   A 383 ? 0.4042 0.8400 0.4912 0.1260  0.0919  -0.0920 362 HIS   A N   
2827 C  CA  . HIS   A 383 ? 0.3995 0.8750 0.4794 0.1242  0.0999  -0.0947 362 HIS   A CA  
2828 C  C   . HIS   A 383 ? 0.4162 0.8904 0.4743 0.1122  0.1047  -0.0838 362 HIS   A C   
2829 O  O   . HIS   A 383 ? 0.4191 0.9222 0.4675 0.1148  0.1089  -0.0895 362 HIS   A O   
2830 C  CB  . HIS   A 383 ? 0.3253 0.8337 0.4182 0.1155  0.1067  -0.0856 362 HIS   A CB  
2831 C  CG  . HIS   A 383 ? 0.3825 0.8763 0.4781 0.0969  0.1087  -0.0651 362 HIS   A CG  
2832 N  ND1 . HIS   A 383 ? 0.3563 0.8275 0.4647 0.0969  0.1024  -0.0621 362 HIS   A ND1 
2833 C  CD2 . HIS   A 383 ? 0.3665 0.8646 0.4545 0.0779  0.1153  -0.0469 362 HIS   A CD2 
2834 C  CE1 . HIS   A 383 ? 0.3681 0.8316 0.4764 0.0788  0.1051  -0.0451 362 HIS   A CE1 
2835 N  NE2 . HIS   A 383 ? 0.4513 0.9287 0.5483 0.0670  0.1128  -0.0355 362 HIS   A NE2 
2836 N  N   . LYS   A 384 ? 0.4154 0.8589 0.4661 0.0999  0.1038  -0.0686 363 LYS   A N   
2837 C  CA  . LYS   A 384 ? 0.4035 0.8475 0.4362 0.0870  0.1086  -0.0547 363 LYS   A CA  
2838 C  C   . LYS   A 384 ? 0.3989 0.8011 0.4245 0.0796  0.1044  -0.0446 363 LYS   A C   
2839 O  O   . LYS   A 384 ? 0.4014 0.7800 0.4374 0.0792  0.1000  -0.0429 363 LYS   A O   
2840 C  CB  . LYS   A 384 ? 0.4025 0.8747 0.4385 0.0712  0.1176  -0.0377 363 LYS   A CB  
2841 C  CG  . LYS   A 384 ? 0.4310 0.9048 0.4504 0.0576  0.1223  -0.0208 363 LYS   A CG  
2842 C  CD  . LYS   A 384 ? 0.4568 0.9562 0.4610 0.0664  0.1236  -0.0302 363 LYS   A CD  
2843 C  CE  . LYS   A 384 ? 0.5362 1.0410 0.5247 0.0530  0.1279  -0.0110 363 LYS   A CE  
2844 N  NZ  . LYS   A 384 ? 0.5074 1.0361 0.5036 0.0372  0.1360  0.0081  363 LYS   A NZ  
2845 N  N   . GLY   A 385 ? 0.4066 0.8025 0.4144 0.0742  0.1055  -0.0379 364 GLY   A N   
2846 C  CA  . GLY   A 385 ? 0.3426 0.7032 0.3424 0.0659  0.1026  -0.0266 364 GLY   A CA  
2847 C  C   . GLY   A 385 ? 0.3830 0.7488 0.3644 0.0588  0.1054  -0.0165 364 GLY   A C   
2848 O  O   . GLY   A 385 ? 0.4631 0.8569 0.4360 0.0642  0.1076  -0.0229 364 GLY   A O   
2849 N  N   . PHE   A 386 ? 0.3430 0.6837 0.3191 0.0469  0.1049  -0.0005 365 PHE   A N   
2850 C  CA  . PHE   A 386 ? 0.3983 0.7408 0.3581 0.0399  0.1065  0.0117  365 PHE   A CA  
2851 C  C   . PHE   A 386 ? 0.4389 0.7436 0.3947 0.0322  0.1026  0.0229  365 PHE   A C   
2852 O  O   . PHE   A 386 ? 0.3702 0.6520 0.3366 0.0302  0.1001  0.0227  365 PHE   A O   
2853 C  CB  . PHE   A 386 ? 0.4116 0.7832 0.3724 0.0280  0.1141  0.0278  365 PHE   A CB  
2854 C  CG  . PHE   A 386 ? 0.4247 0.7926 0.4025 0.0153  0.1176  0.0396  365 PHE   A CG  
2855 C  CD1 . PHE   A 386 ? 0.4259 0.7638 0.4071 0.0026  0.1160  0.0547  365 PHE   A CD1 
2856 C  CD2 . PHE   A 386 ? 0.4217 0.8181 0.4133 0.0161  0.1219  0.0349  365 PHE   A CD2 
2857 C  CE1 . PHE   A 386 ? 0.3504 0.6856 0.3487 -0.0094 0.1184  0.0635  365 PHE   A CE1 
2858 C  CE2 . PHE   A 386 ? 0.3744 0.7693 0.3829 0.0039  0.1245  0.0448  365 PHE   A CE2 
2859 C  CZ  . PHE   A 386 ? 0.3394 0.7035 0.3514 -0.0092 0.1227  0.0587  365 PHE   A CZ  
2860 N  N   . PRO   A 387 ? 0.4223 0.7215 0.3633 0.0284  0.1015  0.0325  366 PRO   A N   
2861 C  CA  . PRO   A 387 ? 0.3935 0.6581 0.3316 0.0213  0.0976  0.0435  366 PRO   A CA  
2862 C  C   . PRO   A 387 ? 0.3413 0.5967 0.2907 0.0056  0.1007  0.0616  366 PRO   A C   
2863 O  O   . PRO   A 387 ? 0.3702 0.6471 0.3245 -0.0023 0.1061  0.0715  366 PRO   A O   
2864 C  CB  . PRO   A 387 ? 0.4527 0.7210 0.3727 0.0223  0.0955  0.0491  366 PRO   A CB  
2865 C  CG  . PRO   A 387 ? 0.4586 0.7616 0.3715 0.0330  0.0971  0.0350  366 PRO   A CG  
2866 C  CD  . PRO   A 387 ? 0.4629 0.7890 0.3893 0.0319  0.1030  0.0323  366 PRO   A CD  
2867 N  N   . VAL   A 388 ? 0.3880 0.6117 0.3429 0.0013  0.0968  0.0650  367 VAL   A N   
2868 C  CA  . VAL   A 388 ? 0.3762 0.5855 0.3430 -0.0132 0.0978  0.0797  367 VAL   A CA  
2869 C  C   . VAL   A 388 ? 0.4317 0.6090 0.3930 -0.0163 0.0922  0.0874  367 VAL   A C   
2870 O  O   . VAL   A 388 ? 0.3813 0.5410 0.3396 -0.0091 0.0875  0.0782  367 VAL   A O   
2871 C  CB  . VAL   A 388 ? 0.3677 0.5748 0.3525 -0.0154 0.0984  0.0729  367 VAL   A CB  
2872 C  CG1 . VAL   A 388 ? 0.3310 0.5210 0.3290 -0.0305 0.0981  0.0856  367 VAL   A CG1 
2873 C  CG2 . VAL   A 388 ? 0.3098 0.5500 0.3019 -0.0120 0.1034  0.0660  367 VAL   A CG2 
2874 N  N   . VAL   A 389 ? 0.3943 0.5650 0.3552 -0.0264 0.0922  0.1046  368 VAL   A N   
2875 C  CA  . VAL   A 389 ? 0.4393 0.5797 0.3977 -0.0293 0.0861  0.1129  368 VAL   A CA  
2876 C  C   . VAL   A 389 ? 0.4113 0.5314 0.3883 -0.0409 0.0850  0.1192  368 VAL   A C   
2877 O  O   . VAL   A 389 ? 0.4474 0.5772 0.4360 -0.0511 0.0889  0.1275  368 VAL   A O   
2878 C  CB  . VAL   A 389 ? 0.4814 0.6265 0.4279 -0.0311 0.0849  0.1276  368 VAL   A CB  
2879 C  CG1 . VAL   A 389 ? 0.5814 0.7486 0.5333 -0.0408 0.0907  0.1415  368 VAL   A CG1 
2880 C  CG2 . VAL   A 389 ? 0.5698 0.6829 0.5180 -0.0344 0.0779  0.1375  368 VAL   A CG2 
2881 N  N   . LEU   A 390 ? 0.3907 0.4846 0.3717 -0.0392 0.0796  0.1143  369 LEU   A N   
2882 C  CA  . LEU   A 390 ? 0.4771 0.5494 0.4757 -0.0493 0.0768  0.1186  369 LEU   A CA  
2883 C  C   . LEU   A 390 ? 0.4195 0.4686 0.4170 -0.0521 0.0711  0.1312  369 LEU   A C   
2884 O  O   . LEU   A 390 ? 0.4661 0.5068 0.4508 -0.0437 0.0669  0.1307  369 LEU   A O   
2885 C  CB  . LEU   A 390 ? 0.4168 0.4772 0.4225 -0.0455 0.0740  0.1054  369 LEU   A CB  
2886 C  CG  . LEU   A 390 ? 0.4678 0.5486 0.4776 -0.0416 0.0780  0.0927  369 LEU   A CG  
2887 C  CD1 . LEU   A 390 ? 0.4257 0.4958 0.4510 -0.0448 0.0753  0.0855  369 LEU   A CD1 
2888 C  CD2 . LEU   A 390 ? 0.4100 0.5168 0.4256 -0.0472 0.0842  0.0956  369 LEU   A CD2 
2889 N  N   . ASP   A 391 ? 0.4661 0.5050 0.4785 -0.0637 0.0702  0.1423  370 ASP   A N   
2890 C  CA  . ASP   A 391 ? 0.5644 0.5806 0.5796 -0.0663 0.0641  0.1551  370 ASP   A CA  
2891 C  C   . ASP   A 391 ? 0.5489 0.5371 0.5851 -0.0718 0.0584  0.1507  370 ASP   A C   
2892 O  O   . ASP   A 391 ? 0.5346 0.5241 0.5880 -0.0819 0.0602  0.1488  370 ASP   A O   
2893 C  CB  . ASP   A 391 ? 0.5179 0.5464 0.5341 -0.0748 0.0671  0.1737  370 ASP   A CB  
2894 C  CG  . ASP   A 391 ? 0.5857 0.5926 0.6042 -0.0760 0.0602  0.1890  370 ASP   A CG  
2895 O  OD1 . ASP   A 391 ? 0.6402 0.6226 0.6605 -0.0697 0.0530  0.1835  370 ASP   A OD1 
2896 O  OD2 . ASP   A 391 ? 0.6437 0.6598 0.6632 -0.0828 0.0618  0.2069  370 ASP   A OD2 
2897 N  N   . SER   A 392 ? 0.5283 0.4929 0.5644 -0.0649 0.0511  0.1476  371 SER   A N   
2898 C  CA  . SER   A 392 ? 0.5409 0.4784 0.5977 -0.0678 0.0444  0.1415  371 SER   A CA  
2899 C  C   . SER   A 392 ? 0.6366 0.5521 0.6969 -0.0658 0.0372  0.1525  371 SER   A C   
2900 O  O   . SER   A 392 ? 0.6611 0.5666 0.7138 -0.0553 0.0323  0.1492  371 SER   A O   
2901 C  CB  . SER   A 392 ? 0.5762 0.5080 0.6334 -0.0596 0.0424  0.1238  371 SER   A CB  
2902 O  OG  . SER   A 392 ? 0.6492 0.5583 0.7277 -0.0617 0.0362  0.1147  371 SER   A OG  
2903 N  N   . PRO   A 393 ? 0.7041 0.6127 0.7770 -0.0754 0.0359  0.1662  372 PRO   A N   
2904 C  CA  . PRO   A 393 ? 0.6989 0.5860 0.7780 -0.0730 0.0283  0.1778  372 PRO   A CA  
2905 C  C   . PRO   A 393 ? 0.7797 0.6388 0.8765 -0.0678 0.0199  0.1637  372 PRO   A C   
2906 O  O   . PRO   A 393 ? 0.8638 0.7177 0.9743 -0.0707 0.0196  0.1475  372 PRO   A O   
2907 C  CB  . PRO   A 393 ? 0.5631 0.4505 0.6555 -0.0865 0.0296  0.1954  372 PRO   A CB  
2908 C  CG  . PRO   A 393 ? 0.6270 0.5439 0.7125 -0.0941 0.0394  0.1954  372 PRO   A CG  
2909 C  CD  . PRO   A 393 ? 0.6431 0.5657 0.7253 -0.0888 0.0417  0.1735  372 PRO   A CD  
2910 N  N   . ARG   A 394 ? 0.8076 0.6508 0.9048 -0.0597 0.0130  0.1691  373 ARG   A N   
2911 C  CA  . ARG   A 394 ? 0.7993 0.6189 0.9127 -0.0521 0.0050  0.1541  373 ARG   A CA  
2912 C  C   . ARG   A 394 ? 0.7745 0.5698 0.9143 -0.0576 -0.0021 0.1595  373 ARG   A C   
2913 O  O   . ARG   A 394 ? 0.7268 0.5223 0.8764 -0.0701 -0.0003 0.1710  373 ARG   A O   
2914 C  CB  . ARG   A 394 ? 0.7471 0.5652 0.8472 -0.0381 0.0011  0.1535  373 ARG   A CB  
2915 N  N   . PHE   A 401 ? 1.2495 1.2183 1.3318 -0.1253 0.0482  0.2921  380 PHE   A N   
2916 C  CA  . PHE   A 401 ? 1.2977 1.3066 1.3686 -0.1312 0.0578  0.3042  380 PHE   A CA  
2917 C  C   . PHE   A 401 ? 1.3032 1.3409 1.3484 -0.1194 0.0641  0.2879  380 PHE   A C   
2918 O  O   . PHE   A 401 ? 1.2473 1.2788 1.2769 -0.1065 0.0603  0.2794  380 PHE   A O   
2919 C  CB  . PHE   A 401 ? 1.2826 1.3004 1.3497 -0.1349 0.0557  0.3333  380 PHE   A CB  
2920 C  CG  . PHE   A 401 ? 1.3450 1.3275 1.4363 -0.1423 0.0464  0.3495  380 PHE   A CG  
2921 C  CD1 . PHE   A 401 ? 1.2464 1.1992 1.3387 -0.1324 0.0362  0.3490  380 PHE   A CD1 
2922 C  CD2 . PHE   A 401 ? 1.4000 1.3792 1.5146 -0.1590 0.0473  0.3647  380 PHE   A CD2 
2923 C  CE1 . PHE   A 401 ? 1.2346 1.1545 1.3511 -0.1378 0.0269  0.3627  380 PHE   A CE1 
2924 C  CE2 . PHE   A 401 ? 1.3847 1.3297 1.5240 -0.1656 0.0377  0.3790  380 PHE   A CE2 
2925 C  CZ  . PHE   A 401 ? 1.3006 1.2154 1.4410 -0.1544 0.0273  0.3776  380 PHE   A CZ  
2926 N  N   . PRO   A 402 ? 1.4102 1.4798 1.4526 -0.1236 0.0735  0.2829  381 PRO   A N   
2927 C  CA  . PRO   A 402 ? 1.2759 1.3725 1.2968 -0.1118 0.0791  0.2656  381 PRO   A CA  
2928 C  C   . PRO   A 402 ? 1.3115 1.4308 1.3095 -0.1038 0.0793  0.2754  381 PRO   A C   
2929 O  O   . PRO   A 402 ? 1.3922 1.5342 1.3882 -0.1106 0.0821  0.2958  381 PRO   A O   
2930 C  CB  . PRO   A 402 ? 1.1688 1.2956 1.1967 -0.1196 0.0885  0.2619  381 PRO   A CB  
2931 C  CG  . PRO   A 402 ? 1.3303 1.4397 1.3851 -0.1359 0.0872  0.2730  381 PRO   A CG  
2932 C  CD  . PRO   A 402 ? 1.3377 1.4214 1.3975 -0.1392 0.0792  0.2931  381 PRO   A CD  
2933 N  N   . VAL   A 403 ? 1.0622 1.1769 1.0435 -0.0900 0.0759  0.2612  382 VAL   A N   
2934 C  CA  . VAL   A 403 ? 0.9362 1.0737 0.8952 -0.0814 0.0754  0.2665  382 VAL   A CA  
2935 C  C   . VAL   A 403 ? 1.0708 1.2546 1.0214 -0.0842 0.0845  0.2708  382 VAL   A C   
2936 O  O   . VAL   A 403 ? 0.9303 1.1326 0.8800 -0.0814 0.0907  0.2539  382 VAL   A O   
2937 C  CB  . VAL   A 403 ? 0.8711 1.0022 0.8148 -0.0667 0.0720  0.2452  382 VAL   A CB  
2938 C  CG1 . VAL   A 403 ? 0.9001 1.0494 0.8232 -0.0587 0.0691  0.2517  382 VAL   A CG1 
2939 C  CG2 . VAL   A 403 ? 0.7862 0.8746 0.7416 -0.0646 0.0644  0.2377  382 VAL   A CG2 
2940 N  N   . LYS   A 404 ? 1.1228 1.3272 1.0686 -0.0894 0.0850  0.2938  383 LYS   A N   
2941 C  CA  . LYS   A 404 ? 1.0040 1.2551 0.9445 -0.0939 0.0937  0.3011  383 LYS   A CA  
2942 C  C   . LYS   A 404 ? 0.9662 1.2524 0.8851 -0.0804 0.0974  0.2819  383 LYS   A C   
2943 O  O   . LYS   A 404 ? 0.9307 1.2517 0.8483 -0.0804 0.1052  0.2742  383 LYS   A O   
2944 C  CB  . LYS   A 404 ? 0.9503 1.2155 0.8913 -0.1033 0.0927  0.3327  383 LYS   A CB  
2945 N  N   . GLU   A 405 ? 0.9908 1.2690 0.8940 -0.0686 0.0914  0.2732  384 GLU   A N   
2946 C  CA  . GLU   A 405 ? 0.9325 1.2407 0.8167 -0.0553 0.0934  0.2528  384 GLU   A CA  
2947 C  C   . GLU   A 405 ? 0.9978 1.2940 0.8858 -0.0477 0.0948  0.2245  384 GLU   A C   
2948 O  O   . GLU   A 405 ? 1.0042 1.3067 0.8793 -0.0351 0.0928  0.2046  384 GLU   A O   
2949 C  CB  . GLU   A 405 ? 0.8243 1.1283 0.6918 -0.0462 0.0858  0.2535  384 GLU   A CB  
2950 N  N   . LEU   A 406 ? 0.9415 1.2212 0.8479 -0.0553 0.0978  0.2228  385 LEU   A N   
2951 C  CA  . LEU   A 406 ? 0.8294 1.0973 0.7410 -0.0486 0.0987  0.1983  385 LEU   A CA  
2952 C  C   . LEU   A 406 ? 0.7804 1.0692 0.7046 -0.0537 0.1065  0.1933  385 LEU   A C   
2953 O  O   . LEU   A 406 ? 0.8296 1.1462 0.7482 -0.0449 0.1105  0.1765  385 LEU   A O   
2954 C  CB  . LEU   A 406 ? 0.7674 0.9879 0.6895 -0.0503 0.0922  0.1960  385 LEU   A CB  
2955 C  CG  . LEU   A 406 ? 0.7609 0.9619 0.6702 -0.0411 0.0842  0.1921  385 LEU   A CG  
2956 C  CD1 . LEU   A 406 ? 0.7497 0.9088 0.6699 -0.0411 0.0784  0.1858  385 LEU   A CD1 
2957 C  CD2 . LEU   A 406 ? 0.7147 0.9388 0.6072 -0.0276 0.0847  0.1725  385 LEU   A CD2 
2958 N  N   . LEU   A 407 ? 0.7456 1.0218 0.6883 -0.0674 0.1083  0.2066  386 LEU   A N   
2959 C  CA  . LEU   A 407 ? 0.7457 1.0418 0.7022 -0.0727 0.1153  0.2014  386 LEU   A CA  
2960 C  C   . LEU   A 407 ? 0.8109 1.1568 0.7604 -0.0730 0.1225  0.2072  386 LEU   A C   
2961 O  O   . LEU   A 407 ? 0.7640 1.1260 0.7045 -0.0768 0.1226  0.2254  386 LEU   A O   
2962 C  CB  . LEU   A 407 ? 0.7045 0.9778 0.6836 -0.0886 0.1151  0.2148  386 LEU   A CB  
2963 C  CG  . LEU   A 407 ? 0.7559 1.0473 0.7527 -0.0957 0.1216  0.2095  386 LEU   A CG  
2964 C  CD1 . LEU   A 407 ? 0.5603 0.8518 0.5579 -0.0841 0.1219  0.1832  386 LEU   A CD1 
2965 C  CD2 . LEU   A 407 ? 0.6911 0.9584 0.7114 -0.1125 0.1203  0.2225  386 LEU   A CD2 
2966 N  N   . GLY   A 408 ? 0.6562 1.0287 0.6102 -0.0684 0.1280  0.1914  387 GLY   A N   
2967 C  CA  . GLY   A 408 ? 0.5855 1.0089 0.5330 -0.0661 0.1348  0.1918  387 GLY   A CA  
2968 C  C   . GLY   A 408 ? 0.5443 0.9888 0.4946 -0.0545 0.1380  0.1662  387 GLY   A C   
2969 O  O   . GLY   A 408 ? 0.5578 0.9788 0.5188 -0.0513 0.1359  0.1521  387 GLY   A O   
2970 N  N   . PRO   A 409 ? 0.4849 0.9759 0.4263 -0.0472 0.1427  0.1597  388 PRO   A N   
2971 C  CA  . PRO   A 409 ? 0.4500 0.9637 0.3961 -0.0352 0.1453  0.1351  388 PRO   A CA  
2972 C  C   . PRO   A 409 ? 0.4661 0.9553 0.4054 -0.0189 0.1386  0.1106  388 PRO   A C   
2973 O  O   . PRO   A 409 ? 0.4810 0.9663 0.4039 -0.0108 0.1342  0.1059  388 PRO   A O   
2974 C  CB  . PRO   A 409 ? 0.4745 1.0445 0.4106 -0.0310 0.1510  0.1349  388 PRO   A CB  
2975 C  CG  . PRO   A 409 ? 0.5032 1.0823 0.4341 -0.0455 0.1530  0.1648  388 PRO   A CG  
2976 C  CD  . PRO   A 409 ? 0.4939 1.0216 0.4219 -0.0499 0.1457  0.1750  388 PRO   A CD  
2977 N  N   . ASP   A 410 ? 0.4365 0.9110 0.3895 -0.0143 0.1375  0.0956  389 ASP   A N   
2978 C  CA  . ASP   A 410 ? 0.4329 0.8829 0.3830 0.0002  0.1310  0.0736  389 ASP   A CA  
2979 C  C   . ASP   A 410 ? 0.4675 0.8761 0.4084 -0.0014 0.1244  0.0794  389 ASP   A C   
2980 O  O   . ASP   A 410 ? 0.4647 0.8604 0.3962 0.0106  0.1189  0.0645  389 ASP   A O   
2981 C  CB  . ASP   A 410 ? 0.4933 0.9729 0.4335 0.0173  0.1303  0.0520  389 ASP   A CB  
2982 C  CG  . ASP   A 410 ? 0.5728 1.0855 0.5256 0.0234  0.1347  0.0388  389 ASP   A CG  
2983 O  OD1 . ASP   A 410 ? 0.5405 1.0452 0.5104 0.0176  0.1364  0.0414  389 ASP   A OD1 
2984 O  OD2 . ASP   A 410 ? 0.7040 1.2522 0.6503 0.0345  0.1360  0.0248  389 ASP   A OD2 
2985 N  N   . PHE   A 411 ? 0.4569 0.8447 0.4020 -0.0162 0.1245  0.1008  390 PHE   A N   
2986 C  CA  . PHE   A 411 ? 0.4768 0.8229 0.4174 -0.0185 0.1180  0.1065  390 PHE   A CA  
2987 C  C   . PHE   A 411 ? 0.4202 0.7409 0.3783 -0.0323 0.1182  0.1184  390 PHE   A C   
2988 O  O   . PHE   A 411 ? 0.4781 0.8041 0.4427 -0.0457 0.1213  0.1376  390 PHE   A O   
2989 C  CB  . PHE   A 411 ? 0.5584 0.9067 0.4830 -0.0208 0.1160  0.1210  390 PHE   A CB  
2990 C  CG  . PHE   A 411 ? 0.4887 0.8081 0.4020 -0.0133 0.1084  0.1147  390 PHE   A CG  
2991 C  CD1 . PHE   A 411 ? 0.5420 0.8215 0.4606 -0.0197 0.1036  0.1235  390 PHE   A CD1 
2992 C  CD2 . PHE   A 411 ? 0.5447 0.8781 0.4433 0.0003  0.1057  0.0988  390 PHE   A CD2 
2993 C  CE1 . PHE   A 411 ? 0.4891 0.7446 0.3980 -0.0128 0.0967  0.1179  390 PHE   A CE1 
2994 C  CE2 . PHE   A 411 ? 0.6157 0.9240 0.5050 0.0065  0.0985  0.0930  390 PHE   A CE2 
2995 C  CZ  . PHE   A 411 ? 0.5627 0.8327 0.4568 -0.0001 0.0943  0.1033  390 PHE   A CZ  
2996 N  N   . GLY   A 412 ? 0.4307 0.7257 0.3975 -0.0292 0.1146  0.1069  391 GLY   A N   
2997 C  CA  . GLY   A 412 ? 0.4092 0.6828 0.3937 -0.0414 0.1142  0.1145  391 GLY   A CA  
2998 C  C   . GLY   A 412 ? 0.4318 0.6700 0.4145 -0.0486 0.1089  0.1272  391 GLY   A C   
2999 O  O   . GLY   A 412 ? 0.4354 0.6582 0.4042 -0.0414 0.1041  0.1251  391 GLY   A O   
3000 N  N   . TYR   A 413 ? 0.4057 0.6313 0.4042 -0.0629 0.1092  0.1398  392 TYR   A N   
3001 C  CA  . TYR   A 413 ? 0.4353 0.6262 0.4363 -0.0700 0.1035  0.1515  392 TYR   A CA  
3002 C  C   . TYR   A 413 ? 0.4306 0.6026 0.4538 -0.0805 0.1020  0.1502  392 TYR   A C   
3003 O  O   . TYR   A 413 ? 0.4591 0.6443 0.4978 -0.0917 0.1060  0.1565  392 TYR   A O   
3004 C  CB  . TYR   A 413 ? 0.5173 0.7137 0.5145 -0.0782 0.1042  0.1734  392 TYR   A CB  
3005 C  CG  . TYR   A 413 ? 0.5940 0.7566 0.5889 -0.0800 0.0966  0.1841  392 TYR   A CG  
3006 C  CD1 . TYR   A 413 ? 0.5569 0.6897 0.5701 -0.0906 0.0925  0.1911  392 TYR   A CD1 
3007 C  CD2 . TYR   A 413 ? 0.5849 0.7466 0.5606 -0.0706 0.0931  0.1861  392 TYR   A CD2 
3008 C  CE1 . TYR   A 413 ? 0.6009 0.7030 0.6138 -0.0906 0.0848  0.1997  392 TYR   A CE1 
3009 C  CE2 . TYR   A 413 ? 0.7148 0.8474 0.6897 -0.0712 0.0856  0.1958  392 TYR   A CE2 
3010 C  CZ  . TYR   A 413 ? 0.7221 0.8245 0.7158 -0.0806 0.0815  0.2026  392 TYR   A CZ  
3011 O  OH  . TYR   A 413 ? 0.7624 0.8361 0.7570 -0.0795 0.0734  0.2109  392 TYR   A OH  
3012 N  N   . VAL   A 414 ? 0.4482 0.5917 0.4736 -0.0773 0.0960  0.1416  393 VAL   A N   
3013 C  CA  . VAL   A 414 ? 0.4970 0.6231 0.5431 -0.0862 0.0934  0.1373  393 VAL   A CA  
3014 C  C   . VAL   A 414 ? 0.5065 0.5963 0.5555 -0.0895 0.0858  0.1437  393 VAL   A C   
3015 O  O   . VAL   A 414 ? 0.4644 0.5390 0.5009 -0.0796 0.0813  0.1391  393 VAL   A O   
3016 C  CB  . VAL   A 414 ? 0.5044 0.6355 0.5532 -0.0782 0.0929  0.1185  393 VAL   A CB  
3017 C  CG1 . VAL   A 414 ? 0.4982 0.6166 0.5694 -0.0883 0.0898  0.1136  393 VAL   A CG1 
3018 C  CG2 . VAL   A 414 ? 0.4608 0.6268 0.5073 -0.0719 0.0990  0.1112  393 VAL   A CG2 
3019 N  N   . THR   A 415 ? 0.5555 0.6316 0.6226 -0.1030 0.0837  0.1534  394 THR   A N   
3020 C  CA  . THR   A 415 ? 0.5665 0.6072 0.6409 -0.1059 0.0754  0.1584  394 THR   A CA  
3021 C  C   . THR   A 415 ? 0.6397 0.6629 0.7329 -0.1100 0.0705  0.1440  394 THR   A C   
3022 O  O   . THR   A 415 ? 0.6499 0.6880 0.7566 -0.1168 0.0735  0.1357  394 THR   A O   
3023 C  CB  . THR   A 415 ? 0.5898 0.6232 0.6743 -0.1175 0.0744  0.1781  394 THR   A CB  
3024 O  OG1 . THR   A 415 ? 0.6993 0.7553 0.7667 -0.1145 0.0793  0.1920  394 THR   A OG1 
3025 C  CG2 . THR   A 415 ? 0.5833 0.5794 0.6750 -0.1170 0.0647  0.1826  394 THR   A CG2 
3026 N  N   . ARG   A 416 ? 0.6477 0.6416 0.7428 -0.1053 0.0625  0.1401  395 ARG   A N   
3027 C  CA  . ARG   A 416 ? 0.6830 0.6601 0.7966 -0.1081 0.0566  0.1251  395 ARG   A CA  
3028 C  C   . ARG   A 416 ? 0.7855 0.7494 0.9240 -0.1228 0.0527  0.1280  395 ARG   A C   
3029 O  O   . ARG   A 416 ? 0.8582 0.8107 1.0002 -0.1279 0.0513  0.1437  395 ARG   A O   
3030 C  CB  . ARG   A 416 ? 0.6348 0.5863 0.7440 -0.0971 0.0493  0.1192  395 ARG   A CB  
3031 C  CG  . ARG   A 416 ? 0.6550 0.5910 0.7829 -0.0975 0.0430  0.1009  395 ARG   A CG  
3032 C  CD  . ARG   A 416 ? 0.5869 0.5278 0.7042 -0.0854 0.0439  0.0887  395 ARG   A CD  
3033 N  NE  . ARG   A 416 ? 0.6154 0.5404 0.7497 -0.0833 0.0378  0.0702  395 ARG   A NE  
3034 C  CZ  . ARG   A 416 ? 0.6852 0.5915 0.8173 -0.0730 0.0330  0.0636  395 ARG   A CZ  
3035 N  NH1 . ARG   A 416 ? 0.6633 0.5636 0.7777 -0.0642 0.0329  0.0751  395 ARG   A NH1 
3036 N  NH2 . ARG   A 416 ? 0.6976 0.5945 0.8455 -0.0710 0.0281  0.0429  395 ARG   A NH2 
3037 N  N   . GLU   A 417 ? 0.9221 0.8888 1.0791 -0.1297 0.0505  0.1128  396 GLU   A N   
3038 C  CA  . GLU   A 417 ? 1.0178 0.9696 1.2003 -0.1433 0.0450  0.1113  396 GLU   A CA  
3039 C  C   . GLU   A 417 ? 1.1604 1.0759 1.3534 -0.1383 0.0342  0.1038  396 GLU   A C   
3040 O  O   . GLU   A 417 ? 1.1203 1.0295 1.3123 -0.1287 0.0302  0.0870  396 GLU   A O   
3041 C  CB  . GLU   A 417 ? 1.0334 1.0048 1.2322 -0.1524 0.0452  0.0952  396 GLU   A CB  
3042 C  CG  . GLU   A 417 ? 1.0974 1.1040 1.2951 -0.1604 0.0551  0.1029  396 GLU   A CG  
3043 C  CD  . GLU   A 417 ? 1.0806 1.1191 1.2688 -0.1525 0.0607  0.0917  396 GLU   A CD  
3044 O  OE1 . GLU   A 417 ? 1.0703 1.1055 1.2586 -0.1453 0.0557  0.0767  396 GLU   A OE1 
3045 O  OE2 . GLU   A 417 ? 0.9256 0.9935 1.1081 -0.1523 0.0698  0.0978  396 GLU   A OE2 
3046 N  N   . PRO   A 418 ? 1.3289 1.2217 1.5338 -0.1438 0.0294  0.1154  397 PRO   A N   
3047 C  CA  . PRO   A 418 ? 1.2709 1.1307 1.4845 -0.1355 0.0195  0.1093  397 PRO   A CA  
3048 C  C   . PRO   A 418 ? 1.2752 1.1243 1.5081 -0.1347 0.0118  0.0821  397 PRO   A C   
3049 O  O   . PRO   A 418 ? 1.2479 1.1085 1.4947 -0.1453 0.0115  0.0711  397 PRO   A O   
3050 C  CB  . PRO   A 418 ? 1.3215 1.1635 1.5484 -0.1443 0.0164  0.1288  397 PRO   A CB  
3051 C  CG  . PRO   A 418 ? 1.3146 1.1832 1.5312 -0.1541 0.0264  0.1490  397 PRO   A CG  
3052 C  CD  . PRO   A 418 ? 1.2993 1.1972 1.5118 -0.1574 0.0330  0.1352  397 PRO   A CD  
3053 N  N   . LEU   A 419 ? 1.2092 1.0390 1.4430 -0.1213 0.0053  0.0700  398 LEU   A N   
3054 C  CA  . LEU   A 419 ? 1.1188 0.9387 1.3707 -0.1176 -0.0026 0.0418  398 LEU   A CA  
3055 C  C   . LEU   A 419 ? 1.0643 0.9099 1.3170 -0.1216 0.0001  0.0229  398 LEU   A C   
3056 O  O   . LEU   A 419 ? 0.9784 0.8267 1.2351 -0.1136 -0.0038 -0.0021 398 LEU   A O   
3057 C  CB  . LEU   A 419 ? 0.9489 0.7456 1.2281 -0.1257 -0.0110 0.0396  398 LEU   A CB  
3058 N  N   . VAL   A 423 ? 0.7032 0.5007 0.9117 -0.0363 -0.0119 -0.0008 402 VAL   A N   
3059 C  CA  . VAL   A 423 ? 0.6881 0.5013 0.8743 -0.0296 -0.0057 0.0022  402 VAL   A CA  
3060 C  C   . VAL   A 423 ? 0.6612 0.4683 0.8415 -0.0158 -0.0088 0.0037  402 VAL   A C   
3061 O  O   . VAL   A 423 ? 0.6744 0.4646 0.8637 -0.0130 -0.0147 0.0113  402 VAL   A O   
3062 C  CB  . VAL   A 423 ? 0.6416 0.4640 0.8095 -0.0376 0.0015  0.0263  402 VAL   A CB  
3063 C  CG1 . VAL   A 423 ? 0.6522 0.4858 0.8266 -0.0511 0.0053  0.0242  402 VAL   A CG1 
3064 C  CG2 . VAL   A 423 ? 0.5958 0.4059 0.7592 -0.0392 -0.0006 0.0506  402 VAL   A CG2 
3065 N  N   . THR   A 424 ? 0.6043 0.4260 0.7710 -0.0076 -0.0050 -0.0035 403 THR   A N   
3066 C  CA  . THR   A 424 ? 0.5265 0.3474 0.6862 0.0048  -0.0072 -0.0016 403 THR   A CA  
3067 C  C   . THR   A 424 ? 0.5689 0.3952 0.7059 0.0050  -0.0032 0.0204  403 THR   A C   
3068 O  O   . THR   A 424 ? 0.5444 0.3778 0.6701 -0.0034 0.0023  0.0321  403 THR   A O   
3069 C  CB  . THR   A 424 ? 0.5223 0.3596 0.6831 0.0144  -0.0060 -0.0255 403 THR   A CB  
3070 O  OG1 . THR   A 424 ? 0.5041 0.3582 0.6491 0.0127  0.0015  -0.0248 403 THR   A OG1 
3071 C  CG2 . THR   A 424 ? 0.5018 0.3426 0.6811 0.0134  -0.0090 -0.0507 403 THR   A CG2 
3072 N  N   . SER   A 425 ? 0.5082 0.3341 0.6390 0.0151  -0.0061 0.0243  404 SER   A N   
3073 C  CA  . SER   A 425 ? 0.5189 0.3518 0.6282 0.0166  -0.0039 0.0423  404 SER   A CA  
3074 C  C   . SER   A 425 ? 0.5130 0.3631 0.6073 0.0144  0.0035  0.0411  404 SER   A C   
3075 O  O   . SER   A 425 ? 0.5331 0.3910 0.6091 0.0132  0.0061  0.0554  404 SER   A O   
3076 C  CB  . SER   A 425 ? 0.5442 0.3770 0.6524 0.0286  -0.0089 0.0416  404 SER   A CB  
3077 O  OG  . SER   A 425 ? 0.6644 0.5059 0.7523 0.0300  -0.0079 0.0565  404 SER   A OG  
3078 N  N   . LEU   A 426 ? 0.4600 0.3177 0.5619 0.0145  0.0071  0.0233  405 LEU   A N   
3079 C  CA  . LEU   A 426 ? 0.4939 0.3710 0.5785 0.0122  0.0142  0.0224  405 LEU   A CA  
3080 C  C   . LEU   A 426 ? 0.4623 0.3428 0.5400 0.0015  0.0189  0.0332  405 LEU   A C   
3081 O  O   . LEU   A 426 ? 0.4264 0.3231 0.4863 0.0004  0.0237  0.0367  405 LEU   A O   
3082 C  CB  . LEU   A 426 ? 0.3819 0.2765 0.4687 0.0143  0.0159  0.0005  405 LEU   A CB  
3083 C  CG  . LEU   A 426 ? 0.3586 0.2657 0.4417 0.0240  0.0150  -0.0072 405 LEU   A CG  
3084 C  CD1 . LEU   A 426 ? 0.4096 0.3016 0.5107 0.0327  0.0085  -0.0109 405 LEU   A CD1 
3085 C  CD2 . LEU   A 426 ? 0.3712 0.3027 0.4521 0.0242  0.0182  -0.0246 405 LEU   A CD2 
3086 N  N   . ASP   A 427 ? 0.4874 0.3533 0.5811 -0.0063 0.0174  0.0382  406 ASP   A N   
3087 C  CA  . ASP   A 427 ? 0.5026 0.3747 0.5919 -0.0172 0.0221  0.0507  406 ASP   A CA  
3088 C  C   . ASP   A 427 ? 0.5382 0.4133 0.6100 -0.0165 0.0216  0.0705  406 ASP   A C   
3089 O  O   . ASP   A 427 ? 0.5675 0.4328 0.6435 -0.0197 0.0175  0.0807  406 ASP   A O   
3090 C  CB  . ASP   A 427 ? 0.4914 0.3545 0.6013 -0.0266 0.0191  0.0461  406 ASP   A CB  
3091 C  CG  . ASP   A 427 ? 0.6313 0.5065 0.7495 -0.0315 0.0219  0.0280  406 ASP   A CG  
3092 O  OD1 . ASP   A 427 ? 0.6176 0.5014 0.7335 -0.0240 0.0205  0.0091  406 ASP   A OD1 
3093 O  OD2 . ASP   A 427 ? 0.6699 0.5529 0.7930 -0.0424 0.0249  0.0324  406 ASP   A OD2 
3094 N  N   . SER   A 428 ? 0.4509 0.3406 0.5031 -0.0122 0.0258  0.0746  407 SER   A N   
3095 C  CA  . SER   A 428 ? 0.4836 0.3801 0.5180 -0.0103 0.0249  0.0885  407 SER   A CA  
3096 C  C   . SER   A 428 ? 0.3889 0.3042 0.4049 -0.0069 0.0303  0.0872  407 SER   A C   
3097 O  O   . SER   A 428 ? 0.3915 0.3087 0.4061 -0.0017 0.0319  0.0769  407 SER   A O   
3098 C  CB  . SER   A 428 ? 0.4669 0.3524 0.5009 -0.0022 0.0174  0.0903  407 SER   A CB  
3099 O  OG  . SER   A 428 ? 0.4572 0.3539 0.4720 0.0016  0.0169  0.0991  407 SER   A OG  
3100 N  N   . PHE   A 429 ? 0.4268 0.3563 0.4290 -0.0093 0.0330  0.0966  408 PHE   A N   
3101 C  CA  . PHE   A 429 ? 0.4300 0.3769 0.4155 -0.0042 0.0368  0.0930  408 PHE   A CA  
3102 C  C   . PHE   A 429 ? 0.4299 0.3741 0.4061 0.0050  0.0320  0.0897  408 PHE   A C   
3103 O  O   . PHE   A 429 ? 0.4314 0.3856 0.3961 0.0103  0.0339  0.0839  408 PHE   A O   
3104 C  CB  . PHE   A 429 ? 0.4249 0.3901 0.3990 -0.0078 0.0408  0.1015  408 PHE   A CB  
3105 C  CG  . PHE   A 429 ? 0.4290 0.4041 0.4111 -0.0161 0.0469  0.1019  408 PHE   A CG  
3106 C  CD1 . PHE   A 429 ? 0.4290 0.4148 0.4124 -0.0145 0.0516  0.0918  408 PHE   A CD1 
3107 C  CD2 . PHE   A 429 ? 0.4298 0.4039 0.4193 -0.0253 0.0476  0.1127  408 PHE   A CD2 
3108 C  CE1 . PHE   A 429 ? 0.4505 0.4484 0.4428 -0.0219 0.0567  0.0916  408 PHE   A CE1 
3109 C  CE2 . PHE   A 429 ? 0.4758 0.4610 0.4745 -0.0337 0.0530  0.1128  408 PHE   A CE2 
3110 C  CZ  . PHE   A 429 ? 0.4508 0.4490 0.4510 -0.0320 0.0574  0.1017  408 PHE   A CZ  
3111 N  N   . GLY   A 430 ? 0.4352 0.3662 0.4174 0.0075  0.0253  0.0928  409 GLY   A N   
3112 C  CA  . GLY   A 430 ? 0.4111 0.3404 0.3891 0.0159  0.0204  0.0880  409 GLY   A CA  
3113 C  C   . GLY   A 430 ? 0.3895 0.3150 0.3752 0.0190  0.0218  0.0752  409 GLY   A C   
3114 O  O   . GLY   A 430 ? 0.3635 0.2944 0.3439 0.0239  0.0191  0.0679  409 GLY   A O   
3115 N  N   . ASN   A 431 ? 0.3586 0.2790 0.3572 0.0145  0.0244  0.0689  410 ASN   A N   
3116 C  CA  . ASN   A 431 ? 0.3765 0.3013 0.3806 0.0154  0.0250  0.0538  410 ASN   A CA  
3117 C  C   . ASN   A 431 ? 0.4076 0.3451 0.4041 0.0126  0.0297  0.0494  410 ASN   A C   
3118 O  O   . ASN   A 431 ? 0.4021 0.3451 0.4039 0.0112  0.0308  0.0401  410 ASN   A O   
3119 C  CB  . ASN   A 431 ? 0.4102 0.3265 0.4324 0.0134  0.0241  0.0464  410 ASN   A CB  
3120 C  CG  . ASN   A 431 ? 0.3674 0.2930 0.3940 0.0159  0.0241  0.0313  410 ASN   A CG  
3121 O  OD1 . ASN   A 431 ? 0.3779 0.3114 0.3988 0.0201  0.0228  0.0289  410 ASN   A OD1 
3122 N  ND2 . ASN   A 431 ? 0.3532 0.2810 0.3904 0.0125  0.0254  0.0210  410 ASN   A ND2 
3123 N  N   . LEU   A 432 ? 0.3643 0.3087 0.3489 0.0125  0.0320  0.0557  411 LEU   A N   
3124 C  CA  . LEU   A 432 ? 0.3636 0.3198 0.3430 0.0120  0.0354  0.0510  411 LEU   A CA  
3125 C  C   . LEU   A 432 ? 0.3951 0.3567 0.3619 0.0177  0.0335  0.0501  411 LEU   A C   
3126 O  O   . LEU   A 432 ? 0.4511 0.4141 0.4093 0.0197  0.0324  0.0563  411 LEU   A O   
3127 C  CB  . LEU   A 432 ? 0.3808 0.3443 0.3622 0.0065  0.0408  0.0559  411 LEU   A CB  
3128 C  CG  . LEU   A 432 ? 0.5009 0.4728 0.4898 0.0033  0.0434  0.0487  411 LEU   A CG  
3129 C  CD1 . LEU   A 432 ? 0.4697 0.4352 0.4705 0.0006  0.0410  0.0418  411 LEU   A CD1 
3130 C  CD2 . LEU   A 432 ? 0.4240 0.4065 0.4161 -0.0026 0.0486  0.0544  411 LEU   A CD2 
3131 N  N   . GLU   A 433 ? 0.4154 0.3804 0.3820 0.0201  0.0323  0.0424  412 GLU   A N   
3132 C  CA  . GLU   A 433 ? 0.3972 0.3658 0.3557 0.0253  0.0296  0.0381  412 GLU   A CA  
3133 C  C   . GLU   A 433 ? 0.3885 0.3631 0.3500 0.0268  0.0312  0.0327  412 GLU   A C   
3134 O  O   . GLU   A 433 ? 0.3968 0.3730 0.3660 0.0237  0.0332  0.0328  412 GLU   A O   
3135 C  CB  . GLU   A 433 ? 0.4088 0.3710 0.3691 0.0272  0.0232  0.0347  412 GLU   A CB  
3136 C  CG  . GLU   A 433 ? 0.6202 0.5843 0.5742 0.0320  0.0186  0.0283  412 GLU   A CG  
3137 C  CD  . GLU   A 433 ? 0.7494 0.7153 0.6952 0.0344  0.0146  0.0298  412 GLU   A CD  
3138 O  OE1 . GLU   A 433 ? 0.6923 0.6541 0.6421 0.0330  0.0126  0.0348  412 GLU   A OE1 
3139 O  OE2 . GLU   A 433 ? 0.6812 0.6549 0.6170 0.0387  0.0129  0.0251  412 GLU   A OE2 
3140 N  N   . VAL   A 434 ? 0.3755 0.3546 0.3315 0.0324  0.0297  0.0268  413 VAL   A N   
3141 C  CA  . VAL   A 434 ? 0.3646 0.3471 0.3262 0.0363  0.0292  0.0206  413 VAL   A CA  
3142 C  C   . VAL   A 434 ? 0.3620 0.3364 0.3252 0.0412  0.0218  0.0126  413 VAL   A C   
3143 O  O   . VAL   A 434 ? 0.4060 0.3815 0.3613 0.0444  0.0191  0.0076  413 VAL   A O   
3144 C  CB  . VAL   A 434 ? 0.3999 0.3987 0.3580 0.0394  0.0351  0.0185  413 VAL   A CB  
3145 C  CG1 . VAL   A 434 ? 0.4126 0.4204 0.3584 0.0443  0.0352  0.0140  413 VAL   A CG1 
3146 C  CG2 . VAL   A 434 ? 0.3374 0.3400 0.3050 0.0446  0.0340  0.0122  413 VAL   A CG2 
3147 N  N   . SER   A 435 ? 0.3965 0.3634 0.3707 0.0413  0.0178  0.0121  414 SER   A N   
3148 C  CA  . SER   A 435 ? 0.3789 0.3345 0.3596 0.0441  0.0096  0.0060  414 SER   A CA  
3149 C  C   . SER   A 435 ? 0.4062 0.3635 0.3893 0.0533  0.0072  -0.0059 414 SER   A C   
3150 O  O   . SER   A 435 ? 0.4235 0.3925 0.4059 0.0576  0.0123  -0.0077 414 SER   A O   
3151 C  CB  . SER   A 435 ? 0.3485 0.2958 0.3416 0.0393  0.0059  0.0137  414 SER   A CB  
3152 O  OG  . SER   A 435 ? 0.3761 0.3246 0.3773 0.0433  0.0054  0.0145  414 SER   A OG  
3153 N  N   . PRO   A 436 ? 0.4170 0.3643 0.4051 0.0569  -0.0009 -0.0159 415 PRO   A N   
3154 C  CA  . PRO   A 436 ? 0.3644 0.3104 0.3601 0.0671  -0.0051 -0.0301 415 PRO   A CA  
3155 C  C   . PRO   A 436 ? 0.3834 0.3210 0.3954 0.0687  -0.0076 -0.0242 415 PRO   A C   
3156 O  O   . PRO   A 436 ? 0.4300 0.3630 0.4466 0.0608  -0.0072 -0.0091 415 PRO   A O   
3157 C  CB  . PRO   A 436 ? 0.4402 0.3730 0.4416 0.0679  -0.0154 -0.0416 415 PRO   A CB  
3158 C  CG  . PRO   A 436 ? 0.4054 0.3415 0.3956 0.0599  -0.0142 -0.0348 415 PRO   A CG  
3159 C  CD  . PRO   A 436 ? 0.3937 0.3322 0.3824 0.0522  -0.0072 -0.0168 415 PRO   A CD  
3160 N  N   . PRO   A 437 ? 0.4062 0.3445 0.4276 0.0796  -0.0104 -0.0357 416 PRO   A N   
3161 C  CA  . PRO   A 437 ? 0.4094 0.3377 0.4490 0.0825  -0.0153 -0.0288 416 PRO   A CA  
3162 C  C   . PRO   A 437 ? 0.4056 0.3113 0.4584 0.0745  -0.0243 -0.0177 416 PRO   A C   
3163 O  O   . PRO   A 437 ? 0.4316 0.3241 0.4880 0.0719  -0.0309 -0.0244 416 PRO   A O   
3164 C  CB  . PRO   A 437 ? 0.3922 0.3211 0.4425 0.0974  -0.0197 -0.0480 416 PRO   A CB  
3165 C  CG  . PRO   A 437 ? 0.4026 0.3554 0.4345 0.1019  -0.0112 -0.0613 416 PRO   A CG  
3166 C  CD  . PRO   A 437 ? 0.3892 0.3412 0.4050 0.0909  -0.0090 -0.0554 416 PRO   A CD  
3167 N  N   . VAL   A 438 ? 0.3845 0.2890 0.4445 0.0697  -0.0246 0.0001  417 VAL   A N   
3168 C  CA  . VAL   A 438 ? 0.4358 0.3272 0.5051 0.0592  -0.0305 0.0153  417 VAL   A CA  
3169 C  C   . VAL   A 438 ? 0.4776 0.3701 0.5557 0.0595  -0.0329 0.0282  417 VAL   A C   
3170 O  O   . VAL   A 438 ? 0.4539 0.3584 0.5316 0.0667  -0.0298 0.0293  417 VAL   A O   
3171 C  CB  . VAL   A 438 ? 0.4356 0.3357 0.4942 0.0474  -0.0250 0.0274  417 VAL   A CB  
3172 C  CG1 . VAL   A 438 ? 0.4128 0.3135 0.4604 0.0452  -0.0231 0.0159  417 VAL   A CG1 
3173 C  CG2 . VAL   A 438 ? 0.3698 0.2909 0.4164 0.0463  -0.0155 0.0341  417 VAL   A CG2 
3174 N  N   . THR   A 439 ? 0.4633 0.3452 0.5509 0.0516  -0.0391 0.0382  418 THR   A N   
3175 C  CA  . THR   A 439 ? 0.4839 0.3679 0.5790 0.0495  -0.0423 0.0539  418 THR   A CA  
3176 C  C   . THR   A 439 ? 0.5211 0.4129 0.6134 0.0352  -0.0410 0.0714  418 THR   A C   
3177 O  O   . THR   A 439 ? 0.5342 0.4195 0.6302 0.0269  -0.0429 0.0717  418 THR   A O   
3178 C  CB  . THR   A 439 ? 0.5777 0.4438 0.6905 0.0539  -0.0515 0.0505  418 THR   A CB  
3179 O  OG1 . THR   A 439 ? 0.5708 0.4346 0.6863 0.0681  -0.0517 0.0318  418 THR   A OG1 
3180 C  CG2 . THR   A 439 ? 0.5278 0.3962 0.6486 0.0519  -0.0554 0.0690  418 THR   A CG2 
3181 N  N   . VAL   A 440 ? 0.5375 0.4469 0.6243 0.0324  -0.0378 0.0850  419 VAL   A N   
3182 C  CA  . VAL   A 440 ? 0.5949 0.5202 0.6773 0.0200  -0.0346 0.0995  419 VAL   A CA  
3183 C  C   . VAL   A 440 ? 0.5962 0.5312 0.6845 0.0180  -0.0380 0.1159  419 VAL   A C   
3184 O  O   . VAL   A 440 ? 0.6043 0.5512 0.6883 0.0239  -0.0369 0.1182  419 VAL   A O   
3185 C  CB  . VAL   A 440 ? 0.5492 0.4938 0.6159 0.0180  -0.0255 0.0975  419 VAL   A CB  
3186 C  CG1 . VAL   A 440 ? 0.5784 0.5407 0.6416 0.0063  -0.0220 0.1081  419 VAL   A CG1 
3187 C  CG2 . VAL   A 440 ? 0.4481 0.3827 0.5095 0.0227  -0.0226 0.0820  419 VAL   A CG2 
3188 N  N   . ASN   A 441 ? 0.6825 0.6147 0.7819 0.0095  -0.0426 0.1282  420 ASN   A N   
3189 C  CA  . ASN   A 441 ? 0.6965 0.6384 0.8029 0.0066  -0.0466 0.1464  420 ASN   A CA  
3190 C  C   . ASN   A 441 ? 0.7033 0.6353 0.8153 0.0186  -0.0519 0.1445  420 ASN   A C   
3191 O  O   . ASN   A 441 ? 0.7699 0.7188 0.8778 0.0212  -0.0515 0.1533  420 ASN   A O   
3192 C  CB  . ASN   A 441 ? 0.6875 0.6625 0.7816 0.0003  -0.0399 0.1567  420 ASN   A CB  
3193 C  CG  . ASN   A 441 ? 0.8961 0.8838 0.9849 -0.0094 -0.0342 0.1562  420 ASN   A CG  
3194 O  OD1 . ASN   A 441 ? 0.9523 0.9539 1.0275 -0.0090 -0.0269 0.1478  420 ASN   A OD1 
3195 N  ND2 . ASN   A 441 ? 0.8801 0.8637 0.9812 -0.0178 -0.0381 0.1655  420 ASN   A ND2 
3196 N  N   . GLY   A 442 ? 0.6631 0.5697 0.7853 0.0266  -0.0571 0.1316  421 GLY   A N   
3197 C  CA  . GLY   A 442 ? 0.6400 0.5367 0.7700 0.0399  -0.0624 0.1270  421 GLY   A CA  
3198 C  C   . GLY   A 442 ? 0.6455 0.5537 0.7643 0.0512  -0.0573 0.1146  421 GLY   A C   
3199 O  O   . GLY   A 442 ? 0.6217 0.5236 0.7481 0.0642  -0.0611 0.1069  421 GLY   A O   
3200 N  N   . LYS   A 443 ? 0.5803 0.5066 0.6836 0.0469  -0.0490 0.1123  422 LYS   A N   
3201 C  CA  . LYS   A 443 ? 0.5370 0.4771 0.6328 0.0560  -0.0442 0.1020  422 LYS   A CA  
3202 C  C   . LYS   A 443 ? 0.5682 0.4977 0.6614 0.0611  -0.0405 0.0829  422 LYS   A C   
3203 O  O   . LYS   A 443 ? 0.5262 0.4528 0.6123 0.0531  -0.0366 0.0806  422 LYS   A O   
3204 C  CB  . LYS   A 443 ? 0.5156 0.4834 0.5986 0.0483  -0.0374 0.1106  422 LYS   A CB  
3205 C  CG  . LYS   A 443 ? 0.5574 0.5461 0.6385 0.0565  -0.0348 0.1070  422 LYS   A CG  
3206 C  CD  . LYS   A 443 ? 0.5820 0.5790 0.6553 0.0577  -0.0260 0.0953  422 LYS   A CD  
3207 C  CE  . LYS   A 443 ? 0.5573 0.5817 0.6301 0.0637  -0.0220 0.0934  422 LYS   A CE  
3208 N  NZ  . LYS   A 443 ? 0.6929 0.7168 0.7795 0.0769  -0.0266 0.0864  422 LYS   A NZ  
3209 N  N   . THR   A 444 ? 0.5477 0.4745 0.6471 0.0748  -0.0415 0.0690  423 THR   A N   
3210 C  CA  . THR   A 444 ? 0.5282 0.4484 0.6259 0.0808  -0.0379 0.0497  423 THR   A CA  
3211 C  C   . THR   A 444 ? 0.4860 0.4271 0.5754 0.0829  -0.0290 0.0442  423 THR   A C   
3212 O  O   . THR   A 444 ? 0.4561 0.4179 0.5473 0.0862  -0.0261 0.0492  423 THR   A O   
3213 C  CB  . THR   A 444 ? 0.5715 0.4831 0.6816 0.0943  -0.0417 0.0353  423 THR   A CB  
3214 O  OG1 . THR   A 444 ? 0.7155 0.6062 0.8376 0.0913  -0.0505 0.0411  423 THR   A OG1 
3215 C  CG2 . THR   A 444 ? 0.5052 0.4158 0.6119 0.0991  -0.0373 0.0138  423 THR   A CG2 
3216 N  N   . TYR   A 445 ? 0.4484 0.3863 0.5298 0.0800  -0.0239 0.0346  424 TYR   A N   
3217 C  CA  . TYR   A 445 ? 0.4234 0.3816 0.4874 0.0778  -0.0123 0.0257  424 TYR   A CA  
3218 C  C   . TYR   A 445 ? 0.4018 0.3578 0.4642 0.0867  -0.0110 0.0057  424 TYR   A C   
3219 O  O   . TYR   A 445 ? 0.4419 0.3907 0.4947 0.0827  -0.0097 -0.0008 424 TYR   A O   
3220 C  CB  . TYR   A 445 ? 0.3963 0.3573 0.4453 0.0642  -0.0066 0.0327  424 TYR   A CB  
3221 C  CG  . TYR   A 445 ? 0.4176 0.3856 0.4673 0.0561  -0.0078 0.0500  424 TYR   A CG  
3222 C  CD1 . TYR   A 445 ? 0.4384 0.3937 0.4962 0.0514  -0.0151 0.0629  424 TYR   A CD1 
3223 C  CD2 . TYR   A 445 ? 0.3755 0.3655 0.4186 0.0527  -0.0020 0.0532  424 TYR   A CD2 
3224 C  CE1 . TYR   A 445 ? 0.4259 0.3936 0.4825 0.0440  -0.0155 0.0794  424 TYR   A CE1 
3225 C  CE2 . TYR   A 445 ? 0.4460 0.4472 0.4882 0.0460  -0.0033 0.0667  424 TYR   A CE2 
3226 C  CZ  . TYR   A 445 ? 0.4420 0.4337 0.4897 0.0420  -0.0096 0.0802  424 TYR   A CZ  
3227 O  OH  . TYR   A 445 ? 0.4378 0.4464 0.4829 0.0353  -0.0104 0.0946  424 TYR   A OH  
3228 N  N   . PRO   A 446 ? 0.4239 0.3892 0.4957 0.0997  -0.0116 -0.0052 425 PRO   A N   
3229 C  CA  . PRO   A 446 ? 0.3748 0.3412 0.4463 0.1101  -0.0113 -0.0266 425 PRO   A CA  
3230 C  C   . PRO   A 446 ? 0.3590 0.3447 0.4096 0.1054  -0.0001 -0.0333 425 PRO   A C   
3231 O  O   . PRO   A 446 ? 0.4118 0.4008 0.4576 0.1120  0.0003  -0.0500 425 PRO   A O   
3232 C  CB  . PRO   A 446 ? 0.4366 0.4161 0.5219 0.1203  -0.0116 -0.0329 425 PRO   A CB  
3233 C  CG  . PRO   A 446 ? 0.4217 0.4163 0.5100 0.1195  -0.0096 -0.0183 425 PRO   A CG  
3234 C  CD  . PRO   A 446 ? 0.4433 0.4221 0.5269 0.1062  -0.0129 0.0006  425 PRO   A CD  
3235 N  N   . LEU   A 447 ? 0.3928 0.3917 0.4316 0.0945  0.0082  -0.0211 426 LEU   A N   
3236 C  CA  . LEU   A 447 ? 0.3523 0.3663 0.3733 0.0885  0.0178  -0.0229 426 LEU   A CA  
3237 C  C   . LEU   A 447 ? 0.3892 0.3902 0.3992 0.0759  0.0182  -0.0125 426 LEU   A C   
3238 O  O   . LEU   A 447 ? 0.3445 0.3555 0.3418 0.0694  0.0254  -0.0091 426 LEU   A O   
3239 C  CB  . LEU   A 447 ? 0.3511 0.3919 0.3711 0.0862  0.0270  -0.0188 426 LEU   A CB  
3240 C  CG  . LEU   A 447 ? 0.3678 0.4275 0.4011 0.0989  0.0274  -0.0284 426 LEU   A CG  
3241 C  CD1 . LEU   A 447 ? 0.3330 0.4209 0.3670 0.0936  0.0364  -0.0225 426 LEU   A CD1 
3242 C  CD2 . LEU   A 447 ? 0.3930 0.4614 0.4245 0.1112  0.0279  -0.0473 426 LEU   A CD2 
3243 N  N   . GLY   A 448 ? 0.3272 0.3074 0.3436 0.0726  0.0104  -0.0068 427 GLY   A N   
3244 C  CA  . GLY   A 448 ? 0.3415 0.3130 0.3500 0.0619  0.0108  0.0019  427 GLY   A CA  
3245 C  C   . GLY   A 448 ? 0.3395 0.3196 0.3462 0.0534  0.0156  0.0139  427 GLY   A C   
3246 O  O   . GLY   A 448 ? 0.3746 0.3672 0.3860 0.0548  0.0180  0.0163  427 GLY   A O   
3247 N  N   . ARG   A 449 ? 0.3334 0.3085 0.3341 0.0451  0.0165  0.0198  428 ARG   A N   
3248 C  CA  . ARG   A 449 ? 0.2967 0.2801 0.2961 0.0375  0.0205  0.0274  428 ARG   A CA  
3249 C  C   . ARG   A 449 ? 0.3429 0.3270 0.3332 0.0324  0.0254  0.0269  428 ARG   A C   
3250 O  O   . ARG   A 449 ? 0.3679 0.3434 0.3534 0.0324  0.0235  0.0253  428 ARG   A O   
3251 C  CB  . ARG   A 449 ? 0.3085 0.2881 0.3134 0.0330  0.0160  0.0358  428 ARG   A CB  
3252 C  CG  . ARG   A 449 ? 0.3249 0.3010 0.3408 0.0374  0.0095  0.0404  428 ARG   A CG  
3253 C  CD  . ARG   A 449 ? 0.3381 0.3165 0.3583 0.0312  0.0061  0.0528  428 ARG   A CD  
3254 N  NE  . ARG   A 449 ? 0.3487 0.3466 0.3654 0.0274  0.0100  0.0568  428 ARG   A NE  
3255 C  CZ  . ARG   A 449 ? 0.3622 0.3714 0.3793 0.0218  0.0088  0.0666  428 ARG   A CZ  
3256 N  NH1 . ARG   A 449 ? 0.3428 0.3460 0.3643 0.0181  0.0046  0.0762  428 ARG   A NH1 
3257 N  NH2 . ARG   A 449 ? 0.3916 0.4213 0.4050 0.0193  0.0118  0.0666  428 ARG   A NH2 
3258 N  N   . ILE   A 450 ? 0.3306 0.3246 0.3204 0.0282  0.0307  0.0286  429 ILE   A N   
3259 C  CA  . ILE   A 450 ? 0.3165 0.3082 0.3015 0.0231  0.0342  0.0299  429 ILE   A CA  
3260 C  C   . ILE   A 450 ? 0.3386 0.3251 0.3256 0.0191  0.0320  0.0314  429 ILE   A C   
3261 O  O   . ILE   A 450 ? 0.3084 0.3012 0.3001 0.0172  0.0307  0.0323  429 ILE   A O   
3262 C  CB  . ILE   A 450 ? 0.3121 0.3146 0.3000 0.0188  0.0396  0.0308  429 ILE   A CB  
3263 C  CG1 . ILE   A 450 ? 0.2560 0.2683 0.2411 0.0224  0.0433  0.0299  429 ILE   A CG1 
3264 C  CG2 . ILE   A 450 ? 0.3900 0.3859 0.3781 0.0127  0.0413  0.0333  429 ILE   A CG2 
3265 C  CD1 . ILE   A 450 ? 0.3279 0.3549 0.3192 0.0171  0.0487  0.0319  429 ILE   A CD1 
3266 N  N   . LEU   A 451 ? 0.3234 0.3019 0.3070 0.0185  0.0315  0.0318  430 LEU   A N   
3267 C  CA  . LEU   A 451 ? 0.3230 0.2992 0.3098 0.0162  0.0296  0.0315  430 LEU   A CA  
3268 C  C   . LEU   A 451 ? 0.2918 0.2650 0.2810 0.0137  0.0319  0.0307  430 LEU   A C   
3269 O  O   . LEU   A 451 ? 0.3912 0.3584 0.3769 0.0143  0.0328  0.0340  430 LEU   A O   
3270 C  CB  . LEU   A 451 ? 0.3423 0.3117 0.3270 0.0186  0.0252  0.0319  430 LEU   A CB  
3271 C  CG  . LEU   A 451 ? 0.3786 0.3463 0.3644 0.0207  0.0215  0.0320  430 LEU   A CG  
3272 C  CD1 . LEU   A 451 ? 0.3858 0.3458 0.3700 0.0230  0.0165  0.0298  430 LEU   A CD1 
3273 C  CD2 . LEU   A 451 ? 0.2918 0.2658 0.2846 0.0175  0.0202  0.0360  430 LEU   A CD2 
3274 N  N   . ILE   A 452 ? 0.3343 0.3127 0.3302 0.0112  0.0323  0.0265  431 ILE   A N   
3275 C  CA  . ILE   A 452 ? 0.3188 0.2927 0.3218 0.0091  0.0332  0.0230  431 ILE   A CA  
3276 C  C   . ILE   A 452 ? 0.2993 0.2745 0.3078 0.0113  0.0312  0.0174  431 ILE   A C   
3277 O  O   . ILE   A 452 ? 0.3591 0.3481 0.3685 0.0110  0.0313  0.0133  431 ILE   A O   
3278 C  CB  . ILE   A 452 ? 0.3368 0.3192 0.3459 0.0046  0.0353  0.0181  431 ILE   A CB  
3279 C  CG1 . ILE   A 452 ? 0.4326 0.4187 0.4383 0.0029  0.0378  0.0233  431 ILE   A CG1 
3280 C  CG2 . ILE   A 452 ? 0.4025 0.3768 0.4227 0.0018  0.0349  0.0127  431 ILE   A CG2 
3281 C  CD1 . ILE   A 452 ? 0.5009 0.4989 0.5140 -0.0020 0.0391  0.0184  431 ILE   A CD1 
3282 N  N   . GLY   A 453 ? 0.3378 0.3013 0.3505 0.0138  0.0293  0.0180  432 GLY   A N   
3283 C  CA  . GLY   A 453 ? 0.2981 0.2648 0.3192 0.0175  0.0272  0.0107  432 GLY   A CA  
3284 C  C   . GLY   A 453 ? 0.3145 0.2870 0.3464 0.0164  0.0281  -0.0017 432 GLY   A C   
3285 O  O   . GLY   A 453 ? 0.3600 0.3237 0.3978 0.0132  0.0283  -0.0034 432 GLY   A O   
3286 N  N   . SER   A 454 ? 0.3222 0.3121 0.3577 0.0188  0.0285  -0.0112 433 SER   A N   
3287 C  CA  . SER   A 454 ? 0.3349 0.3365 0.3795 0.0187  0.0291  -0.0268 433 SER   A CA  
3288 C  C   . SER   A 454 ? 0.3958 0.4129 0.4478 0.0249  0.0288  -0.0379 433 SER   A C   
3289 O  O   . SER   A 454 ? 0.3507 0.3657 0.4036 0.0289  0.0276  -0.0326 433 SER   A O   
3290 C  CB  . SER   A 454 ? 0.3847 0.4052 0.4214 0.0134  0.0317  -0.0275 433 SER   A CB  
3291 O  OG  . SER   A 454 ? 0.4873 0.5214 0.5318 0.0130  0.0315  -0.0443 433 SER   A OG  
3292 N  N   . SER   A 455 ? 0.3523 0.3885 0.4105 0.0260  0.0299  -0.0547 434 SER   A N   
3293 C  CA  . SER   A 455 ? 0.3991 0.4595 0.4639 0.0322  0.0310  -0.0681 434 SER   A CA  
3294 C  C   . SER   A 455 ? 0.3971 0.4945 0.4517 0.0283  0.0352  -0.0704 434 SER   A C   
3295 O  O   . SER   A 455 ? 0.3840 0.4852 0.4283 0.0219  0.0361  -0.0628 434 SER   A O   
3296 C  CB  . SER   A 455 ? 0.3871 0.4409 0.4706 0.0391  0.0278  -0.0895 434 SER   A CB  
3297 O  OG  . SER   A 455 ? 0.4041 0.4586 0.4902 0.0349  0.0270  -0.1011 434 SER   A OG  
3298 N  N   . PHE   A 456 ? 0.4187 0.5461 0.4769 0.0328  0.0377  -0.0804 435 PHE   A N   
3299 C  CA  . PHE   A 456 ? 0.3893 0.5562 0.4372 0.0287  0.0415  -0.0803 435 PHE   A CA  
3300 C  C   . PHE   A 456 ? 0.4582 0.6351 0.5050 0.0276  0.0390  -0.0963 435 PHE   A C   
3301 O  O   . PHE   A 456 ? 0.4637 0.6280 0.5236 0.0324  0.0356  -0.1152 435 PHE   A O   
3302 C  CB  . PHE   A 456 ? 0.3883 0.5782 0.4380 0.0309  0.0419  -0.0814 435 PHE   A CB  
3303 C  CG  . PHE   A 456 ? 0.4349 0.6221 0.4862 0.0299  0.0439  -0.0651 435 PHE   A CG  
3304 C  CD1 . PHE   A 456 ? 0.4197 0.5951 0.4631 0.0232  0.0445  -0.0448 435 PHE   A CD1 
3305 C  CD2 . PHE   A 456 ? 0.4619 0.6570 0.5234 0.0353  0.0435  -0.0701 435 PHE   A CD2 
3306 C  CE1 . PHE   A 456 ? 0.3955 0.5638 0.4409 0.0208  0.0434  -0.0301 435 PHE   A CE1 
3307 C  CE2 . PHE   A 456 ? 0.4558 0.6514 0.5210 0.0337  0.0443  -0.0562 435 PHE   A CE2 
3308 C  CZ  . PHE   A 456 ? 0.4331 0.6149 0.4903 0.0259  0.0439  -0.0363 435 PHE   A CZ  
3309 N  N   . PRO   A 457 ? 0.4643 0.6639 0.4976 0.0211  0.0390  -0.0887 436 PRO   A N   
3310 C  CA  . PRO   A 457 ? 0.5034 0.7166 0.5364 0.0197  0.0357  -0.1042 436 PRO   A CA  
3311 C  C   . PRO   A 457 ? 0.4982 0.7240 0.5428 0.0252  0.0322  -0.1289 436 PRO   A C   
3312 O  O   . PRO   A 457 ? 0.5194 0.7354 0.5753 0.0265  0.0286  -0.1473 436 PRO   A O   
3313 C  CB  . PRO   A 457 ? 0.4026 0.6444 0.4196 0.0134  0.0353  -0.0883 436 PRO   A CB  
3314 C  CG  . PRO   A 457 ? 0.4335 0.6615 0.4442 0.0101  0.0381  -0.0629 436 PRO   A CG  
3315 C  CD  . PRO   A 457 ? 0.4174 0.6299 0.4375 0.0148  0.0406  -0.0649 436 PRO   A CD  
3316 N  N   . LEU   A 458 ? 0.4478 0.6959 0.4919 0.0281  0.0328  -0.1301 437 LEU   A N   
3317 C  CA  . LEU   A 458 ? 0.4863 0.7528 0.5416 0.0339  0.0294  -0.1537 437 LEU   A CA  
3318 C  C   . LEU   A 458 ? 0.4683 0.7102 0.5413 0.0423  0.0281  -0.1646 437 LEU   A C   
3319 O  O   . LEU   A 458 ? 0.5287 0.7865 0.6121 0.0484  0.0254  -0.1825 437 LEU   A O   
3320 C  CB  . LEU   A 458 ? 0.3869 0.6973 0.4327 0.0325  0.0305  -0.1502 437 LEU   A CB  
3321 C  CG  . LEU   A 458 ? 0.4483 0.7876 0.4782 0.0250  0.0302  -0.1373 437 LEU   A CG  
3322 C  CD1 . LEU   A 458 ? 0.3733 0.7571 0.3971 0.0242  0.0307  -0.1343 437 LEU   A CD1 
3323 C  CD2 . LEU   A 458 ? 0.4057 0.7513 0.4390 0.0240  0.0259  -0.1531 437 LEU   A CD2 
3324 N  N   . SER   A 459 ? 0.4815 0.6866 0.5589 0.0434  0.0292  -0.1539 438 SER   A N   
3325 C  CA  . SER   A 459 ? 0.4282 0.6108 0.5216 0.0517  0.0271  -0.1586 438 SER   A CA  
3326 C  C   . SER   A 459 ? 0.4681 0.6257 0.5815 0.0566  0.0203  -0.1772 438 SER   A C   
3327 O  O   . SER   A 459 ? 0.4848 0.6328 0.6134 0.0646  0.0167  -0.1852 438 SER   A O   
3328 C  CB  . SER   A 459 ? 0.4026 0.5576 0.4940 0.0512  0.0296  -0.1385 438 SER   A CB  
3329 O  OG  . SER   A 459 ? 0.4275 0.5536 0.5202 0.0478  0.0285  -0.1351 438 SER   A OG  
3330 N  N   . GLY   A 460 ? 0.4603 0.6074 0.5759 0.0516  0.0179  -0.1831 439 GLY   A N   
3331 C  CA  . GLY   A 460 ? 0.4077 0.5220 0.5445 0.0539  0.0111  -0.1942 439 GLY   A CA  
3332 C  C   . GLY   A 460 ? 0.4683 0.5395 0.6122 0.0553  0.0097  -0.1781 439 GLY   A C   
3333 O  O   . GLY   A 460 ? 0.5348 0.5767 0.6973 0.0574  0.0031  -0.1823 439 GLY   A O   
3334 N  N   . GLY   A 461 ? 0.4081 0.4757 0.5382 0.0538  0.0150  -0.1582 440 GLY   A N   
3335 C  CA  . GLY   A 461 ? 0.4103 0.4414 0.5456 0.0554  0.0131  -0.1414 440 GLY   A CA  
3336 C  C   . GLY   A 461 ? 0.3923 0.3947 0.5287 0.0474  0.0122  -0.1322 440 GLY   A C   
3337 O  O   . GLY   A 461 ? 0.4596 0.4687 0.5954 0.0409  0.0126  -0.1411 440 GLY   A O   
3338 N  N   . ARG   A 462 ? 0.4469 0.4194 0.5851 0.0474  0.0105  -0.1131 441 ARG   A N   
3339 C  CA  . ARG   A 462 ? 0.4603 0.4059 0.5992 0.0383  0.0096  -0.0995 441 ARG   A CA  
3340 C  C   . ARG   A 462 ? 0.4094 0.3716 0.5243 0.0291  0.0157  -0.0853 441 ARG   A C   
3341 O  O   . ARG   A 462 ? 0.4127 0.3971 0.5118 0.0305  0.0199  -0.0800 441 ARG   A O   
3342 C  CB  . ARG   A 462 ? 0.3932 0.3081 0.5358 0.0396  0.0054  -0.0781 441 ARG   A CB  
3343 C  CG  . ARG   A 462 ? 0.4106 0.3117 0.5690 0.0455  -0.0024 -0.0821 441 ARG   A CG  
3344 C  CD  . ARG   A 462 ? 0.4674 0.3472 0.6232 0.0476  -0.0061 -0.0588 441 ARG   A CD  
3345 N  NE  . ARG   A 462 ? 0.4439 0.3368 0.5874 0.0539  -0.0035 -0.0514 441 ARG   A NE  
3346 C  CZ  . ARG   A 462 ? 0.4032 0.2855 0.5388 0.0555  -0.0059 -0.0313 441 ARG   A CZ  
3347 N  NH1 . ARG   A 462 ? 0.4571 0.3175 0.5933 0.0514  -0.0101 -0.0149 441 ARG   A NH1 
3348 N  NH2 . ARG   A 462 ? 0.3900 0.2872 0.5169 0.0609  -0.0042 -0.0276 441 ARG   A NH2 
3349 N  N   . ARG   A 463 ? 0.4262 0.3774 0.5410 0.0196  0.0157  -0.0789 442 ARG   A N   
3350 C  CA  . ARG   A 463 ? 0.4090 0.3738 0.5047 0.0121  0.0205  -0.0663 442 ARG   A CA  
3351 C  C   . ARG   A 463 ? 0.4374 0.3808 0.5361 0.0037  0.0201  -0.0513 442 ARG   A C   
3352 O  O   . ARG   A 463 ? 0.4575 0.3823 0.5750 0.0002  0.0161  -0.0561 442 ARG   A O   
3353 C  CB  . ARG   A 463 ? 0.3994 0.3936 0.4914 0.0093  0.0221  -0.0818 442 ARG   A CB  
3354 C  CG  . ARG   A 463 ? 0.5444 0.5566 0.6170 0.0046  0.0263  -0.0685 442 ARG   A CG  
3355 C  CD  . ARG   A 463 ? 0.5311 0.5764 0.5991 0.0031  0.0269  -0.0820 442 ARG   A CD  
3356 N  NE  . ARG   A 463 ? 0.6083 0.6693 0.6598 0.0001  0.0296  -0.0669 442 ARG   A NE  
3357 C  CZ  . ARG   A 463 ? 0.6105 0.7004 0.6553 -0.0021 0.0296  -0.0714 442 ARG   A CZ  
3358 N  NH1 . ARG   A 463 ? 0.5506 0.6609 0.6015 -0.0020 0.0275  -0.0922 442 ARG   A NH1 
3359 N  NH2 . ARG   A 463 ? 0.5326 0.6320 0.5650 -0.0037 0.0309  -0.0550 442 ARG   A NH2 
3360 N  N   . MET   A 464 ? 0.4015 0.3482 0.4836 0.0005  0.0240  -0.0335 443 MET   A N   
3361 C  CA  . MET   A 464 ? 0.4700 0.4056 0.5537 -0.0079 0.0251  -0.0201 443 MET   A CA  
3362 C  C   . MET   A 464 ? 0.4416 0.3845 0.5374 -0.0159 0.0243  -0.0321 443 MET   A C   
3363 O  O   . MET   A 464 ? 0.4314 0.3963 0.5242 -0.0151 0.0245  -0.0462 443 MET   A O   
3364 C  CB  . MET   A 464 ? 0.4647 0.4102 0.5288 -0.0084 0.0297  -0.0050 443 MET   A CB  
3365 C  CG  . MET   A 464 ? 0.4706 0.4080 0.5347 -0.0152 0.0319  0.0106  443 MET   A CG  
3366 S  SD  . MET   A 464 ? 0.6456 0.5940 0.6875 -0.0120 0.0364  0.0244  443 MET   A SD  
3367 C  CE  . MET   A 464 ? 0.4565 0.3893 0.4922 -0.0052 0.0337  0.0342  443 MET   A CE  
3368 N  N   . THR   A 465 ? 0.4159 0.3423 0.5266 -0.0242 0.0228  -0.0259 444 THR   A N   
3369 C  CA  . THR   A 465 ? 0.4797 0.4120 0.6062 -0.0331 0.0207  -0.0388 444 THR   A CA  
3370 C  C   . THR   A 465 ? 0.4143 0.3753 0.5278 -0.0363 0.0247  -0.0390 444 THR   A C   
3371 O  O   . THR   A 465 ? 0.4278 0.3967 0.5250 -0.0349 0.0294  -0.0237 444 THR   A O   
3372 C  CB  . THR   A 465 ? 0.5243 0.4347 0.6705 -0.0440 0.0187  -0.0276 444 THR   A CB  
3373 O  OG1 . THR   A 465 ? 0.5729 0.4849 0.7063 -0.0476 0.0244  -0.0032 444 THR   A OG1 
3374 C  CG2 . THR   A 465 ? 0.5413 0.4211 0.7056 -0.0404 0.0124  -0.0287 444 THR   A CG2 
3375 N  N   . LYS   A 466 ? 0.3929 0.3707 0.5149 -0.0396 0.0218  -0.0578 445 LYS   A N   
3376 C  CA  . LYS   A 466 ? 0.4455 0.4532 0.5563 -0.0411 0.0240  -0.0590 445 LYS   A CA  
3377 C  C   . LYS   A 466 ? 0.4218 0.4328 0.5332 -0.0487 0.0277  -0.0426 445 LYS   A C   
3378 O  O   . LYS   A 466 ? 0.3950 0.4256 0.4927 -0.0459 0.0307  -0.0357 445 LYS   A O   
3379 C  CB  . LYS   A 466 ? 0.4303 0.4570 0.5521 -0.0442 0.0190  -0.0828 445 LYS   A CB  
3380 C  CG  . LYS   A 466 ? 0.4571 0.5179 0.5679 -0.0449 0.0196  -0.0838 445 LYS   A CG  
3381 C  CD  . LYS   A 466 ? 0.5714 0.6532 0.6945 -0.0496 0.0137  -0.1077 445 LYS   A CD  
3382 C  CE  . LYS   A 466 ? 0.5831 0.7013 0.6944 -0.0494 0.0133  -0.1062 445 LYS   A CE  
3383 N  NZ  . LYS   A 466 ? 0.6248 0.7563 0.7125 -0.0392 0.0164  -0.0956 445 LYS   A NZ  
3384 N  N   . VAL   A 467 ? 0.4356 0.4291 0.5640 -0.0582 0.0273  -0.0359 446 VAL   A N   
3385 C  CA  . VAL   A 467 ? 0.4123 0.4149 0.5425 -0.0661 0.0319  -0.0205 446 VAL   A CA  
3386 C  C   . VAL   A 467 ? 0.3969 0.4011 0.5058 -0.0586 0.0380  -0.0026 446 VAL   A C   
3387 O  O   . VAL   A 467 ? 0.3771 0.4015 0.4786 -0.0580 0.0421  0.0038  446 VAL   A O   
3388 C  CB  . VAL   A 467 ? 0.4736 0.4575 0.6273 -0.0793 0.0307  -0.0132 446 VAL   A CB  
3389 C  CG1 . VAL   A 467 ? 0.5637 0.5172 0.7170 -0.0760 0.0301  -0.0010 446 VAL   A CG1 
3390 C  CG2 . VAL   A 467 ? 0.5237 0.5248 0.6797 -0.0883 0.0366  0.0025  446 VAL   A CG2 
3391 N  N   . VAL   A 468 ? 0.3472 0.3315 0.4476 -0.0520 0.0380  0.0041  447 VAL   A N   
3392 C  CA  . VAL   A 468 ? 0.3699 0.3560 0.4507 -0.0447 0.0425  0.0182  447 VAL   A CA  
3393 C  C   . VAL   A 468 ? 0.4058 0.4094 0.4713 -0.0358 0.0430  0.0123  447 VAL   A C   
3394 O  O   . VAL   A 468 ? 0.3809 0.3981 0.4373 -0.0329 0.0464  0.0189  447 VAL   A O   
3395 C  CB  . VAL   A 468 ? 0.3774 0.3402 0.4537 -0.0397 0.0409  0.0256  447 VAL   A CB  
3396 C  CG1 . VAL   A 468 ? 0.4083 0.3757 0.4643 -0.0322 0.0444  0.0370  447 VAL   A CG1 
3397 C  CG2 . VAL   A 468 ? 0.4656 0.4097 0.5585 -0.0486 0.0395  0.0358  447 VAL   A CG2 
3398 N  N   . ARG   A 469 ? 0.3810 0.3858 0.4448 -0.0311 0.0392  0.0001  448 ARG   A N   
3399 C  CA  . ARG   A 469 ? 0.3625 0.3836 0.4132 -0.0239 0.0390  -0.0020 448 ARG   A CA  
3400 C  C   . ARG   A 469 ? 0.3346 0.3788 0.3874 -0.0263 0.0394  -0.0032 448 ARG   A C   
3401 O  O   . ARG   A 469 ? 0.3155 0.3696 0.3591 -0.0206 0.0404  0.0031  448 ARG   A O   
3402 C  CB  . ARG   A 469 ? 0.3854 0.4100 0.4354 -0.0203 0.0356  -0.0142 448 ARG   A CB  
3403 C  CG  . ARG   A 469 ? 0.4430 0.4500 0.4895 -0.0150 0.0351  -0.0125 448 ARG   A CG  
3404 C  CD  . ARG   A 469 ? 0.4993 0.5174 0.5447 -0.0107 0.0330  -0.0247 448 ARG   A CD  
3405 N  NE  . ARG   A 469 ? 0.4612 0.4792 0.5214 -0.0132 0.0301  -0.0418 448 ARG   A NE  
3406 C  CZ  . ARG   A 469 ? 0.4944 0.5331 0.5588 -0.0161 0.0283  -0.0556 448 ARG   A CZ  
3407 N  NH1 . ARG   A 469 ? 0.5274 0.5895 0.5822 -0.0168 0.0290  -0.0520 448 ARG   A NH1 
3408 N  NH2 . ARG   A 469 ? 0.4650 0.5011 0.5447 -0.0176 0.0248  -0.0742 448 ARG   A NH2 
3409 N  N   . ASP   A 470 ? 0.3078 0.3607 0.3750 -0.0344 0.0377  -0.0119 449 ASP   A N   
3410 C  CA  . ASP   A 470 ? 0.3251 0.4030 0.3964 -0.0368 0.0373  -0.0133 449 ASP   A CA  
3411 C  C   . ASP   A 470 ? 0.3085 0.3905 0.3796 -0.0370 0.0423  -0.0008 449 ASP   A C   
3412 O  O   . ASP   A 470 ? 0.3390 0.4399 0.4070 -0.0321 0.0425  0.0017  449 ASP   A O   
3413 C  CB  . ASP   A 470 ? 0.3665 0.4530 0.4558 -0.0468 0.0338  -0.0266 449 ASP   A CB  
3414 C  CG  . ASP   A 470 ? 0.4926 0.5880 0.5810 -0.0447 0.0285  -0.0432 449 ASP   A CG  
3415 O  OD1 . ASP   A 470 ? 0.5466 0.6479 0.6196 -0.0361 0.0282  -0.0416 449 ASP   A OD1 
3416 O  OD2 . ASP   A 470 ? 0.5430 0.6410 0.6468 -0.0521 0.0245  -0.0582 449 ASP   A OD2 
3417 N  N   . PHE   A 471 ? 0.2840 0.3508 0.3591 -0.0420 0.0461  0.0074  450 PHE   A N   
3418 C  CA  . PHE   A 471 ? 0.2932 0.3697 0.3667 -0.0419 0.0519  0.0187  450 PHE   A CA  
3419 C  C   . PHE   A 471 ? 0.2796 0.3563 0.3358 -0.0291 0.0532  0.0231  450 PHE   A C   
3420 O  O   . PHE   A 471 ? 0.2812 0.3759 0.3366 -0.0241 0.0553  0.0247  450 PHE   A O   
3421 C  CB  . PHE   A 471 ? 0.3372 0.3998 0.4163 -0.0503 0.0557  0.0294  450 PHE   A CB  
3422 C  CG  . PHE   A 471 ? 0.3230 0.3994 0.3965 -0.0491 0.0627  0.0413  450 PHE   A CG  
3423 C  CD1 . PHE   A 471 ? 0.3395 0.4415 0.4251 -0.0559 0.0668  0.0437  450 PHE   A CD1 
3424 C  CD2 . PHE   A 471 ? 0.3344 0.4022 0.3910 -0.0409 0.0650  0.0486  450 PHE   A CD2 
3425 C  CE1 . PHE   A 471 ? 0.3269 0.4473 0.4072 -0.0538 0.0742  0.0530  450 PHE   A CE1 
3426 C  CE2 . PHE   A 471 ? 0.3476 0.4327 0.3979 -0.0388 0.0716  0.0568  450 PHE   A CE2 
3427 C  CZ  . PHE   A 471 ? 0.3505 0.4607 0.4113 -0.0446 0.0758  0.0577  450 PHE   A CZ  
3428 N  N   . LEU   A 472 ? 0.2797 0.3371 0.3246 -0.0235 0.0513  0.0238  451 LEU   A N   
3429 C  CA  . LEU   A 472 ? 0.3048 0.3599 0.3361 -0.0126 0.0513  0.0269  451 LEU   A CA  
3430 C  C   . LEU   A 472 ? 0.3121 0.3803 0.3428 -0.0062 0.0476  0.0229  451 LEU   A C   
3431 O  O   . LEU   A 472 ? 0.2877 0.3626 0.3154 0.0017  0.0478  0.0248  451 LEU   A O   
3432 C  CB  . LEU   A 472 ? 0.2994 0.3331 0.3215 -0.0095 0.0492  0.0282  451 LEU   A CB  
3433 C  CG  . LEU   A 472 ? 0.4048 0.4241 0.4255 -0.0131 0.0514  0.0352  451 LEU   A CG  
3434 C  CD1 . LEU   A 472 ? 0.4038 0.4050 0.4183 -0.0092 0.0478  0.0345  451 LEU   A CD1 
3435 C  CD2 . LEU   A 472 ? 0.3272 0.3545 0.3404 -0.0105 0.0560  0.0427  451 LEU   A CD2 
3436 N  N   . LYS   A 473 ? 0.3041 0.3774 0.3384 -0.0088 0.0436  0.0172  452 LYS   A N   
3437 C  CA  . LYS   A 473 ? 0.3316 0.4206 0.3655 -0.0036 0.0394  0.0166  452 LYS   A CA  
3438 C  C   . LYS   A 473 ? 0.3208 0.4313 0.3640 -0.0029 0.0400  0.0166  452 LYS   A C   
3439 O  O   . LYS   A 473 ? 0.3379 0.4576 0.3811 0.0055  0.0372  0.0197  452 LYS   A O   
3440 C  CB  . LYS   A 473 ? 0.2965 0.3934 0.3310 -0.0073 0.0354  0.0101  452 LYS   A CB  
3441 C  CG  . LYS   A 473 ? 0.5058 0.6250 0.5403 -0.0034 0.0305  0.0116  452 LYS   A CG  
3442 C  CD  . LYS   A 473 ? 0.6999 0.8293 0.7294 -0.0051 0.0270  0.0073  452 LYS   A CD  
3443 C  CE  . LYS   A 473 ? 0.6744 0.8208 0.7117 -0.0125 0.0255  -0.0063 452 LYS   A CE  
3444 N  NZ  . LYS   A 473 ? 0.8245 0.9887 0.8551 -0.0124 0.0221  -0.0121 452 LYS   A NZ  
3445 N  N   . ALA   A 474 ? 0.2775 0.3965 0.3312 -0.0117 0.0432  0.0136  453 ALA   A N   
3446 C  CA  . ALA   A 474 ? 0.2480 0.3921 0.3131 -0.0122 0.0442  0.0130  453 ALA   A CA  
3447 C  C   . ALA   A 474 ? 0.2537 0.4022 0.3171 -0.0034 0.0482  0.0179  453 ALA   A C   
3448 O  O   . ALA   A 474 ? 0.2934 0.4646 0.3656 0.0012  0.0478  0.0169  453 ALA   A O   
3449 C  CB  . ALA   A 474 ? 0.2679 0.4196 0.3472 -0.0258 0.0469  0.0097  453 ALA   A CB  
3450 N  N   . GLN   A 475 ? 0.2655 0.3954 0.3183 -0.0003 0.0517  0.0216  454 GLN   A N   
3451 C  CA  . GLN   A 475 ? 0.2972 0.4331 0.3472 0.0098  0.0547  0.0225  454 GLN   A CA  
3452 C  C   . GLN   A 475 ? 0.2964 0.4293 0.3447 0.0229  0.0482  0.0209  454 GLN   A C   
3453 O  O   . GLN   A 475 ? 0.3187 0.4609 0.3704 0.0334  0.0488  0.0183  454 GLN   A O   
3454 C  CB  . GLN   A 475 ? 0.2632 0.3830 0.3013 0.0096  0.0591  0.0258  454 GLN   A CB  
3455 C  CG  . GLN   A 475 ? 0.2518 0.3688 0.2917 -0.0035 0.0641  0.0314  454 GLN   A CG  
3456 C  CD  . GLN   A 475 ? 0.2365 0.3793 0.2910 -0.0120 0.0690  0.0330  454 GLN   A CD  
3457 O  OE1 . GLN   A 475 ? 0.2818 0.4412 0.3367 -0.0085 0.0729  0.0327  454 GLN   A OE1 
3458 N  NE2 . GLN   A 475 ? 0.3010 0.4437 0.3674 -0.0233 0.0668  0.0319  454 GLN   A NE2 
3459 N  N   . GLN   A 476 ? 0.2989 0.4195 0.3432 0.0226  0.0420  0.0227  455 GLN   A N   
3460 C  CA  . GLN   A 476 ? 0.3372 0.4568 0.3832 0.0323  0.0346  0.0253  455 GLN   A CA  
3461 C  C   . GLN   A 476 ? 0.3308 0.4309 0.3721 0.0420  0.0323  0.0258  455 GLN   A C   
3462 O  O   . GLN   A 476 ? 0.3925 0.4783 0.4312 0.0443  0.0263  0.0307  455 GLN   A O   
3463 C  CB  . GLN   A 476 ? 0.3587 0.5037 0.4180 0.0381  0.0323  0.0242  455 GLN   A CB  
3464 C  CG  . GLN   A 476 ? 0.3796 0.5452 0.4449 0.0297  0.0304  0.0237  455 GLN   A CG  
3465 C  CD  . GLN   A 476 ? 0.4018 0.5928 0.4801 0.0375  0.0252  0.0246  455 GLN   A CD  
3466 O  OE1 . GLN   A 476 ? 0.4435 0.6347 0.5222 0.0446  0.0172  0.0310  455 GLN   A OE1 
3467 N  NE2 . GLN   A 476 ? 0.4310 0.6451 0.5211 0.0362  0.0295  0.0196  455 GLN   A NE2 
3468 N  N   . VAL   A 477 ? 0.2759 0.3775 0.3168 0.0472  0.0369  0.0204  456 VAL   A N   
3469 C  CA  . VAL   A 477 ? 0.2448 0.3332 0.2857 0.0589  0.0331  0.0166  456 VAL   A CA  
3470 C  C   . VAL   A 477 ? 0.2511 0.3140 0.2810 0.0565  0.0312  0.0177  456 VAL   A C   
3471 O  O   . VAL   A 477 ? 0.3225 0.3710 0.3546 0.0646  0.0257  0.0146  456 VAL   A O   
3472 C  CB  . VAL   A 477 ? 0.2861 0.3911 0.3301 0.0667  0.0386  0.0073  456 VAL   A CB  
3473 C  CG1 . VAL   A 477 ? 0.2644 0.3956 0.3239 0.0727  0.0383  0.0053  456 VAL   A CG1 
3474 C  CG2 . VAL   A 477 ? 0.2577 0.3706 0.2918 0.0571  0.0481  0.0078  456 VAL   A CG2 
3475 N  N   . GLN   A 478 ? 0.2951 0.3519 0.3159 0.0458  0.0346  0.0214  457 GLN   A N   
3476 C  CA  . GLN   A 478 ? 0.3317 0.3675 0.3440 0.0436  0.0322  0.0228  457 GLN   A CA  
3477 C  C   . GLN   A 478 ? 0.2947 0.3253 0.3053 0.0354  0.0302  0.0291  457 GLN   A C   
3478 O  O   . GLN   A 478 ? 0.3347 0.3558 0.3387 0.0300  0.0317  0.0298  457 GLN   A O   
3479 C  CB  . GLN   A 478 ? 0.2917 0.3256 0.2941 0.0413  0.0377  0.0199  457 GLN   A CB  
3480 C  CG  . GLN   A 478 ? 0.3119 0.3518 0.3128 0.0509  0.0387  0.0116  457 GLN   A CG  
3481 C  CD  . GLN   A 478 ? 0.2887 0.3365 0.2786 0.0480  0.0453  0.0113  457 GLN   A CD  
3482 O  OE1 . GLN   A 478 ? 0.3321 0.3889 0.3211 0.0395  0.0511  0.0178  457 GLN   A OE1 
3483 N  NE2 . GLN   A 478 ? 0.2791 0.3241 0.2614 0.0546  0.0438  0.0041  457 GLN   A NE2 
3484 N  N   . ALA   A 479 ? 0.3843 0.4243 0.4015 0.0353  0.0266  0.0335  458 ALA   A N   
3485 C  CA  . ALA   A 479 ? 0.4107 0.4535 0.4265 0.0292  0.0242  0.0391  458 ALA   A CA  
3486 C  C   . ALA   A 479 ? 0.3839 0.4155 0.3923 0.0233  0.0261  0.0383  458 ALA   A C   
3487 O  O   . ALA   A 479 ? 0.4012 0.4209 0.4081 0.0240  0.0229  0.0420  458 ALA   A O   
3488 C  CB  . ALA   A 479 ? 0.3695 0.4101 0.3904 0.0336  0.0167  0.0480  458 ALA   A CB  
3489 N  N   . PRO   A 480 ? 0.3258 0.3609 0.3321 0.0173  0.0306  0.0336  459 PRO   A N   
3490 C  CA  . PRO   A 480 ? 0.3310 0.3545 0.3327 0.0139  0.0320  0.0319  459 PRO   A CA  
3491 C  C   . PRO   A 480 ? 0.4098 0.4362 0.4106 0.0118  0.0294  0.0342  459 PRO   A C   
3492 O  O   . PRO   A 480 ? 0.3401 0.3820 0.3425 0.0103  0.0277  0.0363  459 PRO   A O   
3493 C  CB  . PRO   A 480 ? 0.3017 0.3287 0.3061 0.0084  0.0360  0.0268  459 PRO   A CB  
3494 C  CG  . PRO   A 480 ? 0.3341 0.3718 0.3428 0.0089  0.0381  0.0267  459 PRO   A CG  
3495 C  CD  . PRO   A 480 ? 0.3268 0.3746 0.3376 0.0141  0.0342  0.0295  459 PRO   A CD  
3496 N  N   . VAL   A 481 ? 0.3555 0.3703 0.3536 0.0116  0.0292  0.0342  460 VAL   A N   
3497 C  CA  . VAL   A 481 ? 0.3712 0.3912 0.3695 0.0092  0.0278  0.0360  460 VAL   A CA  
3498 C  C   . VAL   A 481 ? 0.3614 0.3776 0.3601 0.0079  0.0302  0.0288  460 VAL   A C   
3499 O  O   . VAL   A 481 ? 0.3658 0.3677 0.3631 0.0096  0.0307  0.0277  460 VAL   A O   
3500 C  CB  . VAL   A 481 ? 0.3632 0.3738 0.3623 0.0105  0.0239  0.0431  460 VAL   A CB  
3501 C  CG1 . VAL   A 481 ? 0.3692 0.3895 0.3701 0.0066  0.0235  0.0463  460 VAL   A CG1 
3502 C  CG2 . VAL   A 481 ? 0.3706 0.3807 0.3732 0.0130  0.0200  0.0502  460 VAL   A CG2 
3503 N  N   . GLU   A 482 ? 0.3741 0.4047 0.3749 0.0058  0.0312  0.0238  461 GLU   A N   
3504 C  CA  . GLU   A 482 ? 0.3435 0.3709 0.3481 0.0064  0.0323  0.0153  461 GLU   A CA  
3505 C  C   . GLU   A 482 ? 0.3421 0.3708 0.3475 0.0075  0.0313  0.0180  461 GLU   A C   
3506 O  O   . GLU   A 482 ? 0.3032 0.3476 0.3081 0.0055  0.0310  0.0229  461 GLU   A O   
3507 C  CB  . GLU   A 482 ? 0.3528 0.3974 0.3616 0.0048  0.0336  0.0039  461 GLU   A CB  
3508 C  CG  . GLU   A 482 ? 0.4356 0.4734 0.4493 0.0029  0.0340  -0.0028 461 GLU   A CG  
3509 C  CD  . GLU   A 482 ? 0.5053 0.5585 0.5255 0.0015  0.0339  -0.0181 461 GLU   A CD  
3510 O  OE1 . GLU   A 482 ? 0.6302 0.7084 0.6466 0.0004  0.0337  -0.0204 461 GLU   A OE1 
3511 O  OE2 . GLU   A 482 ? 0.5548 0.5958 0.5848 0.0019  0.0332  -0.0278 461 GLU   A OE2 
3512 N  N   . LEU   A 483 ? 0.3160 0.3302 0.3235 0.0103  0.0303  0.0162  462 LEU   A N   
3513 C  CA  . LEU   A 483 ? 0.3357 0.3522 0.3463 0.0118  0.0287  0.0172  462 LEU   A CA  
3514 C  C   . LEU   A 483 ? 0.3027 0.3258 0.3215 0.0150  0.0297  0.0064  462 LEU   A C   
3515 O  O   . LEU   A 483 ? 0.3224 0.3465 0.3447 0.0156  0.0310  -0.0025 462 LEU   A O   
3516 C  CB  . LEU   A 483 ? 0.3001 0.2984 0.3076 0.0139  0.0255  0.0226  462 LEU   A CB  
3517 C  CG  . LEU   A 483 ? 0.3066 0.2984 0.3084 0.0124  0.0238  0.0294  462 LEU   A CG  
3518 C  CD1 . LEU   A 483 ? 0.3489 0.3270 0.3470 0.0154  0.0203  0.0307  462 LEU   A CD1 
3519 C  CD2 . LEU   A 483 ? 0.3162 0.3191 0.3215 0.0086  0.0224  0.0351  462 LEU   A CD2 
3520 N  N   . TYR   A 484 ? 0.3103 0.3384 0.3342 0.0175  0.0283  0.0059  463 TYR   A N   
3521 C  CA  . TYR   A 484 ? 0.2688 0.3049 0.3032 0.0228  0.0286  -0.0057 463 TYR   A CA  
3522 C  C   . TYR   A 484 ? 0.3107 0.3265 0.3494 0.0281  0.0243  -0.0039 463 TYR   A C   
3523 O  O   . TYR   A 484 ? 0.2899 0.3067 0.3293 0.0292  0.0216  0.0013  463 TYR   A O   
3524 C  CB  . TYR   A 484 ? 0.2769 0.3420 0.3160 0.0220  0.0306  -0.0076 463 TYR   A CB  
3525 C  CG  . TYR   A 484 ? 0.3079 0.3855 0.3599 0.0295  0.0309  -0.0213 463 TYR   A CG  
3526 C  CD1 . TYR   A 484 ? 0.3483 0.4204 0.4077 0.0352  0.0306  -0.0360 463 TYR   A CD1 
3527 C  CD2 . TYR   A 484 ? 0.3162 0.4124 0.3758 0.0309  0.0308  -0.0206 463 TYR   A CD2 
3528 C  CE1 . TYR   A 484 ? 0.3571 0.4399 0.4311 0.0439  0.0300  -0.0508 463 TYR   A CE1 
3529 C  CE2 . TYR   A 484 ? 0.3524 0.4632 0.4258 0.0395  0.0310  -0.0346 463 TYR   A CE2 
3530 C  CZ  . TYR   A 484 ? 0.4112 0.5145 0.4919 0.0468  0.0304  -0.0503 463 TYR   A CZ  
3531 O  OH  . TYR   A 484 ? 0.4118 0.5283 0.5091 0.0572  0.0297  -0.0665 463 TYR   A OH  
3532 N  N   . SER   A 485 ? 0.3316 0.3296 0.3739 0.0308  0.0231  -0.0071 464 SER   A N   
3533 C  CA  . SER   A 485 ? 0.3645 0.3436 0.4109 0.0359  0.0184  -0.0025 464 SER   A CA  
3534 C  C   . SER   A 485 ? 0.3755 0.3498 0.4389 0.0431  0.0159  -0.0132 464 SER   A C   
3535 O  O   . SER   A 485 ? 0.4272 0.3855 0.4965 0.0483  0.0109  -0.0077 464 SER   A O   
3536 C  CB  . SER   A 485 ? 0.3375 0.2970 0.3750 0.0324  0.0181  0.0081  464 SER   A CB  
3537 O  OG  . SER   A 485 ? 0.3413 0.2932 0.3849 0.0298  0.0197  0.0033  464 SER   A OG  
3538 N  N   . ASP   A 486 ? 0.3514 0.3397 0.4234 0.0443  0.0184  -0.0286 465 ASP   A N   
3539 C  CA  . ASP   A 486 ? 0.4155 0.3969 0.5066 0.0523  0.0150  -0.0423 465 ASP   A CA  
3540 C  C   . ASP   A 486 ? 0.3889 0.3823 0.4919 0.0621  0.0123  -0.0481 465 ASP   A C   
3541 O  O   . ASP   A 486 ? 0.4061 0.3934 0.5279 0.0712  0.0085  -0.0605 465 ASP   A O   
3542 C  CB  . ASP   A 486 ? 0.3537 0.3488 0.4509 0.0512  0.0179  -0.0611 465 ASP   A CB  
3543 C  CG  . ASP   A 486 ? 0.4242 0.3998 0.5424 0.0570  0.0129  -0.0747 465 ASP   A CG  
3544 O  OD1 . ASP   A 486 ? 0.4479 0.3937 0.5725 0.0578  0.0078  -0.0631 465 ASP   A OD1 
3545 O  OD2 . ASP   A 486 ? 0.4361 0.4268 0.5645 0.0605  0.0133  -0.0962 465 ASP   A OD2 
3546 N  N   . TRP   A 487 ? 0.3217 0.3324 0.4169 0.0607  0.0137  -0.0404 466 TRP   A N   
3547 C  CA  . TRP   A 487 ? 0.3464 0.3683 0.4540 0.0696  0.0102  -0.0434 466 TRP   A CA  
3548 C  C   . TRP   A 487 ? 0.3476 0.3442 0.4585 0.0749  0.0024  -0.0314 466 TRP   A C   
3549 O  O   . TRP   A 487 ? 0.3377 0.3407 0.4619 0.0842  -0.0024 -0.0338 466 TRP   A O   
3550 C  CB  . TRP   A 487 ? 0.2972 0.3471 0.3980 0.0643  0.0135  -0.0382 466 TRP   A CB  
3551 C  CG  . TRP   A 487 ? 0.3521 0.3903 0.4361 0.0553  0.0126  -0.0210 466 TRP   A CG  
3552 C  CD1 . TRP   A 487 ? 0.3104 0.3444 0.3797 0.0460  0.0163  -0.0146 466 TRP   A CD1 
3553 C  CD2 . TRP   A 487 ? 0.3326 0.3635 0.4141 0.0560  0.0069  -0.0103 466 TRP   A CD2 
3554 N  NE1 . TRP   A 487 ? 0.3256 0.3488 0.3844 0.0416  0.0134  -0.0019 466 TRP   A NE1 
3555 C  CE2 . TRP   A 487 ? 0.3051 0.3269 0.3702 0.0471  0.0076  0.0004  466 TRP   A CE2 
3556 C  CE3 . TRP   A 487 ? 0.3108 0.3436 0.4028 0.0640  0.0005  -0.0096 466 TRP   A CE3 
3557 C  CZ2 . TRP   A 487 ? 0.3534 0.3686 0.4120 0.0457  0.0023  0.0093  466 TRP   A CZ2 
3558 C  CZ3 . TRP   A 487 ? 0.3081 0.3356 0.3925 0.0619  -0.0050 0.0012  466 TRP   A CZ3 
3559 C  CH2 . TRP   A 487 ? 0.3397 0.3586 0.4072 0.0527  -0.0040 0.0095  466 TRP   A CH2 
3560 N  N   . LEU   A 488 ? 0.3632 0.3349 0.4627 0.0695  0.0009  -0.0180 467 LEU   A N   
3561 C  CA  . LEU   A 488 ? 0.3695 0.3201 0.4689 0.0733  -0.0062 -0.0035 467 LEU   A CA  
3562 C  C   . LEU   A 488 ? 0.3804 0.3066 0.4919 0.0765  -0.0099 -0.0042 467 LEU   A C   
3563 O  O   . LEU   A 488 ? 0.3963 0.3149 0.5095 0.0712  -0.0064 -0.0104 467 LEU   A O   
3564 C  CB  . LEU   A 488 ? 0.3581 0.3018 0.4354 0.0645  -0.0049 0.0124  467 LEU   A CB  
3565 C  CG  . LEU   A 488 ? 0.3829 0.3450 0.4484 0.0608  -0.0040 0.0149  467 LEU   A CG  
3566 C  CD1 . LEU   A 488 ? 0.3774 0.3350 0.4239 0.0516  -0.0003 0.0223  467 LEU   A CD1 
3567 C  CD2 . LEU   A 488 ? 0.3403 0.3046 0.4076 0.0671  -0.0118 0.0220  467 LEU   A CD2 
3568 N  N   . THR   A 489 ? 0.3926 0.3095 0.5078 0.0825  -0.0166 0.0030  468 THR   A N   
3569 C  CA  . THR   A 489 ? 0.4758 0.3709 0.5987 0.0827  -0.0202 0.0046  468 THR   A CA  
3570 C  C   . THR   A 489 ? 0.4557 0.3335 0.5678 0.0717  -0.0181 0.0165  468 THR   A C   
3571 O  O   . THR   A 489 ? 0.4399 0.3074 0.5607 0.0671  -0.0169 0.0094  468 THR   A O   
3572 C  CB  . THR   A 489 ? 0.4804 0.3685 0.6073 0.0906  -0.0277 0.0150  468 THR   A CB  
3573 O  OG1 . THR   A 489 ? 0.4540 0.3614 0.5930 0.1007  -0.0292 0.0033  468 THR   A OG1 
3574 C  CG2 . THR   A 489 ? 0.4332 0.2980 0.5720 0.0909  -0.0319 0.0171  468 THR   A CG2 
3575 N  N   . VAL   A 490 ? 0.4482 0.3260 0.5420 0.0669  -0.0178 0.0335  469 VAL   A N   
3576 C  CA  . VAL   A 490 ? 0.4262 0.2938 0.5091 0.0561  -0.0147 0.0448  469 VAL   A CA  
3577 C  C   . VAL   A 490 ? 0.4728 0.3479 0.5541 0.0497  -0.0072 0.0357  469 VAL   A C   
3578 O  O   . VAL   A 490 ? 0.5097 0.3766 0.5944 0.0421  -0.0045 0.0351  469 VAL   A O   
3579 C  CB  . VAL   A 490 ? 0.4198 0.2906 0.4826 0.0538  -0.0162 0.0633  469 VAL   A CB  
3580 C  CG1 . VAL   A 490 ? 0.4696 0.3382 0.5206 0.0427  -0.0111 0.0728  469 VAL   A CG1 
3581 C  CG2 . VAL   A 490 ? 0.4433 0.3054 0.5084 0.0594  -0.0237 0.0741  469 VAL   A CG2 
3582 N  N   . GLY   A 491 ? 0.4204 0.3120 0.4980 0.0524  -0.0037 0.0293  470 GLY   A N   
3583 C  CA  . GLY   A 491 ? 0.3429 0.2472 0.4154 0.0463  0.0035  0.0187  470 GLY   A CA  
3584 C  C   . GLY   A 491 ? 0.3945 0.3032 0.4469 0.0380  0.0083  0.0287  470 GLY   A C   
3585 O  O   . GLY   A 491 ? 0.4136 0.3258 0.4633 0.0314  0.0131  0.0244  470 GLY   A O   
3586 N  N   . HIS   A 492 ? 0.3636 0.2746 0.4025 0.0391  0.0065  0.0403  471 HIS   A N   
3587 C  CA  . HIS   A 492 ? 0.3617 0.2776 0.3826 0.0333  0.0103  0.0480  471 HIS   A CA  
3588 C  C   . HIS   A 492 ? 0.3662 0.2967 0.3771 0.0342  0.0104  0.0434  471 HIS   A C   
3589 O  O   . HIS   A 492 ? 0.4046 0.3400 0.4176 0.0390  0.0058  0.0422  471 HIS   A O   
3590 C  CB  . HIS   A 492 ? 0.4033 0.3122 0.4160 0.0333  0.0079  0.0647  471 HIS   A CB  
3591 C  CG  . HIS   A 492 ? 0.4644 0.3605 0.4864 0.0289  0.0065  0.0704  471 HIS   A CG  
3592 N  ND1 . HIS   A 492 ? 0.4366 0.3302 0.4510 0.0264  0.0035  0.0840  471 HIS   A ND1 
3593 C  CD2 . HIS   A 492 ? 0.4572 0.3430 0.4958 0.0261  0.0074  0.0637  471 HIS   A CD2 
3594 C  CE1 . HIS   A 492 ? 0.4179 0.2987 0.4441 0.0218  0.0028  0.0870  471 HIS   A CE1 
3595 N  NE2 . HIS   A 492 ? 0.4574 0.3327 0.4988 0.0215  0.0046  0.0739  471 HIS   A NE2 
3596 N  N   . VAL   A 493 ? 0.3635 0.3005 0.3657 0.0294  0.0149  0.0411  472 VAL   A N   
3597 C  CA  . VAL   A 493 ? 0.3383 0.2852 0.3342 0.0294  0.0139  0.0377  472 VAL   A CA  
3598 C  C   . VAL   A 493 ? 0.3834 0.3306 0.3688 0.0323  0.0095  0.0429  472 VAL   A C   
3599 O  O   . VAL   A 493 ? 0.3942 0.3475 0.3792 0.0333  0.0056  0.0393  472 VAL   A O   
3600 C  CB  . VAL   A 493 ? 0.3478 0.2996 0.3394 0.0249  0.0183  0.0350  472 VAL   A CB  
3601 C  CG1 . VAL   A 493 ? 0.3168 0.2743 0.3175 0.0223  0.0215  0.0287  472 VAL   A CG1 
3602 C  CG2 . VAL   A 493 ? 0.3318 0.2804 0.3149 0.0233  0.0214  0.0401  472 VAL   A CG2 
3603 N  N   . ASP   A 494 ? 0.3987 0.3418 0.3761 0.0330  0.0096  0.0515  473 ASP   A N   
3604 C  CA  . ASP   A 494 ? 0.4410 0.3897 0.4061 0.0363  0.0052  0.0553  473 ASP   A CA  
3605 C  C   . ASP   A 494 ? 0.4005 0.3503 0.3706 0.0414  -0.0022 0.0574  473 ASP   A C   
3606 O  O   . ASP   A 494 ? 0.4835 0.4408 0.4437 0.0445  -0.0074 0.0599  473 ASP   A O   
3607 C  CB  . ASP   A 494 ? 0.4517 0.4023 0.4053 0.0352  0.0082  0.0658  473 ASP   A CB  
3608 C  CG  . ASP   A 494 ? 0.5506 0.4925 0.5099 0.0355  0.0066  0.0793  473 ASP   A CG  
3609 O  OD1 . ASP   A 494 ? 0.5722 0.5049 0.5458 0.0380  0.0031  0.0781  473 ASP   A OD1 
3610 O  OD2 . ASP   A 494 ? 0.6356 0.5817 0.5870 0.0324  0.0083  0.0895  473 ASP   A OD2 
3611 N  N   . GLU   A 495 ? 0.4191 0.3644 0.4049 0.0431  -0.0033 0.0551  474 GLU   A N   
3612 C  CA  . GLU   A 495 ? 0.4944 0.4440 0.4885 0.0491  -0.0105 0.0550  474 GLU   A CA  
3613 C  C   . GLU   A 495 ? 0.4068 0.3689 0.4046 0.0480  -0.0129 0.0453  474 GLU   A C   
3614 O  O   . GLU   A 495 ? 0.4764 0.4467 0.4798 0.0522  -0.0196 0.0448  474 GLU   A O   
3615 C  CB  . GLU   A 495 ? 0.4085 0.3505 0.4208 0.0529  -0.0108 0.0538  474 GLU   A CB  
3616 C  CG  . GLU   A 495 ? 0.4718 0.3976 0.4864 0.0529  -0.0101 0.0642  474 GLU   A CG  
3617 C  CD  . GLU   A 495 ? 0.5088 0.4247 0.5448 0.0583  -0.0129 0.0603  474 GLU   A CD  
3618 O  OE1 . GLU   A 495 ? 0.5347 0.4532 0.5784 0.0658  -0.0200 0.0604  474 GLU   A OE1 
3619 O  OE2 . GLU   A 495 ? 0.4842 0.3914 0.5288 0.0549  -0.0087 0.0543  474 GLU   A OE2 
3620 N  N   . PHE   A 496 ? 0.3825 0.3471 0.3791 0.0421  -0.0084 0.0389  475 PHE   A N   
3621 C  CA  . PHE   A 496 ? 0.3806 0.3558 0.3844 0.0391  -0.0108 0.0325  475 PHE   A CA  
3622 C  C   . PHE   A 496 ? 0.3898 0.3640 0.3871 0.0336  -0.0103 0.0293  475 PHE   A C   
3623 O  O   . PHE   A 496 ? 0.3789 0.3597 0.3845 0.0294  -0.0131 0.0258  475 PHE   A O   
3624 C  CB  . PHE   A 496 ? 0.3287 0.3119 0.3475 0.0376  -0.0067 0.0282  475 PHE   A CB  
3625 C  CG  . PHE   A 496 ? 0.3473 0.3274 0.3644 0.0333  0.0008  0.0269  475 PHE   A CG  
3626 C  CD1 . PHE   A 496 ? 0.3420 0.3250 0.3566 0.0269  0.0028  0.0268  475 PHE   A CD1 
3627 C  CD2 . PHE   A 496 ? 0.3661 0.3407 0.3864 0.0357  0.0046  0.0257  475 PHE   A CD2 
3628 C  CE1 . PHE   A 496 ? 0.3625 0.3456 0.3756 0.0236  0.0086  0.0266  475 PHE   A CE1 
3629 C  CE2 . PHE   A 496 ? 0.3421 0.3172 0.3612 0.0316  0.0104  0.0231  475 PHE   A CE2 
3630 C  CZ  . PHE   A 496 ? 0.3067 0.2875 0.3212 0.0259  0.0125  0.0241  475 PHE   A CZ  
3631 N  N   . MET   A 497 ? 0.3709 0.3377 0.3560 0.0335  -0.0074 0.0306  476 MET   A N   
3632 C  CA  . MET   A 497 ? 0.3707 0.3356 0.3530 0.0302  -0.0077 0.0259  476 MET   A CA  
3633 C  C   . MET   A 497 ? 0.3735 0.3363 0.3408 0.0336  -0.0072 0.0249  476 MET   A C   
3634 O  O   . MET   A 497 ? 0.3598 0.3228 0.3188 0.0360  -0.0038 0.0310  476 MET   A O   
3635 C  CB  . MET   A 497 ? 0.4033 0.3663 0.3920 0.0257  -0.0020 0.0267  476 MET   A CB  
3636 C  CG  . MET   A 497 ? 0.4319 0.3916 0.4156 0.0265  0.0049  0.0299  476 MET   A CG  
3637 S  SD  . MET   A 497 ? 0.5027 0.4629 0.4898 0.0223  0.0094  0.0297  476 MET   A SD  
3638 C  CE  . MET   A 497 ? 0.3956 0.3503 0.3778 0.0243  0.0053  0.0256  476 MET   A CE  
3639 N  N   . SER   A 498 ? 0.3679 0.3301 0.3336 0.0335  -0.0106 0.0170  477 SER   A N   
3640 C  CA  . SER   A 498 ? 0.3944 0.3594 0.3470 0.0377  -0.0098 0.0123  477 SER   A CA  
3641 C  C   . SER   A 498 ? 0.4204 0.3805 0.3793 0.0376  -0.0143 0.0010  477 SER   A C   
3642 O  O   . SER   A 498 ? 0.4296 0.3838 0.4023 0.0331  -0.0192 -0.0008 477 SER   A O   
3643 C  CB  . SER   A 498 ? 0.4398 0.4153 0.3793 0.0423  -0.0140 0.0124  477 SER   A CB  
3644 O  OG  . SER   A 498 ? 0.6063 0.5906 0.5315 0.0464  -0.0113 0.0086  477 SER   A OG  
3645 N  N   . PHE   A 499 ? 0.4127 0.3760 0.3633 0.0425  -0.0128 -0.0063 478 PHE   A N   
3646 C  CA  . PHE   A 499 ? 0.4563 0.4136 0.4141 0.0449  -0.0183 -0.0198 478 PHE   A CA  
3647 C  C   . PHE   A 499 ? 0.4300 0.3994 0.3755 0.0519  -0.0226 -0.0339 478 PHE   A C   
3648 O  O   . PHE   A 499 ? 0.4450 0.4298 0.3737 0.0559  -0.0172 -0.0312 478 PHE   A O   
3649 C  CB  . PHE   A 499 ? 0.4084 0.3607 0.3712 0.0467  -0.0130 -0.0195 478 PHE   A CB  
3650 C  CG  . PHE   A 499 ? 0.3721 0.3175 0.3448 0.0403  -0.0089 -0.0066 478 PHE   A CG  
3651 C  CD1 . PHE   A 499 ? 0.3963 0.3306 0.3851 0.0355  -0.0139 -0.0044 478 PHE   A CD1 
3652 C  CD2 . PHE   A 499 ? 0.3666 0.3181 0.3330 0.0386  -0.0005 0.0034  478 PHE   A CD2 
3653 C  CE1 . PHE   A 499 ? 0.3578 0.2915 0.3533 0.0299  -0.0099 0.0076  478 PHE   A CE1 
3654 C  CE2 . PHE   A 499 ? 0.4066 0.3554 0.3813 0.0335  0.0027  0.0122  478 PHE   A CE2 
3655 C  CZ  . PHE   A 499 ? 0.3605 0.3024 0.3482 0.0295  -0.0016 0.0143  478 PHE   A CZ  
3656 N  N   . VAL   A 500 ? 0.4739 0.4377 0.4284 0.0528  -0.0325 -0.0488 479 VAL   A N   
3657 C  CA  . VAL   A 500 ? 0.5099 0.4864 0.4546 0.0606  -0.0378 -0.0677 479 VAL   A CA  
3658 C  C   . VAL   A 500 ? 0.4884 0.4513 0.4491 0.0643  -0.0436 -0.0848 479 VAL   A C   
3659 O  O   . VAL   A 500 ? 0.4818 0.4239 0.4632 0.0583  -0.0476 -0.0806 479 VAL   A O   
3660 C  CB  . VAL   A 500 ? 0.4589 0.4442 0.4002 0.0590  -0.0472 -0.0733 479 VAL   A CB  
3661 C  CG1 . VAL   A 500 ? 0.4255 0.4230 0.3530 0.0572  -0.0426 -0.0552 479 VAL   A CG1 
3662 C  CG2 . VAL   A 500 ? 0.3903 0.3581 0.3551 0.0512  -0.0568 -0.0765 479 VAL   A CG2 
3663 N  N   . PRO   A 501 ? 0.5090 0.4838 0.4621 0.0743  -0.0442 -0.1033 480 PRO   A N   
3664 C  CA  . PRO   A 501 ? 0.5664 0.5265 0.5382 0.0797  -0.0524 -0.1235 480 PRO   A CA  
3665 C  C   . PRO   A 501 ? 0.5326 0.4856 0.5153 0.0774  -0.0668 -0.1406 480 PRO   A C   
3666 O  O   . PRO   A 501 ? 0.5523 0.5211 0.5222 0.0755  -0.0700 -0.1428 480 PRO   A O   
3667 C  CB  . PRO   A 501 ? 0.5439 0.5265 0.5018 0.0927  -0.0471 -0.1396 480 PRO   A CB  
3668 C  CG  . PRO   A 501 ? 0.5845 0.5971 0.5148 0.0929  -0.0415 -0.1340 480 PRO   A CG  
3669 C  CD  . PRO   A 501 ? 0.5232 0.5276 0.4515 0.0816  -0.0370 -0.1062 480 PRO   A CD  
3670 N  N   . ILE   A 502 ? 0.5261 0.4556 0.5349 0.0765  -0.0759 -0.1505 481 ILE   A N   
3671 C  CA  . ILE   A 502 ? 0.5653 0.4907 0.5904 0.0724  -0.0886 -0.1644 481 ILE   A CA  
3672 C  C   . ILE   A 502 ? 0.6043 0.5473 0.6269 0.0831  -0.0900 -0.1856 481 ILE   A C   
3673 O  O   . ILE   A 502 ? 0.6020 0.5373 0.6374 0.0882  -0.0890 -0.1890 481 ILE   A O   
3674 C  CB  . ILE   A 502 ? 0.5792 0.4748 0.6364 0.0622  -0.0959 -0.1552 481 ILE   A CB  
3675 C  CG1 . ILE   A 502 ? 0.5426 0.4268 0.6030 0.0504  -0.0947 -0.1340 481 ILE   A CG1 
3676 C  CG2 . ILE   A 502 ? 0.5616 0.4540 0.6372 0.0591  -0.1086 -0.1712 481 ILE   A CG2 
3677 C  CD1 . ILE   A 502 ? 0.5740 0.4360 0.6644 0.0383  -0.1000 -0.1195 481 ILE   A CD1 
3678 N  N   . PRO   A 503 ? 0.6115 0.5803 0.6182 0.0869  -0.0923 -0.1991 482 PRO   A N   
3679 C  CA  . PRO   A 503 ? 0.5818 0.5724 0.5850 0.0977  -0.0925 -0.2190 482 PRO   A CA  
3680 C  C   . PRO   A 503 ? 0.6728 0.6433 0.7064 0.0994  -0.1019 -0.2328 482 PRO   A C   
3681 O  O   . PRO   A 503 ? 0.7146 0.6609 0.7711 0.0909  -0.1118 -0.2319 482 PRO   A O   
3682 C  CB  . PRO   A 503 ? 0.6016 0.6181 0.5896 0.0979  -0.0971 -0.2290 482 PRO   A CB  
3683 C  CG  . PRO   A 503 ? 0.5669 0.5847 0.5381 0.0906  -0.0936 -0.2096 482 PRO   A CG  
3684 C  CD  . PRO   A 503 ? 0.5164 0.4990 0.5070 0.0820  -0.0948 -0.1954 482 PRO   A CD  
3685 N  N   . GLY   A 504 ? 0.6832 0.6650 0.7179 0.1101  -0.0989 -0.2445 483 GLY   A N   
3686 C  CA  . GLY   A 504 ? 0.6160 0.5813 0.6789 0.1139  -0.1085 -0.2596 483 GLY   A CA  
3687 C  C   . GLY   A 504 ? 0.6905 0.6209 0.7769 0.1083  -0.1105 -0.2441 483 GLY   A C   
3688 O  O   . GLY   A 504 ? 0.7437 0.6543 0.8571 0.1084  -0.1208 -0.2526 483 GLY   A O   
3689 N  N   . THR   A 505 ? 0.6816 0.6046 0.7589 0.1034  -0.1011 -0.2209 484 THR   A N   
3690 C  CA  . THR   A 505 ? 0.6927 0.5870 0.7897 0.0979  -0.1018 -0.2028 484 THR   A CA  
3691 C  C   . THR   A 505 ? 0.6905 0.5925 0.7727 0.1016  -0.0886 -0.1879 484 THR   A C   
3692 O  O   . THR   A 505 ? 0.6720 0.5996 0.7296 0.1067  -0.0790 -0.1899 484 THR   A O   
3693 C  CB  . THR   A 505 ? 0.6753 0.5481 0.7834 0.0829  -0.1065 -0.1851 484 THR   A CB  
3694 O  OG1 . THR   A 505 ? 0.6295 0.5103 0.7165 0.0783  -0.0970 -0.1690 484 THR   A OG1 
3695 C  CG2 . THR   A 505 ? 0.6670 0.5397 0.7846 0.0784  -0.1178 -0.1999 484 THR   A CG2 
3696 N  N   . LYS   A 506 ? 0.7070 0.5882 0.8048 0.0984  -0.0883 -0.1716 485 LYS   A N   
3697 C  CA  . LYS   A 506 ? 0.6346 0.5201 0.7219 0.0994  -0.0768 -0.1539 485 LYS   A CA  
3698 C  C   . LYS   A 506 ? 0.6660 0.5408 0.7493 0.0875  -0.0733 -0.1304 485 LYS   A C   
3699 O  O   . LYS   A 506 ? 0.6740 0.5495 0.7524 0.0868  -0.0651 -0.1135 485 LYS   A O   
3700 C  CB  . LYS   A 506 ? 0.7409 0.6149 0.8463 0.1043  -0.0782 -0.1494 485 LYS   A CB  
3701 C  CG  . LYS   A 506 ? 0.9133 0.7900 1.0320 0.1151  -0.0857 -0.1728 485 LYS   A CG  
3702 C  CD  . LYS   A 506 ? 0.9540 0.8020 1.1020 0.1105  -0.0992 -0.1719 485 LYS   A CD  
3703 C  CE  . LYS   A 506 ? 0.9746 0.8229 1.1393 0.1228  -0.1072 -0.1949 485 LYS   A CE  
3704 N  NZ  . LYS   A 506 ? 0.9962 0.8153 1.1918 0.1182  -0.1212 -0.1939 485 LYS   A NZ  
3705 N  N   . LYS   A 507 ? 0.6087 0.4758 0.6952 0.0783  -0.0796 -0.1294 486 LYS   A N   
3706 C  CA  . LYS   A 507 ? 0.5527 0.4116 0.6380 0.0665  -0.0773 -0.1082 486 LYS   A CA  
3707 C  C   . LYS   A 507 ? 0.5397 0.4151 0.6003 0.0677  -0.0712 -0.1102 486 LYS   A C   
3708 O  O   . LYS   A 507 ? 0.5676 0.4615 0.6121 0.0755  -0.0703 -0.1277 486 LYS   A O   
3709 C  CB  . LYS   A 507 ? 0.6126 0.4551 0.7192 0.0545  -0.0880 -0.1038 486 LYS   A CB  
3710 C  CG  . LYS   A 507 ? 0.6501 0.4754 0.7821 0.0531  -0.0956 -0.1012 486 LYS   A CG  
3711 C  CD  . LYS   A 507 ? 0.8038 0.6159 0.9572 0.0406  -0.1058 -0.0966 486 LYS   A CD  
3712 C  CE  . LYS   A 507 ? 1.1353 0.9295 1.3152 0.0399  -0.1144 -0.0941 486 LYS   A CE  
3713 N  NZ  . LYS   A 507 ? 1.2024 0.9846 1.4049 0.0272  -0.1244 -0.0890 486 LYS   A NZ  
3714 N  N   . PHE   A 508 ? 0.5600 0.4306 0.6175 0.0598  -0.0671 -0.0908 487 PHE   A N   
3715 C  CA  . PHE   A 508 ? 0.4873 0.3788 0.5214 0.0568  -0.0590 -0.0837 487 PHE   A CA  
3716 C  C   . PHE   A 508 ? 0.4747 0.3615 0.5167 0.0432  -0.0612 -0.0680 487 PHE   A C   
3717 O  O   . PHE   A 508 ? 0.4841 0.3537 0.5480 0.0352  -0.0673 -0.0599 487 PHE   A O   
3718 C  CB  . PHE   A 508 ? 0.4628 0.3685 0.4803 0.0600  -0.0453 -0.0707 487 PHE   A CB  
3719 C  CG  . PHE   A 508 ? 0.4149 0.3112 0.4425 0.0534  -0.0412 -0.0500 487 PHE   A CG  
3720 C  CD1 . PHE   A 508 ? 0.4652 0.3654 0.4897 0.0433  -0.0368 -0.0325 487 PHE   A CD1 
3721 C  CD2 . PHE   A 508 ? 0.4121 0.2985 0.4525 0.0582  -0.0422 -0.0489 487 PHE   A CD2 
3722 C  CE1 . PHE   A 508 ? 0.4382 0.3351 0.4701 0.0375  -0.0330 -0.0152 487 PHE   A CE1 
3723 C  CE2 . PHE   A 508 ? 0.4421 0.3241 0.4900 0.0523  -0.0391 -0.0292 487 PHE   A CE2 
3724 C  CZ  . PHE   A 508 ? 0.4740 0.3625 0.5166 0.0416  -0.0342 -0.0128 487 PHE   A CZ  
3725 N  N   . LEU   A 509 ? 0.4401 0.3441 0.4652 0.0408  -0.0564 -0.0626 488 LEU   A N   
3726 C  CA  . LEU   A 509 ? 0.4216 0.3275 0.4530 0.0298  -0.0568 -0.0485 488 LEU   A CA  
3727 C  C   . LEU   A 509 ? 0.4299 0.3488 0.4460 0.0292  -0.0450 -0.0327 488 LEU   A C   
3728 O  O   . LEU   A 509 ? 0.3778 0.3078 0.3752 0.0362  -0.0388 -0.0345 488 LEU   A O   
3729 C  CB  . LEU   A 509 ? 0.4369 0.3508 0.4683 0.0277  -0.0656 -0.0596 488 LEU   A CB  
3730 C  CG  . LEU   A 509 ? 0.4778 0.3779 0.5306 0.0243  -0.0795 -0.0751 488 LEU   A CG  
3731 C  CD1 . LEU   A 509 ? 0.5551 0.4698 0.6011 0.0256  -0.0876 -0.0907 488 LEU   A CD1 
3732 C  CD2 . LEU   A 509 ? 0.4870 0.3741 0.5656 0.0107  -0.0831 -0.0604 488 LEU   A CD2 
3733 N  N   . LEU   A 510 ? 0.3782 0.2970 0.4038 0.0206  -0.0423 -0.0175 489 LEU   A N   
3734 C  CA  . LEU   A 510 ? 0.4207 0.3519 0.4362 0.0196  -0.0336 -0.0059 489 LEU   A CA  
3735 C  C   . LEU   A 510 ? 0.3844 0.3262 0.3999 0.0174  -0.0376 -0.0071 489 LEU   A C   
3736 O  O   . LEU   A 510 ? 0.3902 0.3317 0.4213 0.0104  -0.0444 -0.0076 489 LEU   A O   
3737 C  CB  . LEU   A 510 ? 0.3839 0.3149 0.4091 0.0128  -0.0284 0.0085  489 LEU   A CB  
3738 C  CG  . LEU   A 510 ? 0.2896 0.2344 0.3108 0.0107  -0.0215 0.0173  489 LEU   A CG  
3739 C  CD1 . LEU   A 510 ? 0.3297 0.2776 0.3349 0.0173  -0.0139 0.0175  489 LEU   A CD1 
3740 C  CD2 . LEU   A 510 ? 0.3011 0.2513 0.3337 0.0030  -0.0182 0.0290  489 LEU   A CD2 
3741 N  N   . LEU   A 511 ? 0.4017 0.3535 0.4016 0.0231  -0.0342 -0.0064 490 LEU   A N   
3742 C  CA  . LEU   A 511 ? 0.3958 0.3592 0.3957 0.0230  -0.0379 -0.0054 490 LEU   A CA  
3743 C  C   . LEU   A 511 ? 0.3825 0.3513 0.3854 0.0215  -0.0308 0.0063  490 LEU   A C   
3744 O  O   . LEU   A 511 ? 0.4147 0.3815 0.4089 0.0246  -0.0232 0.0118  490 LEU   A O   
3745 C  CB  . LEU   A 511 ? 0.3926 0.3643 0.3741 0.0309  -0.0403 -0.0105 490 LEU   A CB  
3746 C  CG  . LEU   A 511 ? 0.4360 0.4080 0.4110 0.0347  -0.0467 -0.0260 490 LEU   A CG  
3747 C  CD1 . LEU   A 511 ? 0.4290 0.4172 0.3840 0.0421  -0.0488 -0.0285 490 LEU   A CD1 
3748 C  CD2 . LEU   A 511 ? 0.4114 0.3789 0.4045 0.0289  -0.0574 -0.0366 490 LEU   A CD2 
3749 N  N   . MET   A 512 ? 0.3477 0.3253 0.3649 0.0167  -0.0336 0.0088  491 MET   A N   
3750 C  CA  . MET   A 512 ? 0.3495 0.3361 0.3724 0.0164  -0.0275 0.0162  491 MET   A CA  
3751 C  C   . MET   A 512 ? 0.3690 0.3682 0.3954 0.0205  -0.0324 0.0154  491 MET   A C   
3752 O  O   . MET   A 512 ? 0.3321 0.3385 0.3661 0.0180  -0.0407 0.0107  491 MET   A O   
3753 C  CB  . MET   A 512 ? 0.3220 0.3147 0.3609 0.0075  -0.0248 0.0210  491 MET   A CB  
3754 C  CG  . MET   A 512 ? 0.3783 0.3615 0.4153 0.0041  -0.0198 0.0253  491 MET   A CG  
3755 S  SD  . MET   A 512 ? 0.4791 0.4648 0.5068 0.0084  -0.0091 0.0293  491 MET   A SD  
3756 C  CE  . MET   A 512 ? 0.3089 0.3172 0.3488 0.0068  -0.0057 0.0310  491 MET   A CE  
3757 N  N   . ALA   A 513 ? 0.3566 0.3581 0.3795 0.0270  -0.0285 0.0195  492 ALA   A N   
3758 C  CA  . ALA   A 513 ? 0.3333 0.3480 0.3652 0.0317  -0.0330 0.0198  492 ALA   A CA  
3759 C  C   . ALA   A 513 ? 0.3237 0.3549 0.3754 0.0254  -0.0324 0.0184  492 ALA   A C   
3760 O  O   . ALA   A 513 ? 0.3471 0.3797 0.4039 0.0192  -0.0258 0.0203  492 ALA   A O   
3761 C  CB  . ALA   A 513 ? 0.3407 0.3513 0.3700 0.0399  -0.0291 0.0244  492 ALA   A CB  
3762 N  N   . SER   A 514 ? 0.2938 0.3410 0.3571 0.0265  -0.0395 0.0161  493 SER   A N   
3763 C  CA  . SER   A 514 ? 0.3341 0.4024 0.4181 0.0195  -0.0387 0.0155  493 SER   A CA  
3764 C  C   . SER   A 514 ? 0.3278 0.4161 0.4244 0.0271  -0.0438 0.0132  493 SER   A C   
3765 O  O   . SER   A 514 ? 0.3497 0.4420 0.4461 0.0295  -0.0537 0.0109  493 SER   A O   
3766 C  CB  . SER   A 514 ? 0.3049 0.3737 0.3967 0.0074  -0.0441 0.0142  493 SER   A CB  
3767 O  OG  . SER   A 514 ? 0.3024 0.3951 0.4162 -0.0009 -0.0436 0.0162  493 SER   A OG  
3768 N  N   . THR   A 515 ? 0.3004 0.4037 0.4087 0.0315  -0.0377 0.0126  494 THR   A N   
3769 C  CA  . THR   A 515 ? 0.3619 0.4874 0.4866 0.0396  -0.0427 0.0094  494 THR   A CA  
3770 C  C   . THR   A 515 ? 0.3706 0.5232 0.5147 0.0297  -0.0466 0.0078  494 THR   A C   
3771 O  O   . THR   A 515 ? 0.3382 0.5070 0.4934 0.0342  -0.0553 0.0051  494 THR   A O   
3772 C  CB  . THR   A 515 ? 0.3097 0.4446 0.4438 0.0491  -0.0355 0.0057  494 THR   A CB  
3773 O  OG1 . THR   A 515 ? 0.3366 0.4953 0.4826 0.0409  -0.0269 0.0037  494 THR   A OG1 
3774 C  CG2 . THR   A 515 ? 0.3494 0.4561 0.4670 0.0547  -0.0309 0.0073  494 THR   A CG2 
3775 N  N   . SER   A 516 ? 0.3066 0.4653 0.4562 0.0157  -0.0410 0.0108  495 SER   A N   
3776 C  CA  . SER   A 516 ? 0.3192 0.5036 0.4902 0.0037  -0.0448 0.0115  495 SER   A CA  
3777 C  C   . SER   A 516 ? 0.3184 0.4925 0.4883 -0.0010 -0.0577 0.0088  495 SER   A C   
3778 O  O   . SER   A 516 ? 0.3152 0.5119 0.5032 -0.0045 -0.0655 0.0057  495 SER   A O   
3779 C  CB  . SER   A 516 ? 0.3043 0.4959 0.4817 -0.0114 -0.0365 0.0192  495 SER   A CB  
3780 O  OG  . SER   A 516 ? 0.4807 0.6415 0.6448 -0.0190 -0.0384 0.0231  495 SER   A OG  
3781 N  N   . ALA   A 517 ? 0.3460 0.4891 0.4958 -0.0010 -0.0604 0.0081  496 ALA   A N   
3782 C  CA  . ALA   A 517 ? 0.3152 0.4504 0.4611 -0.0025 -0.0730 0.0017  496 ALA   A CA  
3783 C  C   . ALA   A 517 ? 0.4104 0.5593 0.5548 0.0102  -0.0814 -0.0023 496 ALA   A C   
3784 O  O   . ALA   A 517 ? 0.3730 0.5337 0.5250 0.0075  -0.0932 -0.0085 496 ALA   A O   
3785 C  CB  . ALA   A 517 ? 0.3477 0.4513 0.4706 -0.0012 -0.0730 -0.0001 496 ALA   A CB  
3786 N  N   . CYS   A 518 ? 0.3793 0.5268 0.5155 0.0240  -0.0767 0.0013  497 CYS   A N   
3787 C  CA  . CYS   A 518 ? 0.3487 0.5070 0.4841 0.0371  -0.0858 0.0007  497 CYS   A CA  
3788 C  C   . CYS   A 518 ? 0.3628 0.5556 0.5259 0.0375  -0.0901 -0.0021 497 CYS   A C   
3789 O  O   . CYS   A 518 ? 0.3198 0.5286 0.4884 0.0415  -0.1022 -0.0051 497 CYS   A O   
3790 C  CB  . CYS   A 518 ? 0.3273 0.4704 0.4498 0.0513  -0.0807 0.0068  497 CYS   A CB  
3791 S  SG  . CYS   A 518 ? 0.4142 0.5636 0.5314 0.0676  -0.0936 0.0112  497 CYS   A SG  
3792 N  N   . TYR   A 519 ? 0.3625 0.5713 0.5433 0.0336  -0.0804 -0.0015 498 TYR   A N   
3793 C  CA  . TYR   A 519 ? 0.3723 0.6195 0.5814 0.0337  -0.0831 -0.0046 498 TYR   A CA  
3794 C  C   . TYR   A 519 ? 0.3854 0.6492 0.6100 0.0173  -0.0909 -0.0073 498 TYR   A C   
3795 O  O   . TYR   A 519 ? 0.3453 0.6376 0.5885 0.0188  -0.1002 -0.0113 498 TYR   A O   
3796 C  CB  . TYR   A 519 ? 0.3149 0.5801 0.5378 0.0338  -0.0696 -0.0043 498 TYR   A CB  
3797 C  CG  . TYR   A 519 ? 0.3441 0.6065 0.5656 0.0533  -0.0663 -0.0067 498 TYR   A CG  
3798 C  CD1 . TYR   A 519 ? 0.3889 0.6200 0.5905 0.0589  -0.0595 -0.0046 498 TYR   A CD1 
3799 C  CD2 . TYR   A 519 ? 0.3213 0.6069 0.5613 0.0651  -0.0701 -0.0107 498 TYR   A CD2 
3800 C  CE1 . TYR   A 519 ? 0.3804 0.6058 0.5844 0.0758  -0.0579 -0.0076 498 TYR   A CE1 
3801 C  CE2 . TYR   A 519 ? 0.2847 0.5583 0.5231 0.0815  -0.0672 -0.0124 498 TYR   A CE2 
3802 C  CZ  . TYR   A 519 ? 0.3102 0.5561 0.5334 0.0875  -0.0622 -0.0117 498 TYR   A CZ  
3803 O  OH  . TYR   A 519 ? 0.4015 0.6322 0.6255 0.1019  -0.0600 -0.0137 498 TYR   A OH  
3804 N  N   . LYS   A 520 ? 0.3389 0.5852 0.5584 0.0016  -0.0883 -0.0054 499 LYS   A N   
3805 C  CA  . LYS   A 520 ? 0.3152 0.5706 0.5511 -0.0148 -0.0976 -0.0087 499 LYS   A CA  
3806 C  C   . LYS   A 520 ? 0.3420 0.5968 0.5714 -0.0089 -0.1136 -0.0176 499 LYS   A C   
3807 O  O   . LYS   A 520 ? 0.3730 0.6547 0.6234 -0.0140 -0.1239 -0.0229 499 LYS   A O   
3808 C  CB  . LYS   A 520 ? 0.3956 0.6239 0.6257 -0.0299 -0.0938 -0.0051 499 LYS   A CB  
3809 C  CG  . LYS   A 520 ? 0.3616 0.5947 0.6135 -0.0488 -0.1036 -0.0081 499 LYS   A CG  
3810 C  CD  . LYS   A 520 ? 0.3802 0.6538 0.6654 -0.0604 -0.1015 -0.0028 499 LYS   A CD  
3811 C  CE  . LYS   A 520 ? 0.4122 0.6832 0.7148 -0.0804 -0.1081 -0.0049 499 LYS   A CE  
3812 N  NZ  . LYS   A 520 ? 0.5277 0.8353 0.8536 -0.0889 -0.1039 -0.0037 499 LYS   A NZ  
3813 N  N   . LEU   A 521 ? 0.4023 0.6301 0.6025 0.0018  -0.1159 -0.0192 500 LEU   A N   
3814 C  CA  . LEU   A 521 ? 0.4000 0.6306 0.5894 0.0083  -0.1307 -0.0270 500 LEU   A CA  
3815 C  C   . LEU   A 521 ? 0.3626 0.6238 0.5630 0.0209  -0.1381 -0.0261 500 LEU   A C   
3816 O  O   . LEU   A 521 ? 0.3413 0.6178 0.5460 0.0184  -0.1488 -0.0311 500 LEU   A O   
3817 C  CB  . LEU   A 521 ? 0.4008 0.6021 0.5559 0.0181  -0.1292 -0.0259 500 LEU   A CB  
3818 C  CG  . LEU   A 521 ? 0.3655 0.5728 0.5030 0.0269  -0.1430 -0.0320 500 LEU   A CG  
3819 C  CD1 . LEU   A 521 ? 0.3561 0.5694 0.5014 0.0147  -0.1552 -0.0474 500 LEU   A CD1 
3820 C  CD2 . LEU   A 521 ? 0.4408 0.6243 0.5452 0.0368  -0.1383 -0.0269 500 LEU   A CD2 
3821 N  N   . PHE   A 522 ? 0.3089 0.5732 0.5104 0.0337  -0.1298 -0.0181 501 PHE   A N   
3822 C  CA  . PHE   A 522 ? 0.3498 0.6316 0.5576 0.0460  -0.1337 -0.0142 501 PHE   A CA  
3823 C  C   . PHE   A 522 ? 0.3644 0.6774 0.6018 0.0370  -0.1347 -0.0170 501 PHE   A C   
3824 O  O   . PHE   A 522 ? 0.3703 0.6992 0.6134 0.0401  -0.1441 -0.0178 501 PHE   A O   
3825 C  CB  . PHE   A 522 ? 0.3835 0.6550 0.5877 0.0616  -0.1247 -0.0067 501 PHE   A CB  
3826 C  CG  . PHE   A 522 ? 0.3879 0.6313 0.5637 0.0728  -0.1264 0.0000  501 PHE   A CG  
3827 C  CD1 . PHE   A 522 ? 0.4192 0.6516 0.5724 0.0693  -0.1341 -0.0015 501 PHE   A CD1 
3828 C  CD2 . PHE   A 522 ? 0.4097 0.6381 0.5821 0.0861  -0.1201 0.0077  501 PHE   A CD2 
3829 C  CE1 . PHE   A 522 ? 0.4663 0.6764 0.5925 0.0782  -0.1342 0.0068  501 PHE   A CE1 
3830 C  CE2 . PHE   A 522 ? 0.4573 0.6596 0.6052 0.0938  -0.1211 0.0169  501 PHE   A CE2 
3831 C  CZ  . PHE   A 522 ? 0.5009 0.6956 0.6249 0.0896  -0.1276 0.0176  501 PHE   A CZ  
3832 N  N   . ARG   A 523 ? 0.3366 0.6603 0.5930 0.0252  -0.1250 -0.0171 502 ARG   A N   
3833 C  CA  . ARG   A 523 ? 0.2885 0.6422 0.5732 0.0142  -0.1253 -0.0179 502 ARG   A CA  
3834 C  C   . ARG   A 523 ? 0.3332 0.6917 0.6227 0.0000  -0.1381 -0.0231 502 ARG   A C   
3835 O  O   . ARG   A 523 ? 0.3386 0.7210 0.6468 -0.0037 -0.1442 -0.0243 502 ARG   A O   
3836 C  CB  . ARG   A 523 ? 0.3253 0.6878 0.6261 0.0023  -0.1115 -0.0146 502 ARG   A CB  
3837 C  CG  . ARG   A 523 ? 0.3697 0.7305 0.6656 0.0160  -0.0981 -0.0123 502 ARG   A CG  
3838 C  CD  . ARG   A 523 ? 0.4156 0.7925 0.7261 0.0046  -0.0838 -0.0096 502 ARG   A CD  
3839 N  NE  . ARG   A 523 ? 0.5278 0.9068 0.8336 0.0188  -0.0718 -0.0106 502 ARG   A NE  
3840 C  CZ  . ARG   A 523 ? 0.4766 0.8432 0.7697 0.0187  -0.0609 -0.0087 502 ARG   A CZ  
3841 N  NH1 . ARG   A 523 ? 0.4163 0.7683 0.7003 0.0050  -0.0594 -0.0035 502 ARG   A NH1 
3842 N  NH2 . ARG   A 523 ? 0.3948 0.7631 0.6847 0.0325  -0.0518 -0.0126 502 ARG   A NH2 
3843 N  N   . GLU   A 524 ? 0.3369 0.6723 0.6102 -0.0074 -0.1425 -0.0279 503 GLU   A N   
3844 C  CA  . GLU   A 524 ? 0.3849 0.7207 0.6598 -0.0195 -0.1550 -0.0365 503 GLU   A CA  
3845 C  C   . GLU   A 524 ? 0.3947 0.7384 0.6574 -0.0069 -0.1669 -0.0402 503 GLU   A C   
3846 O  O   . GLU   A 524 ? 0.4143 0.7785 0.6915 -0.0132 -0.1758 -0.0440 503 GLU   A O   
3847 C  CB  . GLU   A 524 ? 0.4414 0.7453 0.7007 -0.0272 -0.1564 -0.0434 503 GLU   A CB  
3848 C  CG  . GLU   A 524 ? 0.6054 0.9068 0.8825 -0.0493 -0.1601 -0.0490 503 GLU   A CG  
3849 C  CD  . GLU   A 524 ? 0.5400 0.8596 0.8442 -0.0639 -0.1495 -0.0391 503 GLU   A CD  
3850 O  OE1 . GLU   A 524 ? 0.5163 0.8350 0.8203 -0.0598 -0.1371 -0.0300 503 GLU   A OE1 
3851 O  OE2 . GLU   A 524 ? 0.5865 0.9237 0.9112 -0.0794 -0.1529 -0.0407 503 GLU   A OE2 
3852 N  N   . LYS   A 525 ? 0.3817 0.7100 0.6177 0.0104  -0.1672 -0.0374 504 LYS   A N   
3853 C  CA  . LYS   A 525 ? 0.4270 0.7632 0.6496 0.0222  -0.1779 -0.0374 504 LYS   A CA  
3854 C  C   . LYS   A 525 ? 0.3942 0.7572 0.6381 0.0291  -0.1795 -0.0318 504 LYS   A C   
3855 O  O   . LYS   A 525 ? 0.3886 0.7682 0.6346 0.0313  -0.1909 -0.0341 504 LYS   A O   
3856 C  CB  . LYS   A 525 ? 0.4399 0.7542 0.6311 0.0380  -0.1761 -0.0309 504 LYS   A CB  
3857 C  CG  . LYS   A 525 ? 0.4880 0.7778 0.6559 0.0331  -0.1755 -0.0378 504 LYS   A CG  
3858 C  CD  . LYS   A 525 ? 0.5287 0.8236 0.6913 0.0239  -0.1870 -0.0518 504 LYS   A CD  
3859 C  CE  . LYS   A 525 ? 0.5600 0.8303 0.7055 0.0180  -0.1857 -0.0620 504 LYS   A CE  
3860 N  NZ  . LYS   A 525 ? 0.6086 0.8827 0.7520 0.0091  -0.1964 -0.0788 504 LYS   A NZ  
3861 N  N   . GLN   A 526 ? 0.3616 0.7301 0.6219 0.0332  -0.1684 -0.0255 505 GLN   A N   
3862 C  CA  . GLN   A 526 ? 0.3314 0.7265 0.6153 0.0397  -0.1689 -0.0226 505 GLN   A CA  
3863 C  C   . GLN   A 526 ? 0.3520 0.7739 0.6623 0.0232  -0.1742 -0.0283 505 GLN   A C   
3864 O  O   . GLN   A 526 ? 0.3699 0.8142 0.6925 0.0267  -0.1833 -0.0293 505 GLN   A O   
3865 C  CB  . GLN   A 526 ? 0.3295 0.7246 0.6242 0.0474  -0.1545 -0.0178 505 GLN   A CB  
3866 C  CG  . GLN   A 526 ? 0.3323 0.7544 0.6516 0.0562  -0.1538 -0.0169 505 GLN   A CG  
3867 C  CD  . GLN   A 526 ? 0.3876 0.8142 0.7198 0.0596  -0.1382 -0.0166 505 GLN   A CD  
3868 O  OE1 . GLN   A 526 ? 0.3310 0.7591 0.6687 0.0461  -0.1286 -0.0179 505 GLN   A OE1 
3869 N  NE2 . GLN   A 526 ? 0.3589 0.7876 0.6959 0.0777  -0.1357 -0.0149 505 GLN   A NE2 
3870 N  N   . LYS   A 527 ? 0.2916 0.7113 0.6124 0.0044  -0.1691 -0.0306 506 LYS   A N   
3871 C  CA  . LYS   A 527 ? 0.3331 0.7745 0.6798 -0.0140 -0.1749 -0.0341 506 LYS   A CA  
3872 C  C   . LYS   A 527 ? 0.4198 0.8631 0.7578 -0.0173 -0.1912 -0.0425 506 LYS   A C   
3873 O  O   . LYS   A 527 ? 0.4380 0.9063 0.7965 -0.0238 -0.1998 -0.0453 506 LYS   A O   
3874 C  CB  . LYS   A 527 ? 0.3636 0.7962 0.7207 -0.0347 -0.1675 -0.0322 506 LYS   A CB  
3875 C  CG  . LYS   A 527 ? 0.4253 0.8817 0.8164 -0.0545 -0.1704 -0.0306 506 LYS   A CG  
3876 C  CD  . LYS   A 527 ? 0.4672 0.9466 0.8847 -0.0507 -0.1586 -0.0250 506 LYS   A CD  
3877 C  CE  . LYS   A 527 ? 0.5210 1.0323 0.9730 -0.0612 -0.1645 -0.0260 506 LYS   A CE  
3878 N  NZ  . LYS   A 527 ? 0.6533 1.1848 1.1040 -0.0467 -0.1746 -0.0304 506 LYS   A NZ  
3879 N  N   . ASP   A 528 ? 0.4156 0.8341 0.7232 -0.0126 -0.1956 -0.0476 507 ASP   A N   
3880 C  CA  . ASP   A 528 ? 0.3794 0.7988 0.6738 -0.0138 -0.2103 -0.0577 507 ASP   A CA  
3881 C  C   . ASP   A 528 ? 0.4667 0.9020 0.7534 0.0038  -0.2187 -0.0543 507 ASP   A C   
3882 O  O   . ASP   A 528 ? 0.4754 0.9134 0.7471 0.0055  -0.2307 -0.0616 507 ASP   A O   
3883 C  CB  . ASP   A 528 ? 0.4917 0.8800 0.7559 -0.0136 -0.2105 -0.0650 507 ASP   A CB  
3884 C  CG  . ASP   A 528 ? 0.5810 0.9506 0.8535 -0.0308 -0.2035 -0.0688 507 ASP   A CG  
3885 O  OD1 . ASP   A 528 ? 0.5597 0.9430 0.8609 -0.0458 -0.2000 -0.0653 507 ASP   A OD1 
3886 O  OD2 . ASP   A 528 ? 0.5916 0.9336 0.8425 -0.0294 -0.2013 -0.0740 507 ASP   A OD2 
3887 N  N   . GLY   A 529 ? 0.4373 0.8830 0.7339 0.0172  -0.2128 -0.0439 508 GLY   A N   
3888 C  CA  . GLY   A 529 ? 0.4070 0.8681 0.7014 0.0333  -0.2213 -0.0391 508 GLY   A CA  
3889 C  C   . GLY   A 529 ? 0.4384 0.8792 0.7015 0.0506  -0.2221 -0.0310 508 GLY   A C   
3890 O  O   . GLY   A 529 ? 0.3794 0.8306 0.6355 0.0616  -0.2324 -0.0267 508 GLY   A O   
3891 N  N   . HIS   A 530 ? 0.4176 0.8303 0.6625 0.0529  -0.2118 -0.0274 509 HIS   A N   
3892 C  CA  . HIS   A 530 ? 0.4099 0.8016 0.6259 0.0675  -0.2113 -0.0176 509 HIS   A CA  
3893 C  C   . HIS   A 530 ? 0.3653 0.7434 0.5865 0.0795  -0.1999 -0.0063 509 HIS   A C   
3894 O  O   . HIS   A 530 ? 0.3958 0.7486 0.5953 0.0865  -0.1948 0.0013  509 HIS   A O   
3895 C  CB  . HIS   A 530 ? 0.4322 0.8014 0.6196 0.0612  -0.2099 -0.0233 509 HIS   A CB  
3896 C  CG  . HIS   A 530 ? 0.5773 0.9570 0.7572 0.0512  -0.2214 -0.0368 509 HIS   A CG  
3897 N  ND1 . HIS   A 530 ? 0.6197 1.0151 0.7887 0.0576  -0.2339 -0.0362 509 HIS   A ND1 
3898 C  CD2 . HIS   A 530 ? 0.5674 0.9438 0.7506 0.0353  -0.2226 -0.0519 509 HIS   A CD2 
3899 C  CE1 . HIS   A 530 ? 0.6347 1.0374 0.7995 0.0465  -0.2419 -0.0521 509 HIS   A CE1 
3900 N  NE2 . HIS   A 530 ? 0.6573 1.0470 0.8314 0.0329  -0.2355 -0.0620 509 HIS   A NE2 
3901 N  N   . GLY   A 531 ? 0.3821 0.7775 0.6326 0.0818  -0.1955 -0.0059 510 GLY   A N   
3902 C  CA  . GLY   A 531 ? 0.4077 0.7914 0.6648 0.0937  -0.1846 0.0015  510 GLY   A CA  
3903 C  C   . GLY   A 531 ? 0.4280 0.7982 0.6736 0.1112  -0.1897 0.0148  510 GLY   A C   
3904 O  O   . GLY   A 531 ? 0.4337 0.7827 0.6761 0.1203  -0.1814 0.0218  510 GLY   A O   
3905 N  N   . GLU   A 532 ? 0.4703 0.8523 0.7106 0.1153  -0.2038 0.0189  511 GLU   A N   
3906 C  CA  . GLU   A 532 ? 0.4367 0.8073 0.6681 0.1304  -0.2107 0.0344  511 GLU   A CA  
3907 C  C   . GLU   A 532 ? 0.5047 0.8503 0.7007 0.1299  -0.2125 0.0424  511 GLU   A C   
3908 O  O   . GLU   A 532 ? 0.5043 0.8396 0.6907 0.1401  -0.2195 0.0574  511 GLU   A O   
3909 C  CB  . GLU   A 532 ? 0.4330 0.8308 0.6765 0.1359  -0.2258 0.0368  511 GLU   A CB  
3910 C  CG  . GLU   A 532 ? 0.5111 0.9142 0.7804 0.1515  -0.2271 0.0460  511 GLU   A CG  
3911 C  CD  . GLU   A 532 ? 0.5909 0.9941 0.8830 0.1526  -0.2120 0.0387  511 GLU   A CD  
3912 O  OE1 . GLU   A 532 ? 0.6410 1.0667 0.9490 0.1425  -0.2076 0.0254  511 GLU   A OE1 
3913 O  OE2 . GLU   A 532 ? 0.6102 0.9914 0.9042 0.1626  -0.2044 0.0461  511 GLU   A OE2 
3914 N  N   . ALA   A 533 ? 0.5032 0.8395 0.6808 0.1180  -0.2069 0.0334  512 ALA   A N   
3915 C  CA  . ALA   A 533 ? 0.5784 0.8920 0.7224 0.1179  -0.2062 0.0401  512 ALA   A CA  
3916 C  C   . ALA   A 533 ? 0.6142 0.8995 0.7555 0.1273  -0.1984 0.0549  512 ALA   A C   
3917 O  O   . ALA   A 533 ? 0.5510 0.8287 0.7110 0.1295  -0.1883 0.0533  512 ALA   A O   
3918 C  CB  . ALA   A 533 ? 0.4790 0.7869 0.6090 0.1044  -0.1999 0.0261  512 ALA   A CB  
3919 N  N   . ILE   A 534 ? 0.6671 0.9373 0.7852 0.1323  -0.2033 0.0690  513 ILE   A N   
3920 C  CA  . ILE   A 534 ? 0.7123 0.9535 0.8294 0.1405  -0.1991 0.0849  513 ILE   A CA  
3921 C  C   . ILE   A 534 ? 0.7443 0.9616 0.8354 0.1341  -0.1887 0.0855  513 ILE   A C   
3922 O  O   . ILE   A 534 ? 0.7429 0.9655 0.8082 0.1270  -0.1892 0.0805  513 ILE   A O   
3923 C  CB  . ILE   A 534 ? 0.6975 0.9354 0.8082 0.1501  -0.2129 0.1020  513 ILE   A CB  
3924 C  CG1 . ILE   A 534 ? 0.7130 0.9616 0.8591 0.1606  -0.2200 0.1062  513 ILE   A CG1 
3925 C  CG2 . ILE   A 534 ? 0.7931 0.9962 0.8850 0.1535  -0.2101 0.1166  513 ILE   A CG2 
3926 C  CD1 . ILE   A 534 ? 0.8104 1.0389 0.9817 0.1666  -0.2104 0.1103  513 ILE   A CD1 
3927 N  N   . MET   A 535 ? 0.7456 0.9381 0.8451 0.1368  -0.1790 0.0905  514 MET   A N   
3928 C  CA  . MET   A 535 ? 0.6764 0.8442 0.7539 0.1318  -0.1690 0.0928  514 MET   A CA  
3929 C  C   . MET   A 535 ? 0.7622 0.9053 0.8233 0.1374  -0.1732 0.1104  514 MET   A C   
3930 O  O   . MET   A 535 ? 0.8061 0.9417 0.8801 0.1473  -0.1823 0.1194  514 MET   A O   
3931 C  CB  . MET   A 535 ? 0.6660 0.8217 0.7612 0.1306  -0.1556 0.0859  514 MET   A CB  
3932 C  CG  . MET   A 535 ? 0.7733 0.9048 0.8478 0.1250  -0.1451 0.0872  514 MET   A CG  
3933 S  SD  . MET   A 535 ? 0.7547 0.8925 0.8315 0.1164  -0.1335 0.0686  514 MET   A SD  
3934 C  CE  . MET   A 535 ? 0.7166 0.8538 0.8276 0.1227  -0.1258 0.0636  514 MET   A CE  
3935 N  N   . PHE   A 536 ? 0.7886 0.9193 0.8205 0.1316  -0.1665 0.1142  515 PHE   A N   
3936 C  CA  . PHE   A 536 ? 0.8242 0.9322 0.8362 0.1348  -0.1663 0.1306  515 PHE   A CA  
3937 C  C   . PHE   A 536 ? 0.9096 1.0320 0.9046 0.1387  -0.1778 0.1426  515 PHE   A C   
3938 O  O   . PHE   A 536 ? 0.9488 1.0554 0.9349 0.1447  -0.1806 0.1592  515 PHE   A O   
3939 C  CB  . PHE   A 536 ? 0.8223 0.9008 0.8516 0.1445  -0.1653 0.1351  515 PHE   A CB  
3940 C  CG  . PHE   A 536 ? 0.8436 0.9092 0.8889 0.1417  -0.1538 0.1225  515 PHE   A CG  
3941 C  CD1 . PHE   A 536 ? 0.7492 0.8058 0.7788 0.1317  -0.1411 0.1208  515 PHE   A CD1 
3942 C  CD2 . PHE   A 536 ? 0.7790 0.8452 0.8547 0.1476  -0.1523 0.1113  515 PHE   A CD2 
3943 C  CE1 . PHE   A 536 ? 0.6951 0.7413 0.7383 0.1294  -0.1308 0.1099  515 PHE   A CE1 
3944 C  CE2 . PHE   A 536 ? 0.7052 0.7637 0.7941 0.1439  -0.1399 0.0995  515 PHE   A CE2 
3945 C  CZ  . PHE   A 536 ? 0.6378 0.6858 0.7095 0.1353  -0.1294 0.0990  515 PHE   A CZ  
3946 N  N   . LYS   A 537 ? 0.9432 1.0966 0.9328 0.1354  -0.1842 0.1343  516 LYS   A N   
3947 C  CA  . LYS   A 537 ? 1.0004 1.1721 0.9716 0.1385  -0.1948 0.1440  516 LYS   A CA  
3948 C  C   . LYS   A 537 ? 1.0259 1.1915 0.9648 0.1345  -0.1880 0.1569  516 LYS   A C   
3949 O  O   . LYS   A 537 ? 0.9917 1.1573 0.9159 0.1261  -0.1769 0.1492  516 LYS   A O   
3950 C  CB  . LYS   A 537 ? 1.0190 1.2252 0.9882 0.1340  -0.2009 0.1277  516 LYS   A CB  
3951 C  CG  . LYS   A 537 ? 0.9890 1.2074 0.9913 0.1359  -0.2065 0.1155  516 LYS   A CG  
3952 C  CD  . LYS   A 537 ? 1.0005 1.2474 1.0005 0.1281  -0.2086 0.0950  516 LYS   A CD  
3953 C  CE  . LYS   A 537 ? 0.9993 1.2698 0.9754 0.1283  -0.2185 0.0958  516 LYS   A CE  
3954 N  NZ  . LYS   A 537 ? 0.9872 1.2698 0.9741 0.1376  -0.2326 0.1077  516 LYS   A NZ  
3955 N  N   . GLY   A 538 ? 1.0016 1.1642 0.9307 0.1408  -0.1945 0.1768  517 GLY   A N   
3956 C  CA  . GLY   A 538 ? 0.9914 1.1501 0.8937 0.1367  -0.1871 0.1927  517 GLY   A CA  
3957 C  C   . GLY   A 538 ? 1.0439 1.1674 0.9520 0.1375  -0.1787 0.2070  517 GLY   A C   
3958 O  O   . GLY   A 538 ? 0.9758 1.0962 0.8649 0.1321  -0.1707 0.2210  517 GLY   A O   
3959 N  N   . LEU   A 539 ? 1.0120 1.1114 0.9468 0.1440  -0.1800 0.2028  518 LEU   A N   
3960 C  CA  . LEU   A 539 ? 1.0088 1.0740 0.9525 0.1464  -0.1729 0.2134  518 LEU   A CA  
3961 C  C   . LEU   A 539 ? 1.0094 1.0628 0.9715 0.1612  -0.1846 0.2224  518 LEU   A C   
3962 O  O   . LEU   A 539 ? 1.0497 1.0988 1.0359 0.1701  -0.1889 0.2083  518 LEU   A O   
3963 C  CB  . LEU   A 539 ? 0.9989 1.0472 0.9570 0.1423  -0.1618 0.1963  518 LEU   A CB  
3964 C  CG  . LEU   A 539 ? 0.8506 0.9122 0.7942 0.1297  -0.1516 0.1842  518 LEU   A CG  
3965 C  CD1 . LEU   A 539 ? 0.8261 0.8721 0.7869 0.1270  -0.1425 0.1684  518 LEU   A CD1 
3966 C  CD2 . LEU   A 539 ? 0.8954 0.9575 0.8138 0.1212  -0.1428 0.1982  518 LEU   A CD2 
3967 N  N   . GLY   A 540 ? 0.9530 1.0032 0.9046 0.1645  -0.1894 0.2460  519 GLY   A N   
3968 C  CA  . GLY   A 540 ? 0.8911 0.9329 0.8585 0.1799  -0.2020 0.2563  519 GLY   A CA  
3969 C  C   . GLY   A 540 ? 0.9333 0.9431 0.9263 0.1890  -0.1975 0.2531  519 GLY   A C   
3970 O  O   . GLY   A 540 ? 0.8543 0.8607 0.8671 0.2047  -0.2068 0.2511  519 GLY   A O   
3971 N  N   . GLY   A 541 ? 0.9819 0.9701 0.9757 0.1797  -0.1830 0.2519  520 GLY   A N   
3972 C  CA  . GLY   A 541 ? 1.0599 1.0200 1.0787 0.1865  -0.1770 0.2467  520 GLY   A CA  
3973 C  C   . GLY   A 541 ? 1.0392 1.0060 1.0780 0.1946  -0.1748 0.2199  520 GLY   A C   
3974 O  O   . GLY   A 541 ? 1.0400 0.9896 1.1019 0.2023  -0.1695 0.2139  520 GLY   A O   
3975 N  N   . MET   A 542 ? 1.1004 1.0937 1.1330 0.1918  -0.1782 0.2042  521 MET   A N   
3976 C  CA  . MET   A 542 ? 1.1004 1.1064 1.1529 0.1986  -0.1763 0.1800  521 MET   A CA  
3977 C  C   . MET   A 542 ? 1.0490 1.0829 1.1090 0.2070  -0.1917 0.1737  521 MET   A C   
3978 O  O   . MET   A 542 ? 1.0678 1.1191 1.1486 0.2117  -0.1896 0.1550  521 MET   A O   
3979 C  CB  . MET   A 542 ? 1.0634 1.0748 1.1093 0.1838  -0.1661 0.1647  521 MET   A CB  
3980 C  CG  . MET   A 542 ? 1.1297 1.1176 1.1642 0.1716  -0.1523 0.1721  521 MET   A CG  
3981 S  SD  . MET   A 542 ? 1.2164 1.2038 1.2561 0.1616  -0.1376 0.1512  521 MET   A SD  
3982 C  CE  . MET   A 542 ? 1.0344 1.0165 1.1068 0.1757  -0.1306 0.1398  521 MET   A CE  
3983 N  N   . LYS   A 545 ? 0.9022 0.9809 1.0385 0.2464  -0.1799 0.1496  524 LYS   A N   
3984 C  CA  . LYS   A 545 ? 0.8947 0.9958 1.0578 0.2397  -0.1619 0.1384  524 LYS   A CA  
3985 C  C   . LYS   A 545 ? 0.8185 0.9704 1.0028 0.2297  -0.1598 0.1379  524 LYS   A C   
3986 O  O   . LYS   A 545 ? 0.8649 1.0329 1.0887 0.2258  -0.1575 0.1301  524 LYS   A O   
3987 C  CB  . LYS   A 545 ? 0.9451 1.0248 1.0932 0.2247  -0.1514 0.1316  524 LYS   A CB  
3988 C  CG  . LYS   A 545 ? 1.0177 1.0546 1.1649 0.2270  -0.1481 0.1376  524 LYS   A CG  
3989 C  CD  . LYS   A 545 ? 1.1084 1.1189 1.2323 0.2296  -0.1603 0.1566  524 LYS   A CD  
3990 C  CE  . LYS   A 545 ? 1.1375 1.1103 1.2728 0.2303  -0.1563 0.1658  524 LYS   A CE  
3991 N  NZ  . LYS   A 545 ? 1.0615 1.0143 1.1804 0.2299  -0.1666 0.1894  524 LYS   A NZ  
3992 N  N   . ARG   A 546 ? 0.8297 0.9989 0.9873 0.2250  -0.1665 0.1406  525 ARG   A N   
3993 C  CA  . ARG   A 546 ? 0.7566 0.9343 0.9749 0.1888  -0.1949 0.1416  525 ARG   A CA  
3994 C  C   . ARG   A 546 ? 0.7780 0.9739 0.9990 0.1861  -0.1793 0.1228  525 ARG   A C   
3995 O  O   . ARG   A 546 ? 0.7546 0.9748 0.9985 0.1928  -0.1770 0.1111  525 ARG   A O   
3996 C  CB  . ARG   A 546 ? 0.6921 0.8980 0.9363 0.2024  -0.2015 0.1490  525 ARG   A CB  
3997 N  N   . ILE   A 547 ? 0.7889 0.9674 0.9878 0.1746  -0.1733 0.1170  526 ILE   A N   
3998 C  CA  . ILE   A 547 ? 0.7319 0.9185 0.9326 0.1696  -0.1612 0.0994  526 ILE   A CA  
3999 C  C   . ILE   A 547 ? 0.6614 0.8707 0.8526 0.1592  -0.1686 0.0870  526 ILE   A C   
4000 O  O   . ILE   A 547 ? 0.6550 0.8598 0.8198 0.1521  -0.1755 0.0897  526 ILE   A O   
4001 C  CB  . ILE   A 547 ? 0.7741 0.9318 0.9558 0.1639  -0.1484 0.1001  526 ILE   A CB  
4002 C  CG1 . ILE   A 547 ? 0.7985 0.9369 0.9796 0.1789  -0.1371 0.1090  526 ILE   A CG1 
4003 C  CG2 . ILE   A 547 ? 0.6200 0.7838 0.8041 0.1576  -0.1383 0.0811  526 ILE   A CG2 
4004 C  CD1 . ILE   A 547 ? 0.8995 1.0076 1.0542 0.1776  -0.1256 0.1071  526 ILE   A CD1 
4005 N  N   . THR   A 548 ? 0.5733 0.8077 0.7829 0.1581  -0.1652 0.0715  527 THR   A N   
4006 C  CA  . THR   A 548 ? 0.5602 0.8190 0.7653 0.1472  -0.1698 0.0589  527 THR   A CA  
4007 C  C   . THR   A 548 ? 0.4906 0.7533 0.6999 0.1374  -0.1574 0.0432  527 THR   A C   
4008 O  O   . THR   A 548 ? 0.5204 0.7710 0.7373 0.1403  -0.1459 0.0403  527 THR   A O   
4009 C  CB  . THR   A 548 ? 0.5203 0.8102 0.7477 0.1519  -0.1798 0.0565  527 THR   A CB  
4010 O  OG1 . THR   A 548 ? 0.5304 0.8312 0.7865 0.1585  -0.1718 0.0496  527 THR   A OG1 
4011 C  CG2 . THR   A 548 ? 0.5230 0.8097 0.7479 0.1619  -0.1936 0.0734  527 THR   A CG2 
4012 N  N   . ILE   A 549 ? 0.4789 0.7593 0.6842 0.1250  -0.1606 0.0330  528 ILE   A N   
4013 C  CA  . ILE   A 549 ? 0.4262 0.7138 0.6398 0.1134  -0.1508 0.0202  528 ILE   A CA  
4014 C  C   . ILE   A 549 ? 0.4400 0.7485 0.6842 0.1166  -0.1446 0.0141  528 ILE   A C   
4015 O  O   . ILE   A 549 ? 0.3954 0.7007 0.6469 0.1146  -0.1323 0.0088  528 ILE   A O   
4016 C  CB  . ILE   A 549 ? 0.4447 0.7469 0.6527 0.0986  -0.1573 0.0115  528 ILE   A CB  
4017 C  CG1 . ILE   A 549 ? 0.4599 0.7410 0.6359 0.0951  -0.1602 0.0138  528 ILE   A CG1 
4018 C  CG2 . ILE   A 549 ? 0.3447 0.6594 0.5701 0.0851  -0.1488 0.0011  528 ILE   A CG2 
4019 C  CD1 . ILE   A 549 ? 0.4174 0.7092 0.5886 0.0805  -0.1662 0.0021  528 ILE   A CD1 
4020 N  N   . ASN   A 550 ? 0.4105 0.7432 0.6725 0.1215  -0.1528 0.0142  529 ASN   A N   
4021 C  CA  . ASN   A 550 ? 0.3627 0.7185 0.6539 0.1257  -0.1471 0.0079  529 ASN   A CA  
4022 C  C   . ASN   A 550 ? 0.3831 0.7214 0.6788 0.1389  -0.1374 0.0094  529 ASN   A C   
4023 O  O   . ASN   A 550 ? 0.3552 0.7038 0.6649 0.1378  -0.1259 0.0003  529 ASN   A O   
4024 C  CB  . ASN   A 550 ? 0.3453 0.7267 0.6537 0.1323  -0.1590 0.0097  529 ASN   A CB  
4025 C  CG  . ASN   A 550 ? 0.3986 0.8031 0.7092 0.1178  -0.1675 0.0043  529 ASN   A CG  
4026 O  OD1 . ASN   A 550 ? 0.4326 0.8418 0.7433 0.1019  -0.1622 -0.0028 529 ASN   A OD1 
4027 N  ND2 . ASN   A 550 ? 0.4410 0.8598 0.7549 0.1228  -0.1815 0.0081  529 ASN   A ND2 
4028 N  N   . LYS   A 551 ? 0.4106 0.7235 0.6950 0.1507  -0.1418 0.0209  530 LYS   A N   
4029 C  CA  . LYS   A 551 ? 0.4456 0.7386 0.7353 0.1629  -0.1336 0.0220  530 LYS   A CA  
4030 C  C   . LYS   A 551 ? 0.4505 0.7253 0.7281 0.1555  -0.1205 0.0154  530 LYS   A C   
4031 O  O   . LYS   A 551 ? 0.4601 0.7310 0.7477 0.1612  -0.1107 0.0077  530 LYS   A O   
4032 C  CB  . LYS   A 551 ? 0.5228 0.7915 0.8035 0.1745  -0.1415 0.0392  530 LYS   A CB  
4033 C  CG  . LYS   A 551 ? 0.6299 0.9175 0.9268 0.1847  -0.1543 0.0471  530 LYS   A CG  
4034 C  CD  . LYS   A 551 ? 0.7085 0.9752 0.9951 0.1934  -0.1633 0.0686  530 LYS   A CD  
4035 C  CE  . LYS   A 551 ? 0.7337 0.9822 1.0325 0.2102  -0.1578 0.0747  530 LYS   A CE  
4036 N  NZ  . LYS   A 551 ? 0.7410 0.9586 1.0256 0.2082  -0.1448 0.0708  530 LYS   A NZ  
4037 N  N   . ILE   A 552 ? 0.4728 0.7378 0.7292 0.1431  -0.1207 0.0172  531 ILE   A N   
4038 C  CA  . ILE   A 552 ? 0.4140 0.6628 0.6594 0.1360  -0.1092 0.0120  531 ILE   A CA  
4039 C  C   . ILE   A 552 ? 0.4328 0.7083 0.6935 0.1263  -0.1000 -0.0007 531 ILE   A C   
4040 O  O   . ILE   A 552 ? 0.4071 0.6788 0.6702 0.1261  -0.0885 -0.0073 531 ILE   A O   
4041 C  CB  . ILE   A 552 ? 0.4210 0.6514 0.6394 0.1269  -0.1127 0.0181  531 ILE   A CB  
4042 C  CG1 . ILE   A 552 ? 0.4456 0.6490 0.6471 0.1353  -0.1186 0.0329  531 ILE   A CG1 
4043 C  CG2 . ILE   A 552 ? 0.3943 0.6142 0.6046 0.1181  -0.1017 0.0120  531 ILE   A CG2 
4044 C  CD1 . ILE   A 552 ? 0.4685 0.6551 0.6415 0.1273  -0.1209 0.0384  531 ILE   A CD1 
4045 N  N   . LEU   A 553 ? 0.3604 0.6645 0.6316 0.1171  -0.1049 -0.0035 532 LEU   A N   
4046 C  CA  . LEU   A 553 ? 0.3825 0.7130 0.6683 0.1047  -0.0959 -0.0118 532 LEU   A CA  
4047 C  C   . LEU   A 553 ? 0.3886 0.7408 0.6963 0.1130  -0.0885 -0.0190 532 LEU   A C   
4048 O  O   . LEU   A 553 ? 0.3885 0.7569 0.7035 0.1057  -0.0769 -0.0253 532 LEU   A O   
4049 C  CB  . LEU   A 553 ? 0.3591 0.7113 0.6514 0.0904  -0.1038 -0.0118 532 LEU   A CB  
4050 C  CG  . LEU   A 553 ? 0.3000 0.6345 0.5719 0.0794  -0.1100 -0.0089 532 LEU   A CG  
4051 C  CD1 . LEU   A 553 ? 0.3349 0.6902 0.6165 0.0658  -0.1195 -0.0112 532 LEU   A CD1 
4052 C  CD2 . LEU   A 553 ? 0.3552 0.6773 0.6188 0.0698  -0.0992 -0.0100 532 LEU   A CD2 
4053 N  N   A SER   A 554 ? 0.3905 0.7445 0.7084 0.1283  -0.0952 -0.0179 533 SER   A N   
4054 N  N   B SER   A 554 ? 0.3907 0.7446 0.7085 0.1283  -0.0952 -0.0179 533 SER   A N   
4055 C  CA  A SER   A 554 ? 0.4031 0.7778 0.7423 0.1384  -0.0894 -0.0266 533 SER   A CA  
4056 C  CA  B SER   A 554 ? 0.4030 0.7776 0.7423 0.1385  -0.0894 -0.0265 533 SER   A CA  
4057 C  C   A SER   A 554 ? 0.4118 0.7658 0.7469 0.1487  -0.0801 -0.0325 533 SER   A C   
4058 C  C   B SER   A 554 ? 0.4118 0.7657 0.7469 0.1489  -0.0802 -0.0325 533 SER   A C   
4059 O  O   A SER   A 554 ? 0.4097 0.7813 0.7603 0.1561  -0.0734 -0.0432 533 SER   A O   
4060 O  O   B SER   A 554 ? 0.4096 0.7810 0.7604 0.1565  -0.0737 -0.0430 533 SER   A O   
4061 C  CB  A SER   A 554 ? 0.3573 0.7420 0.7114 0.1516  -0.1011 -0.0231 533 SER   A CB  
4062 C  CB  B SER   A 554 ? 0.3571 0.7415 0.7111 0.1517  -0.1012 -0.0230 533 SER   A CB  
4063 O  OG  A SER   A 554 ? 0.3389 0.7469 0.6992 0.1418  -0.1100 -0.0201 533 SER   A OG  
4064 O  OG  B SER   A 554 ? 0.3731 0.7248 0.7150 0.1635  -0.1090 -0.0129 533 SER   A OG  
4065 N  N   . ASN   A 555 ? 0.4190 0.7373 0.7337 0.1492  -0.0797 -0.0270 534 ASN   A N   
4066 C  CA  . ASN   A 555 ? 0.4049 0.7002 0.7156 0.1579  -0.0722 -0.0329 534 ASN   A CA  
4067 C  C   . ASN   A 555 ? 0.4609 0.7682 0.7674 0.1468  -0.0586 -0.0427 534 ASN   A C   
4068 O  O   . ASN   A 555 ? 0.4234 0.7172 0.7130 0.1360  -0.0553 -0.0387 534 ASN   A O   
4069 C  CB  . ASN   A 555 ? 0.4257 0.6792 0.7170 0.1613  -0.0773 -0.0214 534 ASN   A CB  
4070 C  CG  . ASN   A 555 ? 0.4861 0.7131 0.7771 0.1715  -0.0724 -0.0265 534 ASN   A CG  
4071 O  OD1 . ASN   A 555 ? 0.4927 0.7296 0.7908 0.1723  -0.0631 -0.0410 534 ASN   A OD1 
4072 N  ND2 . ASN   A 555 ? 0.6413 0.8355 0.9236 0.1786  -0.0789 -0.0144 534 ASN   A ND2 
4073 N  N   . GLU   A 556 ? 0.3865 0.7212 0.7079 0.1498  -0.0509 -0.0553 535 GLU   A N   
4074 C  CA  . GLU   A 556 ? 0.3896 0.7420 0.7063 0.1389  -0.0377 -0.0632 535 GLU   A CA  
4075 C  C   . GLU   A 556 ? 0.3438 0.6664 0.6439 0.1401  -0.0321 -0.0667 535 GLU   A C   
4076 O  O   . GLU   A 556 ? 0.4104 0.7317 0.6966 0.1272  -0.0254 -0.0640 535 GLU   A O   
4077 C  CB  . GLU   A 556 ? 0.3876 0.7760 0.7218 0.1441  -0.0312 -0.0765 535 GLU   A CB  
4078 C  CG  . GLU   A 556 ? 0.5002 0.9166 0.8547 0.1470  -0.0379 -0.0745 535 GLU   A CG  
4079 C  CD  . GLU   A 556 ? 0.5446 0.9892 0.9177 0.1589  -0.0338 -0.0892 535 GLU   A CD  
4080 O  OE1 . GLU   A 556 ? 0.5249 0.9882 0.8952 0.1557  -0.0225 -0.1000 535 GLU   A OE1 
4081 O  OE2 . GLU   A 556 ? 0.5149 0.9641 0.9049 0.1721  -0.0424 -0.0901 535 GLU   A OE2 
4082 N  N   . SER   A 557 ? 0.3824 0.6808 0.6850 0.1548  -0.0350 -0.0726 536 SER   A N   
4083 C  CA  . SER   A 557 ? 0.4444 0.7126 0.7331 0.1556  -0.0310 -0.0765 536 SER   A CA  
4084 C  C   . SER   A 557 ? 0.3820 0.6245 0.6514 0.1457  -0.0330 -0.0627 536 SER   A C   
4085 O  O   . SER   A 557 ? 0.3423 0.5771 0.5983 0.1377  -0.0259 -0.0648 536 SER   A O   
4086 C  CB  . SER   A 557 ? 0.4492 0.6901 0.7460 0.1718  -0.0369 -0.0813 536 SER   A CB  
4087 O  OG  . SER   A 557 ? 0.5911 0.7948 0.8740 0.1707  -0.0364 -0.0793 536 SER   A OG  
4088 N  N   . LEU   A 558 ? 0.4326 0.6635 0.6998 0.1464  -0.0431 -0.0488 537 LEU   A N   
4089 C  CA  . LEU   A 558 ? 0.4113 0.6195 0.6593 0.1379  -0.0460 -0.0367 537 LEU   A CA  
4090 C  C   . LEU   A 558 ? 0.3854 0.6153 0.6277 0.1221  -0.0400 -0.0365 537 LEU   A C   
4091 O  O   . LEU   A 558 ? 0.4134 0.6277 0.6405 0.1146  -0.0370 -0.0329 537 LEU   A O   
4092 C  CB  . LEU   A 558 ? 0.3974 0.5943 0.6427 0.1419  -0.0587 -0.0227 537 LEU   A CB  
4093 C  CG  . LEU   A 558 ? 0.4188 0.5898 0.6422 0.1358  -0.0634 -0.0099 537 LEU   A CG  
4094 C  CD1 . LEU   A 558 ? 0.3438 0.4795 0.5550 0.1382  -0.0591 -0.0081 537 LEU   A CD1 
4095 C  CD2 . LEU   A 558 ? 0.3518 0.5193 0.5719 0.1400  -0.0759 0.0031  537 LEU   A CD2 
4096 N  N   . VAL   A 559 ? 0.3676 0.6337 0.6231 0.1162  -0.0381 -0.0394 538 VAL   A N   
4097 C  CA  . VAL   A 559 ? 0.3404 0.6276 0.5929 0.0990  -0.0322 -0.0368 538 VAL   A CA  
4098 C  C   . VAL   A 559 ? 0.3531 0.6418 0.5970 0.0939  -0.0196 -0.0425 538 VAL   A C   
4099 O  O   . VAL   A 559 ? 0.3259 0.6074 0.5574 0.0831  -0.0163 -0.0368 538 VAL   A O   
4100 C  CB  . VAL   A 559 ? 0.3608 0.6862 0.6311 0.0925  -0.0319 -0.0377 538 VAL   A CB  
4101 C  CG1 . VAL   A 559 ? 0.3244 0.6696 0.5928 0.0731  -0.0241 -0.0332 538 VAL   A CG1 
4102 C  CG2 . VAL   A 559 ? 0.4153 0.7410 0.6923 0.0946  -0.0454 -0.0315 538 VAL   A CG2 
4103 N  N   . GLN   A 560 ? 0.3597 0.6594 0.6097 0.1015  -0.0131 -0.0542 539 GLN   A N   
4104 C  CA  . GLN   A 560 ? 0.3052 0.6092 0.5449 0.0968  -0.0021 -0.0608 539 GLN   A CA  
4105 C  C   . GLN   A 560 ? 0.3384 0.6064 0.5623 0.0981  -0.0027 -0.0589 539 GLN   A C   
4106 O  O   . GLN   A 560 ? 0.3033 0.5719 0.5146 0.0878  0.0039  -0.0561 539 GLN   A O   
4107 C  CB  . GLN   A 560 ? 0.2682 0.5880 0.5164 0.1072  0.0024  -0.0767 539 GLN   A CB  
4108 C  CG  . GLN   A 560 ? 0.3847 0.7454 0.6476 0.1049  0.0050  -0.0793 539 GLN   A CG  
4109 C  CD  . GLN   A 560 ? 0.4099 0.7975 0.6674 0.0860  0.0125  -0.0697 539 GLN   A CD  
4110 O  OE1 . GLN   A 560 ? 0.4475 0.8367 0.6902 0.0778  0.0202  -0.0688 539 GLN   A OE1 
4111 N  NE2 . GLN   A 560 ? 0.4408 0.8486 0.7107 0.0784  0.0096  -0.0614 539 GLN   A NE2 
4112 N  N   . GLU   A 561 ? 0.3425 0.5784 0.5668 0.1101  -0.0108 -0.0587 540 GLU   A N   
4113 C  CA  . GLU   A 561 ? 0.2882 0.4881 0.4983 0.1107  -0.0119 -0.0554 540 GLU   A CA  
4114 C  C   . GLU   A 561 ? 0.3105 0.5064 0.5084 0.0992  -0.0124 -0.0437 540 GLU   A C   
4115 O  O   . GLU   A 561 ? 0.3131 0.5003 0.4990 0.0932  -0.0068 -0.0434 540 GLU   A O   
4116 C  CB  . GLU   A 561 ? 0.3379 0.5045 0.5504 0.1228  -0.0216 -0.0513 540 GLU   A CB  
4117 C  CG  . GLU   A 561 ? 0.3787 0.5448 0.6051 0.1349  -0.0222 -0.0632 540 GLU   A CG  
4118 C  CD  . GLU   A 561 ? 0.4347 0.5688 0.6646 0.1455  -0.0321 -0.0552 540 GLU   A CD  
4119 O  OE1 . GLU   A 561 ? 0.4727 0.5841 0.6907 0.1427  -0.0376 -0.0397 540 GLU   A OE1 
4120 O  OE2 . GLU   A 561 ? 0.5199 0.6525 0.7641 0.1564  -0.0345 -0.0637 540 GLU   A OE2 
4121 N  N   . ASN   A 562 ? 0.2792 0.4824 0.4802 0.0961  -0.0199 -0.0347 541 ASN   A N   
4122 C  CA  . ASN   A 562 ? 0.3025 0.4904 0.4854 0.0825  -0.0213 -0.0225 541 ASN   A CA  
4123 C  C   . ASN   A 562 ? 0.2912 0.5016 0.4719 0.0659  -0.0129 -0.0198 541 ASN   A C   
4124 O  O   . ASN   A 562 ? 0.2835 0.4746 0.4471 0.0540  -0.0119 -0.0108 541 ASN   A O   
4125 C  CB  . ASN   A 562 ? 0.2790 0.4627 0.4621 0.0830  -0.0331 -0.0146 541 ASN   A CB  
4126 C  CG  . ASN   A 562 ? 0.3046 0.4571 0.4795 0.0949  -0.0415 -0.0096 541 ASN   A CG  
4127 O  OD1 . ASN   A 562 ? 0.3516 0.4750 0.5053 0.0903  -0.0421 -0.0015 541 ASN   A OD1 
4128 N  ND2 . ASN   A 562 ? 0.3408 0.4989 0.5320 0.1094  -0.0474 -0.0129 541 ASN   A ND2 
4129 N  N   . LEU   A 563 ? 0.3077 0.5596 0.5064 0.0652  -0.0070 -0.0265 542 LEU   A N   
4130 C  CA  . LEU   A 563 ? 0.2890 0.5639 0.4854 0.0496  0.0024  -0.0215 542 LEU   A CA  
4131 C  C   . LEU   A 563 ? 0.3096 0.5716 0.4899 0.0490  0.0105  -0.0240 542 LEU   A C   
4132 O  O   . LEU   A 563 ? 0.3138 0.5684 0.4806 0.0356  0.0142  -0.0137 542 LEU   A O   
4133 C  CB  . LEU   A 563 ? 0.3103 0.6199 0.5195 0.0466  0.0077  -0.0255 542 LEU   A CB  
4134 C  CG  . LEU   A 563 ? 0.3228 0.6517 0.5480 0.0397  0.0019  -0.0200 542 LEU   A CG  
4135 C  CD1 . LEU   A 563 ? 0.3330 0.6953 0.5689 0.0387  0.0087  -0.0250 542 LEU   A CD1 
4136 C  CD2 . LEU   A 563 ? 0.3449 0.6723 0.5681 0.0209  -0.0002 -0.0057 542 LEU   A CD2 
4137 N  N   . TYR   A 564 ? 0.2820 0.5369 0.4630 0.0627  0.0123  -0.0374 543 TYR   A N   
4138 C  CA  . TYR   A 564 ? 0.2711 0.5134 0.4384 0.0628  0.0183  -0.0423 543 TYR   A CA  
4139 C  C   . TYR   A 564 ? 0.2719 0.4722 0.4210 0.0585  0.0144  -0.0321 543 TYR   A C   
4140 O  O   . TYR   A 564 ? 0.2952 0.4890 0.4296 0.0492  0.0193  -0.0267 543 TYR   A O   
4141 C  CB  . TYR   A 564 ? 0.2722 0.5051 0.4435 0.0764  0.0181  -0.0585 543 TYR   A CB  
4142 C  CG  . TYR   A 564 ? 0.3589 0.5717 0.5184 0.0776  0.0210  -0.0650 543 TYR   A CG  
4143 C  CD1 . TYR   A 564 ? 0.3578 0.5885 0.5057 0.0691  0.0289  -0.0674 543 TYR   A CD1 
4144 C  CD2 . TYR   A 564 ? 0.3015 0.4770 0.4611 0.0862  0.0151  -0.0673 543 TYR   A CD2 
4145 C  CE1 . TYR   A 564 ? 0.3900 0.6046 0.5278 0.0697  0.0305  -0.0741 543 TYR   A CE1 
4146 C  CE2 . TYR   A 564 ? 0.3484 0.5058 0.4993 0.0856  0.0173  -0.0733 543 TYR   A CE2 
4147 C  CZ  . TYR   A 564 ? 0.4341 0.6125 0.5747 0.0776  0.0250  -0.0780 543 TYR   A CZ  
4148 O  OH  . TYR   A 564 ? 0.4810 0.6442 0.6138 0.0766  0.0263  -0.0849 543 TYR   A OH  
4149 N  N   . PHE   A 565 ? 0.3124 0.4836 0.4604 0.0647  0.0054  -0.0283 544 PHE   A N   
4150 C  CA  . PHE   A 565 ? 0.2882 0.4213 0.4169 0.0600  0.0022  -0.0181 544 PHE   A CA  
4151 C  C   . PHE   A 565 ? 0.2941 0.4268 0.4121 0.0451  0.0027  -0.0062 544 PHE   A C   
4152 O  O   . PHE   A 565 ? 0.3025 0.4130 0.4046 0.0394  0.0038  -0.0002 544 PHE   A O   
4153 C  CB  . PHE   A 565 ? 0.2892 0.3987 0.4185 0.0693  -0.0075 -0.0145 544 PHE   A CB  
4154 C  CG  . PHE   A 565 ? 0.3331 0.4340 0.4746 0.0840  -0.0098 -0.0236 544 PHE   A CG  
4155 C  CD1 . PHE   A 565 ? 0.3747 0.4711 0.5174 0.0865  -0.0039 -0.0338 544 PHE   A CD1 
4156 C  CD2 . PHE   A 565 ? 0.3262 0.4236 0.4798 0.0956  -0.0189 -0.0224 544 PHE   A CD2 
4157 C  CE1 . PHE   A 565 ? 0.3981 0.4833 0.5557 0.0999  -0.0073 -0.0440 544 PHE   A CE1 
4158 C  CE2 . PHE   A 565 ? 0.3463 0.4316 0.5134 0.1090  -0.0220 -0.0295 544 PHE   A CE2 
4159 C  CZ  . PHE   A 565 ? 0.3812 0.4573 0.5477 0.1089  -0.0157 -0.0396 544 PHE   A CZ  
4160 N  N   . GLN   A 566 ? 0.2656 0.4227 0.3946 0.0387  0.0013  -0.0030 545 GLN   A N   
4161 C  CA  . GLN   A 566 ? 0.3186 0.4735 0.4418 0.0238  0.0010  0.0079  545 GLN   A CA  
4162 C  C   . GLN   A 566 ? 0.2804 0.4455 0.3979 0.0155  0.0099  0.0117  545 GLN   A C   
4163 O  O   . GLN   A 566 ? 0.3066 0.4544 0.4133 0.0069  0.0096  0.0205  545 GLN   A O   
4164 C  CB  . GLN   A 566 ? 0.2718 0.4507 0.4119 0.0169  -0.0033 0.0110  545 GLN   A CB  
4165 C  CG  . GLN   A 566 ? 0.2927 0.4622 0.4306 0.0016  -0.0067 0.0216  545 GLN   A CG  
4166 C  CD  . GLN   A 566 ? 0.3128 0.4458 0.4357 0.0034  -0.0145 0.0222  545 GLN   A CD  
4167 O  OE1 . GLN   A 566 ? 0.3626 0.4885 0.4843 0.0115  -0.0218 0.0176  545 GLN   A OE1 
4168 N  NE2 . GLN   A 566 ? 0.2483 0.3609 0.3598 -0.0034 -0.0131 0.0278  545 GLN   A NE2 
4169 N  N   . ARG   A 567 ? 0.3106 0.5056 0.4353 0.0190  0.0173  0.0044  546 ARG   A N   
4170 C  CA  . ARG   A 567 ? 0.2938 0.5023 0.4106 0.0125  0.0254  0.0074  546 ARG   A CA  
4171 C  C   . ARG   A 567 ? 0.2869 0.4630 0.3862 0.0155  0.0255  0.0063  546 ARG   A C   
4172 O  O   . ARG   A 567 ? 0.3038 0.4753 0.3928 0.0071  0.0278  0.0154  546 ARG   A O   
4173 C  CB  . ARG   A 567 ? 0.2906 0.5403 0.4169 0.0184  0.0332  -0.0046 546 ARG   A CB  
4174 C  CG  . ARG   A 567 ? 0.3446 0.6269 0.4841 0.0132  0.0345  -0.0024 546 ARG   A CG  
4175 C  CD  . ARG   A 567 ? 0.4437 0.7382 0.5765 -0.0034 0.0379  0.0140  546 ARG   A CD  
4176 N  NE  . ARG   A 567 ? 0.4473 0.7415 0.5621 -0.0054 0.0426  0.0151  546 ARG   A NE  
4177 C  CZ  . ARG   A 567 ? 0.4656 0.7842 0.5735 -0.0046 0.0472  0.0098  546 ARG   A CZ  
4178 N  NH1 . ARG   A 567 ? 0.4270 0.7722 0.5442 -0.0013 0.0492  0.0019  546 ARG   A NH1 
4179 N  NH2 . ARG   A 567 ? 0.4517 0.7704 0.5434 -0.0071 0.0491  0.0124  546 ARG   A NH2 
4180 N  N   . CYS   A 568 ? 0.3060 0.4604 0.4038 0.0271  0.0225  -0.0038 547 CYS   A N   
4181 C  CA  . CYS   A 568 ? 0.3478 0.4724 0.4315 0.0287  0.0223  -0.0040 547 CYS   A CA  
4182 C  C   . CYS   A 568 ? 0.2931 0.3919 0.3653 0.0216  0.0181  0.0085  547 CYS   A C   
4183 O  O   . CYS   A 568 ? 0.2903 0.3782 0.3514 0.0171  0.0202  0.0131  547 CYS   A O   
4184 C  CB  . CYS   A 568 ? 0.2724 0.3779 0.3601 0.0409  0.0189  -0.0139 547 CYS   A CB  
4185 S  SG  . CYS   A 568 ? 0.2964 0.4270 0.4012 0.0525  0.0222  -0.0338 547 CYS   A SG  
4186 N  N   . LEU   A 569 ? 0.2749 0.3655 0.3504 0.0215  0.0116  0.0126  548 LEU   A N   
4187 C  CA  . LEU   A 569 ? 0.2655 0.3346 0.3316 0.0158  0.0070  0.0207  548 LEU   A CA  
4188 C  C   . LEU   A 569 ? 0.2673 0.3441 0.3340 0.0044  0.0090  0.0295  548 LEU   A C   
4189 O  O   . LEU   A 569 ? 0.2828 0.3416 0.3401 0.0013  0.0083  0.0343  548 LEU   A O   
4190 C  CB  . LEU   A 569 ? 0.2352 0.3009 0.3064 0.0175  -0.0011 0.0209  548 LEU   A CB  
4191 C  CG  . LEU   A 569 ? 0.3155 0.3706 0.3848 0.0290  -0.0050 0.0166  548 LEU   A CG  
4192 C  CD1 . LEU   A 569 ? 0.2383 0.3038 0.3175 0.0315  -0.0129 0.0157  548 LEU   A CD1 
4193 C  CD2 . LEU   A 569 ? 0.3079 0.3366 0.3603 0.0306  -0.0065 0.0198  548 LEU   A CD2 
4194 N  N   . ASP   A 570 ? 0.2992 0.4040 0.3783 -0.0018 0.0113  0.0327  549 ASP   A N   
4195 C  CA  . ASP   A 570 ? 0.3109 0.4237 0.3931 -0.0140 0.0124  0.0451  549 ASP   A CA  
4196 C  C   . ASP   A 570 ? 0.3008 0.4179 0.3730 -0.0151 0.0185  0.0487  549 ASP   A C   
4197 O  O   . ASP   A 570 ? 0.2539 0.3638 0.3239 -0.0226 0.0173  0.0603  549 ASP   A O   
4198 C  CB  . ASP   A 570 ? 0.2992 0.4459 0.3983 -0.0215 0.0140  0.0498  549 ASP   A CB  
4199 C  CG  . ASP   A 570 ? 0.3058 0.4498 0.4172 -0.0229 0.0064  0.0478  549 ASP   A CG  
4200 O  OD1 . ASP   A 570 ? 0.3187 0.4336 0.4249 -0.0216 -0.0012 0.0462  549 ASP   A OD1 
4201 O  OD2 . ASP   A 570 ? 0.3619 0.5361 0.4884 -0.0250 0.0078  0.0468  549 ASP   A OD2 
4202 N  N   . TRP   A 571 ? 0.3159 0.4453 0.3837 -0.0075 0.0242  0.0385  550 TRP   A N   
4203 C  CA  . TRP   A 571 ? 0.2647 0.3986 0.3222 -0.0078 0.0288  0.0391  550 TRP   A CA  
4204 C  C   . TRP   A 571 ? 0.2603 0.3607 0.3068 -0.0063 0.0254  0.0415  550 TRP   A C   
4205 O  O   . TRP   A 571 ? 0.3096 0.4091 0.3505 -0.0106 0.0260  0.0499  550 TRP   A O   
4206 C  CB  . TRP   A 571 ? 0.3001 0.4507 0.3573 0.0010  0.0339  0.0232  550 TRP   A CB  
4207 C  CG  . TRP   A 571 ? 0.4024 0.5736 0.4520 -0.0010 0.0391  0.0224  550 TRP   A CG  
4208 C  CD1 . TRP   A 571 ? 0.4317 0.6396 0.4817 -0.0055 0.0435  0.0250  550 TRP   A CD1 
4209 C  CD2 . TRP   A 571 ? 0.3811 0.5376 0.4201 0.0013  0.0392  0.0185  550 TRP   A CD2 
4210 N  NE1 . TRP   A 571 ? 0.4161 0.6274 0.4539 -0.0054 0.0440  0.0220  550 TRP   A NE1 
4211 C  CE2 . TRP   A 571 ? 0.4443 0.6335 0.4784 -0.0017 0.0439  0.0185  550 TRP   A CE2 
4212 C  CE3 . TRP   A 571 ? 0.4219 0.5444 0.4554 0.0050  0.0359  0.0156  550 TRP   A CE3 
4213 C  CZ2 . TRP   A 571 ? 0.4481 0.6335 0.4726 -0.0007 0.0436  0.0142  550 TRP   A CZ2 
4214 C  CZ3 . TRP   A 571 ? 0.4601 0.5811 0.4860 0.0053  0.0371  0.0121  550 TRP   A CZ3 
4215 C  CH2 . TRP   A 571 ? 0.4632 0.6157 0.4851 0.0026  0.0408  0.0110  550 TRP   A CH2 
4216 N  N   . ASN   A 572 ? 0.3115 0.3870 0.3555 0.0002  0.0216  0.0349  551 ASN   A N   
4217 C  CA  . ASN   A 572 ? 0.2750 0.3232 0.3094 0.0016  0.0188  0.0369  551 ASN   A CA  
4218 C  C   . ASN   A 572 ? 0.2737 0.3109 0.3102 -0.0044 0.0137  0.0464  551 ASN   A C   
4219 O  O   . ASN   A 572 ? 0.2933 0.3187 0.3247 -0.0053 0.0128  0.0508  551 ASN   A O   
4220 C  CB  . ASN   A 572 ? 0.2527 0.2825 0.2836 0.0092  0.0163  0.0296  551 ASN   A CB  
4221 C  CG  . ASN   A 572 ? 0.2852 0.3153 0.3147 0.0149  0.0200  0.0213  551 ASN   A CG  
4222 O  OD1 . ASN   A 572 ? 0.3054 0.3290 0.3287 0.0147  0.0224  0.0206  551 ASN   A OD1 
4223 N  ND2 . ASN   A 572 ? 0.2498 0.2875 0.2878 0.0202  0.0198  0.0143  551 ASN   A ND2 
4224 N  N   . ARG   A 573 ? 0.2797 0.3205 0.3262 -0.0083 0.0095  0.0486  552 ARG   A N   
4225 C  CA  . ARG   A 573 ? 0.2642 0.2931 0.3170 -0.0150 0.0032  0.0561  552 ARG   A CA  
4226 C  C   . ARG   A 573 ? 0.2622 0.2962 0.3173 -0.0216 0.0047  0.0687  552 ARG   A C   
4227 O  O   . ARG   A 573 ? 0.3086 0.3234 0.3638 -0.0222 0.0002  0.0728  552 ARG   A O   
4228 C  CB  . ARG   A 573 ? 0.2658 0.3052 0.3330 -0.0208 -0.0011 0.0574  552 ARG   A CB  
4229 C  CG  . ARG   A 573 ? 0.2454 0.2682 0.3225 -0.0272 -0.0101 0.0606  552 ARG   A CG  
4230 C  CD  . ARG   A 573 ? 0.2918 0.3326 0.3870 -0.0365 -0.0131 0.0647  552 ARG   A CD  
4231 N  NE  . ARG   A 573 ? 0.3082 0.3326 0.4146 -0.0414 -0.0236 0.0619  552 ARG   A NE  
4232 C  CZ  . ARG   A 573 ? 0.3654 0.3850 0.4707 -0.0364 -0.0297 0.0495  552 ARG   A CZ  
4233 N  NH1 . ARG   A 573 ? 0.3709 0.3981 0.4648 -0.0261 -0.0265 0.0415  552 ARG   A NH1 
4234 N  NH2 . ARG   A 573 ? 0.3053 0.3124 0.4223 -0.0417 -0.0401 0.0451  552 ARG   A NH2 
4235 N  N   . ASP   A 574 ? 0.2783 0.3399 0.3351 -0.0256 0.0106  0.0746  553 ASP   A N   
4236 C  CA  . ASP   A 574 ? 0.2687 0.3410 0.3270 -0.0326 0.0117  0.0898  553 ASP   A CA  
4237 C  C   . ASP   A 574 ? 0.2818 0.3426 0.3283 -0.0267 0.0126  0.0887  553 ASP   A C   
4238 O  O   . ASP   A 574 ? 0.2955 0.3484 0.3443 -0.0296 0.0088  0.1000  553 ASP   A O   
4239 C  CB  . ASP   A 574 ? 0.2500 0.3619 0.3102 -0.0373 0.0188  0.0946  553 ASP   A CB  
4240 C  CG  . ASP   A 574 ? 0.3404 0.4689 0.4152 -0.0444 0.0181  0.0979  553 ASP   A CG  
4241 O  OD1 . ASP   A 574 ? 0.3452 0.4538 0.4305 -0.0483 0.0111  0.0998  553 ASP   A OD1 
4242 O  OD2 . ASP   A 574 ? 0.3755 0.5345 0.4496 -0.0444 0.0230  0.0946  553 ASP   A OD2 
4243 N  N   . ILE   A 575 ? 0.2428 0.3026 0.2787 -0.0185 0.0167  0.0749  554 ILE   A N   
4244 C  CA  . ILE   A 575 ? 0.3075 0.3579 0.3342 -0.0136 0.0173  0.0727  554 ILE   A CA  
4245 C  C   . ILE   A 575 ? 0.3333 0.3544 0.3608 -0.0105 0.0115  0.0726  554 ILE   A C   
4246 O  O   . ILE   A 575 ? 0.3391 0.3535 0.3662 -0.0094 0.0092  0.0785  554 ILE   A O   
4247 C  CB  . ILE   A 575 ? 0.2901 0.3438 0.3091 -0.0071 0.0222  0.0580  554 ILE   A CB  
4248 C  CG1 . ILE   A 575 ? 0.3792 0.4634 0.3987 -0.0083 0.0275  0.0537  554 ILE   A CG1 
4249 C  CG2 . ILE   A 575 ? 0.3430 0.3884 0.3549 -0.0035 0.0226  0.0558  554 ILE   A CG2 
4250 C  CD1 . ILE   A 575 ? 0.5069 0.5915 0.5220 -0.0023 0.0307  0.0387  554 ILE   A CD1 
4251 N  N   . LEU   A 576 ? 0.2750 0.2808 0.3036 -0.0078 0.0087  0.0647  555 LEU   A N   
4252 C  CA  . LEU   A 576 ? 0.2809 0.2635 0.3088 -0.0034 0.0036  0.0606  555 LEU   A CA  
4253 C  C   . LEU   A 576 ? 0.3188 0.2912 0.3585 -0.0077 -0.0034 0.0700  555 LEU   A C   
4254 O  O   . LEU   A 576 ? 0.3606 0.3197 0.4012 -0.0033 -0.0066 0.0698  555 LEU   A O   
4255 C  CB  . LEU   A 576 ? 0.2968 0.2708 0.3224 -0.0001 0.0013  0.0506  555 LEU   A CB  
4256 C  CG  . LEU   A 576 ? 0.2765 0.2534 0.2914 0.0056  0.0066  0.0431  555 LEU   A CG  
4257 C  CD1 . LEU   A 576 ? 0.3304 0.3071 0.3454 0.0075  0.0044  0.0379  555 LEU   A CD1 
4258 C  CD2 . LEU   A 576 ? 0.3026 0.2689 0.3089 0.0112  0.0076  0.0391  555 LEU   A CD2 
4259 N  N   . LYS   A 577 ? 0.2850 0.2639 0.3364 -0.0163 -0.0062 0.0787  556 LYS   A N   
4260 C  CA  . LYS   A 577 ? 0.3226 0.2902 0.3888 -0.0221 -0.0137 0.0900  556 LYS   A CA  
4261 C  C   . LYS   A 577 ? 0.3611 0.3367 0.4244 -0.0209 -0.0124 0.0975  556 LYS   A C   
4262 O  O   . LYS   A 577 ? 0.4299 0.3903 0.4991 -0.0180 -0.0181 0.0979  556 LYS   A O   
4263 C  CB  . LYS   A 577 ? 0.3363 0.3156 0.4156 -0.0331 -0.0157 0.0981  556 LYS   A CB  
4264 C  CG  . LYS   A 577 ? 0.3692 0.3440 0.4528 -0.0339 -0.0185 0.0874  556 LYS   A CG  
4265 C  CD  . LYS   A 577 ? 0.4236 0.4007 0.5279 -0.0464 -0.0246 0.0966  556 LYS   A CD  
4266 C  CE  . LYS   A 577 ? 0.4056 0.4164 0.5124 -0.0544 -0.0177 0.1086  556 LYS   A CE  
4267 N  NZ  . LYS   A 577 ? 0.4698 0.4874 0.5949 -0.0651 -0.0228 0.1136  556 LYS   A NZ  
4268 N  N   . LYS   A 578 ? 0.3386 0.3394 0.3936 -0.0225 -0.0054 0.1023  557 LYS   A N   
4269 C  CA  . LYS   A 578 ? 0.3503 0.3624 0.4028 -0.0217 -0.0052 0.1098  557 LYS   A CA  
4270 C  C   . LYS   A 578 ? 0.3914 0.3907 0.4377 -0.0127 -0.0056 0.1036  557 LYS   A C   
4271 O  O   . LYS   A 578 ? 0.3936 0.3859 0.4452 -0.0104 -0.0104 0.1086  557 LYS   A O   
4272 C  CB  . LYS   A 578 ? 0.3626 0.4073 0.4069 -0.0245 0.0017  0.1125  557 LYS   A CB  
4273 C  CG  . LYS   A 578 ? 0.3834 0.4424 0.4231 -0.0226 0.0017  0.1180  557 LYS   A CG  
4274 C  CD  . LYS   A 578 ? 0.5676 0.6617 0.6004 -0.0254 0.0067  0.1190  557 LYS   A CD  
4275 C  CE  . LYS   A 578 ? 0.6503 0.7540 0.6711 -0.0206 0.0134  0.1044  557 LYS   A CE  
4276 N  NZ  . LYS   A 578 ? 0.8607 0.9985 0.8748 -0.0214 0.0163  0.1022  557 LYS   A NZ  
4277 N  N   . GLU   A 579 ? 0.3579 0.3555 0.3943 -0.0074 -0.0006 0.0936  558 GLU   A N   
4278 C  CA  . GLU   A 579 ? 0.3177 0.3100 0.3485 0.0006  0.0005  0.0888  558 GLU   A CA  
4279 C  C   . GLU   A 579 ? 0.3956 0.3633 0.4310 0.0078  -0.0043 0.0806  558 GLU   A C   
4280 O  O   . GLU   A 579 ? 0.4017 0.3671 0.4356 0.0150  -0.0042 0.0762  558 GLU   A O   
4281 C  CB  . GLU   A 579 ? 0.3209 0.3253 0.3398 0.0027  0.0082  0.0772  558 GLU   A CB  
4282 C  CG  . GLU   A 579 ? 0.3328 0.3643 0.3474 -0.0021 0.0129  0.0807  558 GLU   A CG  
4283 C  CD  . GLU   A 579 ? 0.3932 0.4406 0.4068 -0.0021 0.0116  0.0900  558 GLU   A CD  
4284 O  OE1 . GLU   A 579 ? 0.4280 0.4663 0.4429 0.0033  0.0091  0.0890  558 GLU   A OE1 
4285 O  OE2 . GLU   A 579 ? 0.5384 0.6092 0.5508 -0.0067 0.0124  0.0947  558 GLU   A OE2 
4286 N  N   . LEU   A 580 ? 0.3796 0.3321 0.4208 0.0064  -0.0085 0.0762  559 LEU   A N   
4287 C  CA  . LEU   A 580 ? 0.3408 0.2735 0.3859 0.0139  -0.0135 0.0645  559 LEU   A CA  
4288 C  C   . LEU   A 580 ? 0.3621 0.2793 0.4222 0.0116  -0.0228 0.0666  559 LEU   A C   
4289 O  O   . LEU   A 580 ? 0.4094 0.3104 0.4748 0.0182  -0.0281 0.0546  559 LEU   A O   
4290 C  CB  . LEU   A 580 ? 0.3198 0.2506 0.3557 0.0154  -0.0112 0.0507  559 LEU   A CB  
4291 C  CG  . LEU   A 580 ? 0.3187 0.2628 0.3394 0.0174  -0.0023 0.0456  559 LEU   A CG  
4292 C  CD1 . LEU   A 580 ? 0.3001 0.2408 0.3134 0.0196  -0.0021 0.0353  559 LEU   A CD1 
4293 C  CD2 . LEU   A 580 ? 0.2746 0.2229 0.2910 0.0237  0.0012  0.0430  559 LEU   A CD2 
4294 N  N   . GLY   A 581 ? 0.3388 0.2633 0.4059 0.0027  -0.0244 0.0796  560 GLY   A N   
4295 C  CA  . GLY   A 581 ? 0.3353 0.2466 0.4188 -0.0007 -0.0329 0.0829  560 GLY   A CA  
4296 C  C   . GLY   A 581 ? 0.4213 0.3202 0.5137 -0.0046 -0.0382 0.0750  560 GLY   A C   
4297 O  O   . GLY   A 581 ? 0.4662 0.3476 0.5716 -0.0027 -0.0464 0.0683  560 GLY   A O   
4298 N  N   . LEU   A 582 ? 0.4198 0.3282 0.5071 -0.0097 -0.0345 0.0748  561 LEU   A N   
4299 C  CA  . LEU   A 582 ? 0.4095 0.3083 0.5050 -0.0132 -0.0402 0.0663  561 LEU   A CA  
4300 C  C   . LEU   A 582 ? 0.4482 0.3551 0.5585 -0.0262 -0.0431 0.0787  561 LEU   A C   
4301 O  O   . LEU   A 582 ? 0.4862 0.4132 0.5948 -0.0324 -0.0377 0.0933  561 LEU   A O   
4302 C  CB  . LEU   A 582 ? 0.4178 0.3230 0.5003 -0.0102 -0.0354 0.0584  561 LEU   A CB  
4303 C  CG  . LEU   A 582 ? 0.4238 0.3298 0.4879 0.0020  -0.0300 0.0450  561 LEU   A CG  
4304 C  CD1 . LEU   A 582 ? 0.4105 0.3305 0.4596 0.0033  -0.0239 0.0383  561 LEU   A CD1 
4305 C  CD2 . LEU   A 582 ? 0.4418 0.3298 0.5100 0.0103  -0.0374 0.0295  561 LEU   A CD2 
4306 N  N   . THR   A 583 ? 0.4363 0.3298 0.5614 -0.0299 -0.0520 0.0716  562 THR   A N   
4307 C  CA  . THR   A 583 ? 0.4496 0.3514 0.5904 -0.0427 -0.0554 0.0811  562 THR   A CA  
4308 C  C   . THR   A 583 ? 0.4625 0.3671 0.6042 -0.0456 -0.0571 0.0709  562 THR   A C   
4309 O  O   . THR   A 583 ? 0.4248 0.3213 0.5555 -0.0372 -0.0574 0.0561  562 THR   A O   
4310 C  CB  . THR   A 583 ? 0.4793 0.3645 0.6407 -0.0462 -0.0658 0.0820  562 THR   A CB  
4311 O  OG1 . THR   A 583 ? 0.4872 0.3528 0.6540 -0.0409 -0.0742 0.0609  562 THR   A OG1 
4312 C  CG2 . THR   A 583 ? 0.3950 0.2740 0.5564 -0.0411 -0.0659 0.0896  562 THR   A CG2 
4313 N  N   . GLU   A 584 ? 0.4404 0.3585 0.5957 -0.0576 -0.0586 0.0791  563 GLU   A N   
4314 C  CA  . GLU   A 584 ? 0.4152 0.3392 0.5753 -0.0617 -0.0617 0.0693  563 GLU   A CA  
4315 C  C   . GLU   A 584 ? 0.4228 0.3244 0.5882 -0.0570 -0.0733 0.0476  563 GLU   A C   
4316 O  O   . GLU   A 584 ? 0.4215 0.3320 0.5798 -0.0534 -0.0749 0.0332  563 GLU   A O   
4317 C  CB  . GLU   A 584 ? 0.3770 0.3232 0.5527 -0.0753 -0.0612 0.0814  563 GLU   A CB  
4318 C  CG  . GLU   A 584 ? 0.4591 0.4372 0.6264 -0.0781 -0.0489 0.0954  563 GLU   A CG  
4319 C  CD  . GLU   A 584 ? 0.4287 0.4196 0.5787 -0.0685 -0.0422 0.0837  563 GLU   A CD  
4320 O  OE1 . GLU   A 584 ? 0.4322 0.4206 0.5807 -0.0638 -0.0472 0.0678  563 GLU   A OE1 
4321 O  OE2 . GLU   A 584 ? 0.4147 0.4192 0.5489 -0.0627 -0.0322 0.0879  563 GLU   A OE2 
4322 N  N   . GLN   A 585 ? 0.4355 0.3173 0.6071 -0.0526 -0.0794 0.0423  564 GLN   A N   
4323 C  CA  . GLN   A 585 ? 0.4687 0.3333 0.6441 -0.0461 -0.0898 0.0187  564 GLN   A CA  
4324 C  C   . GLN   A 585 ? 0.4681 0.3273 0.6221 -0.0316 -0.0879 0.0011  564 GLN   A C   
4325 O  O   . GLN   A 585 ? 0.4399 0.2930 0.5917 -0.0249 -0.0956 -0.0214 564 GLN   A O   
4326 C  CB  . GLN   A 585 ? 0.5208 0.3682 0.7116 -0.0452 -0.0965 0.0184  564 GLN   A CB  
4327 C  CG  . GLN   A 585 ? 0.6289 0.4793 0.8417 -0.0594 -0.0998 0.0357  564 GLN   A CG  
4328 C  CD  . GLN   A 585 ? 0.9323 0.7715 1.1553 -0.0592 -0.1013 0.0490  564 GLN   A CD  
4329 O  OE1 . GLN   A 585 ? 0.9052 0.7252 1.1353 -0.0516 -0.1084 0.0368  564 GLN   A OE1 
4330 N  NE2 . GLN   A 585 ? 0.9273 0.7808 1.1512 -0.0671 -0.0950 0.0734  564 GLN   A NE2 
4331 N  N   . ASP   A 586 ? 0.4513 0.3179 0.5870 -0.0255 -0.0769 0.0103  565 ASP   A N   
4332 C  CA  . ASP   A 586 ? 0.4524 0.3230 0.5630 -0.0105 -0.0710 -0.0031 565 ASP   A CA  
4333 C  C   . ASP   A 586 ? 0.4312 0.3248 0.5208 -0.0077 -0.0628 -0.0037 565 ASP   A C   
4334 O  O   . ASP   A 586 ? 0.4372 0.3367 0.5059 0.0026  -0.0563 -0.0094 565 ASP   A O   
4335 C  CB  . ASP   A 586 ? 0.4657 0.3315 0.5701 -0.0047 -0.0641 0.0065  565 ASP   A CB  
4336 C  CG  . ASP   A 586 ? 0.5241 0.3755 0.6463 -0.0062 -0.0698 0.0105  565 ASP   A CG  
4337 O  OD1 . ASP   A 586 ? 0.5506 0.3907 0.6842 -0.0043 -0.0791 -0.0041 565 ASP   A OD1 
4338 O  OD2 . ASP   A 586 ? 0.5425 0.3989 0.6651 -0.0087 -0.0644 0.0276  565 ASP   A OD2 
4339 N  N   . ILE   A 587 ? 0.4187 0.3261 0.5153 -0.0166 -0.0632 0.0029  566 ILE   A N   
4340 C  CA  . ILE   A 587 ? 0.4063 0.3347 0.4875 -0.0136 -0.0558 0.0050  566 ILE   A CA  
4341 C  C   . ILE   A 587 ? 0.4037 0.3417 0.4893 -0.0153 -0.0639 -0.0053 566 ILE   A C   
4342 O  O   . ILE   A 587 ? 0.4365 0.3742 0.5434 -0.0257 -0.0717 -0.0048 566 ILE   A O   
4343 C  CB  . ILE   A 587 ? 0.3541 0.2973 0.4398 -0.0205 -0.0472 0.0228  566 ILE   A CB  
4344 C  CG1 . ILE   A 587 ? 0.3660 0.3017 0.4493 -0.0200 -0.0414 0.0333  566 ILE   A CG1 
4345 C  CG2 . ILE   A 587 ? 0.3166 0.2782 0.3884 -0.0147 -0.0402 0.0224  566 ILE   A CG2 
4346 C  CD1 . ILE   A 587 ? 0.3948 0.3493 0.4803 -0.0261 -0.0330 0.0491  566 ILE   A CD1 
4347 N  N   . ILE   A 588 ? 0.4111 0.3588 0.4778 -0.0058 -0.0625 -0.0133 567 ILE   A N   
4348 C  CA  . ILE   A 588 ? 0.4235 0.3863 0.4910 -0.0057 -0.0692 -0.0203 567 ILE   A CA  
4349 C  C   . ILE   A 588 ? 0.3872 0.3670 0.4467 -0.0023 -0.0613 -0.0101 567 ILE   A C   
4350 O  O   . ILE   A 588 ? 0.3939 0.3721 0.4371 0.0050  -0.0528 -0.0053 567 ILE   A O   
4351 C  CB  . ILE   A 588 ? 0.4619 0.4247 0.5142 0.0034  -0.0760 -0.0375 567 ILE   A CB  
4352 C  CG1 . ILE   A 588 ? 0.4353 0.3809 0.4985 0.0017  -0.0847 -0.0520 567 ILE   A CG1 
4353 C  CG2 . ILE   A 588 ? 0.4105 0.3924 0.4627 0.0040  -0.0838 -0.0432 567 ILE   A CG2 
4354 C  CD1 . ILE   A 588 ? 0.3913 0.3328 0.4825 -0.0107 -0.0955 -0.0550 567 ILE   A CD1 
4355 N  N   . ASP   A 589 ? 0.3725 0.3688 0.4460 -0.0075 -0.0645 -0.0074 568 ASP   A N   
4356 C  CA  . ASP   A 589 ? 0.3827 0.3961 0.4533 -0.0028 -0.0588 -0.0004 568 ASP   A CA  
4357 C  C   . ASP   A 589 ? 0.3872 0.4107 0.4482 0.0057  -0.0660 -0.0073 568 ASP   A C   
4358 O  O   . ASP   A 589 ? 0.4341 0.4673 0.5050 0.0024  -0.0763 -0.0148 568 ASP   A O   
4359 C  CB  . ASP   A 589 ? 0.3242 0.3551 0.4171 -0.0122 -0.0573 0.0068  568 ASP   A CB  
4360 C  CG  . ASP   A 589 ? 0.4345 0.4618 0.5334 -0.0195 -0.0487 0.0175  568 ASP   A CG  
4361 O  OD1 . ASP   A 589 ? 0.3853 0.4139 0.4738 -0.0140 -0.0392 0.0224  568 ASP   A OD1 
4362 O  OD2 . ASP   A 589 ? 0.5018 0.5250 0.6165 -0.0311 -0.0522 0.0213  568 ASP   A OD2 
4363 N  N   . LEU   A 590 ? 0.3817 0.4035 0.4241 0.0161  -0.0613 -0.0037 569 LEU   A N   
4364 C  CA  . LEU   A 590 ? 0.3937 0.4271 0.4269 0.0244  -0.0684 -0.0060 569 LEU   A CA  
4365 C  C   . LEU   A 590 ? 0.3528 0.4007 0.3962 0.0285  -0.0673 0.0013  569 LEU   A C   
4366 O  O   . LEU   A 590 ? 0.3803 0.4246 0.4264 0.0302  -0.0582 0.0083  569 LEU   A O   
4367 C  CB  . LEU   A 590 ? 0.4270 0.4526 0.4353 0.0330  -0.0654 -0.0040 569 LEU   A CB  
4368 C  CG  . LEU   A 590 ? 0.4744 0.4898 0.4705 0.0324  -0.0658 -0.0133 569 LEU   A CG  
4369 C  CD1 . LEU   A 590 ? 0.4544 0.4709 0.4263 0.0409  -0.0622 -0.0092 569 LEU   A CD1 
4370 C  CD2 . LEU   A 590 ? 0.4576 0.4790 0.4599 0.0291  -0.0778 -0.0286 569 LEU   A CD2 
4371 N  N   . PRO   A 591 ? 0.3634 0.4294 0.4143 0.0310  -0.0771 -0.0016 570 PRO   A N   
4372 C  CA  . PRO   A 591 ? 0.3742 0.4556 0.4382 0.0368  -0.0768 0.0041  570 PRO   A CA  
4373 C  C   . PRO   A 591 ? 0.3206 0.3918 0.3722 0.0478  -0.0715 0.0132  570 PRO   A C   
4374 O  O   . PRO   A 591 ? 0.4043 0.4665 0.4360 0.0531  -0.0731 0.0169  570 PRO   A O   
4375 C  CB  . PRO   A 591 ? 0.3334 0.4354 0.4034 0.0392  -0.0903 -0.0010 570 PRO   A CB  
4376 C  CG  . PRO   A 591 ? 0.3970 0.4926 0.4488 0.0380  -0.0971 -0.0085 570 PRO   A CG  
4377 C  CD  . PRO   A 591 ? 0.4265 0.5015 0.4750 0.0297  -0.0895 -0.0119 570 PRO   A CD  
4378 N  N   . ALA   A 592 ? 0.3435 0.4176 0.4085 0.0508  -0.0650 0.0165  571 ALA   A N   
4379 C  CA  . ALA   A 592 ? 0.3137 0.3765 0.3737 0.0609  -0.0612 0.0239  571 ALA   A CA  
4380 C  C   . ALA   A 592 ? 0.3211 0.3986 0.4036 0.0675  -0.0609 0.0223  571 ALA   A C   
4381 O  O   . ALA   A 592 ? 0.3295 0.4266 0.4293 0.0624  -0.0597 0.0162  571 ALA   A O   
4382 C  CB  . ALA   A 592 ? 0.2994 0.3419 0.3487 0.0574  -0.0504 0.0260  571 ALA   A CB  
4383 N  N   . LEU   A 593 ? 0.3308 0.3997 0.4147 0.0790  -0.0621 0.0280  572 LEU   A N   
4384 C  CA  . LEU   A 593 ? 0.3351 0.4166 0.4420 0.0886  -0.0630 0.0245  572 LEU   A CA  
4385 C  C   . LEU   A 593 ? 0.3409 0.4003 0.4482 0.0969  -0.0593 0.0285  572 LEU   A C   
4386 O  O   . LEU   A 593 ? 0.4153 0.4542 0.5073 0.0987  -0.0617 0.0393  572 LEU   A O   
4387 C  CB  . LEU   A 593 ? 0.3388 0.4386 0.4559 0.0974  -0.0757 0.0268  572 LEU   A CB  
4388 C  CG  . LEU   A 593 ? 0.3942 0.5180 0.5401 0.1063  -0.0776 0.0195  572 LEU   A CG  
4389 C  CD1 . LEU   A 593 ? 0.3944 0.5414 0.5527 0.0952  -0.0697 0.0091  572 LEU   A CD1 
4390 C  CD2 . LEU   A 593 ? 0.3441 0.4833 0.4960 0.1125  -0.0895 0.0240  572 LEU   A CD2 
4391 N  N   . PHE   A 594 ? 0.3190 0.3842 0.4445 0.1012  -0.0537 0.0192  573 PHE   A N   
4392 C  CA  . PHE   A 594 ? 0.3561 0.3996 0.4860 0.1082  -0.0506 0.0190  573 PHE   A CA  
4393 C  C   . PHE   A 594 ? 0.3901 0.4428 0.5418 0.1193  -0.0518 0.0122  573 PHE   A C   
4394 O  O   . PHE   A 594 ? 0.3704 0.4513 0.5370 0.1216  -0.0528 0.0044  573 PHE   A O   
4395 C  CB  . PHE   A 594 ? 0.3560 0.3945 0.4803 0.0991  -0.0386 0.0112  573 PHE   A CB  
4396 C  CG  . PHE   A 594 ? 0.3592 0.3881 0.4598 0.0859  -0.0344 0.0177  573 PHE   A CG  
4397 C  CD1 . PHE   A 594 ? 0.3481 0.3517 0.4331 0.0838  -0.0334 0.0268  573 PHE   A CD1 
4398 C  CD2 . PHE   A 594 ? 0.3504 0.3962 0.4468 0.0756  -0.0316 0.0150  573 PHE   A CD2 
4399 C  CE1 . PHE   A 594 ? 0.3800 0.3776 0.4452 0.0735  -0.0295 0.0308  573 PHE   A CE1 
4400 C  CE2 . PHE   A 594 ? 0.3388 0.3740 0.4165 0.0654  -0.0288 0.0194  573 PHE   A CE2 
4401 C  CZ  . PHE   A 594 ? 0.3117 0.3241 0.3737 0.0652  -0.0276 0.0262  573 PHE   A CZ  
4402 N  N   . LYS   A 595 ? 0.4827 0.5115 0.6346 0.1245  -0.0511 0.0156  574 LYS   A N   
4403 C  CA  . LYS   A 595 ? 0.4550 0.4865 0.6259 0.1342  -0.0507 0.0066  574 LYS   A CA  
4404 C  C   . LYS   A 595 ? 0.4353 0.4534 0.6087 0.1322  -0.0431 -0.0052 574 LYS   A C   
4405 O  O   . LYS   A 595 ? 0.4247 0.4195 0.5850 0.1259  -0.0408 0.0005  574 LYS   A O   
4406 C  CB  . LYS   A 595 ? 0.4264 0.4414 0.5982 0.1430  -0.0588 0.0197  574 LYS   A CB  
4407 N  N   . MET   A 596 ? 0.4276 0.4633 0.6174 0.1370  -0.0392 -0.0224 575 MET   A N   
4408 C  CA  . MET   A 596 ? 0.4202 0.4490 0.6128 0.1354  -0.0327 -0.0369 575 MET   A CA  
4409 C  C   . MET   A 596 ? 0.5327 0.5354 0.7351 0.1430  -0.0376 -0.0381 575 MET   A C   
4410 O  O   . MET   A 596 ? 0.5834 0.5864 0.7981 0.1530  -0.0439 -0.0356 575 MET   A O   
4411 C  CB  . MET   A 596 ? 0.4234 0.4880 0.6261 0.1359  -0.0259 -0.0555 575 MET   A CB  
4412 C  CG  . MET   A 596 ? 0.4480 0.5125 0.6510 0.1336  -0.0194 -0.0722 575 MET   A CG  
4413 S  SD  . MET   A 596 ? 0.5166 0.6301 0.7255 0.1323  -0.0107 -0.0905 575 MET   A SD  
4414 C  CE  . MET   A 596 ? 0.4211 0.5527 0.6138 0.1183  -0.0043 -0.0792 575 MET   A CE  
4415 N  N   . ASP   A 597 ? 0.5840 0.5645 0.7825 0.1381  -0.0353 -0.0418 576 ASP   A N   
4416 C  CA  . ASP   A 597 ? 0.5399 0.4947 0.7503 0.1433  -0.0404 -0.0442 576 ASP   A CA  
4417 C  C   . ASP   A 597 ? 0.5426 0.5088 0.7677 0.1466  -0.0373 -0.0697 576 ASP   A C   
4418 O  O   . ASP   A 597 ? 0.5048 0.5014 0.7289 0.1452  -0.0307 -0.0838 576 ASP   A O   
4419 C  CB  . ASP   A 597 ? 0.5949 0.5173 0.7933 0.1344  -0.0415 -0.0296 576 ASP   A CB  
4420 C  CG  . ASP   A 597 ? 0.6467 0.5698 0.8358 0.1235  -0.0342 -0.0378 576 ASP   A CG  
4421 O  OD1 . ASP   A 597 ? 0.6203 0.5650 0.8145 0.1238  -0.0290 -0.0574 576 ASP   A OD1 
4422 O  OD2 . ASP   A 597 ? 0.6692 0.5735 0.8452 0.1144  -0.0336 -0.0242 576 ASP   A OD2 
4423 N  N   . GLU   A 598 ? 0.6430 0.5858 0.8820 0.1506  -0.0426 -0.0754 577 GLU   A N   
4424 C  CA  . GLU   A 598 ? 0.5837 0.5369 0.8385 0.1550  -0.0418 -0.1015 577 GLU   A CA  
4425 C  C   . GLU   A 598 ? 0.5847 0.5529 0.8289 0.1452  -0.0338 -0.1148 577 GLU   A C   
4426 O  O   . GLU   A 598 ? 0.5465 0.5412 0.7970 0.1481  -0.0305 -0.1368 577 GLU   A O   
4427 C  CB  . GLU   A 598 ? 0.7544 0.6755 1.0274 0.1594  -0.0502 -0.1039 577 GLU   A CB  
4428 C  CG  . GLU   A 598 ? 0.8109 0.6974 1.0754 0.1492  -0.0526 -0.0847 577 GLU   A CG  
4429 C  CD  . GLU   A 598 ? 0.9477 0.8185 1.2035 0.1503  -0.0570 -0.0565 577 GLU   A CD  
4430 O  OE1 . GLU   A 598 ? 0.9476 0.8283 1.2103 0.1612  -0.0608 -0.0534 577 GLU   A OE1 
4431 O  OE2 . GLU   A 598 ? 0.9669 0.8187 1.2088 0.1402  -0.0567 -0.0378 577 GLU   A OE2 
4432 N  N   . ASP   A 599 ? 0.5980 0.5519 0.8258 0.1339  -0.0308 -0.1018 578 ASP   A N   
4433 C  CA  . ASP   A 599 ? 0.5703 0.5386 0.7873 0.1247  -0.0236 -0.1122 578 ASP   A CA  
4434 C  C   . ASP   A 599 ? 0.5311 0.5323 0.7337 0.1214  -0.0157 -0.1105 578 ASP   A C   
4435 O  O   . ASP   A 599 ? 0.5224 0.5367 0.7133 0.1132  -0.0093 -0.1149 578 ASP   A O   
4436 C  CB  . ASP   A 599 ? 0.5674 0.5076 0.7751 0.1140  -0.0238 -0.0995 578 ASP   A CB  
4437 C  CG  . ASP   A 599 ? 0.6749 0.5868 0.8987 0.1142  -0.0307 -0.1036 578 ASP   A CG  
4438 O  OD1 . ASP   A 599 ? 0.6840 0.6022 0.9257 0.1213  -0.0340 -0.1238 578 ASP   A OD1 
4439 O  OD2 . ASP   A 599 ? 0.6849 0.5697 0.9046 0.1069  -0.0330 -0.0866 578 ASP   A OD2 
4440 N  N   . HIS   A 600 ? 0.5051 0.5206 0.7094 0.1270  -0.0164 -0.1034 579 HIS   A N   
4441 C  CA  . HIS   A 600 ? 0.5209 0.5678 0.7149 0.1229  -0.0099 -0.0998 579 HIS   A CA  
4442 C  C   . HIS   A 600 ? 0.4673 0.5025 0.6447 0.1135  -0.0079 -0.0824 579 HIS   A C   
4443 O  O   . HIS   A 600 ? 0.5287 0.5868 0.6965 0.1069  -0.0015 -0.0817 579 HIS   A O   
4444 C  CB  . HIS   A 600 ? 0.4897 0.5721 0.6818 0.1200  -0.0024 -0.1180 579 HIS   A CB  
4445 C  CG  . HIS   A 600 ? 0.5600 0.6586 0.7679 0.1294  -0.0043 -0.1373 579 HIS   A CG  
4446 N  ND1 . HIS   A 600 ? 0.5930 0.7137 0.8111 0.1368  -0.0050 -0.1391 579 HIS   A ND1 
4447 C  CD2 . HIS   A 600 ? 0.5820 0.6793 0.7988 0.1329  -0.0062 -0.1569 579 HIS   A CD2 
4448 C  CE1 . HIS   A 600 ? 0.6112 0.7433 0.8431 0.1451  -0.0069 -0.1589 579 HIS   A CE1 
4449 N  NE2 . HIS   A 600 ? 0.6923 0.8104 0.9238 0.1430  -0.0080 -0.1706 579 HIS   A NE2 
4450 N  N   . ARG   A 601 ? 0.3683 0.3692 0.5419 0.1125  -0.0134 -0.0675 580 ARG   A N   
4451 C  CA  . ARG   A 601 ? 0.4265 0.4152 0.5843 0.1044  -0.0125 -0.0508 580 ARG   A CA  
4452 C  C   . ARG   A 601 ? 0.4504 0.4331 0.6049 0.1076  -0.0188 -0.0332 580 ARG   A C   
4453 O  O   . ARG   A 601 ? 0.4673 0.4454 0.6314 0.1158  -0.0248 -0.0308 580 ARG   A O   
4454 C  CB  . ARG   A 601 ? 0.4148 0.3736 0.5669 0.0979  -0.0130 -0.0460 580 ARG   A CB  
4455 C  CG  . ARG   A 601 ? 0.4697 0.4366 0.6239 0.0936  -0.0076 -0.0637 580 ARG   A CG  
4456 C  CD  . ARG   A 601 ? 0.4519 0.3927 0.6010 0.0851  -0.0078 -0.0572 580 ARG   A CD  
4457 N  NE  . ARG   A 601 ? 0.4556 0.4067 0.6059 0.0804  -0.0033 -0.0740 580 ARG   A NE  
4458 C  CZ  . ARG   A 601 ? 0.4576 0.4005 0.6202 0.0806  -0.0063 -0.0875 580 ARG   A CZ  
4459 N  NH1 . ARG   A 601 ? 0.5450 0.4683 0.7217 0.0857  -0.0135 -0.0865 580 ARG   A NH1 
4460 N  NH2 . ARG   A 601 ? 0.4597 0.4154 0.6212 0.0755  -0.0026 -0.1024 580 ARG   A NH2 
4461 N  N   . ALA   A 602 ? 0.4161 0.4004 0.5573 0.1014  -0.0182 -0.0214 581 ALA   A N   
4462 C  CA  . ALA   A 602 ? 0.3775 0.3640 0.5136 0.1033  -0.0245 -0.0072 581 ALA   A CA  
4463 C  C   . ALA   A 602 ? 0.3822 0.3409 0.5040 0.1006  -0.0290 0.0113  581 ALA   A C   
4464 O  O   . ALA   A 602 ? 0.4475 0.3895 0.5588 0.0930  -0.0255 0.0161  581 ALA   A O   
4465 C  CB  . ALA   A 602 ? 0.2963 0.3035 0.4213 0.0949  -0.0211 -0.0052 581 ALA   A CB  
4466 N  N   . ARG   A 603 ? 0.4144 0.3724 0.5355 0.1064  -0.0363 0.0218  582 ARG   A N   
4467 C  CA  . ARG   A 603 ? 0.4667 0.4084 0.5702 0.1036  -0.0406 0.0405  582 ARG   A CA  
4468 C  C   . ARG   A 603 ? 0.3837 0.3430 0.4807 0.1063  -0.0470 0.0478  582 ARG   A C   
4469 O  O   . ARG   A 603 ? 0.4434 0.4219 0.5549 0.1132  -0.0506 0.0415  582 ARG   A O   
4470 C  CB  . ARG   A 603 ? 0.4818 0.4033 0.5904 0.1085  -0.0447 0.0474  582 ARG   A CB  
4471 C  CG  . ARG   A 603 ? 0.6433 0.5734 0.7714 0.1207  -0.0497 0.0414  582 ARG   A CG  
4472 C  CD  . ARG   A 603 ? 0.7647 0.6720 0.9044 0.1253  -0.0529 0.0434  582 ARG   A CD  
4473 N  NE  . ARG   A 603 ? 0.7845 0.7009 0.9479 0.1358  -0.0544 0.0281  582 ARG   A NE  
4474 C  CZ  . ARG   A 603 ? 0.8872 0.8172 1.0607 0.1465  -0.0602 0.0296  582 ARG   A CZ  
4475 N  NH1 . ARG   A 603 ? 0.9397 0.8765 1.1018 0.1485  -0.0658 0.0456  582 ARG   A NH1 
4476 N  NH2 . ARG   A 603 ? 0.8259 0.7654 1.0216 0.1556  -0.0607 0.0137  582 ARG   A NH2 
4477 N  N   . ALA   A 604 ? 0.4384 0.3940 0.5143 0.1001  -0.0487 0.0597  583 ALA   A N   
4478 C  CA  . ALA   A 604 ? 0.3973 0.3711 0.4653 0.1010  -0.0557 0.0645  583 ALA   A CA  
4479 C  C   . ALA   A 604 ? 0.4206 0.4037 0.4966 0.1117  -0.0643 0.0683  583 ALA   A C   
4480 O  O   . ALA   A 604 ? 0.4291 0.3973 0.5025 0.1165  -0.0673 0.0770  583 ALA   A O   
4481 C  CB  . ALA   A 604 ? 0.4387 0.4066 0.4812 0.0934  -0.0562 0.0761  583 ALA   A CB  
4482 N  N   . PHE   A 605 ? 0.4224 0.4312 0.5104 0.1142  -0.0686 0.0623  584 PHE   A N   
4483 C  CA  . PHE   A 605 ? 0.4155 0.4393 0.5123 0.1232  -0.0769 0.0673  584 PHE   A CA  
4484 C  C   . PHE   A 605 ? 0.5008 0.5249 0.5723 0.1226  -0.0855 0.0782  584 PHE   A C   
4485 O  O   . PHE   A 605 ? 0.4878 0.5053 0.5551 0.1301  -0.0942 0.0854  584 PHE   A O   
4486 C  CB  . PHE   A 605 ? 0.4408 0.4928 0.5576 0.1229  -0.0799 0.0543  584 PHE   A CB  
4487 C  CG  . PHE   A 605 ? 0.4786 0.5481 0.6107 0.1318  -0.0877 0.0574  584 PHE   A CG  
4488 C  CD1 . PHE   A 605 ? 0.5514 0.6320 0.6754 0.1314  -0.0982 0.0681  584 PHE   A CD1 
4489 C  CD2 . PHE   A 605 ? 0.4768 0.5534 0.6320 0.1400  -0.0853 0.0484  584 PHE   A CD2 
4490 C  CE1 . PHE   A 605 ? 0.5762 0.6741 0.7157 0.1394  -0.1063 0.0716  584 PHE   A CE1 
4491 C  CE2 . PHE   A 605 ? 0.4363 0.5296 0.6067 0.1488  -0.0927 0.0513  584 PHE   A CE2 
4492 C  CZ  . PHE   A 605 ? 0.5215 0.6255 0.6842 0.1487  -0.1032 0.0637  584 PHE   A CZ  
4493 N  N   . PHE   A 606 ? 0.5028 0.5305 0.5646 0.1102  -0.0893 0.0786  585 PHE   A N   
4494 C  CA  . PHE   A 606 ? 0.5200 0.5503 0.5559 0.1069  -0.0944 0.0880  585 PHE   A CA  
4495 C  C   . PHE   A 606 ? 0.5348 0.5555 0.5496 0.0986  -0.0845 0.0892  585 PHE   A C   
4496 O  O   . PHE   A 606 ? 0.5497 0.5649 0.5693 0.0956  -0.0755 0.0813  585 PHE   A O   
4497 C  CB  . PHE   A 606 ? 0.5396 0.5992 0.5734 0.1067  -0.1026 0.0827  585 PHE   A CB  
4498 C  CG  . PHE   A 606 ? 0.4783 0.5522 0.5164 0.1027  -0.0992 0.0665  585 PHE   A CG  
4499 C  CD1 . PHE   A 606 ? 0.4962 0.5674 0.5153 0.0942  -0.0943 0.0603  585 PHE   A CD1 
4500 C  CD2 . PHE   A 606 ? 0.4158 0.5050 0.4789 0.1050  -0.1009 0.0560  585 PHE   A CD2 
4501 C  CE1 . PHE   A 606 ? 0.4587 0.5357 0.4854 0.0845  -0.0907 0.0448  585 PHE   A CE1 
4502 C  CE2 . PHE   A 606 ? 0.3731 0.4724 0.4424 0.0950  -0.0968 0.0417  585 PHE   A CE2 
4503 C  CZ  . PHE   A 606 ? 0.3697 0.4605 0.4213 0.0840  -0.0919 0.0370  585 PHE   A CZ  
4504 N  N   . PRO   A 607 ? 0.5425 0.5631 0.5339 0.0950  -0.0855 0.0988  586 PRO   A N   
4505 C  CA  . PRO   A 607 ? 0.5595 0.5715 0.5332 0.0875  -0.0754 0.1007  586 PRO   A CA  
4506 C  C   . PRO   A 607 ? 0.5487 0.5669 0.5208 0.0847  -0.0695 0.0870  586 PRO   A C   
4507 O  O   . PRO   A 607 ? 0.5212 0.5558 0.4927 0.0840  -0.0746 0.0750  586 PRO   A O   
4508 C  CB  . PRO   A 607 ? 0.5385 0.5634 0.4883 0.0857  -0.0792 0.1089  586 PRO   A CB  
4509 C  CG  . PRO   A 607 ? 0.5884 0.6151 0.5442 0.0920  -0.0898 0.1182  586 PRO   A CG  
4510 C  CD  . PRO   A 607 ? 0.5713 0.6027 0.5517 0.0980  -0.0956 0.1081  586 PRO   A CD  
4511 N  N   . ASN   A 608 ? 0.4912 0.4931 0.4644 0.0797  -0.0588 0.0854  587 ASN   A N   
4512 C  CA  A ASN   A 608 ? 0.5061 0.5072 0.4795 0.0717  -0.0518 0.0695  587 ASN   A CA  
4513 C  CA  B ASN   A 608 ? 0.5062 0.5074 0.4797 0.0717  -0.0518 0.0695  587 ASN   A CA  
4514 C  C   . ASN   A 608 ? 0.4803 0.4914 0.4326 0.0681  -0.0521 0.0645  587 ASN   A C   
4515 O  O   . ASN   A 608 ? 0.5119 0.5204 0.4485 0.0667  -0.0470 0.0715  587 ASN   A O   
4516 C  CB  A ASN   A 608 ? 0.4997 0.4831 0.4793 0.0674  -0.0411 0.0697  587 ASN   A CB  
4517 C  CB  B ASN   A 608 ? 0.5037 0.4872 0.4834 0.0674  -0.0412 0.0695  587 ASN   A CB  
4518 C  CG  A ASN   A 608 ? 0.4711 0.4493 0.4738 0.0702  -0.0401 0.0650  587 ASN   A CG  
4519 C  CG  B ASN   A 608 ? 0.4994 0.4825 0.4774 0.0597  -0.0345 0.0568  587 ASN   A CG  
4520 O  OD1 A ASN   A 608 ? 0.4904 0.4808 0.5054 0.0720  -0.0440 0.0568  587 ASN   A OD1 
4521 O  OD1 B ASN   A 608 ? 0.5028 0.4928 0.4914 0.0572  -0.0358 0.0467  587 ASN   A OD1 
4522 N  ND2 A ASN   A 608 ? 0.4097 0.3720 0.4196 0.0704  -0.0351 0.0692  587 ASN   A ND2 
4523 N  ND2 B ASN   A 608 ? 0.5626 0.5388 0.5289 0.0555  -0.0275 0.0587  587 ASN   A ND2 
4524 N  N   . MET   A 609 ? 0.5013 0.5251 0.4552 0.0666  -0.0581 0.0512  588 MET   A N   
4525 C  CA  . MET   A 609 ? 0.4994 0.5331 0.4362 0.0646  -0.0603 0.0418  588 MET   A CA  
4526 C  C   . MET   A 609 ? 0.4830 0.5053 0.4172 0.0587  -0.0512 0.0335  588 MET   A C   
4527 O  O   . MET   A 609 ? 0.4956 0.5246 0.4153 0.0588  -0.0513 0.0257  588 MET   A O   
4528 C  CB  . MET   A 609 ? 0.4057 0.4540 0.3496 0.0638  -0.0710 0.0283  588 MET   A CB  
4529 C  CG  . MET   A 609 ? 0.4792 0.5451 0.4223 0.0708  -0.0820 0.0351  588 MET   A CG  
4530 S  SD  . MET   A 609 ? 0.5306 0.6173 0.4823 0.0685  -0.0956 0.0170  588 MET   A SD  
4531 C  CE  . MET   A 609 ? 0.4360 0.5174 0.4206 0.0637  -0.0938 0.0149  588 MET   A CE  
4532 N  N   . VAL   A 610 ? 0.4983 0.5060 0.4466 0.0545  -0.0439 0.0340  589 VAL   A N   
4533 C  CA  . VAL   A 610 ? 0.5223 0.5203 0.4698 0.0495  -0.0364 0.0274  589 VAL   A CA  
4534 C  C   . VAL   A 610 ? 0.4524 0.4482 0.3844 0.0508  -0.0291 0.0344  589 VAL   A C   
4535 O  O   . VAL   A 610 ? 0.4669 0.4614 0.3933 0.0491  -0.0249 0.0273  589 VAL   A O   
4536 C  CB  . VAL   A 610 ? 0.4680 0.4563 0.4335 0.0448  -0.0311 0.0275  589 VAL   A CB  
4537 C  CG1 . VAL   A 610 ? 0.4427 0.4235 0.4096 0.0396  -0.0263 0.0207  589 VAL   A CG1 
4538 C  CG2 . VAL   A 610 ? 0.5149 0.5113 0.4969 0.0437  -0.0373 0.0241  589 VAL   A CG2 
4539 N  N   . ASN   A 611 ? 0.4575 0.4533 0.3849 0.0535  -0.0278 0.0491  590 ASN   A N   
4540 C  CA  . ASN   A 611 ? 0.5451 0.5404 0.4605 0.0527  -0.0204 0.0590  590 ASN   A CA  
4541 C  C   . ASN   A 611 ? 0.5135 0.5287 0.4079 0.0563  -0.0236 0.0603  590 ASN   A C   
4542 O  O   . ASN   A 611 ? 0.4993 0.5234 0.3850 0.0592  -0.0270 0.0747  590 ASN   A O   
4543 C  CB  . ASN   A 611 ? 0.5741 0.5581 0.4979 0.0525  -0.0182 0.0751  590 ASN   A CB  
4544 C  CG  . ASN   A 611 ? 0.6200 0.6024 0.5365 0.0487  -0.0101 0.0863  590 ASN   A CG  
4545 O  OD1 . ASN   A 611 ? 0.6378 0.6286 0.5442 0.0466  -0.0046 0.0806  590 ASN   A OD1 
4546 N  ND2 . ASN   A 611 ? 0.7964 0.7682 0.7224 0.0461  -0.0100 0.0988  590 ASN   A ND2 
4547 N  N   . MET   A 612 ? 0.4822 0.5059 0.3690 0.0566  -0.0228 0.0448  591 MET   A N   
4548 C  CA  . MET   A 612 ? 0.4593 0.5063 0.3267 0.0611  -0.0269 0.0389  591 MET   A CA  
4549 C  C   . MET   A 612 ? 0.4857 0.5438 0.3406 0.0613  -0.0181 0.0356  591 MET   A C   
4550 O  O   . MET   A 612 ? 0.4824 0.5285 0.3460 0.0581  -0.0104 0.0336  591 MET   A O   
4551 C  CB  . MET   A 612 ? 0.4592 0.5102 0.3309 0.0629  -0.0366 0.0180  591 MET   A CB  
4552 C  CG  . MET   A 612 ? 0.4345 0.4692 0.3212 0.0595  -0.0345 0.0025  591 MET   A CG  
4553 S  SD  . MET   A 612 ? 0.5454 0.5812 0.4425 0.0593  -0.0473 -0.0204 591 MET   A SD  
4554 C  CE  . MET   A 612 ? 0.4464 0.4787 0.3586 0.0561  -0.0540 -0.0104 591 MET   A CE  
4555 N  N   . ILE   A 613 ? 0.4835 0.5688 0.3177 0.0657  -0.0195 0.0349  592 ILE   A N   
4556 C  CA  . ILE   A 613 ? 0.4723 0.5759 0.2958 0.0667  -0.0114 0.0281  592 ILE   A CA  
4557 C  C   . ILE   A 613 ? 0.5082 0.6157 0.3319 0.0725  -0.0160 -0.0011 592 ILE   A C   
4558 O  O   . ILE   A 613 ? 0.5421 0.6595 0.3611 0.0765  -0.0262 -0.0152 592 ILE   A O   
4559 C  CB  . ILE   A 613 ? 0.5164 0.6444 0.3296 0.0649  -0.0099 0.0379  592 ILE   A CB  
4560 C  CG1 . ILE   A 613 ? 0.5753 0.6930 0.3933 0.0590  -0.0100 0.0646  592 ILE   A CG1 
4561 C  CG2 . ILE   A 613 ? 0.4782 0.6248 0.2872 0.0639  0.0002  0.0343  592 ILE   A CG2 
4562 C  CD1 . ILE   A 613 ? 0.6225 0.7625 0.4294 0.0577  -0.0105 0.0763  592 ILE   A CD1 
4563 N  N   . VAL   A 614 ? 0.4299 0.5281 0.2632 0.0724  -0.0095 -0.0110 593 VAL   A N   
4564 C  CA  . VAL   A 614 ? 0.5061 0.6006 0.3474 0.0773  -0.0144 -0.0383 593 VAL   A CA  
4565 C  C   . VAL   A 614 ? 0.5049 0.6261 0.3353 0.0837  -0.0081 -0.0502 593 VAL   A C   
4566 O  O   . VAL   A 614 ? 0.4734 0.5961 0.3077 0.0824  0.0020  -0.0440 593 VAL   A O   
4567 C  CB  . VAL   A 614 ? 0.4547 0.5175 0.3199 0.0732  -0.0137 -0.0405 593 VAL   A CB  
4568 C  CG1 . VAL   A 614 ? 0.4785 0.5335 0.3553 0.0779  -0.0212 -0.0664 593 VAL   A CG1 
4569 C  CG2 . VAL   A 614 ? 0.3962 0.4384 0.2732 0.0661  -0.0177 -0.0270 593 VAL   A CG2 
4570 N  N   . LEU   A 615 ? 0.4620 0.6025 0.2887 0.0877  -0.0141 -0.0659 594 LEU   A N   
4571 C  CA  . LEU   A 615 ? 0.5123 0.6779 0.3378 0.0924  -0.0094 -0.0780 594 LEU   A CA  
4572 C  C   . LEU   A 615 ? 0.5336 0.6929 0.3719 0.0994  -0.0188 -0.1088 594 LEU   A C   
4573 O  O   . LEU   A 615 ? 0.5179 0.6933 0.3534 0.1028  -0.0260 -0.1231 594 LEU   A O   
4574 C  CB  . LEU   A 615 ? 0.4763 0.6735 0.2866 0.0912  -0.0079 -0.0675 594 LEU   A CB  
4575 C  CG  . LEU   A 615 ? 0.4670 0.6665 0.2695 0.0830  -0.0005 -0.0353 594 LEU   A CG  
4576 C  CD1 . LEU   A 615 ? 0.4910 0.7196 0.2796 0.0824  -0.0013 -0.0256 594 LEU   A CD1 
4577 C  CD2 . LEU   A 615 ? 0.4536 0.6531 0.2618 0.0795  0.0114  -0.0252 594 LEU   A CD2 
4578 N  N   . ASP   A 616 ? 0.5780 0.7127 0.4330 0.1011  -0.0192 -0.1183 595 ASP   A N   
4579 C  CA  . ASP   A 616 ? 0.5319 0.6505 0.4057 0.1057  -0.0299 -0.1439 595 ASP   A CA  
4580 C  C   . ASP   A 616 ? 0.5021 0.6102 0.3778 0.1023  -0.0425 -0.1499 595 ASP   A C   
4581 O  O   . ASP   A 616 ? 0.5703 0.6615 0.4440 0.0965  -0.0446 -0.1368 595 ASP   A O   
4582 C  CB  . ASP   A 616 ? 0.5032 0.6465 0.3800 0.1136  -0.0300 -0.1628 595 ASP   A CB  
4583 C  CG  . ASP   A 616 ? 0.7143 0.8640 0.5965 0.1172  -0.0202 -0.1608 595 ASP   A CG  
4584 O  OD1 . ASP   A 616 ? 0.7465 0.8714 0.6398 0.1152  -0.0175 -0.1538 595 ASP   A OD1 
4585 O  OD2 . ASP   A 616 ? 0.7249 0.9062 0.6008 0.1221  -0.0154 -0.1663 595 ASP   A OD2 
4586 N  N   . LYS   A 617 ? 0.4951 0.6147 0.3755 0.1059  -0.0513 -0.1699 596 LYS   A N   
4587 C  CA  . LYS   A 617 ? 0.6000 0.7101 0.4864 0.1017  -0.0641 -0.1770 596 LYS   A CA  
4588 C  C   . LYS   A 617 ? 0.5734 0.7021 0.4390 0.0981  -0.0639 -0.1598 596 LYS   A C   
4589 O  O   . LYS   A 617 ? 0.5534 0.6750 0.4242 0.0936  -0.0742 -0.1618 596 LYS   A O   
4590 C  CB  . LYS   A 617 ? 0.5895 0.7082 0.4881 0.1066  -0.0736 -0.2037 596 LYS   A CB  
4591 C  CG  . LYS   A 617 ? 0.5843 0.7424 0.4675 0.1146  -0.0682 -0.2113 596 LYS   A CG  
4592 C  CD  . LYS   A 617 ? 0.7019 0.8828 0.5788 0.1158  -0.0770 -0.2235 596 LYS   A CD  
4593 C  CE  . LYS   A 617 ? 0.7974 1.0208 0.6586 0.1238  -0.0713 -0.2302 596 LYS   A CE  
4594 N  NZ  . LYS   A 617 ? 0.8398 1.0915 0.6863 0.1238  -0.0767 -0.2319 596 LYS   A NZ  
4595 N  N   . ASP   A 618 ? 0.5320 0.6839 0.3775 0.0989  -0.0530 -0.1413 597 ASP   A N   
4596 C  CA  . ASP   A 618 ? 0.5635 0.7341 0.3915 0.0959  -0.0531 -0.1224 597 ASP   A CA  
4597 C  C   . ASP   A 618 ? 0.5455 0.6999 0.3695 0.0903  -0.0481 -0.0953 597 ASP   A C   
4598 O  O   . ASP   A 618 ? 0.5762 0.7267 0.3977 0.0893  -0.0370 -0.0821 597 ASP   A O   
4599 C  CB  . ASP   A 618 ? 0.5883 0.7951 0.4001 0.0993  -0.0454 -0.1174 597 ASP   A CB  
4600 C  CG  . ASP   A 618 ? 0.7001 0.9291 0.5130 0.1056  -0.0525 -0.1432 597 ASP   A CG  
4601 O  OD1 . ASP   A 618 ? 0.7475 0.9857 0.5566 0.1050  -0.0617 -0.1469 597 ASP   A OD1 
4602 O  OD2 . ASP   A 618 ? 0.7339 0.9717 0.5531 0.1115  -0.0494 -0.1604 597 ASP   A OD2 
4603 N  N   . LEU   A 619 ? 0.5221 0.6681 0.3478 0.0867  -0.0568 -0.0872 598 LEU   A N   
4604 C  CA  . LEU   A 619 ? 0.5237 0.6535 0.3494 0.0826  -0.0544 -0.0628 598 LEU   A CA  
4605 C  C   . LEU   A 619 ? 0.5309 0.6767 0.3463 0.0810  -0.0547 -0.0402 598 LEU   A C   
4606 O  O   . LEU   A 619 ? 0.5114 0.6707 0.3251 0.0819  -0.0640 -0.0460 598 LEU   A O   
4607 C  CB  . LEU   A 619 ? 0.4851 0.5866 0.3352 0.0772  -0.0623 -0.0679 598 LEU   A CB  
4608 C  CG  . LEU   A 619 ? 0.4589 0.5393 0.3288 0.0759  -0.0639 -0.0886 598 LEU   A CG  
4609 C  CD1 . LEU   A 619 ? 0.4368 0.4944 0.3322 0.0680  -0.0718 -0.0892 598 LEU   A CD1 
4610 C  CD2 . LEU   A 619 ? 0.4273 0.4945 0.3003 0.0756  -0.0511 -0.0806 598 LEU   A CD2 
4611 N  N   . GLY   A 620 ? 0.5132 0.6557 0.3242 0.0781  -0.0449 -0.0146 599 GLY   A N   
4612 C  CA  . GLY   A 620 ? 0.5149 0.6635 0.3217 0.0757  -0.0461 0.0092  599 GLY   A CA  
4613 C  C   . GLY   A 620 ? 0.5214 0.6459 0.3420 0.0739  -0.0494 0.0234  599 GLY   A C   
4614 O  O   . GLY   A 620 ? 0.5552 0.6615 0.3825 0.0711  -0.0414 0.0358  599 GLY   A O   
4615 N  N   . ILE   A 621 ? 0.4363 0.5617 0.2637 0.0755  -0.0610 0.0205  600 ILE   A N   
4616 C  CA  . ILE   A 621 ? 0.5469 0.6523 0.3925 0.0751  -0.0653 0.0273  600 ILE   A CA  
4617 C  C   . ILE   A 621 ? 0.4828 0.5879 0.3322 0.0752  -0.0675 0.0500  600 ILE   A C   
4618 O  O   . ILE   A 621 ? 0.4980 0.6210 0.3400 0.0766  -0.0742 0.0515  600 ILE   A O   
4619 C  CB  . ILE   A 621 ? 0.5292 0.6324 0.3906 0.0735  -0.0755 0.0061  600 ILE   A CB  
4620 C  CG1 . ILE   A 621 ? 0.4345 0.5313 0.2991 0.0710  -0.0732 -0.0173 600 ILE   A CG1 
4621 C  CG2 . ILE   A 621 ? 0.4347 0.5180 0.3216 0.0697  -0.0758 0.0128  600 ILE   A CG2 
4622 C  CD1 . ILE   A 621 ? 0.4778 0.5704 0.3609 0.0674  -0.0838 -0.0373 600 ILE   A CD1 
4623 N  N   . PRO   A 622 ? 0.4787 0.5628 0.3413 0.0737  -0.0625 0.0662  601 PRO   A N   
4624 C  CA  . PRO   A 622 ? 0.5156 0.5947 0.3865 0.0743  -0.0664 0.0845  601 PRO   A CA  
4625 C  C   . PRO   A 622 ? 0.4972 0.5889 0.3750 0.0787  -0.0794 0.0785  601 PRO   A C   
4626 O  O   . PRO   A 622 ? 0.5028 0.5945 0.3931 0.0802  -0.0844 0.0648  601 PRO   A O   
4627 C  CB  . PRO   A 622 ? 0.4907 0.5431 0.3811 0.0728  -0.0606 0.0923  601 PRO   A CB  
4628 C  CG  . PRO   A 622 ? 0.4703 0.5158 0.3554 0.0692  -0.0501 0.0861  601 PRO   A CG  
4629 C  CD  . PRO   A 622 ? 0.4832 0.5452 0.3564 0.0707  -0.0532 0.0660  601 PRO   A CD  
4630 N  N   . LYS   A 623 ? 0.5117 0.6496 0.4971 0.0419  -0.1120 0.1036  602 LYS   A N   
4631 C  CA  . LYS   A 623 ? 0.5391 0.6968 0.5329 0.0441  -0.1267 0.1022  602 LYS   A CA  
4632 C  C   . LYS   A 623 ? 0.5120 0.6558 0.5509 0.0487  -0.1294 0.0988  602 LYS   A C   
4633 O  O   . LYS   A 623 ? 0.5108 0.6436 0.5802 0.0537  -0.1306 0.1164  602 LYS   A O   
4634 C  CB  . LYS   A 623 ? 0.5653 0.7526 0.5488 0.0464  -0.1403 0.1310  602 LYS   A CB  
4635 C  CG  . LYS   A 623 ? 0.5668 0.7824 0.5490 0.0476  -0.1564 0.1280  602 LYS   A CG  
4636 C  CD  . LYS   A 623 ? 0.5783 0.8282 0.5498 0.0491  -0.1705 0.1607  602 LYS   A CD  
4637 C  CE  . LYS   A 623 ? 0.7037 0.9883 0.6659 0.0490  -0.1864 0.1542  602 LYS   A CE  
4638 N  NZ  . LYS   A 623 ? 0.7021 1.0009 0.6271 0.0428  -0.1819 0.1218  602 LYS   A NZ  
4639 N  N   . PRO   A 624 ? 0.5040 0.6499 0.5517 0.0470  -0.1307 0.0760  603 PRO   A N   
4640 C  CA  . PRO   A 624 ? 0.5146 0.6512 0.6048 0.0505  -0.1300 0.0676  603 PRO   A CA  
4641 C  C   . PRO   A 624 ? 0.5444 0.6945 0.6685 0.0588  -0.1454 0.0841  603 PRO   A C   
4642 O  O   . PRO   A 624 ? 0.5145 0.6553 0.6810 0.0647  -0.1451 0.0836  603 PRO   A O   
4643 C  CB  . PRO   A 624 ? 0.5272 0.6684 0.6111 0.0439  -0.1269 0.0407  603 PRO   A CB  
4644 C  CG  . PRO   A 624 ? 0.4923 0.6528 0.5438 0.0407  -0.1361 0.0401  603 PRO   A CG  
4645 C  CD  . PRO   A 624 ? 0.4870 0.6466 0.5090 0.0411  -0.1332 0.0558  603 PRO   A CD  
4646 N  N   . PHE   A 625 ? 0.5482 0.7227 0.6563 0.0596  -0.1597 0.0972  604 PHE   A N   
4647 C  CA  . PHE   A 625 ? 0.5502 0.7418 0.6903 0.0673  -0.1768 0.1133  604 PHE   A CA  
4648 C  C   . PHE   A 625 ? 0.5806 0.7756 0.7531 0.0689  -0.1781 0.0903  604 PHE   A C   
4649 O  O   . PHE   A 625 ? 0.5596 0.7525 0.7787 0.0770  -0.1831 0.0940  604 PHE   A O   
4650 C  CB  . PHE   A 625 ? 0.6088 0.7884 0.7827 0.0750  -0.1811 0.1417  604 PHE   A CB  
4651 C  CG  . PHE   A 625 ? 0.6098 0.7974 0.7561 0.0730  -0.1848 0.1725  604 PHE   A CG  
4652 C  CD1 . PHE   A 625 ? 0.6042 0.8231 0.7402 0.0743  -0.2022 0.1981  604 PHE   A CD1 
4653 C  CD2 . PHE   A 625 ? 0.5940 0.7625 0.7244 0.0690  -0.1710 0.1767  604 PHE   A CD2 
4654 C  CE1 . PHE   A 625 ? 0.6570 0.8907 0.7661 0.0710  -0.2051 0.2282  604 PHE   A CE1 
4655 C  CE2 . PHE   A 625 ? 0.6406 0.8213 0.7460 0.0660  -0.1736 0.2059  604 PHE   A CE2 
4656 C  CZ  . PHE   A 625 ? 0.6797 0.8944 0.7738 0.0667  -0.1903 0.2321  604 PHE   A CZ  
4657 N  N   . GLY   A 626 ? 0.5800 0.7817 0.7306 0.0609  -0.1736 0.0660  605 GLY   A N   
4658 C  CA  . GLY   A 626 ? 0.5624 0.7719 0.7400 0.0597  -0.1736 0.0448  605 GLY   A CA  
4659 C  C   . GLY   A 626 ? 0.6335 0.8719 0.8232 0.0628  -0.1917 0.0491  605 GLY   A C   
4660 O  O   . GLY   A 626 ? 0.6278 0.8822 0.8050 0.0662  -0.2056 0.0699  605 GLY   A O   
4661 N  N   . PRO   A 627 ? 0.6746 0.9242 0.8895 0.0609  -0.1921 0.0299  606 PRO   A N   
4662 C  CA  . PRO   A 627 ? 0.6128 0.8921 0.8416 0.0631  -0.2094 0.0311  606 PRO   A CA  
4663 C  C   . PRO   A 627 ? 0.6295 0.9248 0.8157 0.0557  -0.2178 0.0303  606 PRO   A C   
4664 O  O   . PRO   A 627 ? 0.6014 0.8879 0.7583 0.0457  -0.2085 0.0138  606 PRO   A O   
4665 C  CB  . PRO   A 627 ? 0.5272 0.8143 0.7849 0.0588  -0.2030 0.0063  606 PRO   A CB  
4666 C  CG  . PRO   A 627 ? 0.4712 0.7362 0.7424 0.0589  -0.1849 -0.0023 606 PRO   A CG  
4667 C  CD  . PRO   A 627 ? 0.5478 0.7881 0.7803 0.0560  -0.1767 0.0072  606 PRO   A CD  
4668 N  N   . GLN   A 628 ? 0.6849 1.0060 0.8705 0.0609  -0.2362 0.0477  607 GLN   A N   
4669 C  CA  . GLN   A 628 ? 0.7263 1.0705 0.8724 0.0547  -0.2460 0.0460  607 GLN   A CA  
4670 C  C   . GLN   A 628 ? 0.6739 1.0418 0.8304 0.0489  -0.2552 0.0250  607 GLN   A C   
4671 O  O   . GLN   A 628 ? 0.6110 0.9988 0.8009 0.0547  -0.2676 0.0306  607 GLN   A O   
4672 C  CB  . GLN   A 628 ? 0.7366 1.1035 0.8727 0.0617  -0.2617 0.0778  607 GLN   A CB  
4673 C  CG  . GLN   A 628 ? 0.7988 1.1511 0.9064 0.0620  -0.2531 0.0961  607 GLN   A CG  
4674 C  CD  . GLN   A 628 ? 0.8018 1.1895 0.8762 0.0615  -0.2669 0.1177  607 GLN   A CD  
4675 O  OE1 . GLN   A 628 ? 0.9331 1.3491 1.0098 0.0627  -0.2822 0.1219  607 GLN   A OE1 
4676 N  NE2 . GLN   A 628 ? 0.8886 1.2712 0.9300 0.0588  -0.2582 0.1285  607 GLN   A NE2 
4677 N  N   . VAL   A 629 ? 0.7559 1.1216 0.8874 0.0375  -0.2497 0.0009  608 VAL   A N   
4678 C  CA  . VAL   A 629 ? 0.7510 1.1376 0.8907 0.0294  -0.2584 -0.0206 608 VAL   A CA  
4679 C  C   . VAL   A 629 ? 0.8410 1.2506 0.9431 0.0245  -0.2689 -0.0279 608 VAL   A C   
4680 O  O   . VAL   A 629 ? 0.8233 1.2188 0.8962 0.0185  -0.2599 -0.0409 608 VAL   A O   
4681 C  CB  . VAL   A 629 ? 0.7568 1.1222 0.9079 0.0186  -0.2440 -0.0440 608 VAL   A CB  
4682 C  CG1 . VAL   A 629 ? 0.6983 1.0869 0.8760 0.0117  -0.2534 -0.0598 608 VAL   A CG1 
4683 C  CG2 . VAL   A 629 ? 0.7030 1.0423 0.8749 0.0227  -0.2277 -0.0377 608 VAL   A CG2 
4684 N  N   . GLU   A 630 ? 0.8625 1.3048 0.9662 0.0267  -0.2864 -0.0203 609 GLU   A N   
4685 C  CA  . GLU   A 630 ? 0.9306 1.3871 0.9978 0.0209  -0.2919 -0.0261 609 GLU   A CA  
4686 C  C   . GLU   A 630 ? 0.9407 1.3965 0.9718 0.0254  -0.2875 -0.0087 609 GLU   A C   
4687 O  O   . GLU   A 630 ? 0.9566 1.4099 0.9548 0.0195  -0.2803 -0.0240 609 GLU   A O   
4688 C  CB  . GLU   A 630 ? 0.9855 1.4328 1.0435 0.0079  -0.2859 -0.0603 609 GLU   A CB  
4689 C  CG  . GLU   A 630 ? 1.0649 1.5203 1.1525 0.0006  -0.2925 -0.0750 609 GLU   A CG  
4690 C  CD  . GLU   A 630 ? 1.2048 1.6910 1.2919 0.0023  -0.3089 -0.0666 609 GLU   A CD  
4691 O  OE1 . GLU   A 630 ? 1.1638 1.6638 1.2505 0.0126  -0.3172 -0.0399 609 GLU   A OE1 
4692 O  OE2 . GLU   A 630 ? 1.2562 1.7522 1.3453 -0.0067 -0.3141 -0.0861 609 GLU   A OE2 
4693 N  N   . GLU   A 631 ? 0.8860 1.3435 0.9275 0.0358  -0.2911 0.0239  610 GLU   A N   
4694 C  CA  . GLU   A 631 ? 0.8653 1.3223 0.8776 0.0394  -0.2867 0.0471  610 GLU   A CA  
4695 C  C   . GLU   A 631 ? 0.8276 1.2637 0.8177 0.0358  -0.2701 0.0353  610 GLU   A C   
4696 O  O   . GLU   A 631 ? 0.8098 1.2495 0.7656 0.0343  -0.2639 0.0413  610 GLU   A O   
4697 C  CB  . GLU   A 631 ? 0.9709 1.4559 0.9504 0.0361  -0.2941 0.0505  610 GLU   A CB  
4698 C  CG  . GLU   A 631 ? 1.0201 1.5275 1.0183 0.0413  -0.3113 0.0698  610 GLU   A CG  
4699 C  CD  . GLU   A 631 ? 1.1575 1.6757 1.1759 0.0369  -0.3210 0.0460  610 GLU   A CD  
4700 O  OE1 . GLU   A 631 ? 1.1931 1.7171 1.1925 0.0272  -0.3180 0.0162  610 GLU   A OE1 
4701 O  OE2 . GLU   A 631 ? 1.1614 1.6818 1.2181 0.0433  -0.3311 0.0564  610 GLU   A OE2 
4702 N  N   . GLU   A 632 ? 0.7922 1.2029 0.8026 0.0341  -0.2605 0.0178  611 GLU   A N   
4703 C  CA  . GLU   A 632 ? 0.7824 1.1590 0.7764 0.0303  -0.2412 0.0059  611 GLU   A CA  
4704 C  C   . GLU   A 632 ? 0.7429 1.0812 0.7695 0.0325  -0.2281 0.0084  611 GLU   A C   
4705 O  O   . GLU   A 632 ? 0.6359 0.9717 0.6933 0.0310  -0.2299 -0.0019 611 GLU   A O   
4706 C  CB  . GLU   A 632 ? 0.7907 1.1672 0.7685 0.0205  -0.2383 -0.0300 611 GLU   A CB  
4707 C  CG  . GLU   A 632 ? 0.8932 1.3003 0.8373 0.0171  -0.2453 -0.0397 611 GLU   A CG  
4708 C  CD  . GLU   A 632 ? 0.8528 1.2611 0.7628 0.0193  -0.2358 -0.0289 611 GLU   A CD  
4709 O  OE1 . GLU   A 632 ? 0.7723 1.1631 0.6844 0.0240  -0.2276 -0.0107 611 GLU   A OE1 
4710 O  OE2 . GLU   A 632 ? 0.8403 1.2668 0.7235 0.0158  -0.2352 -0.0393 611 GLU   A OE2 
4711 N  N   . CYS   A 633 ? 0.6115 0.9244 0.6315 0.0354  -0.2147 0.0209  612 CYS   A N   
4712 C  CA  . CYS   A 633 ? 0.6351 0.9152 0.6833 0.0369  -0.2013 0.0201  612 CYS   A CA  
4713 C  C   . CYS   A 633 ? 0.5539 0.8188 0.6064 0.0276  -0.1920 -0.0082 612 CYS   A C   
4714 O  O   . CYS   A 633 ? 0.5207 0.7788 0.5483 0.0209  -0.1866 -0.0236 612 CYS   A O   
4715 C  CB  . CYS   A 633 ? 0.6177 0.8753 0.6539 0.0400  -0.1889 0.0355  612 CYS   A CB  
4716 S  SG  . CYS   A 633 ? 0.5058 0.7265 0.5718 0.0408  -0.1714 0.0304  612 CYS   A SG  
4717 N  N   . CYS   A 634 ? 0.5684 0.8303 0.6555 0.0268  -0.1906 -0.0147 613 CYS   A N   
4718 C  CA  . CYS   A 634 ? 0.5801 0.8322 0.6742 0.0161  -0.1827 -0.0369 613 CYS   A CA  
4719 C  C   . CYS   A 634 ? 0.5050 0.7273 0.5923 0.0128  -0.1647 -0.0395 613 CYS   A C   
4720 O  O   . CYS   A 634 ? 0.5000 0.7119 0.5832 0.0029  -0.1585 -0.0543 613 CYS   A O   
4721 C  CB  . CYS   A 634 ? 0.5972 0.8631 0.7297 0.0149  -0.1863 -0.0425 613 CYS   A CB  
4722 S  SG  . CYS   A 634 ? 0.5757 0.8322 0.7441 0.0222  -0.1751 -0.0352 613 CYS   A SG  
4723 N  N   . LEU   A 635 ? 0.4431 0.6519 0.5316 0.0204  -0.1572 -0.0246 614 LEU   A N   
4724 C  CA  . LEU   A 635 ? 0.4503 0.6336 0.5276 0.0174  -0.1413 -0.0265 614 LEU   A CA  
4725 C  C   . LEU   A 635 ? 0.4910 0.6673 0.5317 0.0149  -0.1398 -0.0290 614 LEU   A C   
4726 O  O   . LEU   A 635 ? 0.4732 0.6329 0.5044 0.0084  -0.1303 -0.0396 614 LEU   A O   
4727 C  CB  . LEU   A 635 ? 0.4721 0.6444 0.5641 0.0260  -0.1348 -0.0117 614 LEU   A CB  
4728 C  CG  . LEU   A 635 ? 0.4707 0.6495 0.6039 0.0297  -0.1339 -0.0143 614 LEU   A CG  
4729 C  CD1 . LEU   A 635 ? 0.4478 0.6174 0.6003 0.0401  -0.1324 0.0006  614 LEU   A CD1 
4730 C  CD2 . LEU   A 635 ? 0.3892 0.5640 0.5319 0.0205  -0.1211 -0.0310 614 LEU   A CD2 
4731 N  N   . GLU   A 636 ? 0.4933 0.6858 0.5149 0.0199  -0.1496 -0.0194 615 GLU   A N   
4732 C  CA  . GLU   A 636 ? 0.4452 0.6394 0.4326 0.0178  -0.1483 -0.0253 615 GLU   A CA  
4733 C  C   . GLU   A 636 ? 0.4721 0.6687 0.4553 0.0093  -0.1515 -0.0509 615 GLU   A C   
4734 O  O   . GLU   A 636 ? 0.4457 0.6269 0.4169 0.0052  -0.1437 -0.0635 615 GLU   A O   
4735 C  CB  . GLU   A 636 ? 0.4697 0.6912 0.4379 0.0235  -0.1592 -0.0095 615 GLU   A CB  
4736 C  CG  . GLU   A 636 ? 0.5089 0.7245 0.4711 0.0297  -0.1537 0.0164  615 GLU   A CG  
4737 C  CD  . GLU   A 636 ? 0.5899 0.8382 0.5310 0.0331  -0.1649 0.0356  615 GLU   A CD  
4738 O  OE1 . GLU   A 636 ? 0.5479 0.8247 0.4695 0.0303  -0.1744 0.0233  615 GLU   A OE1 
4739 O  OE2 . GLU   A 636 ? 0.5777 0.8254 0.5233 0.0379  -0.1648 0.0636  615 GLU   A OE2 
4740 N  N   . MET   A 637 ? 0.4074 0.6233 0.4041 0.0066  -0.1640 -0.0590 616 MET   A N   
4741 C  CA  . MET   A 637 ? 0.5078 0.7259 0.5071 -0.0024 -0.1688 -0.0838 616 MET   A CA  
4742 C  C   . MET   A 637 ? 0.4938 0.6846 0.5114 -0.0106 -0.1581 -0.0917 616 MET   A C   
4743 O  O   . MET   A 637 ? 0.5550 0.7355 0.5716 -0.0175 -0.1576 -0.1090 616 MET   A O   
4744 C  CB  . MET   A 637 ? 0.5389 0.7841 0.5538 -0.0045 -0.1844 -0.0894 616 MET   A CB  
4745 C  CG  . MET   A 637 ? 0.6961 0.9750 0.6921 0.0021  -0.1979 -0.0819 616 MET   A CG  
4746 S  SD  . MET   A 637 ? 0.6892 0.9833 0.6455 0.0019  -0.1994 -0.0972 616 MET   A SD  
4747 C  CE  . MET   A 637 ? 0.6753 0.9638 0.6093 0.0109  -0.1889 -0.0675 616 MET   A CE  
4748 N  N   . HIS   A 638 ? 0.4587 0.6401 0.4956 -0.0102 -0.1500 -0.0796 617 HIS   A N   
4749 C  CA  . HIS   A 638 ? 0.4465 0.6088 0.4990 -0.0190 -0.1397 -0.0838 617 HIS   A CA  
4750 C  C   . HIS   A 638 ? 0.4498 0.5885 0.4846 -0.0187 -0.1285 -0.0832 617 HIS   A C   
4751 O  O   . HIS   A 638 ? 0.4560 0.5805 0.4951 -0.0268 -0.1259 -0.0927 617 HIS   A O   
4752 C  CB  . HIS   A 638 ? 0.4383 0.6047 0.5145 -0.0183 -0.1334 -0.0738 617 HIS   A CB  
4753 C  CG  . HIS   A 638 ? 0.4668 0.6230 0.5578 -0.0286 -0.1229 -0.0758 617 HIS   A CG  
4754 N  ND1 . HIS   A 638 ? 0.4509 0.6162 0.5630 -0.0407 -0.1263 -0.0828 617 HIS   A ND1 
4755 C  CD2 . HIS   A 638 ? 0.4798 0.6210 0.5680 -0.0297 -0.1096 -0.0701 617 HIS   A CD2 
4756 C  CE1 . HIS   A 638 ? 0.4647 0.6226 0.5854 -0.0491 -0.1155 -0.0791 617 HIS   A CE1 
4757 N  NE2 . HIS   A 638 ? 0.4633 0.6072 0.5690 -0.0423 -0.1054 -0.0722 617 HIS   A NE2 
4758 N  N   . VAL   A 639 ? 0.4240 0.5583 0.4421 -0.0096 -0.1224 -0.0709 618 VAL   A N   
4759 C  CA  . VAL   A 639 ? 0.4337 0.5483 0.4350 -0.0087 -0.1118 -0.0703 618 VAL   A CA  
4760 C  C   . VAL   A 639 ? 0.5082 0.6228 0.4937 -0.0104 -0.1166 -0.0868 618 VAL   A C   
4761 O  O   . VAL   A 639 ? 0.4624 0.5592 0.4478 -0.0141 -0.1107 -0.0945 618 VAL   A O   
4762 C  CB  . VAL   A 639 ? 0.3923 0.5058 0.3809 0.0006  -0.1059 -0.0533 618 VAL   A CB  
4763 C  CG1 . VAL   A 639 ? 0.3528 0.4509 0.3220 0.0018  -0.0961 -0.0538 618 VAL   A CG1 
4764 C  CG2 . VAL   A 639 ? 0.3859 0.4956 0.3969 0.0021  -0.0998 -0.0427 618 VAL   A CG2 
4765 N  N   . ARG   A 640 ? 0.4621 0.5993 0.4365 -0.0076 -0.1281 -0.0937 619 ARG   A N   
4766 C  CA  . ARG   A 640 ? 0.4662 0.6090 0.4288 -0.0091 -0.1333 -0.1154 619 ARG   A CA  
4767 C  C   . ARG   A 640 ? 0.4555 0.5846 0.4431 -0.0191 -0.1372 -0.1332 619 ARG   A C   
4768 O  O   . ARG   A 640 ? 0.4768 0.5924 0.4659 -0.0212 -0.1355 -0.1487 619 ARG   A O   
4769 C  CB  . ARG   A 640 ? 0.5042 0.6813 0.4511 -0.0054 -0.1460 -0.1207 619 ARG   A CB  
4770 C  CG  . ARG   A 640 ? 0.5494 0.7441 0.4690 0.0031  -0.1436 -0.1027 619 ARG   A CG  
4771 C  CD  . ARG   A 640 ? 0.6007 0.8351 0.5000 0.0049  -0.1560 -0.1126 619 ARG   A CD  
4772 N  NE  . ARG   A 640 ? 0.6716 0.9294 0.5473 0.0113  -0.1561 -0.0888 619 ARG   A NE  
4773 C  CZ  . ARG   A 640 ? 0.6556 0.9224 0.5060 0.0142  -0.1484 -0.0864 619 ARG   A CZ  
4774 N  NH1 . ARG   A 640 ? 0.6217 0.8749 0.4674 0.0128  -0.1396 -0.1081 619 ARG   A NH1 
4775 N  NH2 . ARG   A 640 ? 0.6446 0.9360 0.4767 0.0182  -0.1499 -0.0602 619 ARG   A NH2 
4776 N  N   . GLY   A 641 ? 0.4773 0.6105 0.4884 -0.0255 -0.1428 -0.1305 620 GLY   A N   
4777 C  CA  . GLY   A 641 ? 0.4655 0.5867 0.5042 -0.0370 -0.1468 -0.1426 620 GLY   A CA  
4778 C  C   . GLY   A 641 ? 0.4495 0.5430 0.4992 -0.0420 -0.1358 -0.1351 620 GLY   A C   
4779 O  O   . GLY   A 641 ? 0.5393 0.6182 0.6092 -0.0503 -0.1392 -0.1453 620 GLY   A O   
4780 N  N   . LEU   A 642 ? 0.4156 0.5024 0.4547 -0.0374 -0.1237 -0.1170 621 LEU   A N   
4781 C  CA  . LEU   A 642 ? 0.4243 0.4896 0.4716 -0.0421 -0.1135 -0.1085 621 LEU   A CA  
4782 C  C   . LEU   A 642 ? 0.5153 0.5648 0.5486 -0.0368 -0.1096 -0.1164 621 LEU   A C   
4783 O  O   . LEU   A 642 ? 0.4614 0.4925 0.5098 -0.0425 -0.1080 -0.1181 621 LEU   A O   
4784 C  CB  . LEU   A 642 ? 0.4737 0.5415 0.5178 -0.0397 -0.1023 -0.0897 621 LEU   A CB  
4785 C  CG  . LEU   A 642 ? 0.4385 0.5234 0.5015 -0.0448 -0.1031 -0.0827 621 LEU   A CG  
4786 C  CD1 . LEU   A 642 ? 0.4266 0.5157 0.4856 -0.0387 -0.0925 -0.0703 621 LEU   A CD1 
4787 C  CD2 . LEU   A 642 ? 0.4291 0.5123 0.5174 -0.0595 -0.1036 -0.0811 621 LEU   A CD2 
4788 N  N   . LEU   A 643 ? 0.5196 0.5785 0.5264 -0.0264 -0.1083 -0.1199 622 LEU   A N   
4789 C  CA  . LEU   A 643 ? 0.5217 0.5704 0.5136 -0.0205 -0.1017 -0.1254 622 LEU   A CA  
4790 C  C   . LEU   A 643 ? 0.4774 0.5332 0.4661 -0.0180 -0.1097 -0.1515 622 LEU   A C   
4791 O  O   . LEU   A 643 ? 0.5194 0.5615 0.5128 -0.0166 -0.1067 -0.1626 622 LEU   A O   
4792 C  CB  . LEU   A 643 ? 0.4642 0.5214 0.4299 -0.0115 -0.0931 -0.1107 622 LEU   A CB  
4793 C  CG  . LEU   A 643 ? 0.4683 0.5181 0.4404 -0.0127 -0.0844 -0.0894 622 LEU   A CG  
4794 C  CD1 . LEU   A 643 ? 0.5251 0.5813 0.4775 -0.0043 -0.0777 -0.0755 622 LEU   A CD1 
4795 C  CD2 . LEU   A 643 ? 0.4665 0.4957 0.4523 -0.0184 -0.0770 -0.0862 622 LEU   A CD2 
4796 N  N   . GLU   A 644 ? 0.5015 0.5807 0.4842 -0.0173 -0.1201 -0.1635 623 GLU   A N   
4797 C  CA  . GLU   A 644 ? 0.5201 0.6146 0.4959 -0.0140 -0.1271 -0.1918 623 GLU   A CA  
4798 C  C   . GLU   A 644 ? 0.5812 0.6566 0.5900 -0.0202 -0.1337 -0.2149 623 GLU   A C   
4799 O  O   . GLU   A 644 ? 0.6067 0.6824 0.6163 -0.0158 -0.1340 -0.2383 623 GLU   A O   
4800 C  CB  . GLU   A 644 ? 0.5064 0.6353 0.4688 -0.0128 -0.1380 -0.1985 623 GLU   A CB  
4801 C  CG  . GLU   A 644 ? 0.5812 0.7310 0.5132 -0.0057 -0.1334 -0.1753 623 GLU   A CG  
4802 C  CD  . GLU   A 644 ? 0.6511 0.8409 0.5660 -0.0036 -0.1451 -0.1815 623 GLU   A CD  
4803 O  OE1 . GLU   A 644 ? 0.6395 0.8389 0.5704 -0.0088 -0.1573 -0.1964 623 GLU   A OE1 
4804 O  OE2 . GLU   A 644 ? 0.6919 0.9060 0.5782 0.0025  -0.1425 -0.1701 623 GLU   A OE2 
4805 N  N   . PRO   A 645 ? 0.5215 0.5816 0.5613 -0.0305 -0.1395 -0.2096 624 PRO   A N   
4806 C  CA  . PRO   A 645 ? 0.5257 0.5647 0.6032 -0.0374 -0.1469 -0.2277 624 PRO   A CA  
4807 C  C   . PRO   A 645 ? 0.5408 0.5548 0.6269 -0.0341 -0.1391 -0.2266 624 PRO   A C   
4808 O  O   . PRO   A 645 ? 0.5643 0.5626 0.6815 -0.0362 -0.1460 -0.2466 624 PRO   A O   
4809 C  CB  . PRO   A 645 ? 0.5424 0.5720 0.6480 -0.0504 -0.1512 -0.2102 624 PRO   A CB  
4810 C  CG  . PRO   A 645 ? 0.5211 0.5770 0.6053 -0.0488 -0.1516 -0.1992 624 PRO   A CG  
4811 C  CD  . PRO   A 645 ? 0.4833 0.5483 0.5293 -0.0368 -0.1406 -0.1885 624 PRO   A CD  
4812 N  N   . LEU   A 646 ? 0.5364 0.5467 0.5992 -0.0288 -0.1258 -0.2048 625 LEU   A N   
4813 C  CA  . LEU   A 646 ? 0.4937 0.4836 0.5627 -0.0252 -0.1180 -0.2017 625 LEU   A CA  
4814 C  C   . LEU   A 646 ? 0.4936 0.4967 0.5405 -0.0132 -0.1133 -0.2220 625 LEU   A C   
4815 O  O   . LEU   A 646 ? 0.6475 0.6382 0.6945 -0.0084 -0.1052 -0.2187 625 LEU   A O   
4816 C  CB  . LEU   A 646 ? 0.5810 0.5626 0.6387 -0.0268 -0.1060 -0.1689 625 LEU   A CB  
4817 C  CG  . LEU   A 646 ? 0.5627 0.5371 0.6417 -0.0392 -0.1082 -0.1480 625 LEU   A CG  
4818 C  CD1 . LEU   A 646 ? 0.5569 0.5337 0.6190 -0.0391 -0.0959 -0.1216 625 LEU   A CD1 
4819 C  CD2 . LEU   A 646 ? 0.5928 0.5442 0.7117 -0.0479 -0.1150 -0.1484 625 LEU   A CD2 
4820 N  N   . GLY   A 647 ? 0.5126 0.5447 0.5407 -0.0088 -0.1183 -0.2427 626 GLY   A N   
4821 C  CA  . GLY   A 647 ? 0.5656 0.6202 0.5686 0.0015  -0.1128 -0.2604 626 GLY   A CA  
4822 C  C   . GLY   A 647 ? 0.5577 0.6289 0.5212 0.0068  -0.1008 -0.2360 626 GLY   A C   
4823 O  O   . GLY   A 647 ? 0.6122 0.7036 0.5542 0.0142  -0.0943 -0.2457 626 GLY   A O   
4824 N  N   . LEU   A 648 ? 0.5756 0.6404 0.5320 0.0029  -0.0979 -0.2054 627 LEU   A N   
4825 C  CA  . LEU   A 648 ? 0.5748 0.6529 0.5006 0.0074  -0.0884 -0.1813 627 LEU   A CA  
4826 C  C   . LEU   A 648 ? 0.6127 0.7258 0.5158 0.0090  -0.0951 -0.1811 627 LEU   A C   
4827 O  O   . LEU   A 648 ? 0.6186 0.7379 0.5318 0.0046  -0.1060 -0.1856 627 LEU   A O   
4828 C  CB  . LEU   A 648 ? 0.5092 0.5655 0.4433 0.0032  -0.0825 -0.1519 627 LEU   A CB  
4829 C  CG  . LEU   A 648 ? 0.4891 0.5166 0.4414 0.0010  -0.0752 -0.1461 627 LEU   A CG  
4830 C  CD1 . LEU   A 648 ? 0.5382 0.5517 0.5032 -0.0058 -0.0728 -0.1234 627 LEU   A CD1 
4831 C  CD2 . LEU   A 648 ? 0.4467 0.4762 0.3810 0.0080  -0.0636 -0.1416 627 LEU   A CD2 
4832 N  N   . GLU   A 649 ? 0.5979 0.7366 0.4716 0.0147  -0.0893 -0.1743 628 GLU   A N   
4833 C  CA  . GLU   A 649 ? 0.5968 0.7743 0.4467 0.0162  -0.0960 -0.1694 628 GLU   A CA  
4834 C  C   . GLU   A 649 ? 0.5331 0.7093 0.3732 0.0172  -0.0916 -0.1319 628 GLU   A C   
4835 O  O   . GLU   A 649 ? 0.5462 0.7135 0.3789 0.0195  -0.0803 -0.1153 628 GLU   A O   
4836 C  CB  . GLU   A 649 ? 0.6161 0.8317 0.4413 0.0207  -0.0939 -0.1883 628 GLU   A CB  
4837 C  CG  . GLU   A 649 ? 0.7136 0.9274 0.5574 0.0208  -0.0966 -0.2268 628 GLU   A CG  
4838 C  CD  . GLU   A 649 ? 0.9244 1.1747 0.7540 0.0243  -0.0908 -0.2395 628 GLU   A CD  
4839 O  OE1 . GLU   A 649 ? 0.9618 1.2428 0.7632 0.0256  -0.0860 -0.2194 628 GLU   A OE1 
4840 O  OE2 . GLU   A 649 ? 0.9512 1.2012 0.8014 0.0255  -0.0915 -0.2690 628 GLU   A OE2 
4841 N  N   . CYS   A 650 ? 0.5260 0.7112 0.3701 0.0154  -0.1013 -0.1199 629 CYS   A N   
4842 C  CA  . CYS   A 650 ? 0.5225 0.7014 0.3693 0.0166  -0.0995 -0.0871 629 CYS   A CA  
4843 C  C   . CYS   A 650 ? 0.5425 0.7591 0.3663 0.0197  -0.1048 -0.0690 629 CYS   A C   
4844 O  O   . CYS   A 650 ? 0.5310 0.7788 0.3460 0.0191  -0.1167 -0.0775 629 CYS   A O   
4845 C  CB  . CYS   A 650 ? 0.5559 0.7201 0.4287 0.0131  -0.1067 -0.0844 629 CYS   A CB  
4846 S  SG  . CYS   A 650 ? 0.6227 0.7484 0.5238 0.0069  -0.1012 -0.0983 629 CYS   A SG  
4847 N  N   . THR   A 651 ? 0.5584 0.7741 0.3742 0.0222  -0.0968 -0.0428 630 THR   A N   
4848 C  CA  . THR   A 651 ? 0.5631 0.8097 0.3646 0.0240  -0.1024 -0.0150 630 THR   A CA  
4849 C  C   . THR   A 651 ? 0.5203 0.7425 0.3454 0.0257  -0.1015 0.0144  630 THR   A C   
4850 O  O   . THR   A 651 ? 0.5506 0.7432 0.3871 0.0259  -0.0901 0.0199  630 THR   A O   
4851 C  CB  . THR   A 651 ? 0.5825 0.8557 0.3563 0.0244  -0.0945 -0.0083 630 THR   A CB  
4852 O  OG1 . THR   A 651 ? 0.6358 0.9340 0.3914 0.0238  -0.0946 -0.0417 630 THR   A OG1 
4853 C  CG2 . THR   A 651 ? 0.5083 0.8177 0.2689 0.0245  -0.1020 0.0255  630 THR   A CG2 
4854 N  N   . PHE   A 652 ? 0.4927 0.7282 0.3284 0.0273  -0.1141 0.0310  631 PHE   A N   
4855 C  CA  . PHE   A 652 ? 0.5192 0.7331 0.3847 0.0301  -0.1151 0.0546  631 PHE   A CA  
4856 C  C   . PHE   A 652 ? 0.4880 0.7170 0.3491 0.0320  -0.1166 0.0902  631 PHE   A C   
4857 O  O   . PHE   A 652 ? 0.6034 0.8698 0.4484 0.0319  -0.1272 0.1054  631 PHE   A O   
4858 C  CB  . PHE   A 652 ? 0.4817 0.6997 0.3689 0.0314  -0.1284 0.0519  631 PHE   A CB  
4859 C  CG  . PHE   A 652 ? 0.4715 0.6716 0.3701 0.0280  -0.1262 0.0218  631 PHE   A CG  
4860 C  CD1 . PHE   A 652 ? 0.4493 0.6171 0.3724 0.0272  -0.1170 0.0174  631 PHE   A CD1 
4861 C  CD2 . PHE   A 652 ? 0.4849 0.7032 0.3714 0.0245  -0.1336 -0.0018 631 PHE   A CD2 
4862 C  CE1 . PHE   A 652 ? 0.4368 0.5919 0.3709 0.0222  -0.1152 -0.0056 631 PHE   A CE1 
4863 C  CE2 . PHE   A 652 ? 0.4958 0.6967 0.3972 0.0199  -0.1324 -0.0261 631 PHE   A CE2 
4864 C  CZ  . PHE   A 652 ? 0.4423 0.6123 0.3669 0.0183  -0.1232 -0.0258 631 PHE   A CZ  
4865 N  N   . ILE   A 653 ? 0.5853 0.7879 0.4617 0.0327  -0.1064 0.1042  632 ILE   A N   
4866 C  CA  . ILE   A 653 ? 0.5802 0.7926 0.4567 0.0328  -0.1062 0.1389  632 ILE   A CA  
4867 C  C   . ILE   A 653 ? 0.6170 0.8136 0.5347 0.0371  -0.1147 0.1630  632 ILE   A C   
4868 O  O   . ILE   A 653 ? 0.6214 0.7861 0.5692 0.0394  -0.1104 0.1512  632 ILE   A O   
4869 C  CB  . ILE   A 653 ? 0.5445 0.7402 0.4136 0.0302  -0.0898 0.1381  632 ILE   A CB  
4870 C  CG1 . ILE   A 653 ? 0.5704 0.7754 0.4083 0.0277  -0.0812 0.1071  632 ILE   A CG1 
4871 C  CG2 . ILE   A 653 ? 0.5440 0.7583 0.4089 0.0282  -0.0901 0.1749  632 ILE   A CG2 
4872 C  CD1 . ILE   A 653 ? 0.5601 0.8121 0.3648 0.0262  -0.0880 0.1039  632 ILE   A CD1 
4873 N  N   . ASP   A 654 ? 0.6886 0.9101 0.6095 0.0380  -0.1270 0.1965  633 ASP   A N   
4874 C  CA  . ASP   A 654 ? 0.7367 0.9458 0.7022 0.0430  -0.1378 0.2225  633 ASP   A CA  
4875 C  C   . ASP   A 654 ? 0.8101 1.0024 0.7948 0.0416  -0.1317 0.2501  633 ASP   A C   
4876 O  O   . ASP   A 654 ? 0.8248 1.0419 0.7922 0.0373  -0.1336 0.2797  633 ASP   A O   
4877 C  CB  . ASP   A 654 ? 0.7274 0.9742 0.6902 0.0446  -0.1571 0.2465  633 ASP   A CB  
4878 C  CG  . ASP   A 654 ? 0.8792 1.1133 0.8940 0.0513  -0.1707 0.2716  633 ASP   A CG  
4879 O  OD1 . ASP   A 654 ? 0.9347 1.1320 0.9884 0.0545  -0.1646 0.2705  633 ASP   A OD1 
4880 O  OD2 . ASP   A 654 ? 0.9428 1.1989 0.9611 0.0525  -0.1837 0.2838  633 ASP   A OD2 
4881 N  N   . ASP   A 655 ? 0.9156 1.0691 0.9369 0.0444  -0.1244 0.2400  634 ASP   A N   
4882 C  CA  . ASP   A 655 ? 0.9386 1.0721 0.9849 0.0428  -0.1186 0.2614  634 ASP   A CA  
4883 C  C   . ASP   A 655 ? 1.0078 1.1204 1.1151 0.0492  -0.1293 0.2779  634 ASP   A C   
4884 O  O   . ASP   A 655 ? 1.0521 1.1380 1.1929 0.0492  -0.1234 0.2817  634 ASP   A O   
4885 C  CB  . ASP   A 655 ? 0.9650 1.0731 1.0038 0.0399  -0.0999 0.2335  634 ASP   A CB  
4886 C  CG  . ASP   A 655 ? 1.0083 1.0943 1.0644 0.0436  -0.0955 0.1975  634 ASP   A CG  
4887 O  OD1 . ASP   A 655 ? 1.1536 1.2225 1.2556 0.0488  -0.1005 0.1973  634 ASP   A OD1 
4888 O  OD2 . ASP   A 655 ? 0.8869 0.9745 0.9133 0.0411  -0.0874 0.1696  634 ASP   A OD2 
4889 N  N   . ILE   A 656 ? 0.9870 1.1124 1.1130 0.0550  -0.1456 0.2866  635 ILE   A N   
4890 C  CA  . ILE   A 656 ? 1.0508 1.1565 1.2409 0.0630  -0.1565 0.2964  635 ILE   A CA  
4891 C  C   . ILE   A 656 ? 1.0585 1.1843 1.2578 0.0636  -0.1710 0.3203  635 ILE   A C   
4892 O  O   . ILE   A 656 ? 1.1332 1.2435 1.3822 0.0669  -0.1774 0.3311  635 ILE   A O   
4893 C  CB  . ILE   A 656 ? 1.0246 1.1137 1.2363 0.0688  -0.1520 0.2547  635 ILE   A CB  
4894 C  CG1 . ILE   A 656 ? 0.9253 1.0399 1.1081 0.0696  -0.1584 0.2392  635 ILE   A CG1 
4895 C  CG2 . ILE   A 656 ? 0.8944 0.9621 1.0925 0.0645  -0.1318 0.2224  635 ILE   A CG2 
4896 C  CD1 . ILE   A 656 ? 0.7457 0.8500 0.9468 0.0732  -0.1535 0.2006  635 ILE   A CD1 
4897 N  N   . SER   A 657 ? 1.0067 1.1681 1.1590 0.0597  -0.1756 0.3258  636 SER   A N   
4898 C  CA  . SER   A 657 ? 1.0533 1.2371 1.2116 0.0599  -0.1892 0.3465  636 SER   A CA  
4899 C  C   . SER   A 657 ? 1.0896 1.2704 1.2707 0.0541  -0.1902 0.3810  636 SER   A C   
4900 O  O   . SER   A 657 ? 1.0209 1.2048 1.2349 0.0565  -0.2024 0.3998  636 SER   A O   
4901 C  CB  . SER   A 657 ? 0.9774 1.2028 1.0787 0.0553  -0.1920 0.3424  636 SER   A CB  
4902 O  OG  . SER   A 657 ? 0.9026 1.1361 0.9997 0.0611  -0.1991 0.3165  636 SER   A OG  
4903 N  N   . ALA   A 658 ? 1.1223 1.2993 1.2888 0.0460  -0.1781 0.3904  637 ALA   A N   
4904 C  CA  . ALA   A 658 ? 1.0959 1.2716 1.2890 0.0389  -0.1791 0.4234  637 ALA   A CA  
4905 C  C   . ALA   A 658 ? 1.1396 1.2777 1.4025 0.0440  -0.1837 0.4257  637 ALA   A C   
4906 O  O   . ALA   A 658 ? 1.1184 1.2558 1.4157 0.0392  -0.1894 0.4542  637 ALA   A O   
4907 C  CB  . ALA   A 658 ? 0.8715 1.0525 1.0359 0.0291  -0.1643 0.4288  637 ALA   A CB  
4908 N  N   . TYR   A 659 ? 1.2232 1.3330 1.5100 0.0532  -0.1813 0.3950  638 TYR   A N   
4909 C  CA  . TYR   A 659 ? 1.1928 1.2696 1.5473 0.0587  -0.1846 0.3880  638 TYR   A CA  
4910 C  C   . TYR   A 659 ? 1.2154 1.2932 1.6036 0.0686  -0.1983 0.3815  638 TYR   A C   
4911 O  O   . TYR   A 659 ? 1.1775 1.2343 1.6256 0.0725  -0.2034 0.3799  638 TYR   A O   
4912 C  CB  . TYR   A 659 ? 1.1976 1.2457 1.5631 0.0622  -0.1718 0.3547  638 TYR   A CB  
4913 C  CG  . TYR   A 659 ? 1.2360 1.2817 1.5702 0.0532  -0.1579 0.3589  638 TYR   A CG  
4914 C  CD1 . TYR   A 659 ? 1.2817 1.3461 1.5541 0.0504  -0.1501 0.3524  638 TYR   A CD1 
4915 C  CD2 . TYR   A 659 ? 1.2579 1.2847 1.6262 0.0473  -0.1529 0.3682  638 TYR   A CD2 
4916 C  CE1 . TYR   A 659 ? 1.2971 1.3609 1.5416 0.0425  -0.1368 0.3551  638 TYR   A CE1 
4917 C  CE2 . TYR   A 659 ? 1.3265 1.3532 1.6673 0.0390  -0.1401 0.3716  638 TYR   A CE2 
4918 C  CZ  . TYR   A 659 ? 1.3355 1.3805 1.6140 0.0369  -0.1316 0.3652  638 TYR   A CZ  
4919 O  OH  . TYR   A 659 ? 1.3157 1.3619 1.5679 0.0290  -0.1184 0.3673  638 TYR   A OH  
4920 N  N   . HIS   A 660 ? 1.0721 1.1754 1.4251 0.0723  -0.2043 0.3756  639 HIS   A N   
4921 C  CA  . HIS   A 660 ? 0.9695 1.0824 1.3458 0.0808  -0.2182 0.3721  639 HIS   A CA  
4922 C  C   . HIS   A 660 ? 0.9744 1.0689 1.3843 0.0914  -0.2162 0.3339  639 HIS   A C   
4923 O  O   . HIS   A 660 ? 0.8076 0.9096 1.2425 0.0991  -0.2266 0.3271  639 HIS   A O   
4924 C  CB  . HIS   A 660 ? 0.9390 1.0495 1.3626 0.0802  -0.2304 0.4020  639 HIS   A CB  
4925 C  CG  . HIS   A 660 ? 1.0313 1.1621 1.4326 0.0686  -0.2323 0.4418  639 HIS   A CG  
4926 N  ND1 . HIS   A 660 ? 0.9704 1.1405 1.3193 0.0636  -0.2366 0.4579  639 HIS   A ND1 
4927 C  CD2 . HIS   A 660 ? 1.0138 1.1350 1.4405 0.0601  -0.2305 0.4674  639 HIS   A CD2 
4928 C  CE1 . HIS   A 660 ? 0.9957 1.1814 1.3377 0.0527  -0.2364 0.4920  639 HIS   A CE1 
4929 N  NE2 . HIS   A 660 ? 1.0288 1.1851 1.4182 0.0502  -0.2331 0.4998  639 HIS   A NE2 
4930 N  N   . LYS   A 661 ? 1.0594 1.1334 1.4718 0.0917  -0.2030 0.3082  640 LYS   A N   
4931 C  CA  . LYS   A 661 ? 1.0473 1.1095 1.4920 0.1005  -0.1994 0.2696  640 LYS   A CA  
4932 C  C   . LYS   A 661 ? 1.0852 1.1327 1.5157 0.0980  -0.1837 0.2463  640 LYS   A C   
4933 O  O   . LYS   A 661 ? 1.0936 1.1324 1.5031 0.0906  -0.1760 0.2605  640 LYS   A O   
4934 C  CB  . LYS   A 661 ? 1.0157 1.0589 1.5294 0.1062  -0.2038 0.2626  640 LYS   A CB  
4935 C  CG  . LYS   A 661 ? 1.0296 1.0470 1.5752 0.1006  -0.1988 0.2729  640 LYS   A CG  
4936 C  CD  . LYS   A 661 ? 0.9935 0.9953 1.6104 0.1058  -0.2052 0.2633  640 LYS   A CD  
4937 C  CE  . LYS   A 661 ? 1.0523 1.0318 1.7061 0.0986  -0.2030 0.2755  640 LYS   A CE  
4938 N  NZ  . LYS   A 661 ? 0.9613 0.9490 1.6018 0.0900  -0.2110 0.3236  640 LYS   A NZ  
4939 N  N   . PHE   A 662 ? 1.0191 1.0667 1.4628 0.1039  -0.1788 0.2099  641 PHE   A N   
4940 C  CA  . PHE   A 662 ? 0.9692 1.0068 1.3994 0.1013  -0.1631 0.1826  641 PHE   A CA  
4941 C  C   . PHE   A 662 ? 0.9955 1.0200 1.4816 0.1075  -0.1570 0.1482  641 PHE   A C   
4942 O  O   . PHE   A 662 ? 1.0298 1.0670 1.5394 0.1134  -0.1603 0.1263  641 PHE   A O   
4943 C  CB  . PHE   A 662 ? 0.8875 0.9441 1.2564 0.0944  -0.1545 0.1613  641 PHE   A CB  
4944 C  CG  . PHE   A 662 ? 0.8251 0.8722 1.1672 0.0870  -0.1341 0.1298  641 PHE   A CG  
4945 C  CD1 . PHE   A 662 ? 0.7284 0.7645 1.0362 0.0792  -0.1234 0.1382  641 PHE   A CD1 
4946 C  CD2 . PHE   A 662 ? 0.6232 0.6763 0.9748 0.0873  -0.1259 0.0933  641 PHE   A CD2 
4947 C  CE1 . PHE   A 662 ? 0.7652 0.7940 1.0503 0.0728  -0.1062 0.1114  641 PHE   A CE1 
4948 C  CE2 . PHE   A 662 ? 0.5899 0.6379 0.9171 0.0797  -0.1084 0.0683  641 PHE   A CE2 
4949 C  CZ  . PHE   A 662 ? 0.6612 0.6959 0.9557 0.0728  -0.0991 0.0776  641 PHE   A CZ  
4950 N  N   . LEU   A 663 ? 1.0142 1.0167 1.5176 0.1043  -0.1466 0.1406  642 LEU   A N   
4951 C  CA  . LEU   A 663 ? 1.0154 1.0092 1.5629 0.1068  -0.1376 0.1026  642 LEU   A CA  
4952 C  C   . LEU   A 663 ? 0.9557 0.9496 1.4807 0.1025  -0.1203 0.0733  642 LEU   A C   
4953 O  O   . LEU   A 663 ? 0.9459 0.9318 1.5028 0.1024  -0.1115 0.0464  642 LEU   A O   
4954 C  CB  . LEU   A 663 ? 1.0883 1.0605 1.6795 0.1042  -0.1400 0.1117  642 LEU   A CB  
4955 C  CG  . LEU   A 663 ? 1.0796 1.0505 1.6968 0.1058  -0.1562 0.1423  642 LEU   A CG  
4956 C  CD1 . LEU   A 663 ? 1.0835 1.0542 1.6657 0.0991  -0.1618 0.1888  642 LEU   A CD1 
4957 C  CD2 . LEU   A 663 ? 1.0528 1.0078 1.7347 0.1059  -0.1586 0.1305  642 LEU   A CD2 
4958 N  N   . GLY   A 664 ? 0.9760 0.9805 1.4324 0.0933  -0.1120 0.0744  643 GLY   A N   
4959 C  CA  . GLY   A 664 ? 0.8707 0.8756 1.2900 0.0841  -0.0938 0.0503  643 GLY   A CA  
4960 C  C   . GLY   A 664 ? 1.0124 1.0016 1.4004 0.0765  -0.0869 0.0688  643 GLY   A C   
4961 O  O   . GLY   A 664 ? 1.0312 1.0214 1.3836 0.0687  -0.0728 0.0527  643 GLY   A O   
4962 N  N   . GLU   A 665 ? 1.2327 1.2101 1.6340 0.0781  -0.0966 0.1037  644 GLU   A N   
4963 C  CA  . GLU   A 665 ? 1.3386 1.3038 1.7167 0.0706  -0.0899 0.1224  644 GLU   A CA  
4964 C  C   . GLU   A 665 ? 1.3146 1.2926 1.6360 0.0654  -0.0927 0.1506  644 GLU   A C   
4965 O  O   . GLU   A 665 ? 1.2609 1.2511 1.5818 0.0690  -0.1063 0.1730  644 GLU   A O   
4966 C  CB  . GLU   A 665 ? 1.3221 1.2675 1.7578 0.0737  -0.0978 0.1431  644 GLU   A CB  
4967 C  CG  . GLU   A 665 ? 1.3912 1.3232 1.8157 0.0652  -0.0878 0.1523  644 GLU   A CG  
4968 C  CD  . GLU   A 665 ? 1.3754 1.2884 1.8622 0.0652  -0.0914 0.1553  644 GLU   A CD  
4969 O  OE1 . GLU   A 665 ? 1.3888 1.3008 1.9220 0.0699  -0.0968 0.1358  644 GLU   A OE1 
4970 O  OE2 . GLU   A 665 ? 1.3490 1.2540 1.8309 0.0568  -0.0869 0.1722  644 GLU   A OE2 
4971 N  N   . VAL   A 666 ? 1.2370 1.2155 1.5122 0.0573  -0.0799 0.1474  645 VAL   A N   
4972 C  CA  . VAL   A 666 ? 1.2238 1.2147 1.4516 0.0518  -0.0804 0.1734  645 VAL   A CA  
4973 C  C   . VAL   A 666 ? 1.2339 1.2138 1.4787 0.0479  -0.0795 0.2007  645 VAL   A C   
4974 O  O   . VAL   A 666 ? 1.2112 1.1740 1.4755 0.0455  -0.0701 0.1878  645 VAL   A O   
4975 C  CB  . VAL   A 666 ? 1.1859 1.1848 1.3585 0.0458  -0.0674 0.1522  645 VAL   A CB  
4976 C  CG1 . VAL   A 666 ? 1.0667 1.0874 1.1917 0.0426  -0.0709 0.1714  645 VAL   A CG1 
4977 C  CG2 . VAL   A 666 ? 1.1806 1.1824 1.3516 0.0475  -0.0645 0.1191  645 VAL   A CG2 
4978 N  N   . HIS   A 667 ? 1.1787 1.1713 1.4175 0.0465  -0.0897 0.2391  646 HIS   A N   
4979 C  CA  . HIS   A 667 ? 1.1133 1.0997 1.3680 0.0410  -0.0897 0.2709  646 HIS   A CA  
4980 C  C   . HIS   A 667 ? 1.0626 1.0695 1.2605 0.0322  -0.0804 0.2841  646 HIS   A C   
4981 O  O   . HIS   A 667 ? 1.0987 1.1046 1.3040 0.0257  -0.0776 0.3093  646 HIS   A O   
4982 C  CB  . HIS   A 667 ? 1.1663 1.1569 1.4581 0.0420  -0.1052 0.3022  646 HIS   A CB  
4983 C  CG  . HIS   A 667 ? 1.2151 1.1879 1.5659 0.0503  -0.1135 0.2855  646 HIS   A CG  
4984 N  ND1 . HIS   A 667 ? 1.2776 1.2612 1.6377 0.0575  -0.1259 0.2852  646 HIS   A ND1 
4985 C  CD2 . HIS   A 667 ? 1.1734 1.1221 1.5771 0.0521  -0.1105 0.2651  646 HIS   A CD2 
4986 C  CE1 . HIS   A 667 ? 1.2579 1.2244 1.6742 0.0637  -0.1296 0.2658  646 HIS   A CE1 
4987 N  NE2 . HIS   A 667 ? 1.2179 1.1642 1.6611 0.0604  -0.1204 0.2521  646 HIS   A NE2 
4988 N  N   . CYS   A 668 ? 1.0829 1.1094 1.2282 0.0318  -0.0755 0.2660  647 CYS   A N   
4989 C  CA  . CYS   A 668 ? 0.9317 0.9807 1.0244 0.0250  -0.0661 0.2703  647 CYS   A CA  
4990 C  C   . CYS   A 668 ? 0.9408 0.9790 1.0098 0.0236  -0.0502 0.2327  647 CYS   A C   
4991 O  O   . CYS   A 668 ? 1.0290 1.0544 1.1035 0.0275  -0.0484 0.2024  647 CYS   A O   
4992 C  CB  . CYS   A 668 ? 0.7446 0.8286 0.7968 0.0254  -0.0741 0.2775  647 CYS   A CB  
4993 S  SG  . CYS   A 668 ? 0.9795 1.0889 1.0467 0.0242  -0.0919 0.3269  647 CYS   A SG  
4994 N  N   . GLY   A 669 ? 0.8779 0.9247 0.9213 0.0174  -0.0391 0.2367  648 GLY   A N   
4995 C  CA  . GLY   A 669 ? 0.8293 0.8684 0.8510 0.0161  -0.0251 0.2055  648 GLY   A CA  
4996 C  C   . GLY   A 669 ? 0.7009 0.7678 0.6743 0.0129  -0.0185 0.2037  648 GLY   A C   
4997 O  O   . GLY   A 669 ? 0.6602 0.7544 0.6174 0.0095  -0.0214 0.2294  648 GLY   A O   
4998 N  N   . THR   A 670 ? 0.7183 0.7804 0.6710 0.0138  -0.0099 0.1723  649 THR   A N   
4999 C  CA  . THR   A 670 ? 0.6167 0.7011 0.5311 0.0119  -0.0019 0.1629  649 THR   A CA  
5000 C  C   . THR   A 670 ? 0.6178 0.6841 0.5326 0.0114  0.0099  0.1386  649 THR   A C   
5001 O  O   . THR   A 670 ? 0.6047 0.6466 0.5393 0.0129  0.0103  0.1229  649 THR   A O   
5002 C  CB  . THR   A 670 ? 0.5631 0.6680 0.4489 0.0150  -0.0082 0.1476  649 THR   A CB  
5003 O  OG1 . THR   A 670 ? 0.6451 0.7283 0.5398 0.0183  -0.0103 0.1213  649 THR   A OG1 
5004 C  CG2 . THR   A 670 ? 0.5791 0.7059 0.4642 0.0154  -0.0213 0.1723  649 THR   A CG2 
5005 N  N   . ASN   A 671 ? 0.5835 0.6659 0.4771 0.0092  0.0193  0.1361  650 ASN   A N   
5006 C  CA  . ASN   A 671 ? 0.5708 0.6403 0.4635 0.0091  0.0296  0.1146  650 ASN   A CA  
5007 C  C   . ASN   A 671 ? 0.5723 0.6676 0.4343 0.0102  0.0353  0.1018  650 ASN   A C   
5008 O  O   . ASN   A 671 ? 0.6322 0.7582 0.4771 0.0082  0.0365  0.1163  650 ASN   A O   
5009 C  CB  . ASN   A 671 ? 0.5747 0.6319 0.4905 0.0047  0.0370  0.1268  650 ASN   A CB  
5010 C  CG  . ASN   A 671 ? 0.6632 0.6950 0.5962 0.0051  0.0411  0.1065  650 ASN   A CG  
5011 O  OD1 . ASN   A 671 ? 0.5999 0.6280 0.5215 0.0077  0.0423  0.0843  650 ASN   A OD1 
5012 N  ND2 . ASN   A 671 ? 0.6738 0.6903 0.6368 0.0020  0.0427  0.1142  650 ASN   A ND2 
5013 N  N   . VAL   A 672 ? 0.5289 0.6142 0.3863 0.0133  0.0382  0.0746  651 VAL   A N   
5014 C  CA  . VAL   A 672 ? 0.4988 0.6053 0.3340 0.0162  0.0420  0.0555  651 VAL   A CA  
5015 C  C   . VAL   A 672 ? 0.5534 0.6548 0.3942 0.0161  0.0529  0.0468  651 VAL   A C   
5016 O  O   . VAL   A 672 ? 0.5383 0.6135 0.3966 0.0159  0.0542  0.0400  651 VAL   A O   
5017 C  CB  . VAL   A 672 ? 0.4843 0.5836 0.3155 0.0202  0.0344  0.0308  651 VAL   A CB  
5018 C  CG1 . VAL   A 672 ? 0.4628 0.5851 0.2769 0.0239  0.0372  0.0078  651 VAL   A CG1 
5019 C  CG2 . VAL   A 672 ? 0.4716 0.5755 0.3005 0.0201  0.0231  0.0392  651 VAL   A CG2 
5020 N  N   . ARG   A 673 ? 0.5074 0.6380 0.3338 0.0160  0.0605  0.0471  652 ARG   A N   
5021 C  CA  . ARG   A 673 ? 0.4815 0.6129 0.3126 0.0174  0.0703  0.0347  652 ARG   A CA  
5022 C  C   . ARG   A 673 ? 0.5316 0.6678 0.3563 0.0242  0.0687  0.0033  652 ARG   A C   
5023 O  O   . ARG   A 673 ? 0.5472 0.7113 0.3543 0.0268  0.0665  -0.0077 652 ARG   A O   
5024 C  CB  . ARG   A 673 ? 0.5920 0.7555 0.4148 0.0134  0.0801  0.0503  652 ARG   A CB  
5025 C  CG  . ARG   A 673 ? 0.6317 0.7902 0.4679 0.0129  0.0901  0.0461  652 ARG   A CG  
5026 C  CD  . ARG   A 673 ? 0.6185 0.7987 0.4463 0.0193  0.0958  0.0194  652 ARG   A CD  
5027 N  NE  . ARG   A 673 ? 0.6385 0.8601 0.4540 0.0165  0.1040  0.0258  652 ARG   A NE  
5028 C  CZ  . ARG   A 673 ? 0.7270 0.9674 0.5427 0.0208  0.1083  0.0034  652 ARG   A CZ  
5029 N  NH1 . ARG   A 673 ? 0.7692 0.9992 0.5931 0.0296  0.1077  -0.0257 652 ARG   A NH1 
5030 N  NH2 . ARG   A 673 ? 0.6777 0.9491 0.4886 0.0164  0.1126  0.0108  652 ARG   A NH2 
5031 N  N   . ARG   A 674 ? 0.4842 0.5949 0.3256 0.0268  0.0686  -0.0111 653 ARG   A N   
5032 C  CA  . ARG   A 674 ? 0.5044 0.6114 0.3494 0.0330  0.0642  -0.0389 653 ARG   A CA  
5033 C  C   . ARG   A 674 ? 0.4786 0.5925 0.3332 0.0374  0.0717  -0.0535 653 ARG   A C   
5034 O  O   . ARG   A 674 ? 0.4689 0.5830 0.3299 0.0350  0.0796  -0.0416 653 ARG   A O   
5035 C  CB  . ARG   A 674 ? 0.4119 0.4848 0.2727 0.0319  0.0551  -0.0418 653 ARG   A CB  
5036 C  CG  . ARG   A 674 ? 0.4575 0.5245 0.3130 0.0280  0.0480  -0.0282 653 ARG   A CG  
5037 C  CD  . ARG   A 674 ? 0.4578 0.4984 0.3280 0.0264  0.0397  -0.0329 653 ARG   A CD  
5038 N  NE  . ARG   A 674 ? 0.4984 0.5372 0.3654 0.0237  0.0331  -0.0218 653 ARG   A NE  
5039 C  CZ  . ARG   A 674 ? 0.4744 0.5232 0.3322 0.0250  0.0251  -0.0290 653 ARG   A CZ  
5040 N  NH1 . ARG   A 674 ? 0.4559 0.5168 0.3073 0.0288  0.0225  -0.0500 653 ARG   A NH1 
5041 N  NH2 . ARG   A 674 ? 0.5416 0.5897 0.3994 0.0228  0.0191  -0.0167 653 ARG   A NH2 
5042 N  N   . LYS   A 675 ? 0.4990 0.6198 0.3578 0.0442  0.0686  -0.0807 654 LYS   A N   
5043 C  CA  . LYS   A 675 ? 0.5159 0.6381 0.3920 0.0502  0.0731  -0.0974 654 LYS   A CA  
5044 C  C   . LYS   A 675 ? 0.5225 0.6098 0.4212 0.0482  0.0702  -0.0879 654 LYS   A C   
5045 O  O   . LYS   A 675 ? 0.5403 0.6022 0.4454 0.0449  0.0616  -0.0822 654 LYS   A O   
5046 C  CB  . LYS   A 675 ? 0.4853 0.6155 0.3703 0.0584  0.0675  -0.1309 654 LYS   A CB  
5047 C  CG  . LYS   A 675 ? 0.5518 0.7262 0.4152 0.0610  0.0713  -0.1468 654 LYS   A CG  
5048 C  CD  . LYS   A 675 ? 0.5986 0.7828 0.4826 0.0695  0.0690  -0.1809 654 LYS   A CD  
5049 C  CE  . LYS   A 675 ? 0.7201 0.9236 0.5970 0.0695  0.0612  -0.1989 654 LYS   A CE  
5050 N  NZ  . LYS   A 675 ? 0.7857 0.9675 0.6932 0.0755  0.0500  -0.2275 654 LYS   A NZ  
5051 N  N   . PRO   A 676 ? 0.4511 0.5405 0.3621 0.0496  0.0771  -0.0857 655 PRO   A N   
5052 C  CA  . PRO   A 676 ? 0.4334 0.4957 0.3656 0.0476  0.0733  -0.0773 655 PRO   A CA  
5053 C  C   . PRO   A 676 ? 0.4698 0.5132 0.4241 0.0524  0.0625  -0.0928 655 PRO   A C   
5054 O  O   . PRO   A 676 ? 0.4695 0.5202 0.4286 0.0591  0.0589  -0.1152 655 PRO   A O   
5055 C  CB  . PRO   A 676 ? 0.4000 0.4766 0.3406 0.0493  0.0828  -0.0751 655 PRO   A CB  
5056 C  CG  . PRO   A 676 ? 0.4964 0.6066 0.4266 0.0549  0.0904  -0.0908 655 PRO   A CG  
5057 C  CD  . PRO   A 676 ? 0.4651 0.5861 0.3704 0.0517  0.0888  -0.0879 655 PRO   A CD  
5058 N  N   . PHE   A 677 ? 0.4829 0.5036 0.4527 0.0481  0.0567  -0.0804 656 PHE   A N   
5059 C  CA  . PHE   A 677 ? 0.4834 0.4862 0.4804 0.0512  0.0458  -0.0888 656 PHE   A CA  
5060 C  C   . PHE   A 677 ? 0.4925 0.5048 0.5107 0.0615  0.0472  -0.1074 656 PHE   A C   
5061 O  O   . PHE   A 677 ? 0.4831 0.5124 0.4991 0.0641  0.0567  -0.1066 656 PHE   A O   
5062 C  CB  . PHE   A 677 ? 0.4935 0.4801 0.5033 0.0439  0.0410  -0.0684 656 PHE   A CB  
5063 C  CG  . PHE   A 677 ? 0.4508 0.4288 0.4475 0.0345  0.0380  -0.0546 656 PHE   A CG  
5064 C  CD1 . PHE   A 677 ? 0.4970 0.4615 0.5014 0.0320  0.0277  -0.0569 656 PHE   A CD1 
5065 C  CD2 . PHE   A 677 ? 0.4331 0.4173 0.4142 0.0281  0.0450  -0.0404 656 PHE   A CD2 
5066 C  CE1 . PHE   A 677 ? 0.4506 0.4109 0.4450 0.0236  0.0254  -0.0454 656 PHE   A CE1 
5067 C  CE2 . PHE   A 677 ? 0.4643 0.4429 0.4378 0.0206  0.0422  -0.0310 656 PHE   A CE2 
5068 C  CZ  . PHE   A 677 ? 0.4455 0.4136 0.4246 0.0185  0.0329  -0.0334 656 PHE   A CZ  
5069 N  N   . THR   A 678 ? 0.5060 0.5076 0.5488 0.0676  0.0373  -0.1256 657 THR   A N   
5070 C  CA  . THR   A 678 ? 0.5235 0.5305 0.5965 0.0783  0.0365  -0.1440 657 THR   A CA  
5071 C  C   . THR   A 678 ? 0.4934 0.4861 0.5927 0.0770  0.0316  -0.1254 657 THR   A C   
5072 O  O   . THR   A 678 ? 0.4531 0.4559 0.5715 0.0845  0.0347  -0.1320 657 THR   A O   
5073 C  CB  . THR   A 678 ? 0.4958 0.4955 0.5939 0.0858  0.0263  -0.1720 657 THR   A CB  
5074 O  OG1 . THR   A 678 ? 0.6732 0.6420 0.7951 0.0804  0.0120  -0.1597 657 THR   A OG1 
5075 C  CG2 . THR   A 678 ? 0.4703 0.4884 0.5393 0.0855  0.0300  -0.1890 657 THR   A CG2 
5076 N  N   . PHE   A 679 ? 0.4514 0.4250 0.5517 0.0672  0.0241  -0.1019 658 PHE   A N   
5077 C  CA  . PHE   A 679 ? 0.4685 0.4353 0.5883 0.0634  0.0193  -0.0801 658 PHE   A CA  
5078 C  C   . PHE   A 679 ? 0.4228 0.4086 0.5235 0.0610  0.0316  -0.0698 658 PHE   A C   
5079 O  O   . PHE   A 679 ? 0.4319 0.4252 0.5016 0.0541  0.0399  -0.0623 658 PHE   A O   
5080 C  CB  . PHE   A 679 ? 0.4394 0.3906 0.5584 0.0516  0.0103  -0.0580 658 PHE   A CB  
5081 C  CG  . PHE   A 679 ? 0.4058 0.3546 0.5456 0.0464  0.0031  -0.0343 658 PHE   A CG  
5082 C  CD1 . PHE   A 679 ? 0.4120 0.3757 0.5341 0.0393  0.0100  -0.0175 658 PHE   A CD1 
5083 C  CD2 . PHE   A 679 ? 0.3994 0.3332 0.5791 0.0480  -0.0116 -0.0283 658 PHE   A CD2 
5084 C  CE1 . PHE   A 679 ? 0.4517 0.4197 0.5909 0.0338  0.0029  0.0041  658 PHE   A CE1 
5085 C  CE2 . PHE   A 679 ? 0.3945 0.3306 0.5930 0.0423  -0.0193 -0.0024 658 PHE   A CE2 
5086 C  CZ  . PHE   A 679 ? 0.4244 0.3799 0.6005 0.0352  -0.0118 0.0134  658 PHE   A CZ  
5087 N  N   . LYS   A 680 ? 0.4098 0.4034 0.5327 0.0668  0.0320  -0.0696 659 LYS   A N   
5088 C  CA  . LYS   A 680 ? 0.3753 0.3877 0.4851 0.0639  0.0427  -0.0602 659 LYS   A CA  
5089 C  C   . LYS   A 680 ? 0.3339 0.3432 0.4391 0.0521  0.0389  -0.0347 659 LYS   A C   
5090 O  O   . LYS   A 680 ? 0.3851 0.3848 0.5120 0.0498  0.0269  -0.0219 659 LYS   A O   
5091 C  CB  . LYS   A 680 ? 0.3642 0.3894 0.5017 0.0744  0.0440  -0.0700 659 LYS   A CB  
5092 C  CG  . LYS   A 680 ? 0.3921 0.4235 0.5432 0.0873  0.0457  -0.0997 659 LYS   A CG  
5093 C  CD  . LYS   A 680 ? 0.4003 0.4498 0.5161 0.0864  0.0588  -0.1124 659 LYS   A CD  
5094 C  CE  . LYS   A 680 ? 0.4610 0.5266 0.5895 0.0990  0.0616  -0.1451 659 LYS   A CE  
5095 N  NZ  . LYS   A 680 ? 0.6022 0.6931 0.6948 0.0970  0.0740  -0.1551 659 LYS   A NZ  
5096 N  N   . TRP   A 681 ? 0.3806 0.4005 0.4597 0.0442  0.0485  -0.0272 660 TRP   A N   
5097 C  CA  . TRP   A 681 ? 0.2880 0.3090 0.3612 0.0327  0.0455  -0.0084 660 TRP   A CA  
5098 C  C   . TRP   A 681 ? 0.3230 0.3532 0.4189 0.0318  0.0392  0.0037  660 TRP   A C   
5099 O  O   . TRP   A 681 ? 0.3242 0.3555 0.4242 0.0236  0.0310  0.0197  660 TRP   A O   
5100 C  CB  . TRP   A 681 ? 0.3152 0.3465 0.3645 0.0257  0.0567  -0.0064 660 TRP   A CB  
5101 C  CG  . TRP   A 681 ? 0.3542 0.4022 0.4049 0.0282  0.0667  -0.0100 660 TRP   A CG  
5102 C  CD1 . TRP   A 681 ? 0.3160 0.3718 0.3583 0.0334  0.0763  -0.0204 660 TRP   A CD1 
5103 C  CD2 . TRP   A 681 ? 0.2609 0.3241 0.3224 0.0244  0.0679  -0.0026 660 TRP   A CD2 
5104 N  NE1 . TRP   A 681 ? 0.3404 0.4139 0.3890 0.0328  0.0839  -0.0190 660 TRP   A NE1 
5105 C  CE2 . TRP   A 681 ? 0.2848 0.3618 0.3457 0.0276  0.0786  -0.0091 660 TRP   A CE2 
5106 C  CE3 . TRP   A 681 ? 0.2919 0.3624 0.3632 0.0178  0.0608  0.0093  660 TRP   A CE3 
5107 C  CZ2 . TRP   A 681 ? 0.3004 0.3951 0.3724 0.0247  0.0822  -0.0052 660 TRP   A CZ2 
5108 C  CZ3 . TRP   A 681 ? 0.2596 0.3493 0.3401 0.0153  0.0640  0.0123  660 TRP   A CZ3 
5109 C  CH2 . TRP   A 681 ? 0.2760 0.3761 0.3578 0.0189  0.0745  0.0045  660 TRP   A CH2 
5110 N  N   . TRP   A 682 ? 0.3085 0.3492 0.4196 0.0399  0.0425  -0.0029 661 TRP   A N   
5111 C  CA  . TRP   A 682 ? 0.3281 0.3806 0.4616 0.0393  0.0359  0.0097  661 TRP   A CA  
5112 C  C   . TRP   A 682 ? 0.3412 0.3815 0.5052 0.0427  0.0199  0.0193  661 TRP   A C   
5113 O  O   . TRP   A 682 ? 0.3776 0.4287 0.5610 0.0406  0.0115  0.0356  661 TRP   A O   
5114 C  CB  . TRP   A 682 ? 0.2971 0.3661 0.4415 0.0473  0.0439  -0.0005 661 TRP   A CB  
5115 C  CG  . TRP   A 682 ? 0.3065 0.3716 0.4638 0.0609  0.0468  -0.0215 661 TRP   A CG  
5116 C  CD1 . TRP   A 682 ? 0.3067 0.3661 0.4994 0.0724  0.0375  -0.0285 661 TRP   A CD1 
5117 C  CD2 . TRP   A 682 ? 0.3210 0.3922 0.4583 0.0644  0.0596  -0.0392 661 TRP   A CD2 
5118 N  NE1 . TRP   A 682 ? 0.3539 0.4168 0.5496 0.0833  0.0445  -0.0539 661 TRP   A NE1 
5119 C  CE2 . TRP   A 682 ? 0.4000 0.4725 0.5596 0.0780  0.0583  -0.0596 661 TRP   A CE2 
5120 C  CE3 . TRP   A 682 ? 0.3489 0.4263 0.4540 0.0571  0.0713  -0.0390 661 TRP   A CE3 
5121 C  CZ2 . TRP   A 682 ? 0.3424 0.4278 0.4885 0.0838  0.0693  -0.0807 661 TRP   A CZ2 
5122 C  CZ3 . TRP   A 682 ? 0.3402 0.4280 0.4329 0.0623  0.0812  -0.0551 661 TRP   A CZ3 
5123 C  CH2 . TRP   A 682 ? 0.3771 0.4714 0.4880 0.0752  0.0806  -0.0761 661 TRP   A CH2 
5124 N  N   . HIS   A 683 ? 0.3898 0.4094 0.5612 0.0473  0.0144  0.0109  662 HIS   A N   
5125 C  CA  . HIS   A 683 ? 0.3653 0.3702 0.5698 0.0485  -0.0023 0.0228  662 HIS   A CA  
5126 C  C   . HIS   A 683 ? 0.4344 0.4381 0.6288 0.0339  -0.0098 0.0462  662 HIS   A C   
5127 O  O   . HIS   A 683 ? 0.4819 0.4774 0.7041 0.0315  -0.0245 0.0635  662 HIS   A O   
5128 C  CB  . HIS   A 683 ? 0.4070 0.3910 0.6286 0.0590  -0.0058 0.0013  662 HIS   A CB  
5129 C  CG  . HIS   A 683 ? 0.3592 0.3482 0.6039 0.0744  -0.0023 -0.0218 662 HIS   A CG  
5130 N  ND1 . HIS   A 683 ? 0.3802 0.3610 0.6335 0.0850  -0.0005 -0.0506 662 HIS   A ND1 
5131 C  CD2 . HIS   A 683 ? 0.4092 0.4145 0.6715 0.0811  -0.0001 -0.0222 662 HIS   A CD2 
5132 C  CE1 . HIS   A 683 ? 0.4342 0.4277 0.7094 0.0977  0.0034  -0.0688 662 HIS   A CE1 
5133 N  NE2 . HIS   A 683 ? 0.3736 0.3808 0.6553 0.0958  0.0036  -0.0513 662 HIS   A NE2 
5134 N  N   . MET   A 684 ? 0.4403 0.4540 0.5990 0.0241  -0.0004 0.0475  663 MET   A N   
5135 C  CA  . MET   A 684 ? 0.4351 0.4553 0.5822 0.0101  -0.0052 0.0661  663 MET   A CA  
5136 C  C   . MET   A 684 ? 0.4867 0.5322 0.6425 0.0020  -0.0114 0.0890  663 MET   A C   
5137 O  O   . MET   A 684 ? 0.4782 0.5364 0.6436 0.0068  -0.0100 0.0888  663 MET   A O   
5138 C  CB  . MET   A 684 ? 0.4178 0.4430 0.5288 0.0041  0.0073  0.0558  663 MET   A CB  
5139 C  CG  . MET   A 684 ? 0.5704 0.6072 0.6681 -0.0096 0.0050  0.0691  663 MET   A CG  
5140 S  SD  . MET   A 684 ? 0.5273 0.5612 0.5927 -0.0121 0.0177  0.0522  663 MET   A SD  
5141 C  CE  . MET   A 684 ? 0.4730 0.5251 0.5314 -0.0274 0.0131  0.0666  663 MET   A CE  
5142 N  N   . VAL   A 685 ? 0.5433 0.6003 0.6958 -0.0109 -0.0185 0.1091  664 VAL   A N   
5143 C  CA  . VAL   A 685 ? 0.5551 0.6460 0.7078 -0.0215 -0.0231 0.1304  664 VAL   A CA  
5144 C  C   . VAL   A 685 ? 0.5963 0.7100 0.7195 -0.0354 -0.0169 0.1315  664 VAL   A C   
5145 O  O   . VAL   A 685 ? 0.6365 0.7584 0.7610 -0.0458 -0.0241 0.1484  664 VAL   A O   
5146 C  CB  . VAL   A 685 ? 0.5408 0.6344 0.7268 -0.0246 -0.0411 0.1599  664 VAL   A CB  
5147 C  CG1 . VAL   A 685 ? 0.4909 0.6238 0.6789 -0.0326 -0.0460 0.1804  664 VAL   A CG1 
5148 C  CG2 . VAL   A 685 ? 0.5405 0.6033 0.7629 -0.0094 -0.0486 0.1540  664 VAL   A CG2 
5149 N  N   . PRO   A 686 ? 0.5818 0.7082 0.6822 -0.0366 -0.0041 0.1138  665 PRO   A N   
5150 C  CA  . PRO   A 686 ? 0.5703 0.7190 0.6481 -0.0485 0.0017  0.1101  665 PRO   A CA  
5151 C  C   . PRO   A 686 ? 0.6425 0.8343 0.7213 -0.0619 -0.0054 0.1302  665 PRO   A C   
5152 O  O   . PRO   A 686 ? 0.6657 0.8742 0.7585 -0.0621 -0.0126 0.1449  665 PRO   A O   
5153 C  CB  . PRO   A 686 ? 0.5065 0.6565 0.5698 -0.0449 0.0153  0.0866  665 PRO   A CB  
5154 C  CG  . PRO   A 686 ? 0.4628 0.5863 0.5358 -0.0311 0.0180  0.0780  665 PRO   A CG  
5155 C  CD  . PRO   A 686 ? 0.4900 0.6117 0.5878 -0.0273 0.0056  0.0958  665 PRO   A CD  
5156 N  N   . SER   A 687 ? 0.6277 0.8418 0.6918 -0.0735 -0.0032 0.1306  666 SER   A N   
5157 C  CA  . SER   A 687 ? 0.6847 0.9496 0.7452 -0.0881 -0.0082 0.1470  666 SER   A CA  
5158 C  C   . SER   A 687 ? 0.7624 1.0592 0.8144 -0.0903 -0.0016 0.1319  666 SER   A C   
5159 O  O   . SER   A 687 ? 0.7886 1.0710 0.8336 -0.0840 0.0094  0.1058  666 SER   A O   
5160 C  CB  . SER   A 687 ? 0.6991 0.9840 0.7465 -0.0996 -0.0059 0.1469  666 SER   A CB  
5161 O  OG  . SER   A 687 ? 0.8150 1.0741 0.8732 -0.0996 -0.0135 0.1631  666 SER   A OG  
5162 N  N   . ARG   A 688 ? 0.8420 1.1843 0.8966 -0.1001 -0.0091 0.1497  667 ARG   A N   
5163 C  CA  . ARG   A 688 ? 0.7747 1.1536 0.8239 -0.1037 -0.0049 0.1360  667 ARG   A CA  
5164 C  C   . ARG   A 688 ? 0.7703 1.1777 0.7985 -0.1109 0.0007  0.1115  667 ARG   A C   
5165 O  O   . ARG   A 688 ? 0.8550 1.2691 0.8735 -0.1158 -0.0022 0.1134  667 ARG   A O   
5166 C  CB  . ARG   A 688 ? 0.6512 1.0670 0.7114 -0.1095 -0.0178 0.1640  667 ARG   A CB  
5167 CA CA  . CA    B .   ? 0.6262 0.9423 0.5766 -0.0216 0.1781  0.0635  701 CA    A CA  
5168 CA CA  . CA    C .   ? 0.4530 0.7322 0.4641 -0.0480 0.1803  0.1013  702 CA    A CA  
5169 CA CA  . CA    D .   ? 0.6702 0.9324 0.8300 -0.1104 0.1831  0.1550  703 CA    A CA  
5170 CA CA  . CA    E .   ? 0.5442 0.8070 0.9369 0.1555  0.0830  -0.1433 704 CA    A CA  
5171 C  C4  . A1A8O F .   ? 0.4034 0.3972 0.5891 -0.0410 0.0829  -0.0100 705 A1A8O A C4  
5172 C  C6  . A1A8O F .   ? 0.3901 0.4175 0.5850 -0.0477 0.0850  -0.0508 705 A1A8O A C6  
5173 C  C13 . A1A8O F .   ? 0.4227 0.4520 0.5956 -0.0567 0.1054  0.0206  705 A1A8O A C13 
5174 C  C20 . A1A8O F .   ? 0.5190 0.5820 0.7167 -0.0785 0.1291  0.1013  705 A1A8O A C20 
5175 C  C21 . A1A8O F .   ? 0.5265 0.6121 0.6952 -0.0733 0.1360  0.0942  705 A1A8O A C21 
5176 C  C8  . A1A8O F .   ? 0.3812 0.3951 0.5819 -0.0516 0.0906  -0.0197 705 A1A8O A C8  
5177 C  C16 . A1A8O F .   ? 0.4262 0.4870 0.6046 -0.0659 0.1192  0.0356  705 A1A8O A C16 
5178 O  O17 . A1A8O F .   ? 0.4234 0.4942 0.5781 -0.0602 0.1193  0.0262  705 A1A8O A O17 
5179 C  C19 . A1A8O F .   ? 0.5023 0.5536 0.7156 -0.0772 0.1229  0.0738  705 A1A8O A C19 
5180 C  C26 . A1A8O F .   ? 0.4533 0.4319 0.6215 -0.0303 0.0740  -0.0008 705 A1A8O A C26 
5181 C  C1  . A1A8O F .   ? 0.4514 0.4292 0.6320 -0.0423 0.0855  0.0431  705 A1A8O A C1  
5182 C  C10 . A1A8O F .   ? 0.4000 0.4376 0.6191 -0.0627 0.0974  -0.0288 705 A1A8O A C10 
5183 C  C11 . A1A8O F .   ? 0.4669 0.5056 0.6986 -0.0683 0.1022  -0.0143 705 A1A8O A C11 
5184 C  C12 . A1A8O F .   ? 0.4643 0.5075 0.6599 -0.0639 0.1073  0.0060  705 A1A8O A C12 
5185 C  C14 . A1A8O F .   ? 0.4381 0.4635 0.6026 -0.0520 0.0996  0.0047  705 A1A8O A C14 
5186 C  C15 . A1A8O F .   ? 0.5308 0.5782 0.7409 -0.0701 0.1129  0.0225  705 A1A8O A C15 
5187 C  C2  . A1A8O F .   ? 0.4126 0.4006 0.6040 -0.0470 0.0893  0.0260  705 A1A8O A C2  
5188 C  C22 . A1A8O F .   ? 0.4929 0.5732 0.6462 -0.0650 0.1313  0.0691  705 A1A8O A C22 
5189 C  C24 . A1A8O F .   ? 0.4343 0.4145 0.6104 -0.0356 0.0790  0.0075  705 A1A8O A C24 
5190 C  C25 . A1A8O F .   ? 0.4318 0.4049 0.6050 -0.0363 0.0800  0.0335  705 A1A8O A C25 
5191 C  C27 . A1A8O F .   ? 0.3955 0.3846 0.5305 -0.0278 0.0746  -0.0076 705 A1A8O A C27 
5192 C  C28 . A1A8O F .   ? 0.3643 0.3533 0.4945 -0.0238 0.0698  -0.0144 705 A1A8O A C28 
5193 C  C29 . A1A8O F .   ? 0.4143 0.3934 0.5732 -0.0213 0.0646  -0.0153 705 A1A8O A C29 
5194 C  C3  . A1A8O F .   ? 0.4636 0.4604 0.6567 -0.0464 0.0877  -0.0010 705 A1A8O A C3  
5195 C  C30 . A1A8O F .   ? 0.4346 0.4020 0.6281 -0.0230 0.0634  -0.0082 705 A1A8O A C30 
5196 C  C5  . A1A8O F .   ? 0.3999 0.4094 0.5875 -0.0420 0.0820  -0.0357 705 A1A8O A C5  
5197 N  N18 . A1A8O F .   ? 0.4453 0.5085 0.6257 -0.0690 0.1243  0.0577  705 A1A8O A N18 
5198 N  N23 . A1A8O F .   ? 0.4355 0.4958 0.6694 -0.0774 0.1142  0.0099  705 A1A8O A N23 
5199 N  N31 . A1A8O F .   ? 0.4545 0.4214 0.6529 -0.0280 0.0680  -0.0003 705 A1A8O A N31 
5200 N  N7  . A1A8O F .   ? 0.3554 0.3846 0.5571 -0.0523 0.0889  -0.0437 705 A1A8O A N7  
5201 N  N9  . A1A8O F .   ? 0.3730 0.3935 0.5745 -0.0561 0.0956  -0.0111 705 A1A8O A N9  
5202 CL CL1 . A1A8O F .   ? 0.4902 0.4726 0.6460 -0.0162 0.0588  -0.0246 705 A1A8O A CL1 
5203 CL CL2 . A1A8O F .   ? 0.4258 0.4283 0.5300 -0.0295 0.0801  -0.0069 705 A1A8O A CL2 
# 
